data_7PUV
# 
_entry.id   7PUV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.397 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7PUV         pdb_00007puv 10.2210/pdb7puv/pdb 
WWPDB D_1292118224 ?            ?                   
# 
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 2022-01-12 
2 'Structure model' 1 1 2022-01-26 
3 'Structure model' 1 2 2024-01-31 
4 'Structure model' 1 3 2024-10-23 
# 
_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' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Refinement description' 
4 4 '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' citation                      
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' pdbx_initial_refinement_model 
5 4 'Structure model' pdbx_entry_details            
6 4 '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' '_citation.pdbx_database_id_PubMed'            
2 2 'Structure model' '_citation.title'                              
3 2 'Structure model' '_citation.year'                               
4 4 'Structure model' '_pdbx_entry_details.has_protein_modification' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7PUV 
_pdbx_database_status.recvd_initial_deposition_date   2021-09-30 
_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.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'PDB entry for the same citation' 
_pdbx_database_related.db_id          7PUU 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              grazulis@ibt.lt 
_pdbx_contact_author.name_first         Saulius 
_pdbx_contact_author.name_last          Grazulis 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7928-5218 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Int J Mol Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1422-0067 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            23 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates as High Affinity and Selective Inhibitors of Carbonic Anhydrase IX.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/ijms23010130 
_citation.pdbx_database_id_PubMed   35008553 
_citation.pdbx_database_id_patent   ? 
_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 'Paketuryte-Latve, V.' 3  ? 
primary 'Smirnov, A.'          4  ? 
primary 'Leitans, J.'          5  ? 
primary 'Kazaks, A.'           6  ? 
primary 'Dvinskis, E.'         7  ? 
primary 'Stancaitis, L.'       8  ? 
primary 'Mickeviciute, A.'     9  ? 
primary 'Jachno, J.'           10 ? 
primary 'Jezepcikas, L.'       11 ? 
primary 'Linkuviene, V.'       12 ? 
primary 'Sakalauskas, A.'      13 ? 
primary 'Manakova, E.'         14 ? 
primary 'Grazulis, S.'         15 ? 
primary 'Matuliene, J.'        16 ? 
primary 'Tars, K.'             17 ? 
primary 'Matulis, D.'          18 ? 
# 
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 II' ? 
2 non-polymer syn 'ZINC ION'                                                   65.409    4    ?       ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                               62.068    7    ?       ? ? ? 
4 non-polymer syn 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' 389.831   4    ?       ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                      106.120   1    ?       ? ? ? 
6 water       nat water                                                        18.015    1143 ?       ? ? ? 
# 
_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 1,2-ETHANEDIOL                                               EDO 
4 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' 84Z 
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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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              ? 
_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 
84Z non-polymer         . 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' ?                 'C14 H12 Cl N O6 S2' 
389.831 
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  
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 ?   ?   ?   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 ?   ?   ?   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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        84Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   84Z 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 EDO 1   302 3    EDO EDO A . 
G 3 EDO 1   303 6    EDO EDO A . 
H 4 84Z 1   304 1    84Z E2A A . 
I 2 ZN  1   301 2    ZN  ZN  B . 
J 3 EDO 1   302 5    EDO EDO B . 
K 5 PEG 1   303 8    PEG PEG B . 
L 4 84Z 1   304 2    84Z E2A B . 
M 2 ZN  1   301 3    ZN  ZN  C . 
N 3 EDO 1   302 1    EDO EDO C . 
O 3 EDO 1   303 4    EDO EDO C . 
P 3 EDO 1   304 7    EDO EDO C . 
Q 4 84Z 1   305 3    84Z E2A C . 
R 2 ZN  1   301 4    ZN  ZN  D . 
S 3 EDO 1   302 2    EDO EDO D . 
T 4 84Z 1   303 4    84Z E2A D . 
U 6 HOH 1   401 932  HOH HOH A . 
U 6 HOH 2   402 427  HOH HOH A . 
U 6 HOH 3   403 963  HOH HOH A . 
U 6 HOH 4   404 530  HOH HOH A . 
U 6 HOH 5   405 177  HOH HOH A . 
U 6 HOH 6   406 965  HOH HOH A . 
U 6 HOH 7   407 801  HOH HOH A . 
U 6 HOH 8   408 940  HOH HOH A . 
U 6 HOH 9   409 1026 HOH HOH A . 
U 6 HOH 10  410 887  HOH HOH A . 
U 6 HOH 11  411 501  HOH HOH A . 
U 6 HOH 12  412 1094 HOH HOH A . 
U 6 HOH 13  413 1036 HOH HOH A . 
U 6 HOH 14  414 961  HOH HOH A . 
U 6 HOH 15  415 419  HOH HOH A . 
U 6 HOH 16  416 603  HOH HOH A . 
U 6 HOH 17  417 958  HOH HOH A . 
U 6 HOH 18  418 1013 HOH HOH A . 
U 6 HOH 19  419 1085 HOH HOH A . 
U 6 HOH 20  420 824  HOH HOH A . 
U 6 HOH 21  421 536  HOH HOH A . 
U 6 HOH 22  422 766  HOH HOH A . 
U 6 HOH 23  423 937  HOH HOH A . 
U 6 HOH 24  424 8    HOH HOH A . 
U 6 HOH 25  425 674  HOH HOH A . 
U 6 HOH 26  426 1    HOH HOH A . 
U 6 HOH 27  427 620  HOH HOH A . 
U 6 HOH 28  428 832  HOH HOH A . 
U 6 HOH 29  429 237  HOH HOH A . 
U 6 HOH 30  430 705  HOH HOH A . 
U 6 HOH 31  431 950  HOH HOH A . 
U 6 HOH 32  432 130  HOH HOH A . 
U 6 HOH 33  433 16   HOH HOH A . 
U 6 HOH 34  434 599  HOH HOH A . 
U 6 HOH 35  435 724  HOH HOH A . 
U 6 HOH 36  436 662  HOH HOH A . 
U 6 HOH 37  437 544  HOH HOH A . 
U 6 HOH 38  438 790  HOH HOH A . 
U 6 HOH 39  439 504  HOH HOH A . 
U 6 HOH 40  440 809  HOH HOH A . 
U 6 HOH 41  441 966  HOH HOH A . 
U 6 HOH 42  442 503  HOH HOH A . 
U 6 HOH 43  443 341  HOH HOH A . 
U 6 HOH 44  444 487  HOH HOH A . 
U 6 HOH 45  445 71   HOH HOH A . 
U 6 HOH 46  446 613  HOH HOH A . 
U 6 HOH 47  447 238  HOH HOH A . 
U 6 HOH 48  448 1033 HOH HOH A . 
U 6 HOH 49  449 36   HOH HOH A . 
U 6 HOH 50  450 943  HOH HOH A . 
U 6 HOH 51  451 578  HOH HOH A . 
U 6 HOH 52  452 531  HOH HOH A . 
U 6 HOH 53  453 584  HOH HOH A . 
U 6 HOH 54  454 708  HOH HOH A . 
U 6 HOH 55  455 525  HOH HOH A . 
U 6 HOH 56  456 492  HOH HOH A . 
U 6 HOH 57  457 491  HOH HOH A . 
U 6 HOH 58  458 758  HOH HOH A . 
U 6 HOH 59  459 111  HOH HOH A . 
U 6 HOH 60  460 125  HOH HOH A . 
U 6 HOH 61  461 830  HOH HOH A . 
U 6 HOH 62  462 547  HOH HOH A . 
U 6 HOH 63  463 521  HOH HOH A . 
U 6 HOH 64  464 18   HOH HOH A . 
U 6 HOH 65  465 769  HOH HOH A . 
U 6 HOH 66  466 1019 HOH HOH A . 
U 6 HOH 67  467 904  HOH HOH A . 
U 6 HOH 68  468 103  HOH HOH A . 
U 6 HOH 69  469 1086 HOH HOH A . 
U 6 HOH 70  470 917  HOH HOH A . 
U 6 HOH 71  471 377  HOH HOH A . 
U 6 HOH 72  472 957  HOH HOH A . 
U 6 HOH 73  473 1087 HOH HOH A . 
U 6 HOH 74  474 466  HOH HOH A . 
U 6 HOH 75  475 514  HOH HOH A . 
U 6 HOH 76  476 601  HOH HOH A . 
U 6 HOH 77  477 78   HOH HOH A . 
U 6 HOH 78  478 564  HOH HOH A . 
U 6 HOH 79  479 451  HOH HOH A . 
U 6 HOH 80  480 113  HOH HOH A . 
U 6 HOH 81  481 735  HOH HOH A . 
U 6 HOH 82  482 138  HOH HOH A . 
U 6 HOH 83  483 467  HOH HOH A . 
U 6 HOH 84  484 502  HOH HOH A . 
U 6 HOH 85  485 945  HOH HOH A . 
U 6 HOH 86  486 368  HOH HOH A . 
U 6 HOH 87  487 494  HOH HOH A . 
U 6 HOH 88  488 32   HOH HOH A . 
U 6 HOH 89  489 295  HOH HOH A . 
U 6 HOH 90  490 948  HOH HOH A . 
U 6 HOH 91  491 526  HOH HOH A . 
U 6 HOH 92  492 459  HOH HOH A . 
U 6 HOH 93  493 589  HOH HOH A . 
U 6 HOH 94  494 896  HOH HOH A . 
U 6 HOH 95  495 652  HOH HOH A . 
U 6 HOH 96  496 792  HOH HOH A . 
U 6 HOH 97  497 665  HOH HOH A . 
U 6 HOH 98  498 402  HOH HOH A . 
U 6 HOH 99  499 217  HOH HOH A . 
U 6 HOH 100 500 496  HOH HOH A . 
U 6 HOH 101 501 571  HOH HOH A . 
U 6 HOH 102 502 135  HOH HOH A . 
U 6 HOH 103 503 508  HOH HOH A . 
U 6 HOH 104 504 183  HOH HOH A . 
U 6 HOH 105 505 342  HOH HOH A . 
U 6 HOH 106 506 960  HOH HOH A . 
U 6 HOH 107 507 66   HOH HOH A . 
U 6 HOH 108 508 529  HOH HOH A . 
U 6 HOH 109 509 76   HOH HOH A . 
U 6 HOH 110 510 559  HOH HOH A . 
U 6 HOH 111 511 892  HOH HOH A . 
U 6 HOH 112 512 795  HOH HOH A . 
U 6 HOH 113 513 301  HOH HOH A . 
U 6 HOH 114 514 707  HOH HOH A . 
U 6 HOH 115 515 38   HOH HOH A . 
U 6 HOH 116 516 1014 HOH HOH A . 
U 6 HOH 117 517 27   HOH HOH A . 
U 6 HOH 118 518 533  HOH HOH A . 
U 6 HOH 119 519 964  HOH HOH A . 
U 6 HOH 120 520 310  HOH HOH A . 
U 6 HOH 121 521 517  HOH HOH A . 
U 6 HOH 122 522 718  HOH HOH A . 
U 6 HOH 123 523 170  HOH HOH A . 
U 6 HOH 124 524 551  HOH HOH A . 
U 6 HOH 125 525 538  HOH HOH A . 
U 6 HOH 126 526 725  HOH HOH A . 
U 6 HOH 127 527 35   HOH HOH A . 
U 6 HOH 128 528 734  HOH HOH A . 
U 6 HOH 129 529 595  HOH HOH A . 
U 6 HOH 130 530 275  HOH HOH A . 
U 6 HOH 131 531 946  HOH HOH A . 
U 6 HOH 132 532 191  HOH HOH A . 
U 6 HOH 133 533 686  HOH HOH A . 
U 6 HOH 134 534 630  HOH HOH A . 
U 6 HOH 135 535 67   HOH HOH A . 
U 6 HOH 136 536 629  HOH HOH A . 
U 6 HOH 137 537 572  HOH HOH A . 
U 6 HOH 138 538 555  HOH HOH A . 
U 6 HOH 139 539 518  HOH HOH A . 
U 6 HOH 140 540 805  HOH HOH A . 
U 6 HOH 141 541 102  HOH HOH A . 
U 6 HOH 142 542 737  HOH HOH A . 
U 6 HOH 143 543 520  HOH HOH A . 
U 6 HOH 144 544 1034 HOH HOH A . 
U 6 HOH 145 545 812  HOH HOH A . 
U 6 HOH 146 546 280  HOH HOH A . 
U 6 HOH 147 547 650  HOH HOH A . 
U 6 HOH 148 548 549  HOH HOH A . 
U 6 HOH 149 549 604  HOH HOH A . 
U 6 HOH 150 550 128  HOH HOH A . 
U 6 HOH 151 551 124  HOH HOH A . 
U 6 HOH 152 552 229  HOH HOH A . 
U 6 HOH 153 553 655  HOH HOH A . 
U 6 HOH 154 554 96   HOH HOH A . 
U 6 HOH 155 555 150  HOH HOH A . 
U 6 HOH 156 556 444  HOH HOH A . 
U 6 HOH 157 557 505  HOH HOH A . 
U 6 HOH 158 558 941  HOH HOH A . 
U 6 HOH 159 559 580  HOH HOH A . 
U 6 HOH 160 560 1018 HOH HOH A . 
U 6 HOH 161 561 952  HOH HOH A . 
U 6 HOH 162 562 77   HOH HOH A . 
U 6 HOH 163 563 334  HOH HOH A . 
U 6 HOH 164 564 506  HOH HOH A . 
U 6 HOH 165 565 539  HOH HOH A . 
U 6 HOH 166 566 594  HOH HOH A . 
U 6 HOH 167 567 1022 HOH HOH A . 
U 6 HOH 168 568 845  HOH HOH A . 
U 6 HOH 169 569 426  HOH HOH A . 
U 6 HOH 170 570 425  HOH HOH A . 
U 6 HOH 171 571 519  HOH HOH A . 
U 6 HOH 172 572 947  HOH HOH A . 
U 6 HOH 173 573 949  HOH HOH A . 
U 6 HOH 174 574 647  HOH HOH A . 
U 6 HOH 175 575 205  HOH HOH A . 
U 6 HOH 176 576 268  HOH HOH A . 
U 6 HOH 177 577 857  HOH HOH A . 
U 6 HOH 178 578 338  HOH HOH A . 
U 6 HOH 179 579 181  HOH HOH A . 
U 6 HOH 180 580 23   HOH HOH A . 
U 6 HOH 181 581 1023 HOH HOH A . 
U 6 HOH 182 582 371  HOH HOH A . 
U 6 HOH 183 583 743  HOH HOH A . 
U 6 HOH 184 584 612  HOH HOH A . 
U 6 HOH 185 585 855  HOH HOH A . 
U 6 HOH 186 586 639  HOH HOH A . 
U 6 HOH 187 587 807  HOH HOH A . 
U 6 HOH 188 588 628  HOH HOH A . 
U 6 HOH 189 589 207  HOH HOH A . 
U 6 HOH 190 590 703  HOH HOH A . 
U 6 HOH 191 591 1143 HOH HOH A . 
U 6 HOH 192 592 704  HOH HOH A . 
U 6 HOH 193 593 290  HOH HOH A . 
U 6 HOH 194 594 326  HOH HOH A . 
U 6 HOH 195 595 298  HOH HOH A . 
U 6 HOH 196 596 606  HOH HOH A . 
U 6 HOH 197 597 953  HOH HOH A . 
U 6 HOH 198 598 507  HOH HOH A . 
U 6 HOH 199 599 1093 HOH HOH A . 
U 6 HOH 200 600 740  HOH HOH A . 
U 6 HOH 201 601 320  HOH HOH A . 
U 6 HOH 202 602 1029 HOH HOH A . 
U 6 HOH 203 603 962  HOH HOH A . 
U 6 HOH 204 604 1142 HOH HOH A . 
U 6 HOH 205 605 556  HOH HOH A . 
U 6 HOH 206 606 1098 HOH HOH A . 
U 6 HOH 207 607 1097 HOH HOH A . 
U 6 HOH 208 608 271  HOH HOH A . 
U 6 HOH 209 609 386  HOH HOH A . 
U 6 HOH 210 610 955  HOH HOH A . 
U 6 HOH 211 611 1015 HOH HOH A . 
U 6 HOH 212 612 1038 HOH HOH A . 
U 6 HOH 213 613 1092 HOH HOH A . 
U 6 HOH 214 614 931  HOH HOH A . 
U 6 HOH 215 615 552  HOH HOH A . 
U 6 HOH 216 616 951  HOH HOH A . 
U 6 HOH 217 617 998  HOH HOH A . 
U 6 HOH 218 618 568  HOH HOH A . 
U 6 HOH 219 619 1021 HOH HOH A . 
U 6 HOH 220 620 666  HOH HOH A . 
U 6 HOH 221 621 968  HOH HOH A . 
U 6 HOH 222 622 710  HOH HOH A . 
U 6 HOH 223 623 558  HOH HOH A . 
U 6 HOH 224 624 813  HOH HOH A . 
U 6 HOH 225 625 633  HOH HOH A . 
U 6 HOH 226 626 886  HOH HOH A . 
U 6 HOH 227 627 438  HOH HOH A . 
U 6 HOH 228 628 484  HOH HOH A . 
U 6 HOH 229 629 469  HOH HOH A . 
U 6 HOH 230 630 800  HOH HOH A . 
U 6 HOH 231 631 1096 HOH HOH A . 
U 6 HOH 232 632 566  HOH HOH A . 
U 6 HOH 233 633 954  HOH HOH A . 
U 6 HOH 234 634 1050 HOH HOH A . 
U 6 HOH 235 635 682  HOH HOH A . 
U 6 HOH 236 636 867  HOH HOH A . 
U 6 HOH 237 637 1031 HOH HOH A . 
U 6 HOH 238 638 944  HOH HOH A . 
U 6 HOH 239 639 1028 HOH HOH A . 
U 6 HOH 240 640 722  HOH HOH A . 
U 6 HOH 241 641 959  HOH HOH A . 
U 6 HOH 242 642 391  HOH HOH A . 
U 6 HOH 243 643 1032 HOH HOH A . 
U 6 HOH 244 644 673  HOH HOH A . 
U 6 HOH 245 645 611  HOH HOH A . 
U 6 HOH 246 646 1088 HOH HOH A . 
U 6 HOH 247 647 933  HOH HOH A . 
U 6 HOH 248 648 711  HOH HOH A . 
U 6 HOH 249 649 626  HOH HOH A . 
U 6 HOH 250 650 942  HOH HOH A . 
U 6 HOH 251 651 1027 HOH HOH A . 
U 6 HOH 252 652 1030 HOH HOH A . 
U 6 HOH 253 653 668  HOH HOH A . 
U 6 HOH 254 654 877  HOH HOH A . 
U 6 HOH 255 655 879  HOH HOH A . 
U 6 HOH 256 656 1017 HOH HOH A . 
U 6 HOH 257 657 969  HOH HOH A . 
U 6 HOH 258 658 759  HOH HOH A . 
U 6 HOH 259 659 588  HOH HOH A . 
U 6 HOH 260 660 793  HOH HOH A . 
U 6 HOH 261 661 713  HOH HOH A . 
U 6 HOH 262 662 815  HOH HOH A . 
U 6 HOH 263 663 1020 HOH HOH A . 
U 6 HOH 264 664 449  HOH HOH A . 
U 6 HOH 265 665 810  HOH HOH A . 
U 6 HOH 266 666 919  HOH HOH A . 
U 6 HOH 267 667 842  HOH HOH A . 
U 6 HOH 268 668 1089 HOH HOH A . 
U 6 HOH 269 669 1024 HOH HOH A . 
U 6 HOH 270 670 956  HOH HOH A . 
U 6 HOH 271 671 714  HOH HOH A . 
U 6 HOH 272 672 1016 HOH HOH A . 
U 6 HOH 273 673 1039 HOH HOH A . 
U 6 HOH 274 674 939  HOH HOH A . 
U 6 HOH 275 675 910  HOH HOH A . 
U 6 HOH 276 676 814  HOH HOH A . 
U 6 HOH 277 677 1095 HOH HOH A . 
U 6 HOH 278 678 817  HOH HOH A . 
U 6 HOH 279 679 967  HOH HOH A . 
U 6 HOH 280 680 1100 HOH HOH A . 
V 6 HOH 1   401 974  HOH HOH B . 
V 6 HOH 2   402 697  HOH HOH B . 
V 6 HOH 3   403 1107 HOH HOH B . 
V 6 HOH 4   404 293  HOH HOH B . 
V 6 HOH 5   405 771  HOH HOH B . 
V 6 HOH 6   406 388  HOH HOH B . 
V 6 HOH 7   407 316  HOH HOH B . 
V 6 HOH 8   408 770  HOH HOH B . 
V 6 HOH 9   409 349  HOH HOH B . 
V 6 HOH 10  410 1105 HOH HOH B . 
V 6 HOH 11  411 763  HOH HOH B . 
V 6 HOH 12  412 272  HOH HOH B . 
V 6 HOH 13  413 970  HOH HOH B . 
V 6 HOH 14  414 827  HOH HOH B . 
V 6 HOH 15  415 203  HOH HOH B . 
V 6 HOH 16  416 930  HOH HOH B . 
V 6 HOH 17  417 622  HOH HOH B . 
V 6 HOH 18  418 309  HOH HOH B . 
V 6 HOH 19  419 816  HOH HOH B . 
V 6 HOH 20  420 3    HOH HOH B . 
V 6 HOH 21  421 825  HOH HOH B . 
V 6 HOH 22  422 893  HOH HOH B . 
V 6 HOH 23  423 717  HOH HOH B . 
V 6 HOH 24  424 61   HOH HOH B . 
V 6 HOH 25  425 696  HOH HOH B . 
V 6 HOH 26  426 1054 HOH HOH B . 
V 6 HOH 27  427 499  HOH HOH B . 
V 6 HOH 28  428 468  HOH HOH B . 
V 6 HOH 29  429 73   HOH HOH B . 
V 6 HOH 30  430 56   HOH HOH B . 
V 6 HOH 31  431 784  HOH HOH B . 
V 6 HOH 32  432 1047 HOH HOH B . 
V 6 HOH 33  433 106  HOH HOH B . 
V 6 HOH 34  434 476  HOH HOH B . 
V 6 HOH 35  435 286  HOH HOH B . 
V 6 HOH 36  436 838  HOH HOH B . 
V 6 HOH 37  437 658  HOH HOH B . 
V 6 HOH 38  438 779  HOH HOH B . 
V 6 HOH 39  439 546  HOH HOH B . 
V 6 HOH 40  440 788  HOH HOH B . 
V 6 HOH 41  441 196  HOH HOH B . 
V 6 HOH 42  442 876  HOH HOH B . 
V 6 HOH 43  443 764  HOH HOH B . 
V 6 HOH 44  444 515  HOH HOH B . 
V 6 HOH 45  445 1133 HOH HOH B . 
V 6 HOH 46  446 761  HOH HOH B . 
V 6 HOH 47  447 1046 HOH HOH B . 
V 6 HOH 48  448 254  HOH HOH B . 
V 6 HOH 49  449 593  HOH HOH B . 
V 6 HOH 50  450 1132 HOH HOH B . 
V 6 HOH 51  451 869  HOH HOH B . 
V 6 HOH 52  452 383  HOH HOH B . 
V 6 HOH 53  453 155  HOH HOH B . 
V 6 HOH 54  454 305  HOH HOH B . 
V 6 HOH 55  455 760  HOH HOH B . 
V 6 HOH 56  456 1042 HOH HOH B . 
V 6 HOH 57  457 134  HOH HOH B . 
V 6 HOH 58  458 227  HOH HOH B . 
V 6 HOH 59  459 225  HOH HOH B . 
V 6 HOH 60  460 47   HOH HOH B . 
V 6 HOH 61  461 985  HOH HOH B . 
V 6 HOH 62  462 122  HOH HOH B . 
V 6 HOH 63  463 87   HOH HOH B . 
V 6 HOH 64  464 510  HOH HOH B . 
V 6 HOH 65  465 75   HOH HOH B . 
V 6 HOH 66  466 774  HOH HOH B . 
V 6 HOH 67  467 1043 HOH HOH B . 
V 6 HOH 68  468 497  HOH HOH B . 
V 6 HOH 69  469 98   HOH HOH B . 
V 6 HOH 70  470 614  HOH HOH B . 
V 6 HOH 71  471 498  HOH HOH B . 
V 6 HOH 72  472 121  HOH HOH B . 
V 6 HOH 73  473 347  HOH HOH B . 
V 6 HOH 74  474 209  HOH HOH B . 
V 6 HOH 75  475 829  HOH HOH B . 
V 6 HOH 76  476 432  HOH HOH B . 
V 6 HOH 77  477 640  HOH HOH B . 
V 6 HOH 78  478 85   HOH HOH B . 
V 6 HOH 79  479 154  HOH HOH B . 
V 6 HOH 80  480 738  HOH HOH B . 
V 6 HOH 81  481 648  HOH HOH B . 
V 6 HOH 82  482 488  HOH HOH B . 
V 6 HOH 83  483 723  HOH HOH B . 
V 6 HOH 84  484 489  HOH HOH B . 
V 6 HOH 85  485 25   HOH HOH B . 
V 6 HOH 86  486 562  HOH HOH B . 
V 6 HOH 87  487 699  HOH HOH B . 
V 6 HOH 88  488 197  HOH HOH B . 
V 6 HOH 89  489 12   HOH HOH B . 
V 6 HOH 90  490 46   HOH HOH B . 
V 6 HOH 91  491 1041 HOH HOH B . 
V 6 HOH 92  492 175  HOH HOH B . 
V 6 HOH 93  493 1055 HOH HOH B . 
V 6 HOH 94  494 927  HOH HOH B . 
V 6 HOH 95  495 292  HOH HOH B . 
V 6 HOH 96  496 500  HOH HOH B . 
V 6 HOH 97  497 89   HOH HOH B . 
V 6 HOH 98  498 365  HOH HOH B . 
V 6 HOH 99  499 34   HOH HOH B . 
V 6 HOH 100 500 565  HOH HOH B . 
V 6 HOH 101 501 550  HOH HOH B . 
V 6 HOH 102 502 524  HOH HOH B . 
V 6 HOH 103 503 490  HOH HOH B . 
V 6 HOH 104 504 669  HOH HOH B . 
V 6 HOH 105 505 513  HOH HOH B . 
V 6 HOH 106 506 911  HOH HOH B . 
V 6 HOH 107 507 49   HOH HOH B . 
V 6 HOH 108 508 101  HOH HOH B . 
V 6 HOH 109 509 972  HOH HOH B . 
V 6 HOH 110 510 186  HOH HOH B . 
V 6 HOH 111 511 1141 HOH HOH B . 
V 6 HOH 112 512 246  HOH HOH B . 
V 6 HOH 113 513 644  HOH HOH B . 
V 6 HOH 114 514 187  HOH HOH B . 
V 6 HOH 115 515 321  HOH HOH B . 
V 6 HOH 116 516 91   HOH HOH B . 
V 6 HOH 117 517 422  HOH HOH B . 
V 6 HOH 118 518 441  HOH HOH B . 
V 6 HOH 119 519 92   HOH HOH B . 
V 6 HOH 120 520 712  HOH HOH B . 
V 6 HOH 121 521 543  HOH HOH B . 
V 6 HOH 122 522 976  HOH HOH B . 
V 6 HOH 123 523 782  HOH HOH B . 
V 6 HOH 124 524 1040 HOH HOH B . 
V 6 HOH 125 525 314  HOH HOH B . 
V 6 HOH 126 526 158  HOH HOH B . 
V 6 HOH 127 527 692  HOH HOH B . 
V 6 HOH 128 528 51   HOH HOH B . 
V 6 HOH 129 529 1048 HOH HOH B . 
V 6 HOH 130 530 495  HOH HOH B . 
V 6 HOH 131 531 798  HOH HOH B . 
V 6 HOH 132 532 433  HOH HOH B . 
V 6 HOH 133 533 1110 HOH HOH B . 
V 6 HOH 134 534 570  HOH HOH B . 
V 6 HOH 135 535 123  HOH HOH B . 
V 6 HOH 136 536 231  HOH HOH B . 
V 6 HOH 137 537 129  HOH HOH B . 
V 6 HOH 138 538 19   HOH HOH B . 
V 6 HOH 139 539 65   HOH HOH B . 
V 6 HOH 140 540 592  HOH HOH B . 
V 6 HOH 141 541 757  HOH HOH B . 
V 6 HOH 142 542 596  HOH HOH B . 
V 6 HOH 143 543 58   HOH HOH B . 
V 6 HOH 144 544 576  HOH HOH B . 
V 6 HOH 145 545 597  HOH HOH B . 
V 6 HOH 146 546 434  HOH HOH B . 
V 6 HOH 147 547 139  HOH HOH B . 
V 6 HOH 148 548 511  HOH HOH B . 
V 6 HOH 149 549 243  HOH HOH B . 
V 6 HOH 150 550 574  HOH HOH B . 
V 6 HOH 151 551 105  HOH HOH B . 
V 6 HOH 152 552 1140 HOH HOH B . 
V 6 HOH 153 553 142  HOH HOH B . 
V 6 HOH 154 554 1052 HOH HOH B . 
V 6 HOH 155 555 68   HOH HOH B . 
V 6 HOH 156 556 244  HOH HOH B . 
V 6 HOH 157 557 523  HOH HOH B . 
V 6 HOH 158 558 458  HOH HOH B . 
V 6 HOH 159 559 405  HOH HOH B . 
V 6 HOH 160 560 980  HOH HOH B . 
V 6 HOH 161 561 410  HOH HOH B . 
V 6 HOH 162 562 535  HOH HOH B . 
V 6 HOH 163 563 569  HOH HOH B . 
V 6 HOH 164 564 553  HOH HOH B . 
V 6 HOH 165 565 43   HOH HOH B . 
V 6 HOH 166 566 21   HOH HOH B . 
V 6 HOH 167 567 983  HOH HOH B . 
V 6 HOH 168 568 222  HOH HOH B . 
V 6 HOH 169 569 176  HOH HOH B . 
V 6 HOH 170 570 797  HOH HOH B . 
V 6 HOH 171 571 253  HOH HOH B . 
V 6 HOH 172 572 81   HOH HOH B . 
V 6 HOH 173 573 698  HOH HOH B . 
V 6 HOH 174 574 928  HOH HOH B . 
V 6 HOH 175 575 86   HOH HOH B . 
V 6 HOH 176 576 977  HOH HOH B . 
V 6 HOH 177 577 762  HOH HOH B . 
V 6 HOH 178 578 454  HOH HOH B . 
V 6 HOH 179 579 534  HOH HOH B . 
V 6 HOH 180 580 781  HOH HOH B . 
V 6 HOH 181 581 283  HOH HOH B . 
V 6 HOH 182 582 493  HOH HOH B . 
V 6 HOH 183 583 448  HOH HOH B . 
V 6 HOH 184 584 195  HOH HOH B . 
V 6 HOH 185 585 624  HOH HOH B . 
V 6 HOH 186 586 401  HOH HOH B . 
V 6 HOH 187 587 856  HOH HOH B . 
V 6 HOH 188 588 512  HOH HOH B . 
V 6 HOH 189 589 136  HOH HOH B . 
V 6 HOH 190 590 384  HOH HOH B . 
V 6 HOH 191 591 324  HOH HOH B . 
V 6 HOH 192 592 171  HOH HOH B . 
V 6 HOH 193 593 528  HOH HOH B . 
V 6 HOH 194 594 381  HOH HOH B . 
V 6 HOH 195 595 317  HOH HOH B . 
V 6 HOH 196 596 509  HOH HOH B . 
V 6 HOH 197 597 407  HOH HOH B . 
V 6 HOH 198 598 913  HOH HOH B . 
V 6 HOH 199 599 1025 HOH HOH B . 
V 6 HOH 200 600 522  HOH HOH B . 
V 6 HOH 201 601 94   HOH HOH B . 
V 6 HOH 202 602 242  HOH HOH B . 
V 6 HOH 203 603 661  HOH HOH B . 
V 6 HOH 204 604 319  HOH HOH B . 
V 6 HOH 205 605 352  HOH HOH B . 
V 6 HOH 206 606 643  HOH HOH B . 
V 6 HOH 207 607 540  HOH HOH B . 
V 6 HOH 208 608 1035 HOH HOH B . 
V 6 HOH 209 609 866  HOH HOH B . 
V 6 HOH 210 610 837  HOH HOH B . 
V 6 HOH 211 611 1136 HOH HOH B . 
V 6 HOH 212 612 573  HOH HOH B . 
V 6 HOH 213 613 881  HOH HOH B . 
V 6 HOH 214 614 731  HOH HOH B . 
V 6 HOH 215 615 162  HOH HOH B . 
V 6 HOH 216 616 398  HOH HOH B . 
V 6 HOH 217 617 843  HOH HOH B . 
V 6 HOH 218 618 637  HOH HOH B . 
V 6 HOH 219 619 1051 HOH HOH B . 
V 6 HOH 220 620 554  HOH HOH B . 
V 6 HOH 221 621 739  HOH HOH B . 
V 6 HOH 222 622 602  HOH HOH B . 
V 6 HOH 223 623 706  HOH HOH B . 
V 6 HOH 224 624 934  HOH HOH B . 
V 6 HOH 225 625 651  HOH HOH B . 
V 6 HOH 226 626 684  HOH HOH B . 
V 6 HOH 227 627 978  HOH HOH B . 
V 6 HOH 228 628 982  HOH HOH B . 
V 6 HOH 229 629 281  HOH HOH B . 
V 6 HOH 230 630 463  HOH HOH B . 
V 6 HOH 231 631 636  HOH HOH B . 
V 6 HOH 232 632 938  HOH HOH B . 
V 6 HOH 233 633 616  HOH HOH B . 
V 6 HOH 234 634 1037 HOH HOH B . 
V 6 HOH 235 635 676  HOH HOH B . 
V 6 HOH 236 636 586  HOH HOH B . 
V 6 HOH 237 637 848  HOH HOH B . 
V 6 HOH 238 638 981  HOH HOH B . 
V 6 HOH 239 639 567  HOH HOH B . 
V 6 HOH 240 640 258  HOH HOH B . 
V 6 HOH 241 641 889  HOH HOH B . 
V 6 HOH 242 642 548  HOH HOH B . 
V 6 HOH 243 643 854  HOH HOH B . 
V 6 HOH 244 644 839  HOH HOH B . 
V 6 HOH 245 645 417  HOH HOH B . 
V 6 HOH 246 646 315  HOH HOH B . 
V 6 HOH 247 647 811  HOH HOH B . 
V 6 HOH 248 648 918  HOH HOH B . 
V 6 HOH 249 649 436  HOH HOH B . 
V 6 HOH 250 650 667  HOH HOH B . 
V 6 HOH 251 651 226  HOH HOH B . 
V 6 HOH 252 652 935  HOH HOH B . 
V 6 HOH 253 653 379  HOH HOH B . 
V 6 HOH 254 654 1045 HOH HOH B . 
V 6 HOH 255 655 755  HOH HOH B . 
V 6 HOH 256 656 796  HOH HOH B . 
V 6 HOH 257 657 581  HOH HOH B . 
V 6 HOH 258 658 472  HOH HOH B . 
V 6 HOH 259 659 1053 HOH HOH B . 
V 6 HOH 260 660 841  HOH HOH B . 
V 6 HOH 261 661 872  HOH HOH B . 
V 6 HOH 262 662 973  HOH HOH B . 
V 6 HOH 263 663 853  HOH HOH B . 
V 6 HOH 264 664 542  HOH HOH B . 
V 6 HOH 265 665 828  HOH HOH B . 
V 6 HOH 266 666 220  HOH HOH B . 
V 6 HOH 267 667 239  HOH HOH B . 
V 6 HOH 268 668 610  HOH HOH B . 
V 6 HOH 269 669 247  HOH HOH B . 
V 6 HOH 270 670 880  HOH HOH B . 
V 6 HOH 271 671 1044 HOH HOH B . 
V 6 HOH 272 672 890  HOH HOH B . 
V 6 HOH 273 673 216  HOH HOH B . 
V 6 HOH 274 674 850  HOH HOH B . 
V 6 HOH 275 675 979  HOH HOH B . 
V 6 HOH 276 676 833  HOH HOH B . 
V 6 HOH 277 677 873  HOH HOH B . 
V 6 HOH 278 678 756  HOH HOH B . 
V 6 HOH 279 679 799  HOH HOH B . 
V 6 HOH 280 680 901  HOH HOH B . 
V 6 HOH 281 681 393  HOH HOH B . 
V 6 HOH 282 682 700  HOH HOH B . 
V 6 HOH 283 683 605  HOH HOH B . 
V 6 HOH 284 684 753  HOH HOH B . 
V 6 HOH 285 685 847  HOH HOH B . 
V 6 HOH 286 686 660  HOH HOH B . 
V 6 HOH 287 687 333  HOH HOH B . 
V 6 HOH 288 688 984  HOH HOH B . 
V 6 HOH 289 689 831  HOH HOH B . 
V 6 HOH 290 690 635  HOH HOH B . 
V 6 HOH 291 691 836  HOH HOH B . 
V 6 HOH 292 692 1109 HOH HOH B . 
V 6 HOH 293 693 325  HOH HOH B . 
V 6 HOH 294 694 971  HOH HOH B . 
V 6 HOH 295 695 1106 HOH HOH B . 
V 6 HOH 296 696 1099 HOH HOH B . 
V 6 HOH 297 697 276  HOH HOH B . 
V 6 HOH 298 698 716  HOH HOH B . 
V 6 HOH 299 699 1103 HOH HOH B . 
V 6 HOH 300 700 478  HOH HOH B . 
V 6 HOH 301 701 929  HOH HOH B . 
V 6 HOH 302 702 1049 HOH HOH B . 
V 6 HOH 303 703 618  HOH HOH B . 
V 6 HOH 304 704 670  HOH HOH B . 
V 6 HOH 305 705 634  HOH HOH B . 
V 6 HOH 306 706 975  HOH HOH B . 
V 6 HOH 307 707 1101 HOH HOH B . 
V 6 HOH 308 708 907  HOH HOH B . 
V 6 HOH 309 709 986  HOH HOH B . 
V 6 HOH 310 710 1108 HOH HOH B . 
V 6 HOH 311 711 747  HOH HOH B . 
V 6 HOH 312 712 1102 HOH HOH B . 
V 6 HOH 313 713 1104 HOH HOH B . 
W 6 HOH 1   401 557  HOH HOH C . 
W 6 HOH 2   402 726  HOH HOH C . 
W 6 HOH 3   403 820  HOH HOH C . 
W 6 HOH 4   404 289  HOH HOH C . 
W 6 HOH 5   405 374  HOH HOH C . 
W 6 HOH 6   406 414  HOH HOH C . 
W 6 HOH 7   407 924  HOH HOH C . 
W 6 HOH 8   408 818  HOH HOH C . 
W 6 HOH 9   409 180  HOH HOH C . 
W 6 HOH 10  410 894  HOH HOH C . 
W 6 HOH 11  411 615  HOH HOH C . 
W 6 HOH 12  412 412  HOH HOH C . 
W 6 HOH 13  413 994  HOH HOH C . 
W 6 HOH 14  414 834  HOH HOH C . 
W 6 HOH 15  415 767  HOH HOH C . 
W 6 HOH 16  416 1057 HOH HOH C . 
W 6 HOH 17  417 1120 HOH HOH C . 
W 6 HOH 18  418 224  HOH HOH C . 
W 6 HOH 19  419 408  HOH HOH C . 
W 6 HOH 20  420 585  HOH HOH C . 
W 6 HOH 21  421 44   HOH HOH C . 
W 6 HOH 22  422 897  HOH HOH C . 
W 6 HOH 23  423 4    HOH HOH C . 
W 6 HOH 24  424 860  HOH HOH C . 
W 6 HOH 25  425 70   HOH HOH C . 
W 6 HOH 26  426 356  HOH HOH C . 
W 6 HOH 27  427 745  HOH HOH C . 
W 6 HOH 28  428 152  HOH HOH C . 
W 6 HOH 29  429 715  HOH HOH C . 
W 6 HOH 30  430 173  HOH HOH C . 
W 6 HOH 31  431 372  HOH HOH C . 
W 6 HOH 32  432 409  HOH HOH C . 
W 6 HOH 33  433 399  HOH HOH C . 
W 6 HOH 34  434 288  HOH HOH C . 
W 6 HOH 35  435 328  HOH HOH C . 
W 6 HOH 36  436 167  HOH HOH C . 
W 6 HOH 37  437 156  HOH HOH C . 
W 6 HOH 38  438 733  HOH HOH C . 
W 6 HOH 39  439 95   HOH HOH C . 
W 6 HOH 40  440 200  HOH HOH C . 
W 6 HOH 41  441 210  HOH HOH C . 
W 6 HOH 42  442 193  HOH HOH C . 
W 6 HOH 43  443 791  HOH HOH C . 
W 6 HOH 44  444 362  HOH HOH C . 
W 6 HOH 45  445 63   HOH HOH C . 
W 6 HOH 46  446 527  HOH HOH C . 
W 6 HOH 47  447 840  HOH HOH C . 
W 6 HOH 48  448 1073 HOH HOH C . 
W 6 HOH 49  449 1071 HOH HOH C . 
W 6 HOH 50  450 694  HOH HOH C . 
W 6 HOH 51  451 261  HOH HOH C . 
W 6 HOH 52  452 864  HOH HOH C . 
W 6 HOH 53  453 80   HOH HOH C . 
W 6 HOH 54  454 218  HOH HOH C . 
W 6 HOH 55  455 423  HOH HOH C . 
W 6 HOH 56  456 773  HOH HOH C . 
W 6 HOH 57  457 79   HOH HOH C . 
W 6 HOH 58  458 709  HOH HOH C . 
W 6 HOH 59  459 178  HOH HOH C . 
W 6 HOH 60  460 395  HOH HOH C . 
W 6 HOH 61  461 1065 HOH HOH C . 
W 6 HOH 62  462 2    HOH HOH C . 
W 6 HOH 63  463 641  HOH HOH C . 
W 6 HOH 64  464 259  HOH HOH C . 
W 6 HOH 65  465 257  HOH HOH C . 
W 6 HOH 66  466 33   HOH HOH C . 
W 6 HOH 67  467 285  HOH HOH C . 
W 6 HOH 68  468 31   HOH HOH C . 
W 6 HOH 69  469 1067 HOH HOH C . 
W 6 HOH 70  470 680  HOH HOH C . 
W 6 HOH 71  471 789  HOH HOH C . 
W 6 HOH 72  472 989  HOH HOH C . 
W 6 HOH 73  473 202  HOH HOH C . 
W 6 HOH 74  474 645  HOH HOH C . 
W 6 HOH 75  475 57   HOH HOH C . 
W 6 HOH 76  476 213  HOH HOH C . 
W 6 HOH 77  477 188  HOH HOH C . 
W 6 HOH 78  478 145  HOH HOH C . 
W 6 HOH 79  479 446  HOH HOH C . 
W 6 HOH 80  480 400  HOH HOH C . 
W 6 HOH 81  481 858  HOH HOH C . 
W 6 HOH 82  482 120  HOH HOH C . 
W 6 HOH 83  483 312  HOH HOH C . 
W 6 HOH 84  484 396  HOH HOH C . 
W 6 HOH 85  485 844  HOH HOH C . 
W 6 HOH 86  486 870  HOH HOH C . 
W 6 HOH 87  487 284  HOH HOH C . 
W 6 HOH 88  488 642  HOH HOH C . 
W 6 HOH 89  489 48   HOH HOH C . 
W 6 HOH 90  490 821  HOH HOH C . 
W 6 HOH 91  491 7    HOH HOH C . 
W 6 HOH 92  492 266  HOH HOH C . 
W 6 HOH 93  493 119  HOH HOH C . 
W 6 HOH 94  494 221  HOH HOH C . 
W 6 HOH 95  495 925  HOH HOH C . 
W 6 HOH 96  496 39   HOH HOH C . 
W 6 HOH 97  497 1115 HOH HOH C . 
W 6 HOH 98  498 230  HOH HOH C . 
W 6 HOH 99  499 411  HOH HOH C . 
W 6 HOH 100 500 851  HOH HOH C . 
W 6 HOH 101 501 394  HOH HOH C . 
W 6 HOH 102 502 60   HOH HOH C . 
W 6 HOH 103 503 428  HOH HOH C . 
W 6 HOH 104 504 450  HOH HOH C . 
W 6 HOH 105 505 619  HOH HOH C . 
W 6 HOH 106 506 15   HOH HOH C . 
W 6 HOH 107 507 287  HOH HOH C . 
W 6 HOH 108 508 355  HOH HOH C . 
W 6 HOH 109 509 146  HOH HOH C . 
W 6 HOH 110 510 895  HOH HOH C . 
W 6 HOH 111 511 598  HOH HOH C . 
W 6 HOH 112 512 262  HOH HOH C . 
W 6 HOH 113 513 115  HOH HOH C . 
W 6 HOH 114 514 82   HOH HOH C . 
W 6 HOH 115 515 164  HOH HOH C . 
W 6 HOH 116 516 168  HOH HOH C . 
W 6 HOH 117 517 993  HOH HOH C . 
W 6 HOH 118 518 361  HOH HOH C . 
W 6 HOH 119 519 659  HOH HOH C . 
W 6 HOH 120 520 37   HOH HOH C . 
W 6 HOH 121 521 638  HOH HOH C . 
W 6 HOH 122 522 212  HOH HOH C . 
W 6 HOH 123 523 430  HOH HOH C . 
W 6 HOH 124 524 359  HOH HOH C . 
W 6 HOH 125 525 744  HOH HOH C . 
W 6 HOH 126 526 282  HOH HOH C . 
W 6 HOH 127 527 701  HOH HOH C . 
W 6 HOH 128 528 1059 HOH HOH C . 
W 6 HOH 129 529 1079 HOH HOH C . 
W 6 HOH 130 530 390  HOH HOH C . 
W 6 HOH 131 531 42   HOH HOH C . 
W 6 HOH 132 532 921  HOH HOH C . 
W 6 HOH 133 533 72   HOH HOH C . 
W 6 HOH 134 534 545  HOH HOH C . 
W 6 HOH 135 535 24   HOH HOH C . 
W 6 HOH 136 536 688  HOH HOH C . 
W 6 HOH 137 537 252  HOH HOH C . 
W 6 HOH 138 538 732  HOH HOH C . 
W 6 HOH 139 539 313  HOH HOH C . 
W 6 HOH 140 540 278  HOH HOH C . 
W 6 HOH 141 541 679  HOH HOH C . 
W 6 HOH 142 542 163  HOH HOH C . 
W 6 HOH 143 543 600  HOH HOH C . 
W 6 HOH 144 544 888  HOH HOH C . 
W 6 HOH 145 545 376  HOH HOH C . 
W 6 HOH 146 546 369  HOH HOH C . 
W 6 HOH 147 547 577  HOH HOH C . 
W 6 HOH 148 548 995  HOH HOH C . 
W 6 HOH 149 549 304  HOH HOH C . 
W 6 HOH 150 550 859  HOH HOH C . 
W 6 HOH 151 551 804  HOH HOH C . 
W 6 HOH 152 552 346  HOH HOH C . 
W 6 HOH 153 553 1068 HOH HOH C . 
W 6 HOH 154 554 992  HOH HOH C . 
W 6 HOH 155 555 470  HOH HOH C . 
W 6 HOH 156 556 675  HOH HOH C . 
W 6 HOH 157 557 1116 HOH HOH C . 
W 6 HOH 158 558 367  HOH HOH C . 
W 6 HOH 159 559 351  HOH HOH C . 
W 6 HOH 160 560 214  HOH HOH C . 
W 6 HOH 161 561 583  HOH HOH C . 
W 6 HOH 162 562 1070 HOH HOH C . 
W 6 HOH 163 563 794  HOH HOH C . 
W 6 HOH 164 564 471  HOH HOH C . 
W 6 HOH 165 565 480  HOH HOH C . 
W 6 HOH 166 566 1069 HOH HOH C . 
W 6 HOH 167 567 997  HOH HOH C . 
W 6 HOH 168 568 147  HOH HOH C . 
W 6 HOH 169 569 582  HOH HOH C . 
W 6 HOH 170 570 473  HOH HOH C . 
W 6 HOH 171 571 923  HOH HOH C . 
W 6 HOH 172 572 678  HOH HOH C . 
W 6 HOH 173 573 687  HOH HOH C . 
W 6 HOH 174 574 806  HOH HOH C . 
W 6 HOH 175 575 1111 HOH HOH C . 
W 6 HOH 176 576 375  HOH HOH C . 
W 6 HOH 177 577 862  HOH HOH C . 
W 6 HOH 178 578 730  HOH HOH C . 
W 6 HOH 179 579 1061 HOH HOH C . 
W 6 HOH 180 580 672  HOH HOH C . 
W 6 HOH 181 581 464  HOH HOH C . 
W 6 HOH 182 582 617  HOH HOH C . 
W 6 HOH 183 583 609  HOH HOH C . 
W 6 HOH 184 584 1118 HOH HOH C . 
W 6 HOH 185 585 685  HOH HOH C . 
W 6 HOH 186 586 1074 HOH HOH C . 
W 6 HOH 187 587 1112 HOH HOH C . 
W 6 HOH 188 588 327  HOH HOH C . 
W 6 HOH 189 589 1064 HOH HOH C . 
W 6 HOH 190 590 999  HOH HOH C . 
W 6 HOH 191 591 996  HOH HOH C . 
W 6 HOH 192 592 922  HOH HOH C . 
W 6 HOH 193 593 1117 HOH HOH C . 
W 6 HOH 194 594 1119 HOH HOH C . 
W 6 HOH 195 595 1063 HOH HOH C . 
W 6 HOH 196 596 460  HOH HOH C . 
W 6 HOH 197 597 808  HOH HOH C . 
W 6 HOH 198 598 1075 HOH HOH C . 
W 6 HOH 199 599 903  HOH HOH C . 
W 6 HOH 200 600 1060 HOH HOH C . 
W 6 HOH 201 601 909  HOH HOH C . 
W 6 HOH 202 602 447  HOH HOH C . 
W 6 HOH 203 603 591  HOH HOH C . 
W 6 HOH 204 604 783  HOH HOH C . 
W 6 HOH 205 605 1062 HOH HOH C . 
W 6 HOH 206 606 1072 HOH HOH C . 
W 6 HOH 207 607 482  HOH HOH C . 
W 6 HOH 208 608 654  HOH HOH C . 
W 6 HOH 209 609 442  HOH HOH C . 
W 6 HOH 210 610 1058 HOH HOH C . 
W 6 HOH 211 611 768  HOH HOH C . 
W 6 HOH 212 612 988  HOH HOH C . 
W 6 HOH 213 613 1114 HOH HOH C . 
W 6 HOH 214 614 775  HOH HOH C . 
W 6 HOH 215 615 849  HOH HOH C . 
W 6 HOH 216 616 1137 HOH HOH C . 
W 6 HOH 217 617 990  HOH HOH C . 
W 6 HOH 218 618 1056 HOH HOH C . 
W 6 HOH 219 619 835  HOH HOH C . 
W 6 HOH 220 620 720  HOH HOH C . 
W 6 HOH 221 621 1113 HOH HOH C . 
X 6 HOH 1   401 53   HOH HOH D . 
X 6 HOH 2   402 234  HOH HOH D . 
X 6 HOH 3   403 623  HOH HOH D . 
X 6 HOH 4   404 516  HOH HOH D . 
X 6 HOH 5   405 357  HOH HOH D . 
X 6 HOH 6   406 1131 HOH HOH D . 
X 6 HOH 7   407 418  HOH HOH D . 
X 6 HOH 8   408 729  HOH HOH D . 
X 6 HOH 9   409 306  HOH HOH D . 
X 6 HOH 10  410 906  HOH HOH D . 
X 6 HOH 11  411 457  HOH HOH D . 
X 6 HOH 12  412 1090 HOH HOH D . 
X 6 HOH 13  413 5    HOH HOH D . 
X 6 HOH 14  414 114  HOH HOH D . 
X 6 HOH 15  415 84   HOH HOH D . 
X 6 HOH 16  416 41   HOH HOH D . 
X 6 HOH 17  417 826  HOH HOH D . 
X 6 HOH 18  418 153  HOH HOH D . 
X 6 HOH 19  419 621  HOH HOH D . 
X 6 HOH 20  420 126  HOH HOH D . 
X 6 HOH 21  421 256  HOH HOH D . 
X 6 HOH 22  422 453  HOH HOH D . 
X 6 HOH 23  423 1005 HOH HOH D . 
X 6 HOH 24  424 852  HOH HOH D . 
X 6 HOH 25  425 671  HOH HOH D . 
X 6 HOH 26  426 54   HOH HOH D . 
X 6 HOH 27  427 17   HOH HOH D . 
X 6 HOH 28  428 882  HOH HOH D . 
X 6 HOH 29  429 693  HOH HOH D . 
X 6 HOH 30  430 415  HOH HOH D . 
X 6 HOH 31  431 1126 HOH HOH D . 
X 6 HOH 32  432 1003 HOH HOH D . 
X 6 HOH 33  433 885  HOH HOH D . 
X 6 HOH 34  434 702  HOH HOH D . 
X 6 HOH 35  435 902  HOH HOH D . 
X 6 HOH 36  436 406  HOH HOH D . 
X 6 HOH 37  437 240  HOH HOH D . 
X 6 HOH 38  438 754  HOH HOH D . 
X 6 HOH 39  439 343  HOH HOH D . 
X 6 HOH 40  440 117  HOH HOH D . 
X 6 HOH 41  441 52   HOH HOH D . 
X 6 HOH 42  442 631  HOH HOH D . 
X 6 HOH 43  443 348  HOH HOH D . 
X 6 HOH 44  444 1129 HOH HOH D . 
X 6 HOH 45  445 587  HOH HOH D . 
X 6 HOH 46  446 891  HOH HOH D . 
X 6 HOH 47  447 632  HOH HOH D . 
X 6 HOH 48  448 50   HOH HOH D . 
X 6 HOH 49  449 1066 HOH HOH D . 
X 6 HOH 50  450 190  HOH HOH D . 
X 6 HOH 51  451 137  HOH HOH D . 
X 6 HOH 52  452 785  HOH HOH D . 
X 6 HOH 53  453 1008 HOH HOH D . 
X 6 HOH 54  454 719  HOH HOH D . 
X 6 HOH 55  455 364  HOH HOH D . 
X 6 HOH 56  456 429  HOH HOH D . 
X 6 HOH 57  457 192  HOH HOH D . 
X 6 HOH 58  458 765  HOH HOH D . 
X 6 HOH 59  459 55   HOH HOH D . 
X 6 HOH 60  460 541  HOH HOH D . 
X 6 HOH 61  461 385  HOH HOH D . 
X 6 HOH 62  462 40   HOH HOH D . 
X 6 HOH 63  463 1124 HOH HOH D . 
X 6 HOH 64  464 780  HOH HOH D . 
X 6 HOH 65  465 294  HOH HOH D . 
X 6 HOH 66  466 110  HOH HOH D . 
X 6 HOH 67  467 140  HOH HOH D . 
X 6 HOH 68  468 232  HOH HOH D . 
X 6 HOH 69  469 920  HOH HOH D . 
X 6 HOH 70  470 11   HOH HOH D . 
X 6 HOH 71  471 28   HOH HOH D . 
X 6 HOH 72  472 752  HOH HOH D . 
X 6 HOH 73  473 59   HOH HOH D . 
X 6 HOH 74  474 26   HOH HOH D . 
X 6 HOH 75  475 118  HOH HOH D . 
X 6 HOH 76  476 174  HOH HOH D . 
X 6 HOH 77  477 728  HOH HOH D . 
X 6 HOH 78  478 270  HOH HOH D . 
X 6 HOH 79  479 14   HOH HOH D . 
X 6 HOH 80  480 908  HOH HOH D . 
X 6 HOH 81  481 165  HOH HOH D . 
X 6 HOH 82  482 45   HOH HOH D . 
X 6 HOH 83  483 277  HOH HOH D . 
X 6 HOH 84  484 182  HOH HOH D . 
X 6 HOH 85  485 251  HOH HOH D . 
X 6 HOH 86  486 440  HOH HOH D . 
X 6 HOH 87  487 90   HOH HOH D . 
X 6 HOH 88  488 198  HOH HOH D . 
X 6 HOH 89  489 392  HOH HOH D . 
X 6 HOH 90  490 189  HOH HOH D . 
X 6 HOH 91  491 803  HOH HOH D . 
X 6 HOH 92  492 108  HOH HOH D . 
X 6 HOH 93  493 148  HOH HOH D . 
X 6 HOH 94  494 340  HOH HOH D . 
X 6 HOH 95  495 461  HOH HOH D . 
X 6 HOH 96  496 331  HOH HOH D . 
X 6 HOH 97  497 822  HOH HOH D . 
X 6 HOH 98  498 97   HOH HOH D . 
X 6 HOH 99  499 330  HOH HOH D . 
X 6 HOH 100 500 228  HOH HOH D . 
X 6 HOH 101 501 435  HOH HOH D . 
X 6 HOH 102 502 437  HOH HOH D . 
X 6 HOH 103 503 300  HOH HOH D . 
X 6 HOH 104 504 249  HOH HOH D . 
X 6 HOH 105 505 354  HOH HOH D . 
X 6 HOH 106 506 69   HOH HOH D . 
X 6 HOH 107 507 88   HOH HOH D . 
X 6 HOH 108 508 13   HOH HOH D . 
X 6 HOH 109 509 10   HOH HOH D . 
X 6 HOH 110 510 681  HOH HOH D . 
X 6 HOH 111 511 905  HOH HOH D . 
X 6 HOH 112 512 560  HOH HOH D . 
X 6 HOH 113 513 625  HOH HOH D . 
X 6 HOH 114 514 30   HOH HOH D . 
X 6 HOH 115 515 353  HOH HOH D . 
X 6 HOH 116 516 64   HOH HOH D . 
X 6 HOH 117 517 899  HOH HOH D . 
X 6 HOH 118 518 161  HOH HOH D . 
X 6 HOH 119 519 311  HOH HOH D . 
X 6 HOH 120 520 914  HOH HOH D . 
X 6 HOH 121 521 360  HOH HOH D . 
X 6 HOH 122 522 431  HOH HOH D . 
X 6 HOH 123 523 141  HOH HOH D . 
X 6 HOH 124 524 29   HOH HOH D . 
X 6 HOH 125 525 22   HOH HOH D . 
X 6 HOH 126 526 413  HOH HOH D . 
X 6 HOH 127 527 265  HOH HOH D . 
X 6 HOH 128 528 318  HOH HOH D . 
X 6 HOH 129 529 421  HOH HOH D . 
X 6 HOH 130 530 778  HOH HOH D . 
X 6 HOH 131 531 112  HOH HOH D . 
X 6 HOH 132 532 875  HOH HOH D . 
X 6 HOH 133 533 107  HOH HOH D . 
X 6 HOH 134 534 370  HOH HOH D . 
X 6 HOH 135 535 871  HOH HOH D . 
X 6 HOH 136 536 878  HOH HOH D . 
X 6 HOH 137 537 420  HOH HOH D . 
X 6 HOH 138 538 691  HOH HOH D . 
X 6 HOH 139 539 380  HOH HOH D . 
X 6 HOH 140 540 776  HOH HOH D . 
X 6 HOH 141 541 260  HOH HOH D . 
X 6 HOH 142 542 74   HOH HOH D . 
X 6 HOH 143 543 160  HOH HOH D . 
X 6 HOH 144 544 201  HOH HOH D . 
X 6 HOH 145 545 116  HOH HOH D . 
X 6 HOH 146 546 109  HOH HOH D . 
X 6 HOH 147 547 235  HOH HOH D . 
X 6 HOH 148 548 127  HOH HOH D . 
X 6 HOH 149 549 236  HOH HOH D . 
X 6 HOH 150 550 563  HOH HOH D . 
X 6 HOH 151 551 322  HOH HOH D . 
X 6 HOH 152 552 663  HOH HOH D . 
X 6 HOH 153 553 727  HOH HOH D . 
X 6 HOH 154 554 93   HOH HOH D . 
X 6 HOH 155 555 653  HOH HOH D . 
X 6 HOH 156 556 742  HOH HOH D . 
X 6 HOH 157 557 211  HOH HOH D . 
X 6 HOH 158 558 151  HOH HOH D . 
X 6 HOH 159 559 748  HOH HOH D . 
X 6 HOH 160 560 241  HOH HOH D . 
X 6 HOH 161 561 184  HOH HOH D . 
X 6 HOH 162 562 649  HOH HOH D . 
X 6 HOH 163 563 20   HOH HOH D . 
X 6 HOH 164 564 291  HOH HOH D . 
X 6 HOH 165 565 656  HOH HOH D . 
X 6 HOH 166 566 608  HOH HOH D . 
X 6 HOH 167 567 267  HOH HOH D . 
X 6 HOH 168 568 382  HOH HOH D . 
X 6 HOH 169 569 296  HOH HOH D . 
X 6 HOH 170 570 677  HOH HOH D . 
X 6 HOH 171 571 219  HOH HOH D . 
X 6 HOH 172 572 99   HOH HOH D . 
X 6 HOH 173 573 194  HOH HOH D . 
X 6 HOH 174 574 274  HOH HOH D . 
X 6 HOH 175 575 185  HOH HOH D . 
X 6 HOH 176 576 9    HOH HOH D . 
X 6 HOH 177 577 772  HOH HOH D . 
X 6 HOH 178 578 204  HOH HOH D . 
X 6 HOH 179 579 62   HOH HOH D . 
X 6 HOH 180 580 297  HOH HOH D . 
X 6 HOH 181 581 144  HOH HOH D . 
X 6 HOH 182 582 455  HOH HOH D . 
X 6 HOH 183 583 736  HOH HOH D . 
X 6 HOH 184 584 279  HOH HOH D . 
X 6 HOH 185 585 307  HOH HOH D . 
X 6 HOH 186 586 802  HOH HOH D . 
X 6 HOH 187 587 206  HOH HOH D . 
X 6 HOH 188 588 404  HOH HOH D . 
X 6 HOH 189 589 1139 HOH HOH D . 
X 6 HOH 190 590 452  HOH HOH D . 
X 6 HOH 191 591 883  HOH HOH D . 
X 6 HOH 192 592 1130 HOH HOH D . 
X 6 HOH 193 593 172  HOH HOH D . 
X 6 HOH 194 594 6    HOH HOH D . 
X 6 HOH 195 595 223  HOH HOH D . 
X 6 HOH 196 596 179  HOH HOH D . 
X 6 HOH 197 597 575  HOH HOH D . 
X 6 HOH 198 598 378  HOH HOH D . 
X 6 HOH 199 599 131  HOH HOH D . 
X 6 HOH 200 600 445  HOH HOH D . 
X 6 HOH 201 601 159  HOH HOH D . 
X 6 HOH 202 602 475  HOH HOH D . 
X 6 HOH 203 603 389  HOH HOH D . 
X 6 HOH 204 604 303  HOH HOH D . 
X 6 HOH 205 605 100  HOH HOH D . 
X 6 HOH 206 606 786  HOH HOH D . 
X 6 HOH 207 607 299  HOH HOH D . 
X 6 HOH 208 608 537  HOH HOH D . 
X 6 HOH 209 609 424  HOH HOH D . 
X 6 HOH 210 610 149  HOH HOH D . 
X 6 HOH 211 611 823  HOH HOH D . 
X 6 HOH 212 612 336  HOH HOH D . 
X 6 HOH 213 613 104  HOH HOH D . 
X 6 HOH 214 614 302  HOH HOH D . 
X 6 HOH 215 615 721  HOH HOH D . 
X 6 HOH 216 616 83   HOH HOH D . 
X 6 HOH 217 617 245  HOH HOH D . 
X 6 HOH 218 618 133  HOH HOH D . 
X 6 HOH 219 619 157  HOH HOH D . 
X 6 HOH 220 620 462  HOH HOH D . 
X 6 HOH 221 621 263  HOH HOH D . 
X 6 HOH 222 622 363  HOH HOH D . 
X 6 HOH 223 623 874  HOH HOH D . 
X 6 HOH 224 624 926  HOH HOH D . 
X 6 HOH 225 625 132  HOH HOH D . 
X 6 HOH 226 626 215  HOH HOH D . 
X 6 HOH 227 627 143  HOH HOH D . 
X 6 HOH 228 628 1004 HOH HOH D . 
X 6 HOH 229 629 323  HOH HOH D . 
X 6 HOH 230 630 255  HOH HOH D . 
X 6 HOH 231 631 579  HOH HOH D . 
X 6 HOH 232 632 1082 HOH HOH D . 
X 6 HOH 233 633 335  HOH HOH D . 
X 6 HOH 234 634 898  HOH HOH D . 
X 6 HOH 235 635 329  HOH HOH D . 
X 6 HOH 236 636 483  HOH HOH D . 
X 6 HOH 237 637 366  HOH HOH D . 
X 6 HOH 238 638 1083 HOH HOH D . 
X 6 HOH 239 639 690  HOH HOH D . 
X 6 HOH 240 640 846  HOH HOH D . 
X 6 HOH 241 641 387  HOH HOH D . 
X 6 HOH 242 642 1081 HOH HOH D . 
X 6 HOH 243 643 339  HOH HOH D . 
X 6 HOH 244 644 332  HOH HOH D . 
X 6 HOH 245 645 916  HOH HOH D . 
X 6 HOH 246 646 646  HOH HOH D . 
X 6 HOH 247 647 749  HOH HOH D . 
X 6 HOH 248 648 863  HOH HOH D . 
X 6 HOH 249 649 1091 HOH HOH D . 
X 6 HOH 250 650 474  HOH HOH D . 
X 6 HOH 251 651 865  HOH HOH D . 
X 6 HOH 252 652 1123 HOH HOH D . 
X 6 HOH 253 653 1001 HOH HOH D . 
X 6 HOH 254 654 695  HOH HOH D . 
X 6 HOH 255 655 485  HOH HOH D . 
X 6 HOH 256 656 987  HOH HOH D . 
X 6 HOH 257 657 416  HOH HOH D . 
X 6 HOH 258 658 861  HOH HOH D . 
X 6 HOH 259 659 1084 HOH HOH D . 
X 6 HOH 260 660 1122 HOH HOH D . 
X 6 HOH 261 661 477  HOH HOH D . 
X 6 HOH 262 662 915  HOH HOH D . 
X 6 HOH 263 663 166  HOH HOH D . 
X 6 HOH 264 664 465  HOH HOH D . 
X 6 HOH 265 665 1134 HOH HOH D . 
X 6 HOH 266 666 750  HOH HOH D . 
X 6 HOH 267 667 1000 HOH HOH D . 
X 6 HOH 268 668 350  HOH HOH D . 
X 6 HOH 269 669 456  HOH HOH D . 
X 6 HOH 270 670 208  HOH HOH D . 
X 6 HOH 271 671 439  HOH HOH D . 
X 6 HOH 272 672 689  HOH HOH D . 
X 6 HOH 273 673 199  HOH HOH D . 
X 6 HOH 274 674 912  HOH HOH D . 
X 6 HOH 275 675 657  HOH HOH D . 
X 6 HOH 276 676 590  HOH HOH D . 
X 6 HOH 277 677 1007 HOH HOH D . 
X 6 HOH 278 678 169  HOH HOH D . 
X 6 HOH 279 679 248  HOH HOH D . 
X 6 HOH 280 680 1010 HOH HOH D . 
X 6 HOH 281 681 337  HOH HOH D . 
X 6 HOH 282 682 991  HOH HOH D . 
X 6 HOH 283 683 1138 HOH HOH D . 
X 6 HOH 284 684 664  HOH HOH D . 
X 6 HOH 285 685 443  HOH HOH D . 
X 6 HOH 286 686 403  HOH HOH D . 
X 6 HOH 287 687 1002 HOH HOH D . 
X 6 HOH 288 688 1006 HOH HOH D . 
X 6 HOH 289 689 884  HOH HOH D . 
X 6 HOH 290 690 741  HOH HOH D . 
X 6 HOH 291 691 479  HOH HOH D . 
X 6 HOH 292 692 683  HOH HOH D . 
X 6 HOH 293 693 269  HOH HOH D . 
X 6 HOH 294 694 397  HOH HOH D . 
X 6 HOH 295 695 273  HOH HOH D . 
X 6 HOH 296 696 250  HOH HOH D . 
X 6 HOH 297 697 373  HOH HOH D . 
X 6 HOH 298 698 1009 HOH HOH D . 
X 6 HOH 299 699 751  HOH HOH D . 
X 6 HOH 300 700 1078 HOH HOH D . 
X 6 HOH 301 701 1012 HOH HOH D . 
X 6 HOH 302 702 1011 HOH HOH D . 
X 6 HOH 303 703 607  HOH HOH D . 
X 6 HOH 304 704 746  HOH HOH D . 
X 6 HOH 305 705 532  HOH HOH D . 
X 6 HOH 306 706 264  HOH HOH D . 
X 6 HOH 307 707 1135 HOH HOH D . 
X 6 HOH 308 708 627  HOH HOH D . 
X 6 HOH 309 709 1076 HOH HOH D . 
X 6 HOH 310 710 1127 HOH HOH D . 
X 6 HOH 311 711 345  HOH HOH D . 
X 6 HOH 312 712 344  HOH HOH D . 
X 6 HOH 313 713 819  HOH HOH D . 
X 6 HOH 314 714 787  HOH HOH D . 
X 6 HOH 315 715 936  HOH HOH D . 
X 6 HOH 316 716 1125 HOH HOH D . 
X 6 HOH 317 717 1121 HOH HOH D . 
X 6 HOH 318 718 900  HOH HOH D . 
X 6 HOH 319 719 1077 HOH HOH D . 
X 6 HOH 320 720 561  HOH HOH D . 
X 6 HOH 321 721 233  HOH HOH D . 
X 6 HOH 322 722 358  HOH HOH D . 
X 6 HOH 323 723 308  HOH HOH D . 
X 6 HOH 324 724 1080 HOH HOH D . 
X 6 HOH 325 725 481  HOH HOH D . 
X 6 HOH 326 726 1128 HOH HOH D . 
X 6 HOH 327 727 777  HOH HOH D . 
X 6 HOH 328 728 486  HOH HOH D . 
X 6 HOH 329 729 868  HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A PHE 7   ? CG  ? A PHE 7   CG  
2  1 Y 1 A PHE 7   ? CD1 ? A PHE 7   CD1 
3  1 Y 1 A PHE 7   ? CD2 ? A PHE 7   CD2 
4  1 Y 1 A PHE 7   ? CE1 ? A PHE 7   CE1 
5  1 Y 1 A PHE 7   ? CE2 ? A PHE 7   CE2 
6  1 Y 1 A PHE 7   ? CZ  ? A PHE 7   CZ  
7  1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
8  1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
9  1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
10 1 Y 1 A MET 148 ? CE  ? A MET 148 CE  
11 1 Y 1 A ASP 235 ? OD1 ? A ASP 235 OD1 
12 1 Y 1 B LYS 135 ? CG  ? B LYS 135 CG  
13 1 Y 1 B LYS 135 ? CD  ? B LYS 135 CD  
14 1 Y 1 B LYS 135 ? CE  ? B LYS 135 CE  
15 1 Y 1 B LYS 135 ? NZ  ? B LYS 135 NZ  
16 1 Y 1 B GLU 137 ? CD  ? B GLU 137 CD  
17 1 Y 1 B GLU 137 ? OE1 ? B GLU 137 OE1 
18 1 Y 1 B GLU 137 ? OE2 ? B GLU 137 OE2 
19 1 Y 1 B LYS 166 ? NZ  ? B LYS 166 NZ  
20 1 Y 1 C LYS 3   ? CE  ? C LYS 3   CE  
21 1 Y 1 C LYS 3   ? NZ  ? C LYS 3   NZ  
22 1 Y 1 C GLU 47  ? CD  ? C GLU 47  CD  
23 1 Y 1 C GLU 47  ? OE1 ? C GLU 47  OE1 
24 1 Y 1 C GLU 47  ? OE2 ? C GLU 47  OE2 
25 1 Y 1 C LYS 57  ? CE  ? C LYS 57  CE  
26 1 Y 1 C LYS 57  ? NZ  ? C LYS 57  NZ  
27 1 Y 1 C GLU 137 ? CD  ? C GLU 137 CD  
28 1 Y 1 C GLU 137 ? OE1 ? C GLU 137 OE1 
29 1 Y 1 C GLU 137 ? OE2 ? C GLU 137 OE2 
30 1 Y 1 C MET 148 ? CE  ? C MET 148 CE  
31 1 Y 1 C ARG 240 ? CD  ? C ARG 240 CD  
32 1 Y 1 C ARG 240 ? NE  ? C ARG 240 NE  
33 1 Y 1 C ARG 240 ? CZ  ? C ARG 240 CZ  
34 1 Y 1 C ARG 240 ? NH1 ? C ARG 240 NH1 
35 1 Y 1 C ARG 240 ? NH2 ? C ARG 240 NH2 
# 
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 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.950 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7PUV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.434 
_cell.length_a_esd                 ? 
_cell.length_b                     74.460 
_cell.length_b_esd                 ? 
_cell.length_c                     91.913 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7PUV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   7PUV 
_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            2.09 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         41.27 
_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              ? 
_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    '0.1M ammonium citrate (pH 7.0), 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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-06-26 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   0.97970 
_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 P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97970 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7PUV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.399 
_reflns.d_resolution_low                               86.933 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     189636 
_reflns.number_obs                                     189636 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.600 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.200 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.080 
_reflns.pdbx_netI_over_av_sigmaI                       2.300 
_reflns.pdbx_netI_over_sigmaI                          11.400 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.112 
_reflns.pdbx_Rpim_I_all                                0.052 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       801850 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.400 1.480  ? 4.000 84178  ? ? ? 24043 85.200 ? ? ? ? 0.158 ? ? ? ? ? ? ? ? 3.500 0.158 ? ? 5.500  0.214 0.107 ? 1  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.480 1.560  ? 4.500 115244 ? ? ? 26639 99.700 ? ? ? ? 0.131 ? ? ? ? ? ? ? ? 4.300 0.131 ? ? 7.500  0.177 0.083 ? 2  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.560 1.670  ? 5.300 104085 ? ? ? 25098 99.700 ? ? ? ? 0.107 ? ? ? ? ? ? ? ? 4.100 0.107 ? ? 8.700  0.146 0.070 ? 3  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.670 1.810  ? 5.800 103208 ? ? ? 23385 99.800 ? ? ? ? 0.090 ? ? ? ? ? ? ? ? 4.400 0.090 ? ? 10.700 0.124 0.058 ? 4  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.810 1.980  ? 6.100 89958  ? ? ? 21496 99.700 ? ? ? ? 0.077 ? ? ? ? ? ? ? ? 4.200 0.077 ? ? 12.300 0.107 0.051 ? 5  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.980 2.210  ? 6.100 87645  ? ? ? 19518 99.900 ? ? ? ? 0.072 ? ? ? ? ? ? ? ? 4.500 0.072 ? ? 14.600 0.100 0.046 ? 6  1 ? ? ? ? ? ? 
? ? ? ? ? 
2.210 2.550  ? 5.700 73924  ? ? ? 17234 99.800 ? ? ? ? 0.070 ? ? ? ? ? ? ? ? 4.300 0.070 ? ? 15.100 0.099 0.047 ? 7  1 ? ? ? ? ? ? 
? ? ? ? ? 
2.550 3.130  ? 5.200 66710  ? ? ? 14566 99.900 ? ? ? ? 0.071 ? ? ? ? ? ? ? ? 4.600 0.071 ? ? 16.700 0.100 0.046 ? 8  1 ? ? ? ? ? ? 
? ? ? ? ? 
3.130 4.430  ? 4.500 49387  ? ? ? 11337 99.800 ? ? ? ? 0.077 ? ? ? ? ? ? ? ? 4.400 0.077 ? ? 17.600 0.108 0.051 ? 9  1 ? ? ? ? ? ? 
? ? ? ? ? 
4.430 86.933 ? 3.400 27511  ? ? ? 6320  99.900 ? ? ? ? 0.090 ? ? ? ? ? ? ? ? 4.400 0.090 ? ? 16.900 0.125 0.058 ? 10 1 ? ? ? ? ? ? 
? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.8800 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.0700 
_refine.aniso_B[2][2]                            2.1700 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -1.0000 
_refine.B_iso_max                                117.020 
_refine.B_iso_mean                               18.5360 
_refine.B_iso_min                                5.800 
_refine.correlation_coeff_Fo_to_Fc               0.9680 
_refine.correlation_coeff_Fo_to_Fc_free          0.9490 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7PUV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.4000 
_refine.ls_d_res_low                             73.2400 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     170686 
_refine.ls_number_reflns_R_free                  18914 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.5800 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1649 
_refine.ls_R_factor_R_free                       0.2170 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1592 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4HT2 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0800 
_refine.pdbx_overall_ESU_R_Free                  0.0760 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.4000 
_refine_hist.d_res_low                        73.2400 
_refine_hist.number_atoms_solvent             1143 
_refine_hist.number_atoms_total               9614 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       1042 
_refine_hist.pdbx_B_iso_mean_ligand           17.70 
_refine_hist.pdbx_B_iso_mean_solvent          28.65 
_refine_hist.pdbx_number_atoms_protein        8336 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         135 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.014  0.012  8941  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.047  1.651  12213 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.451  5.000  1085  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.704 23.708 472   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.621 15.000 1377  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 18.618 15.000 31    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.221  0.200  1109  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.018  0.020  7111  ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 7.396  3.000  8941  ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 26.512 5.000  708   ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 17.811 5.000  9109  ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.4000 
_refine_ls_shell.d_res_low                        1.4360 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             1016 
_refine_ls_shell.number_reflns_R_work             9197 
_refine_ls_shell.percent_reflns_obs               71.2400 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2540 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1660 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     7PUV 
_struct.title                        
'Crystal structure of carbonic anhydrase XII with methyl 2-(benzenesulfonyl)-4-chloro-5-sulfamoylbenzoate' 
_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        7PUV 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 2 ? 
J N N 3 ? 
K N N 5 ? 
L N N 4 ? 
M N N 2 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 4 ? 
R N N 2 ? 
S N N 3 ? 
T N N 4 ? 
U N N 6 ? 
V N N 6 ? 
W N N 6 ? 
X 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 7PUV A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 7PUV B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 7PUV C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 7PUV 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 7PUV MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 7PUV MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 7PUV MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 7PUV 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,U,V 
2 1 C,D,M,N,O,P,Q,R,S,T,W,X 
# 
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 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PHE A 7   ? LYS A 18  ? PHE A 7   LYS A 18  5 ? 12 
HELX_P HELX_P2  AA2 TYR A 19  ? GLY A 24  ? TYR A 19  GLY A 24  5 ? 6  
HELX_P HELX_P3  AA3 HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P4  AA4 ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P6  AA6 HIS A 161 ? LYS A 166 ? HIS A 161 LYS A 166 5 ? 6  
HELX_P HELX_P7  AA7 ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P8  AA8 SER A 218 ? LEU A 229 ? SER A 218 LEU A 229 1 ? 12 
HELX_P HELX_P9  AA9 GLY B 11  ? LYS B 18  ? GLY B 11  LYS B 18  5 ? 8  
HELX_P HELX_P10 AB1 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P11 AB2 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P12 AB3 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P13 AB4 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P14 AB5 HIS B 161 ? LYS B 166 ? HIS B 161 LYS B 166 5 ? 6  
HELX_P HELX_P15 AB6 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P16 AB7 SER B 218 ? ALA B 228 ? SER B 218 ALA B 228 1 ? 11 
HELX_P HELX_P17 AB8 PHE C 7   ? LYS C 18  ? PHE C 7   LYS C 18  5 ? 12 
HELX_P HELX_P18 AB9 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P19 AC1 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P20 AC2 ASP C 128 ? ASN C 134 ? ASP C 128 ASN C 134 1 ? 7  
HELX_P HELX_P21 AC3 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P22 AC4 HIS C 161 ? LYS C 166 ? HIS C 161 LYS C 166 5 ? 6  
HELX_P HELX_P23 AC5 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P24 AC6 SER C 218 ? LEU C 229 ? SER C 218 LEU C 229 1 ? 12 
HELX_P HELX_P25 AC7 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P26 AC8 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P27 AC9 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P28 AD1 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P29 AD2 ASN D 152 ? SER D 160 ? ASN D 152 SER D 160 1 ? 9  
HELX_P HELX_P30 AD3 HIS D 161 ? LYS D 166 ? HIS D 161 LYS D 166 5 ? 6  
HELX_P HELX_P31 AD4 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P32 AD5 SER D 218 ? LEU D 229 ? SER D 218 LEU D 229 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG  ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG  ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG  ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG  ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 1.952 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.071 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 H 84Z .   S7  ? ? A ZN  301 A 84Z 304 1_555 ? ? ? ? ? ? ? 2.983 ? ? 
metalc5  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 I ZN  .   ZN  ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.002 ? ? 
metalc6  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 I ZN  .   ZN  ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc7  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 I ZN  .   ZN  ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc8  metalc ? ? I ZN  .   ZN  ? ? ? 1_555 L 84Z .   N10 ? ? B ZN  301 B 84Z 304 1_555 ? ? ? ? ? ? ? 1.751 ? ? 
metalc9  metalc ? ? I ZN  .   ZN  ? ? ? 1_555 L 84Z .   S7  ? ? B ZN  301 B 84Z 304 1_555 ? ? ? ? ? ? ? 2.990 ? ? 
metalc10 metalc ? ? C HIS 91  NE2 ? ? ? 1_555 M ZN  .   ZN  ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc11 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 M ZN  .   ZN  ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc12 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 M ZN  .   ZN  ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 1.897 ? ? 
metalc13 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 Q 84Z .   N10 ? ? C ZN  301 C 84Z 305 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc14 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 R ZN  .   ZN  ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc15 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 R ZN  .   ZN  ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc16 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 R ZN  .   ZN  ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 1.945 ? ? 
metalc17 metalc ? ? R ZN  .   ZN  ? ? ? 1_555 T 84Z .   N10 ? ? D ZN  301 D 84Z 303 1_555 ? ? ? ? ? ? ? 1.946 ? ? 
# 
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 99.3  ? 
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_555 113.4 ? 
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_555 100.8 ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  ? H 84Z .   ? A 84Z 304 ? 1_555 100.5 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  ? H 84Z .   ? A 84Z 304 ? 1_555 143.4 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  ? H 84Z .   ? A 84Z 304 ? 1_555 99.1  ? 
7  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 102.2 ? 
8  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 112.2 ? 
9  NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 98.7  ? 
10 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N10 ? L 84Z .   ? B 84Z 304 ? 1_555 96.1  ? 
11 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N10 ? L 84Z .   ? B 84Z 304 ? 1_555 109.8 ? 
12 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N10 ? L 84Z .   ? B 84Z 304 ? 1_555 134.3 ? 
13 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 S7  ? L 84Z .   ? B 84Z 304 ? 1_555 100.6 ? 
14 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 S7  ? L 84Z .   ? B 84Z 304 ? 1_555 143.1 ? 
15 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 S7  ? L 84Z .   ? B 84Z 304 ? 1_555 99.1  ? 
16 N10 ? L 84Z .   ? B 84Z 304 ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 S7  ? L 84Z .   ? B 84Z 304 ? 1_555 38.7  ? 
17 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 101.0 ? 
18 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 108.0 ? 
19 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 97.5  ? 
20 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N10 ? Q 84Z .   ? C 84Z 305 ? 1_555 114.8 ? 
21 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N10 ? Q 84Z .   ? C 84Z 305 ? 1_555 111.4 ? 
22 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N10 ? Q 84Z .   ? C 84Z 305 ? 1_555 121.0 ? 
23 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 104.1 ? 
24 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 108.8 ? 
25 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 97.4  ? 
26 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 N10 ? T 84Z .   ? D 84Z 303 ? 1_555 110.8 ? 
27 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 N10 ? T 84Z .   ? D 84Z 303 ? 1_555 114.0 ? 
28 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 N10 ? T 84Z .   ? D 84Z 303 ? 1_555 120.0 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 22 ? CYS A 202 ? CYS A 22 ? 1_555 CYS A 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 22 ? CYS B 202 ? CYS B 22 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS C 22 ? CYS C 202 ? CYS C 22 ? 1_555 CYS C 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 22 ? CYS D 202 ? CYS D 22 ? 1_555 CYS D 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 2.94  
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 1.36  
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -2.40 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 4.00  
5 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 6.91  
6 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 -1.61 
7 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 0.03  
8 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 -1.47 
9 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 2.18  
# 
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 ? MET D 148 ? LEU D 139 MET D 148 
AB2 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB2 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB2 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
AB2 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
AB2 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
AB3 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
AB3 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
AB3 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB3 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB3 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB3 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
AA2 1 2  N GLN A 38  ? N GLN A 38  O VAL A 257 ? O VAL A 257 
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 ILE A 146 ? O ILE A 146 N ALA A 114 ? N ALA A 114 
AA2 6 7  O VAL A 119 ? O VAL A 119 N THR A 88  ? N THR A 88  
AA2 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
AA2 8 9  O ASN A 71  ? O ASN A 71  N LEU A 60  ? N LEU A 60  
AA2 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
AA3 1 2  N GLN A 49  ? N GLN A 49  O HIS A 77  ? O HIS A 77  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N THR A 88  ? N THR A 88  O VAL A 119 ? O VAL A 119 
AA3 4 5  N ALA A 114 ? N ALA A 114 O ILE A 146 ? O ILE A 146 
AA3 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
AA4 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
AA5 1 2  N GLN B 38  ? N GLN B 38  O THR B 259 ? O THR B 259 
AA5 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
AA5 3 4  N TYR B 191 ? N TYR B 191 O VAL B 210 ? O VAL B 210 
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 HIS B 117 ? O HIS B 117 N HIS B 91  ? N HIS B 91  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O ASN B 71  ? O ASN B 71  N LEU B 60  ? N LEU B 60  
AA5 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
AA6 1 2  N GLN B 49  ? N GLN B 49  O HIS B 77  ? O HIS B 77  
AA6 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
AA6 3 4  N HIS B 91  ? N HIS B 91  O HIS B 117 ? O HIS B 117 
AA6 4 5  N ILE B 118 ? N ILE B 118 O LEU B 142 ? O LEU B 142 
AA6 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
AA7 1 2  N LEU C 32  ? N LEU C 32  O THR C 106 ? O THR C 106 
AA8 1 2  N GLN C 38  ? N GLN C 38  O THR C 259 ? O THR C 259 
AA8 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
AA8 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
AA8 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
AA8 5 6  O VAL C 144 ? O VAL C 144 N LEU C 116 ? N LEU C 116 
AA8 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
AA8 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
AA8 8 9  O LYS C 69  ? O LYS C 69  N THR C 62  ? N THR C 62  
AA8 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
AA9 1 2  N GLU C 47  ? N GLU C 47  O GLN C 79  ? O GLN C 79  
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 TYR D 191 ? N TYR D 191 O VAL D 210 ? O VAL D 210 
AB2 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
AB2 5 6  O LEU D 142 ? O LEU D 142 N ILE D 118 ? N ILE D 118 
AB2 6 7  O HIS D 117 ? O HIS D 117 N HIS D 91  ? N HIS D 91  
AB2 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
AB2 8 9  O ASN D 71  ? O ASN D 71  N LEU D 60  ? N LEU D 60  
AB2 9 10 N LEU D 61  ? N LEU D 61  O ALA D 172 ? O ALA D 172 
AB3 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
AB3 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
AB3 3 4  N HIS D 91  ? N HIS D 91  O HIS D 117 ? O HIS D 117 
AB3 4 5  N ILE D 118 ? N ILE D 118 O LEU D 142 ? O LEU D 142 
AB3 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 215 
# 
_pdbx_entry_details.entry_id                   7PUV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 ZN  A ZN  301 ? ? N10 A 84Z 304 ? ? 1.67 
2 1 OE2 D GLU 180 ? B O   D HOH 401 ? ? 2.03 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PHE 
_pdbx_validate_rmsd_angle.auth_seq_id_1              252 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PHE 
_pdbx_validate_rmsd_angle.auth_seq_id_2              252 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PHE 
_pdbx_validate_rmsd_angle.auth_seq_id_3              252 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                131.20 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            20.80 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                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  ? ? -150.77 78.24  
2 1 ASN A 245 ? ? -90.54  53.65  
3 1 ASP B 99  ? ? -155.10 81.58  
4 1 ASN B 122 ? ? -69.36  93.76  
5 1 ASN B 245 ? ? -92.62  58.36  
6 1 ALA C 41  ? B -20.44  -51.64 
7 1 ASN C 245 ? ? -94.94  53.35  
8 1 HIS D 66  ? ? -131.15 -32.41 
9 1 ASN D 245 ? ? -95.46  54.51  
# 
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 680 ? 6.76 . 
2 1 O ? B HOH 712 ? 5.83 . 
3 1 O ? B HOH 713 ? 5.83 . 
4 1 O ? C HOH 621 ? 5.83 . 
5 1 O ? D HOH 728 ? 5.94 . 
6 1 O ? D HOH 729 ? 6.22 . 
# 
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 A GLN 263 ? A GLN 263 
4  1 Y 1 B MET 1   ? B MET 1   
5  1 Y 1 B SER 2   ? B SER 2   
6  1 Y 1 C MET 1   ? C MET 1   
7  1 Y 1 C SER 2   ? C SER 2   
8  1 Y 1 C GLN 263 ? C GLN 263 
9  1 Y 1 D MET 1   ? D MET 1   
10 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 
84Z O18  O  N N 1   
84Z S16  S  N N 2   
84Z O17  O  N N 3   
84Z C19  C  Y N 4   
84Z C24  C  Y N 5   
84Z C23  C  Y N 6   
84Z C22  C  Y N 7   
84Z C21  C  Y N 8   
84Z C20  C  Y N 9   
84Z C3   C  Y N 10  
84Z C2   C  Y N 11  
84Z C4   C  Y N 12  
84Z C12  C  N N 13  
84Z O14  O  N N 14  
84Z C15  C  N N 15  
84Z O13  O  N N 16  
84Z C5   C  Y N 17  
84Z C6   C  Y N 18  
84Z C1   C  Y N 19  
84Z CL1  CL N N 20  
84Z S7   S  N N 21  
84Z O8   O  N N 22  
84Z O9   O  N N 23  
84Z N10  N  N N 24  
84Z H1   H  N N 25  
84Z H2   H  N N 26  
84Z H3   H  N N 27  
84Z H4   H  N N 28  
84Z H5   H  N N 29  
84Z H6   H  N N 30  
84Z H7   H  N N 31  
84Z H8   H  N N 32  
84Z H9   H  N N 33  
84Z H10  H  N N 34  
84Z H11  H  N N 35  
84Z H12  H  N N 36  
ALA N    N  N N 37  
ALA CA   C  N S 38  
ALA C    C  N N 39  
ALA O    O  N N 40  
ALA CB   C  N N 41  
ALA OXT  O  N N 42  
ALA H    H  N N 43  
ALA H2   H  N N 44  
ALA HA   H  N N 45  
ALA HB1  H  N N 46  
ALA HB2  H  N N 47  
ALA HB3  H  N N 48  
ALA HXT  H  N N 49  
ARG N    N  N N 50  
ARG CA   C  N S 51  
ARG C    C  N N 52  
ARG O    O  N N 53  
ARG CB   C  N N 54  
ARG CG   C  N N 55  
ARG CD   C  N N 56  
ARG NE   N  N N 57  
ARG CZ   C  N N 58  
ARG NH1  N  N N 59  
ARG NH2  N  N N 60  
ARG OXT  O  N N 61  
ARG H    H  N N 62  
ARG H2   H  N N 63  
ARG HA   H  N N 64  
ARG HB2  H  N N 65  
ARG HB3  H  N N 66  
ARG HG2  H  N N 67  
ARG HG3  H  N N 68  
ARG HD2  H  N N 69  
ARG HD3  H  N N 70  
ARG HE   H  N N 71  
ARG HH11 H  N N 72  
ARG HH12 H  N N 73  
ARG HH21 H  N N 74  
ARG HH22 H  N N 75  
ARG HXT  H  N N 76  
ASN N    N  N N 77  
ASN CA   C  N S 78  
ASN C    C  N N 79  
ASN O    O  N N 80  
ASN CB   C  N N 81  
ASN CG   C  N N 82  
ASN OD1  O  N N 83  
ASN ND2  N  N N 84  
ASN OXT  O  N N 85  
ASN H    H  N N 86  
ASN H2   H  N N 87  
ASN HA   H  N N 88  
ASN HB2  H  N N 89  
ASN HB3  H  N N 90  
ASN HD21 H  N N 91  
ASN HD22 H  N N 92  
ASN HXT  H  N N 93  
ASP N    N  N N 94  
ASP CA   C  N S 95  
ASP C    C  N N 96  
ASP O    O  N N 97  
ASP CB   C  N N 98  
ASP CG   C  N N 99  
ASP OD1  O  N N 100 
ASP OD2  O  N N 101 
ASP OXT  O  N N 102 
ASP H    H  N N 103 
ASP H2   H  N N 104 
ASP HA   H  N N 105 
ASP HB2  H  N N 106 
ASP HB3  H  N N 107 
ASP HD2  H  N N 108 
ASP HXT  H  N N 109 
CYS N    N  N N 110 
CYS CA   C  N R 111 
CYS C    C  N N 112 
CYS O    O  N N 113 
CYS CB   C  N N 114 
CYS SG   S  N N 115 
CYS OXT  O  N N 116 
CYS H    H  N N 117 
CYS H2   H  N N 118 
CYS HA   H  N N 119 
CYS HB2  H  N N 120 
CYS HB3  H  N N 121 
CYS HG   H  N N 122 
CYS HXT  H  N N 123 
EDO C1   C  N N 124 
EDO O1   O  N N 125 
EDO C2   C  N N 126 
EDO O2   O  N N 127 
EDO H11  H  N N 128 
EDO H12  H  N N 129 
EDO HO1  H  N N 130 
EDO H21  H  N N 131 
EDO H22  H  N N 132 
EDO HO2  H  N N 133 
GLN N    N  N N 134 
GLN CA   C  N S 135 
GLN C    C  N N 136 
GLN O    O  N N 137 
GLN CB   C  N N 138 
GLN CG   C  N N 139 
GLN CD   C  N N 140 
GLN OE1  O  N N 141 
GLN NE2  N  N N 142 
GLN OXT  O  N N 143 
GLN H    H  N N 144 
GLN H2   H  N N 145 
GLN HA   H  N N 146 
GLN HB2  H  N N 147 
GLN HB3  H  N N 148 
GLN HG2  H  N N 149 
GLN HG3  H  N N 150 
GLN HE21 H  N N 151 
GLN HE22 H  N N 152 
GLN HXT  H  N N 153 
GLU N    N  N N 154 
GLU CA   C  N S 155 
GLU C    C  N N 156 
GLU O    O  N N 157 
GLU CB   C  N N 158 
GLU CG   C  N N 159 
GLU CD   C  N N 160 
GLU OE1  O  N N 161 
GLU OE2  O  N N 162 
GLU OXT  O  N N 163 
GLU H    H  N N 164 
GLU H2   H  N N 165 
GLU HA   H  N N 166 
GLU HB2  H  N N 167 
GLU HB3  H  N N 168 
GLU HG2  H  N N 169 
GLU HG3  H  N N 170 
GLU HE2  H  N N 171 
GLU HXT  H  N N 172 
GLY N    N  N N 173 
GLY CA   C  N N 174 
GLY C    C  N N 175 
GLY O    O  N N 176 
GLY OXT  O  N N 177 
GLY H    H  N N 178 
GLY H2   H  N N 179 
GLY HA2  H  N N 180 
GLY HA3  H  N N 181 
GLY HXT  H  N N 182 
HIS N    N  N N 183 
HIS CA   C  N S 184 
HIS C    C  N N 185 
HIS O    O  N N 186 
HIS CB   C  N N 187 
HIS CG   C  Y N 188 
HIS ND1  N  Y N 189 
HIS CD2  C  Y N 190 
HIS CE1  C  Y N 191 
HIS NE2  N  Y N 192 
HIS OXT  O  N N 193 
HIS H    H  N N 194 
HIS H2   H  N N 195 
HIS HA   H  N N 196 
HIS HB2  H  N N 197 
HIS HB3  H  N N 198 
HIS HD1  H  N N 199 
HIS HD2  H  N N 200 
HIS HE1  H  N N 201 
HIS HE2  H  N N 202 
HIS HXT  H  N N 203 
HOH O    O  N N 204 
HOH H1   H  N N 205 
HOH H2   H  N N 206 
ILE N    N  N N 207 
ILE CA   C  N S 208 
ILE C    C  N N 209 
ILE O    O  N N 210 
ILE CB   C  N S 211 
ILE CG1  C  N N 212 
ILE CG2  C  N N 213 
ILE CD1  C  N N 214 
ILE OXT  O  N N 215 
ILE H    H  N N 216 
ILE H2   H  N N 217 
ILE HA   H  N N 218 
ILE HB   H  N N 219 
ILE HG12 H  N N 220 
ILE HG13 H  N N 221 
ILE HG21 H  N N 222 
ILE HG22 H  N N 223 
ILE HG23 H  N N 224 
ILE HD11 H  N N 225 
ILE HD12 H  N N 226 
ILE HD13 H  N N 227 
ILE HXT  H  N N 228 
LEU N    N  N N 229 
LEU CA   C  N S 230 
LEU C    C  N N 231 
LEU O    O  N N 232 
LEU CB   C  N N 233 
LEU CG   C  N N 234 
LEU CD1  C  N N 235 
LEU CD2  C  N N 236 
LEU OXT  O  N N 237 
LEU H    H  N N 238 
LEU H2   H  N N 239 
LEU HA   H  N N 240 
LEU HB2  H  N N 241 
LEU HB3  H  N N 242 
LEU HG   H  N N 243 
LEU HD11 H  N N 244 
LEU HD12 H  N N 245 
LEU HD13 H  N N 246 
LEU HD21 H  N N 247 
LEU HD22 H  N N 248 
LEU HD23 H  N N 249 
LEU HXT  H  N N 250 
LYS N    N  N N 251 
LYS CA   C  N S 252 
LYS C    C  N N 253 
LYS O    O  N N 254 
LYS CB   C  N N 255 
LYS CG   C  N N 256 
LYS CD   C  N N 257 
LYS CE   C  N N 258 
LYS NZ   N  N N 259 
LYS OXT  O  N N 260 
LYS H    H  N N 261 
LYS H2   H  N N 262 
LYS HA   H  N N 263 
LYS HB2  H  N N 264 
LYS HB3  H  N N 265 
LYS HG2  H  N N 266 
LYS HG3  H  N N 267 
LYS HD2  H  N N 268 
LYS HD3  H  N N 269 
LYS HE2  H  N N 270 
LYS HE3  H  N N 271 
LYS HZ1  H  N N 272 
LYS HZ2  H  N N 273 
LYS HZ3  H  N N 274 
LYS HXT  H  N N 275 
MET N    N  N N 276 
MET CA   C  N S 277 
MET C    C  N N 278 
MET O    O  N N 279 
MET CB   C  N N 280 
MET CG   C  N N 281 
MET SD   S  N N 282 
MET CE   C  N N 283 
MET OXT  O  N N 284 
MET H    H  N N 285 
MET H2   H  N N 286 
MET HA   H  N N 287 
MET HB2  H  N N 288 
MET HB3  H  N N 289 
MET HG2  H  N N 290 
MET HG3  H  N N 291 
MET HE1  H  N N 292 
MET HE2  H  N N 293 
MET HE3  H  N N 294 
MET HXT  H  N N 295 
PEG C1   C  N N 296 
PEG O1   O  N N 297 
PEG C2   C  N N 298 
PEG O2   O  N N 299 
PEG C3   C  N N 300 
PEG C4   C  N N 301 
PEG O4   O  N N 302 
PEG H11  H  N N 303 
PEG H12  H  N N 304 
PEG HO1  H  N N 305 
PEG H21  H  N N 306 
PEG H22  H  N N 307 
PEG H31  H  N N 308 
PEG H32  H  N N 309 
PEG H41  H  N N 310 
PEG H42  H  N N 311 
PEG HO4  H  N N 312 
PHE N    N  N N 313 
PHE CA   C  N S 314 
PHE C    C  N N 315 
PHE O    O  N N 316 
PHE CB   C  N N 317 
PHE CG   C  Y N 318 
PHE CD1  C  Y N 319 
PHE CD2  C  Y N 320 
PHE CE1  C  Y N 321 
PHE CE2  C  Y N 322 
PHE CZ   C  Y N 323 
PHE OXT  O  N N 324 
PHE H    H  N N 325 
PHE H2   H  N N 326 
PHE HA   H  N N 327 
PHE HB2  H  N N 328 
PHE HB3  H  N N 329 
PHE HD1  H  N N 330 
PHE HD2  H  N N 331 
PHE HE1  H  N N 332 
PHE HE2  H  N N 333 
PHE HZ   H  N N 334 
PHE HXT  H  N N 335 
PRO N    N  N N 336 
PRO CA   C  N S 337 
PRO C    C  N N 338 
PRO O    O  N N 339 
PRO CB   C  N N 340 
PRO CG   C  N N 341 
PRO CD   C  N N 342 
PRO OXT  O  N N 343 
PRO H    H  N N 344 
PRO HA   H  N N 345 
PRO HB2  H  N N 346 
PRO HB3  H  N N 347 
PRO HG2  H  N N 348 
PRO HG3  H  N N 349 
PRO HD2  H  N N 350 
PRO HD3  H  N N 351 
PRO HXT  H  N N 352 
SER N    N  N N 353 
SER CA   C  N S 354 
SER C    C  N N 355 
SER O    O  N N 356 
SER CB   C  N N 357 
SER OG   O  N N 358 
SER OXT  O  N N 359 
SER H    H  N N 360 
SER H2   H  N N 361 
SER HA   H  N N 362 
SER HB2  H  N N 363 
SER HB3  H  N N 364 
SER HG   H  N N 365 
SER HXT  H  N N 366 
THR N    N  N N 367 
THR CA   C  N S 368 
THR C    C  N N 369 
THR O    O  N N 370 
THR CB   C  N R 371 
THR OG1  O  N N 372 
THR CG2  C  N N 373 
THR OXT  O  N N 374 
THR H    H  N N 375 
THR H2   H  N N 376 
THR HA   H  N N 377 
THR HB   H  N N 378 
THR HG1  H  N N 379 
THR HG21 H  N N 380 
THR HG22 H  N N 381 
THR HG23 H  N N 382 
THR HXT  H  N N 383 
TRP N    N  N N 384 
TRP CA   C  N S 385 
TRP C    C  N N 386 
TRP O    O  N N 387 
TRP CB   C  N N 388 
TRP CG   C  Y N 389 
TRP CD1  C  Y N 390 
TRP CD2  C  Y N 391 
TRP NE1  N  Y N 392 
TRP CE2  C  Y N 393 
TRP CE3  C  Y N 394 
TRP CZ2  C  Y N 395 
TRP CZ3  C  Y N 396 
TRP CH2  C  Y N 397 
TRP OXT  O  N N 398 
TRP H    H  N N 399 
TRP H2   H  N N 400 
TRP HA   H  N N 401 
TRP HB2  H  N N 402 
TRP HB3  H  N N 403 
TRP HD1  H  N N 404 
TRP HE1  H  N N 405 
TRP HE3  H  N N 406 
TRP HZ2  H  N N 407 
TRP HZ3  H  N N 408 
TRP HH2  H  N N 409 
TRP HXT  H  N N 410 
TYR N    N  N N 411 
TYR CA   C  N S 412 
TYR C    C  N N 413 
TYR O    O  N N 414 
TYR CB   C  N N 415 
TYR CG   C  Y N 416 
TYR CD1  C  Y N 417 
TYR CD2  C  Y N 418 
TYR CE1  C  Y N 419 
TYR CE2  C  Y N 420 
TYR CZ   C  Y N 421 
TYR OH   O  N N 422 
TYR OXT  O  N N 423 
TYR H    H  N N 424 
TYR H2   H  N N 425 
TYR HA   H  N N 426 
TYR HB2  H  N N 427 
TYR HB3  H  N N 428 
TYR HD1  H  N N 429 
TYR HD2  H  N N 430 
TYR HE1  H  N N 431 
TYR HE2  H  N N 432 
TYR HH   H  N N 433 
TYR HXT  H  N N 434 
VAL N    N  N N 435 
VAL CA   C  N S 436 
VAL C    C  N N 437 
VAL O    O  N N 438 
VAL CB   C  N N 439 
VAL CG1  C  N N 440 
VAL CG2  C  N N 441 
VAL OXT  O  N N 442 
VAL H    H  N N 443 
VAL H2   H  N N 444 
VAL HA   H  N N 445 
VAL HB   H  N N 446 
VAL HG11 H  N N 447 
VAL HG12 H  N N 448 
VAL HG13 H  N N 449 
VAL HG21 H  N N 450 
VAL HG22 H  N N 451 
VAL HG23 H  N N 452 
VAL HXT  H  N N 453 
ZN  ZN   ZN N N 454 
# 
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 
84Z CL1 C1   sing N N 1   
84Z O9  S7   doub N N 2   
84Z C21 C20  doub Y N 3   
84Z C21 C22  sing Y N 4   
84Z C1  C2   doub Y N 5   
84Z C1  C6   sing Y N 6   
84Z C20 C19  sing Y N 7   
84Z C2  C3   sing Y N 8   
84Z O8  S7   doub N N 9   
84Z C22 C23  doub Y N 10  
84Z S7  C6   sing N N 11  
84Z S7  N10  sing N N 12  
84Z C6  C5   doub Y N 13  
84Z O17 S16  doub N N 14  
84Z C19 S16  sing N N 15  
84Z C19 C24  doub Y N 16  
84Z C3  S16  sing N N 17  
84Z C3  C4   doub Y N 18  
84Z C23 C24  sing Y N 19  
84Z C5  C4   sing Y N 20  
84Z S16 O18  doub N N 21  
84Z C4  C12  sing N N 22  
84Z O14 C12  sing N N 23  
84Z O14 C15  sing N N 24  
84Z C12 O13  doub N N 25  
84Z C24 H1   sing N N 26  
84Z C23 H2   sing N N 27  
84Z C22 H3   sing N N 28  
84Z C21 H4   sing N N 29  
84Z C20 H5   sing N N 30  
84Z C2  H6   sing N N 31  
84Z C15 H7   sing N N 32  
84Z C15 H8   sing N N 33  
84Z C15 H9   sing N N 34  
84Z C5  H10  sing N N 35  
84Z N10 H11  sing N N 36  
84Z N10 H12  sing N N 37  
ALA N   CA   sing N N 38  
ALA N   H    sing N N 39  
ALA N   H2   sing N N 40  
ALA CA  C    sing N N 41  
ALA CA  CB   sing N N 42  
ALA CA  HA   sing N N 43  
ALA C   O    doub N N 44  
ALA C   OXT  sing N N 45  
ALA CB  HB1  sing N N 46  
ALA CB  HB2  sing N N 47  
ALA CB  HB3  sing N N 48  
ALA OXT HXT  sing N N 49  
ARG N   CA   sing N N 50  
ARG N   H    sing N N 51  
ARG N   H2   sing N N 52  
ARG CA  C    sing N N 53  
ARG CA  CB   sing N N 54  
ARG CA  HA   sing N N 55  
ARG C   O    doub N N 56  
ARG C   OXT  sing N N 57  
ARG CB  CG   sing N N 58  
ARG CB  HB2  sing N N 59  
ARG CB  HB3  sing N N 60  
ARG CG  CD   sing N N 61  
ARG CG  HG2  sing N N 62  
ARG CG  HG3  sing N N 63  
ARG CD  NE   sing N N 64  
ARG CD  HD2  sing N N 65  
ARG CD  HD3  sing N N 66  
ARG NE  CZ   sing N N 67  
ARG NE  HE   sing N N 68  
ARG CZ  NH1  sing N N 69  
ARG CZ  NH2  doub N N 70  
ARG NH1 HH11 sing N N 71  
ARG NH1 HH12 sing N N 72  
ARG NH2 HH21 sing N N 73  
ARG NH2 HH22 sing N N 74  
ARG OXT HXT  sing N N 75  
ASN N   CA   sing N N 76  
ASN N   H    sing N N 77  
ASN N   H2   sing N N 78  
ASN CA  C    sing N N 79  
ASN CA  CB   sing N N 80  
ASN CA  HA   sing N N 81  
ASN C   O    doub N N 82  
ASN C   OXT  sing N N 83  
ASN CB  CG   sing N N 84  
ASN CB  HB2  sing N N 85  
ASN CB  HB3  sing N N 86  
ASN CG  OD1  doub N N 87  
ASN CG  ND2  sing N N 88  
ASN ND2 HD21 sing N N 89  
ASN ND2 HD22 sing N N 90  
ASN OXT HXT  sing N N 91  
ASP N   CA   sing N N 92  
ASP N   H    sing N N 93  
ASP N   H2   sing N N 94  
ASP CA  C    sing N N 95  
ASP CA  CB   sing N N 96  
ASP CA  HA   sing N N 97  
ASP C   O    doub N N 98  
ASP C   OXT  sing N N 99  
ASP CB  CG   sing N N 100 
ASP CB  HB2  sing N N 101 
ASP CB  HB3  sing N N 102 
ASP CG  OD1  doub N N 103 
ASP CG  OD2  sing N N 104 
ASP OD2 HD2  sing N N 105 
ASP OXT HXT  sing N N 106 
CYS N   CA   sing N N 107 
CYS N   H    sing N N 108 
CYS N   H2   sing N N 109 
CYS CA  C    sing N N 110 
CYS CA  CB   sing N N 111 
CYS CA  HA   sing N N 112 
CYS C   O    doub N N 113 
CYS C   OXT  sing N N 114 
CYS CB  SG   sing N N 115 
CYS CB  HB2  sing N N 116 
CYS CB  HB3  sing N N 117 
CYS SG  HG   sing N N 118 
CYS OXT HXT  sing N N 119 
EDO C1  O1   sing N N 120 
EDO C1  C2   sing N N 121 
EDO C1  H11  sing N N 122 
EDO C1  H12  sing N N 123 
EDO O1  HO1  sing N N 124 
EDO C2  O2   sing N N 125 
EDO C2  H21  sing N N 126 
EDO C2  H22  sing N N 127 
EDO O2  HO2  sing N N 128 
GLN N   CA   sing N N 129 
GLN N   H    sing N N 130 
GLN N   H2   sing N N 131 
GLN CA  C    sing N N 132 
GLN CA  CB   sing N N 133 
GLN CA  HA   sing N N 134 
GLN C   O    doub N N 135 
GLN C   OXT  sing N N 136 
GLN CB  CG   sing N N 137 
GLN CB  HB2  sing N N 138 
GLN CB  HB3  sing N N 139 
GLN CG  CD   sing N N 140 
GLN CG  HG2  sing N N 141 
GLN CG  HG3  sing N N 142 
GLN CD  OE1  doub N N 143 
GLN CD  NE2  sing N N 144 
GLN NE2 HE21 sing N N 145 
GLN NE2 HE22 sing N N 146 
GLN OXT HXT  sing N N 147 
GLU N   CA   sing N N 148 
GLU N   H    sing N N 149 
GLU N   H2   sing N N 150 
GLU CA  C    sing N N 151 
GLU CA  CB   sing N N 152 
GLU CA  HA   sing N N 153 
GLU C   O    doub N N 154 
GLU C   OXT  sing N N 155 
GLU CB  CG   sing N N 156 
GLU CB  HB2  sing N N 157 
GLU CB  HB3  sing N N 158 
GLU CG  CD   sing N N 159 
GLU CG  HG2  sing N N 160 
GLU CG  HG3  sing N N 161 
GLU CD  OE1  doub N N 162 
GLU CD  OE2  sing N N 163 
GLU OE2 HE2  sing N N 164 
GLU OXT HXT  sing N N 165 
GLY N   CA   sing N N 166 
GLY N   H    sing N N 167 
GLY N   H2   sing N N 168 
GLY CA  C    sing N N 169 
GLY CA  HA2  sing N N 170 
GLY CA  HA3  sing N N 171 
GLY C   O    doub N N 172 
GLY C   OXT  sing N N 173 
GLY OXT HXT  sing N N 174 
HIS N   CA   sing N N 175 
HIS N   H    sing N N 176 
HIS N   H2   sing N N 177 
HIS CA  C    sing N N 178 
HIS CA  CB   sing N N 179 
HIS CA  HA   sing N N 180 
HIS C   O    doub N N 181 
HIS C   OXT  sing N N 182 
HIS CB  CG   sing N N 183 
HIS CB  HB2  sing N N 184 
HIS CB  HB3  sing N N 185 
HIS CG  ND1  sing Y N 186 
HIS CG  CD2  doub Y N 187 
HIS ND1 CE1  doub Y N 188 
HIS ND1 HD1  sing N N 189 
HIS CD2 NE2  sing Y N 190 
HIS CD2 HD2  sing N N 191 
HIS CE1 NE2  sing Y N 192 
HIS CE1 HE1  sing N N 193 
HIS NE2 HE2  sing N N 194 
HIS OXT HXT  sing N N 195 
HOH O   H1   sing N N 196 
HOH O   H2   sing N N 197 
ILE N   CA   sing N N 198 
ILE N   H    sing N N 199 
ILE N   H2   sing N N 200 
ILE CA  C    sing N N 201 
ILE CA  CB   sing N N 202 
ILE CA  HA   sing N N 203 
ILE C   O    doub N N 204 
ILE C   OXT  sing N N 205 
ILE CB  CG1  sing N N 206 
ILE CB  CG2  sing N N 207 
ILE CB  HB   sing N N 208 
ILE CG1 CD1  sing N N 209 
ILE CG1 HG12 sing N N 210 
ILE CG1 HG13 sing N N 211 
ILE CG2 HG21 sing N N 212 
ILE CG2 HG22 sing N N 213 
ILE CG2 HG23 sing N N 214 
ILE CD1 HD11 sing N N 215 
ILE CD1 HD12 sing N N 216 
ILE CD1 HD13 sing N N 217 
ILE OXT HXT  sing N N 218 
LEU N   CA   sing N N 219 
LEU N   H    sing N N 220 
LEU N   H2   sing N N 221 
LEU CA  C    sing N N 222 
LEU CA  CB   sing N N 223 
LEU CA  HA   sing N N 224 
LEU C   O    doub N N 225 
LEU C   OXT  sing N N 226 
LEU CB  CG   sing N N 227 
LEU CB  HB2  sing N N 228 
LEU CB  HB3  sing N N 229 
LEU CG  CD1  sing N N 230 
LEU CG  CD2  sing N N 231 
LEU CG  HG   sing N N 232 
LEU CD1 HD11 sing N N 233 
LEU CD1 HD12 sing N N 234 
LEU CD1 HD13 sing N N 235 
LEU CD2 HD21 sing N N 236 
LEU CD2 HD22 sing N N 237 
LEU CD2 HD23 sing N N 238 
LEU OXT HXT  sing N N 239 
LYS N   CA   sing N N 240 
LYS N   H    sing N N 241 
LYS N   H2   sing N N 242 
LYS CA  C    sing N N 243 
LYS CA  CB   sing N N 244 
LYS CA  HA   sing N N 245 
LYS C   O    doub N N 246 
LYS C   OXT  sing N N 247 
LYS CB  CG   sing N N 248 
LYS CB  HB2  sing N N 249 
LYS CB  HB3  sing N N 250 
LYS CG  CD   sing N N 251 
LYS CG  HG2  sing N N 252 
LYS CG  HG3  sing N N 253 
LYS CD  CE   sing N N 254 
LYS CD  HD2  sing N N 255 
LYS CD  HD3  sing N N 256 
LYS CE  NZ   sing N N 257 
LYS CE  HE2  sing N N 258 
LYS CE  HE3  sing N N 259 
LYS NZ  HZ1  sing N N 260 
LYS NZ  HZ2  sing N N 261 
LYS NZ  HZ3  sing N N 262 
LYS OXT HXT  sing N N 263 
MET N   CA   sing N N 264 
MET N   H    sing N N 265 
MET N   H2   sing N N 266 
MET CA  C    sing N N 267 
MET CA  CB   sing N N 268 
MET CA  HA   sing N N 269 
MET C   O    doub N N 270 
MET C   OXT  sing N N 271 
MET CB  CG   sing N N 272 
MET CB  HB2  sing N N 273 
MET CB  HB3  sing N N 274 
MET CG  SD   sing N N 275 
MET CG  HG2  sing N N 276 
MET CG  HG3  sing N N 277 
MET SD  CE   sing N N 278 
MET CE  HE1  sing N N 279 
MET CE  HE2  sing N N 280 
MET CE  HE3  sing N N 281 
MET OXT HXT  sing N N 282 
PEG C1  O1   sing N N 283 
PEG C1  C2   sing N N 284 
PEG C1  H11  sing N N 285 
PEG C1  H12  sing N N 286 
PEG O1  HO1  sing N N 287 
PEG C2  O2   sing N N 288 
PEG C2  H21  sing N N 289 
PEG C2  H22  sing N N 290 
PEG O2  C3   sing N N 291 
PEG C3  C4   sing N N 292 
PEG C3  H31  sing N N 293 
PEG C3  H32  sing N N 294 
PEG C4  O4   sing N N 295 
PEG C4  H41  sing N N 296 
PEG C4  H42  sing N N 297 
PEG O4  HO4  sing N N 298 
PHE N   CA   sing N N 299 
PHE N   H    sing N N 300 
PHE N   H2   sing N N 301 
PHE CA  C    sing N N 302 
PHE CA  CB   sing N N 303 
PHE CA  HA   sing N N 304 
PHE C   O    doub N N 305 
PHE C   OXT  sing N N 306 
PHE CB  CG   sing N N 307 
PHE CB  HB2  sing N N 308 
PHE CB  HB3  sing N N 309 
PHE CG  CD1  doub Y N 310 
PHE CG  CD2  sing Y N 311 
PHE CD1 CE1  sing Y N 312 
PHE CD1 HD1  sing N N 313 
PHE CD2 CE2  doub Y N 314 
PHE CD2 HD2  sing N N 315 
PHE CE1 CZ   doub Y N 316 
PHE CE1 HE1  sing N N 317 
PHE CE2 CZ   sing Y N 318 
PHE CE2 HE2  sing N N 319 
PHE CZ  HZ   sing N N 320 
PHE OXT HXT  sing N N 321 
PRO N   CA   sing N N 322 
PRO N   CD   sing N N 323 
PRO N   H    sing N N 324 
PRO CA  C    sing N N 325 
PRO CA  CB   sing N N 326 
PRO CA  HA   sing N N 327 
PRO C   O    doub N N 328 
PRO C   OXT  sing N N 329 
PRO CB  CG   sing N N 330 
PRO CB  HB2  sing N N 331 
PRO CB  HB3  sing N N 332 
PRO CG  CD   sing N N 333 
PRO CG  HG2  sing N N 334 
PRO CG  HG3  sing N N 335 
PRO CD  HD2  sing N N 336 
PRO CD  HD3  sing N N 337 
PRO OXT HXT  sing N N 338 
SER N   CA   sing N N 339 
SER N   H    sing N N 340 
SER N   H2   sing N N 341 
SER CA  C    sing N N 342 
SER CA  CB   sing N N 343 
SER CA  HA   sing N N 344 
SER C   O    doub N N 345 
SER C   OXT  sing N N 346 
SER CB  OG   sing N N 347 
SER CB  HB2  sing N N 348 
SER CB  HB3  sing N N 349 
SER OG  HG   sing N N 350 
SER OXT HXT  sing N N 351 
THR N   CA   sing N N 352 
THR N   H    sing N N 353 
THR N   H2   sing N N 354 
THR CA  C    sing N N 355 
THR CA  CB   sing N N 356 
THR CA  HA   sing N N 357 
THR C   O    doub N N 358 
THR C   OXT  sing N N 359 
THR CB  OG1  sing N N 360 
THR CB  CG2  sing N N 361 
THR CB  HB   sing N N 362 
THR OG1 HG1  sing N N 363 
THR CG2 HG21 sing N N 364 
THR CG2 HG22 sing N N 365 
THR CG2 HG23 sing N N 366 
THR OXT HXT  sing N N 367 
TRP N   CA   sing N N 368 
TRP N   H    sing N N 369 
TRP N   H2   sing N N 370 
TRP CA  C    sing N N 371 
TRP CA  CB   sing N N 372 
TRP CA  HA   sing N N 373 
TRP C   O    doub N N 374 
TRP C   OXT  sing N N 375 
TRP CB  CG   sing N N 376 
TRP CB  HB2  sing N N 377 
TRP CB  HB3  sing N N 378 
TRP CG  CD1  doub Y N 379 
TRP CG  CD2  sing Y N 380 
TRP CD1 NE1  sing Y N 381 
TRP CD1 HD1  sing N N 382 
TRP CD2 CE2  doub Y N 383 
TRP CD2 CE3  sing Y N 384 
TRP NE1 CE2  sing Y N 385 
TRP NE1 HE1  sing N N 386 
TRP CE2 CZ2  sing Y N 387 
TRP CE3 CZ3  doub Y N 388 
TRP CE3 HE3  sing N N 389 
TRP CZ2 CH2  doub Y N 390 
TRP CZ2 HZ2  sing N N 391 
TRP CZ3 CH2  sing Y N 392 
TRP CZ3 HZ3  sing N N 393 
TRP CH2 HH2  sing N N 394 
TRP OXT HXT  sing N N 395 
TYR N   CA   sing N N 396 
TYR N   H    sing N N 397 
TYR N   H2   sing N N 398 
TYR CA  C    sing N N 399 
TYR CA  CB   sing N N 400 
TYR CA  HA   sing N N 401 
TYR C   O    doub N N 402 
TYR C   OXT  sing N N 403 
TYR CB  CG   sing N N 404 
TYR CB  HB2  sing N N 405 
TYR CB  HB3  sing N N 406 
TYR CG  CD1  doub Y N 407 
TYR CG  CD2  sing Y N 408 
TYR CD1 CE1  sing Y N 409 
TYR CD1 HD1  sing N N 410 
TYR CD2 CE2  doub Y N 411 
TYR CD2 HD2  sing N N 412 
TYR CE1 CZ   doub Y N 413 
TYR CE1 HE1  sing N N 414 
TYR CE2 CZ   sing Y N 415 
TYR CE2 HE2  sing N N 416 
TYR CZ  OH   sing N N 417 
TYR OH  HH   sing N N 418 
TYR OXT HXT  sing N N 419 
VAL N   CA   sing N N 420 
VAL N   H    sing N N 421 
VAL N   H2   sing N N 422 
VAL CA  C    sing N N 423 
VAL CA  CB   sing N N 424 
VAL CA  HA   sing N N 425 
VAL C   O    doub N N 426 
VAL C   OXT  sing N N 427 
VAL CB  CG1  sing N N 428 
VAL CB  CG2  sing N N 429 
VAL CB  HB   sing N N 430 
VAL CG1 HG11 sing N N 431 
VAL CG1 HG12 sing N N 432 
VAL CG1 HG13 sing N N 433 
VAL CG2 HG21 sing N N 434 
VAL CG2 HG22 sing N N 435 
VAL CG2 HG23 sing N N 436 
VAL OXT HXT  sing N N 437 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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   4HT2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7PUV 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.012914 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004433 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013430 
_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]   0.011503 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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   ? 18.447  15.913  18.736  1.00 52.95  ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 3   ? 17.893  16.471  17.456  1.00 47.16  ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 3   ? 16.989  15.475  16.720  1.00 32.01  ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A 1 3   ? 16.405  15.873  15.722  1.00 45.10  ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 3   ? 19.007  16.990  16.532  1.00 75.33  ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 3   ? 20.119  16.000  16.196  1.00 72.73  ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 3   ? 21.107  15.764  17.317  1.00 64.62  ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 3   ? 21.920  16.995  17.645  1.00 86.58  ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 3   ? 22.798  17.384  16.517  1.00 77.68  ? 3   LYS A NZ  1 
ATOM   10   N  N   . TRP A 1 4   ? 16.901  14.212  17.172  1.00 19.88  ? 4   TRP A N   1 
ATOM   11   C  CA  . TRP A 1 4   ? 16.048  13.163  16.630  1.00 14.65  ? 4   TRP A CA  1 
ATOM   12   C  C   . TRP A 1 4   ? 16.002  12.019  17.630  1.00 13.25  ? 4   TRP A C   1 
ATOM   13   O  O   . TRP A 1 4   ? 16.976  11.775  18.347  1.00 17.90  ? 4   TRP A O   1 
ATOM   14   C  CB  . TRP A 1 4   ? 16.582  12.718  15.249  1.00 13.27  ? 4   TRP A CB  1 
ATOM   15   C  CG  . TRP A 1 4   ? 17.985  12.160  15.205  1.00 12.19  ? 4   TRP A CG  1 
ATOM   16   C  CD1 . TRP A 1 4   ? 19.141  12.838  15.059  1.00 13.91  ? 4   TRP A CD1 1 
ATOM   17   C  CD2 . TRP A 1 4   ? 18.359  10.784  15.323  1.00 11.09  ? 4   TRP A CD2 1 
ATOM   18   N  NE1 . TRP A 1 4   ? 20.235  12.009  15.034  1.00 14.29  ? 4   TRP A NE1 1 
ATOM   19   C  CE2 . TRP A 1 4   ? 19.773  10.708  15.191  1.00 13.94  ? 4   TRP A CE2 1 
ATOM   20   C  CE3 . TRP A 1 4   ? 17.606  9.618   15.449  1.00 12.07  ? 4   TRP A CE3 1 
ATOM   21   C  CZ2 . TRP A 1 4   ? 20.473  9.513   15.224  1.00 13.98  ? 4   TRP A CZ2 1 
ATOM   22   C  CZ3 . TRP A 1 4   ? 18.292  8.419   15.444  1.00 13.05  ? 4   TRP A CZ3 1 
ATOM   23   C  CH2 . TRP A 1 4   ? 19.693  8.368   15.374  1.00 14.38  ? 4   TRP A CH2 1 
ATOM   24   N  N   . THR A 1 5   ? 14.910  11.241  17.586  1.00 13.14  ? 5   THR A N   1 
ATOM   25   C  CA  . THR A 1 5   ? 14.705  10.105  18.469  1.00 13.51  ? 5   THR A CA  1 
ATOM   26   C  C   . THR A 1 5   ? 14.043  9.021   17.664  1.00 10.18  ? 5   THR A C   1 
ATOM   27   O  O   . THR A 1 5   ? 13.834  9.144   16.468  1.00 11.91  ? 5   THR A O   1 
ATOM   28   C  CB  . THR A 1 5   ? 13.826  10.474  19.685  1.00 15.17  ? 5   THR A CB  1 
ATOM   29   O  OG1 . THR A 1 5   ? 12.549  10.701  19.075  1.00 17.90  ? 5   THR A OG1 1 
ATOM   30   C  CG2 . THR A 1 5   ? 14.267  11.683  20.483  1.00 18.13  ? 5   THR A CG2 1 
ATOM   31   N  N   . TYR A 1 6   ? 13.725  7.935   18.372  1.00 12.09  ? 6   TYR A N   1 
ATOM   32   C  CA  . TYR A 1 6   ? 12.929  6.857   17.800  1.00 11.87  ? 6   TYR A CA  1 
ATOM   33   C  C   . TYR A 1 6   ? 11.513  6.863   18.372  1.00 13.17  ? 6   TYR A C   1 
ATOM   34   O  O   . TYR A 1 6   ? 10.716  5.945   18.115  1.00 14.41  ? 6   TYR A O   1 
ATOM   35   C  CB  . TYR A 1 6   ? 13.568  5.493   18.072  1.00 13.32  ? 6   TYR A CB  1 
ATOM   36   C  CG  . TYR A 1 6   ? 14.834  5.257   17.290  1.00 11.71  ? 6   TYR A CG  1 
ATOM   37   C  CD1 . TYR A 1 6   ? 14.790  4.671   16.018  1.00 11.51  ? 6   TYR A CD1 1 
ATOM   38   C  CD2 . TYR A 1 6   ? 16.082  5.575   17.825  1.00 11.34  ? 6   TYR A CD2 1 
ATOM   39   C  CE1 . TYR A 1 6   ? 15.948  4.417   15.289  1.00 12.07  ? 6   TYR A CE1 1 
ATOM   40   C  CE2 . TYR A 1 6   ? 17.245  5.365   17.098  1.00 11.62  ? 6   TYR A CE2 1 
ATOM   41   C  CZ  . TYR A 1 6   ? 17.183  4.751   15.849  1.00 10.07  ? 6   TYR A CZ  1 
ATOM   42   O  OH  . TYR A 1 6   ? 18.319  4.536   15.142  1.00 12.31  ? 6   TYR A OH  1 
ATOM   43   N  N   . PHE A 1 7   ? 11.174  7.897   19.151  1.00 20.52  ? 7   PHE A N   1 
ATOM   44   C  CA  . PHE A 1 7   ? 9.894   7.894   19.860  1.00 24.26  ? 7   PHE A CA  1 
ATOM   45   C  C   . PHE A 1 7   ? 9.425   9.317   20.105  1.00 30.56  ? 7   PHE A C   1 
ATOM   46   O  O   . PHE A 1 7   ? 10.231  10.208  20.283  1.00 44.79  ? 7   PHE A O   1 
ATOM   47   C  CB  . PHE A 1 7   ? 9.942   7.037   21.141  1.00 26.77  ? 7   PHE A CB  1 
ATOM   48   N  N   . GLY A 1 8   ? 8.121   9.525   20.007  1.00 23.36  ? 8   GLY A N   1 
ATOM   49   C  CA  . GLY A 1 8   ? 7.568   10.825  20.408  1.00 20.15  ? 8   GLY A CA  1 
ATOM   50   C  C   . GLY A 1 8   ? 7.643   11.771  19.219  1.00 21.21  ? 8   GLY A C   1 
ATOM   51   O  O   . GLY A 1 8   ? 7.727   11.311  18.058  1.00 25.48  ? 8   GLY A O   1 
ATOM   52   N  N   . PRO A 1 9   ? 7.596   13.102  19.429  1.00 21.05  ? 9   PRO A N   1 
ATOM   53   C  CA  . PRO A 1 9   ? 7.480   14.049  18.324  1.00 22.93  ? 9   PRO A CA  1 
ATOM   54   C  C   . PRO A 1 9   ? 8.699   14.189  17.423  1.00 19.41  ? 9   PRO A C   1 
ATOM   55   O  O   . PRO A 1 9   ? 8.577   14.725  16.320  1.00 19.68  ? 9   PRO A O   1 
ATOM   56   C  CB  . PRO A 1 9   ? 7.281   15.440  18.950  1.00 30.34  ? 9   PRO A CB  1 
ATOM   57   C  CG  . PRO A 1 9   ? 7.464   15.252  20.440  1.00 31.55  ? 9   PRO A CG  1 
ATOM   58   C  CD  . PRO A 1 9   ? 7.596   13.770  20.738  1.00 23.73  ? 9   PRO A CD  1 
ATOM   59   N  N   . ASP A 1 10  ? 9.849   13.637  17.868  1.00 18.80  ? 10  ASP A N   1 
ATOM   60   C  CA  . ASP A 1 10  ? 11.097  13.799  17.131  1.00 17.44  ? 10  ASP A CA  1 
ATOM   61   C  C   . ASP A 1 10  ? 11.478  12.478  16.469  1.00 14.90  ? 10  ASP A C   1 
ATOM   62   O  O   . ASP A 1 10  ? 12.639  12.284  16.062  1.00 14.82  ? 10  ASP A O   1 
ATOM   63   C  CB  . ASP A 1 10  ? 12.207  14.407  18.009  1.00 23.04  ? 10  ASP A CB  1 
ATOM   64   C  CG  . ASP A 1 10  ? 11.963  15.866  18.360  1.00 25.32  ? 10  ASP A CG  1 
ATOM   65   O  OD1 . ASP A 1 10  ? 11.614  16.672  17.438  1.00 30.65  ? 10  ASP A OD1 1 
ATOM   66   O  OD2 . ASP A 1 10  ? 12.085  16.211  19.566  1.00 31.15  ? 10  ASP A OD2 1 
ATOM   67   N  N   . GLY A 1 11  ? 10.516  11.545  16.372  1.00 14.71  ? 11  GLY A N   1 
ATOM   68   C  CA  . GLY A 1 11  ? 10.763  10.183  15.914  1.00 11.48  ? 11  GLY A CA  1 
ATOM   69   C  C   . GLY A 1 11  ? 10.852  10.115  14.400  1.00 9.67   ? 11  GLY A C   1 
ATOM   70   O  O   . GLY A 1 11  ? 10.912  11.130  13.707  1.00 11.30  ? 11  GLY A O   1 
ATOM   71   N  N   . GLU A 1 12  ? 10.838  8.888   13.846  1.00 9.61   ? 12  GLU A N   1 
ATOM   72   C  CA  . GLU A 1 12  ? 11.344  8.704   12.476  1.00 10.20  ? 12  GLU A CA  1 
ATOM   73   C  C   . GLU A 1 12  ? 10.432  9.354   11.424  1.00 10.17  ? 12  GLU A C   1 
ATOM   74   O  O   . GLU A 1 12  ? 10.952  9.674   10.362  1.00 9.27   ? 12  GLU A O   1 
ATOM   75   C  CB  . GLU A 1 12  ? 11.533  7.215   12.120  1.00 10.42  ? 12  GLU A CB  1 
ATOM   76   C  CG  . GLU A 1 12  ? 10.233  6.413   12.101  1.00 9.11   ? 12  GLU A CG  1 
ATOM   77   C  CD  . GLU A 1 12  ? 10.514  4.909   12.273  1.00 8.60   ? 12  GLU A CD  1 
ATOM   78   O  OE1 . GLU A 1 12  ? 10.760  4.233   11.261  1.00 8.50   ? 12  GLU A OE1 1 
ATOM   79   O  OE2 . GLU A 1 12  ? 10.529  4.470   13.442  1.00 10.12  ? 12  GLU A OE2 1 
ATOM   80   N  N   . ASN A 1 13  ? 9.116   9.492   11.677  1.00 10.93  ? 13  ASN A N   1 
ATOM   81   C  CA  . ASN A 1 13  ? 8.268   10.156  10.681  1.00 9.96   ? 13  ASN A CA  1 
ATOM   82   C  C   . ASN A 1 13  ? 8.649   11.628  10.497  1.00 9.19   ? 13  ASN A C   1 
ATOM   83   O  O   . ASN A 1 13  ? 8.210   12.221  9.505   1.00 9.74   ? 13  ASN A O   1 
ATOM   84   C  CB  . ASN A 1 13  ? 6.758   10.006  10.933  1.00 9.25   ? 13  ASN A CB  1 
ATOM   85   C  CG  . ASN A 1 13  ? 6.284   8.574   10.807  1.00 11.81  ? 13  ASN A CG  1 
ATOM   86   O  OD1 . ASN A 1 13  ? 7.006   7.729   10.260  1.00 10.43  ? 13  ASN A OD1 1 
ATOM   87   N  ND2 . ASN A 1 13  ? 5.100   8.371   11.342  1.00 11.75  ? 13  ASN A ND2 1 
ATOM   88   N  N   . SER A 1 14  ? 9.353   12.205  11.485  1.00 10.60  ? 14  SER A N   1 
ATOM   89   C  CA  . SER A 1 14  ? 9.719   13.633  11.474  1.00 9.11   ? 14  SER A CA  1 
ATOM   90   C  C   . SER A 1 14  ? 11.159  13.863  11.078  1.00 9.75   ? 14  SER A C   1 
ATOM   91   O  O   . SER A 1 14  ? 11.571  14.992  10.896  1.00 9.71   ? 14  SER A O   1 
ATOM   92   C  CB  . SER A 1 14  ? 9.481   14.189  12.883  1.00 13.03  ? 14  SER A CB  1 
ATOM   93   O  OG  . SER A 1 14  ? 8.082   14.280  13.092  1.00 17.71  ? 14  SER A OG  1 
ATOM   94   N  N   . TRP A 1 15  ? 11.982  12.832  10.885  1.00 9.37   ? 15  TRP A N   1 
ATOM   95   C  CA  . TRP A 1 15  ? 13.397  13.035  10.575  1.00 10.20  ? 15  TRP A CA  1 
ATOM   96   C  C   . TRP A 1 15  ? 13.583  13.854  9.310   1.00 9.15   ? 15  TRP A C   1 
ATOM   97   O  O   . TRP A 1 15  ? 14.515  14.656  9.246   1.00 10.77  ? 15  TRP A O   1 
ATOM   98   C  CB  . TRP A 1 15  ? 14.089  11.679  10.333  1.00 10.62  ? 15  TRP A CB  1 
ATOM   99   C  CG  . TRP A 1 15  ? 14.292  10.849  11.580  1.00 9.41   ? 15  TRP A CG  1 
ATOM   100  C  CD1 . TRP A 1 15  ? 13.991  11.146  12.895  1.00 11.30  ? 15  TRP A CD1 1 
ATOM   101  C  CD2 . TRP A 1 15  ? 14.695  9.451   11.594  1.00 9.40   ? 15  TRP A CD2 1 
ATOM   102  N  NE1 . TRP A 1 15  ? 14.243  10.077  13.723  1.00 10.52  ? 15  TRP A NE1 1 
ATOM   103  C  CE2 . TRP A 1 15  ? 14.775  9.058   12.956  1.00 9.98   ? 15  TRP A CE2 1 
ATOM   104  C  CE3 . TRP A 1 15  ? 15.234  8.599   10.612  1.00 8.88   ? 15  TRP A CE3 1 
ATOM   105  C  CZ2 . TRP A 1 15  ? 15.147  7.755   13.326  1.00 9.73   ? 15  TRP A CZ2 1 
ATOM   106  C  CZ3 . TRP A 1 15  ? 15.573  7.286   10.961  1.00 10.15  ? 15  TRP A CZ3 1 
ATOM   107  C  CH2 . TRP A 1 15  ? 15.553  6.889   12.318  1.00 10.00  ? 15  TRP A CH2 1 
ATOM   108  N  N   . SER A 1 16  ? 12.650  13.717  8.362   1.00 8.75   ? 16  SER A N   1 
ATOM   109  C  CA  . SER A 1 16  ? 12.815  14.368  7.088   1.00 9.75   ? 16  SER A CA  1 
ATOM   110  C  C   . SER A 1 16  ? 12.771  15.885  7.195   1.00 9.30   ? 16  SER A C   1 
ATOM   111  O  O   . SER A 1 16  ? 13.176  16.540  6.238   1.00 10.24  ? 16  SER A O   1 
ATOM   112  C  CB  . SER A 1 16  ? 11.821  13.898  6.066   1.00 9.56   ? 16  SER A CB  1 
ATOM   113  O  OG  . SER A 1 16  ? 10.500  14.239  6.497   1.00 11.44  ? 16  SER A OG  1 
ATOM   114  N  N   A LYS A 1 17  ? 12.220  16.418  8.283   0.50 9.46   ? 17  LYS A N   1 
ATOM   115  N  N   B LYS A 1 17  ? 12.213  16.425  8.277   0.50 9.67   ? 17  LYS A N   1 
ATOM   116  C  CA  A LYS A 1 17  ? 12.165  17.891  8.395   0.50 11.51  ? 17  LYS A CA  1 
ATOM   117  C  CA  B LYS A 1 17  ? 12.165  17.899  8.348   0.50 10.68  ? 17  LYS A CA  1 
ATOM   118  C  C   A LYS A 1 17  ? 13.562  18.497  8.456   0.50 10.62  ? 17  LYS A C   1 
ATOM   119  C  C   B LYS A 1 17  ? 13.563  18.489  8.439   0.50 10.71  ? 17  LYS A C   1 
ATOM   120  O  O   A LYS A 1 17  ? 13.831  19.440  7.743   0.50 12.36  ? 17  LYS A O   1 
ATOM   121  O  O   B LYS A 1 17  ? 13.855  19.433  7.737   0.50 12.34  ? 17  LYS A O   1 
ATOM   122  C  CB  A LYS A 1 17  ? 11.370  18.219  9.665   0.50 13.93  ? 17  LYS A CB  1 
ATOM   123  C  CB  B LYS A 1 17  ? 11.468  18.330  9.639   0.50 12.67  ? 17  LYS A CB  1 
ATOM   124  C  CG  A LYS A 1 17  ? 9.886   17.850  9.573   0.50 15.91  ? 17  LYS A CG  1 
ATOM   125  C  CG  B LYS A 1 17  ? 11.383  19.851  9.791   0.50 11.32  ? 17  LYS A CG  1 
ATOM   126  C  CD  A LYS A 1 17  ? 9.054   18.400  10.724  0.50 20.92  ? 17  LYS A CD  1 
ATOM   127  C  CD  B LYS A 1 17  ? 10.368  20.212  10.877  0.50 15.53  ? 17  LYS A CD  1 
ATOM   128  C  CE  A LYS A 1 17  ? 9.002   19.927  10.716  0.50 21.20  ? 17  LYS A CE  1 
ATOM   129  C  CE  B LYS A 1 17  ? 8.918   20.153  10.430  0.50 16.79  ? 17  LYS A CE  1 
ATOM   130  N  NZ  A LYS A 1 17  ? 8.092   20.405  11.781  0.50 23.56  ? 17  LYS A NZ  1 
ATOM   131  N  NZ  B LYS A 1 17  ? 7.980   20.557  11.509  0.50 26.21  ? 17  LYS A NZ  1 
ATOM   132  N  N   A LYS A 1 18  ? 14.462  17.942  9.274   0.50 11.50  ? 18  LYS A N   1 
ATOM   133  N  N   B LYS A 1 18  ? 14.418  17.944  9.311   0.50 11.51  ? 18  LYS A N   1 
ATOM   134  C  CA  A LYS A 1 18  ? 15.799  18.512  9.394   0.50 12.29  ? 18  LYS A CA  1 
ATOM   135  C  CA  B LYS A 1 18  ? 15.783  18.435  9.434   0.50 11.70  ? 18  LYS A CA  1 
ATOM   136  C  C   A LYS A 1 18  ? 16.850  17.694  8.635   0.50 10.99  ? 18  LYS A C   1 
ATOM   137  C  C   B LYS A 1 18  ? 16.689  17.808  8.380   0.50 11.68  ? 18  LYS A C   1 
ATOM   138  O  O   A LYS A 1 18  ? 17.993  18.146  8.510   0.50 9.23   ? 18  LYS A O   1 
ATOM   139  O  O   B LYS A 1 18  ? 17.550  18.493  7.829   0.50 11.39  ? 18  LYS A O   1 
ATOM   140  C  CB  A LYS A 1 18  ? 16.183  18.658  10.869  0.50 14.83  ? 18  LYS A CB  1 
ATOM   141  C  CB  B LYS A 1 18  ? 16.339  18.199  10.840  0.50 12.74  ? 18  LYS A CB  1 
ATOM   142  C  CG  A LYS A 1 18  ? 15.634  19.875  11.616  0.50 19.47  ? 18  LYS A CG  1 
ATOM   143  C  CG  B LYS A 1 18  ? 17.767  18.686  11.076  0.50 13.63  ? 18  LYS A CG  1 
ATOM   144  C  CD  A LYS A 1 18  ? 16.351  21.207  11.408  0.50 22.10  ? 18  LYS A CD  1 
ATOM   145  C  CD  B LYS A 1 18  ? 18.042  18.829  12.566  0.50 19.99  ? 18  LYS A CD  1 
ATOM   146  C  CE  A LYS A 1 18  ? 15.927  22.251  12.427  0.50 20.82  ? 18  LYS A CE  1 
ATOM   147  C  CE  B LYS A 1 18  ? 19.349  19.524  12.886  0.50 24.97  ? 18  LYS A CE  1 
ATOM   148  N  NZ  A LYS A 1 18  ? 16.777  23.460  12.371  0.50 28.06  ? 18  LYS A NZ  1 
ATOM   149  N  NZ  B LYS A 1 18  ? 19.909  19.114  14.196  0.50 29.83  ? 18  LYS A NZ  1 
ATOM   150  N  N   . TYR A 1 19  ? 16.461  16.505  8.126   1.00 10.55  ? 19  TYR A N   1 
ATOM   151  C  CA  . TYR A 1 19  ? 17.376  15.651  7.372   1.00 11.08  ? 19  TYR A CA  1 
ATOM   152  C  C   . TYR A 1 19  ? 16.617  15.246  6.096   1.00 9.50   ? 19  TYR A C   1 
ATOM   153  O  O   . TYR A 1 19  ? 15.991  14.144  6.027   1.00 9.53   ? 19  TYR A O   1 
ATOM   154  C  CB  . TYR A 1 19  ? 17.769  14.375  8.166   1.00 11.19  ? 19  TYR A CB  1 
ATOM   155  C  CG  . TYR A 1 19  ? 18.401  14.746  9.483   1.00 10.22  ? 19  TYR A CG  1 
ATOM   156  C  CD1 . TYR A 1 19  ? 19.739  15.153  9.550   1.00 12.80  ? 19  TYR A CD1 1 
ATOM   157  C  CD2 . TYR A 1 19  ? 17.668  14.750  10.658  1.00 12.37  ? 19  TYR A CD2 1 
ATOM   158  C  CE1 . TYR A 1 19  ? 20.331  15.472  10.773  1.00 12.39  ? 19  TYR A CE1 1 
ATOM   159  C  CE2 . TYR A 1 19  ? 18.224  15.121  11.879  1.00 12.94  ? 19  TYR A CE2 1 
ATOM   160  C  CZ  . TYR A 1 19  ? 19.573  15.431  11.946  1.00 14.30  ? 19  TYR A CZ  1 
ATOM   161  O  OH  . TYR A 1 19  ? 20.105  15.744  13.168  1.00 17.33  ? 19  TYR A OH  1 
ATOM   162  N  N   . PRO A 1 20  ? 16.635  16.034  5.044   1.00 10.16  ? 20  PRO A N   1 
ATOM   163  C  CA  . PRO A 1 20  ? 15.772  15.801  3.898   1.00 10.11  ? 20  PRO A CA  1 
ATOM   164  C  C   . PRO A 1 20  ? 15.987  14.454  3.200   1.00 10.69  ? 20  PRO A C   1 
ATOM   165  O  O   . PRO A 1 20  ? 15.047  13.892  2.628   1.00 10.64  ? 20  PRO A O   1 
ATOM   166  C  CB  . PRO A 1 20  ? 16.084  16.907  2.929   1.00 10.56  ? 20  PRO A CB  1 
ATOM   167  C  CG  . PRO A 1 20  ? 16.701  17.944  3.716   1.00 17.09  ? 20  PRO A CG  1 
ATOM   168  C  CD  . PRO A 1 20  ? 17.369  17.293  4.896   1.00 11.29  ? 20  PRO A CD  1 
ATOM   169  N  N   . SER A 1 21  ? 17.211  13.891  3.254   1.00 10.42  ? 21  SER A N   1 
ATOM   170  C  CA  . SER A 1 21  ? 17.418  12.581  2.632   1.00 9.17   ? 21  SER A CA  1 
ATOM   171  C  C   . SER A 1 21  ? 16.535  11.512  3.254   1.00 9.63   ? 21  SER A C   1 
ATOM   172  O  O   . SER A 1 21  ? 16.328  10.490  2.600   1.00 9.30   ? 21  SER A O   1 
ATOM   173  C  CB  . SER A 1 21  ? 18.904  12.174  2.662   1.00 10.96  ? 21  SER A CB  1 
ATOM   174  O  OG  . SER A 1 21  ? 19.663  13.039  1.828   1.00 12.53  ? 21  SER A OG  1 
ATOM   175  N  N   . CYS A 1 22  ? 16.060  11.691  4.501   1.00 8.18   ? 22  CYS A N   1 
ATOM   176  C  CA  . CYS A 1 22  ? 15.271  10.635  5.147   1.00 8.36   ? 22  CYS A CA  1 
ATOM   177  C  C   . CYS A 1 22  ? 13.903  10.520  4.476   1.00 7.10   ? 22  CYS A C   1 
ATOM   178  O  O   . CYS A 1 22  ? 13.235  9.512   4.656   1.00 8.86   ? 22  CYS A O   1 
ATOM   179  C  CB  . CYS A 1 22  ? 15.073  10.960  6.615   1.00 9.33   ? 22  CYS A CB  1 
ATOM   180  S  SG  . CYS A 1 22  ? 16.608  10.985  7.573   1.00 10.83  ? 22  CYS A SG  1 
ATOM   181  N  N   . GLY A 1 23  ? 13.529  11.469  3.613   1.00 9.31   ? 23  GLY A N   1 
ATOM   182  C  CA  . GLY A 1 23  ? 12.382  11.310  2.730   1.00 9.59   ? 23  GLY A CA  1 
ATOM   183  C  C   . GLY A 1 23  ? 12.700  11.140  1.262   1.00 10.90  ? 23  GLY A C   1 
ATOM   184  O  O   . GLY A 1 23  ? 11.764  11.240  0.454   1.00 10.71  ? 23  GLY A O   1 
ATOM   185  N  N   . GLY A 1 24  ? 13.971  10.890  0.936   1.00 10.95  ? 24  GLY A N   1 
ATOM   186  C  CA  . GLY A 1 24  ? 14.407  10.738  -0.446  1.00 12.58  ? 24  GLY A CA  1 
ATOM   187  C  C   . GLY A 1 24  ? 14.408  9.290   -0.869  1.00 10.08  ? 24  GLY A C   1 
ATOM   188  O  O   . GLY A 1 24  ? 13.747  8.453   -0.243  1.00 12.22  ? 24  GLY A O   1 
ATOM   189  N  N   . LEU A 1 25  ? 15.184  9.034   -1.926  1.00 12.56  ? 25  LEU A N   1 
ATOM   190  C  CA  . LEU A 1 25  ? 15.265  7.695   -2.502  1.00 13.31  ? 25  LEU A CA  1 
ATOM   191  C  C   . LEU A 1 25  ? 16.227  6.792   -1.741  1.00 10.76  ? 25  LEU A C   1 
ATOM   192  O  O   . LEU A 1 25  ? 16.984  7.217   -0.868  1.00 11.66  ? 25  LEU A O   1 
ATOM   193  C  CB  . LEU A 1 25  ? 15.749  7.832   -3.947  1.00 17.25  ? 25  LEU A CB  1 
ATOM   194  C  CG  . LEU A 1 25  ? 14.958  8.796   -4.846  1.00 24.58  ? 25  LEU A CG  1 
ATOM   195  C  CD1 . LEU A 1 25  ? 15.637  8.925   -6.195  1.00 23.78  ? 25  LEU A CD1 1 
ATOM   196  C  CD2 . LEU A 1 25  ? 13.513  8.319   -4.984  1.00 23.12  ? 25  LEU A CD2 1 
ATOM   197  N  N   . LEU A 1 26  ? 16.119  5.506   -2.067  1.00 12.81  ? 26  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 26  ? 17.042  4.448   -1.693  1.00 12.11  ? 26  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 26  ? 17.066  4.221   -0.173  1.00 10.22  ? 26  LEU A C   1 
ATOM   200  O  O   . LEU A 1 26  ? 18.127  3.944   0.394   1.00 13.64  ? 26  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 26  ? 18.463  4.721   -2.237  1.00 14.75  ? 26  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 26  ? 18.682  4.784   -3.754  1.00 23.79  ? 26  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 26  ? 20.175  4.774   -4.077  1.00 28.11  ? 26  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 26  ? 18.013  3.619   -4.425  1.00 23.02  ? 26  LEU A CD2 1 
ATOM   205  N  N   . GLN A 1 27  ? 15.944  4.431   0.538   1.00 9.35   ? 27  GLN A N   1 
ATOM   206  C  CA  . GLN A 1 27  ? 16.002  4.334   2.005   1.00 8.03   ? 27  GLN A CA  1 
ATOM   207  C  C   . GLN A 1 27  ? 16.032  2.890   2.513   1.00 8.51   ? 27  GLN A C   1 
ATOM   208  O  O   . GLN A 1 27  ? 15.376  1.988   1.985   1.00 9.85   ? 27  GLN A O   1 
ATOM   209  C  CB  . GLN A 1 27  ? 14.831  5.063   2.665   1.00 9.16   ? 27  GLN A CB  1 
ATOM   210  C  CG  . GLN A 1 27  ? 14.886  6.560   2.373   1.00 7.00   ? 27  GLN A CG  1 
ATOM   211  C  CD  . GLN A 1 27  ? 16.086  7.174   3.057   1.00 8.47   ? 27  GLN A CD  1 
ATOM   212  O  OE1 . GLN A 1 27  ? 16.058  7.384   4.273   1.00 9.16   ? 27  GLN A OE1 1 
ATOM   213  N  NE2 . GLN A 1 27  ? 17.123  7.484   2.263   1.00 8.89   ? 27  GLN A NE2 1 
ATOM   214  N  N   . SER A 1 28  ? 16.813  2.739   3.614   1.00 7.14   ? 28  SER A N   1 
ATOM   215  C  CA  . SER A 1 28  ? 16.952  1.485   4.324   1.00 8.11   ? 28  SER A CA  1 
ATOM   216  C  C   . SER A 1 28  ? 16.399  1.665   5.730   1.00 8.54   ? 28  SER A C   1 
ATOM   217  O  O   . SER A 1 28  ? 16.255  2.781   6.196   1.00 8.84   ? 28  SER A O   1 
ATOM   218  C  CB  . SER A 1 28  ? 18.416  1.145   4.469   1.00 7.65   ? 28  SER A CB  1 
ATOM   219  O  OG  . SER A 1 28  ? 18.976  0.913   3.200   1.00 8.80   ? 28  SER A OG  1 
ATOM   220  N  N   . PRO A 1 29  ? 16.011  0.594   6.462   1.00 7.07   ? 29  PRO A N   1 
ATOM   221  C  CA  . PRO A 1 29  ? 16.138  -0.809  6.017   1.00 8.54   ? 29  PRO A CA  1 
ATOM   222  C  C   . PRO A 1 29  ? 14.940  -1.212  5.172   1.00 7.38   ? 29  PRO A C   1 
ATOM   223  O  O   . PRO A 1 29  ? 13.978  -0.447  5.028   1.00 9.43   ? 29  PRO A O   1 
ATOM   224  C  CB  . PRO A 1 29  ? 16.169  -1.521  7.405   1.00 9.23   ? 29  PRO A CB  1 
ATOM   225  C  CG  . PRO A 1 29  ? 15.138  -0.770  8.265   1.00 9.18   ? 29  PRO A CG  1 
ATOM   226  C  CD  . PRO A 1 29  ? 15.436  0.667   7.857   1.00 6.85   ? 29  PRO A CD  1 
ATOM   227  N  N   . ILE A 1 30  ? 14.943  -2.508  4.781   1.00 9.35   ? 30  ILE A N   1 
ATOM   228  C  CA  . ILE A 1 30  ? 13.891  -3.107  3.986   1.00 9.17   ? 30  ILE A CA  1 
ATOM   229  C  C   . ILE A 1 30  ? 13.623  -4.550  4.399   1.00 9.68   ? 30  ILE A C   1 
ATOM   230  O  O   . ILE A 1 30  ? 14.402  -5.124  5.131   1.00 9.30   ? 30  ILE A O   1 
ATOM   231  C  CB  . ILE A 1 30  ? 14.326  -3.074  2.504   1.00 10.13  ? 30  ILE A CB  1 
ATOM   232  C  CG1 . ILE A 1 30  ? 15.609  -3.891  2.265   1.00 10.38  ? 30  ILE A CG1 1 
ATOM   233  C  CG2 . ILE A 1 30  ? 14.530  -1.617  2.069   1.00 10.17  ? 30  ILE A CG2 1 
ATOM   234  C  CD1 . ILE A 1 30  ? 15.901  -4.101  0.798   1.00 14.88  ? 30  ILE A CD1 1 
ATOM   235  N  N   . ASP A 1 31  ? 12.455  -5.025  4.012   1.00 7.87   ? 31  ASP A N   1 
ATOM   236  C  CA  . ASP A 1 31  ? 12.099  -6.425  4.129   1.00 10.51  ? 31  ASP A CA  1 
ATOM   237  C  C   . ASP A 1 31  ? 12.806  -7.177  3.008   1.00 10.14  ? 31  ASP A C   1 
ATOM   238  O  O   . ASP A 1 31  ? 12.591  -6.922  1.819   1.00 12.00  ? 31  ASP A O   1 
ATOM   239  C  CB  . ASP A 1 31  ? 10.568  -6.559  4.078   1.00 11.04  ? 31  ASP A CB  1 
ATOM   240  C  CG  . ASP A 1 31  ? 10.136  -7.986  4.300   1.00 12.82  ? 31  ASP A CG  1 
ATOM   241  O  OD1 . ASP A 1 31  ? 10.768  -8.662  5.146   1.00 11.14  ? 31  ASP A OD1 1 
ATOM   242  O  OD2 . ASP A 1 31  ? 9.145   -8.354  3.683   1.00 17.07  ? 31  ASP A OD2 1 
ATOM   243  N  N   . LEU A 1 32  ? 13.568  -8.184  3.419   1.00 9.57   ? 32  LEU A N   1 
ATOM   244  C  CA  . LEU A 1 32  ? 14.207  -9.054  2.454   1.00 11.30  ? 32  LEU A CA  1 
ATOM   245  C  C   . LEU A 1 32  ? 13.247  -10.200 2.229   1.00 15.30  ? 32  LEU A C   1 
ATOM   246  O  O   . LEU A 1 32  ? 13.190  -11.160 2.998   1.00 13.16  ? 32  LEU A O   1 
ATOM   247  C  CB  . LEU A 1 32  ? 15.531  -9.545  3.068   1.00 10.89  ? 32  LEU A CB  1 
ATOM   248  C  CG  . LEU A 1 32  ? 16.475  -8.428  3.482   1.00 10.52  ? 32  LEU A CG  1 
ATOM   249  C  CD1 . LEU A 1 32  ? 17.607  -8.892  4.407   1.00 12.95  ? 32  LEU A CD1 1 
ATOM   250  C  CD2 . LEU A 1 32  ? 17.061  -7.630  2.288   1.00 14.23  ? 32  LEU A CD2 1 
ATOM   251  N  N   A HIS A 1 33  ? 12.319  -10.040 1.300   0.50 19.10  ? 33  HIS A N   1 
ATOM   252  N  N   B HIS A 1 33  ? 12.451  -10.041 1.151   0.50 15.58  ? 33  HIS A N   1 
ATOM   253  C  CA  A HIS A 1 33  ? 11.393  -11.152 1.193   0.50 22.00  ? 33  HIS A CA  1 
ATOM   254  C  CA  B HIS A 1 33  ? 11.257  -10.825 0.828   0.50 16.67  ? 33  HIS A CA  1 
ATOM   255  C  C   A HIS A 1 33  ? 11.695  -11.890 -0.098  0.50 22.32  ? 33  HIS A C   1 
ATOM   256  C  C   B HIS A 1 33  ? 11.581  -11.826 -0.294  0.50 19.31  ? 33  HIS A C   1 
ATOM   257  O  O   A HIS A 1 33  ? 12.392  -11.361 -0.956  0.50 22.04  ? 33  HIS A O   1 
ATOM   258  O  O   B HIS A 1 33  ? 12.217  -11.457 -1.272  0.50 16.44  ? 33  HIS A O   1 
ATOM   259  C  CB  A HIS A 1 33  ? 9.955   -10.675 1.377   0.50 23.97  ? 33  HIS A CB  1 
ATOM   260  C  CB  B HIS A 1 33  ? 10.090  -9.846  0.531   0.50 15.19  ? 33  HIS A CB  1 
ATOM   261  C  CG  A HIS A 1 33  ? 9.595   -9.670  0.340   0.50 24.29  ? 33  HIS A CG  1 
ATOM   262  C  CG  B HIS A 1 33  ? 8.748   -10.509 0.427   0.50 13.05  ? 33  HIS A CG  1 
ATOM   263  N  ND1 A HIS A 1 33  ? 10.032  -8.373  0.403   0.50 24.20  ? 33  HIS A ND1 1 
ATOM   264  N  ND1 B HIS A 1 33  ? 8.462   -11.441 -0.569  0.50 18.09  ? 33  HIS A ND1 1 
ATOM   265  C  CD2 A HIS A 1 33  ? 8.922   -9.792  -0.825  0.50 28.80  ? 33  HIS A CD2 1 
ATOM   266  C  CD2 B HIS A 1 33  ? 7.618   -10.394 1.168   0.50 14.80  ? 33  HIS A CD2 1 
ATOM   267  C  CE1 A HIS A 1 33  ? 9.590   -7.715  -0.653  0.50 28.78  ? 33  HIS A CE1 1 
ATOM   268  C  CE1 B HIS A 1 33  ? 7.235   -11.899 -0.401  0.50 17.62  ? 33  HIS A CE1 1 
ATOM   269  N  NE2 A HIS A 1 33  ? 8.905   -8.557  -1.412  0.50 28.86  ? 33  HIS A NE2 1 
ATOM   270  N  NE2 B HIS A 1 33  ? 6.682   -11.256 0.639   0.50 19.40  ? 33  HIS A NE2 1 
ATOM   271  N  N   . SER A 1 34  ? 11.138  -13.093 -0.208  1.00 23.88  ? 34  SER A N   1 
ATOM   272  C  CA  . SER A 1 34  ? 11.490  -14.047 -1.257  1.00 27.93  ? 34  SER A CA  1 
ATOM   273  C  C   . SER A 1 34  ? 11.263  -13.498 -2.675  1.00 28.27  ? 34  SER A C   1 
ATOM   274  O  O   . SER A 1 34  ? 12.052  -13.791 -3.568  1.00 33.96  ? 34  SER A O   1 
ATOM   275  C  CB  . SER A 1 34  ? 10.851  -15.412 -1.043  1.00 43.92  ? 34  SER A CB  1 
ATOM   276  O  OG  . SER A 1 34  ? 9.574   -15.256 -0.446  1.00 54.17  ? 34  SER A OG  1 
ATOM   277  N  N   . ASP A 1 35  ? 10.220  -12.673 -2.884  1.00 31.49  ? 35  ASP A N   1 
ATOM   278  C  CA  . ASP A 1 35  ? 9.826   -12.273 -4.229  1.00 31.99  ? 35  ASP A CA  1 
ATOM   279  C  C   . ASP A 1 35  ? 10.794  -11.267 -4.850  1.00 30.67  ? 35  ASP A C   1 
ATOM   280  O  O   . ASP A 1 35  ? 10.762  -11.072 -6.062  1.00 37.09  ? 35  ASP A O   1 
ATOM   281  C  CB  . ASP A 1 35  ? 8.412   -11.687 -4.260  1.00 33.70  ? 35  ASP A CB  1 
ATOM   282  C  CG  . ASP A 1 35  ? 7.312   -12.674 -3.909  1.00 41.67  ? 35  ASP A CG  1 
ATOM   283  O  OD1 . ASP A 1 35  ? 7.543   -13.902 -4.067  1.00 49.77  ? 35  ASP A OD1 1 
ATOM   284  O  OD2 . ASP A 1 35  ? 6.214   -12.212 -3.492  1.00 45.89  ? 35  ASP A OD2 1 
ATOM   285  N  N   . ILE A 1 36  ? 11.625  -10.589 -4.040  1.00 23.10  ? 36  ILE A N   1 
ATOM   286  C  CA  . ILE A 1 36  ? 12.517  -9.586  -4.610  1.00 24.75  ? 36  ILE A CA  1 
ATOM   287  C  C   . ILE A 1 36  ? 13.969  -10.073 -4.557  1.00 20.33  ? 36  ILE A C   1 
ATOM   288  O  O   . ILE A 1 36  ? 14.865  -9.282  -4.858  1.00 25.01  ? 36  ILE A O   1 
ATOM   289  C  CB  . ILE A 1 36  ? 12.395  -8.237  -3.878  1.00 22.49  ? 36  ILE A CB  1 
ATOM   290  C  CG1 . ILE A 1 36  ? 12.823  -8.423  -2.419  1.00 20.93  ? 36  ILE A CG1 1 
ATOM   291  C  CG2 . ILE A 1 36  ? 10.995  -7.645  -4.012  1.00 28.80  ? 36  ILE A CG2 1 
ATOM   292  C  CD1 . ILE A 1 36  ? 12.978  -7.141  -1.690  1.00 22.82  ? 36  ILE A CD1 1 
ATOM   293  N  N   . LEU A 1 37  ? 14.228  -11.320 -4.116  1.00 21.42  ? 37  LEU A N   1 
ATOM   294  C  CA  . LEU A 1 37  ? 15.613  -11.843 -4.093  1.00 20.94  ? 37  LEU A CA  1 
ATOM   295  C  C   . LEU A 1 37  ? 16.015  -12.372 -5.471  1.00 23.69  ? 37  LEU A C   1 
ATOM   296  O  O   . LEU A 1 37  ? 15.228  -13.083 -6.113  1.00 26.99  ? 37  LEU A O   1 
ATOM   297  C  CB  . LEU A 1 37  ? 15.730  -13.010 -3.107  1.00 21.64  ? 37  LEU A CB  1 
ATOM   298  C  CG  . LEU A 1 37  ? 15.317  -12.696 -1.680  1.00 20.54  ? 37  LEU A CG  1 
ATOM   299  C  CD1 . LEU A 1 37  ? 15.497  -13.898 -0.741  1.00 23.83  ? 37  LEU A CD1 1 
ATOM   300  C  CD2 . LEU A 1 37  ? 16.012  -11.449 -1.151  1.00 18.90  ? 37  LEU A CD2 1 
ATOM   301  N  N   . GLN A 1 38  ? 17.283  -12.152 -5.860  1.00 21.65  ? 38  GLN A N   1 
ATOM   302  C  CA  . GLN A 1 38  ? 17.806  -12.619 -7.147  1.00 22.51  ? 38  GLN A CA  1 
ATOM   303  C  C   . GLN A 1 38  ? 19.255  -13.074 -6.953  1.00 19.18  ? 38  GLN A C   1 
ATOM   304  O  O   . GLN A 1 38  ? 20.115  -12.274 -6.613  1.00 20.91  ? 38  GLN A O   1 
ATOM   305  C  CB  . GLN A 1 38  ? 17.702  -11.515 -8.214  1.00 25.39  ? 38  GLN A CB  1 
ATOM   306  C  CG  . GLN A 1 38  ? 18.326  -11.884 -9.559  1.00 30.13  ? 38  GLN A CG  1 
ATOM   307  C  CD  . GLN A 1 38  ? 17.934  -11.007 -10.726 1.00 31.13  ? 38  GLN A CD  1 
ATOM   308  O  OE1 . GLN A 1 38  ? 16.805  -11.081 -11.245 1.00 40.24  ? 38  GLN A OE1 1 
ATOM   309  N  NE2 . GLN A 1 38  ? 18.876  -10.172 -11.150 1.00 38.90  ? 38  GLN A NE2 1 
ATOM   310  N  N   . TYR A 1 39  ? 19.528  -14.358 -7.215  1.00 23.13  ? 39  TYR A N   1 
ATOM   311  C  CA  . TYR A 1 39  ? 20.887  -14.868 -7.111  1.00 18.42  ? 39  TYR A CA  1 
ATOM   312  C  C   . TYR A 1 39  ? 21.771  -14.140 -8.117  1.00 19.68  ? 39  TYR A C   1 
ATOM   313  O  O   . TYR A 1 39  ? 21.381  -13.970 -9.268  1.00 20.07  ? 39  TYR A O   1 
ATOM   314  C  CB  . TYR A 1 39  ? 20.917  -16.360 -7.406  1.00 19.92  ? 39  TYR A CB  1 
ATOM   315  C  CG  . TYR A 1 39  ? 22.300  -16.935 -7.544  1.00 19.49  ? 39  TYR A CG  1 
ATOM   316  C  CD1 . TYR A 1 39  ? 23.194  -16.936 -6.485  1.00 22.76  ? 39  TYR A CD1 1 
ATOM   317  C  CD2 . TYR A 1 39  ? 22.686  -17.542 -8.733  1.00 25.57  ? 39  TYR A CD2 1 
ATOM   318  C  CE1 . TYR A 1 39  ? 24.459  -17.494 -6.612  1.00 20.39  ? 39  TYR A CE1 1 
ATOM   319  C  CE2 . TYR A 1 39  ? 23.949  -18.106 -8.867  1.00 33.12  ? 39  TYR A CE2 1 
ATOM   320  C  CZ  . TYR A 1 39  ? 24.842  -18.082 -7.805  1.00 28.60  ? 39  TYR A CZ  1 
ATOM   321  O  OH  . TYR A 1 39  ? 26.077  -18.659 -7.932  1.00 36.94  ? 39  TYR A OH  1 
ATOM   322  N  N   . ASP A 1 40  ? 22.975  -13.770 -7.668  1.00 18.37  ? 40  ASP A N   1 
ATOM   323  C  CA  . ASP A 1 40  ? 23.956  -13.099 -8.499  1.00 18.80  ? 40  ASP A CA  1 
ATOM   324  C  C   . ASP A 1 40  ? 25.315  -13.762 -8.248  1.00 16.03  ? 40  ASP A C   1 
ATOM   325  O  O   . ASP A 1 40  ? 25.930  -13.570 -7.198  1.00 16.47  ? 40  ASP A O   1 
ATOM   326  C  CB  . ASP A 1 40  ? 23.887  -11.568 -8.291  1.00 17.98  ? 40  ASP A CB  1 
ATOM   327  C  CG  . ASP A 1 40  ? 24.902  -10.721 -9.055  1.00 25.01  ? 40  ASP A CG  1 
ATOM   328  O  OD1 . ASP A 1 40  ? 25.858  -11.280 -9.637  1.00 28.03  ? 40  ASP A OD1 1 
ATOM   329  O  OD2 . ASP A 1 40  ? 24.772  -9.489  -8.979  1.00 33.45  ? 40  ASP A OD2 1 
ATOM   330  N  N   . ALA A 1 41  ? 25.848  -14.448 -9.273  1.00 24.34  ? 41  ALA A N   1 
ATOM   331  C  CA  . ALA A 1 41  ? 27.099  -15.192 -9.166  1.00 29.33  ? 41  ALA A CA  1 
ATOM   332  C  C   . ALA A 1 41  ? 28.321  -14.289 -8.974  1.00 30.29  ? 41  ALA A C   1 
ATOM   333  O  O   . ALA A 1 41  ? 29.375  -14.797 -8.592  1.00 35.06  ? 41  ALA A O   1 
ATOM   334  C  CB  . ALA A 1 41  ? 27.273  -16.132 -10.349 1.00 35.62  ? 41  ALA A CB  1 
ATOM   335  N  N   . SER A 1 42  ? 28.195  -12.981 -9.262  1.00 29.46  ? 42  SER A N   1 
ATOM   336  C  CA  . SER A 1 42  ? 29.313  -12.054 -9.157  1.00 27.83  ? 42  SER A CA  1 
ATOM   337  C  C   . SER A 1 42  ? 29.569  -11.703 -7.690  1.00 30.65  ? 42  SER A C   1 
ATOM   338  O  O   . SER A 1 42  ? 30.545  -11.015 -7.379  1.00 35.06  ? 42  SER A O   1 
ATOM   339  C  CB  . SER A 1 42  ? 29.069  -10.821 -9.997  1.00 34.13  ? 42  SER A CB  1 
ATOM   340  O  OG  . SER A 1 42  ? 28.169  -9.950  -9.352  1.00 41.24  ? 42  SER A OG  1 
ATOM   341  N  N   . LEU A 1 43  ? 28.670  -12.135 -6.802  1.00 20.24  ? 43  LEU A N   1 
ATOM   342  C  CA  . LEU A 1 43  ? 28.820  -11.817 -5.385  1.00 20.25  ? 43  LEU A CA  1 
ATOM   343  C  C   . LEU A 1 43  ? 29.718  -12.799 -4.646  1.00 19.78  ? 43  LEU A C   1 
ATOM   344  O  O   . LEU A 1 43  ? 29.251  -13.789 -4.054  1.00 23.71  ? 43  LEU A O   1 
ATOM   345  C  CB  . LEU A 1 43  ? 27.439  -11.727 -4.735  1.00 16.80  ? 43  LEU A CB  1 
ATOM   346  C  CG  . LEU A 1 43  ? 26.588  -10.571 -5.259  1.00 18.17  ? 43  LEU A CG  1 
ATOM   347  C  CD1 . LEU A 1 43  ? 25.229  -10.606 -4.585  1.00 16.28  ? 43  LEU A CD1 1 
ATOM   348  C  CD2 . LEU A 1 43  ? 27.242  -9.175  -5.123  1.00 17.17  ? 43  LEU A CD2 1 
ATOM   349  N  N   . THR A 1 44  ? 31.004  -12.491 -4.692  1.00 18.36  ? 44  THR A N   1 
ATOM   350  C  CA  . THR A 1 44  ? 32.079  -13.339 -4.213  1.00 19.03  ? 44  THR A CA  1 
ATOM   351  C  C   . THR A 1 44  ? 32.337  -13.050 -2.739  1.00 17.64  ? 44  THR A C   1 
ATOM   352  O  O   . THR A 1 44  ? 31.793  -12.096 -2.154  1.00 17.80  ? 44  THR A O   1 
ATOM   353  C  CB  . THR A 1 44  ? 33.332  -13.108 -5.069  1.00 23.70  ? 44  THR A CB  1 
ATOM   354  O  OG1 . THR A 1 44  ? 33.578  -11.709 -4.980  1.00 24.48  ? 44  THR A OG1 1 
ATOM   355  C  CG2 . THR A 1 44  ? 33.092  -13.449 -6.516  1.00 29.02  ? 44  THR A CG2 1 
ATOM   356  N  N   . PRO A 1 45  ? 33.022  -13.968 -2.026  1.00 16.85  ? 45  PRO A N   1 
ATOM   357  C  CA  . PRO A 1 45  ? 33.181  -13.752 -0.585  1.00 15.91  ? 45  PRO A CA  1 
ATOM   358  C  C   . PRO A 1 45  ? 34.036  -12.527 -0.272  1.00 17.10  ? 45  PRO A C   1 
ATOM   359  O  O   . PRO A 1 45  ? 35.054  -12.302 -0.893  1.00 21.10  ? 45  PRO A O   1 
ATOM   360  C  CB  . PRO A 1 45  ? 33.914  -15.027 -0.150  1.00 20.28  ? 45  PRO A CB  1 
ATOM   361  C  CG  . PRO A 1 45  ? 33.647  -16.065 -1.261  1.00 21.83  ? 45  PRO A CG  1 
ATOM   362  C  CD  . PRO A 1 45  ? 33.555  -15.246 -2.525  1.00 20.63  ? 45  PRO A CD  1 
ATOM   363  N  N   . LEU A 1 46  ? 33.601  -11.735 0.699   1.00 14.03  ? 46  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 46  ? 34.437  -10.652 1.181   1.00 15.86  ? 46  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 46  ? 35.550  -11.207 2.075   1.00 15.76  ? 46  LEU A C   1 
ATOM   366  O  O   . LEU A 1 46  ? 35.450  -12.291 2.672   1.00 19.22  ? 46  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 46  ? 33.527  -9.746  2.005   1.00 13.62  ? 46  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 46  ? 32.413  -9.004  1.233   1.00 15.57  ? 46  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 46  ? 31.616  -8.203  2.235   1.00 18.11  ? 46  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 46  ? 33.014  -8.070  0.174   1.00 20.22  ? 46  LEU A CD2 1 
ATOM   371  N  N   . GLU A 1 47  ? 36.629  -10.429 2.163   1.00 14.89  ? 47  GLU A N   1 
ATOM   372  C  CA  . GLU A 1 47  ? 37.760  -10.720 3.042   1.00 15.49  ? 47  GLU A CA  1 
ATOM   373  C  C   . GLU A 1 47  ? 37.858  -9.612  4.095   1.00 15.43  ? 47  GLU A C   1 
ATOM   374  O  O   . GLU A 1 47  ? 37.685  -8.420  3.774   1.00 15.80  ? 47  GLU A O   1 
ATOM   375  C  CB  . GLU A 1 47  ? 39.095  -10.889 2.303   1.00 18.71  ? 47  GLU A CB  1 
ATOM   376  C  CG  . GLU A 1 47  ? 39.059  -12.027 1.298   1.00 28.58  ? 47  GLU A CG  1 
ATOM   377  N  N   . PHE A 1 48  ? 38.021  -10.030 5.348   1.00 12.84  ? 48  PHE A N   1 
ATOM   378  C  CA  . PHE A 1 48  ? 37.955  -9.133  6.494   1.00 14.20  ? 48  PHE A CA  1 
ATOM   379  C  C   . PHE A 1 48  ? 39.387  -8.952  7.004   1.00 12.78  ? 48  PHE A C   1 
ATOM   380  O  O   . PHE A 1 48  ? 40.009  -9.915  7.488   1.00 17.75  ? 48  PHE A O   1 
ATOM   381  C  CB  . PHE A 1 48  ? 37.021  -9.759  7.539   1.00 16.05  ? 48  PHE A CB  1 
ATOM   382  C  CG  . PHE A 1 48  ? 35.693  -10.148 6.920   1.00 13.14  ? 48  PHE A CG  1 
ATOM   383  C  CD1 . PHE A 1 48  ? 34.797  -9.170  6.512   1.00 15.84  ? 48  PHE A CD1 1 
ATOM   384  C  CD2 . PHE A 1 48  ? 35.334  -11.493 6.789   1.00 15.79  ? 48  PHE A CD2 1 
ATOM   385  C  CE1 . PHE A 1 48  ? 33.600  -9.514  5.896   1.00 15.26  ? 48  PHE A CE1 1 
ATOM   386  C  CE2 . PHE A 1 48  ? 34.127  -11.830 6.205   1.00 16.16  ? 48  PHE A CE2 1 
ATOM   387  C  CZ  . PHE A 1 48  ? 33.257  -10.845 5.768   1.00 16.15  ? 48  PHE A CZ  1 
ATOM   388  N  N   . GLN A 1 49  ? 39.982  -7.804  6.663   1.00 12.23  ? 49  GLN A N   1 
ATOM   389  C  CA  . GLN A 1 49  ? 41.416  -7.555  6.829   1.00 13.54  ? 49  GLN A CA  1 
ATOM   390  C  C   . GLN A 1 49  ? 41.638  -6.665  8.042   1.00 11.65  ? 49  GLN A C   1 
ATOM   391  O  O   . GLN A 1 49  ? 40.941  -5.657  8.201   1.00 12.38  ? 49  GLN A O   1 
ATOM   392  C  CB  . GLN A 1 49  ? 42.012  -6.892  5.585   1.00 14.16  ? 49  GLN A CB  1 
ATOM   393  C  CG  . GLN A 1 49  ? 41.882  -7.700  4.319   1.00 17.93  ? 49  GLN A CG  1 
ATOM   394  C  CD  . GLN A 1 49  ? 42.925  -8.778  4.149   1.00 31.09  ? 49  GLN A CD  1 
ATOM   395  O  OE1 . GLN A 1 49  ? 42.907  -9.528  3.166   1.00 38.28  ? 49  GLN A OE1 1 
ATOM   396  N  NE2 . GLN A 1 49  ? 43.897  -8.804  5.055   1.00 32.40  ? 49  GLN A NE2 1 
ATOM   397  N  N   . GLY A 1 50  ? 42.587  -7.032  8.905   1.00 11.86  ? 50  GLY A N   1 
ATOM   398  C  CA  . GLY A 1 50  ? 42.823  -6.179  10.067  1.00 15.04  ? 50  GLY A CA  1 
ATOM   399  C  C   . GLY A 1 50  ? 41.700  -6.171  11.108  1.00 14.54  ? 50  GLY A C   1 
ATOM   400  O  O   . GLY A 1 50  ? 41.658  -5.283  11.965  1.00 14.65  ? 50  GLY A O   1 
ATOM   401  N  N   . TYR A 1 51  ? 40.821  -7.177  11.040  1.00 13.99  ? 51  TYR A N   1 
ATOM   402  C  CA  . TYR A 1 51  ? 39.777  -7.330  12.049  1.00 14.38  ? 51  TYR A CA  1 
ATOM   403  C  C   . TYR A 1 51  ? 40.293  -7.851  13.386  1.00 13.26  ? 51  TYR A C   1 
ATOM   404  O  O   . TYR A 1 51  ? 39.598  -7.745  14.402  1.00 13.91  ? 51  TYR A O   1 
ATOM   405  C  CB  . TYR A 1 51  ? 38.655  -8.249  11.552  1.00 13.48  ? 51  TYR A CB  1 
ATOM   406  C  CG  . TYR A 1 51  ? 37.623  -7.573  10.682  1.00 11.88  ? 51  TYR A CG  1 
ATOM   407  C  CD1 . TYR A 1 51  ? 37.948  -6.707  9.633   1.00 12.87  ? 51  TYR A CD1 1 
ATOM   408  C  CD2 . TYR A 1 51  ? 36.278  -7.845  10.914  1.00 11.08  ? 51  TYR A CD2 1 
ATOM   409  C  CE1 . TYR A 1 51  ? 36.965  -6.117  8.816   1.00 12.39  ? 51  TYR A CE1 1 
ATOM   410  C  CE2 . TYR A 1 51  ? 35.295  -7.291  10.088  1.00 9.69   ? 51  TYR A CE2 1 
ATOM   411  C  CZ  . TYR A 1 51  ? 35.623  -6.380  9.092   1.00 11.86  ? 51  TYR A CZ  1 
ATOM   412  O  OH  . TYR A 1 51  ? 34.611  -5.763  8.390   1.00 12.82  ? 51  TYR A OH  1 
ATOM   413  N  N   . ASN A 1 52  ? 41.481  -8.515  13.372  1.00 15.22  ? 52  ASN A N   1 
ATOM   414  C  CA  . ASN A 1 52  ? 42.023  -9.020  14.619  1.00 17.89  ? 52  ASN A CA  1 
ATOM   415  C  C   . ASN A 1 52  ? 42.746  -7.875  15.341  1.00 18.03  ? 52  ASN A C   1 
ATOM   416  O  O   . ASN A 1 52  ? 43.960  -7.686  15.180  1.00 22.54  ? 52  ASN A O   1 
ATOM   417  C  CB  . ASN A 1 52  ? 42.932  -10.225 14.389  1.00 17.83  ? 52  ASN A CB  1 
ATOM   418  C  CG  . ASN A 1 52  ? 43.292  -10.980 15.662  1.00 23.96  ? 52  ASN A CG  1 
ATOM   419  O  OD1 . ASN A 1 52  ? 42.598  -10.881 16.663  1.00 25.85  ? 52  ASN A OD1 1 
ATOM   420  N  ND2 . ASN A 1 52  ? 44.373  -11.756 15.637  1.00 36.13  ? 52  ASN A ND2 1 
ATOM   421  N  N   . LEU A 1 53  ? 41.987  -7.104  16.117  1.00 16.47  ? 53  LEU A N   1 
ATOM   422  C  CA  . LEU A 1 53  ? 42.554  -5.902  16.721  1.00 17.99  ? 53  LEU A CA  1 
ATOM   423  C  C   . LEU A 1 53  ? 43.539  -6.234  17.835  1.00 23.29  ? 53  LEU A C   1 
ATOM   424  O  O   . LEU A 1 53  ? 43.314  -7.115  18.668  1.00 31.24  ? 53  LEU A O   1 
ATOM   425  C  CB  . LEU A 1 53  ? 41.449  -5.015  17.271  1.00 15.99  ? 53  LEU A CB  1 
ATOM   426  C  CG  . LEU A 1 53  ? 40.322  -4.624  16.306  1.00 14.33  ? 53  LEU A CG  1 
ATOM   427  C  CD1 . LEU A 1 53  ? 39.384  -3.675  17.057  1.00 19.15  ? 53  LEU A CD1 1 
ATOM   428  C  CD2 . LEU A 1 53  ? 40.842  -3.989  14.984  1.00 21.86  ? 53  LEU A CD2 1 
ATOM   429  N  N   . SER A 1 54  ? 44.598  -5.426  17.885  1.00 28.09  ? 54  SER A N   1 
ATOM   430  C  CA  . SER A 1 54  ? 45.661  -5.630  18.837  1.00 31.22  ? 54  SER A CA  1 
ATOM   431  C  C   . SER A 1 54  ? 45.053  -5.681  20.238  1.00 29.20  ? 54  SER A C   1 
ATOM   432  O  O   . SER A 1 54  ? 44.363  -4.750  20.651  1.00 30.96  ? 54  SER A O   1 
ATOM   433  C  CB  . SER A 1 54  ? 46.677  -4.524  18.674  1.00 27.31  ? 54  SER A CB  1 
ATOM   434  O  OG  . SER A 1 54  ? 47.698  -4.613  19.631  1.00 33.76  ? 54  SER A OG  1 
ATOM   435  N  N   . ALA A 1 55  ? 45.306  -6.785  20.945  1.00 34.68  ? 55  ALA A N   1 
ATOM   436  C  CA  . ALA A 1 55  ? 45.019  -6.898  22.368  1.00 37.16  ? 55  ALA A CA  1 
ATOM   437  C  C   . ALA A 1 55  ? 45.651  -5.746  23.164  1.00 43.09  ? 55  ALA A C   1 
ATOM   438  O  O   . ALA A 1 55  ? 45.172  -5.415  24.251  1.00 41.83  ? 55  ALA A O   1 
ATOM   439  C  CB  . ALA A 1 55  ? 45.513  -8.238  22.872  1.00 47.84  ? 55  ALA A CB  1 
ATOM   440  N  N   . ASN A 1 56  ? 46.712  -5.123  22.609  1.00 46.01  ? 56  ASN A N   1 
ATOM   441  C  CA  . ASN A 1 56  ? 47.475  -4.083  23.293  1.00 47.86  ? 56  ASN A CA  1 
ATOM   442  C  C   . ASN A 1 56  ? 46.887  -2.679  23.084  1.00 41.53  ? 56  ASN A C   1 
ATOM   443  O  O   . ASN A 1 56  ? 47.192  -1.781  23.873  1.00 42.97  ? 56  ASN A O   1 
ATOM   444  C  CB  . ASN A 1 56  ? 48.962  -4.120  22.894  1.00 55.48  ? 56  ASN A CB  1 
ATOM   445  C  CG  . ASN A 1 56  ? 49.626  -5.469  23.082  1.00 45.42  ? 56  ASN A CG  1 
ATOM   446  O  OD1 . ASN A 1 56  ? 49.670  -5.989  24.193  1.00 62.54  ? 56  ASN A OD1 1 
ATOM   447  N  ND2 . ASN A 1 56  ? 50.174  -6.035  22.018  1.00 52.43  ? 56  ASN A ND2 1 
ATOM   448  N  N   . LYS A 1 57  ? 46.061  -2.490  22.032  1.00 26.57  ? 57  LYS A N   1 
ATOM   449  C  CA  . LYS A 1 57  ? 45.389  -1.229  21.759  1.00 22.58  ? 57  LYS A CA  1 
ATOM   450  C  C   . LYS A 1 57  ? 44.033  -1.226  22.482  1.00 21.26  ? 57  LYS A C   1 
ATOM   451  O  O   . LYS A 1 57  ? 43.469  -2.277  22.818  1.00 22.96  ? 57  LYS A O   1 
ATOM   452  C  CB  . LYS A 1 57  ? 45.288  -0.886  20.254  1.00 19.85  ? 57  LYS A CB  1 
ATOM   453  C  CG  . LYS A 1 57  ? 46.557  -0.879  19.403  1.00 21.36  ? 57  LYS A CG  1 
ATOM   454  C  CD  . LYS A 1 57  ? 46.237  -0.801  17.896  1.00 24.54  ? 57  LYS A CD  1 
ATOM   455  C  CE  . LYS A 1 57  ? 47.457  -0.636  16.983  1.00 24.82  ? 57  LYS A CE  1 
ATOM   456  N  NZ  . LYS A 1 57  ? 48.088  0.706   17.115  1.00 30.96  ? 57  LYS A NZ  1 
ATOM   457  N  N   . GLN A 1 58  ? 43.497  -0.032  22.740  1.00 22.51  ? 58  GLN A N   1 
ATOM   458  C  CA  . GLN A 1 58  ? 42.164  0.132   23.307  1.00 19.29  ? 58  GLN A CA  1 
ATOM   459  C  C   . GLN A 1 58  ? 41.317  1.036   22.425  1.00 20.43  ? 58  GLN A C   1 
ATOM   460  O  O   . GLN A 1 58  ? 41.818  1.995   21.826  1.00 24.30  ? 58  GLN A O   1 
ATOM   461  C  CB  . GLN A 1 58  ? 42.241  0.725   24.714  1.00 20.38  ? 58  GLN A CB  1 
ATOM   462  C  CG  . GLN A 1 58  ? 42.785  -0.270  25.727  1.00 18.36  ? 58  GLN A CG  1 
ATOM   463  C  CD  . GLN A 1 58  ? 42.928  0.307   27.116  1.00 20.01  ? 58  GLN A CD  1 
ATOM   464  O  OE1 . GLN A 1 58  ? 42.526  1.447   27.408  1.00 21.55  ? 58  GLN A OE1 1 
ATOM   465  N  NE2 . GLN A 1 58  ? 43.494  -0.481  28.019  1.00 22.54  ? 58  GLN A NE2 1 
ATOM   466  N  N   . PHE A 1 59  ? 40.033  0.687   22.325  1.00 20.48  ? 59  PHE A N   1 
ATOM   467  C  CA  . PHE A 1 59  ? 39.145  1.323   21.374  1.00 18.43  ? 59  PHE A CA  1 
ATOM   468  C  C   . PHE A 1 59  ? 38.000  1.965   22.129  1.00 19.55  ? 59  PHE A C   1 
ATOM   469  O  O   . PHE A 1 59  ? 37.470  1.383   23.069  1.00 21.37  ? 59  PHE A O   1 
ATOM   470  C  CB  . PHE A 1 59  ? 38.686  0.288   20.360  1.00 19.80  ? 59  PHE A CB  1 
ATOM   471  C  CG  . PHE A 1 59  ? 39.872  -0.271  19.633  1.00 16.89  ? 59  PHE A CG  1 
ATOM   472  C  CD1 . PHE A 1 59  ? 40.327  0.342   18.482  1.00 22.33  ? 59  PHE A CD1 1 
ATOM   473  C  CD2 . PHE A 1 59  ? 40.578  -1.348  20.159  1.00 21.16  ? 59  PHE A CD2 1 
ATOM   474  C  CE1 . PHE A 1 59  ? 41.456  -0.147  17.841  1.00 22.46  ? 59  PHE A CE1 1 
ATOM   475  C  CE2 . PHE A 1 59  ? 41.687  -1.856  19.495  1.00 18.32  ? 59  PHE A CE2 1 
ATOM   476  C  CZ  . PHE A 1 59  ? 42.133  -1.235  18.345  1.00 22.16  ? 59  PHE A CZ  1 
ATOM   477  N  N   . LEU A 1 60  ? 37.628  3.156   21.674  1.00 19.26  ? 60  LEU A N   1 
ATOM   478  C  CA  . LEU A 1 60  ? 36.690  3.991   22.411  1.00 18.88  ? 60  LEU A CA  1 
ATOM   479  C  C   . LEU A 1 60  ? 35.240  3.525   22.192  1.00 21.27  ? 60  LEU A C   1 
ATOM   480  O  O   . LEU A 1 60  ? 34.737  3.437   21.083  1.00 20.18  ? 60  LEU A O   1 
ATOM   481  C  CB  . LEU A 1 60  ? 36.885  5.458   21.991  1.00 24.47  ? 60  LEU A CB  1 
ATOM   482  C  CG  . LEU A 1 60  ? 36.169  6.515   22.837  1.00 25.09  ? 60  LEU A CG  1 
ATOM   483  C  CD1 . LEU A 1 60  ? 36.610  6.473   24.298  1.00 29.80  ? 60  LEU A CD1 1 
ATOM   484  C  CD2 . LEU A 1 60  ? 36.385  7.904   22.265  1.00 31.92  ? 60  LEU A CD2 1 
ATOM   485  N  N   . LEU A 1 61  ? 34.554  3.217   23.291  1.00 22.16  ? 61  LEU A N   1 
ATOM   486  C  CA  . LEU A 1 61  ? 33.130  2.949   23.298  1.00 18.98  ? 61  LEU A CA  1 
ATOM   487  C  C   . LEU A 1 61  ? 32.436  4.202   23.819  1.00 19.68  ? 61  LEU A C   1 
ATOM   488  O  O   . LEU A 1 61  ? 32.798  4.661   24.886  1.00 24.07  ? 61  LEU A O   1 
ATOM   489  C  CB  . LEU A 1 61  ? 32.898  1.699   24.168  1.00 20.44  ? 61  LEU A CB  1 
ATOM   490  C  CG  . LEU A 1 61  ? 31.462  1.157   24.218  1.00 20.50  ? 61  LEU A CG  1 
ATOM   491  C  CD1 . LEU A 1 61  ? 31.137  0.354   22.951  1.00 21.08  ? 61  LEU A CD1 1 
ATOM   492  C  CD2 . LEU A 1 61  ? 31.255  0.302   25.462  1.00 23.51  ? 61  LEU A CD2 1 
ATOM   493  N  N   . THR A 1 62  ? 31.437  4.706   23.078  1.00 21.49  ? 62  THR A N   1 
ATOM   494  C  CA  . THR A 1 62  ? 30.695  5.921   23.428  1.00 25.18  ? 62  THR A CA  1 
ATOM   495  C  C   . THR A 1 62  ? 29.172  5.720   23.370  1.00 28.60  ? 62  THR A C   1 
ATOM   496  O  O   . THR A 1 62  ? 28.643  5.002   22.527  1.00 28.16  ? 62  THR A O   1 
ATOM   497  C  CB  . THR A 1 62  ? 31.093  7.122   22.554  1.00 31.05  ? 62  THR A CB  1 
ATOM   498  O  OG1 . THR A 1 62  ? 30.828  6.831   21.189  1.00 33.88  ? 62  THR A OG1 1 
ATOM   499  C  CG2 . THR A 1 62  ? 32.557  7.479   22.588  1.00 30.42  ? 62  THR A CG2 1 
ATOM   500  N  N   . ASN A 1 63  ? 28.459  6.343   24.314  1.00 31.14  ? 63  ASN A N   1 
ATOM   501  C  CA  . ASN A 1 63  ? 27.019  6.533   24.205  1.00 32.90  ? 63  ASN A CA  1 
ATOM   502  C  C   . ASN A 1 63  ? 26.796  7.968   23.723  1.00 33.69  ? 63  ASN A C   1 
ATOM   503  O  O   . ASN A 1 63  ? 27.093  8.908   24.464  1.00 36.68  ? 63  ASN A O   1 
ATOM   504  C  CB  . ASN A 1 63  ? 26.351  6.154   25.537  1.00 28.93  ? 63  ASN A CB  1 
ATOM   505  C  CG  . ASN A 1 63  ? 24.848  6.380   25.594  1.00 29.90  ? 63  ASN A CG  1 
ATOM   506  O  OD1 . ASN A 1 63  ? 24.276  7.090   24.755  1.00 25.55  ? 63  ASN A OD1 1 
ATOM   507  N  ND2 . ASN A 1 63  ? 24.199  5.791   26.598  1.00 22.96  ? 63  ASN A ND2 1 
ATOM   508  N  N   . ASN A 1 64  ? 26.336  8.171   22.477  1.00 42.92  ? 64  ASN A N   1 
ATOM   509  C  CA  . ASN A 1 64  ? 26.124  9.553   22.041  1.00 45.68  ? 64  ASN A CA  1 
ATOM   510  C  C   . ASN A 1 64  ? 24.642  9.919   22.106  1.00 47.65  ? 64  ASN A C   1 
ATOM   511  O  O   . ASN A 1 64  ? 24.277  11.011  21.655  1.00 50.26  ? 64  ASN A O   1 
ATOM   512  C  CB  . ASN A 1 64  ? 26.584  9.814   20.603  1.00 55.30  ? 64  ASN A CB  1 
ATOM   513  C  CG  . ASN A 1 64  ? 25.723  9.121   19.559  1.00 70.67  ? 64  ASN A CG  1 
ATOM   514  O  OD1 . ASN A 1 64  ? 24.894  8.258   19.862  1.00 66.07  ? 64  ASN A OD1 1 
ATOM   515  N  ND2 . ASN A 1 64  ? 25.940  9.458   18.301  1.00 69.75  ? 64  ASN A ND2 1 
ATOM   516  N  N   . GLY A 1 65  ? 23.804  8.989   22.595  1.00 39.12  ? 65  GLY A N   1 
ATOM   517  C  CA  . GLY A 1 65  ? 22.390  9.279   22.759  1.00 38.04  ? 65  GLY A CA  1 
ATOM   518  C  C   . GLY A 1 65  ? 21.433  8.457   21.882  1.00 38.25  ? 65  GLY A C   1 
ATOM   519  O  O   . GLY A 1 65  ? 20.250  8.532   22.203  1.00 26.84  ? 65  GLY A O   1 
ATOM   520  N  N   . HIS A 1 66  ? 21.906  7.692   20.846  1.00 40.06  ? 66  HIS A N   1 
ATOM   521  C  CA  . HIS A 1 66  ? 21.072  6.945   19.877  1.00 33.11  ? 66  HIS A CA  1 
ATOM   522  C  C   . HIS A 1 66  ? 21.378  5.432   19.756  1.00 24.12  ? 66  HIS A C   1 
ATOM   523  O  O   . HIS A 1 66  ? 20.522  4.599   19.356  1.00 24.38  ? 66  HIS A O   1 
ATOM   524  C  CB  . HIS A 1 66  ? 21.079  7.636   18.500  1.00 30.59  ? 66  HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 66  ? 20.988  9.132   18.498  1.00 31.26  ? 66  HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 66  ? 19.753  9.863   18.536  1.00 44.77  ? 66  HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 66  ? 21.945  10.081  18.389  1.00 36.61  ? 66  HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 66  ? 19.985  11.168  18.483  1.00 25.96  ? 66  HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 66  ? 21.337  11.315  18.413  1.00 34.95  ? 66  HIS A NE2 1 
ATOM   530  N  N   . SER A 1 67  ? 22.620  5.040   20.107  1.00 25.86  ? 67  SER A N   1 
ATOM   531  C  CA  . SER A 1 67  ? 23.076  3.643   20.138  1.00 23.50  ? 67  SER A CA  1 
ATOM   532  C  C   . SER A 1 67  ? 24.288  3.592   21.044  1.00 24.23  ? 67  SER A C   1 
ATOM   533  O  O   . SER A 1 67  ? 24.631  4.556   21.686  1.00 27.35  ? 67  SER A O   1 
ATOM   534  C  CB  . SER A 1 67  ? 23.413  3.146   18.728  1.00 19.75  ? 67  SER A CB  1 
ATOM   535  O  OG  . SER A 1 67  ? 23.752  1.741   18.648  1.00 24.31  ? 67  SER A OG  1 
ATOM   536  N  N   . VAL A 1 68  ? 24.974  2.480   21.053  1.00 25.24  ? 68  VAL A N   1 
ATOM   537  C  CA  . VAL A 1 68  ? 26.297  2.654   21.601  1.00 27.83  ? 68  VAL A CA  1 
ATOM   538  C  C   . VAL A 1 68  ? 27.253  2.360   20.442  1.00 26.20  ? 68  VAL A C   1 
ATOM   539  O  O   . VAL A 1 68  ? 26.943  1.430   19.702  1.00 25.29  ? 68  VAL A O   1 
ATOM   540  C  CB  . VAL A 1 68  ? 26.444  1.698   22.793  1.00 32.12  ? 68  VAL A CB  1 
ATOM   541  C  CG1 . VAL A 1 68  ? 25.799  0.329   22.601  1.00 31.80  ? 68  VAL A CG1 1 
ATOM   542  C  CG2 . VAL A 1 68  ? 27.862  1.566   23.265  1.00 27.86  ? 68  VAL A CG2 1 
ATOM   543  N  N   . LYS A 1 69  ? 28.368  3.121   20.282  1.00 22.14  ? 69  LYS A N   1 
ATOM   544  C  CA  . LYS A 1 69  ? 29.318  2.930   19.182  1.00 17.77  ? 69  LYS A CA  1 
ATOM   545  C  C   . LYS A 1 69  ? 30.690  2.511   19.732  1.00 16.83  ? 69  LYS A C   1 
ATOM   546  O  O   . LYS A 1 69  ? 31.186  3.106   20.711  1.00 21.04  ? 69  LYS A O   1 
ATOM   547  C  CB  . LYS A 1 69  ? 29.627  4.183   18.313  1.00 25.01  ? 69  LYS A CB  1 
ATOM   548  C  CG  . LYS A 1 69  ? 28.547  5.150   17.834  1.00 30.70  ? 69  LYS A CG  1 
ATOM   549  C  CD  . LYS A 1 69  ? 29.187  6.313   17.082  1.00 32.98  ? 69  LYS A CD  1 
ATOM   550  C  CE  . LYS A 1 69  ? 30.281  6.959   17.904  1.00 33.59  ? 69  LYS A CE  1 
ATOM   551  N  NZ  . LYS A 1 69  ? 30.871  8.128   17.219  1.00 29.78  ? 69  LYS A NZ  1 
ATOM   552  N  N   . LEU A 1 70  ? 31.312  1.515   19.060  1.00 13.15  ? 70  LEU A N   1 
ATOM   553  C  CA  . LEU A 1 70  ? 32.728  1.197   19.269  1.00 13.47  ? 70  LEU A CA  1 
ATOM   554  C  C   . LEU A 1 70  ? 33.527  1.728   18.072  1.00 13.55  ? 70  LEU A C   1 
ATOM   555  O  O   . LEU A 1 70  ? 33.224  1.362   16.929  1.00 14.19  ? 70  LEU A O   1 
ATOM   556  C  CB  . LEU A 1 70  ? 32.919  -0.308  19.382  1.00 17.39  ? 70  LEU A CB  1 
ATOM   557  C  CG  . LEU A 1 70  ? 34.377  -0.747  19.631  1.00 16.31  ? 70  LEU A CG  1 
ATOM   558  C  CD1 . LEU A 1 70  ? 34.868  -0.270  21.000  1.00 19.21  ? 70  LEU A CD1 1 
ATOM   559  C  CD2 . LEU A 1 70  ? 34.490  -2.242  19.509  1.00 18.34  ? 70  LEU A CD2 1 
ATOM   560  N  N   . ASN A 1 71  ? 34.500  2.610   18.365  1.00 15.21  ? 71  ASN A N   1 
ATOM   561  C  CA  . ASN A 1 71  ? 35.340  3.133   17.307  1.00 16.02  ? 71  ASN A CA  1 
ATOM   562  C  C   . ASN A 1 71  ? 36.298  2.050   16.834  1.00 16.84  ? 71  ASN A C   1 
ATOM   563  O  O   . ASN A 1 71  ? 36.780  1.270   17.637  1.00 18.25  ? 71  ASN A O   1 
ATOM   564  C  CB  . ASN A 1 71  ? 36.130  4.369   17.739  1.00 17.44  ? 71  ASN A CB  1 
ATOM   565  C  CG  . ASN A 1 71  ? 35.273  5.614   17.861  1.00 24.69  ? 71  ASN A CG  1 
ATOM   566  O  OD1 . ASN A 1 71  ? 34.097  5.617   17.478  1.00 24.82  ? 71  ASN A OD1 1 
ATOM   567  N  ND2 . ASN A 1 71  ? 35.854  6.679   18.391  1.00 27.05  ? 71  ASN A ND2 1 
ATOM   568  N  N   . LEU A 1 72  ? 36.589  2.059   15.538  1.00 16.24  ? 72  LEU A N   1 
ATOM   569  C  CA  . LEU A 1 72  ? 37.432  1.059   14.920  1.00 13.33  ? 72  LEU A CA  1 
ATOM   570  C  C   . LEU A 1 72  ? 38.560  1.752   14.180  1.00 14.20  ? 72  LEU A C   1 
ATOM   571  O  O   . LEU A 1 72  ? 38.386  2.841   13.650  1.00 17.92  ? 72  LEU A O   1 
ATOM   572  C  CB  . LEU A 1 72  ? 36.598  0.163   13.975  1.00 13.91  ? 72  LEU A CB  1 
ATOM   573  C  CG  . LEU A 1 72  ? 35.517  -0.638  14.677  1.00 12.80  ? 72  LEU A CG  1 
ATOM   574  C  CD1 . LEU A 1 72  ? 34.557  -1.216  13.653  1.00 11.83  ? 72  LEU A CD1 1 
ATOM   575  C  CD2 . LEU A 1 72  ? 36.076  -1.774  15.540  1.00 15.48  ? 72  LEU A CD2 1 
ATOM   576  N  N   . PRO A 1 73  ? 39.728  1.095   14.039  1.00 16.90  ? 73  PRO A N   1 
ATOM   577  C  CA  . PRO A 1 73  ? 40.857  1.742   13.393  1.00 15.85  ? 73  PRO A CA  1 
ATOM   578  C  C   . PRO A 1 73  ? 40.756  1.630   11.871  1.00 14.03  ? 73  PRO A C   1 
ATOM   579  O  O   . PRO A 1 73  ? 40.285  0.641   11.324  1.00 14.43  ? 73  PRO A O   1 
ATOM   580  C  CB  . PRO A 1 73  ? 42.039  0.933   13.949  1.00 16.75  ? 73  PRO A CB  1 
ATOM   581  C  CG  . PRO A 1 73  ? 41.491  -0.478  14.140  1.00 17.83  ? 73  PRO A CG  1 
ATOM   582  C  CD  . PRO A 1 73  ? 40.028  -0.276  14.498  1.00 17.44  ? 73  PRO A CD  1 
ATOM   583  N  N   . SER A 1 74  ? 41.371  2.583   11.184  1.00 18.35  ? 74  SER A N   1 
ATOM   584  C  CA  . SER A 1 74  ? 41.226  2.629   9.736   1.00 16.50  ? 74  SER A CA  1 
ATOM   585  C  C   . SER A 1 74  ? 42.033  1.575   8.958   1.00 15.03  ? 74  SER A C   1 
ATOM   586  O  O   . SER A 1 74  ? 41.852  1.462   7.739   1.00 19.73  ? 74  SER A O   1 
ATOM   587  C  CB  . SER A 1 74  ? 41.429  4.028   9.225   1.00 21.28  ? 74  SER A CB  1 
ATOM   588  O  OG  . SER A 1 74  ? 42.772  4.419   9.445   1.00 23.66  ? 74  SER A OG  1 
ATOM   589  N  N   . ASP A 1 75  ? 42.963  0.859   9.597   1.00 17.49  ? 75  ASP A N   1 
ATOM   590  C  CA  . ASP A 1 75  ? 43.671  -0.199  8.896   1.00 16.18  ? 75  ASP A CA  1 
ATOM   591  C  C   . ASP A 1 75  ? 42.789  -1.454  8.812   1.00 12.83  ? 75  ASP A C   1 
ATOM   592  O  O   . ASP A 1 75  ? 43.102  -2.368  8.064   1.00 15.85  ? 75  ASP A O   1 
ATOM   593  C  CB  . ASP A 1 75  ? 45.020  -0.462  9.579   1.00 21.25  ? 75  ASP A CB  1 
ATOM   594  C  CG  . ASP A 1 75  ? 44.838  -0.876  11.037  1.00 20.96  ? 75  ASP A CG  1 
ATOM   595  O  OD1 . ASP A 1 75  ? 44.401  -0.067  11.859  1.00 24.66  ? 75  ASP A OD1 1 
ATOM   596  O  OD2 . ASP A 1 75  ? 45.110  -1.998  11.343  1.00 23.04  ? 75  ASP A OD2 1 
ATOM   597  N  N   . MET A 1 76  ? 41.701  -1.515  9.565   1.00 11.90  ? 76  MET A N   1 
ATOM   598  C  CA  . MET A 1 76  ? 40.723  -2.596  9.473   1.00 12.62  ? 76  MET A CA  1 
ATOM   599  C  C   . MET A 1 76  ? 39.893  -2.326  8.210   1.00 12.11  ? 76  MET A C   1 
ATOM   600  O  O   . MET A 1 76  ? 39.452  -1.210  8.009   1.00 11.67  ? 76  MET A O   1 
ATOM   601  C  CB  . MET A 1 76  ? 39.824  -2.541  10.716  1.00 13.06  ? 76  MET A CB  1 
ATOM   602  C  CG  . MET A 1 76  ? 38.724  -3.580  10.708  1.00 14.26  ? 76  MET A CG  1 
ATOM   603  S  SD  . MET A 1 76  ? 37.893  -3.485  12.288  1.00 14.46  ? 76  MET A SD  1 
ATOM   604  C  CE  . MET A 1 76  ? 36.342  -4.249  11.837  1.00 15.43  ? 76  MET A CE  1 
ATOM   605  N  N   . HIS A 1 77  ? 39.669  -3.313  7.340   1.00 10.76  ? 77  HIS A N   1 
ATOM   606  C  CA  . HIS A 1 77  ? 38.981  -3.014  6.090   1.00 10.49  ? 77  HIS A CA  1 
ATOM   607  C  C   . HIS A 1 77  ? 38.392  -4.251  5.438   1.00 10.95  ? 77  HIS A C   1 
ATOM   608  O  O   . HIS A 1 77  ? 38.751  -5.356  5.834   1.00 11.76  ? 77  HIS A O   1 
ATOM   609  C  CB  . HIS A 1 77  ? 39.918  -2.303  5.099   1.00 11.33  ? 77  HIS A CB  1 
ATOM   610  C  CG  . HIS A 1 77  ? 41.088  -3.102  4.633   1.00 12.74  ? 77  HIS A CG  1 
ATOM   611  N  ND1 . HIS A 1 77  ? 42.323  -3.118  5.272   1.00 16.75  ? 77  HIS A ND1 1 
ATOM   612  C  CD2 . HIS A 1 77  ? 41.229  -3.872  3.517   1.00 14.61  ? 77  HIS A CD2 1 
ATOM   613  C  CE1 . HIS A 1 77  ? 43.155  -3.884  4.566   1.00 16.91  ? 77  HIS A CE1 1 
ATOM   614  N  NE2 . HIS A 1 77  ? 42.512  -4.361  3.479   1.00 15.19  ? 77  HIS A NE2 1 
ATOM   615  N  N   . ILE A 1 78  ? 37.452  -3.995  4.509   1.00 12.13  ? 78  ILE A N   1 
ATOM   616  C  CA  . ILE A 1 78  ? 36.889  -5.030  3.655   1.00 11.77  ? 78  ILE A CA  1 
ATOM   617  C  C   . ILE A 1 78  ? 37.671  -5.056  2.354   1.00 12.33  ? 78  ILE A C   1 
ATOM   618  O  O   . ILE A 1 78  ? 37.960  -4.023  1.810   1.00 14.64  ? 78  ILE A O   1 
ATOM   619  C  CB  . ILE A 1 78  ? 35.417  -4.720  3.317   1.00 13.27  ? 78  ILE A CB  1 
ATOM   620  C  CG1 . ILE A 1 78  ? 34.501  -4.691  4.545   1.00 15.41  ? 78  ILE A CG1 1 
ATOM   621  C  CG2 . ILE A 1 78  ? 34.955  -5.663  2.221   1.00 16.08  ? 78  ILE A CG2 1 
ATOM   622  C  CD1 . ILE A 1 78  ? 33.159  -3.985  4.274   1.00 19.80  ? 78  ILE A CD1 1 
ATOM   623  N  N   . GLN A 1 79  ? 38.131  -6.239  1.946   1.00 14.24  ? 79  GLN A N   1 
ATOM   624  C  CA  . GLN A 1 79  ? 38.640  -6.476  0.603   1.00 16.27  ? 79  GLN A CA  1 
ATOM   625  C  C   . GLN A 1 79  ? 37.587  -7.241  -0.203  1.00 15.20  ? 79  GLN A C   1 
ATOM   626  O  O   . GLN A 1 79  ? 36.897  -8.129  0.316   1.00 17.67  ? 79  GLN A O   1 
ATOM   627  C  CB  . GLN A 1 79  ? 39.938  -7.294  0.699   1.00 17.59  ? 79  GLN A CB  1 
ATOM   628  C  CG  . GLN A 1 79  ? 40.560  -7.604  -0.646  1.00 25.04  ? 79  GLN A CG  1 
ATOM   629  C  CD  . GLN A 1 79  ? 42.041  -7.400  -0.460  1.00 33.17  ? 79  GLN A CD  1 
ATOM   630  O  OE1 . GLN A 1 79  ? 42.578  -6.287  -0.600  1.00 39.36  ? 79  GLN A OE1 1 
ATOM   631  N  NE2 . GLN A 1 79  ? 42.671  -8.447  0.027   1.00 47.76  ? 79  GLN A NE2 1 
ATOM   632  N  N   . GLY A 1 80  ? 37.469  -6.889  -1.491  1.00 17.74  ? 80  GLY A N   1 
ATOM   633  C  CA  . GLY A 1 80  ? 36.581  -7.587  -2.419  1.00 20.30  ? 80  GLY A CA  1 
ATOM   634  C  C   . GLY A 1 80  ? 35.528  -6.682  -3.089  1.00 18.44  ? 80  GLY A C   1 
ATOM   635  O  O   . GLY A 1 80  ? 34.914  -7.091  -4.067  1.00 21.28  ? 80  GLY A O   1 
ATOM   636  N  N   . LEU A 1 81  ? 35.311  -5.466  -2.565  1.00 16.66  ? 81  LEU A N   1 
ATOM   637  C  CA  . LEU A 1 81  ? 34.468  -4.474  -3.243  1.00 17.76  ? 81  LEU A CA  1 
ATOM   638  C  C   . LEU A 1 81  ? 35.291  -3.698  -4.285  1.00 18.47  ? 81  LEU A C   1 
ATOM   639  O  O   . LEU A 1 81  ? 36.506  -3.948  -4.438  1.00 24.60  ? 81  LEU A O   1 
ATOM   640  C  CB  . LEU A 1 81  ? 33.807  -3.571  -2.199  1.00 16.74  ? 81  LEU A CB  1 
ATOM   641  C  CG  . LEU A 1 81  ? 32.888  -4.299  -1.213  1.00 15.99  ? 81  LEU A CG  1 
ATOM   642  C  CD1 . LEU A 1 81  ? 32.460  -3.359  -0.089  1.00 17.51  ? 81  LEU A CD1 1 
ATOM   643  C  CD2 . LEU A 1 81  ? 31.668  -4.887  -1.947  1.00 18.98  ? 81  LEU A CD2 1 
ATOM   644  N  N   . GLN A 1 82  ? 34.650  -2.710  -4.961  1.00 20.13  ? 82  GLN A N   1 
ATOM   645  C  CA  . GLN A 1 82  ? 35.247  -2.025  -6.113  1.00 21.69  ? 82  GLN A CA  1 
ATOM   646  C  C   . GLN A 1 82  ? 36.272  -0.988  -5.661  1.00 24.29  ? 82  GLN A C   1 
ATOM   647  O  O   . GLN A 1 82  ? 37.057  -0.420  -6.438  1.00 28.15  ? 82  GLN A O   1 
ATOM   648  C  CB  . GLN A 1 82  ? 34.232  -1.249  -6.973  1.00 25.18  ? 82  GLN A CB  1 
ATOM   649  C  CG  . GLN A 1 82  ? 33.298  -2.123  -7.790  1.00 27.46  ? 82  GLN A CG  1 
ATOM   650  C  CD  . GLN A 1 82  ? 33.866  -2.671  -9.081  1.00 34.75  ? 82  GLN A CD  1 
ATOM   651  O  OE1 . GLN A 1 82  ? 34.859  -2.163  -9.631  1.00 35.34  ? 82  GLN A OE1 1 
ATOM   652  N  NE2 . GLN A 1 82  ? 33.199  -3.700  -9.618  1.00 32.51  ? 82  GLN A NE2 1 
ATOM   653  N  N   . SER A 1 83  ? 36.229  -0.730  -4.373  1.00 19.28  ? 83  SER A N   1 
ATOM   654  C  CA  . SER A 1 83  ? 37.233  0.074   -3.698  1.00 17.47  ? 83  SER A CA  1 
ATOM   655  C  C   . SER A 1 83  ? 37.469  -0.586  -2.340  1.00 14.59  ? 83  SER A C   1 
ATOM   656  O  O   . SER A 1 83  ? 36.619  -1.352  -1.868  1.00 16.46  ? 83  SER A O   1 
ATOM   657  C  CB  . SER A 1 83  ? 36.686  1.468   -3.495  1.00 18.89  ? 83  SER A CB  1 
ATOM   658  O  OG  . SER A 1 83  ? 36.419  2.066   -4.744  1.00 20.76  ? 83  SER A OG  1 
ATOM   659  N  N   . ARG A 1 84  ? 38.575  -0.218  -1.678  1.00 15.17  ? 84  ARG A N   1 
ATOM   660  C  CA  . ARG A 1 84  ? 38.770  -0.603  -0.291  1.00 12.76  ? 84  ARG A CA  1 
ATOM   661  C  C   . ARG A 1 84  ? 37.857  0.235   0.598   1.00 15.12  ? 84  ARG A C   1 
ATOM   662  O  O   . ARG A 1 84  ? 37.770  1.453   0.433   1.00 14.27  ? 84  ARG A O   1 
ATOM   663  C  CB  . ARG A 1 84  ? 40.225  -0.421  0.144   1.00 15.69  ? 84  ARG A CB  1 
ATOM   664  C  CG  . ARG A 1 84  ? 40.414  -0.708  1.633   1.00 14.51  ? 84  ARG A CG  1 
ATOM   665  C  CD  . ARG A 1 84  ? 41.855  -0.548  2.086   1.00 15.81  ? 84  ARG A CD  1 
ATOM   666  N  NE  . ARG A 1 84  ? 42.666  -1.595  1.479   1.00 15.46  ? 84  ARG A NE  1 
ATOM   667  C  CZ  . ARG A 1 84  ? 43.956  -1.797  1.827   1.00 15.13  ? 84  ARG A CZ  1 
ATOM   668  N  NH1 . ARG A 1 84  ? 44.522  -0.937  2.657   1.00 17.59  ? 84  ARG A NH1 1 
ATOM   669  N  NH2 . ARG A 1 84  ? 44.700  -2.729  1.243   1.00 16.48  ? 84  ARG A NH2 1 
ATOM   670  N  N   . TYR A 1 85  ? 37.123  -0.444  1.491   1.00 12.85  ? 85  TYR A N   1 
ATOM   671  C  CA  . TYR A 1 85  ? 36.297  0.222   2.475   1.00 12.04  ? 85  TYR A CA  1 
ATOM   672  C  C   . TYR A 1 85  ? 36.859  -0.064  3.880   1.00 11.14  ? 85  TYR A C   1 
ATOM   673  O  O   . TYR A 1 85  ? 36.992  -1.220  4.299   1.00 14.03  ? 85  TYR A O   1 
ATOM   674  C  CB  . TYR A 1 85  ? 34.843  -0.296  2.426   1.00 12.89  ? 85  TYR A CB  1 
ATOM   675  C  CG  . TYR A 1 85  ? 34.071  0.280   1.257   1.00 11.85  ? 85  TYR A CG  1 
ATOM   676  C  CD1 . TYR A 1 85  ? 34.230  -0.224  -0.033  1.00 14.90  ? 85  TYR A CD1 1 
ATOM   677  C  CD2 . TYR A 1 85  ? 33.220  1.357   1.417   1.00 14.19  ? 85  TYR A CD2 1 
ATOM   678  C  CE1 . TYR A 1 85  ? 33.533  0.271   -1.139  1.00 13.52  ? 85  TYR A CE1 1 
ATOM   679  C  CE2 . TYR A 1 85  ? 32.538  1.855   0.325   1.00 13.85  ? 85  TYR A CE2 1 
ATOM   680  C  CZ  . TYR A 1 85  ? 32.711  1.366   -0.956  1.00 14.47  ? 85  TYR A CZ  1 
ATOM   681  O  OH  . TYR A 1 85  ? 32.014  1.907   -2.007  1.00 19.39  ? 85  TYR A OH  1 
ATOM   682  N  N   . SER A 1 86  ? 37.286  1.008   4.548   1.00 11.80  ? 86  SER A N   1 
ATOM   683  C  CA  . SER A 1 86  ? 37.965  0.946   5.853   1.00 10.75  ? 86  SER A CA  1 
ATOM   684  C  C   . SER A 1 86  ? 36.959  1.113   6.972   1.00 10.44  ? 86  SER A C   1 
ATOM   685  O  O   . SER A 1 86  ? 36.011  1.880   6.808   1.00 13.12  ? 86  SER A O   1 
ATOM   686  C  CB  . SER A 1 86  ? 39.060  1.974   5.950   1.00 11.53  ? 86  SER A CB  1 
ATOM   687  O  OG  . SER A 1 86  ? 40.059  1.702   4.977   1.00 13.52  ? 86  SER A OG  1 
ATOM   688  N  N   . ALA A 1 87  ? 37.166  0.360   8.057   1.00 12.07  ? 87  ALA A N   1 
ATOM   689  C  CA  . ALA A 1 87  ? 36.285  0.450   9.193   1.00 13.60  ? 87  ALA A CA  1 
ATOM   690  C  C   . ALA A 1 87  ? 36.289  1.826   9.827   1.00 12.54  ? 87  ALA A C   1 
ATOM   691  O  O   . ALA A 1 87  ? 37.345  2.510   9.946   1.00 14.70  ? 87  ALA A O   1 
ATOM   692  C  CB  . ALA A 1 87  ? 36.578  -0.613  10.211  1.00 13.59  ? 87  ALA A CB  1 
ATOM   693  N  N   . THR A 1 88  ? 35.115  2.202   10.362  1.00 12.06  ? 88  THR A N   1 
ATOM   694  C  CA  . THR A 1 88  ? 35.102  3.398   11.222  1.00 11.71  ? 88  THR A CA  1 
ATOM   695  C  C   . THR A 1 88  ? 34.468  3.159   12.605  1.00 10.35  ? 88  THR A C   1 
ATOM   696  O  O   . THR A 1 88  ? 34.966  3.654   13.625  1.00 12.69  ? 88  THR A O   1 
ATOM   697  C  CB  . THR A 1 88  ? 34.456  4.622   10.542  1.00 13.36  ? 88  THR A CB  1 
ATOM   698  O  OG1 . THR A 1 88  ? 34.472  5.787   11.375  1.00 21.19  ? 88  THR A OG1 1 
ATOM   699  C  CG2 . THR A 1 88  ? 33.005  4.372   10.218  1.00 17.37  ? 88  THR A CG2 1 
ATOM   700  N  N   . GLN A 1 89  ? 33.420  2.308   12.664  1.00 10.88  ? 89  GLN A N   1 
ATOM   701  C  CA  . GLN A 1 89  ? 32.752  2.072   13.944  1.00 11.38  ? 89  GLN A CA  1 
ATOM   702  C  C   . GLN A 1 89  ? 31.779  0.907   13.812  1.00 11.13  ? 89  GLN A C   1 
ATOM   703  O  O   . GLN A 1 89  ? 31.371  0.586   12.706  1.00 11.61  ? 89  GLN A O   1 
ATOM   704  C  CB  . GLN A 1 89  ? 32.007  3.310   14.473  1.00 12.34  ? 89  GLN A CB  1 
ATOM   705  C  CG  . GLN A 1 89  ? 30.959  3.923   13.507  1.00 13.96  ? 89  GLN A CG  1 
ATOM   706  C  CD  . GLN A 1 89  ? 29.554  3.669   14.007  1.00 11.59  ? 89  GLN A CD  1 
ATOM   707  O  OE1 . GLN A 1 89  ? 29.216  2.522   14.359  1.00 13.39  ? 89  GLN A OE1 1 
ATOM   708  N  NE2 . GLN A 1 89  ? 28.728  4.669   14.005  1.00 19.97  ? 89  GLN A NE2 1 
ATOM   709  N  N   . LEU A 1 90  ? 31.408  0.282   14.933  1.00 10.27  ? 90  LEU A N   1 
ATOM   710  C  CA  . LEU A 1 90  ? 30.269  -0.620  14.953  1.00 10.32  ? 90  LEU A CA  1 
ATOM   711  C  C   . LEU A 1 90  ? 29.269  -0.182  16.009  1.00 9.69   ? 90  LEU A C   1 
ATOM   712  O  O   . LEU A 1 90  ? 29.627  0.523   16.969  1.00 12.49  ? 90  LEU A O   1 
ATOM   713  C  CB  . LEU A 1 90  ? 30.700  -2.097  15.045  1.00 11.24  ? 90  LEU A CB  1 
ATOM   714  C  CG  . LEU A 1 90  ? 31.521  -2.554  16.275  1.00 12.48  ? 90  LEU A CG  1 
ATOM   715  C  CD1 . LEU A 1 90  ? 30.596  -2.755  17.483  1.00 13.64  ? 90  LEU A CD1 1 
ATOM   716  C  CD2 . LEU A 1 90  ? 32.197  -3.894  15.954  1.00 14.12  ? 90  LEU A CD2 1 
ATOM   717  N  N   . HIS A 1 91  ? 28.022  -0.619  15.816  1.00 10.64  ? 91  HIS A N   1 
ATOM   718  C  CA  . HIS A 1 91  ? 26.938  -0.327  16.749  1.00 8.85   ? 91  HIS A CA  1 
ATOM   719  C  C   . HIS A 1 91  ? 25.790  -1.298  16.532  1.00 10.13  ? 91  HIS A C   1 
ATOM   720  O  O   . HIS A 1 91  ? 25.893  -2.161  15.659  1.00 10.22  ? 91  HIS A O   1 
ATOM   721  C  CB  . HIS A 1 91  ? 26.495  1.115   16.587  1.00 9.03   ? 91  HIS A CB  1 
ATOM   722  C  CG  . HIS A 1 91  ? 25.875  1.333   15.229  1.00 9.01   ? 91  HIS A CG  1 
ATOM   723  N  ND1 . HIS A 1 91  ? 26.601  1.759   14.160  1.00 10.67  ? 91  HIS A ND1 1 
ATOM   724  C  CD2 . HIS A 1 91  ? 24.644  1.062   14.731  1.00 8.83   ? 91  HIS A CD2 1 
ATOM   725  C  CE1 . HIS A 1 91  ? 25.805  1.775   13.069  1.00 9.67   ? 91  HIS A CE1 1 
ATOM   726  N  NE2 . HIS A 1 91  ? 24.585  1.332   13.416  1.00 8.51   ? 91  HIS A NE2 1 
ATOM   727  N  N   . LEU A 1 92  ? 24.777  -1.228  17.426  1.00 9.53   ? 92  LEU A N   1 
ATOM   728  C  CA  . LEU A 1 92  ? 23.673  -2.173  17.368  1.00 9.29   ? 92  LEU A CA  1 
ATOM   729  C  C   . LEU A 1 92  ? 22.331  -1.439  17.401  1.00 9.64   ? 92  LEU A C   1 
ATOM   730  O  O   . LEU A 1 92  ? 22.273  -0.243  17.772  1.00 10.47  ? 92  LEU A O   1 
ATOM   731  C  CB  . LEU A 1 92  ? 23.784  -3.164  18.553  1.00 12.14  ? 92  LEU A CB  1 
ATOM   732  C  CG  . LEU A 1 92  ? 25.026  -4.078  18.600  1.00 9.94   ? 92  LEU A CG  1 
ATOM   733  C  CD1 . LEU A 1 92  ? 26.106  -3.544  19.527  1.00 14.81  ? 92  LEU A CD1 1 
ATOM   734  C  CD2 . LEU A 1 92  ? 24.632  -5.486  18.983  1.00 14.92  ? 92  LEU A CD2 1 
ATOM   735  N  N   . HIS A 1 93  ? 21.289  -2.217  17.050  1.00 9.05   ? 93  HIS A N   1 
ATOM   736  C  CA  . HIS A 1 93  ? 19.885  -1.798  17.148  1.00 9.15   ? 93  HIS A CA  1 
ATOM   737  C  C   . HIS A 1 93  ? 19.135  -2.919  17.788  1.00 7.16   ? 93  HIS A C   1 
ATOM   738  O  O   . HIS A 1 93  ? 19.436  -4.117  17.506  1.00 9.34   ? 93  HIS A O   1 
ATOM   739  C  CB  . HIS A 1 93  ? 19.340  -1.529  15.721  1.00 8.34   ? 93  HIS A CB  1 
ATOM   740  C  CG  . HIS A 1 93  ? 20.123  -0.552  14.916  1.00 8.27   ? 93  HIS A CG  1 
ATOM   741  N  ND1 . HIS A 1 93  ? 19.769  0.792   14.900  1.00 9.00   ? 93  HIS A ND1 1 
ATOM   742  C  CD2 . HIS A 1 93  ? 21.209  -0.651  14.110  1.00 9.49   ? 93  HIS A CD2 1 
ATOM   743  C  CE1 . HIS A 1 93  ? 20.618  1.471   14.097  1.00 12.42  ? 93  HIS A CE1 1 
ATOM   744  N  NE2 . HIS A 1 93  ? 21.545  0.632   13.661  1.00 9.73   ? 93  HIS A NE2 1 
ATOM   745  N  N   . TRP A 1 94  ? 18.103  -2.571  18.582  1.00 8.29   ? 94  TRP A N   1 
ATOM   746  C  CA  . TRP A 1 94  ? 17.368  -3.581  19.346  1.00 8.83   ? 94  TRP A CA  1 
ATOM   747  C  C   . TRP A 1 94  ? 15.980  -3.022  19.733  1.00 10.45  ? 94  TRP A C   1 
ATOM   748  O  O   . TRP A 1 94  ? 15.639  -1.856  19.491  1.00 10.82  ? 94  TRP A O   1 
ATOM   749  C  CB  . TRP A 1 94  ? 18.195  -4.041  20.591  1.00 10.10  ? 94  TRP A CB  1 
ATOM   750  C  CG  . TRP A 1 94  ? 18.443  -2.890  21.536  1.00 9.65   ? 94  TRP A CG  1 
ATOM   751  C  CD1 . TRP A 1 94  ? 17.630  -2.429  22.568  1.00 10.08  ? 94  TRP A CD1 1 
ATOM   752  C  CD2 . TRP A 1 94  ? 19.656  -2.084  21.561  1.00 10.52  ? 94  TRP A CD2 1 
ATOM   753  N  NE1 . TRP A 1 94  ? 18.216  -1.291  23.115  1.00 11.02  ? 94  TRP A NE1 1 
ATOM   754  C  CE2 . TRP A 1 94  ? 19.481  -1.112  22.580  1.00 10.09  ? 94  TRP A CE2 1 
ATOM   755  C  CE3 . TRP A 1 94  ? 20.844  -2.040  20.807  1.00 10.47  ? 94  TRP A CE3 1 
ATOM   756  C  CZ2 . TRP A 1 94  ? 20.455  -0.140  22.857  1.00 12.03  ? 94  TRP A CZ2 1 
ATOM   757  C  CZ3 . TRP A 1 94  ? 21.799  -1.065  21.037  1.00 11.24  ? 94  TRP A CZ3 1 
ATOM   758  C  CH2 . TRP A 1 94  ? 21.642  -0.189  22.125  1.00 11.29  ? 94  TRP A CH2 1 
ATOM   759  N  N   . GLY A 1 95  ? 15.166  -3.896  20.322  1.00 10.54  ? 95  GLY A N   1 
ATOM   760  C  CA  . GLY A 1 95  ? 13.797  -3.614  20.677  1.00 11.44  ? 95  GLY A CA  1 
ATOM   761  C  C   . GLY A 1 95  ? 13.672  -3.322  22.165  1.00 10.41  ? 95  GLY A C   1 
ATOM   762  O  O   . GLY A 1 95  ? 14.317  -2.433  22.682  1.00 11.80  ? 95  GLY A O   1 
ATOM   763  N  N   . ASN A 1 96  ? 12.875  -4.143  22.847  1.00 11.99  ? 96  ASN A N   1 
ATOM   764  C  CA  . ASN A 1 96  ? 12.617  -3.959  24.282  1.00 12.04  ? 96  ASN A CA  1 
ATOM   765  C  C   . ASN A 1 96  ? 12.121  -5.252  24.877  1.00 12.38  ? 96  ASN A C   1 
ATOM   766  O  O   . ASN A 1 96  ? 11.728  -6.123  24.100  1.00 12.56  ? 96  ASN A O   1 
ATOM   767  C  CB  . ASN A 1 96  ? 11.646  -2.809  24.561  1.00 13.54  ? 96  ASN A CB  1 
ATOM   768  C  CG  . ASN A 1 96  ? 10.206  -3.158  24.220  1.00 13.42  ? 96  ASN A CG  1 
ATOM   769  O  OD1 . ASN A 1 96  ? 9.518   -3.769  25.037  1.00 16.68  ? 96  ASN A OD1 1 
ATOM   770  N  ND2 . ASN A 1 96  ? 9.749   -2.841  22.996  1.00 16.08  ? 96  ASN A ND2 1 
ATOM   771  N  N   . PRO A 1 97  ? 12.212  -5.420  26.215  1.00 13.26  ? 97  PRO A N   1 
ATOM   772  C  CA  . PRO A 1 97  ? 11.961  -6.728  26.821  1.00 14.74  ? 97  PRO A CA  1 
ATOM   773  C  C   . PRO A 1 97  ? 10.542  -7.179  26.518  1.00 12.45  ? 97  PRO A C   1 
ATOM   774  O  O   . PRO A 1 97  ? 10.279  -8.399  26.535  1.00 17.11  ? 97  PRO A O   1 
ATOM   775  C  CB  . PRO A 1 97  ? 12.250  -6.510  28.317  1.00 15.91  ? 97  PRO A CB  1 
ATOM   776  C  CG  . PRO A 1 97  ? 13.239  -5.375  28.304  1.00 16.40  ? 97  PRO A CG  1 
ATOM   777  C  CD  . PRO A 1 97  ? 12.811  -4.462  27.157  1.00 15.32  ? 97  PRO A CD  1 
ATOM   778  N  N   . ASN A 1 98  ? 9.570   -6.268  26.389  1.00 13.18  ? 98  ASN A N   1 
ATOM   779  C  CA  . ASN A 1 98  ? 8.196   -6.707  26.156  1.00 13.55  ? 98  ASN A CA  1 
ATOM   780  C  C   . ASN A 1 98  ? 7.913   -7.031  24.685  1.00 15.68  ? 98  ASN A C   1 
ATOM   781  O  O   . ASN A 1 98  ? 6.862   -7.569  24.383  1.00 19.24  ? 98  ASN A O   1 
ATOM   782  C  CB  . ASN A 1 98  ? 7.204   -5.610  26.549  1.00 16.88  ? 98  ASN A CB  1 
ATOM   783  C  CG  . ASN A 1 98  ? 6.961   -5.614  28.050  1.00 23.21  ? 98  ASN A CG  1 
ATOM   784  O  OD1 . ASN A 1 98  ? 7.269   -6.566  28.766  1.00 33.12  ? 98  ASN A OD1 1 
ATOM   785  N  ND2 . ASN A 1 98  ? 6.466   -4.500  28.545  1.00 32.92  ? 98  ASN A ND2 1 
ATOM   786  N  N   . ASP A 1 99  ? 8.808   -6.645  23.773  1.00 12.80  ? 99  ASP A N   1 
ATOM   787  C  CA  . ASP A 1 99  ? 8.683   -6.975  22.357  1.00 11.66  ? 99  ASP A CA  1 
ATOM   788  C  C   . ASP A 1 99  ? 10.099  -7.054  21.790  1.00 13.71  ? 99  ASP A C   1 
ATOM   789  O  O   . ASP A 1 99  ? 10.582  -6.089  21.186  1.00 13.49  ? 99  ASP A O   1 
ATOM   790  C  CB  . ASP A 1 99  ? 7.814   -5.956  21.606  1.00 13.97  ? 99  ASP A CB  1 
ATOM   791  C  CG  . ASP A 1 99  ? 7.327   -6.441  20.251  1.00 12.26  ? 99  ASP A CG  1 
ATOM   792  O  OD1 . ASP A 1 99  ? 7.809   -7.480  19.733  1.00 17.25  ? 99  ASP A OD1 1 
ATOM   793  O  OD2 . ASP A 1 99  ? 6.460   -5.780  19.736  1.00 21.02  ? 99  ASP A OD2 1 
ATOM   794  N  N   . PRO A 1 100 ? 10.796  -8.183  22.051  1.00 12.14  ? 100 PRO A N   1 
ATOM   795  C  CA  . PRO A 1 100 ? 12.250  -8.273  21.835  1.00 12.16  ? 100 PRO A CA  1 
ATOM   796  C  C   . PRO A 1 100 ? 12.609  -8.575  20.369  1.00 12.26  ? 100 PRO A C   1 
ATOM   797  O  O   . PRO A 1 100 ? 13.205  -9.609  20.035  1.00 14.23  ? 100 PRO A O   1 
ATOM   798  C  CB  . PRO A 1 100 ? 12.651  -9.364  22.836  1.00 13.76  ? 100 PRO A CB  1 
ATOM   799  C  CG  . PRO A 1 100 ? 11.458  -10.287 22.829  1.00 13.34  ? 100 PRO A CG  1 
ATOM   800  C  CD  . PRO A 1 100 ? 10.246  -9.396  22.749  1.00 12.74  ? 100 PRO A CD  1 
ATOM   801  N  N   . HIS A 1 101 ? 12.156  -7.718  19.475  1.00 13.87  ? 101 HIS A N   1 
ATOM   802  C  CA  . HIS A 1 101 ? 12.270  -7.968  18.032  1.00 13.06  ? 101 HIS A CA  1 
ATOM   803  C  C   . HIS A 1 101 ? 12.665  -6.710  17.279  1.00 12.57  ? 101 HIS A C   1 
ATOM   804  O  O   . HIS A 1 101 ? 11.919  -6.249  16.410  1.00 19.62  ? 101 HIS A O   1 
ATOM   805  C  CB  . HIS A 1 101 ? 10.912  -8.440  17.515  1.00 15.59  ? 101 HIS A CB  1 
ATOM   806  C  CG  . HIS A 1 101 ? 10.424  -9.642  18.233  1.00 12.57  ? 101 HIS A CG  1 
ATOM   807  N  ND1 . HIS A 1 101 ? 10.877  -10.966 18.035  1.00 17.94  ? 101 HIS A ND1 1 
ATOM   808  C  CD2 . HIS A 1 101 ? 9.433   -9.702  19.151  1.00 13.20  ? 101 HIS A CD2 1 
ATOM   809  C  CE1 . HIS A 1 101 ? 10.167  -11.742 18.836  1.00 18.81  ? 101 HIS A CE1 1 
ATOM   810  N  NE2 . HIS A 1 101 ? 9.295   -11.014 19.508  1.00 16.53  ? 101 HIS A NE2 1 
ATOM   811  N  N   . GLY A 1 102 ? 13.896  -6.299  17.484  1.00 10.02  ? 102 GLY A N   1 
ATOM   812  C  CA  . GLY A 1 102 ? 14.336  -4.946  17.153  1.00 9.37   ? 102 GLY A CA  1 
ATOM   813  C  C   . GLY A 1 102 ? 15.424  -4.892  16.060  1.00 8.70   ? 102 GLY A C   1 
ATOM   814  O  O   . GLY A 1 102 ? 16.124  -3.917  15.943  1.00 10.16  ? 102 GLY A O   1 
ATOM   815  N  N   . SER A 1 103 ? 15.619  -5.927  15.221  1.00 8.62   ? 103 SER A N   1 
ATOM   816  C  CA  . SER A 1 103 ? 16.438  -5.804  14.017  1.00 7.66   ? 103 SER A CA  1 
ATOM   817  C  C   . SER A 1 103 ? 15.853  -4.688  13.124  1.00 8.81   ? 103 SER A C   1 
ATOM   818  O  O   . SER A 1 103 ? 14.685  -4.364  13.235  1.00 10.34  ? 103 SER A O   1 
ATOM   819  C  CB  . SER A 1 103 ? 16.613  -7.120  13.287  1.00 9.59   ? 103 SER A CB  1 
ATOM   820  O  OG  . SER A 1 103 ? 15.392  -7.461  12.638  1.00 8.70   ? 103 SER A OG  1 
ATOM   821  N  N   . GLU A 1 104 ? 16.687  -4.133  12.253  1.00 8.79   ? 104 GLU A N   1 
ATOM   822  C  CA  . GLU A 1 104 ? 16.233  -3.162  11.272  1.00 8.12   ? 104 GLU A CA  1 
ATOM   823  C  C   . GLU A 1 104 ? 15.737  -3.899  10.017  1.00 7.47   ? 104 GLU A C   1 
ATOM   824  O  O   . GLU A 1 104 ? 14.570  -3.759  9.615   1.00 8.19   ? 104 GLU A O   1 
ATOM   825  C  CB  . GLU A 1 104 ? 17.366  -2.156  10.944  1.00 9.90   ? 104 GLU A CB  1 
ATOM   826  C  CG  . GLU A 1 104 ? 17.896  -1.495  12.223  1.00 10.24  ? 104 GLU A CG  1 
ATOM   827  C  CD  . GLU A 1 104 ? 18.301  -0.055  11.952  1.00 6.97   ? 104 GLU A CD  1 
ATOM   828  O  OE1 . GLU A 1 104 ? 19.369  0.124   11.331  1.00 9.32   ? 104 GLU A OE1 1 
ATOM   829  O  OE2 . GLU A 1 104 ? 17.502  0.829   12.215  1.00 9.88   ? 104 GLU A OE2 1 
ATOM   830  N  N   . HIS A 1 105 ? 16.626  -4.686  9.392   1.00 8.72   ? 105 HIS A N   1 
ATOM   831  C  CA  . HIS A 1 105 ? 16.152  -5.540  8.298   1.00 8.28   ? 105 HIS A CA  1 
ATOM   832  C  C   . HIS A 1 105 ? 15.270  -6.687  8.814   1.00 8.45   ? 105 HIS A C   1 
ATOM   833  O  O   . HIS A 1 105 ? 15.452  -7.195  9.928   1.00 9.17   ? 105 HIS A O   1 
ATOM   834  C  CB  . HIS A 1 105 ? 17.338  -6.100  7.516   1.00 8.99   ? 105 HIS A CB  1 
ATOM   835  C  CG  . HIS A 1 105 ? 18.101  -5.019  6.831   1.00 8.62   ? 105 HIS A CG  1 
ATOM   836  N  ND1 . HIS A 1 105 ? 19.179  -4.332  7.406   1.00 8.71   ? 105 HIS A ND1 1 
ATOM   837  C  CD2 . HIS A 1 105 ? 17.933  -4.514  5.578   1.00 8.72   ? 105 HIS A CD2 1 
ATOM   838  C  CE1 . HIS A 1 105 ? 19.587  -3.385  6.567   1.00 9.10   ? 105 HIS A CE1 1 
ATOM   839  N  NE2 . HIS A 1 105 ? 18.811  -3.457  5.443   1.00 9.11   ? 105 HIS A NE2 1 
ATOM   840  N  N   . THR A 1 106 ? 14.269  -7.045  8.009   1.00 8.42   ? 106 THR A N   1 
ATOM   841  C  CA  . THR A 1 106 ? 13.451  -8.217  8.272   1.00 8.74   ? 106 THR A CA  1 
ATOM   842  C  C   . THR A 1 106 ? 13.645  -9.230  7.142   1.00 8.22   ? 106 THR A C   1 
ATOM   843  O  O   . THR A 1 106 ? 14.144  -8.899  6.065   1.00 10.06  ? 106 THR A O   1 
ATOM   844  C  CB  . THR A 1 106 ? 11.976  -7.796  8.453   1.00 8.62   ? 106 THR A CB  1 
ATOM   845  O  OG1 . THR A 1 106 ? 11.524  -7.206  7.229   1.00 9.32   ? 106 THR A OG1 1 
ATOM   846  C  CG2 . THR A 1 106 ? 11.763  -6.854  9.618   1.00 11.07  ? 106 THR A CG2 1 
ATOM   847  N  N   . VAL A 1 107 ? 13.292  -10.491 7.434   1.00 10.08  ? 107 VAL A N   1 
ATOM   848  C  CA  . VAL A 1 107 ? 13.431  -11.549 6.431   1.00 10.87  ? 107 VAL A CA  1 
ATOM   849  C  C   . VAL A 1 107 ? 12.055  -12.187 6.309   1.00 10.39  ? 107 VAL A C   1 
ATOM   850  O  O   . VAL A 1 107 ? 11.520  -12.700 7.294   1.00 12.16  ? 107 VAL A O   1 
ATOM   851  C  CB  . VAL A 1 107 ? 14.501  -12.614 6.764   1.00 11.69  ? 107 VAL A CB  1 
ATOM   852  C  CG1 . VAL A 1 107 ? 14.528  -13.761 5.761   1.00 12.18  ? 107 VAL A CG1 1 
ATOM   853  C  CG2 . VAL A 1 107 ? 15.893  -11.974 6.923   1.00 13.15  ? 107 VAL A CG2 1 
ATOM   854  N  N   . SER A 1 108 ? 11.447  -12.065 5.127   1.00 11.55  ? 108 SER A N   1 
ATOM   855  C  CA  . SER A 1 108 ? 10.080  -12.582 4.943   1.00 10.56  ? 108 SER A CA  1 
ATOM   856  C  C   . SER A 1 108 ? 9.130   -12.019 6.017   1.00 13.91  ? 108 SER A C   1 
ATOM   857  O  O   . SER A 1 108 ? 8.276   -12.748 6.530   1.00 13.30  ? 108 SER A O   1 
ATOM   858  C  CB  . SER A 1 108 ? 10.100  -14.084 5.010   1.00 16.13  ? 108 SER A CB  1 
ATOM   859  O  OG  . SER A 1 108 ? 10.757  -14.557 3.852   1.00 21.49  ? 108 SER A OG  1 
ATOM   860  N  N   . GLY A 1 109 ? 9.301   -10.731 6.343   1.00 11.15  ? 109 GLY A N   1 
ATOM   861  C  CA  . GLY A 1 109 ? 8.452   -9.974  7.252   1.00 13.58  ? 109 GLY A CA  1 
ATOM   862  C  C   . GLY A 1 109 ? 8.782   -10.156 8.745   1.00 14.53  ? 109 GLY A C   1 
ATOM   863  O  O   . GLY A 1 109 ? 8.163   -9.530  9.613   1.00 19.56  ? 109 GLY A O   1 
ATOM   864  N  N   . GLN A 1 110 ? 9.772   -10.987 9.065   1.00 13.23  ? 110 GLN A N   1 
ATOM   865  C  CA  . GLN A 1 110 ? 10.147  -11.312 10.441  1.00 12.98  ? 110 GLN A CA  1 
ATOM   866  C  C   . GLN A 1 110 ? 11.366  -10.536 10.930  1.00 10.68  ? 110 GLN A C   1 
ATOM   867  O  O   . GLN A 1 110 ? 12.387  -10.467 10.255  1.00 10.47  ? 110 GLN A O   1 
ATOM   868  C  CB  . GLN A 1 110 ? 10.426  -12.801 10.537  1.00 16.62  ? 110 GLN A CB  1 
ATOM   869  C  CG  . GLN A 1 110 ? 9.282   -13.629 10.001  1.00 18.92  ? 110 GLN A CG  1 
ATOM   870  C  CD  . GLN A 1 110 ? 7.897   -13.181 10.456  1.00 20.88  ? 110 GLN A CD  1 
ATOM   871  O  OE1 . GLN A 1 110 ? 7.569   -13.182 11.660  1.00 19.42  ? 110 GLN A OE1 1 
ATOM   872  N  NE2 . GLN A 1 110 ? 7.051   -12.811 9.485   1.00 19.71  ? 110 GLN A NE2 1 
ATOM   873  N  N   . HIS A 1 111 ? 11.176  -9.879  12.070  1.00 13.12  ? 111 HIS A N   1 
ATOM   874  C  CA  . HIS A 1 111 ? 12.269  -9.235  12.772  1.00 12.69  ? 111 HIS A CA  1 
ATOM   875  C  C   . HIS A 1 111 ? 13.098  -10.264 13.507  1.00 12.71  ? 111 HIS A C   1 
ATOM   876  O  O   . HIS A 1 111 ? 12.610  -11.347 13.869  1.00 21.62  ? 111 HIS A O   1 
ATOM   877  C  CB  . HIS A 1 111 ? 11.766  -8.259  13.838  1.00 17.86  ? 111 HIS A CB  1 
ATOM   878  C  CG  . HIS A 1 111 ? 11.434  -6.912  13.336  1.00 12.12  ? 111 HIS A CG  1 
ATOM   879  N  ND1 . HIS A 1 111 ? 10.173  -6.553  12.866  1.00 20.33  ? 111 HIS A ND1 1 
ATOM   880  C  CD2 . HIS A 1 111 ? 12.246  -5.829  13.184  1.00 11.53  ? 111 HIS A CD2 1 
ATOM   881  C  CE1 . HIS A 1 111 ? 10.213  -5.273  12.496  1.00 17.52  ? 111 HIS A CE1 1 
ATOM   882  N  NE2 . HIS A 1 111 ? 11.483  -4.843  12.634  1.00 19.33  ? 111 HIS A NE2 1 
ATOM   883  N  N   . PHE A 1 112 ? 14.378  -10.014 13.585  1.00 10.37  ? 112 PHE A N   1 
ATOM   884  C  CA  . PHE A 1 112 ? 15.290  -10.671 14.498  1.00 9.98   ? 112 PHE A CA  1 
ATOM   885  C  C   . PHE A 1 112 ? 15.330  -9.848  15.773  1.00 10.96  ? 112 PHE A C   1 
ATOM   886  O  O   . PHE A 1 112 ? 14.803  -8.727  15.837  1.00 10.12  ? 112 PHE A O   1 
ATOM   887  C  CB  . PHE A 1 112 ? 16.651  -10.844 13.819  1.00 10.68  ? 112 PHE A CB  1 
ATOM   888  C  CG  . PHE A 1 112 ? 16.648  -11.952 12.808  1.00 11.70  ? 112 PHE A CG  1 
ATOM   889  C  CD1 . PHE A 1 112 ? 16.130  -11.767 11.523  1.00 14.56  ? 112 PHE A CD1 1 
ATOM   890  C  CD2 . PHE A 1 112 ? 17.081  -13.224 13.179  1.00 15.24  ? 112 PHE A CD2 1 
ATOM   891  C  CE1 . PHE A 1 112 ? 16.075  -12.873 10.656  1.00 17.65  ? 112 PHE A CE1 1 
ATOM   892  C  CE2 . PHE A 1 112 ? 17.000  -14.324 12.318  1.00 16.74  ? 112 PHE A CE2 1 
ATOM   893  C  CZ  . PHE A 1 112 ? 16.506  -14.127 11.051  1.00 19.98  ? 112 PHE A CZ  1 
ATOM   894  N  N   . ALA A 1 113 ? 15.957  -10.398 16.802  1.00 9.58   ? 113 ALA A N   1 
ATOM   895  C  CA  . ALA A 1 113 ? 15.946  -9.741  18.092  1.00 10.19  ? 113 ALA A CA  1 
ATOM   896  C  C   . ALA A 1 113 ? 16.712  -8.431  18.000  1.00 10.41  ? 113 ALA A C   1 
ATOM   897  O  O   . ALA A 1 113 ? 16.374  -7.482  18.685  1.00 10.71  ? 113 ALA A O   1 
ATOM   898  C  CB  . ALA A 1 113 ? 16.575  -10.703 19.114  1.00 11.54  ? 113 ALA A CB  1 
ATOM   899  N  N   . ALA A 1 114 ? 17.829  -8.423  17.278  1.00 9.25   ? 114 ALA A N   1 
ATOM   900  C  CA  . ALA A 1 114 ? 18.662  -7.227  17.221  1.00 8.05   ? 114 ALA A CA  1 
ATOM   901  C  C   . ALA A 1 114 ? 19.488  -7.275  15.925  1.00 7.92   ? 114 ALA A C   1 
ATOM   902  O  O   . ALA A 1 114 ? 19.427  -8.300  15.186  1.00 9.42   ? 114 ALA A O   1 
ATOM   903  C  CB  . ALA A 1 114 ? 19.590  -7.135  18.445  1.00 10.95  ? 114 ALA A CB  1 
ATOM   904  N  N   . GLU A 1 115 ? 20.304  -6.247  15.709  1.00 9.44   ? 115 GLU A N   1 
ATOM   905  C  CA  . GLU A 1 115 ? 21.151  -6.204  14.522  1.00 8.06   ? 115 GLU A CA  1 
ATOM   906  C  C   . GLU A 1 115 ? 22.418  -5.403  14.808  1.00 10.14  ? 115 GLU A C   1 
ATOM   907  O  O   . GLU A 1 115 ? 22.372  -4.322  15.430  1.00 9.94   ? 115 GLU A O   1 
ATOM   908  C  CB  . GLU A 1 115 ? 20.352  -5.592  13.359  1.00 9.16   ? 115 GLU A CB  1 
ATOM   909  C  CG  . GLU A 1 115 ? 20.991  -5.635  11.985  1.00 8.81   ? 115 GLU A CG  1 
ATOM   910  C  CD  . GLU A 1 115 ? 20.050  -5.238  10.835  1.00 7.62   ? 115 GLU A CD  1 
ATOM   911  O  OE1 . GLU A 1 115 ? 18.857  -5.498  11.001  1.00 8.24   ? 115 GLU A OE1 1 
ATOM   912  O  OE2 . GLU A 1 115 ? 20.511  -4.706  9.796   1.00 8.60   ? 115 GLU A OE2 1 
ATOM   913  N  N   . LEU A 1 116 ? 23.548  -5.958  14.359  1.00 8.79   ? 116 LEU A N   1 
ATOM   914  C  CA  . LEU A 1 116 ? 24.859  -5.301  14.502  1.00 9.71   ? 116 LEU A CA  1 
ATOM   915  C  C   . LEU A 1 116 ? 25.207  -4.720  13.127  1.00 9.39   ? 116 LEU A C   1 
ATOM   916  O  O   . LEU A 1 116 ? 25.105  -5.425  12.120  1.00 8.60   ? 116 LEU A O   1 
ATOM   917  C  CB  . LEU A 1 116 ? 25.914  -6.366  14.848  1.00 12.27  ? 116 LEU A CB  1 
ATOM   918  C  CG  . LEU A 1 116 ? 27.387  -5.918  14.712  1.00 12.89  ? 116 LEU A CG  1 
ATOM   919  C  CD1 . LEU A 1 116 ? 27.741  -5.012  15.841  1.00 16.23  ? 116 LEU A CD1 1 
ATOM   920  C  CD2 . LEU A 1 116 ? 28.326  -7.155  14.660  1.00 14.73  ? 116 LEU A CD2 1 
ATOM   921  N  N   . HIS A 1 117 ? 25.702  -3.482  13.125  1.00 8.96   ? 117 HIS A N   1 
ATOM   922  C  CA  . HIS A 1 117 ? 26.262  -2.826  11.927  1.00 9.87   ? 117 HIS A CA  1 
ATOM   923  C  C   . HIS A 1 117 ? 27.734  -2.498  12.101  1.00 7.93   ? 117 HIS A C   1 
ATOM   924  O  O   . HIS A 1 117 ? 28.072  -1.863  13.100  1.00 10.08  ? 117 HIS A O   1 
ATOM   925  C  CB  . HIS A 1 117 ? 25.508  -1.574  11.660  1.00 8.97   ? 117 HIS A CB  1 
ATOM   926  C  CG  . HIS A 1 117 ? 24.104  -1.883  11.218  1.00 7.30   ? 117 HIS A CG  1 
ATOM   927  N  ND1 . HIS A 1 117 ? 23.073  -0.959  11.343  1.00 8.56   ? 117 HIS A ND1 1 
ATOM   928  C  CD2 . HIS A 1 117 ? 23.564  -3.030  10.688  1.00 7.81   ? 117 HIS A CD2 1 
ATOM   929  C  CE1 . HIS A 1 117 ? 21.970  -1.454  10.835  1.00 9.05   ? 117 HIS A CE1 1 
ATOM   930  N  NE2 . HIS A 1 117 ? 22.231  -2.743  10.487  1.00 9.38   ? 117 HIS A NE2 1 
ATOM   931  N  N   . ILE A 1 118 ? 28.566  -2.888  11.135  1.00 8.49   ? 118 ILE A N   1 
ATOM   932  C  CA  . ILE A 1 118 ? 29.998  -2.525  11.125  1.00 9.67   ? 118 ILE A CA  1 
ATOM   933  C  C   . ILE A 1 118 ? 30.108  -1.586  9.924   1.00 11.59  ? 118 ILE A C   1 
ATOM   934  O  O   . ILE A 1 118 ? 29.935  -1.981  8.789   1.00 10.82  ? 118 ILE A O   1 
ATOM   935  C  CB  . ILE A 1 118 ? 30.947  -3.741  10.957  1.00 10.70  ? 118 ILE A CB  1 
ATOM   936  C  CG1 . ILE A 1 118 ? 30.590  -4.827  11.983  1.00 9.62   ? 118 ILE A CG1 1 
ATOM   937  C  CG2 . ILE A 1 118 ? 32.416  -3.283  11.124  1.00 11.28  ? 118 ILE A CG2 1 
ATOM   938  C  CD1 . ILE A 1 118 ? 31.458  -6.067  11.849  1.00 11.58  ? 118 ILE A CD1 1 
ATOM   939  N  N   . VAL A 1 119 ? 30.299  -0.284  10.220  1.00 9.22   ? 119 VAL A N   1 
ATOM   940  C  CA  . VAL A 1 119 ? 30.332  0.824   9.249   1.00 10.41  ? 119 VAL A CA  1 
ATOM   941  C  C   . VAL A 1 119 ? 31.729  0.917   8.674   1.00 8.75   ? 119 VAL A C   1 
ATOM   942  O  O   . VAL A 1 119 ? 32.704  1.028   9.446   1.00 10.77  ? 119 VAL A O   1 
ATOM   943  C  CB  . VAL A 1 119 ? 29.871  2.135   9.903   1.00 9.87   ? 119 VAL A CB  1 
ATOM   944  C  CG1 . VAL A 1 119 ? 29.870  3.247   8.845   1.00 12.12  ? 119 VAL A CG1 1 
ATOM   945  C  CG2 . VAL A 1 119 ? 28.482  1.976   10.553  1.00 11.80  ? 119 VAL A CG2 1 
ATOM   946  N  N   . HIS A 1 120 ? 31.779  1.021   7.338   1.00 9.88   ? 120 HIS A N   1 
ATOM   947  C  CA  . HIS A 1 120 ? 33.075  1.257   6.663   1.00 11.11  ? 120 HIS A CA  1 
ATOM   948  C  C   . HIS A 1 120 ? 32.865  2.394   5.679   1.00 10.84  ? 120 HIS A C   1 
ATOM   949  O  O   . HIS A 1 120 ? 31.737  2.591   5.218   1.00 10.98  ? 120 HIS A O   1 
ATOM   950  C  CB  . HIS A 1 120 ? 33.504  0.007   5.871   1.00 11.75  ? 120 HIS A CB  1 
ATOM   951  C  CG  . HIS A 1 120 ? 33.684  -1.230  6.686   1.00 12.06  ? 120 HIS A CG  1 
ATOM   952  N  ND1 . HIS A 1 120 ? 32.620  -1.931  7.266   1.00 10.62  ? 120 HIS A ND1 1 
ATOM   953  C  CD2 . HIS A 1 120 ? 34.784  -1.961  6.994   1.00 10.75  ? 120 HIS A CD2 1 
ATOM   954  C  CE1 . HIS A 1 120 ? 33.086  -3.029  7.856   1.00 11.36  ? 120 HIS A CE1 1 
ATOM   955  N  NE2 . HIS A 1 120 ? 34.382  -3.088  7.686   1.00 12.00  ? 120 HIS A NE2 1 
ATOM   956  N  N   . TYR A 1 121 ? 33.955  3.045   5.272   1.00 11.68  ? 121 TYR A N   1 
ATOM   957  C  CA  . TYR A 1 121 ? 33.916  4.138   4.291   1.00 13.26  ? 121 TYR A CA  1 
ATOM   958  C  C   . TYR A 1 121 ? 34.909  3.854   3.160   1.00 11.77  ? 121 TYR A C   1 
ATOM   959  O  O   . TYR A 1 121 ? 35.921  3.181   3.358   1.00 12.71  ? 121 TYR A O   1 
ATOM   960  C  CB  . TYR A 1 121 ? 34.181  5.534   4.874   1.00 15.14  ? 121 TYR A CB  1 
ATOM   961  C  CG  . TYR A 1 121 ? 35.580  5.715   5.431   1.00 16.28  ? 121 TYR A CG  1 
ATOM   962  C  CD1 . TYR A 1 121 ? 35.942  5.166   6.656   1.00 17.47  ? 121 TYR A CD1 1 
ATOM   963  C  CD2 . TYR A 1 121 ? 36.556  6.411   4.723   1.00 17.43  ? 121 TYR A CD2 1 
ATOM   964  C  CE1 . TYR A 1 121 ? 37.249  5.252   7.127   1.00 16.44  ? 121 TYR A CE1 1 
ATOM   965  C  CE2 . TYR A 1 121 ? 37.858  6.555   5.201   1.00 18.58  ? 121 TYR A CE2 1 
ATOM   966  C  CZ  . TYR A 1 121 ? 38.192  5.986   6.428   1.00 18.84  ? 121 TYR A CZ  1 
ATOM   967  O  OH  . TYR A 1 121 ? 39.472  6.082   6.895   1.00 20.49  ? 121 TYR A OH  1 
ATOM   968  N  N   . ASN A 1 122 ? 34.667  4.437   1.991   1.00 14.02  ? 122 ASN A N   1 
ATOM   969  C  CA  . ASN A 1 122 ? 35.532  4.313   0.837   1.00 14.83  ? 122 ASN A CA  1 
ATOM   970  C  C   . ASN A 1 122 ? 36.797  5.137   1.069   1.00 15.77  ? 122 ASN A C   1 
ATOM   971  O  O   . ASN A 1 122 ? 36.853  6.346   0.824   1.00 16.73  ? 122 ASN A O   1 
ATOM   972  C  CB  . ASN A 1 122 ? 34.786  4.716   -0.428  1.00 17.09  ? 122 ASN A CB  1 
ATOM   973  C  CG  . ASN A 1 122 ? 35.580  4.407   -1.672  1.00 19.15  ? 122 ASN A CG  1 
ATOM   974  O  OD1 . ASN A 1 122 ? 36.828  4.304   -1.650  1.00 19.13  ? 122 ASN A OD1 1 
ATOM   975  N  ND2 . ASN A 1 122 ? 34.831  4.171   -2.737  1.00 24.91  ? 122 ASN A ND2 1 
ATOM   976  N  N   . SER A 1 123 ? 37.831  4.421   1.505   1.00 14.18  ? 123 SER A N   1 
ATOM   977  C  CA  . SER A 1 123 ? 39.085  5.090   1.821   1.00 13.43  ? 123 SER A CA  1 
ATOM   978  C  C   . SER A 1 123 ? 39.991  5.293   0.599   1.00 15.17  ? 123 SER A C   1 
ATOM   979  O  O   . SER A 1 123 ? 40.979  6.037   0.695   1.00 18.93  ? 123 SER A O   1 
ATOM   980  C  CB  . SER A 1 123 ? 39.853  4.378   2.911   1.00 11.59  ? 123 SER A CB  1 
ATOM   981  O  OG  . SER A 1 123 ? 39.947  2.976   2.630   1.00 15.14  ? 123 SER A OG  1 
ATOM   982  N  N   . ASP A 1 124 ? 39.664  4.651   -0.531  1.00 15.55  ? 124 ASP A N   1 
ATOM   983  C  CA  . ASP A 1 124 ? 40.381  4.967   -1.758  1.00 20.07  ? 124 ASP A CA  1 
ATOM   984  C  C   . ASP A 1 124 ? 40.003  6.360   -2.240  1.00 21.32  ? 124 ASP A C   1 
ATOM   985  O  O   . ASP A 1 124 ? 40.805  6.997   -2.896  1.00 28.23  ? 124 ASP A O   1 
ATOM   986  C  CB  . ASP A 1 124 ? 40.132  3.931   -2.848  1.00 19.23  ? 124 ASP A CB  1 
ATOM   987  C  CG  . ASP A 1 124 ? 40.718  2.567   -2.535  1.00 14.45  ? 124 ASP A CG  1 
ATOM   988  O  OD1 . ASP A 1 124 ? 41.763  2.502   -1.822  1.00 17.42  ? 124 ASP A OD1 1 
ATOM   989  O  OD2 . ASP A 1 124 ? 40.187  1.580   -3.049  1.00 19.56  ? 124 ASP A OD2 1 
ATOM   990  N  N   . LEU A 1 125 ? 38.787  6.826   -1.911  1.00 24.22  ? 125 LEU A N   1 
ATOM   991  C  CA  . LEU A 1 125 ? 38.288  8.118   -2.395  1.00 26.05  ? 125 LEU A CA  1 
ATOM   992  C  C   . LEU A 1 125 ? 38.290  9.236   -1.347  1.00 26.95  ? 125 LEU A C   1 
ATOM   993  O  O   . LEU A 1 125 ? 38.370  10.399  -1.723  1.00 33.26  ? 125 LEU A O   1 
ATOM   994  C  CB  . LEU A 1 125 ? 36.894  7.928   -3.007  1.00 26.52  ? 125 LEU A CB  1 
ATOM   995  C  CG  . LEU A 1 125 ? 36.797  7.653   -4.503  1.00 35.68  ? 125 LEU A CG  1 
ATOM   996  C  CD1 . LEU A 1 125 ? 37.310  6.269   -4.886  1.00 38.80  ? 125 LEU A CD1 1 
ATOM   997  C  CD2 . LEU A 1 125 ? 35.339  7.776   -4.930  1.00 42.53  ? 125 LEU A CD2 1 
ATOM   998  N  N   . TYR A 1 126 ? 38.057  8.907   -0.073  1.00 20.99  ? 126 TYR A N   1 
ATOM   999  C  CA  . TYR A 1 126 ? 37.763  9.899   0.943   1.00 24.56  ? 126 TYR A CA  1 
ATOM   1000 C  C   . TYR A 1 126 ? 38.650  9.705   2.165   1.00 22.49  ? 126 TYR A C   1 
ATOM   1001 O  O   . TYR A 1 126 ? 38.993  8.583   2.525   1.00 21.73  ? 126 TYR A O   1 
ATOM   1002 C  CB  . TYR A 1 126 ? 36.298  9.804   1.356   1.00 19.91  ? 126 TYR A CB  1 
ATOM   1003 C  CG  . TYR A 1 126 ? 35.389  9.902   0.157   1.00 19.53  ? 126 TYR A CG  1 
ATOM   1004 C  CD1 . TYR A 1 126 ? 35.346  11.082  -0.581  1.00 21.37  ? 126 TYR A CD1 1 
ATOM   1005 C  CD2 . TYR A 1 126 ? 34.554  8.862   -0.203  1.00 26.10  ? 126 TYR A CD2 1 
ATOM   1006 C  CE1 . TYR A 1 126 ? 34.559  11.181  -1.715  1.00 24.39  ? 126 TYR A CE1 1 
ATOM   1007 C  CE2 . TYR A 1 126 ? 33.766  8.948   -1.333  1.00 24.18  ? 126 TYR A CE2 1 
ATOM   1008 C  CZ  . TYR A 1 126 ? 33.743  10.117  -2.075  1.00 27.67  ? 126 TYR A CZ  1 
ATOM   1009 O  OH  . TYR A 1 126 ? 32.943  10.193  -3.181  1.00 33.68  ? 126 TYR A OH  1 
ATOM   1010 N  N   . PRO A 1 127 ? 39.009  10.786  2.864   1.00 27.66  ? 127 PRO A N   1 
ATOM   1011 C  CA  . PRO A 1 127 ? 39.789  10.700  4.098   1.00 30.94  ? 127 PRO A CA  1 
ATOM   1012 C  C   . PRO A 1 127 ? 39.141  10.140  5.369   1.00 26.81  ? 127 PRO A C   1 
ATOM   1013 O  O   . PRO A 1 127 ? 39.865  9.674   6.256   1.00 34.44  ? 127 PRO A O   1 
ATOM   1014 C  CB  . PRO A 1 127 ? 40.234  12.153  4.337   1.00 36.92  ? 127 PRO A CB  1 
ATOM   1015 C  CG  . PRO A 1 127 ? 39.178  12.971  3.652   1.00 36.34  ? 127 PRO A CG  1 
ATOM   1016 C  CD  . PRO A 1 127 ? 38.783  12.172  2.432   1.00 30.86  ? 127 PRO A CD  1 
ATOM   1017 N  N   . ASP A 1 128 ? 37.805  10.228  5.486   1.00 29.69  ? 128 ASP A N   1 
ATOM   1018 C  CA  . ASP A 1 128 ? 37.135  9.803   6.713   1.00 30.90  ? 128 ASP A CA  1 
ATOM   1019 C  C   . ASP A 1 128 ? 35.695  9.464   6.349   1.00 25.73  ? 128 ASP A C   1 
ATOM   1020 O  O   . ASP A 1 128 ? 35.292  9.764   5.233   1.00 23.62  ? 128 ASP A O   1 
ATOM   1021 C  CB  . ASP A 1 128 ? 37.376  10.799  7.871   1.00 30.80  ? 128 ASP A CB  1 
ATOM   1022 C  CG  . ASP A 1 128 ? 37.133  12.243  7.455   1.00 34.26  ? 128 ASP A CG  1 
ATOM   1023 O  OD1 . ASP A 1 128 ? 36.102  12.510  6.823   1.00 34.13  ? 128 ASP A OD1 1 
ATOM   1024 O  OD2 . ASP A 1 128 ? 37.991  13.108  7.768   1.00 42.21  ? 128 ASP A OD2 1 
ATOM   1025 N  N   . ALA A 1 129 ? 34.973  8.777   7.240   1.00 25.50  ? 129 ALA A N   1 
ATOM   1026 C  CA  . ALA A 1 129 ? 33.565  8.453   7.032   1.00 26.86  ? 129 ALA A CA  1 
ATOM   1027 C  C   . ALA A 1 129 ? 32.709  9.719   6.923   1.00 25.79  ? 129 ALA A C   1 
ATOM   1028 O  O   . ALA A 1 129 ? 31.754  9.726   6.143   1.00 29.42  ? 129 ALA A O   1 
ATOM   1029 C  CB  . ALA A 1 129 ? 33.056  7.594   8.169   1.00 26.16  ? 129 ALA A CB  1 
ATOM   1030 N  N   . SER A 1 130 ? 33.035  10.756  7.713   1.00 32.25  ? 130 SER A N   1 
ATOM   1031 C  CA  . SER A 1 130 ? 32.276  12.001  7.731   1.00 29.45  ? 130 SER A CA  1 
ATOM   1032 C  C   . SER A 1 130 ? 32.157  12.560  6.311   1.00 30.04  ? 130 SER A C   1 
ATOM   1033 O  O   . SER A 1 130 ? 31.048  12.881  5.841   1.00 32.85  ? 130 SER A O   1 
ATOM   1034 C  CB  . SER A 1 130 ? 32.872  12.982  8.735   1.00 36.19  ? 130 SER A CB  1 
ATOM   1035 O  OG  . SER A 1 130 ? 32.174  14.202  8.701   1.00 40.11  ? 130 SER A OG  1 
ATOM   1036 N  N   . THR A 1 131 ? 33.311  12.621  5.617   1.00 25.73  ? 131 THR A N   1 
ATOM   1037 C  CA  . THR A 1 131 ? 33.434  13.222  4.289   1.00 22.86  ? 131 THR A CA  1 
ATOM   1038 C  C   . THR A 1 131 ? 32.830  12.260  3.257   1.00 18.68  ? 131 THR A C   1 
ATOM   1039 O  O   . THR A 1 131 ? 32.138  12.686  2.331   1.00 23.43  ? 131 THR A O   1 
ATOM   1040 C  CB  . THR A 1 131 ? 34.910  13.520  3.990   1.00 20.18  ? 131 THR A CB  1 
ATOM   1041 O  OG1 . THR A 1 131 ? 35.496  14.299  5.040   1.00 33.28  ? 131 THR A OG1 1 
ATOM   1042 C  CG2 . THR A 1 131 ? 35.117  14.110  2.607   1.00 24.34  ? 131 THR A CG2 1 
ATOM   1043 N  N   . ALA A 1 132 ? 33.066  10.949  3.451   1.00 20.50  ? 132 ALA A N   1 
ATOM   1044 C  CA  . ALA A 1 132 ? 32.472  9.921   2.600   1.00 19.78  ? 132 ALA A CA  1 
ATOM   1045 C  C   . ALA A 1 132 ? 30.937  9.871   2.660   1.00 21.43  ? 132 ALA A C   1 
ATOM   1046 O  O   . ALA A 1 132 ? 30.297  9.451   1.693   1.00 21.77  ? 132 ALA A O   1 
ATOM   1047 C  CB  . ALA A 1 132 ? 33.030  8.547   2.939   1.00 19.80  ? 132 ALA A CB  1 
ATOM   1048 N  N   . SER A 1 133 ? 30.325  10.210  3.798   1.00 21.32  ? 133 SER A N   1 
ATOM   1049 C  CA  . SER A 1 133 ? 28.946  9.794   4.074   1.00 23.25  ? 133 SER A CA  1 
ATOM   1050 C  C   . SER A 1 133 ? 27.894  10.414  3.137   1.00 25.28  ? 133 SER A C   1 
ATOM   1051 O  O   . SER A 1 133 ? 26.833  9.846   2.879   1.00 24.61  ? 133 SER A O   1 
ATOM   1052 C  CB  . SER A 1 133 ? 28.631  10.093  5.493   1.00 26.92  ? 133 SER A CB  1 
ATOM   1053 O  OG  . SER A 1 133 ? 28.585  11.492  5.664   1.00 22.08  ? 133 SER A OG  1 
ATOM   1054 N  N   . ASN A 1 134 ? 28.190  11.591  2.601   1.00 24.88  ? 134 ASN A N   1 
ATOM   1055 C  CA  . ASN A 1 134 ? 27.244  12.245  1.705   1.00 25.34  ? 134 ASN A CA  1 
ATOM   1056 C  C   . ASN A 1 134 ? 27.745  12.207  0.259   1.00 26.57  ? 134 ASN A C   1 
ATOM   1057 O  O   . ASN A 1 134 ? 27.332  13.009  -0.579  1.00 36.04  ? 134 ASN A O   1 
ATOM   1058 C  CB  . ASN A 1 134 ? 26.867  13.668  2.152   1.00 23.43  ? 134 ASN A CB  1 
ATOM   1059 C  CG  . ASN A 1 134 ? 28.039  14.637  2.085   1.00 27.30  ? 134 ASN A CG  1 
ATOM   1060 O  OD1 . ASN A 1 134 ? 29.190  14.228  1.966   1.00 33.80  ? 134 ASN A OD1 1 
ATOM   1061 N  ND2 . ASN A 1 134 ? 27.786  15.930  2.191   1.00 31.09  ? 134 ASN A ND2 1 
ATOM   1062 N  N   . LYS A 1 135 ? 28.589  11.237  -0.043  1.00 23.83  ? 135 LYS A N   1 
ATOM   1063 C  CA  . LYS A 1 135 ? 29.294  11.208  -1.312  1.00 27.20  ? 135 LYS A CA  1 
ATOM   1064 C  C   . LYS A 1 135 ? 29.029  9.882   -2.024  1.00 22.26  ? 135 LYS A C   1 
ATOM   1065 O  O   . LYS A 1 135 ? 28.770  8.846   -1.392  1.00 21.18  ? 135 LYS A O   1 
ATOM   1066 C  CB  . LYS A 1 135 ? 30.782  11.609  -1.157  1.00 24.09  ? 135 LYS A CB  1 
ATOM   1067 C  CG  . LYS A 1 135 ? 30.933  13.131  -1.082  1.00 32.36  ? 135 LYS A CG  1 
ATOM   1068 C  CD  . LYS A 1 135 ? 32.347  13.620  -0.947  1.00 34.18  ? 135 LYS A CD  1 
ATOM   1069 C  CE  . LYS A 1 135 ? 32.492  15.043  -0.454  1.00 35.86  ? 135 LYS A CE  1 
ATOM   1070 N  NZ  . LYS A 1 135 ? 31.974  15.188  0.926   1.00 34.10  ? 135 LYS A NZ  1 
ATOM   1071 N  N   . SER A 1 136 ? 29.099  9.914   -3.352  1.00 26.30  ? 136 SER A N   1 
ATOM   1072 C  CA  . SER A 1 136 ? 28.876  8.715   -4.142  1.00 25.87  ? 136 SER A CA  1 
ATOM   1073 C  C   . SER A 1 136 ? 29.775  7.560   -3.657  1.00 21.73  ? 136 SER A C   1 
ATOM   1074 O  O   . SER A 1 136 ? 30.988  7.718   -3.469  1.00 29.80  ? 136 SER A O   1 
ATOM   1075 C  CB  . SER A 1 136 ? 29.117  9.028   -5.612  1.00 36.49  ? 136 SER A CB  1 
ATOM   1076 O  OG  . SER A 1 136 ? 28.918  7.873   -6.404  1.00 40.95  ? 136 SER A OG  1 
ATOM   1077 N  N   . GLU A 1 137 ? 29.170  6.379   -3.515  1.00 24.85  ? 137 GLU A N   1 
ATOM   1078 C  CA  . GLU A 1 137 ? 29.853  5.152   -3.119  1.00 21.86  ? 137 GLU A CA  1 
ATOM   1079 C  C   . GLU A 1 137 ? 30.586  5.329   -1.785  1.00 19.61  ? 137 GLU A C   1 
ATOM   1080 O  O   . GLU A 1 137 ? 31.622  4.698   -1.555  1.00 21.33  ? 137 GLU A O   1 
ATOM   1081 C  CB  . GLU A 1 137 ? 30.662  4.564   -4.284  1.00 27.55  ? 137 GLU A CB  1 
ATOM   1082 C  CG  . GLU A 1 137 ? 29.741  4.318   -5.481  1.00 29.65  ? 137 GLU A CG  1 
ATOM   1083 C  CD  . GLU A 1 137 ? 30.071  3.267   -6.526  1.00 47.83  ? 137 GLU A CD  1 
ATOM   1084 O  OE1 . GLU A 1 137 ? 29.353  3.230   -7.561  1.00 51.77  ? 137 GLU A OE1 1 
ATOM   1085 O  OE2 . GLU A 1 137 ? 31.037  2.487   -6.317  1.00 65.76  ? 137 GLU A OE2 1 
ATOM   1086 N  N   . GLY A 1 138 ? 30.022  6.152   -0.882  1.00 17.43  ? 138 GLY A N   1 
ATOM   1087 C  CA  . GLY A 1 138 ? 30.819  6.578   0.257   1.00 17.04  ? 138 GLY A CA  1 
ATOM   1088 C  C   . GLY A 1 138 ? 30.982  5.483   1.307   1.00 13.58  ? 138 GLY A C   1 
ATOM   1089 O  O   . GLY A 1 138 ? 32.037  5.426   1.939   1.00 17.65  ? 138 GLY A O   1 
ATOM   1090 N  N   . LEU A 1 139 ? 29.913  4.737   1.570   1.00 14.12  ? 139 LEU A N   1 
ATOM   1091 C  CA  . LEU A 1 139 ? 29.872  3.810   2.713   1.00 11.81  ? 139 LEU A CA  1 
ATOM   1092 C  C   . LEU A 1 139 ? 29.536  2.369   2.333   1.00 11.16  ? 139 LEU A C   1 
ATOM   1093 O  O   . LEU A 1 139 ? 28.831  2.151   1.364   1.00 11.30  ? 139 LEU A O   1 
ATOM   1094 C  CB  . LEU A 1 139 ? 28.845  4.286   3.740   1.00 11.76  ? 139 LEU A CB  1 
ATOM   1095 C  CG  . LEU A 1 139 ? 29.059  5.700   4.282   1.00 10.71  ? 139 LEU A CG  1 
ATOM   1096 C  CD1 . LEU A 1 139 ? 27.864  6.164   5.111   1.00 13.89  ? 139 LEU A CD1 1 
ATOM   1097 C  CD2 . LEU A 1 139 ? 30.320  5.831   5.137   1.00 15.21  ? 139 LEU A CD2 1 
ATOM   1098 N  N   . ALA A 1 140 ? 29.993  1.446   3.181   1.00 9.75   ? 140 ALA A N   1 
ATOM   1099 C  CA  . ALA A 1 140 ? 29.560  0.060   3.098   1.00 11.39  ? 140 ALA A CA  1 
ATOM   1100 C  C   . ALA A 1 140 ? 29.355  -0.430  4.526   1.00 9.36   ? 140 ALA A C   1 
ATOM   1101 O  O   . ALA A 1 140 ? 30.194  -0.254  5.382   1.00 11.27  ? 140 ALA A O   1 
ATOM   1102 C  CB  . ALA A 1 140 ? 30.628  -0.802  2.430   1.00 11.89  ? 140 ALA A CB  1 
ATOM   1103 N  N   . VAL A 1 141 ? 28.241  -1.115  4.749   1.00 10.11  ? 141 VAL A N   1 
ATOM   1104 C  CA  . VAL A 1 141 ? 27.920  -1.656  6.081   1.00 8.96   ? 141 VAL A CA  1 
ATOM   1105 C  C   . VAL A 1 141 ? 27.783  -3.168  5.997   1.00 9.43   ? 141 VAL A C   1 
ATOM   1106 O  O   . VAL A 1 141 ? 27.156  -3.659  5.065   1.00 10.64  ? 141 VAL A O   1 
ATOM   1107 C  CB  . VAL A 1 141 ? 26.611  -1.072  6.658   1.00 9.05   ? 141 VAL A CB  1 
ATOM   1108 C  CG1 . VAL A 1 141 ? 26.291  -1.669  8.033   1.00 11.46  ? 141 VAL A CG1 1 
ATOM   1109 C  CG2 . VAL A 1 141 ? 26.793  0.426   6.763   1.00 9.65   ? 141 VAL A CG2 1 
ATOM   1110 N  N   . LEU A 1 142 ? 28.369  -3.840  6.995   1.00 8.81   ? 142 LEU A N   1 
ATOM   1111 C  CA  . LEU A 1 142 ? 28.075  -5.248  7.205   1.00 9.33   ? 142 LEU A CA  1 
ATOM   1112 C  C   . LEU A 1 142 ? 27.022  -5.352  8.315   1.00 8.11   ? 142 LEU A C   1 
ATOM   1113 O  O   . LEU A 1 142 ? 27.219  -4.775  9.416   1.00 10.44  ? 142 LEU A O   1 
ATOM   1114 C  CB  . LEU A 1 142 ? 29.370  -5.976  7.669   1.00 10.17  ? 142 LEU A CB  1 
ATOM   1115 C  CG  . LEU A 1 142 ? 30.601  -5.831  6.758   1.00 12.27  ? 142 LEU A CG  1 
ATOM   1116 C  CD1 . LEU A 1 142 ? 31.815  -6.567  7.356   1.00 12.94  ? 142 LEU A CD1 1 
ATOM   1117 C  CD2 . LEU A 1 142 ? 30.254  -6.326  5.355   1.00 11.20  ? 142 LEU A CD2 1 
ATOM   1118 N  N   . ALA A 1 143 ? 25.950  -6.107  8.026   1.00 8.80   ? 143 ALA A N   1 
ATOM   1119 C  CA  . ALA A 1 143 ? 24.857  -6.279  8.982   1.00 9.17   ? 143 ALA A CA  1 
ATOM   1120 C  C   . ALA A 1 143 ? 24.762  -7.737  9.429   1.00 8.86   ? 143 ALA A C   1 
ATOM   1121 O  O   . ALA A 1 143 ? 24.713  -8.620  8.558   1.00 10.27  ? 143 ALA A O   1 
ATOM   1122 C  CB  . ALA A 1 143 ? 23.515  -5.809  8.371   1.00 10.60  ? 143 ALA A CB  1 
ATOM   1123 N  N   . VAL A 1 144 ? 24.772  -7.942  10.783  1.00 7.82   ? 144 VAL A N   1 
ATOM   1124 C  CA  . VAL A 1 144 ? 24.575  -9.287  11.308  1.00 8.96   ? 144 VAL A CA  1 
ATOM   1125 C  C   . VAL A 1 144 ? 23.236  -9.281  12.023  1.00 9.55   ? 144 VAL A C   1 
ATOM   1126 O  O   . VAL A 1 144 ? 23.029  -8.505  12.943  1.00 9.93   ? 144 VAL A O   1 
ATOM   1127 C  CB  . VAL A 1 144 ? 25.685  -9.622  12.331  1.00 8.90   ? 144 VAL A CB  1 
ATOM   1128 C  CG1 . VAL A 1 144 ? 25.515  -11.095 12.834  1.00 12.64  ? 144 VAL A CG1 1 
ATOM   1129 C  CG2 . VAL A 1 144 ? 27.049  -9.431  11.639  1.00 10.47  ? 144 VAL A CG2 1 
ATOM   1130 N  N   . LEU A 1 145 ? 22.369  -10.242 11.660  1.00 9.72   ? 145 LEU A N   1 
ATOM   1131 C  CA  . LEU A 1 145 ? 21.142  -10.460 12.386  1.00 10.64  ? 145 LEU A CA  1 
ATOM   1132 C  C   . LEU A 1 145 ? 21.417  -11.233 13.660  1.00 9.62   ? 145 LEU A C   1 
ATOM   1133 O  O   . LEU A 1 145 ? 22.169  -12.187 13.610  1.00 10.57  ? 145 LEU A O   1 
ATOM   1134 C  CB  . LEU A 1 145 ? 20.160  -11.148 11.430  1.00 9.36   ? 145 LEU A CB  1 
ATOM   1135 C  CG  . LEU A 1 145 ? 19.816  -10.369 10.150  1.00 11.02  ? 145 LEU A CG  1 
ATOM   1136 C  CD1 . LEU A 1 145 ? 19.238  -11.317 9.117   1.00 12.75  ? 145 LEU A CD1 1 
ATOM   1137 C  CD2 . LEU A 1 145 ? 18.925  -9.152  10.409  1.00 12.88  ? 145 LEU A CD2 1 
ATOM   1138 N  N   . ILE A 1 146 ? 20.688  -10.933 14.725  1.00 10.29  ? 146 ILE A N   1 
ATOM   1139 C  CA  . ILE A 1 146 ? 20.949  -11.535 16.015  1.00 9.76   ? 146 ILE A CA  1 
ATOM   1140 C  C   . ILE A 1 146 ? 19.663  -12.111 16.570  1.00 9.27   ? 146 ILE A C   1 
ATOM   1141 O  O   . ILE A 1 146 ? 18.631  -11.438 16.573  1.00 12.23  ? 146 ILE A O   1 
ATOM   1142 C  CB  . ILE A 1 146 ? 21.470  -10.473 17.002  1.00 10.52  ? 146 ILE A CB  1 
ATOM   1143 C  CG1 . ILE A 1 146 ? 22.795  -9.893  16.509  1.00 12.42  ? 146 ILE A CG1 1 
ATOM   1144 C  CG2 . ILE A 1 146 ? 21.628  -11.076 18.417  1.00 12.52  ? 146 ILE A CG2 1 
ATOM   1145 C  CD1 . ILE A 1 146 ? 23.159  -8.586  17.221  1.00 12.34  ? 146 ILE A CD1 1 
ATOM   1146 N  N   . GLU A 1 147 ? 19.737  -13.397 16.990  1.00 11.20  ? 147 GLU A N   1 
ATOM   1147 C  CA  . GLU A 1 147 ? 18.576  -13.988 17.624  1.00 13.27  ? 147 GLU A CA  1 
ATOM   1148 C  C   . GLU A 1 147 ? 18.953  -14.556 18.994  1.00 12.14  ? 147 GLU A C   1 
ATOM   1149 O  O   . GLU A 1 147 ? 20.129  -14.720 19.327  1.00 12.68  ? 147 GLU A O   1 
ATOM   1150 C  CB  . GLU A 1 147 ? 18.000  -15.109 16.764  1.00 14.21  ? 147 GLU A CB  1 
ATOM   1151 C  CG  . GLU A 1 147 ? 18.972  -16.270 16.508  1.00 14.19  ? 147 GLU A CG  1 
ATOM   1152 C  CD  . GLU A 1 147 ? 18.490  -17.357 15.526  1.00 16.86  ? 147 GLU A CD  1 
ATOM   1153 O  OE1 . GLU A 1 147 ? 17.518  -17.082 14.749  1.00 19.53  ? 147 GLU A OE1 1 
ATOM   1154 O  OE2 . GLU A 1 147 ? 19.059  -18.500 15.492  1.00 24.35  ? 147 GLU A OE2 1 
ATOM   1155 N  N   . MET A 1 148 ? 17.957  -14.801 19.832  1.00 14.64  ? 148 MET A N   1 
ATOM   1156 C  CA  . MET A 1 148 ? 18.177  -15.323 21.164  1.00 16.25  ? 148 MET A CA  1 
ATOM   1157 C  C   . MET A 1 148 ? 18.540  -16.813 21.044  1.00 18.44  ? 148 MET A C   1 
ATOM   1158 O  O   . MET A 1 148 ? 17.902  -17.559 20.312  1.00 22.27  ? 148 MET A O   1 
ATOM   1159 C  CB  . MET A 1 148 ? 16.934  -15.075 22.042  1.00 18.42  ? 148 MET A CB  1 
ATOM   1160 C  CG  . MET A 1 148 ? 17.218  -15.286 23.535  1.00 22.49  ? 148 MET A CG  1 
ATOM   1161 S  SD  . MET A 1 148 ? 17.027  -17.012 23.956  1.00 27.23  ? 148 MET A SD  1 
ATOM   1162 N  N   . GLY A 1 149 ? 19.603  -17.233 21.749  1.00 18.05  ? 149 GLY A N   1 
ATOM   1163 C  CA  . GLY A 1 149 ? 19.957  -18.644 21.750  1.00 18.49  ? 149 GLY A CA  1 
ATOM   1164 C  C   . GLY A 1 149 ? 21.098  -18.894 22.742  1.00 18.12  ? 149 GLY A C   1 
ATOM   1165 O  O   . GLY A 1 149 ? 20.985  -18.563 23.927  1.00 18.49  ? 149 GLY A O   1 
ATOM   1166 N  N   . SER A 1 150 ? 22.162  -19.573 22.319  1.00 21.23  ? 150 SER A N   1 
ATOM   1167 C  CA  . SER A 1 150 ? 23.266  -19.789 23.239  1.00 21.43  ? 150 SER A CA  1 
ATOM   1168 C  C   . SER A 1 150 ? 24.032  -18.512 23.598  1.00 20.89  ? 150 SER A C   1 
ATOM   1169 O  O   . SER A 1 150 ? 24.155  -17.579 22.828  1.00 20.93  ? 150 SER A O   1 
ATOM   1170 C  CB  . SER A 1 150 ? 24.173  -20.873 22.719  1.00 28.87  ? 150 SER A CB  1 
ATOM   1171 O  OG  . SER A 1 150 ? 24.739  -20.414 21.518  1.00 37.60  ? 150 SER A OG  1 
ATOM   1172 N  N   . PHE A 1 151 ? 24.642  -18.512 24.775  1.00 17.78  ? 151 PHE A N   1 
ATOM   1173 C  CA  . PHE A 1 151 ? 25.541  -17.441 25.171  1.00 19.03  ? 151 PHE A CA  1 
ATOM   1174 C  C   . PHE A 1 151 ? 26.682  -17.284 24.157  1.00 18.23  ? 151 PHE A C   1 
ATOM   1175 O  O   . PHE A 1 151 ? 27.239  -18.272 23.625  1.00 20.79  ? 151 PHE A O   1 
ATOM   1176 C  CB  . PHE A 1 151 ? 26.110  -17.747 26.560  1.00 18.84  ? 151 PHE A CB  1 
ATOM   1177 C  CG  . PHE A 1 151 ? 27.106  -16.714 27.047  1.00 21.91  ? 151 PHE A CG  1 
ATOM   1178 C  CD1 . PHE A 1 151 ? 26.653  -15.505 27.544  1.00 19.15  ? 151 PHE A CD1 1 
ATOM   1179 C  CD2 . PHE A 1 151 ? 28.478  -16.966 27.094  1.00 20.23  ? 151 PHE A CD2 1 
ATOM   1180 C  CE1 . PHE A 1 151 ? 27.521  -14.528 27.997  1.00 20.76  ? 151 PHE A CE1 1 
ATOM   1181 C  CE2 . PHE A 1 151 ? 29.356  -15.987 27.558  1.00 21.54  ? 151 PHE A CE2 1 
ATOM   1182 C  CZ  . PHE A 1 151 ? 28.875  -14.777 28.021  1.00 21.59  ? 151 PHE A CZ  1 
ATOM   1183 N  N   . ASN A 1 152 ? 27.054  -16.044 23.908  1.00 17.61  ? 152 ASN A N   1 
ATOM   1184 C  CA  . ASN A 1 152 ? 28.063  -15.660 22.932  1.00 18.35  ? 152 ASN A CA  1 
ATOM   1185 C  C   . ASN A 1 152 ? 29.204  -14.882 23.589  1.00 18.05  ? 152 ASN A C   1 
ATOM   1186 O  O   . ASN A 1 152 ? 29.072  -13.687 23.848  1.00 19.35  ? 152 ASN A O   1 
ATOM   1187 C  CB  . ASN A 1 152 ? 27.388  -14.826 21.845  1.00 16.67  ? 152 ASN A CB  1 
ATOM   1188 C  CG  . ASN A 1 152 ? 28.260  -14.715 20.606  1.00 15.79  ? 152 ASN A CG  1 
ATOM   1189 O  OD1 . ASN A 1 152 ? 29.455  -14.387 20.702  1.00 15.79  ? 152 ASN A OD1 1 
ATOM   1190 N  ND2 . ASN A 1 152 ? 27.671  -14.951 19.437  1.00 15.30  ? 152 ASN A ND2 1 
ATOM   1191 N  N   . PRO A 1 153 ? 30.328  -15.553 23.918  1.00 17.03  ? 153 PRO A N   1 
ATOM   1192 C  CA  . PRO A 1 153 ? 31.453  -14.904 24.603  1.00 18.11  ? 153 PRO A CA  1 
ATOM   1193 C  C   . PRO A 1 153 ? 32.010  -13.720 23.811  1.00 18.48  ? 153 PRO A C   1 
ATOM   1194 O  O   . PRO A 1 153 ? 32.447  -12.714 24.392  1.00 21.76  ? 153 PRO A O   1 
ATOM   1195 C  CB  . PRO A 1 153 ? 32.531  -16.008 24.654  1.00 22.59  ? 153 PRO A CB  1 
ATOM   1196 C  CG  . PRO A 1 153 ? 31.766  -17.318 24.499  1.00 25.89  ? 153 PRO A CG  1 
ATOM   1197 C  CD  . PRO A 1 153 ? 30.530  -17.007 23.687  1.00 21.68  ? 153 PRO A CD  1 
ATOM   1198 N  N   . SER A 1 154 ? 31.953  -13.822 22.471  1.00 18.41  ? 154 SER A N   1 
ATOM   1199 C  CA  . SER A 1 154 ? 32.565  -12.759 21.682  1.00 17.75  ? 154 SER A CA  1 
ATOM   1200 C  C   . SER A 1 154 ? 31.738  -11.467 21.816  1.00 15.40  ? 154 SER A C   1 
ATOM   1201 O  O   . SER A 1 154 ? 32.280  -10.362 21.919  1.00 16.63  ? 154 SER A O   1 
ATOM   1202 C  CB  . SER A 1 154 ? 32.771  -13.179 20.226  1.00 17.14  ? 154 SER A CB  1 
ATOM   1203 O  OG  . SER A 1 154 ? 33.565  -14.377 20.123  1.00 22.00  ? 154 SER A OG  1 
ATOM   1204 N  N   . TYR A 1 155 ? 30.412  -11.602 21.692  1.00 15.17  ? 155 TYR A N   1 
ATOM   1205 C  CA  . TYR A 1 155 ? 29.590  -10.423 21.877  1.00 14.04  ? 155 TYR A CA  1 
ATOM   1206 C  C   . TYR A 1 155 ? 29.772  -9.854  23.298  1.00 18.01  ? 155 TYR A C   1 
ATOM   1207 O  O   . TYR A 1 155 ? 29.545  -8.661  23.521  1.00 18.40  ? 155 TYR A O   1 
ATOM   1208 C  CB  . TYR A 1 155 ? 28.102  -10.640 21.522  1.00 14.73  ? 155 TYR A CB  1 
ATOM   1209 C  CG  . TYR A 1 155 ? 27.828  -10.452 20.048  1.00 13.22  ? 155 TYR A CG  1 
ATOM   1210 C  CD1 . TYR A 1 155 ? 28.217  -11.454 19.149  1.00 12.44  ? 155 TYR A CD1 1 
ATOM   1211 C  CD2 . TYR A 1 155 ? 27.244  -9.300  19.532  1.00 12.80  ? 155 TYR A CD2 1 
ATOM   1212 C  CE1 . TYR A 1 155 ? 28.030  -11.362 17.786  1.00 12.45  ? 155 TYR A CE1 1 
ATOM   1213 C  CE2 . TYR A 1 155 ? 27.053  -9.195  18.149  1.00 11.60  ? 155 TYR A CE2 1 
ATOM   1214 C  CZ  . TYR A 1 155 ? 27.452  -10.191 17.285  1.00 11.81  ? 155 TYR A CZ  1 
ATOM   1215 O  OH  . TYR A 1 155 ? 27.262  -10.027 15.937  1.00 12.71  ? 155 TYR A OH  1 
ATOM   1216 N  N   . ASP A 1 156 ? 30.080  -10.712 24.284  1.00 18.46  ? 156 ASP A N   1 
ATOM   1217 C  CA  . ASP A 1 156 ? 30.223  -10.211 25.638  1.00 16.95  ? 156 ASP A CA  1 
ATOM   1218 C  C   . ASP A 1 156 ? 31.451  -9.307  25.751  1.00 15.28  ? 156 ASP A C   1 
ATOM   1219 O  O   . ASP A 1 156 ? 31.562  -8.553  26.733  1.00 20.02  ? 156 ASP A O   1 
ATOM   1220 C  CB  . ASP A 1 156 ? 30.172  -11.339 26.668  1.00 21.18  ? 156 ASP A CB  1 
ATOM   1221 C  CG  . ASP A 1 156 ? 29.139  -11.039 27.764  1.00 18.69  ? 156 ASP A CG  1 
ATOM   1222 O  OD1 . ASP A 1 156 ? 27.996  -10.604 27.402  1.00 19.81  ? 156 ASP A OD1 1 
ATOM   1223 O  OD2 . ASP A 1 156 ? 29.492  -11.130 28.931  1.00 24.64  ? 156 ASP A OD2 1 
ATOM   1224 N  N   . LYS A 1 157 ? 32.339  -9.365  24.755  1.00 18.14  ? 157 LYS A N   1 
ATOM   1225 C  CA  . LYS A 1 157 ? 33.536  -8.543  24.804  1.00 19.58  ? 157 LYS A CA  1 
ATOM   1226 C  C   . LYS A 1 157 ? 33.118  -7.079  24.637  1.00 19.78  ? 157 LYS A C   1 
ATOM   1227 O  O   . LYS A 1 157 ? 33.832  -6.176  25.047  1.00 21.42  ? 157 LYS A O   1 
ATOM   1228 C  CB  . LYS A 1 157 ? 34.601  -8.995  23.794  1.00 20.40  ? 157 LYS A CB  1 
ATOM   1229 C  CG  . LYS A 1 157 ? 35.140  -10.401 24.053  1.00 19.33  ? 157 LYS A CG  1 
ATOM   1230 C  CD  . LYS A 1 157 ? 36.120  -10.956 23.027  1.00 21.59  ? 157 LYS A CD  1 
ATOM   1231 C  CE  . LYS A 1 157 ? 36.495  -12.402 23.306  1.00 23.72  ? 157 LYS A CE  1 
ATOM   1232 N  NZ  . LYS A 1 157 ? 37.420  -12.985 22.300  1.00 21.13  ? 157 LYS A NZ  1 
ATOM   1233 N  N   . ILE A 1 158 ? 31.949  -6.847  24.014  1.00 16.52  ? 158 ILE A N   1 
ATOM   1234 C  CA  . ILE A 1 158 ? 31.348  -5.525  23.964  1.00 16.77  ? 158 ILE A CA  1 
ATOM   1235 C  C   . ILE A 1 158 ? 30.382  -5.348  25.137  1.00 17.79  ? 158 ILE A C   1 
ATOM   1236 O  O   . ILE A 1 158 ? 30.467  -4.359  25.871  1.00 18.63  ? 158 ILE A O   1 
ATOM   1237 C  CB  . ILE A 1 158 ? 30.599  -5.277  22.650  1.00 19.07  ? 158 ILE A CB  1 
ATOM   1238 C  CG1 . ILE A 1 158 ? 31.555  -5.340  21.459  1.00 22.52  ? 158 ILE A CG1 1 
ATOM   1239 C  CG2 . ILE A 1 158 ? 29.861  -3.948  22.755  1.00 17.07  ? 158 ILE A CG2 1 
ATOM   1240 C  CD1 . ILE A 1 158 ? 30.857  -5.530  20.140  1.00 24.18  ? 158 ILE A CD1 1 
ATOM   1241 N  N   . PHE A 1 159 ? 29.471  -6.311  25.337  1.00 19.67  ? 159 PHE A N   1 
ATOM   1242 C  CA  . PHE A 1 159 ? 28.373  -6.106  26.285  1.00 17.27  ? 159 PHE A CA  1 
ATOM   1243 C  C   . PHE A 1 159 ? 28.841  -5.936  27.736  1.00 20.03  ? 159 PHE A C   1 
ATOM   1244 O  O   . PHE A 1 159 ? 28.158  -5.261  28.521  1.00 22.03  ? 159 PHE A O   1 
ATOM   1245 C  CB  . PHE A 1 159 ? 27.340  -7.225  26.221  1.00 15.10  ? 159 PHE A CB  1 
ATOM   1246 C  CG  . PHE A 1 159 ? 26.648  -7.392  24.890  1.00 14.75  ? 159 PHE A CG  1 
ATOM   1247 C  CD1 . PHE A 1 159 ? 26.518  -6.362  23.960  1.00 20.79  ? 159 PHE A CD1 1 
ATOM   1248 C  CD2 . PHE A 1 159 ? 26.023  -8.612  24.629  1.00 15.70  ? 159 PHE A CD2 1 
ATOM   1249 C  CE1 . PHE A 1 159 ? 25.848  -6.606  22.762  1.00 19.52  ? 159 PHE A CE1 1 
ATOM   1250 C  CE2 . PHE A 1 159 ? 25.337  -8.832  23.446  1.00 18.27  ? 159 PHE A CE2 1 
ATOM   1251 C  CZ  . PHE A 1 159 ? 25.261  -7.833  22.512  1.00 17.32  ? 159 PHE A CZ  1 
ATOM   1252 N  N   . SER A 1 160 ? 29.975  -6.560  28.084  1.00 18.39  ? 160 SER A N   1 
ATOM   1253 C  CA  . SER A 1 160 ? 30.505  -6.480  29.449  1.00 21.37  ? 160 SER A CA  1 
ATOM   1254 C  C   . SER A 1 160 ? 30.905  -5.050  29.796  1.00 17.07  ? 160 SER A C   1 
ATOM   1255 O  O   . SER A 1 160 ? 31.169  -4.753  30.971  1.00 22.56  ? 160 SER A O   1 
ATOM   1256 C  CB  . SER A 1 160 ? 31.646  -7.434  29.667  1.00 20.97  ? 160 SER A CB  1 
ATOM   1257 O  OG  . SER A 1 160 ? 32.741  -7.085  28.823  1.00 22.62  ? 160 SER A OG  1 
ATOM   1258 N  N   . HIS A 1 161 ? 30.916  -4.165  28.785  1.00 20.26  ? 161 HIS A N   1 
ATOM   1259 C  CA  . HIS A 1 161 ? 31.280  -2.765  29.012  1.00 18.05  ? 161 HIS A CA  1 
ATOM   1260 C  C   . HIS A 1 161 ? 30.074  -1.817  29.021  1.00 23.53  ? 161 HIS A C   1 
ATOM   1261 O  O   . HIS A 1 161 ? 30.247  -0.632  29.303  1.00 22.73  ? 161 HIS A O   1 
ATOM   1262 C  CB  . HIS A 1 161 ? 32.343  -2.277  28.018  1.00 21.34  ? 161 HIS A CB  1 
ATOM   1263 C  CG  . HIS A 1 161 ? 33.645  -2.991  28.139  1.00 20.84  ? 161 HIS A CG  1 
ATOM   1264 N  ND1 . HIS A 1 161 ? 34.629  -2.549  29.001  1.00 24.67  ? 161 HIS A ND1 1 
ATOM   1265 C  CD2 . HIS A 1 161 ? 34.131  -4.094  27.508  1.00 21.44  ? 161 HIS A CD2 1 
ATOM   1266 C  CE1 . HIS A 1 161 ? 35.679  -3.355  28.919  1.00 27.76  ? 161 HIS A CE1 1 
ATOM   1267 N  NE2 . HIS A 1 161 ? 35.406  -4.324  27.995  1.00 23.63  ? 161 HIS A NE2 1 
ATOM   1268 N  N   . LEU A 1 162 ? 28.868  -2.342  28.739  1.00 23.09  ? 162 LEU A N   1 
ATOM   1269 C  CA  . LEU A 1 162 ? 27.691  -1.491  28.610  1.00 25.55  ? 162 LEU A CA  1 
ATOM   1270 C  C   . LEU A 1 162 ? 27.496  -0.618  29.852  1.00 23.08  ? 162 LEU A C   1 
ATOM   1271 O  O   . LEU A 1 162 ? 27.070  0.519   29.736  1.00 26.02  ? 162 LEU A O   1 
ATOM   1272 C  CB  . LEU A 1 162 ? 26.434  -2.314  28.310  1.00 25.15  ? 162 LEU A CB  1 
ATOM   1273 C  CG  . LEU A 1 162 ? 26.508  -2.999  26.959  1.00 25.55  ? 162 LEU A CG  1 
ATOM   1274 C  CD1 . LEU A 1 162 ? 25.309  -3.900  26.723  1.00 28.62  ? 162 LEU A CD1 1 
ATOM   1275 C  CD2 . LEU A 1 162 ? 26.657  -1.966  25.859  1.00 31.51  ? 162 LEU A CD2 1 
ATOM   1276 N  N   . GLN A 1 163 ? 27.793  -1.151  31.037  1.00 26.93  ? 163 GLN A N   1 
ATOM   1277 C  CA  . GLN A 1 163 ? 27.391  -0.433  32.236  1.00 28.91  ? 163 GLN A CA  1 
ATOM   1278 C  C   . GLN A 1 163 ? 28.240  0.827   32.443  1.00 29.77  ? 163 GLN A C   1 
ATOM   1279 O  O   . GLN A 1 163 ? 27.835  1.716   33.181  1.00 30.95  ? 163 GLN A O   1 
ATOM   1280 C  CB  . GLN A 1 163 ? 27.326  -1.318  33.478  1.00 36.25  ? 163 GLN A CB  1 
ATOM   1281 C  CG  . GLN A 1 163 ? 28.630  -1.386  34.255  1.00 48.17  ? 163 GLN A CG  1 
ATOM   1282 C  CD  . GLN A 1 163 ? 29.506  -2.560  33.884  1.00 43.44  ? 163 GLN A CD  1 
ATOM   1283 O  OE1 . GLN A 1 163 ? 30.035  -3.263  34.748  1.00 58.76  ? 163 GLN A OE1 1 
ATOM   1284 N  NE2 . GLN A 1 163 ? 29.687  -2.756  32.585  1.00 54.25  ? 163 GLN A NE2 1 
ATOM   1285 N  N   . HIS A 1 164 ? 29.389  0.922   31.752  1.00 26.81  ? 164 HIS A N   1 
ATOM   1286 C  CA  . HIS A 1 164 ? 30.244  2.098   31.844  1.00 24.13  ? 164 HIS A CA  1 
ATOM   1287 C  C   . HIS A 1 164 ? 29.806  3.203   30.896  1.00 24.45  ? 164 HIS A C   1 
ATOM   1288 O  O   . HIS A 1 164 ? 30.379  4.291   30.951  1.00 28.01  ? 164 HIS A O   1 
ATOM   1289 C  CB  . HIS A 1 164 ? 31.709  1.768   31.547  1.00 21.73  ? 164 HIS A CB  1 
ATOM   1290 C  CG  . HIS A 1 164 ? 32.299  0.806   32.505  1.00 23.54  ? 164 HIS A CG  1 
ATOM   1291 N  ND1 . HIS A 1 164 ? 32.153  0.941   33.873  1.00 26.46  ? 164 HIS A ND1 1 
ATOM   1292 C  CD2 . HIS A 1 164 ? 33.021  -0.306  32.288  1.00 26.14  ? 164 HIS A CD2 1 
ATOM   1293 C  CE1 . HIS A 1 164 ? 32.730  -0.070  34.473  1.00 25.08  ? 164 HIS A CE1 1 
ATOM   1294 N  NE2 . HIS A 1 164 ? 33.257  -0.856  33.518  1.00 31.92  ? 164 HIS A NE2 1 
ATOM   1295 N  N   . VAL A 1 165 ? 28.894  2.868   29.967  1.00 22.78  ? 165 VAL A N   1 
ATOM   1296 C  CA  . VAL A 1 165 ? 28.428  3.840   28.989  1.00 23.97  ? 165 VAL A CA  1 
ATOM   1297 C  C   . VAL A 1 165 ? 26.916  3.993   29.104  1.00 21.81  ? 165 VAL A C   1 
ATOM   1298 O  O   . VAL A 1 165 ? 26.269  4.318   28.123  1.00 25.06  ? 165 VAL A O   1 
ATOM   1299 C  CB  . VAL A 1 165 ? 28.949  3.575   27.555  1.00 22.94  ? 165 VAL A CB  1 
ATOM   1300 C  CG1 . VAL A 1 165 ? 30.484  3.609   27.568  1.00 25.90  ? 165 VAL A CG1 1 
ATOM   1301 C  CG2 . VAL A 1 165 ? 28.476  2.226   27.006  1.00 26.18  ? 165 VAL A CG2 1 
ATOM   1302 N  N   . LYS A 1 166 ? 26.366  3.816   30.320  1.00 22.30  ? 166 LYS A N   1 
ATOM   1303 C  CA  . LYS A 1 166 ? 24.920  3.828   30.540  1.00 20.43  ? 166 LYS A CA  1 
ATOM   1304 C  C   . LYS A 1 166 ? 24.249  5.123   30.060  1.00 20.51  ? 166 LYS A C   1 
ATOM   1305 O  O   . LYS A 1 166 ? 23.130  5.086   29.547  1.00 21.78  ? 166 LYS A O   1 
ATOM   1306 C  CB  . LYS A 1 166 ? 24.643  3.537   32.019  1.00 27.62  ? 166 LYS A CB  1 
ATOM   1307 C  CG  . LYS A 1 166 ? 23.197  3.501   32.500  1.00 26.85  ? 166 LYS A CG  1 
ATOM   1308 C  CD  . LYS A 1 166 ? 23.039  3.039   33.939  1.00 30.78  ? 166 LYS A CD  1 
ATOM   1309 C  CE  . LYS A 1 166 ? 23.103  1.529   34.100  1.00 36.52  ? 166 LYS A CE  1 
ATOM   1310 N  NZ  . LYS A 1 166 ? 22.131  0.775   33.250  1.00 43.46  ? 166 LYS A NZ  1 
ATOM   1311 N  N   . TYR A 1 167 ? 24.925  6.269   30.265  1.00 19.75  ? 167 TYR A N   1 
ATOM   1312 C  CA  . TYR A 1 167 ? 24.314  7.565   29.973  1.00 20.51  ? 167 TYR A CA  1 
ATOM   1313 C  C   . TYR A 1 167 ? 24.982  8.262   28.795  1.00 19.49  ? 167 TYR A C   1 
ATOM   1314 O  O   . TYR A 1 167 ? 26.135  8.017   28.472  1.00 22.05  ? 167 TYR A O   1 
ATOM   1315 C  CB  . TYR A 1 167 ? 24.337  8.464   31.213  1.00 18.79  ? 167 TYR A CB  1 
ATOM   1316 C  CG  . TYR A 1 167 ? 23.560  7.890   32.378  1.00 17.22  ? 167 TYR A CG  1 
ATOM   1317 C  CD1 . TYR A 1 167 ? 22.173  7.897   32.355  1.00 19.21  ? 167 TYR A CD1 1 
ATOM   1318 C  CD2 . TYR A 1 167 ? 24.199  7.233   33.442  1.00 18.64  ? 167 TYR A CD2 1 
ATOM   1319 C  CE1 . TYR A 1 167 ? 21.435  7.344   33.386  1.00 21.49  ? 167 TYR A CE1 1 
ATOM   1320 C  CE2 . TYR A 1 167 ? 23.466  6.711   34.488  1.00 22.39  ? 167 TYR A CE2 1 
ATOM   1321 C  CZ  . TYR A 1 167 ? 22.083  6.760   34.457  1.00 26.48  ? 167 TYR A CZ  1 
ATOM   1322 O  OH  . TYR A 1 167 ? 21.386  6.206   35.486  1.00 28.66  ? 167 TYR A OH  1 
ATOM   1323 N  N   . LYS A 1 168 ? 24.210  9.135   28.132  1.00 24.48  ? 168 LYS A N   1 
ATOM   1324 C  CA  . LYS A 1 168 ? 24.721  10.015  27.080  1.00 28.30  ? 168 LYS A CA  1 
ATOM   1325 C  C   . LYS A 1 168 ? 26.002  10.724  27.543  1.00 31.80  ? 168 LYS A C   1 
ATOM   1326 O  O   . LYS A 1 168 ? 26.033  11.336  28.607  1.00 36.18  ? 168 LYS A O   1 
ATOM   1327 C  CB  . LYS A 1 168 ? 23.665  11.048  26.651  1.00 31.96  ? 168 LYS A CB  1 
ATOM   1328 C  CG  . LYS A 1 168 ? 24.041  11.942  25.474  1.00 38.73  ? 168 LYS A CG  1 
ATOM   1329 C  CD  . LYS A 1 168 ? 22.806  12.620  24.851  1.00 36.69  ? 168 LYS A CD  1 
ATOM   1330 C  CE  . LYS A 1 168 ? 23.085  13.443  23.613  1.00 44.09  ? 168 LYS A CE  1 
ATOM   1331 N  NZ  . LYS A 1 168 ? 23.708  14.735  23.978  1.00 40.25  ? 168 LYS A NZ  1 
ATOM   1332 N  N   . GLY A 1 169 ? 27.053  10.669  26.713  1.00 30.25  ? 169 GLY A N   1 
ATOM   1333 C  CA  . GLY A 1 169 ? 28.309  11.359  26.993  1.00 36.66  ? 169 GLY A CA  1 
ATOM   1334 C  C   . GLY A 1 169 ? 29.358  10.461  27.649  1.00 34.61  ? 169 GLY A C   1 
ATOM   1335 O  O   . GLY A 1 169 ? 30.554  10.772  27.658  1.00 42.27  ? 169 GLY A O   1 
ATOM   1336 N  N   . GLN A 1 170 ? 28.900  9.346   28.219  1.00 22.88  ? 170 GLN A N   1 
ATOM   1337 C  CA  . GLN A 1 170 ? 29.813  8.412   28.862  1.00 21.00  ? 170 GLN A CA  1 
ATOM   1338 C  C   . GLN A 1 170 ? 30.619  7.685   27.789  1.00 25.65  ? 170 GLN A C   1 
ATOM   1339 O  O   . GLN A 1 170 ? 30.142  7.463   26.667  1.00 28.86  ? 170 GLN A O   1 
ATOM   1340 C  CB  . GLN A 1 170 ? 29.064  7.487   29.825  1.00 20.86  ? 170 GLN A CB  1 
ATOM   1341 C  CG  . GLN A 1 170 ? 28.468  8.259   31.002  1.00 19.82  ? 170 GLN A CG  1 
ATOM   1342 C  CD  . GLN A 1 170 ? 27.945  7.389   32.104  1.00 20.49  ? 170 GLN A CD  1 
ATOM   1343 O  OE1 . GLN A 1 170 ? 27.366  6.341   31.850  1.00 22.91  ? 170 GLN A OE1 1 
ATOM   1344 N  NE2 . GLN A 1 170 ? 28.269  7.748   33.335  1.00 24.39  ? 170 GLN A NE2 1 
ATOM   1345 N  N   . GLU A 1 171 ? 31.832  7.274   28.181  1.00 27.73  ? 171 GLU A N   1 
ATOM   1346 C  CA  . GLU A 1 171 ? 32.732  6.537   27.312  1.00 26.78  ? 171 GLU A CA  1 
ATOM   1347 C  C   . GLU A 1 171 ? 33.550  5.568   28.150  1.00 24.48  ? 171 GLU A C   1 
ATOM   1348 O  O   . GLU A 1 171 ? 33.716  5.780   29.349  1.00 33.19  ? 171 GLU A O   1 
ATOM   1349 C  CB  . GLU A 1 171 ? 33.737  7.459   26.628  1.00 29.99  ? 171 GLU A CB  1 
ATOM   1350 C  CG  . GLU A 1 171 ? 33.229  8.865   26.384  1.00 41.65  ? 171 GLU A CG  1 
ATOM   1351 C  CD  . GLU A 1 171 ? 34.189  9.766   25.621  1.00 35.57  ? 171 GLU A CD  1 
ATOM   1352 O  OE1 . GLU A 1 171 ? 35.433  9.665   25.845  1.00 38.18  ? 171 GLU A OE1 1 
ATOM   1353 O  OE2 . GLU A 1 171 ? 33.684  10.577  24.795  1.00 47.11  ? 171 GLU A OE2 1 
ATOM   1354 N  N   . ALA A 1 172 ? 33.988  4.494   27.494  1.00 22.82  ? 172 ALA A N   1 
ATOM   1355 C  CA  . ALA A 1 172 ? 34.831  3.479   28.101  1.00 24.92  ? 172 ALA A CA  1 
ATOM   1356 C  C   . ALA A 1 172 ? 35.830  2.982   27.057  1.00 22.29  ? 172 ALA A C   1 
ATOM   1357 O  O   . ALA A 1 172 ? 35.613  3.091   25.871  1.00 25.62  ? 172 ALA A O   1 
ATOM   1358 C  CB  . ALA A 1 172 ? 33.972  2.352   28.612  1.00 24.90  ? 172 ALA A CB  1 
ATOM   1359 N  N   . PHE A 1 173 ? 36.960  2.444   27.513  1.00 26.60  ? 173 PHE A N   1 
ATOM   1360 C  CA  . PHE A 1 173 ? 37.961  1.897   26.622  1.00 24.47  ? 173 PHE A CA  1 
ATOM   1361 C  C   . PHE A 1 173 ? 37.790  0.386   26.598  1.00 28.42  ? 173 PHE A C   1 
ATOM   1362 O  O   . PHE A 1 173 ? 37.640  -0.234  27.639  1.00 30.78  ? 173 PHE A O   1 
ATOM   1363 C  CB  . PHE A 1 173 ? 39.358  2.385   27.020  1.00 26.82  ? 173 PHE A CB  1 
ATOM   1364 C  CG  . PHE A 1 173 ? 39.712  3.770   26.525  1.00 25.71  ? 173 PHE A CG  1 
ATOM   1365 C  CD1 . PHE A 1 173 ? 39.880  4.008   25.163  1.00 30.20  ? 173 PHE A CD1 1 
ATOM   1366 C  CD2 . PHE A 1 173 ? 39.934  4.822   27.413  1.00 32.47  ? 173 PHE A CD2 1 
ATOM   1367 C  CE1 . PHE A 1 173 ? 40.243  5.267   24.699  1.00 31.61  ? 173 PHE A CE1 1 
ATOM   1368 C  CE2 . PHE A 1 173 ? 40.260  6.091   26.944  1.00 31.88  ? 173 PHE A CE2 1 
ATOM   1369 C  CZ  . PHE A 1 173 ? 40.423  6.307   25.588  1.00 35.86  ? 173 PHE A CZ  1 
ATOM   1370 N  N   . VAL A 1 174 ? 37.831  -0.191  25.392  1.00 26.03  ? 174 VAL A N   1 
ATOM   1371 C  CA  . VAL A 1 174 ? 37.628  -1.613  25.190  1.00 22.48  ? 174 VAL A CA  1 
ATOM   1372 C  C   . VAL A 1 174 ? 38.921  -2.174  24.592  1.00 19.10  ? 174 VAL A C   1 
ATOM   1373 O  O   . VAL A 1 174 ? 39.361  -1.708  23.555  1.00 23.03  ? 174 VAL A O   1 
ATOM   1374 C  CB  . VAL A 1 174 ? 36.417  -1.892  24.283  1.00 21.36  ? 174 VAL A CB  1 
ATOM   1375 C  CG1 . VAL A 1 174 ? 36.288  -3.389  24.029  1.00 23.55  ? 174 VAL A CG1 1 
ATOM   1376 C  CG2 . VAL A 1 174 ? 35.128  -1.339  24.882  1.00 22.67  ? 174 VAL A CG2 1 
ATOM   1377 N  N   . PRO A 1 175 ? 39.578  -3.193  25.196  1.00 22.69  ? 175 PRO A N   1 
ATOM   1378 C  CA  . PRO A 1 175 ? 40.813  -3.761  24.629  1.00 25.09  ? 175 PRO A CA  1 
ATOM   1379 C  C   . PRO A 1 175 ? 40.504  -4.445  23.303  1.00 22.51  ? 175 PRO A C   1 
ATOM   1380 O  O   . PRO A 1 175 ? 39.411  -4.966  23.155  1.00 21.37  ? 175 PRO A O   1 
ATOM   1381 C  CB  . PRO A 1 175 ? 41.204  -4.850  25.633  1.00 27.55  ? 175 PRO A CB  1 
ATOM   1382 C  CG  . PRO A 1 175 ? 40.549  -4.379  26.915  1.00 24.75  ? 175 PRO A CG  1 
ATOM   1383 C  CD  . PRO A 1 175 ? 39.214  -3.804  26.484  1.00 22.78  ? 175 PRO A CD  1 
ATOM   1384 N  N   . GLY A 1 176 ? 41.438  -4.402  22.347  1.00 19.70  ? 176 GLY A N   1 
ATOM   1385 C  CA  . GLY A 1 176 ? 41.177  -4.997  21.056  1.00 20.71  ? 176 GLY A CA  1 
ATOM   1386 C  C   . GLY A 1 176 ? 40.841  -6.475  21.191  1.00 19.37  ? 176 GLY A C   1 
ATOM   1387 O  O   . GLY A 1 176 ? 41.417  -7.180  22.011  1.00 22.15  ? 176 GLY A O   1 
ATOM   1388 N  N   . PHE A 1 177 ? 39.965  -6.932  20.283  1.00 19.08  ? 177 PHE A N   1 
ATOM   1389 C  CA  . PHE A 1 177 ? 39.695  -8.340  20.082  1.00 17.97  ? 177 PHE A CA  1 
ATOM   1390 C  C   . PHE A 1 177 ? 39.391  -8.548  18.599  1.00 17.23  ? 177 PHE A C   1 
ATOM   1391 O  O   . PHE A 1 177 ? 39.342  -7.603  17.816  1.00 18.98  ? 177 PHE A O   1 
ATOM   1392 C  CB  . PHE A 1 177 ? 38.569  -8.772  21.023  1.00 17.95  ? 177 PHE A CB  1 
ATOM   1393 C  CG  . PHE A 1 177 ? 37.209  -8.218  20.687  1.00 17.08  ? 177 PHE A CG  1 
ATOM   1394 C  CD1 . PHE A 1 177 ? 36.853  -6.943  21.119  1.00 18.31  ? 177 PHE A CD1 1 
ATOM   1395 C  CD2 . PHE A 1 177 ? 36.292  -8.948  19.929  1.00 17.52  ? 177 PHE A CD2 1 
ATOM   1396 C  CE1 . PHE A 1 177 ? 35.593  -6.418  20.856  1.00 20.41  ? 177 PHE A CE1 1 
ATOM   1397 C  CE2 . PHE A 1 177 ? 35.056  -8.398  19.632  1.00 16.31  ? 177 PHE A CE2 1 
ATOM   1398 C  CZ  . PHE A 1 177 ? 34.695  -7.158  20.121  1.00 17.76  ? 177 PHE A CZ  1 
ATOM   1399 N  N   . ASN A 1 178 ? 39.150  -9.806  18.224  1.00 14.52  ? 178 ASN A N   1 
ATOM   1400 C  CA  . ASN A 1 178 ? 38.973  -10.163 16.841  1.00 13.51  ? 178 ASN A CA  1 
ATOM   1401 C  C   . ASN A 1 178 ? 37.493  -9.911  16.449  1.00 12.29  ? 178 ASN A C   1 
ATOM   1402 O  O   . ASN A 1 178 ? 36.584  -10.676 16.765  1.00 16.07  ? 178 ASN A O   1 
ATOM   1403 C  CB  . ASN A 1 178 ? 39.401  -11.615 16.584  1.00 17.05  ? 178 ASN A CB  1 
ATOM   1404 C  CG  . ASN A 1 178 ? 39.219  -12.018 15.123  1.00 16.40  ? 178 ASN A CG  1 
ATOM   1405 O  OD1 . ASN A 1 178 ? 38.980  -11.161 14.276  1.00 16.83  ? 178 ASN A OD1 1 
ATOM   1406 N  ND2 . ASN A 1 178 ? 39.324  -13.301 14.799  1.00 20.54  ? 178 ASN A ND2 1 
ATOM   1407 N  N   . ILE A 1 179 ? 37.244  -8.783  15.793  1.00 14.36  ? 179 ILE A N   1 
ATOM   1408 C  CA  . ILE A 1 179 ? 35.898  -8.421  15.360  1.00 13.47  ? 179 ILE A CA  1 
ATOM   1409 C  C   . ILE A 1 179 ? 35.246  -9.466  14.436  1.00 13.30  ? 179 ILE A C   1 
ATOM   1410 O  O   . ILE A 1 179 ? 34.019  -9.542  14.400  1.00 13.13  ? 179 ILE A O   1 
ATOM   1411 C  CB  . ILE A 1 179 ? 35.931  -7.044  14.658  1.00 13.41  ? 179 ILE A CB  1 
ATOM   1412 C  CG1 . ILE A 1 179 ? 36.586  -5.977  15.544  1.00 13.64  ? 179 ILE A CG1 1 
ATOM   1413 C  CG2 . ILE A 1 179 ? 34.522  -6.602  14.257  1.00 14.35  ? 179 ILE A CG2 1 
ATOM   1414 C  CD1 . ILE A 1 179 ? 36.002  -5.801  16.936  1.00 13.37  ? 179 ILE A CD1 1 
ATOM   1415 N  N   . GLU A 1 180 ? 36.073  -10.310 13.778  1.00 13.98  ? 180 GLU A N   1 
ATOM   1416 C  CA  . GLU A 1 180 ? 35.485  -11.340 12.917  1.00 13.51  ? 180 GLU A CA  1 
ATOM   1417 C  C   . GLU A 1 180 ? 34.683  -12.373 13.741  1.00 14.58  ? 180 GLU A C   1 
ATOM   1418 O  O   . GLU A 1 180 ? 33.790  -13.039 13.184  1.00 17.17  ? 180 GLU A O   1 
ATOM   1419 C  CB  . GLU A 1 180 ? 36.549  -12.016 12.050  1.00 16.58  ? 180 GLU A CB  1 
ATOM   1420 C  CG  . GLU A 1 180 ? 35.955  -12.814 10.938  1.00 22.82  ? 180 GLU A CG  1 
ATOM   1421 C  CD  . GLU A 1 180 ? 36.971  -13.259 9.902   1.00 24.06  ? 180 GLU A CD  1 
ATOM   1422 O  OE1 . GLU A 1 180 ? 38.184  -12.973 10.043  1.00 26.27  ? 180 GLU A OE1 1 
ATOM   1423 O  OE2 . GLU A 1 180 ? 36.537  -13.883 8.951   1.00 24.70  ? 180 GLU A OE2 1 
ATOM   1424 N  N   . GLU A 1 181 ? 34.942  -12.450 15.067  1.00 12.81  ? 181 GLU A N   1 
ATOM   1425 C  CA  . GLU A 1 181 ? 34.205  -13.368 15.922  1.00 14.11  ? 181 GLU A CA  1 
ATOM   1426 C  C   . GLU A 1 181 ? 32.726  -12.959 15.993  1.00 14.46  ? 181 GLU A C   1 
ATOM   1427 O  O   . GLU A 1 181 ? 31.900  -13.743 16.432  1.00 14.12  ? 181 GLU A O   1 
ATOM   1428 C  CB  . GLU A 1 181 ? 34.767  -13.396 17.357  1.00 14.48  ? 181 GLU A CB  1 
ATOM   1429 C  CG  . GLU A 1 181 ? 36.185  -13.919 17.456  1.00 17.98  ? 181 GLU A CG  1 
ATOM   1430 C  CD  . GLU A 1 181 ? 36.837  -13.751 18.812  1.00 19.32  ? 181 GLU A CD  1 
ATOM   1431 O  OE1 . GLU A 1 181 ? 36.122  -13.343 19.767  1.00 19.75  ? 181 GLU A OE1 1 
ATOM   1432 O  OE2 . GLU A 1 181 ? 38.081  -14.010 18.915  1.00 19.79  ? 181 GLU A OE2 1 
ATOM   1433 N  N   . LEU A 1 182 ? 32.421  -11.678 15.721  1.00 11.20  ? 182 LEU A N   1 
ATOM   1434 C  CA  . LEU A 1 182 ? 31.039  -11.217 15.741  1.00 11.25  ? 182 LEU A CA  1 
ATOM   1435 C  C   . LEU A 1 182 ? 30.223  -11.618 14.496  1.00 11.48  ? 182 LEU A C   1 
ATOM   1436 O  O   . LEU A 1 182 ? 28.996  -11.435 14.465  1.00 13.41  ? 182 LEU A O   1 
ATOM   1437 C  CB  . LEU A 1 182 ? 30.978  -9.692  15.891  1.00 11.40  ? 182 LEU A CB  1 
ATOM   1438 C  CG  . LEU A 1 182 ? 31.771  -9.147  17.066  1.00 13.31  ? 182 LEU A CG  1 
ATOM   1439 C  CD1 . LEU A 1 182 ? 31.719  -7.638  17.035  1.00 12.75  ? 182 LEU A CD1 1 
ATOM   1440 C  CD2 . LEU A 1 182 ? 31.247  -9.680  18.416  1.00 12.83  ? 182 LEU A CD2 1 
ATOM   1441 N  N   . LEU A 1 183 ? 30.893  -12.096 13.445  1.00 12.46  ? 183 LEU A N   1 
ATOM   1442 C  CA  . LEU A 1 183 ? 30.213  -12.456 12.223  1.00 12.06  ? 183 LEU A CA  1 
ATOM   1443 C  C   . LEU A 1 183 ? 29.670  -13.875 12.337  1.00 12.86  ? 183 LEU A C   1 
ATOM   1444 O  O   . LEU A 1 183 ? 30.225  -14.726 13.027  1.00 14.64  ? 183 LEU A O   1 
ATOM   1445 C  CB  . LEU A 1 183 ? 31.195  -12.374 11.044  1.00 13.32  ? 183 LEU A CB  1 
ATOM   1446 C  CG  . LEU A 1 183 ? 31.912  -11.041 10.899  1.00 13.57  ? 183 LEU A CG  1 
ATOM   1447 C  CD1 . LEU A 1 183 ? 32.778  -11.032 9.628   1.00 17.80  ? 183 LEU A CD1 1 
ATOM   1448 C  CD2 . LEU A 1 183 ? 30.913  -9.846  10.837  1.00 15.83  ? 183 LEU A CD2 1 
ATOM   1449 N  N   . PRO A 1 184 ? 28.606  -14.160 11.575  1.00 11.83  ? 184 PRO A N   1 
ATOM   1450 C  CA  . PRO A 1 184 ? 27.947  -15.465 11.584  1.00 13.63  ? 184 PRO A CA  1 
ATOM   1451 C  C   . PRO A 1 184 ? 28.711  -16.521 10.793  1.00 14.08  ? 184 PRO A C   1 
ATOM   1452 O  O   . PRO A 1 184 ? 29.739  -16.244 10.151  1.00 15.85  ? 184 PRO A O   1 
ATOM   1453 C  CB  . PRO A 1 184 ? 26.608  -15.175 10.930  1.00 14.28  ? 184 PRO A CB  1 
ATOM   1454 C  CG  . PRO A 1 184 ? 26.923  -14.073 9.937   1.00 13.99  ? 184 PRO A CG  1 
ATOM   1455 C  CD  . PRO A 1 184 ? 27.959  -13.226 10.659  1.00 12.26  ? 184 PRO A CD  1 
ATOM   1456 N  N   . GLU A 1 185 ? 28.155  -17.735 10.844  1.00 16.66  ? 185 GLU A N   1 
ATOM   1457 C  CA  . GLU A 1 185 ? 28.600  -18.836 9.986   1.00 17.67  ? 185 GLU A CA  1 
ATOM   1458 C  C   . GLU A 1 185 ? 28.374  -18.468 8.516   1.00 17.66  ? 185 GLU A C   1 
ATOM   1459 O  O   . GLU A 1 185 ? 27.385  -17.826 8.151   1.00 15.70  ? 185 GLU A O   1 
ATOM   1460 C  CB  . GLU A 1 185 ? 27.919  -20.192 10.293  1.00 21.46  ? 185 GLU A CB  1 
ATOM   1461 C  CG  . GLU A 1 185 ? 28.155  -20.581 11.735  1.00 26.95  ? 185 GLU A CG  1 
ATOM   1462 C  CD  . GLU A 1 185 ? 29.635  -20.709 12.083  1.00 35.46  ? 185 GLU A CD  1 
ATOM   1463 O  OE1 . GLU A 1 185 ? 30.362  -21.303 11.303  1.00 39.55  ? 185 GLU A OE1 1 
ATOM   1464 O  OE2 . GLU A 1 185 ? 30.047  -20.189 13.125  1.00 53.07  ? 185 GLU A OE2 1 
ATOM   1465 N  N   . ARG A 1 186 ? 29.270  -18.985 7.673   1.00 14.89  ? 186 ARG A N   1 
ATOM   1466 C  CA  . ARG A 1 186 ? 29.100  -18.932 6.227   1.00 17.89  ? 186 ARG A CA  1 
ATOM   1467 C  C   . ARG A 1 186 ? 28.879  -17.495 5.758   1.00 14.53  ? 186 ARG A C   1 
ATOM   1468 O  O   . ARG A 1 186 ? 27.900  -17.180 5.058   1.00 14.71  ? 186 ARG A O   1 
ATOM   1469 C  CB  . ARG A 1 186 ? 28.020  -19.887 5.733   1.00 20.18  ? 186 ARG A CB  1 
ATOM   1470 C  CG  . ARG A 1 186 ? 28.376  -21.333 6.030   1.00 24.68  ? 186 ARG A CG  1 
ATOM   1471 C  CD  . ARG A 1 186 ? 27.532  -22.453 5.439   1.00 27.32  ? 186 ARG A CD  1 
ATOM   1472 N  NE  . ARG A 1 186 ? 26.104  -22.322 5.640   1.00 31.22  ? 186 ARG A NE  1 
ATOM   1473 C  CZ  . ARG A 1 186 ? 25.456  -22.434 6.793   1.00 37.95  ? 186 ARG A CZ  1 
ATOM   1474 N  NH1 . ARG A 1 186 ? 26.125  -22.622 7.921   1.00 46.61  ? 186 ARG A NH1 1 
ATOM   1475 N  NH2 . ARG A 1 186 ? 24.134  -22.292 6.824   1.00 35.08  ? 186 ARG A NH2 1 
ATOM   1476 N  N   . THR A 1 187 ? 29.867  -16.666 6.087   1.00 14.53  ? 187 THR A N   1 
ATOM   1477 C  CA  . THR A 1 187 ? 29.815  -15.268 5.654   1.00 12.00  ? 187 THR A CA  1 
ATOM   1478 C  C   . THR A 1 187 ? 29.835  -15.091 4.116   1.00 13.80  ? 187 THR A C   1 
ATOM   1479 O  O   . THR A 1 187 ? 29.489  -14.009 3.608   1.00 14.05  ? 187 THR A O   1 
ATOM   1480 C  CB  . THR A 1 187 ? 30.913  -14.397 6.256   1.00 15.27  ? 187 THR A CB  1 
ATOM   1481 O  OG1 . THR A 1 187 ? 32.161  -15.040 5.971   1.00 17.28  ? 187 THR A OG1 1 
ATOM   1482 C  CG2 . THR A 1 187 ? 30.754  -14.173 7.742   1.00 17.10  ? 187 THR A CG2 1 
ATOM   1483 N  N   . ALA A 1 188 ? 30.131  -16.163 3.357   1.00 15.00  ? 188 ALA A N   1 
ATOM   1484 C  CA  . ALA A 1 188 ? 30.041  -16.080 1.907   1.00 15.10  ? 188 ALA A CA  1 
ATOM   1485 C  C   . ALA A 1 188 ? 28.587  -15.913 1.461   1.00 14.18  ? 188 ALA A C   1 
ATOM   1486 O  O   . ALA A 1 188 ? 28.342  -15.520 0.330   1.00 15.93  ? 188 ALA A O   1 
ATOM   1487 C  CB  . ALA A 1 188 ? 30.606  -17.354 1.294   1.00 18.22  ? 188 ALA A CB  1 
ATOM   1488 N  N   . GLU A 1 189 ? 27.629  -16.247 2.347   1.00 14.46  ? 189 GLU A N   1 
ATOM   1489 C  CA  . GLU A 1 189 ? 26.211  -16.163 2.059   1.00 13.21  ? 189 GLU A CA  1 
ATOM   1490 C  C   . GLU A 1 189 ? 25.656  -14.854 2.581   1.00 10.92  ? 189 GLU A C   1 
ATOM   1491 O  O   . GLU A 1 189 ? 25.597  -14.655 3.810   1.00 12.46  ? 189 GLU A O   1 
ATOM   1492 C  CB  . GLU A 1 189 ? 25.466  -17.343 2.696   1.00 15.20  ? 189 GLU A CB  1 
ATOM   1493 C  CG  . GLU A 1 189 ? 25.848  -18.741 2.160   1.00 21.02  ? 189 GLU A CG  1 
ATOM   1494 C  CD  . GLU A 1 189 ? 25.297  -19.947 2.927   1.00 23.07  ? 189 GLU A CD  1 
ATOM   1495 O  OE1 . GLU A 1 189 ? 24.518  -19.755 3.914   1.00 29.13  ? 189 GLU A OE1 1 
ATOM   1496 O  OE2 . GLU A 1 189 ? 25.714  -21.111 2.603   1.00 32.65  ? 189 GLU A OE2 1 
ATOM   1497 N  N   . TYR A 1 190 ? 25.200  -14.002 1.648   1.00 11.53  ? 190 TYR A N   1 
ATOM   1498 C  CA  . TYR A 1 190 ? 24.765  -12.657 2.018   1.00 9.83   ? 190 TYR A CA  1 
ATOM   1499 C  C   . TYR A 1 190 ? 23.753  -12.075 1.018   1.00 10.79  ? 190 TYR A C   1 
ATOM   1500 O  O   . TYR A 1 190 ? 23.660  -12.512 -0.134  1.00 11.25  ? 190 TYR A O   1 
ATOM   1501 C  CB  . TYR A 1 190 ? 25.912  -11.671 2.307   1.00 11.12  ? 190 TYR A CB  1 
ATOM   1502 C  CG  . TYR A 1 190 ? 26.843  -11.490 1.137   1.00 10.82  ? 190 TYR A CG  1 
ATOM   1503 C  CD1 . TYR A 1 190 ? 26.538  -10.628 0.099   1.00 11.63  ? 190 TYR A CD1 1 
ATOM   1504 C  CD2 . TYR A 1 190 ? 28.031  -12.202 1.042   1.00 11.97  ? 190 TYR A CD2 1 
ATOM   1505 C  CE1 . TYR A 1 190 ? 27.399  -10.423 -0.971  1.00 12.23  ? 190 TYR A CE1 1 
ATOM   1506 C  CE2 . TYR A 1 190 ? 28.894  -12.043 -0.029  1.00 12.46  ? 190 TYR A CE2 1 
ATOM   1507 C  CZ  . TYR A 1 190 ? 28.593  -11.129 -1.029  1.00 11.69  ? 190 TYR A CZ  1 
ATOM   1508 O  OH  . TYR A 1 190 ? 29.433  -10.968 -2.103  1.00 13.06  ? 190 TYR A OH  1 
ATOM   1509 N  N   . TYR A 1 191 ? 22.974  -11.087 1.514   1.00 10.24  ? 191 TYR A N   1 
ATOM   1510 C  CA  . TYR A 1 191 ? 22.097  -10.213 0.719   1.00 10.17  ? 191 TYR A CA  1 
ATOM   1511 C  C   . TYR A 1 191 ? 22.840  -8.910  0.459   1.00 9.27   ? 191 TYR A C   1 
ATOM   1512 O  O   . TYR A 1 191 ? 23.595  -8.449  1.308   1.00 11.45  ? 191 TYR A O   1 
ATOM   1513 C  CB  . TYR A 1 191 ? 20.821  -9.872  1.483   1.00 9.94   ? 191 TYR A CB  1 
ATOM   1514 C  CG  . TYR A 1 191 ? 20.029  -11.019 2.092   1.00 10.75  ? 191 TYR A CG  1 
ATOM   1515 C  CD1 . TYR A 1 191 ? 18.943  -11.551 1.403   1.00 11.39  ? 191 TYR A CD1 1 
ATOM   1516 C  CD2 . TYR A 1 191 ? 20.254  -11.433 3.401   1.00 10.97  ? 191 TYR A CD2 1 
ATOM   1517 C  CE1 . TYR A 1 191 ? 18.157  -12.564 1.921   1.00 12.53  ? 191 TYR A CE1 1 
ATOM   1518 C  CE2 . TYR A 1 191 ? 19.447  -12.415 3.962   1.00 12.39  ? 191 TYR A CE2 1 
ATOM   1519 C  CZ  . TYR A 1 191 ? 18.393  -12.975 3.228   1.00 12.43  ? 191 TYR A CZ  1 
ATOM   1520 O  OH  . TYR A 1 191 ? 17.628  -13.971 3.755   1.00 14.55  ? 191 TYR A OH  1 
ATOM   1521 N  N   . ARG A 1 192 ? 22.644  -8.360  -0.727  1.00 10.95  ? 192 ARG A N   1 
ATOM   1522 C  CA  . ARG A 1 192 ? 23.368  -7.140  -1.112  1.00 10.24  ? 192 ARG A CA  1 
ATOM   1523 C  C   . ARG A 1 192 ? 22.428  -6.199  -1.850  1.00 11.52  ? 192 ARG A C   1 
ATOM   1524 O  O   . ARG A 1 192 ? 21.697  -6.648  -2.762  1.00 11.47  ? 192 ARG A O   1 
ATOM   1525 C  CB  . ARG A 1 192 ? 24.468  -7.522  -2.139  1.00 11.28  ? 192 ARG A CB  1 
ATOM   1526 C  CG  . ARG A 1 192 ? 25.144  -6.383  -2.894  1.00 12.47  ? 192 ARG A CG  1 
ATOM   1527 C  CD  . ARG A 1 192 ? 25.937  -5.419  -2.052  1.00 13.31  ? 192 ARG A CD  1 
ATOM   1528 N  NE  . ARG A 1 192 ? 26.937  -6.022  -1.170  1.00 12.18  ? 192 ARG A NE  1 
ATOM   1529 C  CZ  . ARG A 1 192 ? 28.055  -6.645  -1.588  1.00 13.15  ? 192 ARG A CZ  1 
ATOM   1530 N  NH1 . ARG A 1 192 ? 28.403  -6.638  -2.868  1.00 12.79  ? 192 ARG A NH1 1 
ATOM   1531 N  NH2 . ARG A 1 192 ? 28.872  -7.183  -0.702  1.00 14.29  ? 192 ARG A NH2 1 
ATOM   1532 N  N   . TYR A 1 193 ? 22.429  -4.921  -1.388  1.00 10.24  ? 193 TYR A N   1 
ATOM   1533 C  CA  . TYR A 1 193 ? 21.605  -3.941  -2.109  1.00 10.61  ? 193 TYR A CA  1 
ATOM   1534 C  C   . TYR A 1 193 ? 22.186  -2.555  -1.835  1.00 9.52   ? 193 TYR A C   1 
ATOM   1535 O  O   . TYR A 1 193 ? 22.898  -2.393  -0.838  1.00 10.73  ? 193 TYR A O   1 
ATOM   1536 C  CB  . TYR A 1 193 ? 20.103  -4.041  -1.776  1.00 10.87  ? 193 TYR A CB  1 
ATOM   1537 C  CG  . TYR A 1 193 ? 19.732  -3.484  -0.427  1.00 10.70  ? 193 TYR A CG  1 
ATOM   1538 C  CD1 . TYR A 1 193 ? 19.919  -4.210  0.757   1.00 10.57  ? 193 TYR A CD1 1 
ATOM   1539 C  CD2 . TYR A 1 193 ? 19.195  -2.202  -0.324  1.00 10.41  ? 193 TYR A CD2 1 
ATOM   1540 C  CE1 . TYR A 1 193 ? 19.643  -3.700  2.016   1.00 9.80   ? 193 TYR A CE1 1 
ATOM   1541 C  CE2 . TYR A 1 193 ? 18.847  -1.705  0.911   1.00 9.32   ? 193 TYR A CE2 1 
ATOM   1542 C  CZ  . TYR A 1 193 ? 19.069  -2.425  2.077   1.00 8.27   ? 193 TYR A CZ  1 
ATOM   1543 O  OH  . TYR A 1 193 ? 18.744  -1.867  3.280   1.00 9.94   ? 193 TYR A OH  1 
ATOM   1544 N  N   . ARG A 1 194 ? 21.814  -1.626  -2.709  1.00 11.42  ? 194 ARG A N   1 
ATOM   1545 C  CA  . ARG A 1 194 ? 22.180  -0.230  -2.513  1.00 8.72   ? 194 ARG A CA  1 
ATOM   1546 C  C   . ARG A 1 194 ? 21.079  0.480   -1.725  1.00 9.05   ? 194 ARG A C   1 
ATOM   1547 O  O   . ARG A 1 194 ? 19.904  0.491   -2.132  1.00 11.45  ? 194 ARG A O   1 
ATOM   1548 C  CB  . ARG A 1 194 ? 22.359  0.500   -3.852  1.00 12.85  ? 194 ARG A CB  1 
ATOM   1549 C  CG  . ARG A 1 194 ? 23.650  0.137   -4.560  1.00 17.92  ? 194 ARG A CG  1 
ATOM   1550 C  CD  . ARG A 1 194 ? 23.963  0.845   -5.882  1.00 28.02  ? 194 ARG A CD  1 
ATOM   1551 N  NE  . ARG A 1 194 ? 25.243  0.317   -6.368  1.00 41.59  ? 194 ARG A NE  1 
ATOM   1552 C  CZ  . ARG A 1 194 ? 26.474  0.667   -5.950  1.00 45.60  ? 194 ARG A CZ  1 
ATOM   1553 N  NH1 . ARG A 1 194 ? 26.665  1.591   -5.015  1.00 44.94  ? 194 ARG A NH1 1 
ATOM   1554 N  NH2 . ARG A 1 194 ? 27.517  0.071   -6.480  1.00 52.86  ? 194 ARG A NH2 1 
ATOM   1555 N  N   . GLY A 1 195 ? 21.470  1.065   -0.591  1.00 10.63  ? 195 GLY A N   1 
ATOM   1556 C  CA  . GLY A 1 195 ? 20.495  1.774   0.216   1.00 10.46  ? 195 GLY A CA  1 
ATOM   1557 C  C   . GLY A 1 195 ? 21.073  2.960   0.956   1.00 8.81   ? 195 GLY A C   1 
ATOM   1558 O  O   . GLY A 1 195 ? 21.920  3.707   0.410   1.00 11.00  ? 195 GLY A O   1 
ATOM   1559 N  N   . SER A 1 196 ? 20.607  3.150   2.199   1.00 8.61   ? 196 SER A N   1 
ATOM   1560 C  CA  . SER A 1 196 ? 20.925  4.420   2.860   1.00 8.41   ? 196 SER A CA  1 
ATOM   1561 C  C   . SER A 1 196 ? 21.414  4.133   4.305   1.00 7.69   ? 196 SER A C   1 
ATOM   1562 O  O   . SER A 1 196 ? 21.260  3.013   4.853   1.00 9.10   ? 196 SER A O   1 
ATOM   1563 C  CB  . SER A 1 196 ? 19.711  5.367   2.969   1.00 9.84   ? 196 SER A CB  1 
ATOM   1564 O  OG  . SER A 1 196 ? 18.789  4.849   3.941   1.00 9.82   ? 196 SER A OG  1 
ATOM   1565 N  N   . LEU A 1 197 ? 21.884  5.179   4.976   1.00 8.56   ? 197 LEU A N   1 
ATOM   1566 C  CA  . LEU A 1 197 ? 21.954  5.136   6.437   1.00 9.12   ? 197 LEU A CA  1 
ATOM   1567 C  C   . LEU A 1 197 ? 20.538  4.879   6.967   1.00 9.22   ? 197 LEU A C   1 
ATOM   1568 O  O   . LEU A 1 197 ? 19.567  5.442   6.410   1.00 9.20   ? 197 LEU A O   1 
ATOM   1569 C  CB  . LEU A 1 197 ? 22.439  6.480   6.986   1.00 10.97  ? 197 LEU A CB  1 
ATOM   1570 C  CG  . LEU A 1 197 ? 23.944  6.732   7.031   1.00 13.31  ? 197 LEU A CG  1 
ATOM   1571 C  CD1 . LEU A 1 197 ? 24.382  7.187   5.639   1.00 18.21  ? 197 LEU A CD1 1 
ATOM   1572 C  CD2 . LEU A 1 197 ? 24.187  7.904   7.990   1.00 15.41  ? 197 LEU A CD2 1 
ATOM   1573 N  N   . THR A 1 198 ? 20.424  4.119   8.084   1.00 8.92   ? 198 THR A N   1 
ATOM   1574 C  CA  . THR A 1 198 ? 19.115  3.926   8.703   1.00 8.22   ? 198 THR A CA  1 
ATOM   1575 C  C   . THR A 1 198 ? 18.812  4.945   9.778   1.00 9.82   ? 198 THR A C   1 
ATOM   1576 O  O   . THR A 1 198 ? 17.747  4.892   10.420  1.00 10.12  ? 198 THR A O   1 
ATOM   1577 C  CB  . THR A 1 198 ? 18.975  2.521   9.284   1.00 7.89   ? 198 THR A CB  1 
ATOM   1578 O  OG1 . THR A 1 198 ? 19.913  2.404   10.339  1.00 8.94   ? 198 THR A OG1 1 
ATOM   1579 C  CG2 . THR A 1 198 ? 19.190  1.450   8.245   1.00 9.67   ? 198 THR A CG2 1 
ATOM   1580 N  N   . THR A 1 199 ? 19.765  5.856   9.976   1.00 8.21   ? 199 THR A N   1 
ATOM   1581 C  CA  . THR A 1 199 ? 19.649  6.959   10.941  1.00 9.32   ? 199 THR A CA  1 
ATOM   1582 C  C   . THR A 1 199 ? 19.792  8.252   10.170  1.00 10.30  ? 199 THR A C   1 
ATOM   1583 O  O   . THR A 1 199 ? 20.437  8.273   9.123   1.00 10.76  ? 199 THR A O   1 
ATOM   1584 C  CB  . THR A 1 199 ? 20.757  6.965   12.019  1.00 8.99   ? 199 THR A CB  1 
ATOM   1585 O  OG1 . THR A 1 199 ? 22.011  7.017   11.332  1.00 12.30  ? 199 THR A OG1 1 
ATOM   1586 C  CG2 . THR A 1 199 ? 20.721  5.667   12.830  1.00 11.75  ? 199 THR A CG2 1 
ATOM   1587 N  N   . PRO A 1 200 ? 19.313  9.374   10.748  1.00 10.14  ? 200 PRO A N   1 
ATOM   1588 C  CA  . PRO A 1 200 ? 19.701  10.664  10.188  1.00 8.79   ? 200 PRO A CA  1 
ATOM   1589 C  C   . PRO A 1 200 ? 21.216  10.703  10.035  1.00 11.97  ? 200 PRO A C   1 
ATOM   1590 O  O   . PRO A 1 200 ? 21.931  10.162  10.878  1.00 12.35  ? 200 PRO A O   1 
ATOM   1591 C  CB  . PRO A 1 200 ? 19.169  11.643  11.258  1.00 11.65  ? 200 PRO A CB  1 
ATOM   1592 C  CG  . PRO A 1 200 ? 17.946  10.947  11.781  1.00 10.26  ? 200 PRO A CG  1 
ATOM   1593 C  CD  . PRO A 1 200 ? 18.432  9.507   11.918  1.00 11.11  ? 200 PRO A CD  1 
ATOM   1594 N  N   . PRO A 1 201 ? 21.797  11.328  8.968   1.00 11.15  ? 201 PRO A N   1 
ATOM   1595 C  CA  . PRO A 1 201 ? 21.038  12.026  7.915   1.00 12.04  ? 201 PRO A CA  1 
ATOM   1596 C  C   . PRO A 1 201 ? 20.459  11.217  6.740   1.00 9.59   ? 201 PRO A C   1 
ATOM   1597 O  O   . PRO A 1 201 ? 20.003  11.802  5.783   1.00 12.54  ? 201 PRO A O   1 
ATOM   1598 C  CB  . PRO A 1 201 ? 22.097  12.991  7.325   1.00 12.53  ? 201 PRO A CB  1 
ATOM   1599 C  CG  . PRO A 1 201 ? 23.320  12.897  8.218   1.00 15.02  ? 201 PRO A CG  1 
ATOM   1600 C  CD  . PRO A 1 201 ? 23.250  11.517  8.840   1.00 13.98  ? 201 PRO A CD  1 
ATOM   1601 N  N   . CYS A 1 202 ? 20.437  9.863   6.821   1.00 9.67   ? 202 CYS A N   1 
ATOM   1602 C  CA  . CYS A 1 202 ? 19.758  8.952   5.897   1.00 9.95   ? 202 CYS A CA  1 
ATOM   1603 C  C   . CYS A 1 202 ? 20.375  9.027   4.493   1.00 10.09  ? 202 CYS A C   1 
ATOM   1604 O  O   . CYS A 1 202 ? 19.666  8.748   3.525   1.00 9.36   ? 202 CYS A O   1 
ATOM   1605 C  CB  . CYS A 1 202 ? 18.246  9.237   5.802   1.00 9.92   ? 202 CYS A CB  1 
ATOM   1606 S  SG  . CYS A 1 202 ? 17.365  9.130   7.399   1.00 9.80   ? 202 CYS A SG  1 
ATOM   1607 N  N   . ASN A 1 203 ? 21.656  9.435   4.320   1.00 10.35  ? 203 ASN A N   1 
ATOM   1608 C  CA  . ASN A 1 203 ? 22.189  9.574   2.967   1.00 11.76  ? 203 ASN A CA  1 
ATOM   1609 C  C   . ASN A 1 203 ? 22.128  8.275   2.181   1.00 10.23  ? 203 ASN A C   1 
ATOM   1610 O  O   . ASN A 1 203 ? 22.374  7.223   2.771   1.00 10.42  ? 203 ASN A O   1 
ATOM   1611 C  CB  . ASN A 1 203 ? 23.651  10.015  3.006   1.00 16.94  ? 203 ASN A CB  1 
ATOM   1612 C  CG  . ASN A 1 203 ? 23.808  11.250  3.871   1.00 16.41  ? 203 ASN A CG  1 
ATOM   1613 O  OD1 . ASN A 1 203 ? 23.812  11.138  5.099   1.00 20.62  ? 203 ASN A OD1 1 
ATOM   1614 N  ND2 . ASN A 1 203 ? 23.858  12.426  3.244   1.00 19.34  ? 203 ASN A ND2 1 
ATOM   1615 N  N   . PRO A 1 204 ? 21.727  8.325   0.877   1.00 11.79  ? 204 PRO A N   1 
ATOM   1616 C  CA  . PRO A 1 204 ? 21.531  7.123   0.043   1.00 11.03  ? 204 PRO A CA  1 
ATOM   1617 C  C   . PRO A 1 204 ? 22.874  6.649   -0.520  1.00 11.91  ? 204 PRO A C   1 
ATOM   1618 O  O   . PRO A 1 204 ? 23.040  6.545   -1.727  1.00 15.48  ? 204 PRO A O   1 
ATOM   1619 C  CB  . PRO A 1 204 ? 20.520  7.567   -1.036  1.00 13.70  ? 204 PRO A CB  1 
ATOM   1620 C  CG  . PRO A 1 204 ? 20.890  9.043   -1.222  1.00 12.14  ? 204 PRO A CG  1 
ATOM   1621 C  CD  . PRO A 1 204 ? 21.256  9.536   0.176   1.00 12.08  ? 204 PRO A CD  1 
ATOM   1622 N  N   . THR A 1 205 ? 23.848  6.379   0.384   1.00 11.50  ? 205 THR A N   1 
ATOM   1623 C  CA  . THR A 1 205 ? 25.242  6.206   -0.013  1.00 12.92  ? 205 THR A CA  1 
ATOM   1624 C  C   . THR A 1 205 ? 25.832  4.908   0.552   1.00 11.74  ? 205 THR A C   1 
ATOM   1625 O  O   . THR A 1 205 ? 27.049  4.767   0.547   1.00 11.49  ? 205 THR A O   1 
ATOM   1626 C  CB  . THR A 1 205 ? 26.044  7.385   0.538   1.00 13.01  ? 205 THR A CB  1 
ATOM   1627 O  OG1 . THR A 1 205 ? 25.790  7.446   1.938   1.00 14.25  ? 205 THR A OG1 1 
ATOM   1628 C  CG2 . THR A 1 205 ? 25.650  8.713   -0.067  1.00 13.34  ? 205 THR A CG2 1 
ATOM   1629 N  N   . VAL A 1 206 ? 24.954  4.011   1.017   1.00 11.80  ? 206 VAL A N   1 
ATOM   1630 C  CA  . VAL A 1 206 ? 25.431  2.791   1.655   1.00 10.14  ? 206 VAL A CA  1 
ATOM   1631 C  C   . VAL A 1 206 ? 25.242  1.560   0.760   1.00 11.47  ? 206 VAL A C   1 
ATOM   1632 O  O   . VAL A 1 206 ? 24.144  1.271   0.313   1.00 12.10  ? 206 VAL A O   1 
ATOM   1633 C  CB  . VAL A 1 206 ? 24.720  2.561   3.006   1.00 10.38  ? 206 VAL A CB  1 
ATOM   1634 C  CG1 . VAL A 1 206 ? 25.132  1.203   3.603   1.00 10.80  ? 206 VAL A CG1 1 
ATOM   1635 C  CG2 . VAL A 1 206 ? 24.940  3.704   3.972   1.00 11.49  ? 206 VAL A CG2 1 
ATOM   1636 N  N   . LEU A 1 207 ? 26.336  0.848   0.552   1.00 9.77   ? 207 LEU A N   1 
ATOM   1637 C  CA  . LEU A 1 207 ? 26.269  -0.496  -0.019  1.00 12.04  ? 207 LEU A CA  1 
ATOM   1638 C  C   . LEU A 1 207 ? 26.058  -1.463  1.159   1.00 10.77  ? 207 LEU A C   1 
ATOM   1639 O  O   . LEU A 1 207 ? 26.937  -1.593  2.014   1.00 10.11  ? 207 LEU A O   1 
ATOM   1640 C  CB  . LEU A 1 207 ? 27.565  -0.831  -0.785  1.00 12.82  ? 207 LEU A CB  1 
ATOM   1641 C  CG  . LEU A 1 207 ? 27.462  -2.105  -1.622  1.00 17.73  ? 207 LEU A CG  1 
ATOM   1642 C  CD1 . LEU A 1 207 ? 26.420  -1.964  -2.736  1.00 18.65  ? 207 LEU A CD1 1 
ATOM   1643 C  CD2 . LEU A 1 207 ? 28.816  -2.519  -2.166  1.00 26.42  ? 207 LEU A CD2 1 
ATOM   1644 N  N   . TRP A 1 208 ? 24.873  -2.092  1.204   1.00 9.60   ? 208 TRP A N   1 
ATOM   1645 C  CA  . TRP A 1 208 ? 24.553  -3.012  2.301   1.00 9.51   ? 208 TRP A CA  1 
ATOM   1646 C  C   . TRP A 1 208 ? 24.964  -4.439  1.953   1.00 9.72   ? 208 TRP A C   1 
ATOM   1647 O  O   . TRP A 1 208 ? 24.645  -4.943  0.874   1.00 10.22  ? 208 TRP A O   1 
ATOM   1648 C  CB  . TRP A 1 208 ? 23.021  -3.002  2.570   1.00 8.79   ? 208 TRP A CB  1 
ATOM   1649 C  CG  . TRP A 1 208 ? 22.633  -1.758  3.324   1.00 8.21   ? 208 TRP A CG  1 
ATOM   1650 C  CD1 . TRP A 1 208 ? 22.152  -0.535  2.846   1.00 9.65   ? 208 TRP A CD1 1 
ATOM   1651 C  CD2 . TRP A 1 208 ? 22.731  -1.610  4.758   1.00 9.09   ? 208 TRP A CD2 1 
ATOM   1652 N  NE1 . TRP A 1 208 ? 21.964  0.305   3.905   1.00 11.20  ? 208 TRP A NE1 1 
ATOM   1653 C  CE2 . TRP A 1 208 ? 22.363  -0.277  5.085   1.00 8.52   ? 208 TRP A CE2 1 
ATOM   1654 C  CE3 . TRP A 1 208 ? 23.135  -2.461  5.805   1.00 8.59   ? 208 TRP A CE3 1 
ATOM   1655 C  CZ2 . TRP A 1 208 ? 22.312  0.183   6.415   1.00 9.70   ? 208 TRP A CZ2 1 
ATOM   1656 C  CZ3 . TRP A 1 208 ? 23.154  -1.995  7.092   1.00 8.84   ? 208 TRP A CZ3 1 
ATOM   1657 C  CH2 . TRP A 1 208 ? 22.821  -0.659  7.388   1.00 8.37   ? 208 TRP A CH2 1 
ATOM   1658 N  N   . THR A 1 209 ? 25.534  -5.090  2.980   1.00 7.56   ? 209 THR A N   1 
ATOM   1659 C  CA  . THR A 1 209 ? 25.744  -6.538  2.952   1.00 7.64   ? 209 THR A CA  1 
ATOM   1660 C  C   . THR A 1 209 ? 25.119  -7.068  4.252   1.00 8.46   ? 209 THR A C   1 
ATOM   1661 O  O   . THR A 1 209 ? 25.598  -6.753  5.337   1.00 9.68   ? 209 THR A O   1 
ATOM   1662 C  CB  . THR A 1 209 ? 27.248  -6.915  2.906   1.00 8.21   ? 209 THR A CB  1 
ATOM   1663 O  OG1 . THR A 1 209 ? 27.807  -6.311  1.737   1.00 10.72  ? 209 THR A OG1 1 
ATOM   1664 C  CG2 . THR A 1 209 ? 27.472  -8.406  2.920   1.00 11.94  ? 209 THR A CG2 1 
ATOM   1665 N  N   . VAL A 1 210 ? 23.985  -7.785  4.123   1.00 9.45   ? 210 VAL A N   1 
ATOM   1666 C  CA  . VAL A 1 210 ? 23.330  -8.435  5.263   1.00 8.26   ? 210 VAL A CA  1 
ATOM   1667 C  C   . VAL A 1 210 ? 23.609  -9.942  5.219   1.00 9.87   ? 210 VAL A C   1 
ATOM   1668 O  O   . VAL A 1 210 ? 23.253  -10.592 4.253   1.00 10.64  ? 210 VAL A O   1 
ATOM   1669 C  CB  . VAL A 1 210 ? 21.806  -8.189  5.271   1.00 8.47   ? 210 VAL A CB  1 
ATOM   1670 C  CG1 . VAL A 1 210 ? 21.160  -8.755  6.530   1.00 10.61  ? 210 VAL A CG1 1 
ATOM   1671 C  CG2 . VAL A 1 210 ? 21.511  -6.709  5.148   1.00 9.12   ? 210 VAL A CG2 1 
ATOM   1672 N  N   . PHE A 1 211 ? 24.359  -10.442 6.205   1.00 9.46   ? 211 PHE A N   1 
ATOM   1673 C  CA  . PHE A 1 211 ? 24.654  -11.864 6.144   1.00 10.98  ? 211 PHE A CA  1 
ATOM   1674 C  C   . PHE A 1 211 ? 23.359  -12.667 6.209   1.00 8.66   ? 211 PHE A C   1 
ATOM   1675 O  O   . PHE A 1 211 ? 22.420  -12.346 6.939   1.00 11.07  ? 211 PHE A O   1 
ATOM   1676 C  CB  . PHE A 1 211 ? 25.675  -12.263 7.214   1.00 10.55  ? 211 PHE A CB  1 
ATOM   1677 C  CG  . PHE A 1 211 ? 27.028  -11.637 6.938   1.00 10.99  ? 211 PHE A CG  1 
ATOM   1678 C  CD1 . PHE A 1 211 ? 27.810  -11.982 5.836   1.00 11.83  ? 211 PHE A CD1 1 
ATOM   1679 C  CD2 . PHE A 1 211 ? 27.487  -10.582 7.738   1.00 10.47  ? 211 PHE A CD2 1 
ATOM   1680 C  CE1 . PHE A 1 211 ? 29.015  -11.323 5.585   1.00 14.12  ? 211 PHE A CE1 1 
ATOM   1681 C  CE2 . PHE A 1 211 ? 28.711  -9.960  7.496   1.00 10.51  ? 211 PHE A CE2 1 
ATOM   1682 C  CZ  . PHE A 1 211 ? 29.464  -10.308 6.401   1.00 12.86  ? 211 PHE A CZ  1 
ATOM   1683 N  N   . ARG A 1 212 ? 23.385  -13.829 5.526   1.00 10.71  ? 212 ARG A N   1 
ATOM   1684 C  CA  . ARG A 1 212 ? 22.190  -14.681 5.462   1.00 9.99   ? 212 ARG A CA  1 
ATOM   1685 C  C   . ARG A 1 212 ? 21.874  -15.319 6.826   1.00 12.16  ? 212 ARG A C   1 
ATOM   1686 O  O   . ARG A 1 212 ? 20.711  -15.436 7.242   1.00 12.88  ? 212 ARG A O   1 
ATOM   1687 C  CB  . ARG A 1 212 ? 22.406  -15.834 4.490   1.00 13.10  ? 212 ARG A CB  1 
ATOM   1688 C  CG  . ARG A 1 212 ? 21.183  -16.746 4.376   1.00 14.05  ? 212 ARG A CG  1 
ATOM   1689 C  CD  . ARG A 1 212 ? 21.523  -17.971 3.556   1.00 21.05  ? 212 ARG A CD  1 
ATOM   1690 N  NE  . ARG A 1 212 ? 20.343  -18.734 3.159   1.00 23.65  ? 212 ARG A NE  1 
ATOM   1691 C  CZ  . ARG A 1 212 ? 20.364  -19.726 2.267   1.00 27.74  ? 212 ARG A CZ  1 
ATOM   1692 N  NH1 . ARG A 1 212 ? 21.518  -20.173 1.778   1.00 31.50  ? 212 ARG A NH1 1 
ATOM   1693 N  NH2 . ARG A 1 212 ? 19.229  -20.299 1.902   1.00 37.06  ? 212 ARG A NH2 1 
ATOM   1694 N  N   . ASN A 1 213 ? 22.914  -15.678 7.586   1.00 12.28  ? 213 ASN A N   1 
ATOM   1695 C  CA  . ASN A 1 213 ? 22.752  -16.468 8.805   1.00 13.43  ? 213 ASN A CA  1 
ATOM   1696 C  C   . ASN A 1 213 ? 22.852  -15.543 10.019  1.00 11.72  ? 213 ASN A C   1 
ATOM   1697 O  O   . ASN A 1 213 ? 23.771  -14.753 10.090  1.00 12.71  ? 213 ASN A O   1 
ATOM   1698 C  CB  . ASN A 1 213 ? 23.747  -17.632 8.821   1.00 15.17  ? 213 ASN A CB  1 
ATOM   1699 C  CG  . ASN A 1 213 ? 23.661  -18.494 7.591   1.00 17.81  ? 213 ASN A CG  1 
ATOM   1700 O  OD1 . ASN A 1 213 ? 24.665  -18.752 6.930   1.00 22.10  ? 213 ASN A OD1 1 
ATOM   1701 N  ND2 . ASN A 1 213 ? 22.465  -18.947 7.300   1.00 17.06  ? 213 ASN A ND2 1 
ATOM   1702 N  N   . PRO A 1 214 ? 21.959  -15.707 11.032  1.00 11.76  ? 214 PRO A N   1 
ATOM   1703 C  CA  . PRO A 1 214 ? 22.074  -14.932 12.256  1.00 12.35  ? 214 PRO A CA  1 
ATOM   1704 C  C   . PRO A 1 214 ? 23.114  -15.537 13.187  1.00 11.09  ? 214 PRO A C   1 
ATOM   1705 O  O   . PRO A 1 214 ? 23.535  -16.686 13.034  1.00 14.07  ? 214 PRO A O   1 
ATOM   1706 C  CB  . PRO A 1 214 ? 20.692  -15.119 12.869  1.00 12.56  ? 214 PRO A CB  1 
ATOM   1707 C  CG  . PRO A 1 214 ? 20.297  -16.530 12.475  1.00 14.85  ? 214 PRO A CG  1 
ATOM   1708 C  CD  . PRO A 1 214 ? 20.833  -16.666 11.049  1.00 14.80  ? 214 PRO A CD  1 
ATOM   1709 N  N   . VAL A 1 215 ? 23.556  -14.717 14.122  1.00 11.04  ? 215 VAL A N   1 
ATOM   1710 C  CA  . VAL A 1 215 ? 24.255  -15.195 15.320  1.00 11.79  ? 215 VAL A CA  1 
ATOM   1711 C  C   . VAL A 1 215 ? 23.261  -15.329 16.466  1.00 13.32  ? 215 VAL A C   1 
ATOM   1712 O  O   . VAL A 1 215 ? 22.189  -14.769 16.414  1.00 13.11  ? 215 VAL A O   1 
ATOM   1713 C  CB  . VAL A 1 215 ? 25.438  -14.300 15.728  1.00 11.98  ? 215 VAL A CB  1 
ATOM   1714 C  CG1 . VAL A 1 215 ? 26.443  -14.217 14.597  1.00 13.88  ? 215 VAL A CG1 1 
ATOM   1715 C  CG2 . VAL A 1 215 ? 24.983  -12.904 16.100  1.00 12.02  ? 215 VAL A CG2 1 
ATOM   1716 N  N   . GLN A 1 216 ? 23.680  -16.023 17.523  1.00 14.51  ? 216 GLN A N   1 
ATOM   1717 C  CA  . GLN A 1 216 ? 22.898  -16.102 18.745  1.00 13.33  ? 216 GLN A CA  1 
ATOM   1718 C  C   . GLN A 1 216 ? 23.610  -15.463 19.917  1.00 15.10  ? 216 GLN A C   1 
ATOM   1719 O  O   . GLN A 1 216 ? 24.841  -15.518 20.044  1.00 15.73  ? 216 GLN A O   1 
ATOM   1720 C  CB  . GLN A 1 216 ? 22.708  -17.546 19.173  1.00 15.84  ? 216 GLN A CB  1 
ATOM   1721 C  CG  . GLN A 1 216 ? 21.898  -18.297 18.131  1.00 14.06  ? 216 GLN A CG  1 
ATOM   1722 C  CD  . GLN A 1 216 ? 21.423  -19.662 18.517  1.00 18.38  ? 216 GLN A CD  1 
ATOM   1723 O  OE1 . GLN A 1 216 ? 21.864  -20.286 19.505  1.00 18.53  ? 216 GLN A OE1 1 
ATOM   1724 N  NE2 . GLN A 1 216 ? 20.475  -20.139 17.709  1.00 25.79  ? 216 GLN A NE2 1 
ATOM   1725 N  N   . ILE A 1 217 ? 22.776  -14.871 20.771  1.00 15.16  ? 217 ILE A N   1 
ATOM   1726 C  CA  . ILE A 1 217 ? 23.221  -14.409 22.092  1.00 14.33  ? 217 ILE A CA  1 
ATOM   1727 C  C   . ILE A 1 217 ? 22.203  -14.926 23.104  1.00 16.44  ? 217 ILE A C   1 
ATOM   1728 O  O   . ILE A 1 217 ? 21.062  -15.256 22.756  1.00 16.02  ? 217 ILE A O   1 
ATOM   1729 C  CB  . ILE A 1 217 ? 23.308  -12.855 22.142  1.00 13.40  ? 217 ILE A CB  1 
ATOM   1730 C  CG1 . ILE A 1 217 ? 21.957  -12.149 21.939  1.00 14.53  ? 217 ILE A CG1 1 
ATOM   1731 C  CG2 . ILE A 1 217 ? 24.369  -12.289 21.176  1.00 14.58  ? 217 ILE A CG2 1 
ATOM   1732 C  CD1 . ILE A 1 217 ? 21.978  -10.641 22.155  1.00 11.56  ? 217 ILE A CD1 1 
ATOM   1733 N  N   . SER A 1 218 ? 22.607  -14.975 24.374  1.00 15.45  ? 218 SER A N   1 
ATOM   1734 C  CA  . SER A 1 218 ? 21.727  -15.591 25.335  1.00 15.50  ? 218 SER A CA  1 
ATOM   1735 C  C   . SER A 1 218 ? 20.570  -14.649 25.704  1.00 16.40  ? 218 SER A C   1 
ATOM   1736 O  O   . SER A 1 218 ? 20.594  -13.432 25.470  1.00 15.85  ? 218 SER A O   1 
ATOM   1737 C  CB  . SER A 1 218 ? 22.469  -15.991 26.600  1.00 17.71  ? 218 SER A CB  1 
ATOM   1738 O  OG  . SER A 1 218 ? 22.809  -14.788 27.304  1.00 16.90  ? 218 SER A OG  1 
ATOM   1739 N  N   . GLN A 1 219 ? 19.544  -15.231 26.316  1.00 16.35  ? 219 GLN A N   1 
ATOM   1740 C  CA  . GLN A 1 219 ? 18.445  -14.398 26.782  1.00 17.03  ? 219 GLN A CA  1 
ATOM   1741 C  C   . GLN A 1 219 ? 18.949  -13.318 27.736  1.00 17.35  ? 219 GLN A C   1 
ATOM   1742 O  O   . GLN A 1 219 ? 18.466  -12.208 27.680  1.00 16.44  ? 219 GLN A O   1 
ATOM   1743 C  CB  . GLN A 1 219 ? 17.323  -15.216 27.380  1.00 20.96  ? 219 GLN A CB  1 
ATOM   1744 C  CG  . GLN A 1 219 ? 17.753  -16.025 28.571  1.00 26.20  ? 219 GLN A CG  1 
ATOM   1745 C  CD  . GLN A 1 219 ? 16.543  -16.758 29.090  1.00 27.57  ? 219 GLN A CD  1 
ATOM   1746 O  OE1 . GLN A 1 219 ? 16.311  -17.911 28.759  1.00 48.42  ? 219 GLN A OE1 1 
ATOM   1747 N  NE2 . GLN A 1 219 ? 15.772  -16.061 29.915  1.00 43.41  ? 219 GLN A NE2 1 
ATOM   1748 N  N   . GLU A 1 220 ? 19.949  -13.642 28.571  1.00 14.93  ? 220 GLU A N   1 
ATOM   1749 C  CA  . GLU A 1 220 ? 20.460  -12.682 29.537  1.00 16.70  ? 220 GLU A CA  1 
ATOM   1750 C  C   . GLU A 1 220 ? 21.213  -11.567 28.804  1.00 16.58  ? 220 GLU A C   1 
ATOM   1751 O  O   . GLU A 1 220 ? 21.144  -10.384 29.207  1.00 15.88  ? 220 GLU A O   1 
ATOM   1752 C  CB  . GLU A 1 220 ? 21.341  -13.420 30.559  1.00 21.57  ? 220 GLU A CB  1 
ATOM   1753 C  CG  . GLU A 1 220 ? 20.548  -14.388 31.439  1.00 22.13  ? 220 GLU A CG  1 
ATOM   1754 C  CD  . GLU A 1 220 ? 20.313  -15.797 30.881  1.00 25.43  ? 220 GLU A CD  1 
ATOM   1755 O  OE1 . GLU A 1 220 ? 20.810  -16.148 29.737  1.00 25.17  ? 220 GLU A OE1 1 
ATOM   1756 O  OE2 . GLU A 1 220 ? 19.576  -16.534 31.541  1.00 31.24  ? 220 GLU A OE2 1 
ATOM   1757 N  N   . GLN A 1 221 ? 21.994  -11.955 27.788  1.00 15.88  ? 221 GLN A N   1 
ATOM   1758 C  CA  . GLN A 1 221 ? 22.713  -10.937 27.048  1.00 13.41  ? 221 GLN A CA  1 
ATOM   1759 C  C   . GLN A 1 221 ? 21.739  -9.975  26.374  1.00 14.43  ? 221 GLN A C   1 
ATOM   1760 O  O   . GLN A 1 221 ? 21.997  -8.759  26.306  1.00 14.33  ? 221 GLN A O   1 
ATOM   1761 C  CB  . GLN A 1 221 ? 23.635  -11.563 25.998  1.00 14.53  ? 221 GLN A CB  1 
ATOM   1762 C  CG  . GLN A 1 221 ? 24.857  -12.279 26.620  1.00 17.55  ? 221 GLN A CG  1 
ATOM   1763 C  CD  . GLN A 1 221 ? 25.733  -12.888 25.548  1.00 14.46  ? 221 GLN A CD  1 
ATOM   1764 O  OE1 . GLN A 1 221 ? 25.315  -13.796 24.824  1.00 16.14  ? 221 GLN A OE1 1 
ATOM   1765 N  NE2 . GLN A 1 221 ? 26.960  -12.408 25.438  1.00 17.16  ? 221 GLN A NE2 1 
ATOM   1766 N  N   . LEU A 1 222 ? 20.702  -10.516 25.714  1.00 15.58  ? 222 LEU A N   1 
ATOM   1767 C  CA  . LEU A 1 222 ? 19.747  -9.671  25.002  1.00 14.89  ? 222 LEU A CA  1 
ATOM   1768 C  C   . LEU A 1 222 ? 19.096  -8.695  25.996  1.00 16.69  ? 222 LEU A C   1 
ATOM   1769 O  O   . LEU A 1 222 ? 18.914  -7.501  25.718  1.00 14.33  ? 222 LEU A O   1 
ATOM   1770 C  CB  . LEU A 1 222 ? 18.689  -10.563 24.316  1.00 15.84  ? 222 LEU A CB  1 
ATOM   1771 C  CG  . LEU A 1 222 ? 17.575  -9.813  23.570  1.00 13.76  ? 222 LEU A CG  1 
ATOM   1772 C  CD1 . LEU A 1 222 ? 18.185  -8.952  22.447  1.00 14.59  ? 222 LEU A CD1 1 
ATOM   1773 C  CD2 . LEU A 1 222 ? 16.567  -10.776 22.951  1.00 17.09  ? 222 LEU A CD2 1 
ATOM   1774 N  N   . LEU A 1 223 ? 18.701  -9.204  27.171  1.00 14.24  ? 223 LEU A N   1 
ATOM   1775 C  CA  . LEU A 1 223 ? 18.023  -8.386  28.163  1.00 14.98  ? 223 LEU A CA  1 
ATOM   1776 C  C   . LEU A 1 223 ? 18.984  -7.284  28.637  1.00 14.85  ? 223 LEU A C   1 
ATOM   1777 O  O   . LEU A 1 223 ? 18.586  -6.122  28.844  1.00 14.49  ? 223 LEU A O   1 
ATOM   1778 C  CB  . LEU A 1 223 ? 17.583  -9.297  29.307  1.00 17.35  ? 223 LEU A CB  1 
ATOM   1779 C  CG  . LEU A 1 223 ? 16.858  -8.572  30.427  1.00 16.62  ? 223 LEU A CG  1 
ATOM   1780 C  CD1 . LEU A 1 223 ? 15.536  -8.000  29.895  1.00 20.73  ? 223 LEU A CD1 1 
ATOM   1781 C  CD2 . LEU A 1 223 ? 16.678  -9.478  31.622  1.00 21.84  ? 223 LEU A CD2 1 
ATOM   1782 N  N   . ALA A 1 224 ? 20.270  -7.619  28.810  1.00 14.00  ? 224 ALA A N   1 
ATOM   1783 C  CA  . ALA A 1 224 ? 21.238  -6.615  29.258  1.00 15.30  ? 224 ALA A CA  1 
ATOM   1784 C  C   . ALA A 1 224 ? 21.343  -5.509  28.213  1.00 16.96  ? 224 ALA A C   1 
ATOM   1785 O  O   . ALA A 1 224 ? 21.299  -4.323  28.560  1.00 15.69  ? 224 ALA A O   1 
ATOM   1786 C  CB  . ALA A 1 224 ? 22.603  -7.200  29.522  1.00 17.85  ? 224 ALA A CB  1 
ATOM   1787 N  N   . LEU A 1 225 ? 21.466  -5.895  26.937  1.00 15.07  ? 225 LEU A N   1 
ATOM   1788 C  CA  . LEU A 1 225 ? 21.508  -4.902  25.868  1.00 13.86  ? 225 LEU A CA  1 
ATOM   1789 C  C   . LEU A 1 225 ? 20.266  -3.997  25.938  1.00 15.29  ? 225 LEU A C   1 
ATOM   1790 O  O   . LEU A 1 225 ? 20.364  -2.771  25.801  1.00 16.44  ? 225 LEU A O   1 
ATOM   1791 C  CB  . LEU A 1 225 ? 21.605  -5.613  24.504  1.00 15.64  ? 225 LEU A CB  1 
ATOM   1792 C  CG  . LEU A 1 225 ? 21.698  -4.684  23.288  1.00 13.94  ? 225 LEU A CG  1 
ATOM   1793 C  CD1 . LEU A 1 225 ? 22.979  -3.850  23.330  1.00 17.63  ? 225 LEU A CD1 1 
ATOM   1794 C  CD2 . LEU A 1 225 ? 21.635  -5.472  22.003  1.00 16.66  ? 225 LEU A CD2 1 
ATOM   1795 N  N   . GLU A 1 226 ? 19.077  -4.617  26.090  1.00 13.80  ? 226 GLU A N   1 
ATOM   1796 C  CA  . GLU A 1 226 ? 17.824  -3.875  26.090  1.00 15.78  ? 226 GLU A CA  1 
ATOM   1797 C  C   . GLU A 1 226 ? 17.629  -2.969  27.314  1.00 17.59  ? 226 GLU A C   1 
ATOM   1798 O  O   . GLU A 1 226 ? 16.747  -2.117  27.286  1.00 19.89  ? 226 GLU A O   1 
ATOM   1799 C  CB  . GLU A 1 226 ? 16.636  -4.841  26.006  1.00 15.34  ? 226 GLU A CB  1 
ATOM   1800 C  CG  . GLU A 1 226 ? 16.552  -5.592  24.679  1.00 12.26  ? 226 GLU A CG  1 
ATOM   1801 C  CD  . GLU A 1 226 ? 15.646  -6.810  24.733  1.00 12.47  ? 226 GLU A CD  1 
ATOM   1802 O  OE1 . GLU A 1 226 ? 15.345  -7.306  25.898  1.00 15.27  ? 226 GLU A OE1 1 
ATOM   1803 O  OE2 . GLU A 1 226 ? 15.245  -7.239  23.637  1.00 13.55  ? 226 GLU A OE2 1 
ATOM   1804 N  N   . THR A 1 227 ? 18.396  -3.162  28.396  1.00 16.17  ? 227 THR A N   1 
ATOM   1805 C  CA  . THR A 1 227 ? 18.107  -2.501  29.664  1.00 17.77  ? 227 THR A CA  1 
ATOM   1806 C  C   . THR A 1 227 ? 19.291  -1.675  30.178  1.00 19.76  ? 227 THR A C   1 
ATOM   1807 O  O   . THR A 1 227 ? 19.132  -0.949  31.153  1.00 23.54  ? 227 THR A O   1 
ATOM   1808 C  CB  . THR A 1 227 ? 17.615  -3.493  30.733  1.00 18.57  ? 227 THR A CB  1 
ATOM   1809 O  OG1 . THR A 1 227 ? 18.592  -4.499  30.970  1.00 18.97  ? 227 THR A OG1 1 
ATOM   1810 C  CG2 . THR A 1 227 ? 16.301  -4.150  30.365  1.00 21.93  ? 227 THR A CG2 1 
ATOM   1811 N  N   . ALA A 1 228 ? 20.469  -1.783  29.548  1.00 18.15  ? 228 ALA A N   1 
ATOM   1812 C  CA  . ALA A 1 228 ? 21.693  -1.249  30.130  1.00 16.50  ? 228 ALA A CA  1 
ATOM   1813 C  C   . ALA A 1 228 ? 21.766  0.249   29.840  1.00 17.18  ? 228 ALA A C   1 
ATOM   1814 O  O   . ALA A 1 228 ? 22.419  0.977   30.573  1.00 24.82  ? 228 ALA A O   1 
ATOM   1815 C  CB  . ALA A 1 228 ? 22.908  -1.903  29.535  1.00 21.24  ? 228 ALA A CB  1 
ATOM   1816 N  N   . LEU A 1 229 ? 21.116  0.685   28.741  1.00 16.43  ? 229 LEU A N   1 
ATOM   1817 C  CA  . LEU A 1 229 ? 21.453  2.034   28.291  1.00 16.59  ? 229 LEU A CA  1 
ATOM   1818 C  C   . LEU A 1 229 ? 20.278  3.010   28.319  1.00 19.59  ? 229 LEU A C   1 
ATOM   1819 O  O   . LEU A 1 229 ? 19.103  2.617   28.140  1.00 17.54  ? 229 LEU A O   1 
ATOM   1820 C  CB  . LEU A 1 229 ? 22.009  1.960   26.863  1.00 17.20  ? 229 LEU A CB  1 
ATOM   1821 C  CG  . LEU A 1 229 ? 23.163  0.986   26.627  1.00 17.25  ? 229 LEU A CG  1 
ATOM   1822 C  CD1 . LEU A 1 229 ? 23.451  0.885   25.131  1.00 18.48  ? 229 LEU A CD1 1 
ATOM   1823 C  CD2 . LEU A 1 229 ? 24.413  1.332   27.449  1.00 23.04  ? 229 LEU A CD2 1 
ATOM   1824 N  N   . TYR A 1 230 ? 20.649  4.298   28.447  1.00 16.83  ? 230 TYR A N   1 
ATOM   1825 C  CA  . TYR A 1 230 ? 19.734  5.419   28.358  1.00 19.77  ? 230 TYR A CA  1 
ATOM   1826 C  C   . TYR A 1 230 ? 20.171  6.353   27.225  1.00 19.19  ? 230 TYR A C   1 
ATOM   1827 O  O   . TYR A 1 230 ? 21.352  6.423   26.898  1.00 20.62  ? 230 TYR A O   1 
ATOM   1828 C  CB  . TYR A 1 230 ? 19.711  6.230   29.654  1.00 20.37  ? 230 TYR A CB  1 
ATOM   1829 C  CG  . TYR A 1 230 ? 19.001  5.578   30.811  1.00 23.86  ? 230 TYR A CG  1 
ATOM   1830 C  CD1 . TYR A 1 230 ? 19.583  4.525   31.487  1.00 30.91  ? 230 TYR A CD1 1 
ATOM   1831 C  CD2 . TYR A 1 230 ? 17.767  6.030   31.263  1.00 29.47  ? 230 TYR A CD2 1 
ATOM   1832 C  CE1 . TYR A 1 230 ? 18.952  3.927   32.567  1.00 40.31  ? 230 TYR A CE1 1 
ATOM   1833 C  CE2 . TYR A 1 230 ? 17.120  5.442   32.343  1.00 33.53  ? 230 TYR A CE2 1 
ATOM   1834 C  CZ  . TYR A 1 230 ? 17.731  4.404   33.021  1.00 37.28  ? 230 TYR A CZ  1 
ATOM   1835 O  OH  . TYR A 1 230 ? 17.110  3.813   34.086  1.00 51.90  ? 230 TYR A OH  1 
ATOM   1836 N  N   . CYS A 1 231 ? 19.203  7.084   26.661  1.00 18.47  ? 231 CYS A N   1 
ATOM   1837 C  CA  . CYS A 1 231 ? 19.472  8.135   25.690  1.00 21.20  ? 231 CYS A CA  1 
ATOM   1838 C  C   . CYS A 1 231 ? 19.870  9.468   26.299  1.00 22.66  ? 231 CYS A C   1 
ATOM   1839 O  O   . CYS A 1 231 ? 20.355  10.324  25.568  1.00 24.02  ? 231 CYS A O   1 
ATOM   1840 C  CB  . CYS A 1 231 ? 18.258  8.504   24.846  1.00 21.01  ? 231 CYS A CB  1 
ATOM   1841 S  SG  . CYS A 1 231 ? 17.671  7.107   23.895  1.00 21.92  ? 231 CYS A SG  1 
ATOM   1842 N  N   . THR A 1 232 ? 19.632  9.620   27.604  1.00 21.68  ? 232 THR A N   1 
ATOM   1843 C  CA  . THR A 1 232 ? 19.787  10.894  28.292  1.00 21.32  ? 232 THR A CA  1 
ATOM   1844 C  C   . THR A 1 232 ? 21.060  10.935  29.143  1.00 20.56  ? 232 THR A C   1 
ATOM   1845 O  O   . THR A 1 232 ? 21.611  9.906   29.552  1.00 20.32  ? 232 THR A O   1 
ATOM   1846 C  CB  . THR A 1 232 ? 18.548  11.171  29.162  1.00 20.72  ? 232 THR A CB  1 
ATOM   1847 O  OG1 . THR A 1 232 ? 18.278  9.927   29.813  1.00 20.07  ? 232 THR A OG1 1 
ATOM   1848 C  CG2 . THR A 1 232 ? 17.353  11.615  28.337  1.00 24.13  ? 232 THR A CG2 1 
ATOM   1849 N  N   . HIS A 1 233 ? 21.506  12.174  29.410  1.00 18.40  ? 233 HIS A N   1 
ATOM   1850 C  CA  . HIS A 1 233 ? 22.597  12.445  30.330  1.00 24.18  ? 233 HIS A CA  1 
ATOM   1851 C  C   . HIS A 1 233 ? 22.255  11.965  31.737  1.00 26.62  ? 233 HIS A C   1 
ATOM   1852 O  O   . HIS A 1 233 ? 21.093  11.956  32.137  1.00 24.50  ? 233 HIS A O   1 
ATOM   1853 C  CB  . HIS A 1 233 ? 22.843  13.948  30.440  1.00 27.90  ? 233 HIS A CB  1 
ATOM   1854 C  CG  . HIS A 1 233 ? 23.631  14.550  29.316  1.00 47.08  ? 233 HIS A CG  1 
ATOM   1855 N  ND1 . HIS A 1 233 ? 23.061  15.405  28.377  1.00 50.67  ? 233 HIS A ND1 1 
ATOM   1856 C  CD2 . HIS A 1 233 ? 24.944  14.453  28.982  1.00 54.13  ? 233 HIS A CD2 1 
ATOM   1857 C  CE1 . HIS A 1 233 ? 23.989  15.802  27.516  1.00 58.86  ? 233 HIS A CE1 1 
ATOM   1858 N  NE2 . HIS A 1 233 ? 25.154  15.230  27.861  1.00 55.10  ? 233 HIS A NE2 1 
ATOM   1859 N  N   . MET A 1 234 ? 23.287  11.571  32.475  1.00 26.99  ? 234 MET A N   1 
ATOM   1860 C  CA  . MET A 1 234 ? 23.178  11.080  33.845  1.00 29.27  ? 234 MET A CA  1 
ATOM   1861 C  C   . MET A 1 234 ? 22.263  11.973  34.701  1.00 26.84  ? 234 MET A C   1 
ATOM   1862 O  O   . MET A 1 234 ? 21.572  11.480  35.592  1.00 29.93  ? 234 MET A O   1 
ATOM   1863 C  CB  . MET A 1 234 ? 24.590  11.016  34.447  1.00 39.68  ? 234 MET A CB  1 
ATOM   1864 C  CG  . MET A 1 234 ? 24.656  10.665  35.914  1.00 39.53  ? 234 MET A CG  1 
ATOM   1865 S  SD  . MET A 1 234 ? 26.312  10.106  36.371  1.00 52.94  ? 234 MET A SD  1 
ATOM   1866 C  CE  . MET A 1 234 ? 27.236  11.620  36.107  1.00 50.40  ? 234 MET A CE  1 
ATOM   1867 N  N   . ASP A 1 235 ? 22.340  13.298  34.470  1.00 26.61  ? 235 ASP A N   1 
ATOM   1868 C  CA  . ASP A 1 235 ? 21.681  14.346  35.312  1.00 28.98  ? 235 ASP A CA  1 
ATOM   1869 C  C   . ASP A 1 235 ? 20.312  14.829  34.808  1.00 29.35  ? 235 ASP A C   1 
ATOM   1870 O  O   . ASP A 1 235 ? 19.751  15.742  35.445  1.00 36.26  ? 235 ASP A O   1 
ATOM   1871 C  CB  . ASP A 1 235 ? 22.591  15.564  35.483  1.00 42.04  ? 235 ASP A CB  1 
ATOM   1872 C  CG  . ASP A 1 235 ? 24.069  15.222  35.450  1.00 44.47  ? 235 ASP A CG  1 
ATOM   1873 O  OD2 . ASP A 1 235 ? 24.692  15.252  36.524  1.00 61.24  ? 235 ASP A OD2 1 
ATOM   1874 N  N   . ASP A 1 236 ? 19.790  14.245  33.710  1.00 26.78  ? 236 ASP A N   1 
ATOM   1875 C  CA  . ASP A 1 236 ? 18.487  14.563  33.156  1.00 30.61  ? 236 ASP A CA  1 
ATOM   1876 C  C   . ASP A 1 236 ? 17.448  14.107  34.179  1.00 32.01  ? 236 ASP A C   1 
ATOM   1877 O  O   . ASP A 1 236 ? 17.399  12.944  34.579  1.00 30.16  ? 236 ASP A O   1 
ATOM   1878 C  CB  . ASP A 1 236 ? 18.306  13.890  31.785  1.00 31.00  ? 236 ASP A CB  1 
ATOM   1879 C  CG  . ASP A 1 236 ? 17.245  14.507  30.887  1.00 33.03  ? 236 ASP A CG  1 
ATOM   1880 O  OD1 . ASP A 1 236 ? 16.204  14.991  31.397  1.00 38.88  ? 236 ASP A OD1 1 
ATOM   1881 O  OD2 . ASP A 1 236 ? 17.467  14.506  29.677  1.00 36.73  ? 236 ASP A OD2 1 
ATOM   1882 N  N   . PRO A 1 237 ? 16.603  15.016  34.699  1.00 38.27  ? 237 PRO A N   1 
ATOM   1883 C  CA  . PRO A 1 237 ? 15.590  14.603  35.667  1.00 36.45  ? 237 PRO A CA  1 
ATOM   1884 C  C   . PRO A 1 237 ? 14.489  13.787  34.989  1.00 46.19  ? 237 PRO A C   1 
ATOM   1885 O  O   . PRO A 1 237 ? 13.653  13.172  35.661  1.00 37.71  ? 237 PRO A O   1 
ATOM   1886 C  CB  . PRO A 1 237 ? 15.085  15.945  36.193  1.00 38.55  ? 237 PRO A CB  1 
ATOM   1887 C  CG  . PRO A 1 237 ? 15.295  16.914  35.048  1.00 46.59  ? 237 PRO A CG  1 
ATOM   1888 C  CD  . PRO A 1 237 ? 16.563  16.442  34.359  1.00 41.08  ? 237 PRO A CD  1 
ATOM   1889 N  N   . SER A 1 238 ? 14.543  13.723  33.648  1.00 34.33  ? 238 SER A N   1 
ATOM   1890 C  CA  . SER A 1 238 ? 13.538  12.986  32.909  1.00 31.41  ? 238 SER A CA  1 
ATOM   1891 C  C   . SER A 1 238 ? 14.220  11.979  31.976  1.00 31.49  ? 238 SER A C   1 
ATOM   1892 O  O   . SER A 1 238 ? 14.240  12.099  30.741  1.00 33.90  ? 238 SER A O   1 
ATOM   1893 C  CB  . SER A 1 238 ? 12.538  13.908  32.259  1.00 46.41  ? 238 SER A CB  1 
ATOM   1894 O  OG  . SER A 1 238 ? 12.846  14.122  30.896  1.00 49.50  ? 238 SER A OG  1 
ATOM   1895 N  N   . PRO A 1 239 ? 14.794  10.907  32.560  1.00 28.39  ? 239 PRO A N   1 
ATOM   1896 C  CA  . PRO A 1 239 ? 15.527  9.914   31.793  1.00 29.30  ? 239 PRO A CA  1 
ATOM   1897 C  C   . PRO A 1 239 ? 14.635  9.211   30.769  1.00 27.36  ? 239 PRO A C   1 
ATOM   1898 O  O   . PRO A 1 239 ? 13.413  9.077   30.947  1.00 30.35  ? 239 PRO A O   1 
ATOM   1899 C  CB  . PRO A 1 239 ? 16.065  8.964   32.877  1.00 26.52  ? 239 PRO A CB  1 
ATOM   1900 C  CG  . PRO A 1 239 ? 15.092  9.107   34.020  1.00 35.71  ? 239 PRO A CG  1 
ATOM   1901 C  CD  . PRO A 1 239 ? 14.726  10.577  33.997  1.00 28.06  ? 239 PRO A CD  1 
ATOM   1902 N  N   . ARG A 1 240 ? 15.280  8.825   29.662  1.00 23.58  ? 240 ARG A N   1 
ATOM   1903 C  CA  . ARG A 1 240 ? 14.674  8.072   28.575  1.00 22.15  ? 240 ARG A CA  1 
ATOM   1904 C  C   . ARG A 1 240 ? 15.548  6.850   28.322  1.00 20.43  ? 240 ARG A C   1 
ATOM   1905 O  O   . ARG A 1 240 ? 16.727  6.998   28.012  1.00 23.03  ? 240 ARG A O   1 
ATOM   1906 C  CB  . ARG A 1 240 ? 14.586  8.918   27.287  1.00 26.28  ? 240 ARG A CB  1 
ATOM   1907 C  CG  . ARG A 1 240 ? 13.593  10.077  27.300  1.00 29.88  ? 240 ARG A CG  1 
ATOM   1908 C  CD  . ARG A 1 240 ? 13.587  10.930  26.031  1.00 28.88  ? 240 ARG A CD  1 
ATOM   1909 N  NE  . ARG A 1 240 ? 14.795  11.741  25.799  1.00 35.55  ? 240 ARG A NE  1 
ATOM   1910 C  CZ  . ARG A 1 240 ? 15.722  11.546  24.851  1.00 34.13  ? 240 ARG A CZ  1 
ATOM   1911 N  NH1 . ARG A 1 240 ? 15.625  10.536  23.983  1.00 34.38  ? 240 ARG A NH1 1 
ATOM   1912 N  NH2 . ARG A 1 240 ? 16.769  12.366  24.803  1.00 33.89  ? 240 ARG A NH2 1 
ATOM   1913 N  N   . GLU A 1 241 ? 14.939  5.655   28.383  1.00 22.04  ? 241 GLU A N   1 
ATOM   1914 C  CA  . GLU A 1 241 ? 15.646  4.418   28.094  1.00 18.07  ? 241 GLU A CA  1 
ATOM   1915 C  C   . GLU A 1 241 ? 16.007  4.319   26.615  1.00 18.51  ? 241 GLU A C   1 
ATOM   1916 O  O   . GLU A 1 241 ? 15.234  4.730   25.744  1.00 18.50  ? 241 GLU A O   1 
ATOM   1917 C  CB  . GLU A 1 241 ? 14.737  3.212   28.368  1.00 20.46  ? 241 GLU A CB  1 
ATOM   1918 C  CG  . GLU A 1 241 ? 14.477  2.970   29.829  1.00 21.67  ? 241 GLU A CG  1 
ATOM   1919 C  CD  . GLU A 1 241 ? 13.421  1.921   30.185  1.00 33.46  ? 241 GLU A CD  1 
ATOM   1920 O  OE1 . GLU A 1 241 ? 12.583  1.557   29.316  1.00 45.94  ? 241 GLU A OE1 1 
ATOM   1921 O  OE2 . GLU A 1 241 ? 13.447  1.447   31.320  1.00 42.65  ? 241 GLU A OE2 1 
ATOM   1922 N  N   . MET A 1 242 ? 17.179  3.732   26.341  1.00 16.29  ? 242 MET A N   1 
ATOM   1923 C  CA  . MET A 1 242 ? 17.582  3.458   24.962  1.00 14.28  ? 242 MET A CA  1 
ATOM   1924 C  C   . MET A 1 242 ? 17.028  2.114   24.518  1.00 13.68  ? 242 MET A C   1 
ATOM   1925 O  O   . MET A 1 242 ? 17.647  1.079   24.736  1.00 14.87  ? 242 MET A O   1 
ATOM   1926 C  CB  . MET A 1 242 ? 19.095  3.521   24.738  1.00 14.64  ? 242 MET A CB  1 
ATOM   1927 C  CG  . MET A 1 242 ? 19.479  3.446   23.275  1.00 16.10  ? 242 MET A CG  1 
ATOM   1928 S  SD  . MET A 1 242 ? 21.247  3.503   22.997  1.00 17.89  ? 242 MET A SD  1 
ATOM   1929 C  CE  . MET A 1 242 ? 21.603  5.203   23.297  1.00 15.68  ? 242 MET A CE  1 
ATOM   1930 N  N   . ILE A 1 243 ? 15.821  2.152   23.949  1.00 12.97  ? 243 ILE A N   1 
ATOM   1931 C  CA  . ILE A 1 243 ? 15.130  0.946   23.472  1.00 12.05  ? 243 ILE A CA  1 
ATOM   1932 C  C   . ILE A 1 243 ? 14.522  1.239   22.101  1.00 12.29  ? 243 ILE A C   1 
ATOM   1933 O  O   . ILE A 1 243 ? 14.291  2.383   21.758  1.00 12.58  ? 243 ILE A O   1 
ATOM   1934 C  CB  . ILE A 1 243 ? 13.998  0.552   24.447  1.00 15.48  ? 243 ILE A CB  1 
ATOM   1935 C  CG1 . ILE A 1 243 ? 13.090  1.749   24.787  1.00 14.86  ? 243 ILE A CG1 1 
ATOM   1936 C  CG2 . ILE A 1 243 ? 14.611  -0.051  25.702  1.00 18.54  ? 243 ILE A CG2 1 
ATOM   1937 C  CD1 . ILE A 1 243 ? 11.853  1.355   25.663  1.00 18.38  ? 243 ILE A CD1 1 
ATOM   1938 N  N   . ASN A 1 244 ? 14.121  0.189   21.367  1.00 9.65   ? 244 ASN A N   1 
ATOM   1939 C  CA  . ASN A 1 244 ? 13.404  0.326   20.109  1.00 10.46  ? 244 ASN A CA  1 
ATOM   1940 C  C   . ASN A 1 244 ? 14.147  1.306   19.187  1.00 8.96   ? 244 ASN A C   1 
ATOM   1941 O  O   . ASN A 1 244 ? 13.495  2.070   18.443  1.00 10.85  ? 244 ASN A O   1 
ATOM   1942 C  CB  . ASN A 1 244 ? 11.970  0.791   20.381  1.00 11.16  ? 244 ASN A CB  1 
ATOM   1943 C  CG  . ASN A 1 244 ? 11.237  -0.119  21.318  1.00 11.69  ? 244 ASN A CG  1 
ATOM   1944 O  OD1 . ASN A 1 244 ? 11.460  -1.335  21.217  1.00 15.13  ? 244 ASN A OD1 1 
ATOM   1945 N  ND2 . ASN A 1 244 ? 10.354  0.426   22.144  1.00 15.33  ? 244 ASN A ND2 1 
ATOM   1946 N  N   . ASN A 1 245 ? 15.499  1.220   19.186  1.00 8.72   ? 245 ASN A N   1 
ATOM   1947 C  CA  . ASN A 1 245 ? 16.325  2.115   18.382  1.00 10.37  ? 245 ASN A CA  1 
ATOM   1948 C  C   . ASN A 1 245 ? 16.561  1.481   17.004  1.00 9.03   ? 245 ASN A C   1 
ATOM   1949 O  O   . ASN A 1 245 ? 17.688  1.345   16.565  1.00 9.60   ? 245 ASN A O   1 
ATOM   1950 C  CB  . ASN A 1 245 ? 17.621  2.459   19.122  1.00 10.97  ? 245 ASN A CB  1 
ATOM   1951 C  CG  . ASN A 1 245 ? 18.503  1.276   19.414  1.00 8.89   ? 245 ASN A CG  1 
ATOM   1952 O  OD1 . ASN A 1 245 ? 18.008  0.135   19.479  1.00 11.81  ? 245 ASN A OD1 1 
ATOM   1953 N  ND2 . ASN A 1 245 ? 19.797  1.501   19.560  1.00 12.65  ? 245 ASN A ND2 1 
ATOM   1954 N  N   . PHE A 1 246 ? 15.476  1.105   16.327  1.00 8.72   ? 246 PHE A N   1 
ATOM   1955 C  CA  . PHE A 1 246 ? 15.498  0.616   14.941  1.00 7.67   ? 246 PHE A CA  1 
ATOM   1956 C  C   . PHE A 1 246 ? 14.531  1.452   14.106  1.00 7.19   ? 246 PHE A C   1 
ATOM   1957 O  O   . PHE A 1 246 ? 13.495  1.863   14.656  1.00 8.93   ? 246 PHE A O   1 
ATOM   1958 C  CB  . PHE A 1 246 ? 15.160  -0.914  14.896  1.00 8.55   ? 246 PHE A CB  1 
ATOM   1959 C  CG  . PHE A 1 246 ? 13.780  -1.287  15.379  1.00 8.55   ? 246 PHE A CG  1 
ATOM   1960 C  CD1 . PHE A 1 246 ? 13.524  -1.452  16.744  1.00 8.24   ? 246 PHE A CD1 1 
ATOM   1961 C  CD2 . PHE A 1 246 ? 12.724  -1.393  14.478  1.00 10.75  ? 246 PHE A CD2 1 
ATOM   1962 C  CE1 . PHE A 1 246 ? 12.260  -1.758  17.232  1.00 9.58   ? 246 PHE A CE1 1 
ATOM   1963 C  CE2 . PHE A 1 246 ? 11.434  -1.614  14.947  1.00 10.57  ? 246 PHE A CE2 1 
ATOM   1964 C  CZ  . PHE A 1 246 ? 11.196  -1.825  16.321  1.00 9.56   ? 246 PHE A CZ  1 
ATOM   1965 N  N   . ARG A 1 247 ? 14.813  1.540   12.790  1.00 7.14   ? 247 ARG A N   1 
ATOM   1966 C  CA  . ARG A 1 247 ? 13.879  2.219   11.862  1.00 8.47   ? 247 ARG A CA  1 
ATOM   1967 C  C   . ARG A 1 247 ? 12.918  1.216   11.281  1.00 7.82   ? 247 ARG A C   1 
ATOM   1968 O  O   . ARG A 1 247 ? 13.298  0.045   11.081  1.00 8.83   ? 247 ARG A O   1 
ATOM   1969 C  CB  . ARG A 1 247 ? 14.657  2.973   10.764  1.00 8.30   ? 247 ARG A CB  1 
ATOM   1970 C  CG  . ARG A 1 247 ? 13.832  3.932   9.911   1.00 8.72   ? 247 ARG A CG  1 
ATOM   1971 C  CD  . ARG A 1 247 ? 14.707  4.405   8.769   1.00 8.72   ? 247 ARG A CD  1 
ATOM   1972 N  NE  . ARG A 1 247 ? 14.097  5.608   8.151   1.00 7.63   ? 247 ARG A NE  1 
ATOM   1973 C  CZ  . ARG A 1 247 ? 14.569  6.210   7.081   1.00 8.92   ? 247 ARG A CZ  1 
ATOM   1974 N  NH1 . ARG A 1 247 ? 15.602  5.674   6.430   1.00 8.79   ? 247 ARG A NH1 1 
ATOM   1975 N  NH2 . ARG A 1 247 ? 14.021  7.329   6.598   1.00 9.01   ? 247 ARG A NH2 1 
ATOM   1976 N  N   . GLN A 1 248 ? 11.646  1.616   11.123  1.00 7.96   ? 248 GLN A N   1 
ATOM   1977 C  CA  . GLN A 1 248 ? 10.694  0.773   10.431  1.00 6.21   ? 248 GLN A CA  1 
ATOM   1978 C  C   . GLN A 1 248 ? 11.153  0.521   8.994   1.00 7.11   ? 248 GLN A C   1 
ATOM   1979 O  O   . GLN A 1 248 ? 11.865  1.301   8.392   1.00 8.86   ? 248 GLN A O   1 
ATOM   1980 C  CB  . GLN A 1 248 ? 9.323   1.461   10.324  1.00 8.36   ? 248 GLN A CB  1 
ATOM   1981 C  CG  . GLN A 1 248 ? 8.637   1.745   11.698  1.00 8.66   ? 248 GLN A CG  1 
ATOM   1982 C  CD  . GLN A 1 248 ? 8.280   0.481   12.428  1.00 8.89   ? 248 GLN A CD  1 
ATOM   1983 O  OE1 . GLN A 1 248 ? 9.068   0.080   13.327  1.00 9.59   ? 248 GLN A OE1 1 
ATOM   1984 N  NE2 . GLN A 1 248 ? 7.122   -0.104  12.090  1.00 10.00  ? 248 GLN A NE2 1 
ATOM   1985 N  N   . VAL A 1 249 ? 10.789  -0.661  8.425   1.00 7.32   ? 249 VAL A N   1 
ATOM   1986 C  CA  . VAL A 1 249 ? 11.134  -0.954  7.046   1.00 7.50   ? 249 VAL A CA  1 
ATOM   1987 C  C   . VAL A 1 249 ? 10.520  0.062   6.082   1.00 8.34   ? 249 VAL A C   1 
ATOM   1988 O  O   . VAL A 1 249 ? 9.400   0.557   6.318   1.00 8.90   ? 249 VAL A O   1 
ATOM   1989 C  CB  . VAL A 1 249 ? 10.840  -2.415  6.639   1.00 11.63  ? 249 VAL A CB  1 
ATOM   1990 C  CG1 . VAL A 1 249 ? 11.693  -3.396  7.446   1.00 10.83  ? 249 VAL A CG1 1 
ATOM   1991 C  CG2 . VAL A 1 249 ? 9.378   -2.711  6.738   1.00 11.50  ? 249 VAL A CG2 1 
ATOM   1992 N  N   . GLN A 1 250 ? 11.262  0.273   5.006   1.00 7.99   ? 250 GLN A N   1 
ATOM   1993 C  CA  . GLN A 1 250 ? 10.911  1.262   4.005   1.00 8.47   ? 250 GLN A CA  1 
ATOM   1994 C  C   . GLN A 1 250 ? 10.307  0.590   2.772   1.00 9.52   ? 250 GLN A C   1 
ATOM   1995 O  O   . GLN A 1 250 ? 10.655  -0.567  2.479   1.00 11.34  ? 250 GLN A O   1 
ATOM   1996 C  CB  . GLN A 1 250 ? 12.180  1.996   3.523   1.00 9.47   ? 250 GLN A CB  1 
ATOM   1997 C  CG  . GLN A 1 250 ? 12.988  2.650   4.684   1.00 9.32   ? 250 GLN A CG  1 
ATOM   1998 C  CD  . GLN A 1 250 ? 12.183  3.746   5.336   1.00 9.08   ? 250 GLN A CD  1 
ATOM   1999 O  OE1 . GLN A 1 250 ? 11.916  4.779   4.682   1.00 10.19  ? 250 GLN A OE1 1 
ATOM   2000 N  NE2 . GLN A 1 250 ? 11.898  3.608   6.619   1.00 8.22   ? 250 GLN A NE2 1 
ATOM   2001 N  N   . LYS A 1 251 ? 9.393   1.278   2.056   1.00 9.57   ? 251 LYS A N   1 
ATOM   2002 C  CA  . LYS A 1 251 ? 8.966   0.750   0.762   1.00 11.46  ? 251 LYS A CA  1 
ATOM   2003 C  C   . LYS A 1 251 ? 10.198  0.553   -0.144  1.00 10.94  ? 251 LYS A C   1 
ATOM   2004 O  O   . LYS A 1 251 ? 11.122  1.358   -0.152  1.00 13.77  ? 251 LYS A O   1 
ATOM   2005 C  CB  . LYS A 1 251 ? 8.027   1.749   0.099   1.00 12.55  ? 251 LYS A CB  1 
ATOM   2006 C  CG  . LYS A 1 251 ? 6.668   1.707   0.769   1.00 13.95  ? 251 LYS A CG  1 
ATOM   2007 C  CD  . LYS A 1 251 ? 5.708   2.611   0.218   1.00 14.46  ? 251 LYS A CD  1 
ATOM   2008 C  CE  . LYS A 1 251 ? 4.248   2.309   0.603   1.00 10.24  ? 251 LYS A CE  1 
ATOM   2009 N  NZ  . LYS A 1 251 ? 4.022   2.284   2.071   1.00 8.24   ? 251 LYS A NZ  1 
ATOM   2010 N  N   . PHE A 1 252 ? 10.175  -0.515  -0.922  1.00 13.59  ? 252 PHE A N   1 
ATOM   2011 C  CA  . PHE A 1 252 ? 11.303  -0.862  -1.782  1.00 14.40  ? 252 PHE A CA  1 
ATOM   2012 C  C   . PHE A 1 252 ? 10.641  -1.363  -3.067  1.00 22.51  ? 252 PHE A C   1 
ATOM   2013 O  O   . PHE A 1 252 ? 10.244  -2.519  -3.116  1.00 33.55  ? 252 PHE A O   1 
ATOM   2014 C  CB  . PHE A 1 252 ? 12.071  -2.041  -1.172  1.00 16.17  ? 252 PHE A CB  1 
ATOM   2015 C  CG  . PHE A 1 252 ? 13.385  -2.340  -1.851  1.00 16.20  ? 252 PHE A CG  1 
ATOM   2016 C  CD1 . PHE A 1 252 ? 14.477  -1.499  -1.702  1.00 17.64  ? 252 PHE A CD1 1 
ATOM   2017 C  CD2 . PHE A 1 252 ? 13.557  -3.539  -2.551  1.00 22.03  ? 252 PHE A CD2 1 
ATOM   2018 C  CE1 . PHE A 1 252 ? 15.717  -1.825  -2.255  1.00 20.99  ? 252 PHE A CE1 1 
ATOM   2019 C  CE2 . PHE A 1 252 ? 14.779  -3.841  -3.129  1.00 21.88  ? 252 PHE A CE2 1 
ATOM   2020 C  CZ  . PHE A 1 252 ? 15.869  -2.994  -2.975  1.00 22.96  ? 252 PHE A CZ  1 
ATOM   2021 N  N   . ASP A 1 253 ? 10.385  -0.500  -4.042  1.00 27.40  ? 253 ASP A N   1 
ATOM   2022 C  CA  . ASP A 1 253 ? 9.536   -0.907  -5.159  1.00 31.27  ? 253 ASP A CA  1 
ATOM   2023 C  C   . ASP A 1 253 ? 10.342  -0.968  -6.450  1.00 25.96  ? 253 ASP A C   1 
ATOM   2024 O  O   . ASP A 1 253 ? 11.173  -0.103  -6.688  1.00 29.66  ? 253 ASP A O   1 
ATOM   2025 C  CB  . ASP A 1 253 ? 8.332   0.026   -5.347  1.00 31.78  ? 253 ASP A CB  1 
ATOM   2026 C  CG  . ASP A 1 253 ? 7.251   -0.545  -6.261  1.00 39.88  ? 253 ASP A CG  1 
ATOM   2027 O  OD1 . ASP A 1 253 ? 6.962   -1.777  -6.143  1.00 39.61  ? 253 ASP A OD1 1 
ATOM   2028 O  OD2 . ASP A 1 253 ? 6.713   0.234   -7.104  1.00 40.21  ? 253 ASP A OD2 1 
ATOM   2029 N  N   . GLU A 1 254 ? 10.053  -1.988  -7.282  1.00 27.67  ? 254 GLU A N   1 
ATOM   2030 C  CA  . GLU A 1 254 ? 10.648  -2.123  -8.601  1.00 29.01  ? 254 GLU A CA  1 
ATOM   2031 C  C   . GLU A 1 254 ? 12.163  -2.188  -8.453  1.00 28.79  ? 254 GLU A C   1 
ATOM   2032 O  O   . GLU A 1 254 ? 12.891  -1.617  -9.273  1.00 37.40  ? 254 GLU A O   1 
ATOM   2033 C  CB  . GLU A 1 254 ? 10.193  -0.980  -9.516  1.00 25.76  ? 254 GLU A CB  1 
ATOM   2034 C  CG  . GLU A 1 254 ? 8.690   -1.013  -9.754  1.00 30.02  ? 254 GLU A CG  1 
ATOM   2035 C  CD  . GLU A 1 254 ? 8.202   0.082   -10.672 1.00 37.94  ? 254 GLU A CD  1 
ATOM   2036 O  OE1 . GLU A 1 254 ? 8.729   1.213   -10.600 1.00 41.16  ? 254 GLU A OE1 1 
ATOM   2037 O  OE2 . GLU A 1 254 ? 7.278   -0.195  -11.427 1.00 38.78  ? 254 GLU A OE2 1 
ATOM   2038 N  N   . ARG A 1 255 ? 12.605  -2.906  -7.411  1.00 29.75  ? 255 ARG A N   1 
ATOM   2039 C  CA  . ARG A 1 255 ? 14.013  -3.079  -7.104  1.00 22.06  ? 255 ARG A CA  1 
ATOM   2040 C  C   . ARG A 1 255 ? 14.295  -4.464  -6.530  1.00 25.30  ? 255 ARG A C   1 
ATOM   2041 O  O   . ARG A 1 255 ? 13.396  -5.169  -6.047  1.00 28.36  ? 255 ARG A O   1 
ATOM   2042 C  CB  . ARG A 1 255 ? 14.546  -2.082  -6.076  1.00 24.22  ? 255 ARG A CB  1 
ATOM   2043 C  CG  . ARG A 1 255 ? 14.484  -0.626  -6.507  1.00 27.16  ? 255 ARG A CG  1 
ATOM   2044 C  CD  . ARG A 1 255 ? 14.936  0.354   -5.422  1.00 25.06  ? 255 ARG A CD  1 
ATOM   2045 N  NE  . ARG A 1 255 ? 16.348  0.043   -5.281  1.00 27.78  ? 255 ARG A NE  1 
ATOM   2046 C  CZ  . ARG A 1 255 ? 17.082  0.287   -4.204  1.00 25.20  ? 255 ARG A CZ  1 
ATOM   2047 N  NH1 . ARG A 1 255 ? 16.524  0.870   -3.147  1.00 29.88  ? 255 ARG A NH1 1 
ATOM   2048 N  NH2 . ARG A 1 255 ? 18.351  -0.093  -4.211  1.00 19.17  ? 255 ARG A NH2 1 
ATOM   2049 N  N   . LEU A 1 256 ? 15.572  -4.872  -6.654  1.00 25.04  ? 256 LEU A N   1 
ATOM   2050 C  CA  . LEU A 1 256 ? 15.937  -6.219  -6.258  1.00 22.47  ? 256 LEU A CA  1 
ATOM   2051 C  C   . LEU A 1 256 ? 16.929  -6.191  -5.121  1.00 17.23  ? 256 LEU A C   1 
ATOM   2052 O  O   . LEU A 1 256 ? 17.676  -5.216  -4.950  1.00 23.30  ? 256 LEU A O   1 
ATOM   2053 C  CB  . LEU A 1 256 ? 16.529  -6.942  -7.467  1.00 24.82  ? 256 LEU A CB  1 
ATOM   2054 C  CG  . LEU A 1 256 ? 15.563  -7.202  -8.635  1.00 27.35  ? 256 LEU A CG  1 
ATOM   2055 C  CD1 . LEU A 1 256 ? 16.315  -7.755  -9.829  1.00 32.31  ? 256 LEU A CD1 1 
ATOM   2056 C  CD2 . LEU A 1 256 ? 14.496  -8.205  -8.198  1.00 35.47  ? 256 LEU A CD2 1 
ATOM   2057 N  N   . VAL A 1 257 ? 16.908  -7.320  -4.393  1.00 20.89  ? 257 VAL A N   1 
ATOM   2058 C  CA  . VAL A 1 257 ? 17.999  -7.612  -3.516  1.00 16.82  ? 257 VAL A CA  1 
ATOM   2059 C  C   . VAL A 1 257 ? 18.727  -8.799  -4.101  1.00 17.30  ? 257 VAL A C   1 
ATOM   2060 O  O   . VAL A 1 257 ? 18.145  -9.868  -4.322  1.00 19.23  ? 257 VAL A O   1 
ATOM   2061 C  CB  . VAL A 1 257 ? 17.484  -7.951  -2.114  1.00 15.01  ? 257 VAL A CB  1 
ATOM   2062 C  CG1 . VAL A 1 257 ? 18.617  -8.478  -1.221  1.00 13.34  ? 257 VAL A CG1 1 
ATOM   2063 C  CG2 . VAL A 1 257 ? 16.807  -6.723  -1.514  1.00 16.34  ? 257 VAL A CG2 1 
ATOM   2064 N  N   . TYR A 1 258 ? 20.023  -8.634  -4.271  1.00 14.69  ? 258 TYR A N   1 
ATOM   2065 C  CA  . TYR A 1 258 ? 20.832  -9.686  -4.856  1.00 13.94  ? 258 TYR A CA  1 
ATOM   2066 C  C   . TYR A 1 258 ? 21.346  -10.595 -3.749  1.00 14.26  ? 258 TYR A C   1 
ATOM   2067 O  O   . TYR A 1 258 ? 21.683  -10.137 -2.676  1.00 15.35  ? 258 TYR A O   1 
ATOM   2068 C  CB  . TYR A 1 258 ? 21.977  -9.023  -5.639  1.00 17.30  ? 258 TYR A CB  1 
ATOM   2069 C  CG  . TYR A 1 258 ? 21.437  -8.092  -6.697  1.00 20.66  ? 258 TYR A CG  1 
ATOM   2070 C  CD1 . TYR A 1 258 ? 20.894  -8.593  -7.867  1.00 22.75  ? 258 TYR A CD1 1 
ATOM   2071 C  CD2 . TYR A 1 258 ? 21.337  -6.741  -6.449  1.00 20.26  ? 258 TYR A CD2 1 
ATOM   2072 C  CE1 . TYR A 1 258 ? 20.346  -7.733  -8.820  1.00 25.99  ? 258 TYR A CE1 1 
ATOM   2073 C  CE2 . TYR A 1 258 ? 20.783  -5.870  -7.370  1.00 26.88  ? 258 TYR A CE2 1 
ATOM   2074 C  CZ  . TYR A 1 258 ? 20.284  -6.364  -8.567  1.00 23.47  ? 258 TYR A CZ  1 
ATOM   2075 O  OH  . TYR A 1 258 ? 19.722  -5.506  -9.471  1.00 34.64  ? 258 TYR A OH  1 
ATOM   2076 N  N   . THR A 1 259 ? 21.442  -11.893 -4.033  1.00 14.55  ? 259 THR A N   1 
ATOM   2077 C  CA  . THR A 1 259 ? 21.941  -12.848 -3.056  1.00 13.35  ? 259 THR A CA  1 
ATOM   2078 C  C   . THR A 1 259 ? 23.150  -13.575 -3.629  1.00 11.35  ? 259 THR A C   1 
ATOM   2079 O  O   . THR A 1 259 ? 23.206  -13.878 -4.823  1.00 13.32  ? 259 THR A O   1 
ATOM   2080 C  CB  . THR A 1 259 ? 20.845  -13.836 -2.602  1.00 13.59  ? 259 THR A CB  1 
ATOM   2081 O  OG1 . THR A 1 259 ? 20.377  -14.521 -3.768  1.00 16.97  ? 259 THR A OG1 1 
ATOM   2082 C  CG2 . THR A 1 259 ? 19.667  -13.140 -1.936  1.00 14.79  ? 259 THR A CG2 1 
ATOM   2083 N  N   . SER A 1 260 ? 24.112  -13.842 -2.728  1.00 12.78  ? 260 SER A N   1 
ATOM   2084 C  CA  . SER A 1 260 ? 25.295  -14.625 -3.109  1.00 12.88  ? 260 SER A CA  1 
ATOM   2085 C  C   . SER A 1 260 ? 25.008  -16.127 -3.055  1.00 14.82  ? 260 SER A C   1 
ATOM   2086 O  O   . SER A 1 260 ? 25.893  -16.948 -3.412  1.00 17.62  ? 260 SER A O   1 
ATOM   2087 C  CB  . SER A 1 260 ? 26.482  -14.353 -2.229  1.00 13.34  ? 260 SER A CB  1 
ATOM   2088 O  OG  . SER A 1 260 ? 26.166  -14.776 -0.926  1.00 12.74  ? 260 SER A OG  1 
ATOM   2089 N  N   . PHE A 1 261 ? 23.785  -16.521 -2.647  1.00 14.77  ? 261 PHE A N   1 
ATOM   2090 C  CA  . PHE A 1 261 ? 23.374  -17.937 -2.545  1.00 16.12  ? 261 PHE A CA  1 
ATOM   2091 C  C   . PHE A 1 261 ? 22.110  -18.082 -3.399  1.00 16.55  ? 261 PHE A C   1 
ATOM   2092 O  O   . PHE A 1 261 ? 21.423  -17.078 -3.651  1.00 19.58  ? 261 PHE A O   1 
ATOM   2093 C  CB  . PHE A 1 261 ? 23.120  -18.251 -1.069  1.00 14.74  ? 261 PHE A CB  1 
ATOM   2094 C  CG  . PHE A 1 261 ? 22.144  -17.304 -0.405  1.00 16.35  ? 261 PHE A CG  1 
ATOM   2095 C  CD1 . PHE A 1 261 ? 22.588  -16.134 0.179   1.00 14.49  ? 261 PHE A CD1 1 
ATOM   2096 C  CD2 . PHE A 1 261 ? 20.787  -17.606 -0.313  1.00 18.63  ? 261 PHE A CD2 1 
ATOM   2097 C  CE1 . PHE A 1 261 ? 21.696  -15.270 0.796   1.00 16.79  ? 261 PHE A CE1 1 
ATOM   2098 C  CE2 . PHE A 1 261 ? 19.893  -16.771 0.343   1.00 22.30  ? 261 PHE A CE2 1 
ATOM   2099 C  CZ  . PHE A 1 261 ? 20.332  -15.581 0.867   1.00 15.93  ? 261 PHE A CZ  1 
ATOM   2100 N  N   . SER A 1 262 ? 21.754  -19.326 -3.805  1.00 23.79  ? 262 SER A N   1 
ATOM   2101 C  CA  . SER A 1 262 ? 20.501  -19.605 -4.497  1.00 30.62  ? 262 SER A CA  1 
ATOM   2102 C  C   . SER A 1 262 ? 19.573  -20.453 -3.613  1.00 36.32  ? 262 SER A C   1 
ATOM   2103 O  O   . SER A 1 262 ? 19.324  -20.041 -2.482  1.00 44.19  ? 262 SER A O   1 
ATOM   2104 C  CB  . SER A 1 262 ? 20.747  -20.305 -5.814  1.00 38.68  ? 262 SER A CB  1 
ATOM   2105 O  OG  . SER A 1 262 ? 21.644  -21.397 -5.646  1.00 48.75  ? 262 SER A OG  1 
ATOM   2106 N  N   . LYS B 1 3   ? 1.267   18.041  -3.629  1.00 39.64  ? 3   LYS B N   1 
ATOM   2107 C  CA  . LYS B 1 3   ? 0.380   17.421  -2.580  1.00 35.98  ? 3   LYS B CA  1 
ATOM   2108 C  C   . LYS B 1 3   ? 0.812   15.982  -2.314  1.00 22.24  ? 3   LYS B C   1 
ATOM   2109 O  O   . LYS B 1 3   ? 1.596   15.413  -3.071  1.00 21.57  ? 3   LYS B O   1 
ATOM   2110 C  CB  . LYS B 1 3   ? -1.119  17.651  -2.798  1.00 41.77  ? 3   LYS B CB  1 
ATOM   2111 C  CG  . LYS B 1 3   ? -2.022  17.149  -1.662  1.00 36.63  ? 3   LYS B CG  1 
ATOM   2112 C  CD  . LYS B 1 3   ? -3.436  17.735  -1.667  1.00 51.11  ? 3   LYS B CD  1 
ATOM   2113 C  CE  . LYS B 1 3   ? -3.487  19.239  -1.849  1.00 62.09  ? 3   LYS B CE  1 
ATOM   2114 N  NZ  . LYS B 1 3   ? -4.880  19.735  -1.742  1.00 50.41  ? 3   LYS B NZ  1 
ATOM   2115 N  N   . TRP B 1 4   ? 0.384   15.469  -1.151  1.00 16.35  ? 4   TRP B N   1 
ATOM   2116 C  CA  . TRP B 1 4   ? 0.941   14.284  -0.554  1.00 13.00  ? 4   TRP B CA  1 
ATOM   2117 C  C   . TRP B 1 4   ? 0.662   13.090  -1.461  1.00 13.10  ? 4   TRP B C   1 
ATOM   2118 O  O   . TRP B 1 4   ? -0.333  13.061  -2.206  1.00 13.58  ? 4   TRP B O   1 
ATOM   2119 C  CB  . TRP B 1 4   ? 0.368   14.116  0.864   1.00 12.93  ? 4   TRP B CB  1 
ATOM   2120 C  CG  . TRP B 1 4   ? -1.105  13.818  1.004   1.00 10.50  ? 4   TRP B CG  1 
ATOM   2121 C  CD1 . TRP B 1 4   ? -2.123  14.700  1.214   1.00 11.20  ? 4   TRP B CD1 1 
ATOM   2122 C  CD2 . TRP B 1 4   ? -1.732  12.505  1.013   1.00 11.01  ? 4   TRP B CD2 1 
ATOM   2123 N  NE1 . TRP B 1 4   ? -3.295  14.049  1.365   1.00 11.40  ? 4   TRP B NE1 1 
ATOM   2124 C  CE2 . TRP B 1 4   ? -3.119  12.694  1.238   1.00 9.29   ? 4   TRP B CE2 1 
ATOM   2125 C  CE3 . TRP B 1 4   ? -1.269  11.202  0.854   1.00 10.21  ? 4   TRP B CE3 1 
ATOM   2126 C  CZ2 . TRP B 1 4   ? -4.037  11.644  1.357   1.00 12.57  ? 4   TRP B CZ2 1 
ATOM   2127 C  CZ3 . TRP B 1 4   ? -2.157  10.130  0.990   1.00 11.16  ? 4   TRP B CZ3 1 
ATOM   2128 C  CH2 . TRP B 1 4   ? -3.523  10.360  1.170   1.00 12.25  ? 4   TRP B CH2 1 
ATOM   2129 N  N   . THR B 1 5   ? 1.611   12.132  -1.459  1.00 10.83  ? 5   THR B N   1 
ATOM   2130 C  CA  . THR B 1 5   ? 1.499   10.924  -2.254  1.00 11.59  ? 5   THR B CA  1 
ATOM   2131 C  C   . THR B 1 5   ? 1.999   9.740   -1.437  1.00 9.56   ? 5   THR B C   1 
ATOM   2132 O  O   . THR B 1 5   ? 2.322   9.876   -0.234  1.00 10.05  ? 5   THR B O   1 
ATOM   2133 C  CB  . THR B 1 5   ? 2.428   11.059  -3.473  1.00 12.25  ? 5   THR B CB  1 
ATOM   2134 O  OG1 . THR B 1 5   ? 3.757   11.029  -2.940  1.00 13.14  ? 5   THR B OG1 1 
ATOM   2135 C  CG2 . THR B 1 5   ? 2.157   12.302  -4.291  1.00 14.52  ? 5   THR B CG2 1 
ATOM   2136 N  N   . TYR B 1 6   ? 2.061   8.587   -2.084  1.00 10.78  ? 6   TYR B N   1 
ATOM   2137 C  CA  . TYR B 1 6   ? 2.600   7.395   -1.440  1.00 9.45   ? 6   TYR B CA  1 
ATOM   2138 C  C   . TYR B 1 6   ? 3.992   7.092   -1.998  1.00 10.18  ? 6   TYR B C   1 
ATOM   2139 O  O   . TYR B 1 6   ? 4.518   6.008   -1.744  1.00 12.53  ? 6   TYR B O   1 
ATOM   2140 C  CB  . TYR B 1 6   ? 1.659   6.209   -1.626  1.00 9.59   ? 6   TYR B CB  1 
ATOM   2141 C  CG  . TYR B 1 6   ? 0.407   6.288   -0.788  1.00 9.27   ? 6   TYR B CG  1 
ATOM   2142 C  CD1 . TYR B 1 6   ? -0.752  6.913   -1.267  1.00 9.43   ? 6   TYR B CD1 1 
ATOM   2143 C  CD2 . TYR B 1 6   ? 0.392   5.729   0.510   1.00 9.80   ? 6   TYR B CD2 1 
ATOM   2144 C  CE1 . TYR B 1 6   ? -1.923  6.912   -0.530  1.00 9.48   ? 6   TYR B CE1 1 
ATOM   2145 C  CE2 . TYR B 1 6   ? -0.776  5.721   1.258   1.00 10.51  ? 6   TYR B CE2 1 
ATOM   2146 C  CZ  . TYR B 1 6   ? -1.937  6.340   0.741   1.00 10.20  ? 6   TYR B CZ  1 
ATOM   2147 O  OH  . TYR B 1 6   ? -3.083  6.360   1.457   1.00 10.59  ? 6   TYR B OH  1 
ATOM   2148 N  N   . PHE B 1 7   ? 4.549   7.969   -2.842  1.00 11.69  ? 7   PHE B N   1 
ATOM   2149 C  CA  . PHE B 1 7   ? 5.751   7.609   -3.581  1.00 13.57  ? 7   PHE B CA  1 
ATOM   2150 C  C   . PHE B 1 7   ? 6.505   8.871   -3.950  1.00 13.14  ? 7   PHE B C   1 
ATOM   2151 O  O   . PHE B 1 7   ? 5.952   9.727   -4.610  1.00 13.30  ? 7   PHE B O   1 
ATOM   2152 C  CB  . PHE B 1 7   ? 5.478   6.824   -4.877  1.00 20.80  ? 7   PHE B CB  1 
ATOM   2153 C  CG  . PHE B 1 7   ? 6.736   6.473   -5.634  1.00 21.56  ? 7   PHE B CG  1 
ATOM   2154 C  CD1 . PHE B 1 7   ? 7.651   5.535   -5.153  1.00 26.41  ? 7   PHE B CD1 1 
ATOM   2155 C  CD2 . PHE B 1 7   ? 7.071   7.188   -6.782  1.00 37.58  ? 7   PHE B CD2 1 
ATOM   2156 C  CE1 . PHE B 1 7   ? 8.826   5.275   -5.840  1.00 33.00  ? 7   PHE B CE1 1 
ATOM   2157 C  CE2 . PHE B 1 7   ? 8.234   6.900   -7.483  1.00 43.82  ? 7   PHE B CE2 1 
ATOM   2158 C  CZ  . PHE B 1 7   ? 9.111   5.951   -7.006  1.00 49.59  ? 7   PHE B CZ  1 
ATOM   2159 N  N   . GLY B 1 8   ? 7.791   8.953   -3.600  1.00 15.80  ? 8   GLY B N   1 
ATOM   2160 C  CA  . GLY B 1 8   ? 8.617   10.057  -4.070  1.00 16.69  ? 8   GLY B CA  1 
ATOM   2161 C  C   . GLY B 1 8   ? 8.695   11.160  -3.020  1.00 18.06  ? 8   GLY B C   1 
ATOM   2162 O  O   . GLY B 1 8   ? 8.521   10.939  -1.806  1.00 17.29  ? 8   GLY B O   1 
ATOM   2163 N  N   . PRO B 1 9   ? 9.112   12.364  -3.435  1.00 18.35  ? 9   PRO B N   1 
ATOM   2164 C  CA  . PRO B 1 9   ? 9.424   13.407  -2.467  1.00 21.08  ? 9   PRO B CA  1 
ATOM   2165 C  C   . PRO B 1 9   ? 8.297   13.792  -1.529  1.00 13.93  ? 9   PRO B C   1 
ATOM   2166 O  O   . PRO B 1 9   ? 8.624   14.314  -0.481  1.00 17.21  ? 9   PRO B O   1 
ATOM   2167 C  CB  . PRO B 1 9   ? 9.721   14.651  -3.293  1.00 24.63  ? 9   PRO B CB  1 
ATOM   2168 C  CG  . PRO B 1 9   ? 10.088  14.097  -4.626  1.00 27.71  ? 9   PRO B CG  1 
ATOM   2169 C  CD  . PRO B 1 9   ? 9.361   12.791  -4.826  1.00 21.88  ? 9   PRO B CD  1 
ATOM   2170 N  N   . ASP B 1 10  ? 7.025   13.540  -1.914  1.00 13.74  ? 10  ASP B N   1 
ATOM   2171 C  CA  . ASP B 1 10  ? 5.862   13.903  -1.098  1.00 12.90  ? 10  ASP B CA  1 
ATOM   2172 C  C   . ASP B 1 10  ? 5.255   12.662  -0.436  1.00 11.62  ? 10  ASP B C   1 
ATOM   2173 O  O   . ASP B 1 10  ? 4.143   12.757  0.056   1.00 11.22  ? 10  ASP B O   1 
ATOM   2174 C  CB  . ASP B 1 10  ? 4.853   14.693  -1.966  1.00 15.16  ? 10  ASP B CB  1 
ATOM   2175 C  CG  . ASP B 1 10  ? 5.445   15.965  -2.528  1.00 17.68  ? 10  ASP B CG  1 
ATOM   2176 O  OD1 . ASP B 1 10  ? 6.029   16.708  -1.737  1.00 26.23  ? 10  ASP B OD1 1 
ATOM   2177 O  OD2 . ASP B 1 10  ? 5.438   16.110  -3.762  1.00 24.97  ? 10  ASP B OD2 1 
ATOM   2178 N  N   . GLY B 1 11  ? 6.020   11.552  -0.379  1.00 9.76   ? 11  GLY B N   1 
ATOM   2179 C  CA  . GLY B 1 11  ? 5.586   10.282  0.176   1.00 9.38   ? 11  GLY B CA  1 
ATOM   2180 C  C   . GLY B 1 11  ? 5.632   10.320  1.697   1.00 9.29   ? 11  GLY B C   1 
ATOM   2181 O  O   . GLY B 1 11  ? 5.829   11.342  2.302   1.00 9.23   ? 11  GLY B O   1 
ATOM   2182 N  N   . GLU B 1 12  ? 5.366   9.152   2.305   1.00 9.13   ? 12  GLU B N   1 
ATOM   2183 C  CA  . GLU B 1 12  ? 4.919   9.111   3.682   1.00 7.64   ? 12  GLU B CA  1 
ATOM   2184 C  C   . GLU B 1 12  ? 5.976   9.581   4.663   1.00 8.20   ? 12  GLU B C   1 
ATOM   2185 O  O   . GLU B 1 12  ? 5.557   10.002  5.734   1.00 7.71   ? 12  GLU B O   1 
ATOM   2186 C  CB  . GLU B 1 12  ? 4.462   7.686   4.061   1.00 9.69   ? 12  GLU B CB  1 
ATOM   2187 C  CG  . GLU B 1 12  ? 5.547   6.629   4.127   1.00 9.19   ? 12  GLU B CG  1 
ATOM   2188 C  CD  . GLU B 1 12  ? 4.966   5.232   4.100   1.00 9.31   ? 12  GLU B CD  1 
ATOM   2189 O  OE1 . GLU B 1 12  ? 4.575   4.753   5.160   1.00 9.49   ? 12  GLU B OE1 1 
ATOM   2190 O  OE2 . GLU B 1 12  ? 4.884   4.718   2.972   1.00 9.58   ? 12  GLU B OE2 1 
ATOM   2191 N  N   . ASN B 1 13  ? 7.287   9.477   4.378   1.00 8.43   ? 13  ASN B N   1 
ATOM   2192 C  CA  . ASN B 1 13  ? 8.259   9.997   5.336   1.00 8.73   ? 13  ASN B CA  1 
ATOM   2193 C  C   . ASN B 1 13  ? 8.275   11.540  5.364   1.00 8.52   ? 13  ASN B C   1 
ATOM   2194 O  O   . ASN B 1 13  ? 8.858   12.053  6.318   1.00 11.87  ? 13  ASN B O   1 
ATOM   2195 C  CB  . ASN B 1 13  ? 9.648   9.440   5.035   1.00 8.87   ? 13  ASN B CB  1 
ATOM   2196 C  CG  . ASN B 1 13  ? 9.810   7.975   5.235   1.00 8.22   ? 13  ASN B CG  1 
ATOM   2197 O  OD1 . ASN B 1 13  ? 8.910   7.315   5.722   1.00 10.01  ? 13  ASN B OD1 1 
ATOM   2198 N  ND2 . ASN B 1 13  ? 11.009  7.536   4.912   1.00 9.82   ? 13  ASN B ND2 1 
ATOM   2199 N  N   . SER B 1 14  ? 7.599   12.153  4.404   1.00 8.16   ? 14  SER B N   1 
ATOM   2200 C  CA  . SER B 1 14  ? 7.520   13.610  4.348   1.00 9.06   ? 14  SER B CA  1 
ATOM   2201 C  C   . SER B 1 14  ? 6.142   14.124  4.788   1.00 9.07   ? 14  SER B C   1 
ATOM   2202 O  O   . SER B 1 14  ? 5.988   15.337  4.900   1.00 8.64   ? 14  SER B O   1 
ATOM   2203 C  CB  . SER B 1 14  ? 7.819   14.116  2.945   1.00 10.04  ? 14  SER B CB  1 
ATOM   2204 O  OG  . SER B 1 14  ? 9.162   13.846  2.654   1.00 10.15  ? 14  SER B OG  1 
ATOM   2205 N  N   . TRP B 1 15  ? 5.118   13.316  5.058   1.00 8.40   ? 15  TRP B N   1 
ATOM   2206 C  CA  . TRP B 1 15  ? 3.776   13.842  5.377   1.00 8.85   ? 15  TRP B CA  1 
ATOM   2207 C  C   . TRP B 1 15  ? 3.861   14.757  6.592   1.00 8.78   ? 15  TRP B C   1 
ATOM   2208 O  O   . TRP B 1 15  ? 3.117   15.733  6.655   1.00 9.99   ? 15  TRP B O   1 
ATOM   2209 C  CB  . TRP B 1 15  ? 2.856   12.693  5.709   1.00 9.36   ? 15  TRP B CB  1 
ATOM   2210 C  CG  . TRP B 1 15  ? 2.445   11.833  4.544   1.00 8.80   ? 15  TRP B CG  1 
ATOM   2211 C  CD1 . TRP B 1 15  ? 2.725   11.967  3.210   1.00 9.44   ? 15  TRP B CD1 1 
ATOM   2212 C  CD2 . TRP B 1 15  ? 1.731   10.555  4.668   1.00 10.39  ? 15  TRP B CD2 1 
ATOM   2213 N  NE1 . TRP B 1 15  ? 2.180   10.960  2.489   1.00 8.82   ? 15  TRP B NE1 1 
ATOM   2214 C  CE2 . TRP B 1 15  ? 1.530   10.102  3.341   1.00 9.32   ? 15  TRP B CE2 1 
ATOM   2215 C  CE3 . TRP B 1 15  ? 1.121   9.869   5.718   1.00 8.55   ? 15  TRP B CE3 1 
ATOM   2216 C  CZ2 . TRP B 1 15  ? 0.846   8.908   3.050   1.00 7.86   ? 15  TRP B CZ2 1 
ATOM   2217 C  CZ3 . TRP B 1 15  ? 0.451   8.661   5.440   1.00 7.93   ? 15  TRP B CZ3 1 
ATOM   2218 C  CH2 . TRP B 1 15  ? 0.309   8.225   4.118   1.00 8.46   ? 15  TRP B CH2 1 
ATOM   2219 N  N   . SER B 1 16  ? 4.679   14.430  7.584   1.00 9.76   ? 16  SER B N   1 
ATOM   2220 C  CA  . SER B 1 16  ? 4.764   15.174  8.845   1.00 10.34  ? 16  SER B CA  1 
ATOM   2221 C  C   . SER B 1 16  ? 5.212   16.641  8.620   1.00 9.01   ? 16  SER B C   1 
ATOM   2222 O  O   . SER B 1 16  ? 4.959   17.484  9.508   1.00 11.42  ? 16  SER B O   1 
ATOM   2223 C  CB  . SER B 1 16  ? 5.711   14.564  9.820   1.00 11.21  ? 16  SER B CB  1 
ATOM   2224 O  OG  . SER B 1 16  ? 7.013   14.682  9.340   1.00 14.89  ? 16  SER B OG  1 
ATOM   2225 N  N   . LYS B 1 17  ? 5.865   16.922  7.501   1.00 11.11  ? 17  LYS B N   1 
ATOM   2226 C  CA  . LYS B 1 17  ? 6.280   18.312  7.227   1.00 8.87   ? 17  LYS B CA  1 
ATOM   2227 C  C   . LYS B 1 17  ? 5.071   19.215  7.066   1.00 10.99  ? 17  LYS B C   1 
ATOM   2228 O  O   . LYS B 1 17  ? 5.217   20.406  7.343   1.00 12.43  ? 17  LYS B O   1 
ATOM   2229 C  CB  . LYS B 1 17  ? 7.057   18.332  5.924   1.00 9.74   ? 17  LYS B CB  1 
ATOM   2230 C  CG  . LYS B 1 17  ? 8.355   17.554  5.882   1.00 11.87  ? 17  LYS B CG  1 
ATOM   2231 C  CD  . LYS B 1 17  ? 8.967   17.604  4.474   1.00 12.26  ? 17  LYS B CD  1 
ATOM   2232 C  CE  . LYS B 1 17  ? 10.139  16.631  4.310   1.00 10.06  ? 17  LYS B CE  1 
ATOM   2233 N  NZ  . LYS B 1 17  ? 10.809  16.787  2.992   1.00 10.97  ? 17  LYS B NZ  1 
ATOM   2234 N  N   . LYS B 1 18  ? 3.947   18.777  6.543   1.00 11.25  ? 18  LYS B N   1 
ATOM   2235 C  CA  . LYS B 1 18  ? 2.742   19.569  6.357   1.00 11.10  ? 18  LYS B CA  1 
ATOM   2236 C  C   . LYS B 1 18  ? 1.636   19.196  7.311   1.00 11.30  ? 18  LYS B C   1 
ATOM   2237 O  O   . LYS B 1 18  ? 0.653   19.931  7.410   1.00 15.33  ? 18  LYS B O   1 
ATOM   2238 C  CB  . LYS B 1 18  ? 2.266   19.401  4.911   1.00 15.11  ? 18  LYS B CB  1 
ATOM   2239 C  CG  . LYS B 1 18  ? 3.127   20.103  3.853   1.00 20.93  ? 18  LYS B CG  1 
ATOM   2240 C  CD  . LYS B 1 18  ? 2.644   19.975  2.399   1.00 22.63  ? 18  LYS B CD  1 
ATOM   2241 C  CE  . LYS B 1 18  ? 3.453   20.737  1.356   1.00 28.84  ? 18  LYS B CE  1 
ATOM   2242 N  NZ  . LYS B 1 18  ? 2.932   20.454  -0.013  1.00 39.32  ? 18  LYS B NZ  1 
ATOM   2243 N  N   . TYR B 1 19  ? 1.650   17.973  7.816   1.00 10.02  ? 19  TYR B N   1 
ATOM   2244 C  CA  . TYR B 1 19  ? 0.564   17.421  8.592   1.00 11.15  ? 19  TYR B CA  1 
ATOM   2245 C  C   . TYR B 1 19  ? 1.194   16.968  9.900   1.00 12.68  ? 19  TYR B C   1 
ATOM   2246 O  O   . TYR B 1 19  ? 1.620   15.783  9.985   1.00 10.84  ? 19  TYR B O   1 
ATOM   2247 C  CB  . TYR B 1 19  ? -0.096  16.219  7.862   1.00 12.12  ? 19  TYR B CB  1 
ATOM   2248 C  CG  . TYR B 1 19  ? -0.699  16.636  6.527   1.00 12.16  ? 19  TYR B CG  1 
ATOM   2249 C  CD1 . TYR B 1 19  ? -1.948  17.259  6.455   1.00 12.17  ? 19  TYR B CD1 1 
ATOM   2250 C  CD2 . TYR B 1 19  ? 0.004   16.455  5.346   1.00 12.19  ? 19  TYR B CD2 1 
ATOM   2251 C  CE1 . TYR B 1 19  ? -2.444  17.675  5.230   1.00 14.21  ? 19  TYR B CE1 1 
ATOM   2252 C  CE2 . TYR B 1 19  ? -0.482  16.871  4.108   1.00 12.14  ? 19  TYR B CE2 1 
ATOM   2253 C  CZ  . TYR B 1 19  ? -1.739  17.434  4.052   1.00 13.11  ? 19  TYR B CZ  1 
ATOM   2254 O  OH  . TYR B 1 19  ? -2.217  17.875  2.845   1.00 18.31  ? 19  TYR B OH  1 
ATOM   2255 N  N   . PRO B 1 20  ? 1.295   17.786  10.955  1.00 12.18  ? 20  PRO B N   1 
ATOM   2256 C  CA  . PRO B 1 20  ? 2.046   17.411  12.154  1.00 13.25  ? 20  PRO B CA  1 
ATOM   2257 C  C   . PRO B 1 20  ? 1.615   16.147  12.894  1.00 11.33  ? 20  PRO B C   1 
ATOM   2258 O  O   . PRO B 1 20  ? 2.476   15.474  13.460  1.00 14.15  ? 20  PRO B O   1 
ATOM   2259 C  CB  . PRO B 1 20  ? 1.994   18.646  13.058  1.00 16.83  ? 20  PRO B CB  1 
ATOM   2260 C  CG  . PRO B 1 20  ? 1.545   19.744  12.181  1.00 18.73  ? 20  PRO B CG  1 
ATOM   2261 C  CD  . PRO B 1 20  ? 0.908   19.216  10.934  1.00 14.54  ? 20  PRO B CD  1 
ATOM   2262 N  N   . SER B 1 21  ? 0.331   15.822  12.859  1.00 10.41  ? 21  SER B N   1 
ATOM   2263 C  CA  . SER B 1 21  ? -0.129  14.631  13.524  1.00 11.32  ? 21  SER B CA  1 
ATOM   2264 C  C   . SER B 1 21  ? 0.537   13.387  12.904  1.00 10.76  ? 21  SER B C   1 
ATOM   2265 O  O   . SER B 1 21  ? 0.542   12.358  13.590  1.00 11.40  ? 21  SER B O   1 
ATOM   2266 C  CB  . SER B 1 21  ? -1.674  14.574  13.461  1.00 12.86  ? 21  SER B CB  1 
ATOM   2267 O  OG  . SER B 1 21  ? -2.272  15.583  14.286  1.00 15.02  ? 21  SER B OG  1 
ATOM   2268 N  N   . CYS B 1 22  ? 0.929   13.407  11.617  1.00 9.55   ? 22  CYS B N   1 
ATOM   2269 C  CA  . CYS B 1 22  ? 1.585   12.263  10.956  1.00 8.64   ? 22  CYS B CA  1 
ATOM   2270 C  C   . CYS B 1 22  ? 2.876   11.867  11.658  1.00 9.77   ? 22  CYS B C   1 
ATOM   2271 O  O   . CYS B 1 22  ? 3.357   10.771  11.470  1.00 10.82  ? 22  CYS B O   1 
ATOM   2272 C  CB  . CYS B 1 22  ? 1.728   12.419  9.422   1.00 9.22   ? 22  CYS B CB  1 
ATOM   2273 S  SG  . CYS B 1 22  ? 0.120   12.690  8.627   1.00 9.81   ? 22  CYS B SG  1 
ATOM   2274 N  N   . GLY B 1 23  ? 3.477   12.829  12.387  1.00 11.06  ? 23  GLY B N   1 
ATOM   2275 C  CA  . GLY B 1 23  ? 4.656   12.605  13.205  1.00 10.64  ? 23  GLY B CA  1 
ATOM   2276 C  C   . GLY B 1 23  ? 4.379   12.495  14.709  1.00 11.19  ? 23  GLY B C   1 
ATOM   2277 O  O   . GLY B 1 23  ? 5.324   12.481  15.534  1.00 13.58  ? 23  GLY B O   1 
ATOM   2278 N  N   . GLY B 1 24  ? 3.094   12.385  15.103  1.00 11.78  ? 24  GLY B N   1 
ATOM   2279 C  CA  . GLY B 1 24  ? 2.813   12.353  16.552  1.00 14.98  ? 24  GLY B CA  1 
ATOM   2280 C  C   . GLY B 1 24  ? 2.382   10.958  17.005  1.00 18.55  ? 24  GLY B C   1 
ATOM   2281 O  O   . GLY B 1 24  ? 2.877   9.987   16.435  1.00 18.98  ? 24  GLY B O   1 
ATOM   2282 N  N   . LEU B 1 25  ? 1.529   10.919  18.053  1.00 17.61  ? 25  LEU B N   1 
ATOM   2283 C  CA  . LEU B 1 25  ? 1.300   9.693   18.773  1.00 19.12  ? 25  LEU B CA  1 
ATOM   2284 C  C   . LEU B 1 25  ? 0.174   8.941   18.107  1.00 16.30  ? 25  LEU B C   1 
ATOM   2285 O  O   . LEU B 1 25  ? -0.548  9.484   17.295  1.00 14.52  ? 25  LEU B O   1 
ATOM   2286 C  CB  . LEU B 1 25  ? 0.932   10.012  20.232  1.00 30.61  ? 25  LEU B CB  1 
ATOM   2287 C  CG  . LEU B 1 25  ? 1.931   10.894  20.981  1.00 36.78  ? 25  LEU B CG  1 
ATOM   2288 C  CD1 . LEU B 1 25  ? 1.280   11.490  22.234  1.00 40.56  ? 25  LEU B CD1 1 
ATOM   2289 C  CD2 . LEU B 1 25  ? 3.167   10.076  21.348  1.00 45.74  ? 25  LEU B CD2 1 
ATOM   2290 N  N   . LEU B 1 26  ? 0.031   7.678   18.480  1.00 18.01  ? 26  LEU B N   1 
ATOM   2291 C  CA  . LEU B 1 26  ? -1.138  6.828   18.241  1.00 14.50  ? 26  LEU B CA  1 
ATOM   2292 C  C   . LEU B 1 26  ? -1.286  6.552   16.728  1.00 11.73  ? 26  LEU B C   1 
ATOM   2293 O  O   . LEU B 1 26  ? -2.414  6.420   16.236  1.00 11.54  ? 26  LEU B O   1 
ATOM   2294 C  CB  . LEU B 1 26  ? -2.426  7.479   18.801  1.00 22.53  ? 26  LEU B CB  1 
ATOM   2295 C  CG  . LEU B 1 26  ? -2.677  7.531   20.324  1.00 25.70  ? 26  LEU B CG  1 
ATOM   2296 C  CD1 . LEU B 1 26  ? -4.120  7.955   20.590  1.00 32.10  ? 26  LEU B CD1 1 
ATOM   2297 C  CD2 . LEU B 1 26  ? -2.503  6.173   20.937  1.00 22.07  ? 26  LEU B CD2 1 
ATOM   2298 N  N   . GLN B 1 27  ? -0.175  6.431   15.975  1.00 9.86   ? 27  GLN B N   1 
ATOM   2299 C  CA  . GLN B 1 27  ? -0.281  6.281   14.520  1.00 8.31   ? 27  GLN B CA  1 
ATOM   2300 C  C   . GLN B 1 27  ? -0.691  4.881   14.072  1.00 9.34   ? 27  GLN B C   1 
ATOM   2301 O  O   . GLN B 1 27  ? -0.268  3.866   14.654  1.00 9.94   ? 27  GLN B O   1 
ATOM   2302 C  CB  . GLN B 1 27  ? 0.957   6.760   13.790  1.00 9.62   ? 27  GLN B CB  1 
ATOM   2303 C  CG  . GLN B 1 27  ? 1.189   8.286   13.988  1.00 8.71   ? 27  GLN B CG  1 
ATOM   2304 C  CD  . GLN B 1 27  ? 0.102   9.099   13.323  1.00 8.75   ? 27  GLN B CD  1 
ATOM   2305 O  OE1 . GLN B 1 27  ? 0.103   9.240   12.092  1.00 9.14   ? 27  GLN B OE1 1 
ATOM   2306 N  NE2 . GLN B 1 27  ? -0.828  9.639   14.117  1.00 10.78  ? 27  GLN B NE2 1 
ATOM   2307 N  N   . SER B 1 28  ? -1.397  4.872   12.917  1.00 7.43   ? 28  SER B N   1 
ATOM   2308 C  CA  . SER B 1 28  ? -1.830  3.605   12.319  1.00 6.83   ? 28  SER B CA  1 
ATOM   2309 C  C   . SER B 1 28  ? -1.251  3.584   10.921  1.00 8.66   ? 28  SER B C   1 
ATOM   2310 O  O   . SER B 1 28  ? -0.927  4.626   10.346  1.00 7.48   ? 28  SER B O   1 
ATOM   2311 C  CB  . SER B 1 28  ? -3.321  3.574   12.255  1.00 7.20   ? 28  SER B CB  1 
ATOM   2312 O  OG  . SER B 1 28  ? -3.835  3.389   13.554  1.00 8.30   ? 28  SER B OG  1 
ATOM   2313 N  N   . PRO B 1 29  ? -1.129  2.444   10.198  1.00 7.78   ? 29  PRO B N   1 
ATOM   2314 C  CA  . PRO B 1 29  ? -1.497  1.091   10.707  1.00 7.64   ? 29  PRO B CA  1 
ATOM   2315 C  C   . PRO B 1 29  ? -0.339  0.473   11.494  1.00 7.28   ? 29  PRO B C   1 
ATOM   2316 O  O   . PRO B 1 29  ? 0.706   1.056   11.691  1.00 8.93   ? 29  PRO B O   1 
ATOM   2317 C  CB  . PRO B 1 29  ? -1.697  0.406   9.357   1.00 8.00   ? 29  PRO B CB  1 
ATOM   2318 C  CG  . PRO B 1 29  ? -0.589  0.928   8.437   1.00 8.90   ? 29  PRO B CG  1 
ATOM   2319 C  CD  . PRO B 1 29  ? -0.552  2.413   8.812   1.00 7.05   ? 29  PRO B CD  1 
ATOM   2320 N  N   . ILE B 1 30  ? -0.590  -0.758  11.992  1.00 7.30   ? 30  ILE B N   1 
ATOM   2321 C  CA  . ILE B 1 30  ? 0.420   -1.493  12.768  1.00 7.41   ? 30  ILE B CA  1 
ATOM   2322 C  C   . ILE B 1 30  ? 0.460   -2.979  12.323  1.00 7.35   ? 30  ILE B C   1 
ATOM   2323 O  O   . ILE B 1 30  ? -0.433  -3.450  11.640  1.00 8.23   ? 30  ILE B O   1 
ATOM   2324 C  CB  . ILE B 1 30  ? 0.042   -1.387  14.265  1.00 8.74   ? 30  ILE B CB  1 
ATOM   2325 C  CG1 . ILE B 1 30  ? -1.382  -1.900  14.574  1.00 8.39   ? 30  ILE B CG1 1 
ATOM   2326 C  CG2 . ILE B 1 30  ? 0.214   0.091   14.700  1.00 8.84   ? 30  ILE B CG2 1 
ATOM   2327 C  CD1 . ILE B 1 30  ? -1.664  -2.073  16.060  1.00 11.59  ? 30  ILE B CD1 1 
ATOM   2328 N  N   . ASP B 1 31  ? 1.564   -3.597  12.754  1.00 7.02   ? 31  ASP B N   1 
ATOM   2329 C  CA  . ASP B 1 31  ? 1.666   -5.056  12.586  1.00 8.18   ? 31  ASP B CA  1 
ATOM   2330 C  C   . ASP B 1 31  ? 1.055   -5.720  13.802  1.00 9.29   ? 31  ASP B C   1 
ATOM   2331 O  O   . ASP B 1 31  ? 1.453   -5.526  14.944  1.00 10.52  ? 31  ASP B O   1 
ATOM   2332 C  CB  . ASP B 1 31  ? 3.142   -5.421  12.471  1.00 8.35   ? 31  ASP B CB  1 
ATOM   2333 C  CG  . ASP B 1 31  ? 3.293   -6.926  12.342  1.00 9.73   ? 31  ASP B CG  1 
ATOM   2334 O  OD1 . ASP B 1 31  ? 2.866   -7.487  11.349  1.00 11.07  ? 31  ASP B OD1 1 
ATOM   2335 O  OD2 . ASP B 1 31  ? 3.929   -7.506  13.266  1.00 12.89  ? 31  ASP B OD2 1 
ATOM   2336 N  N   . LEU B 1 32  ? 0.118   -6.621  13.508  1.00 8.64   ? 32  LEU B N   1 
ATOM   2337 C  CA  . LEU B 1 32  ? -0.489  -7.434  14.544  1.00 10.57  ? 32  LEU B CA  1 
ATOM   2338 C  C   . LEU B 1 32  ? 0.305   -8.716  14.791  1.00 10.61  ? 32  LEU B C   1 
ATOM   2339 O  O   . LEU B 1 32  ? 0.392   -9.541  13.895  1.00 14.13  ? 32  LEU B O   1 
ATOM   2340 C  CB  . LEU B 1 32  ? -1.945  -7.715  14.119  1.00 10.45  ? 32  LEU B CB  1 
ATOM   2341 C  CG  . LEU B 1 32  ? -2.767  -6.478  13.746  1.00 11.65  ? 32  LEU B CG  1 
ATOM   2342 C  CD1 . LEU B 1 32  ? -4.078  -6.840  13.052  1.00 13.35  ? 32  LEU B CD1 1 
ATOM   2343 C  CD2 . LEU B 1 32  ? -2.981  -5.555  14.961  1.00 16.03  ? 32  LEU B CD2 1 
ATOM   2344 N  N   . HIS B 1 33  ? 0.928   -8.819  15.982  1.00 11.40  ? 33  HIS B N   1 
ATOM   2345 C  CA  . HIS B 1 33  ? 1.797   -9.937  16.264  1.00 11.34  ? 33  HIS B CA  1 
ATOM   2346 C  C   . HIS B 1 33  ? 1.727   -10.217 17.749  1.00 10.00  ? 33  HIS B C   1 
ATOM   2347 O  O   . HIS B 1 33  ? 1.277   -9.403  18.544  1.00 11.11  ? 33  HIS B O   1 
ATOM   2348 C  CB  . HIS B 1 33  ? 3.263   -9.660  15.843  1.00 11.54  ? 33  HIS B CB  1 
ATOM   2349 C  CG  . HIS B 1 33  ? 3.889   -8.513  16.584  1.00 12.68  ? 33  HIS B CG  1 
ATOM   2350 N  ND1 . HIS B 1 33  ? 3.693   -7.214  16.172  1.00 16.58  ? 33  HIS B ND1 1 
ATOM   2351 C  CD2 . HIS B 1 33  ? 4.709   -8.425  17.664  1.00 12.39  ? 33  HIS B CD2 1 
ATOM   2352 C  CE1 . HIS B 1 33  ? 4.366   -6.409  16.946  1.00 17.79  ? 33  HIS B CE1 1 
ATOM   2353 N  NE2 . HIS B 1 33  ? 4.989   -7.080  17.856  1.00 12.66  ? 33  HIS B NE2 1 
ATOM   2354 N  N   . SER B 1 34  ? 2.087   -11.468 18.101  1.00 11.81  ? 34  SER B N   1 
ATOM   2355 C  CA  . SER B 1 34  ? 1.701   -12.075 19.361  1.00 11.55  ? 34  SER B CA  1 
ATOM   2356 C  C   . SER B 1 34  ? 2.095   -11.201 20.547  1.00 12.86  ? 34  SER B C   1 
ATOM   2357 O  O   . SER B 1 34  ? 1.327   -11.136 21.501  1.00 12.77  ? 34  SER B O   1 
ATOM   2358 C  CB  . SER B 1 34  ? 2.215   -13.485 19.462  1.00 14.70  ? 34  SER B CB  1 
ATOM   2359 O  OG  . SER B 1 34  ? 3.622   -13.456 19.493  1.00 19.85  ? 34  SER B OG  1 
ATOM   2360 N  N   . ASP B 1 35  ? 3.268   -10.558 20.512  1.00 12.54  ? 35  ASP B N   1 
ATOM   2361 C  CA  . ASP B 1 35  ? 3.808   -9.921  21.709  1.00 13.47  ? 35  ASP B CA  1 
ATOM   2362 C  C   . ASP B 1 35  ? 2.955   -8.743  22.166  1.00 12.21  ? 35  ASP B C   1 
ATOM   2363 O  O   . ASP B 1 35  ? 3.025   -8.390  23.344  1.00 16.60  ? 35  ASP B O   1 
ATOM   2364 C  CB  . ASP B 1 35  ? 5.234   -9.397  21.516  1.00 16.93  ? 35  ASP B CB  1 
ATOM   2365 C  CG  . ASP B 1 35  ? 6.154   -10.397 20.871  1.00 15.66  ? 35  ASP B CG  1 
ATOM   2366 O  OD1 . ASP B 1 35  ? 5.875   -10.777 19.671  1.00 15.50  ? 35  ASP B OD1 1 
ATOM   2367 O  OD2 . ASP B 1 35  ? 7.194   -10.681 21.496  1.00 16.85  ? 35  ASP B OD2 1 
ATOM   2368 N  N   . ILE B 1 36  ? 2.119   -8.193  21.261  1.00 12.15  ? 36  ILE B N   1 
ATOM   2369 C  CA  . ILE B 1 36  ? 1.370   -7.013  21.658  1.00 12.15  ? 36  ILE B CA  1 
ATOM   2370 C  C   . ILE B 1 36  ? -0.137  -7.306  21.743  1.00 10.29  ? 36  ILE B C   1 
ATOM   2371 O  O   . ILE B 1 36  ? -0.915  -6.426  21.987  1.00 13.71  ? 36  ILE B O   1 
ATOM   2372 C  CB  . ILE B 1 36  ? 1.693   -5.842  20.709  1.00 15.55  ? 36  ILE B CB  1 
ATOM   2373 C  CG1 . ILE B 1 36  ? 1.538   -6.258  19.249  1.00 16.49  ? 36  ILE B CG1 1 
ATOM   2374 C  CG2 . ILE B 1 36  ? 3.130   -5.409  20.923  1.00 19.22  ? 36  ILE B CG2 1 
ATOM   2375 C  CD1 . ILE B 1 36  ? 0.290   -5.986  18.631  1.00 23.14  ? 36  ILE B CD1 1 
ATOM   2376 N  N   . LEU B 1 37  ? -0.583  -8.586  21.602  1.00 10.86  ? 37  LEU B N   1 
ATOM   2377 C  CA  . LEU B 1 37  ? -2.003  -8.934  21.670  1.00 11.10  ? 37  LEU B CA  1 
ATOM   2378 C  C   . LEU B 1 37  ? -2.374  -9.308  23.116  1.00 13.53  ? 37  LEU B C   1 
ATOM   2379 O  O   . LEU B 1 37  ? -1.569  -9.890  23.859  1.00 18.36  ? 37  LEU B O   1 
ATOM   2380 C  CB  . LEU B 1 37  ? -2.302  -10.155 20.770  1.00 11.96  ? 37  LEU B CB  1 
ATOM   2381 C  CG  . LEU B 1 37  ? -1.986  -9.935  19.294  1.00 10.96  ? 37  LEU B CG  1 
ATOM   2382 C  CD1 . LEU B 1 37  ? -2.201  -11.190 18.449  1.00 17.11  ? 37  LEU B CD1 1 
ATOM   2383 C  CD2 . LEU B 1 37  ? -2.728  -8.751  18.749  1.00 13.54  ? 37  LEU B CD2 1 
ATOM   2384 N  N   . GLN B 1 38  ? -3.590  -8.957  23.515  1.00 12.01  ? 38  GLN B N   1 
ATOM   2385 C  CA  . GLN B 1 38  ? -4.123  -9.310  24.813  1.00 14.06  ? 38  GLN B CA  1 
ATOM   2386 C  C   . GLN B 1 38  ? -5.615  -9.562  24.683  1.00 13.63  ? 38  GLN B C   1 
ATOM   2387 O  O   . GLN B 1 38  ? -6.380  -8.713  24.236  1.00 12.11  ? 38  GLN B O   1 
ATOM   2388 C  CB  . GLN B 1 38  ? -3.904  -8.178  25.815  1.00 19.60  ? 38  GLN B CB  1 
ATOM   2389 C  CG  . GLN B 1 38  ? -4.117  -8.626  27.266  1.00 23.32  ? 38  GLN B CG  1 
ATOM   2390 C  CD  . GLN B 1 38  ? -3.607  -7.644  28.299  1.00 27.82  ? 38  GLN B CD  1 
ATOM   2391 O  OE1 . GLN B 1 38  ? -2.406  -7.547  28.558  1.00 41.02  ? 38  GLN B OE1 1 
ATOM   2392 N  NE2 . GLN B 1 38  ? -4.528  -6.932  28.923  1.00 32.16  ? 38  GLN B NE2 1 
ATOM   2393 N  N   . TYR B 1 39  ? -6.052  -10.761 25.061  1.00 12.96  ? 39  TYR B N   1 
ATOM   2394 C  CA  . TYR B 1 39  ? -7.467  -11.093 25.078  1.00 11.81  ? 39  TYR B CA  1 
ATOM   2395 C  C   . TYR B 1 39  ? -8.213  -10.196 26.054  1.00 11.66  ? 39  TYR B C   1 
ATOM   2396 O  O   . TYR B 1 39  ? -7.746  -9.929  27.160  1.00 12.77  ? 39  TYR B O   1 
ATOM   2397 C  CB  . TYR B 1 39  ? -7.640  -12.582 25.419  1.00 11.59  ? 39  TYR B CB  1 
ATOM   2398 C  CG  . TYR B 1 39  ? -9.076  -13.044 25.591  1.00 12.29  ? 39  TYR B CG  1 
ATOM   2399 C  CD1 . TYR B 1 39  ? -10.013 -12.890 24.574  1.00 11.95  ? 39  TYR B CD1 1 
ATOM   2400 C  CD2 . TYR B 1 39  ? -9.556  -13.476 26.822  1.00 13.50  ? 39  TYR B CD2 1 
ATOM   2401 C  CE1 . TYR B 1 39  ? -11.341 -13.304 24.716  1.00 14.21  ? 39  TYR B CE1 1 
ATOM   2402 C  CE2 . TYR B 1 39  ? -10.881 -13.840 26.982  1.00 13.96  ? 39  TYR B CE2 1 
ATOM   2403 C  CZ  . TYR B 1 39  ? -11.777 -13.804 25.931  1.00 14.10  ? 39  TYR B CZ  1 
ATOM   2404 O  OH  . TYR B 1 39  ? -13.090 -14.164 26.095  1.00 15.04  ? 39  TYR B OH  1 
ATOM   2405 N  N   . ASP B 1 40  ? -9.387  -9.736  25.596  1.00 11.46  ? 40  ASP B N   1 
ATOM   2406 C  CA  . ASP B 1 40  ? -10.257 -8.882  26.385  1.00 10.91  ? 40  ASP B CA  1 
ATOM   2407 C  C   . ASP B 1 40  ? -11.674 -9.470  26.264  1.00 12.31  ? 40  ASP B C   1 
ATOM   2408 O  O   . ASP B 1 40  ? -12.318 -9.266  25.237  1.00 11.71  ? 40  ASP B O   1 
ATOM   2409 C  CB  . ASP B 1 40  ? -10.031 -7.408  26.022  1.00 13.53  ? 40  ASP B CB  1 
ATOM   2410 C  CG  . ASP B 1 40  ? -10.929 -6.474  26.826  1.00 16.54  ? 40  ASP B CG  1 
ATOM   2411 O  OD1 . ASP B 1 40  ? -11.733 -6.944  27.685  1.00 15.59  ? 40  ASP B OD1 1 
ATOM   2412 O  OD2 . ASP B 1 40  ? -10.758 -5.262  26.602  1.00 18.76  ? 40  ASP B OD2 1 
ATOM   2413 N  N   . ALA B 1 41  ? -12.162 -10.189 27.287  1.00 12.67  ? 41  ALA B N   1 
ATOM   2414 C  CA  . ALA B 1 41  ? -13.506 -10.764 27.245  1.00 12.06  ? 41  ALA B CA  1 
ATOM   2415 C  C   . ALA B 1 41  ? -14.670 -9.738  27.148  1.00 12.85  ? 41  ALA B C   1 
ATOM   2416 O  O   . ALA B 1 41  ? -15.825 -10.138 26.887  1.00 16.42  ? 41  ALA B O   1 
ATOM   2417 C  CB  . ALA B 1 41  ? -13.679 -11.630 28.508  1.00 14.23  ? 41  ALA B CB  1 
ATOM   2418 N  N   A SER B 1 42  ? -14.391 -8.445  27.413  0.50 14.82  ? 42  SER B N   1 
ATOM   2419 N  N   B SER B 1 42  ? -14.402 -8.443  27.399  0.50 14.41  ? 42  SER B N   1 
ATOM   2420 C  CA  A SER B 1 42  ? -15.396 -7.374  27.352  0.50 14.97  ? 42  SER B CA  1 
ATOM   2421 C  CA  B SER B 1 42  ? -15.424 -7.388  27.328  0.50 14.49  ? 42  SER B CA  1 
ATOM   2422 C  C   A SER B 1 42  ? -15.669 -6.926  25.913  0.50 16.15  ? 42  SER B C   1 
ATOM   2423 C  C   B SER B 1 42  ? -15.718 -6.975  25.888  0.50 14.60  ? 42  SER B C   1 
ATOM   2424 O  O   A SER B 1 42  ? -16.573 -6.121  25.710  0.50 18.01  ? 42  SER B O   1 
ATOM   2425 O  O   B SER B 1 42  ? -16.611 -6.158  25.681  0.50 18.86  ? 42  SER B O   1 
ATOM   2426 C  CB  A SER B 1 42  ? -15.074 -6.227  28.283  0.50 16.60  ? 42  SER B CB  1 
ATOM   2427 C  CB  B SER B 1 42  ? -15.030 -6.208  28.118  0.50 13.36  ? 42  SER B CB  1 
ATOM   2428 O  OG  A SER B 1 42  ? -13.987 -5.397  27.833  0.50 14.82  ? 42  SER B OG  1 
ATOM   2429 O  OG  B SER B 1 42  ? -14.885 -6.576  29.471  0.50 15.55  ? 42  SER B OG  1 
ATOM   2430 N  N   . LEU B 1 43  ? -14.886 -7.421  24.940  1.00 13.78  ? 43  LEU B N   1 
ATOM   2431 C  CA  . LEU B 1 43  ? -15.059 -7.064  23.520  1.00 13.40  ? 43  LEU B CA  1 
ATOM   2432 C  C   . LEU B 1 43  ? -16.154 -7.932  22.929  1.00 13.64  ? 43  LEU B C   1 
ATOM   2433 O  O   . LEU B 1 43  ? -15.887 -8.987  22.354  1.00 15.05  ? 43  LEU B O   1 
ATOM   2434 C  CB  . LEU B 1 43  ? -13.738 -7.202  22.770  1.00 10.98  ? 43  LEU B CB  1 
ATOM   2435 C  CG  . LEU B 1 43  ? -12.623 -6.218  23.168  1.00 11.92  ? 43  LEU B CG  1 
ATOM   2436 C  CD1 . LEU B 1 43  ? -11.365 -6.556  22.400  1.00 13.23  ? 43  LEU B CD1 1 
ATOM   2437 C  CD2 . LEU B 1 43  ? -13.101 -4.780  22.953  1.00 11.12  ? 43  LEU B CD2 1 
ATOM   2438 N  N   . THR B 1 44  ? -17.397 -7.487  23.119  1.00 16.01  ? 44  THR B N   1 
ATOM   2439 C  CA  . THR B 1 44  ? -18.586 -8.194  22.701  1.00 16.81  ? 44  THR B CA  1 
ATOM   2440 C  C   . THR B 1 44  ? -18.894 -7.931  21.234  1.00 15.01  ? 44  THR B C   1 
ATOM   2441 O  O   . THR B 1 44  ? -18.282 -7.061  20.614  1.00 15.69  ? 44  THR B O   1 
ATOM   2442 C  CB  . THR B 1 44  ? -19.733 -7.834  23.661  1.00 19.93  ? 44  THR B CB  1 
ATOM   2443 O  OG1 . THR B 1 44  ? -19.739 -6.392  23.658  1.00 25.37  ? 44  THR B OG1 1 
ATOM   2444 C  CG2 . THR B 1 44  ? -19.517 -8.373  25.064  1.00 21.78  ? 44  THR B CG2 1 
ATOM   2445 N  N   . PRO B 1 45  ? -19.827 -8.668  20.593  1.00 14.44  ? 45  PRO B N   1 
ATOM   2446 C  CA  . PRO B 1 45  ? -19.974 -8.554  19.143  1.00 15.74  ? 45  PRO B CA  1 
ATOM   2447 C  C   . PRO B 1 45  ? -20.571 -7.201  18.777  1.00 13.84  ? 45  PRO B C   1 
ATOM   2448 O  O   . PRO B 1 45  ? -21.436 -6.679  19.505  1.00 17.86  ? 45  PRO B O   1 
ATOM   2449 C  CB  . PRO B 1 45  ? -20.930 -9.731  18.776  1.00 19.62  ? 45  PRO B CB  1 
ATOM   2450 C  CG  . PRO B 1 45  ? -20.695 -10.713 19.917  1.00 22.13  ? 45  PRO B CG  1 
ATOM   2451 C  CD  . PRO B 1 45  ? -20.543 -9.824  21.131  1.00 18.24  ? 45  PRO B CD  1 
ATOM   2452 N  N   . LEU B 1 46  ? -20.135 -6.675  17.627  1.00 13.43  ? 46  LEU B N   1 
ATOM   2453 C  CA  . LEU B 1 46  ? -20.802 -5.532  16.993  1.00 14.20  ? 46  LEU B CA  1 
ATOM   2454 C  C   . LEU B 1 46  ? -22.045 -5.977  16.220  1.00 13.94  ? 46  LEU B C   1 
ATOM   2455 O  O   . LEU B 1 46  ? -22.078 -7.071  15.653  1.00 15.92  ? 46  LEU B O   1 
ATOM   2456 C  CB  . LEU B 1 46  ? -19.829 -4.775  16.073  1.00 12.11  ? 46  LEU B CB  1 
ATOM   2457 C  CG  . LEU B 1 46  ? -18.580 -4.222  16.766  1.00 15.75  ? 46  LEU B CG  1 
ATOM   2458 C  CD1 . LEU B 1 46  ? -17.607 -3.688  15.738  1.00 16.86  ? 46  LEU B CD1 1 
ATOM   2459 C  CD2 . LEU B 1 46  ? -18.971 -3.176  17.815  1.00 23.61  ? 46  LEU B CD2 1 
ATOM   2460 N  N   . GLU B 1 47  ? -23.015 -5.068  16.123  1.00 12.43  ? 47  GLU B N   1 
ATOM   2461 C  CA  . GLU B 1 47  ? -24.193 -5.261  15.304  1.00 14.64  ? 47  GLU B CA  1 
ATOM   2462 C  C   . GLU B 1 47  ? -24.210 -4.205  14.182  1.00 15.39  ? 47  GLU B C   1 
ATOM   2463 O  O   . GLU B 1 47  ? -23.984 -2.997  14.367  1.00 16.16  ? 47  GLU B O   1 
ATOM   2464 C  CB  . GLU B 1 47  ? -25.471 -5.223  16.163  1.00 16.17  ? 47  GLU B CB  1 
ATOM   2465 C  CG  . GLU B 1 47  ? -25.478 -6.239  17.298  1.00 21.68  ? 47  GLU B CG  1 
ATOM   2466 C  CD  . GLU B 1 47  ? -26.541 -6.062  18.376  1.00 29.47  ? 47  GLU B CD  1 
ATOM   2467 O  OE1 . GLU B 1 47  ? -27.628 -5.627  18.051  1.00 31.73  ? 47  GLU B OE1 1 
ATOM   2468 O  OE2 . GLU B 1 47  ? -26.263 -6.360  19.558  1.00 38.37  ? 47  GLU B OE2 1 
ATOM   2469 N  N   . PHE B 1 48  ? -24.466 -4.678  12.979  1.00 12.63  ? 48  PHE B N   1 
ATOM   2470 C  CA  . PHE B 1 48  ? -24.388 -3.822  11.790  1.00 12.07  ? 48  PHE B CA  1 
ATOM   2471 C  C   . PHE B 1 48  ? -25.807 -3.456  11.363  1.00 13.06  ? 48  PHE B C   1 
ATOM   2472 O  O   . PHE B 1 48  ? -26.507 -4.340  10.846  1.00 17.19  ? 48  PHE B O   1 
ATOM   2473 C  CB  . PHE B 1 48  ? -23.557 -4.487  10.687  1.00 14.30  ? 48  PHE B CB  1 
ATOM   2474 C  CG  . PHE B 1 48  ? -22.274 -5.032  11.258  1.00 14.32  ? 48  PHE B CG  1 
ATOM   2475 C  CD1 . PHE B 1 48  ? -21.244 -4.190  11.642  1.00 12.81  ? 48  PHE B CD1 1 
ATOM   2476 C  CD2 . PHE B 1 48  ? -22.088 -6.410  11.423  1.00 14.74  ? 48  PHE B CD2 1 
ATOM   2477 C  CE1 . PHE B 1 48  ? -20.086 -4.687  12.255  1.00 13.17  ? 48  PHE B CE1 1 
ATOM   2478 C  CE2 . PHE B 1 48  ? -20.918 -6.921  11.984  1.00 15.55  ? 48  PHE B CE2 1 
ATOM   2479 C  CZ  . PHE B 1 48  ? -19.915 -6.054  12.365  1.00 14.44  ? 48  PHE B CZ  1 
ATOM   2480 N  N   . GLN B 1 49  ? -26.186 -2.181  11.571  1.00 12.78  ? 49  GLN B N   1 
ATOM   2481 C  CA  . GLN B 1 49  ? -27.559 -1.751  11.361  1.00 11.98  ? 49  GLN B CA  1 
ATOM   2482 C  C   . GLN B 1 49  ? -27.662 -0.913  10.101  1.00 11.33  ? 49  GLN B C   1 
ATOM   2483 O  O   . GLN B 1 49  ? -26.877 0.020   9.891   1.00 12.60  ? 49  GLN B O   1 
ATOM   2484 C  CB  . GLN B 1 49  ? -28.051 -0.952  12.577  1.00 13.21  ? 49  GLN B CB  1 
ATOM   2485 C  CG  . GLN B 1 49  ? -28.002 -1.749  13.891  1.00 17.11  ? 49  GLN B CG  1 
ATOM   2486 C  CD  . GLN B 1 49  ? -28.797 -3.038  13.835  1.00 18.45  ? 49  GLN B CD  1 
ATOM   2487 O  OE1 . GLN B 1 49  ? -28.242 -4.125  13.977  1.00 23.67  ? 49  GLN B OE1 1 
ATOM   2488 N  NE2 . GLN B 1 49  ? -30.091 -2.920  13.598  1.00 23.58  ? 49  GLN B NE2 1 
ATOM   2489 N  N   . GLY B 1 50  ? -28.708 -1.148  9.308   1.00 12.11  ? 50  GLY B N   1 
ATOM   2490 C  CA  . GLY B 1 50  ? -28.936 -0.354  8.084   1.00 12.14  ? 50  GLY B CA  1 
ATOM   2491 C  C   . GLY B 1 50  ? -27.812 -0.513  7.053   1.00 11.30  ? 50  GLY B C   1 
ATOM   2492 O  O   . GLY B 1 50  ? -27.615 0.342   6.187   1.00 12.79  ? 50  GLY B O   1 
ATOM   2493 N  N   . TYR B 1 51  ? -27.026 -1.610  7.153   1.00 10.52  ? 51  TYR B N   1 
ATOM   2494 C  CA  . TYR B 1 51  ? -26.036 -1.951  6.132   1.00 11.00  ? 51  TYR B CA  1 
ATOM   2495 C  C   . TYR B 1 51  ? -26.660 -2.416  4.806   1.00 10.48  ? 51  TYR B C   1 
ATOM   2496 O  O   . TYR B 1 51  ? -25.990 -2.390  3.789   1.00 10.54  ? 51  TYR B O   1 
ATOM   2497 C  CB  . TYR B 1 51  ? -25.036 -3.015  6.650   1.00 11.21  ? 51  TYR B CB  1 
ATOM   2498 C  CG  . TYR B 1 51  ? -23.886 -2.488  7.474   1.00 9.62   ? 51  TYR B CG  1 
ATOM   2499 C  CD1 . TYR B 1 51  ? -24.064 -1.534  8.476   1.00 11.15  ? 51  TYR B CD1 1 
ATOM   2500 C  CD2 . TYR B 1 51  ? -22.590 -2.948  7.256   1.00 10.66  ? 51  TYR B CD2 1 
ATOM   2501 C  CE1 . TYR B 1 51  ? -22.995 -1.024  9.188   1.00 11.33  ? 51  TYR B CE1 1 
ATOM   2502 C  CE2 . TYR B 1 51  ? -21.500 -2.440  7.963   1.00 10.34  ? 51  TYR B CE2 1 
ATOM   2503 C  CZ  . TYR B 1 51  ? -21.700 -1.435  8.902   1.00 10.65  ? 51  TYR B CZ  1 
ATOM   2504 O  OH  . TYR B 1 51  ? -20.617 -0.976  9.598   1.00 12.04  ? 51  TYR B OH  1 
ATOM   2505 N  N   . ASN B 1 52  ? -27.907 -2.908  4.816   1.00 10.60  ? 52  ASN B N   1 
ATOM   2506 C  CA  . ASN B 1 52  ? -28.513 -3.430  3.604   1.00 12.68  ? 52  ASN B CA  1 
ATOM   2507 C  C   . ASN B 1 52  ? -29.142 -2.252  2.838   1.00 12.03  ? 52  ASN B C   1 
ATOM   2508 O  O   . ASN B 1 52  ? -30.290 -1.960  3.001   1.00 13.96  ? 52  ASN B O   1 
ATOM   2509 C  CB  . ASN B 1 52  ? -29.629 -4.381  4.049   1.00 14.19  ? 52  ASN B CB  1 
ATOM   2510 C  CG  . ASN B 1 52  ? -30.217 -5.145  2.890   1.00 18.80  ? 52  ASN B CG  1 
ATOM   2511 O  OD1 . ASN B 1 52  ? -29.698 -5.078  1.776   1.00 24.53  ? 52  ASN B OD1 1 
ATOM   2512 N  ND2 . ASN B 1 52  ? -31.331 -5.831  3.125   1.00 20.47  ? 52  ASN B ND2 1 
ATOM   2513 N  N   . LEU B 1 53  ? -28.310 -1.518  2.110   1.00 11.79  ? 53  LEU B N   1 
ATOM   2514 C  CA  . LEU B 1 53  ? -28.744 -0.290  1.442   1.00 12.01  ? 53  LEU B CA  1 
ATOM   2515 C  C   . LEU B 1 53  ? -29.669 -0.600  0.272   1.00 10.77  ? 53  LEU B C   1 
ATOM   2516 O  O   . LEU B 1 53  ? -29.487 -1.630  -0.390  1.00 12.67  ? 53  LEU B O   1 
ATOM   2517 C  CB  . LEU B 1 53  ? -27.509 0.386   0.856   1.00 10.90  ? 53  LEU B CB  1 
ATOM   2518 C  CG  . LEU B 1 53  ? -26.382 0.739   1.808   1.00 12.78  ? 53  LEU B CG  1 
ATOM   2519 C  CD1 . LEU B 1 53  ? -25.312 1.462   1.016   1.00 14.87  ? 53  LEU B CD1 1 
ATOM   2520 C  CD2 . LEU B 1 53  ? -26.866 1.581   2.997   1.00 16.33  ? 53  LEU B CD2 1 
ATOM   2521 N  N   . SER B 1 54  ? -30.775 0.131   0.160   1.00 11.86  ? 54  SER B N   1 
ATOM   2522 C  CA  . SER B 1 54  ? -31.746 -0.128  -0.880  1.00 12.79  ? 54  SER B CA  1 
ATOM   2523 C  C   . SER B 1 54  ? -31.137 -0.176  -2.280  1.00 12.08  ? 54  SER B C   1 
ATOM   2524 O  O   . SER B 1 54  ? -30.504 0.762   -2.712  1.00 12.83  ? 54  SER B O   1 
ATOM   2525 C  CB  . SER B 1 54  ? -32.832 0.885   -0.856  1.00 13.11  ? 54  SER B CB  1 
ATOM   2526 O  OG  . SER B 1 54  ? -33.702 0.664   -1.952  1.00 15.75  ? 54  SER B OG  1 
ATOM   2527 N  N   . ALA B 1 55  ? -31.427 -1.246  -3.038  1.00 14.03  ? 55  ALA B N   1 
ATOM   2528 C  CA  . ALA B 1 55  ? -30.928 -1.403  -4.396  1.00 15.98  ? 55  ALA B CA  1 
ATOM   2529 C  C   . ALA B 1 55  ? -31.552 -0.367  -5.317  1.00 14.67  ? 55  ALA B C   1 
ATOM   2530 O  O   . ALA B 1 55  ? -31.035 -0.164  -6.436  1.00 21.43  ? 55  ALA B O   1 
ATOM   2531 C  CB  . ALA B 1 55  ? -31.208 -2.808  -4.903  1.00 22.39  ? 55  ALA B CB  1 
ATOM   2532 N  N   . ASN B 1 56  ? -32.631 0.310   -4.845  1.00 15.34  ? 56  ASN B N   1 
ATOM   2533 C  CA  . ASN B 1 56  ? -33.306 1.316   -5.664  1.00 16.39  ? 56  ASN B CA  1 
ATOM   2534 C  C   . ASN B 1 56  ? -32.769 2.712   -5.402  1.00 15.51  ? 56  ASN B C   1 
ATOM   2535 O  O   . ASN B 1 56  ? -33.156 3.643   -6.092  1.00 22.79  ? 56  ASN B O   1 
ATOM   2536 C  CB  . ASN B 1 56  ? -34.827 1.244   -5.524  1.00 16.75  ? 56  ASN B CB  1 
ATOM   2537 C  CG  . ASN B 1 56  ? -35.391 -0.109  -5.871  1.00 20.70  ? 56  ASN B CG  1 
ATOM   2538 O  OD1 . ASN B 1 56  ? -34.779 -0.894  -6.596  1.00 24.92  ? 56  ASN B OD1 1 
ATOM   2539 N  ND2 . ASN B 1 56  ? -36.552 -0.379  -5.311  1.00 31.06  ? 56  ASN B ND2 1 
ATOM   2540 N  N   . LYS B 1 57  ? -31.904 2.840   -4.412  1.00 15.09  ? 57  LYS B N   1 
ATOM   2541 C  CA  . LYS B 1 57  ? -31.220 4.100   -4.141  1.00 13.63  ? 57  LYS B CA  1 
ATOM   2542 C  C   . LYS B 1 57  ? -29.789 4.028   -4.704  1.00 12.60  ? 57  LYS B C   1 
ATOM   2543 O  O   . LYS B 1 57  ? -29.275 2.946   -5.066  1.00 14.38  ? 57  LYS B O   1 
ATOM   2544 C  CB  . LYS B 1 57  ? -31.205 4.326   -2.624  1.00 16.93  ? 57  LYS B CB  1 
ATOM   2545 C  CG  . LYS B 1 57  ? -32.529 4.740   -1.981  1.00 17.54  ? 57  LYS B CG  1 
ATOM   2546 C  CD  . LYS B 1 57  ? -32.418 5.036   -0.472  1.00 27.47  ? 57  LYS B CD  1 
ATOM   2547 C  CE  . LYS B 1 57  ? -33.416 6.052   0.058   1.00 34.17  ? 57  LYS B CE  1 
ATOM   2548 N  NZ  . LYS B 1 57  ? -33.319 6.235   1.534   1.00 33.87  ? 57  LYS B NZ  1 
ATOM   2549 N  N   A GLN B 1 58  ? -29.179 5.211   -4.774  0.50 13.64  ? 58  GLN B N   1 
ATOM   2550 N  N   B GLN B 1 58  ? -29.154 5.183   -4.851  0.50 13.13  ? 58  GLN B N   1 
ATOM   2551 C  CA  A GLN B 1 58  ? -27.877 5.427   -5.383  0.50 12.98  ? 58  GLN B CA  1 
ATOM   2552 C  CA  B GLN B 1 58  ? -27.812 5.221   -5.410  0.50 12.54  ? 58  GLN B CA  1 
ATOM   2553 C  C   A GLN B 1 58  ? -26.931 6.070   -4.362  0.50 10.45  ? 58  GLN B C   1 
ATOM   2554 C  C   B GLN B 1 58  ? -26.916 6.101   -4.538  0.50 10.49  ? 58  GLN B C   1 
ATOM   2555 O  O   A GLN B 1 58  ? -27.365 6.856   -3.493  0.50 12.26  ? 58  GLN B O   1 
ATOM   2556 O  O   B GLN B 1 58  ? -27.361 7.137   -4.019  0.50 14.12  ? 58  GLN B O   1 
ATOM   2557 C  CB  A GLN B 1 58  ? -27.998 6.241   -6.693  0.50 16.18  ? 58  GLN B CB  1 
ATOM   2558 C  CB  B GLN B 1 58  ? -27.808 5.817   -6.826  0.50 15.25  ? 58  GLN B CB  1 
ATOM   2559 C  CG  A GLN B 1 58  ? -28.219 7.737   -6.531  0.50 19.74  ? 58  GLN B CG  1 
ATOM   2560 C  CG  B GLN B 1 58  ? -28.671 5.050   -7.817  0.50 16.54  ? 58  GLN B CG  1 
ATOM   2561 C  CD  A GLN B 1 58  ? -28.470 8.415   -7.860  0.50 23.86  ? 58  GLN B CD  1 
ATOM   2562 C  CD  B GLN B 1 58  ? -28.825 5.721   -9.160  0.50 19.65  ? 58  GLN B CD  1 
ATOM   2563 O  OE1 A GLN B 1 58  ? -28.465 7.780   -8.912  0.50 26.43  ? 58  GLN B OE1 1 
ATOM   2564 O  OE1 B GLN B 1 58  ? -29.817 6.383   -9.453  0.50 27.09  ? 58  GLN B OE1 1 
ATOM   2565 N  NE2 A GLN B 1 58  ? -28.677 9.723   -7.828  0.50 25.28  ? 58  GLN B NE2 1 
ATOM   2566 N  NE2 B GLN B 1 58  ? -27.857 5.492   -10.010 0.50 16.93  ? 58  GLN B NE2 1 
ATOM   2567 N  N   . PHE B 1 59  ? -25.639 5.692   -4.444  1.00 12.95  ? 59  PHE B N   1 
ATOM   2568 C  CA  . PHE B 1 59  ? -24.659 6.210   -3.498  1.00 11.16  ? 59  PHE B CA  1 
ATOM   2569 C  C   . PHE B 1 59  ? -23.455 6.727   -4.279  1.00 10.21  ? 59  PHE B C   1 
ATOM   2570 O  O   . PHE B 1 59  ? -23.058 6.148   -5.294  1.00 11.79  ? 59  PHE B O   1 
ATOM   2571 C  CB  . PHE B 1 59  ? -24.280 5.151   -2.453  1.00 10.84  ? 59  PHE B CB  1 
ATOM   2572 C  CG  . PHE B 1 59  ? -25.531 4.762   -1.707  1.00 11.26  ? 59  PHE B CG  1 
ATOM   2573 C  CD1 . PHE B 1 59  ? -26.389 3.749   -2.185  1.00 10.62  ? 59  PHE B CD1 1 
ATOM   2574 C  CD2 . PHE B 1 59  ? -25.901 5.482   -0.585  1.00 12.03  ? 59  PHE B CD2 1 
ATOM   2575 C  CE1 . PHE B 1 59  ? -27.587 3.492   -1.520  1.00 11.25  ? 59  PHE B CE1 1 
ATOM   2576 C  CE2 . PHE B 1 59  ? -27.109 5.220   0.058   1.00 14.99  ? 59  PHE B CE2 1 
ATOM   2577 C  CZ  . PHE B 1 59  ? -27.946 4.235   -0.416  1.00 12.46  ? 59  PHE B CZ  1 
ATOM   2578 N  N   . LEU B 1 60  ? -23.021 7.939   -3.898  1.00 10.96  ? 60  LEU B N   1 
ATOM   2579 C  CA  . LEU B 1 60  ? -21.959 8.590   -4.633  1.00 12.39  ? 60  LEU B CA  1 
ATOM   2580 C  C   . LEU B 1 60  ? -20.575 8.020   -4.370  1.00 10.25  ? 60  LEU B C   1 
ATOM   2581 O  O   . LEU B 1 60  ? -20.090 7.983   -3.245  1.00 12.15  ? 60  LEU B O   1 
ATOM   2582 C  CB  . LEU B 1 60  ? -21.935 10.051  -4.211  1.00 13.37  ? 60  LEU B CB  1 
ATOM   2583 C  CG  . LEU B 1 60  ? -21.129 10.995  -5.102  1.00 16.92  ? 60  LEU B CG  1 
ATOM   2584 C  CD1 . LEU B 1 60  ? -21.807 11.156  -6.472  1.00 20.49  ? 60  LEU B CD1 1 
ATOM   2585 C  CD2 . LEU B 1 60  ? -20.993 12.374  -4.442  1.00 17.14  ? 60  LEU B CD2 1 
ATOM   2586 N  N   . LEU B 1 61  ? -19.895 7.717   -5.464  1.00 11.31  ? 61  LEU B N   1 
ATOM   2587 C  CA  . LEU B 1 61  ? -18.518 7.261   -5.505  1.00 12.16  ? 61  LEU B CA  1 
ATOM   2588 C  C   . LEU B 1 61  ? -17.694 8.426   -6.047  1.00 11.18  ? 61  LEU B C   1 
ATOM   2589 O  O   . LEU B 1 61  ? -18.055 8.998   -7.074  1.00 13.57  ? 61  LEU B O   1 
ATOM   2590 C  CB  . LEU B 1 61  ? -18.505 6.054   -6.451  1.00 14.13  ? 61  LEU B CB  1 
ATOM   2591 C  CG  . LEU B 1 61  ? -17.206 5.270   -6.591  1.00 12.59  ? 61  LEU B CG  1 
ATOM   2592 C  CD1 . LEU B 1 61  ? -16.928 4.497   -5.293  1.00 15.00  ? 61  LEU B CD1 1 
ATOM   2593 C  CD2 . LEU B 1 61  ? -17.279 4.326   -7.784  1.00 13.64  ? 61  LEU B CD2 1 
ATOM   2594 N  N   A THR B 1 62  ? -16.526 8.668   -5.448  0.50 13.37  ? 62  THR B N   1 
ATOM   2595 N  N   B THR B 1 62  ? -16.615 8.814   -5.356  0.50 11.11  ? 62  THR B N   1 
ATOM   2596 C  CA  A THR B 1 62  ? -15.767 9.864   -5.765  0.50 13.43  ? 62  THR B CA  1 
ATOM   2597 C  CA  B THR B 1 62  ? -15.811 9.947   -5.794  0.50 10.22  ? 62  THR B CA  1 
ATOM   2598 C  C   A THR B 1 62  ? -14.263 9.553   -5.796  0.50 15.06  ? 62  THR B C   1 
ATOM   2599 C  C   B THR B 1 62  ? -14.318 9.569   -5.818  0.50 12.56  ? 62  THR B C   1 
ATOM   2600 O  O   A THR B 1 62  ? -13.758 8.771   -4.987  0.50 13.38  ? 62  THR B O   1 
ATOM   2601 O  O   B THR B 1 62  ? -13.876 8.751   -5.008  0.50 10.97  ? 62  THR B O   1 
ATOM   2602 C  CB  A THR B 1 62  ? -16.118 10.948  -4.737  0.50 20.80  ? 62  THR B CB  1 
ATOM   2603 C  CB  B THR B 1 62  ? -16.007 11.144  -4.845  0.50 12.34  ? 62  THR B CB  1 
ATOM   2604 O  OG1 A THR B 1 62  ? -17.508 11.273  -4.822  0.50 25.25  ? 62  THR B OG1 1 
ATOM   2605 O  OG1 B THR B 1 62  ? -15.492 10.750  -3.566  0.50 9.75   ? 62  THR B OG1 1 
ATOM   2606 C  CG2 A THR B 1 62  ? -15.276 12.199  -4.850  0.50 23.55  ? 62  THR B CG2 1 
ATOM   2607 C  CG2 B THR B 1 62  ? -17.428 11.665  -4.703  0.50 13.27  ? 62  THR B CG2 1 
ATOM   2608 N  N   . ASN B 1 63  ? -13.539 10.198  -6.723  1.00 12.74  ? 63  ASN B N   1 
ATOM   2609 C  CA  . ASN B 1 63  ? -12.085 10.150  -6.747  1.00 11.58  ? 63  ASN B CA  1 
ATOM   2610 C  C   . ASN B 1 63  ? -11.533 11.545  -6.462  1.00 10.78  ? 63  ASN B C   1 
ATOM   2611 O  O   . ASN B 1 63  ? -11.657 12.425  -7.292  1.00 14.65  ? 63  ASN B O   1 
ATOM   2612 C  CB  . ASN B 1 63  ? -11.592 9.627   -8.115  1.00 12.85  ? 63  ASN B CB  1 
ATOM   2613 C  CG  . ASN B 1 63  ? -10.088 9.455   -8.215  1.00 11.94  ? 63  ASN B CG  1 
ATOM   2614 O  OD1 . ASN B 1 63  ? -9.353  9.922   -7.351  1.00 13.45  ? 63  ASN B OD1 1 
ATOM   2615 N  ND2 . ASN B 1 63  ? -9.599  8.734   -9.228  1.00 12.50  ? 63  ASN B ND2 1 
ATOM   2616 N  N   . ASN B 1 64  ? -10.966 11.761  -5.254  1.00 12.13  ? 64  ASN B N   1 
ATOM   2617 C  CA  . ASN B 1 64  ? -10.406 13.056  -4.896  1.00 11.43  ? 64  ASN B CA  1 
ATOM   2618 C  C   . ASN B 1 64  ? -8.908  13.110  -5.194  1.00 14.91  ? 64  ASN B C   1 
ATOM   2619 O  O   . ASN B 1 64  ? -8.246  14.106  -4.850  1.00 16.92  ? 64  ASN B O   1 
ATOM   2620 C  CB  . ASN B 1 64  ? -10.629 13.401  -3.422  1.00 13.48  ? 64  ASN B CB  1 
ATOM   2621 C  CG  . ASN B 1 64  ? -9.911  12.503  -2.450  1.00 12.98  ? 64  ASN B CG  1 
ATOM   2622 O  OD1 . ASN B 1 64  ? -9.117  11.639  -2.874  1.00 14.13  ? 64  ASN B OD1 1 
ATOM   2623 N  ND2 . ASN B 1 64  ? -10.186 12.664  -1.155  1.00 16.94  ? 64  ASN B ND2 1 
ATOM   2624 N  N   . GLY B 1 65  ? -8.354  12.073  -5.876  1.00 12.73  ? 65  GLY B N   1 
ATOM   2625 C  CA  . GLY B 1 65  ? -6.925  12.035  -6.157  1.00 16.89  ? 65  GLY B CA  1 
ATOM   2626 C  C   . GLY B 1 65  ? -6.060  11.258  -5.162  1.00 13.79  ? 65  GLY B C   1 
ATOM   2627 O  O   . GLY B 1 65  ? -4.850  11.008  -5.408  1.00 15.21  ? 65  GLY B O   1 
ATOM   2628 N  N   . HIS B 1 66  ? -6.657  10.966  -4.001  1.00 15.84  ? 66  HIS B N   1 
ATOM   2629 C  CA  . HIS B 1 66  ? -5.946  10.304  -2.913  1.00 12.26  ? 66  HIS B CA  1 
ATOM   2630 C  C   . HIS B 1 66  ? -6.672  9.025   -2.556  1.00 13.56  ? 66  HIS B C   1 
ATOM   2631 O  O   . HIS B 1 66  ? -6.016  7.980   -2.443  1.00 14.22  ? 66  HIS B O   1 
ATOM   2632 C  CB  . HIS B 1 66  ? -5.773  11.182  -1.656  1.00 13.70  ? 66  HIS B CB  1 
ATOM   2633 C  CG  . HIS B 1 66  ? -4.941  12.385  -1.864  1.00 12.53  ? 66  HIS B CG  1 
ATOM   2634 N  ND1 . HIS B 1 66  ? -3.558  12.338  -2.006  1.00 14.36  ? 66  HIS B ND1 1 
ATOM   2635 C  CD2 . HIS B 1 66  ? -5.289  13.669  -1.828  1.00 12.53  ? 66  HIS B CD2 1 
ATOM   2636 C  CE1 . HIS B 1 66  ? -3.092  13.560  -2.081  1.00 14.87  ? 66  HIS B CE1 1 
ATOM   2637 N  NE2 . HIS B 1 66  ? -4.146  14.375  -2.012  1.00 16.28  ? 66  HIS B NE2 1 
ATOM   2638 N  N   . SER B 1 67  ? -8.015  9.088   -2.453  1.00 12.90  ? 67  SER B N   1 
ATOM   2639 C  CA  . SER B 1 67  ? -8.760  7.919   -2.041  1.00 13.06  ? 67  SER B CA  1 
ATOM   2640 C  C   . SER B 1 67  ? -10.057 7.941   -2.814  1.00 15.16  ? 67  SER B C   1 
ATOM   2641 O  O   . SER B 1 67  ? -10.709 9.005   -2.860  1.00 20.07  ? 67  SER B O   1 
ATOM   2642 C  CB  . SER B 1 67  ? -8.990  7.966   -0.526  1.00 13.91  ? 67  SER B CB  1 
ATOM   2643 O  OG  . SER B 1 67  ? -9.763  6.848   -0.057  1.00 15.57  ? 67  SER B OG  1 
ATOM   2644 N  N   . VAL B 1 68  ? -10.408 6.855   -3.459  1.00 12.69  ? 68  VAL B N   1 
ATOM   2645 C  CA  . VAL B 1 68  ? -11.750 6.723   -4.025  1.00 10.43  ? 68  VAL B CA  1 
ATOM   2646 C  C   . VAL B 1 68  ? -12.684 6.199   -2.940  1.00 12.83  ? 68  VAL B C   1 
ATOM   2647 O  O   . VAL B 1 68  ? -12.506 5.095   -2.389  1.00 13.87  ? 68  VAL B O   1 
ATOM   2648 C  CB  . VAL B 1 68  ? -11.725 5.773   -5.227  1.00 10.40  ? 68  VAL B CB  1 
ATOM   2649 C  CG1 . VAL B 1 68  ? -13.115 5.407   -5.705  1.00 13.53  ? 68  VAL B CG1 1 
ATOM   2650 C  CG2 . VAL B 1 68  ? -10.864 6.362   -6.346  1.00 16.38  ? 68  VAL B CG2 1 
ATOM   2651 N  N   . LYS B 1 69  ? -13.705 7.002   -2.681  1.00 10.80  ? 69  LYS B N   1 
ATOM   2652 C  CA  . LYS B 1 69  ? -14.624 6.763   -1.554  1.00 8.88   ? 69  LYS B CA  1 
ATOM   2653 C  C   . LYS B 1 69  ? -16.054 6.511   -2.043  1.00 9.62   ? 69  LYS B C   1 
ATOM   2654 O  O   . LYS B 1 69  ? -16.492 7.109   -3.020  1.00 11.98  ? 69  LYS B O   1 
ATOM   2655 C  CB  . LYS B 1 69  ? -14.710 8.077   -0.752  1.00 12.50  ? 69  LYS B CB  1 
ATOM   2656 C  CG  . LYS B 1 69  ? -13.442 8.580   -0.126  1.00 10.82  ? 69  LYS B CG  1 
ATOM   2657 C  CD  . LYS B 1 69  ? -13.668 9.915   0.581   1.00 11.13  ? 69  LYS B CD  1 
ATOM   2658 C  CE  . LYS B 1 69  ? -12.377 10.544  1.054   1.00 10.88  ? 69  LYS B CE  1 
ATOM   2659 N  NZ  . LYS B 1 69  ? -12.600 11.840  1.714   1.00 12.46  ? 69  LYS B NZ  1 
ATOM   2660 N  N   . LEU B 1 70  ? -16.718 5.460   -1.492  1.00 8.32   ? 70  LEU B N   1 
ATOM   2661 C  CA  . LEU B 1 70  ? -18.162 5.307   -1.623  1.00 7.68   ? 70  LEU B CA  1 
ATOM   2662 C  C   . LEU B 1 70  ? -18.822 5.936   -0.426  1.00 9.21   ? 70  LEU B C   1 
ATOM   2663 O  O   . LEU B 1 70  ? -18.603 5.496   0.678   1.00 9.36   ? 70  LEU B O   1 
ATOM   2664 C  CB  . LEU B 1 70  ? -18.528 3.812   -1.731  1.00 9.40   ? 70  LEU B CB  1 
ATOM   2665 C  CG  . LEU B 1 70  ? -20.032 3.582   -1.852  1.00 8.46   ? 70  LEU B CG  1 
ATOM   2666 C  CD1 . LEU B 1 70  ? -20.592 4.154   -3.186  1.00 11.66  ? 70  LEU B CD1 1 
ATOM   2667 C  CD2 . LEU B 1 70  ? -20.363 2.100   -1.683  1.00 11.78  ? 70  LEU B CD2 1 
ATOM   2668 N  N   A ASN B 1 71  ? -19.636 6.988   -0.660  0.50 10.44  ? 71  ASN B N   1 
ATOM   2669 N  N   B ASN B 1 71  ? -19.561 7.012   -0.658  0.50 10.61  ? 71  ASN B N   1 
ATOM   2670 C  CA  A ASN B 1 71  ? -20.343 7.664   0.415   0.50 10.61  ? 71  ASN B CA  1 
ATOM   2671 C  CA  B ASN B 1 71  ? -20.262 7.667   0.428   0.50 10.81  ? 71  ASN B CA  1 
ATOM   2672 C  C   A ASN B 1 71  ? -21.508 6.802   0.874   0.50 11.89  ? 71  ASN B C   1 
ATOM   2673 C  C   B ASN B 1 71  ? -21.430 6.797   0.878   0.50 12.05  ? 71  ASN B C   1 
ATOM   2674 O  O   A ASN B 1 71  ? -22.160 6.107   0.086   0.50 14.09  ? 71  ASN B O   1 
ATOM   2675 O  O   B ASN B 1 71  ? -22.057 6.098   0.078   0.50 14.20  ? 71  ASN B O   1 
ATOM   2676 C  CB  A ASN B 1 71  ? -20.923 9.015   -0.040  0.50 12.88  ? 71  ASN B CB  1 
ATOM   2677 C  CB  B ASN B 1 71  ? -20.820 9.022   -0.032  0.50 13.25  ? 71  ASN B CB  1 
ATOM   2678 C  CG  A ASN B 1 71  ? -19.962 10.191  -0.040  0.50 17.07  ? 71  ASN B CG  1 
ATOM   2679 C  CG  B ASN B 1 71  ? -19.777 10.099  -0.267  0.50 20.77  ? 71  ASN B CG  1 
ATOM   2680 O  OD1 A ASN B 1 71  ? -18.825 10.098  0.405   0.50 20.68  ? 71  ASN B OD1 1 
ATOM   2681 O  OD1 B ASN B 1 71  ? -18.920 10.001  -1.146  0.50 24.47  ? 71  ASN B OD1 1 
ATOM   2682 N  ND2 A ASN B 1 71  ? -20.443 11.345  -0.495  0.50 21.26  ? 71  ASN B ND2 1 
ATOM   2683 N  ND2 B ASN B 1 71  ? -19.854 11.162  0.515   0.50 30.38  ? 71  ASN B ND2 1 
ATOM   2684 N  N   . LEU B 1 72  ? -21.677 6.816   2.185   1.00 9.84   ? 72  LEU B N   1 
ATOM   2685 C  CA  . LEU B 1 72  ? -22.650 5.986   2.890   1.00 8.96   ? 72  LEU B CA  1 
ATOM   2686 C  C   . LEU B 1 72  ? -23.578 6.882   3.711   1.00 11.61  ? 72  LEU B C   1 
ATOM   2687 O  O   . LEU B 1 72  ? -23.203 8.010   4.114   1.00 12.87  ? 72  LEU B O   1 
ATOM   2688 C  CB  . LEU B 1 72  ? -21.887 5.025   3.814   1.00 10.70  ? 72  LEU B CB  1 
ATOM   2689 C  CG  . LEU B 1 72  ? -20.963 4.040   3.103   1.00 9.70   ? 72  LEU B CG  1 
ATOM   2690 C  CD1 . LEU B 1 72  ? -20.042 3.340   4.119   1.00 11.02  ? 72  LEU B CD1 1 
ATOM   2691 C  CD2 . LEU B 1 72  ? -21.769 3.029   2.309   1.00 11.03  ? 72  LEU B CD2 1 
ATOM   2692 N  N   . PRO B 1 73  ? -24.837 6.411   3.888   1.00 10.06  ? 73  PRO B N   1 
ATOM   2693 C  CA  . PRO B 1 73  ? -25.852 7.209   4.563   1.00 11.34  ? 73  PRO B CA  1 
ATOM   2694 C  C   . PRO B 1 73  ? -25.703 7.107   6.075   1.00 12.79  ? 73  PRO B C   1 
ATOM   2695 O  O   . PRO B 1 73  ? -25.283 6.086   6.643   1.00 13.92  ? 73  PRO B O   1 
ATOM   2696 C  CB  . PRO B 1 73  ? -27.123 6.561   4.008   1.00 12.81  ? 73  PRO B CB  1 
ATOM   2697 C  CG  . PRO B 1 73  ? -26.782 5.062   3.935   1.00 12.37  ? 73  PRO B CG  1 
ATOM   2698 C  CD  . PRO B 1 73  ? -25.368 5.118   3.372   1.00 12.53  ? 73  PRO B CD  1 
ATOM   2699 N  N   A SER B 1 74  ? -26.042 8.188   6.783   0.50 14.92  ? 74  SER B N   1 
ATOM   2700 N  N   B SER B 1 74  ? -26.034 8.219   6.729   0.50 15.28  ? 74  SER B N   1 
ATOM   2701 C  CA  A SER B 1 74  ? -25.923 8.199   8.241   0.50 14.41  ? 74  SER B CA  1 
ATOM   2702 C  CA  B SER B 1 74  ? -26.014 8.306   8.181   0.50 14.81  ? 74  SER B CA  1 
ATOM   2703 C  C   A SER B 1 74  ? -26.962 7.341   8.974   0.50 14.53  ? 74  SER B C   1 
ATOM   2704 C  C   B SER B 1 74  ? -26.850 7.242   8.899   0.50 14.55  ? 74  SER B C   1 
ATOM   2705 O  O   A SER B 1 74  ? -26.988 7.363   10.202  0.50 15.89  ? 74  SER B O   1 
ATOM   2706 O  O   B SER B 1 74  ? -26.576 6.975   10.062  0.50 13.41  ? 74  SER B O   1 
ATOM   2707 C  CB  A SER B 1 74  ? -25.980 9.610   8.764   0.50 15.57  ? 74  SER B CB  1 
ATOM   2708 C  CB  B SER B 1 74  ? -26.334 9.703   8.644   0.50 18.62  ? 74  SER B CB  1 
ATOM   2709 O  OG  A SER B 1 74  ? -27.279 10.116  8.553   0.50 15.11  ? 74  SER B OG  1 
ATOM   2710 O  OG  B SER B 1 74  ? -25.141 10.466  8.611   0.50 24.66  ? 74  SER B OG  1 
ATOM   2711 N  N   . ASP B 1 75  ? -27.910 6.722   8.256   1.00 14.39  ? 75  ASP B N   1 
ATOM   2712 C  CA  . ASP B 1 75  ? -28.810 5.766   8.910   1.00 15.72  ? 75  ASP B CA  1 
ATOM   2713 C  C   . ASP B 1 75  ? -28.099 4.428   9.101   1.00 14.18  ? 75  ASP B C   1 
ATOM   2714 O  O   . ASP B 1 75  ? -28.472 3.659   9.956   1.00 17.39  ? 75  ASP B O   1 
ATOM   2715 C  CB  . ASP B 1 75  ? -30.167 5.533   8.229   1.00 17.19  ? 75  ASP B CB  1 
ATOM   2716 C  CG  . ASP B 1 75  ? -30.278 5.505   6.710   1.00 30.19  ? 75  ASP B CG  1 
ATOM   2717 O  OD1 . ASP B 1 75  ? -29.314 5.127   6.048   1.00 30.79  ? 75  ASP B OD1 1 
ATOM   2718 O  OD2 . ASP B 1 75  ? -31.406 5.834   6.200   1.00 48.17  ? 75  ASP B OD2 1 
ATOM   2719 N  N   . MET B 1 76  ? -27.007 4.212   8.347   1.00 12.93  ? 76  MET B N   1 
ATOM   2720 C  CA  . MET B 1 76  ? -26.172 3.028   8.517   1.00 10.86  ? 76  MET B CA  1 
ATOM   2721 C  C   . MET B 1 76  ? -25.273 3.221   9.737   1.00 11.15  ? 76  MET B C   1 
ATOM   2722 O  O   . MET B 1 76  ? -24.629 4.260   9.851   1.00 13.34  ? 76  MET B O   1 
ATOM   2723 C  CB  . MET B 1 76  ? -25.365 2.831   7.236   1.00 11.50  ? 76  MET B CB  1 
ATOM   2724 C  CG  . MET B 1 76  ? -24.333 1.708   7.291   1.00 11.55  ? 76  MET B CG  1 
ATOM   2725 S  SD  . MET B 1 76  ? -23.612 1.581   5.637   1.00 11.35  ? 76  MET B SD  1 
ATOM   2726 C  CE  . MET B 1 76  ? -22.117 0.688   6.067   1.00 10.86  ? 76  MET B CE  1 
ATOM   2727 N  N   . HIS B 1 77  ? -25.264 2.249   10.646  1.00 11.62  ? 77  HIS B N   1 
ATOM   2728 C  CA  . HIS B 1 77  ? -24.515 2.496   11.882  1.00 11.96  ? 77  HIS B CA  1 
ATOM   2729 C  C   . HIS B 1 77  ? -24.077 1.197   12.558  1.00 9.70   ? 77  HIS B C   1 
ATOM   2730 O  O   . HIS B 1 77  ? -24.628 0.103   12.265  1.00 13.76  ? 77  HIS B O   1 
ATOM   2731 C  CB  . HIS B 1 77  ? -25.297 3.395   12.833  1.00 13.03  ? 77  HIS B CB  1 
ATOM   2732 C  CG  . HIS B 1 77  ? -26.495 2.734   13.408  1.00 14.73  ? 77  HIS B CG  1 
ATOM   2733 N  ND1 . HIS B 1 77  ? -27.711 2.740   12.753  1.00 15.43  ? 77  HIS B ND1 1 
ATOM   2734 C  CD2 . HIS B 1 77  ? -26.694 2.136   14.601  1.00 16.59  ? 77  HIS B CD2 1 
ATOM   2735 C  CE1 . HIS B 1 77  ? -28.610 2.172   13.544  1.00 16.45  ? 77  HIS B CE1 1 
ATOM   2736 N  NE2 . HIS B 1 77  ? -28.019 1.771   14.678  1.00 19.79  ? 77  HIS B NE2 1 
ATOM   2737 N  N   . ILE B 1 78  ? -23.109 1.310   13.456  1.00 10.35  ? 78  ILE B N   1 
ATOM   2738 C  CA  . ILE B 1 78  ? -22.689 0.190   14.308  1.00 11.28  ? 78  ILE B CA  1 
ATOM   2739 C  C   . ILE B 1 78  ? -23.389 0.332   15.637  1.00 14.11  ? 78  ILE B C   1 
ATOM   2740 O  O   . ILE B 1 78  ? -23.386 1.438   16.221  1.00 15.18  ? 78  ILE B O   1 
ATOM   2741 C  CB  . ILE B 1 78  ? -21.170 0.265   14.553  1.00 13.80  ? 78  ILE B CB  1 
ATOM   2742 C  CG1 . ILE B 1 78  ? -20.363 0.055   13.276  1.00 17.33  ? 78  ILE B CG1 1 
ATOM   2743 C  CG2 . ILE B 1 78  ? -20.768 -0.699  15.663  1.00 16.33  ? 78  ILE B CG2 1 
ATOM   2744 C  CD1 . ILE B 1 78  ? -18.921 0.548   13.426  1.00 14.90  ? 78  ILE B CD1 1 
ATOM   2745 N  N   . GLN B 1 79  ? -23.975 -0.758  16.112  1.00 14.48  ? 79  GLN B N   1 
ATOM   2746 C  CA  . GLN B 1 79  ? -24.492 -0.905  17.480  1.00 15.85  ? 79  GLN B CA  1 
ATOM   2747 C  C   . GLN B 1 79  ? -23.458 -1.735  18.280  1.00 17.85  ? 79  GLN B C   1 
ATOM   2748 O  O   . GLN B 1 79  ? -22.913 -2.724  17.786  1.00 18.00  ? 79  GLN B O   1 
ATOM   2749 C  CB  . GLN B 1 79  ? -25.909 -1.508  17.405  1.00 21.80  ? 79  GLN B CB  1 
ATOM   2750 C  CG  . GLN B 1 79  ? -26.514 -2.006  18.714  1.00 25.79  ? 79  GLN B CG  1 
ATOM   2751 C  CD  . GLN B 1 79  ? -26.912 -0.918  19.691  1.00 34.07  ? 79  GLN B CD  1 
ATOM   2752 O  OE1 . GLN B 1 79  ? -27.360 0.181   19.325  1.00 31.89  ? 79  GLN B OE1 1 
ATOM   2753 N  NE2 . GLN B 1 79  ? -26.766 -1.230  20.970  1.00 37.51  ? 79  GLN B NE2 1 
ATOM   2754 N  N   . GLY B 1 80  ? -23.174 -1.344  19.524  1.00 17.94  ? 80  GLY B N   1 
ATOM   2755 C  CA  . GLY B 1 80  ? -22.282 -2.135  20.371  1.00 16.05  ? 80  GLY B CA  1 
ATOM   2756 C  C   . GLY B 1 80  ? -21.104 -1.344  20.972  1.00 16.94  ? 80  GLY B C   1 
ATOM   2757 O  O   . GLY B 1 80  ? -20.533 -1.771  21.974  1.00 22.80  ? 80  GLY B O   1 
ATOM   2758 N  N   . LEU B 1 81  ? -20.700 -0.217  20.347  1.00 17.61  ? 81  LEU B N   1 
ATOM   2759 C  CA  . LEU B 1 81  ? -19.621 0.603   20.891  1.00 17.78  ? 81  LEU B CA  1 
ATOM   2760 C  C   . LEU B 1 81  ? -20.182 1.542   21.952  1.00 19.92  ? 81  LEU B C   1 
ATOM   2761 O  O   . LEU B 1 81  ? -21.376 1.443   22.274  1.00 20.37  ? 81  LEU B O   1 
ATOM   2762 C  CB  . LEU B 1 81  ? -18.929 1.368   19.756  1.00 17.59  ? 81  LEU B CB  1 
ATOM   2763 C  CG  . LEU B 1 81  ? -18.207 0.488   18.739  1.00 15.56  ? 81  LEU B CG  1 
ATOM   2764 C  CD1 . LEU B 1 81  ? -17.838 1.315   17.506  1.00 16.97  ? 81  LEU B CD1 1 
ATOM   2765 C  CD2 . LEU B 1 81  ? -16.995 -0.183  19.393  1.00 19.00  ? 81  LEU B CD2 1 
ATOM   2766 N  N   . GLN B 1 82  ? -19.359 2.474   22.471  1.00 21.81  ? 82  GLN B N   1 
ATOM   2767 C  CA  . GLN B 1 82  ? -19.792 3.267   23.626  1.00 23.06  ? 82  GLN B CA  1 
ATOM   2768 C  C   . GLN B 1 82  ? -20.679 4.453   23.245  1.00 18.57  ? 82  GLN B C   1 
ATOM   2769 O  O   . GLN B 1 82  ? -21.286 5.090   24.134  1.00 22.98  ? 82  GLN B O   1 
ATOM   2770 C  CB  . GLN B 1 82  ? -18.607 3.812   24.420  1.00 22.71  ? 82  GLN B CB  1 
ATOM   2771 C  CG  . GLN B 1 82  ? -17.879 2.756   25.225  1.00 22.07  ? 82  GLN B CG  1 
ATOM   2772 C  CD  . GLN B 1 82  ? -18.643 2.438   26.486  1.00 32.15  ? 82  GLN B CD  1 
ATOM   2773 O  OE1 . GLN B 1 82  ? -18.475 3.041   27.570  1.00 39.31  ? 82  GLN B OE1 1 
ATOM   2774 N  NE2 . GLN B 1 82  ? -19.550 1.508   26.303  1.00 26.11  ? 82  GLN B NE2 1 
ATOM   2775 N  N   . SER B 1 83  ? -20.803 4.713   21.942  1.00 16.12  ? 83  SER B N   1 
ATOM   2776 C  CA  . SER B 1 83  ? -21.761 5.636   21.348  1.00 16.77  ? 83  SER B CA  1 
ATOM   2777 C  C   . SER B 1 83  ? -22.191 4.930   20.063  1.00 13.64  ? 83  SER B C   1 
ATOM   2778 O  O   . SER B 1 83  ? -21.427 4.075   19.566  1.00 15.93  ? 83  SER B O   1 
ATOM   2779 C  CB  . SER B 1 83  ? -21.095 6.975   20.984  1.00 19.25  ? 83  SER B CB  1 
ATOM   2780 O  OG  . SER B 1 83  ? -20.744 7.789   22.133  1.00 22.22  ? 83  SER B OG  1 
ATOM   2781 N  N   . ARG B 1 84  ? -23.296 5.427   19.458  1.00 14.80  ? 84  ARG B N   1 
ATOM   2782 C  CA  . ARG B 1 84  ? -23.629 5.062   18.094  1.00 14.21  ? 84  ARG B CA  1 
ATOM   2783 C  C   . ARG B 1 84  ? -22.592 5.681   17.162  1.00 14.09  ? 84  ARG B C   1 
ATOM   2784 O  O   . ARG B 1 84  ? -22.281 6.888   17.215  1.00 16.38  ? 84  ARG B O   1 
ATOM   2785 C  CB  . ARG B 1 84  ? -25.001 5.599   17.648  1.00 15.08  ? 84  ARG B CB  1 
ATOM   2786 C  CG  . ARG B 1 84  ? -25.293 5.401   16.158  1.00 18.16  ? 84  ARG B CG  1 
ATOM   2787 C  CD  . ARG B 1 84  ? -26.769 5.589   15.822  1.00 20.90  ? 84  ARG B CD  1 
ATOM   2788 N  NE  . ARG B 1 84  ? -26.906 5.820   14.403  1.00 20.08  ? 84  ARG B NE  1 
ATOM   2789 C  CZ  . ARG B 1 84  ? -28.078 5.834   13.804  1.00 18.54  ? 84  ARG B CZ  1 
ATOM   2790 N  NH1 . ARG B 1 84  ? -29.205 5.696   14.501  1.00 25.87  ? 84  ARG B NH1 1 
ATOM   2791 N  NH2 . ARG B 1 84  ? -28.116 6.045   12.512  1.00 21.02  ? 84  ARG B NH2 1 
ATOM   2792 N  N   . TYR B 1 85  ? -22.084 4.834   16.272  1.00 13.29  ? 85  TYR B N   1 
ATOM   2793 C  CA  . TYR B 1 85  ? -21.161 5.339   15.256  1.00 11.54  ? 85  TYR B CA  1 
ATOM   2794 C  C   . TYR B 1 85  ? -21.825 5.156   13.923  1.00 11.19  ? 85  TYR B C   1 
ATOM   2795 O  O   . TYR B 1 85  ? -22.185 4.039   13.609  1.00 12.71  ? 85  TYR B O   1 
ATOM   2796 C  CB  . TYR B 1 85  ? -19.792 4.651   15.259  1.00 12.88  ? 85  TYR B CB  1 
ATOM   2797 C  CG  . TYR B 1 85  ? -18.878 5.154   16.347  1.00 11.25  ? 85  TYR B CG  1 
ATOM   2798 C  CD1 . TYR B 1 85  ? -19.007 4.699   17.646  1.00 12.01  ? 85  TYR B CD1 1 
ATOM   2799 C  CD2 . TYR B 1 85  ? -17.881 6.088   16.082  1.00 13.28  ? 85  TYR B CD2 1 
ATOM   2800 C  CE1 . TYR B 1 85  ? -18.177 5.144   18.655  1.00 13.04  ? 85  TYR B CE1 1 
ATOM   2801 C  CE2 . TYR B 1 85  ? -17.014 6.501   17.074  1.00 13.86  ? 85  TYR B CE2 1 
ATOM   2802 C  CZ  . TYR B 1 85  ? -17.164 6.039   18.366  1.00 12.74  ? 85  TYR B CZ  1 
ATOM   2803 O  OH  . TYR B 1 85  ? -16.342 6.448   19.392  1.00 16.61  ? 85  TYR B OH  1 
ATOM   2804 N  N   . SER B 1 86  ? -22.116 6.269   13.233  1.00 13.14  ? 86  SER B N   1 
ATOM   2805 C  CA  . SER B 1 86  ? -22.809 6.148   11.945  1.00 11.84  ? 86  SER B CA  1 
ATOM   2806 C  C   . SER B 1 86  ? -21.818 6.182   10.770  1.00 10.10  ? 86  SER B C   1 
ATOM   2807 O  O   . SER B 1 86  ? -20.757 6.855   10.853  1.00 11.38  ? 86  SER B O   1 
ATOM   2808 C  CB  . SER B 1 86  ? -23.825 7.311   11.767  1.00 13.27  ? 86  SER B CB  1 
ATOM   2809 O  OG  . SER B 1 86  ? -24.838 7.306   12.766  1.00 15.01  ? 86  SER B OG  1 
ATOM   2810 N  N   . ALA B 1 87  ? -22.173 5.528   9.646   1.00 10.81  ? 87  ALA B N   1 
ATOM   2811 C  CA  . ALA B 1 87  ? -21.270 5.421   8.522   1.00 10.44  ? 87  ALA B CA  1 
ATOM   2812 C  C   . ALA B 1 87  ? -21.133 6.764   7.834   1.00 9.12   ? 87  ALA B C   1 
ATOM   2813 O  O   . ALA B 1 87  ? -22.084 7.554   7.795   1.00 12.14  ? 87  ALA B O   1 
ATOM   2814 C  CB  . ALA B 1 87  ? -21.746 4.331   7.559   1.00 14.66  ? 87  ALA B CB  1 
ATOM   2815 N  N   . THR B 1 88  ? -19.969 6.946   7.215   1.00 8.74   ? 88  THR B N   1 
ATOM   2816 C  CA  . THR B 1 88  ? -19.763 8.087   6.336   1.00 10.85  ? 88  THR B CA  1 
ATOM   2817 C  C   . THR B 1 88  ? -19.251 7.659   4.956   1.00 9.27   ? 88  THR B C   1 
ATOM   2818 O  O   . THR B 1 88  ? -19.691 8.200   3.947   1.00 10.56  ? 88  THR B O   1 
ATOM   2819 C  CB  . THR B 1 88  ? -19.016 9.175   7.121   1.00 11.49  ? 88  THR B CB  1 
ATOM   2820 O  OG1 . THR B 1 88  ? -18.997 10.316  6.254   1.00 18.31  ? 88  THR B OG1 1 
ATOM   2821 C  CG2 . THR B 1 88  ? -17.581 8.765   7.374   1.00 14.53  ? 88  THR B CG2 1 
ATOM   2822 N  N   . GLN B 1 89  ? -18.280 6.713   4.905   1.00 7.91   ? 89  GLN B N   1 
ATOM   2823 C  CA  . GLN B 1 89  ? -17.744 6.354   3.605   1.00 9.74   ? 89  GLN B CA  1 
ATOM   2824 C  C   . GLN B 1 89  ? -16.971 5.049   3.765   1.00 7.42   ? 89  GLN B C   1 
ATOM   2825 O  O   . GLN B 1 89  ? -16.533 4.709   4.863   1.00 8.02   ? 89  GLN B O   1 
ATOM   2826 C  CB  . GLN B 1 89  ? -16.864 7.478   3.026   1.00 9.84   ? 89  GLN B CB  1 
ATOM   2827 C  CG  . GLN B 1 89  ? -15.697 7.875   3.935   1.00 9.62   ? 89  GLN B CG  1 
ATOM   2828 C  CD  . GLN B 1 89  ? -14.365 7.408   3.440   1.00 9.26   ? 89  GLN B CD  1 
ATOM   2829 O  OE1 . GLN B 1 89  ? -14.218 6.238   3.044   1.00 11.11  ? 89  GLN B OE1 1 
ATOM   2830 N  NE2 . GLN B 1 89  ? -13.354 8.189   3.529   1.00 12.37  ? 89  GLN B NE2 1 
ATOM   2831 N  N   . LEU B 1 90  ? -16.784 4.325   2.653   1.00 8.00   ? 90  LEU B N   1 
ATOM   2832 C  CA  . LEU B 1 90  ? -15.791 3.272   2.654   1.00 7.04   ? 90  LEU B CA  1 
ATOM   2833 C  C   . LEU B 1 90  ? -14.816 3.453   1.478   1.00 6.66   ? 90  LEU B C   1 
ATOM   2834 O  O   . LEU B 1 90  ? -15.095 4.163   0.471   1.00 7.56   ? 90  LEU B O   1 
ATOM   2835 C  CB  . LEU B 1 90  ? -16.415 1.844   2.627   1.00 8.27   ? 90  LEU B CB  1 
ATOM   2836 C  CG  . LEU B 1 90  ? -17.368 1.524   1.472   1.00 8.30   ? 90  LEU B CG  1 
ATOM   2837 C  CD1 . LEU B 1 90  ? -16.573 1.191   0.186   1.00 8.31   ? 90  LEU B CD1 1 
ATOM   2838 C  CD2 . LEU B 1 90  ? -18.272 0.368   1.822   1.00 9.22   ? 90  LEU B CD2 1 
ATOM   2839 N  N   . HIS B 1 91  ? -13.609 2.846   1.589   1.00 7.34   ? 91  HIS B N   1 
ATOM   2840 C  CA  . HIS B 1 91  ? -12.594 2.933   0.552   1.00 7.07   ? 91  HIS B CA  1 
ATOM   2841 C  C   . HIS B 1 91  ? -11.636 1.742   0.737   1.00 6.30   ? 91  HIS B C   1 
ATOM   2842 O  O   . HIS B 1 91  ? -11.764 1.063   1.761   1.00 8.06   ? 91  HIS B O   1 
ATOM   2843 C  CB  . HIS B 1 91  ? -11.926 4.335   0.678   1.00 6.66   ? 91  HIS B CB  1 
ATOM   2844 C  CG  . HIS B 1 91  ? -11.185 4.455   1.973   1.00 7.16   ? 91  HIS B CG  1 
ATOM   2845 N  ND1 . HIS B 1 91  ? -11.796 4.966   3.102   1.00 7.53   ? 91  HIS B ND1 1 
ATOM   2846 C  CD2 . HIS B 1 91  ? -9.952  4.015   2.398   1.00 8.02   ? 91  HIS B CD2 1 
ATOM   2847 C  CE1 . HIS B 1 91  ? -10.988 4.877   4.131   1.00 7.31   ? 91  HIS B CE1 1 
ATOM   2848 N  NE2 . HIS B 1 91  ? -9.778  4.307   3.725   1.00 7.82   ? 91  HIS B NE2 1 
ATOM   2849 N  N   . LEU B 1 92  ? -10.664 1.650   -0.150  1.00 6.92   ? 92  LEU B N   1 
ATOM   2850 C  CA  . LEU B 1 92  ? -9.695  0.559   -0.118  1.00 7.12   ? 92  LEU B CA  1 
ATOM   2851 C  C   . LEU B 1 92  ? -8.268  1.041   -0.178  1.00 7.93   ? 92  LEU B C   1 
ATOM   2852 O  O   . LEU B 1 92  ? -8.003  2.224   -0.591  1.00 8.04   ? 92  LEU B O   1 
ATOM   2853 C  CB  . LEU B 1 92  ? -9.988  -0.426  -1.256  1.00 9.57   ? 92  LEU B CB  1 
ATOM   2854 C  CG  . LEU B 1 92  ? -11.374 -1.110  -1.133  1.00 7.98   ? 92  LEU B CG  1 
ATOM   2855 C  CD1 . LEU B 1 92  ? -12.413 -0.499  -2.043  1.00 13.30  ? 92  LEU B CD1 1 
ATOM   2856 C  CD2 . LEU B 1 92  ? -11.270 -2.590  -1.471  1.00 11.81  ? 92  LEU B CD2 1 
ATOM   2857 N  N   . HIS B 1 93  ? -7.328  0.152   0.100   1.00 7.79   ? 93  HIS B N   1 
ATOM   2858 C  CA  . HIS B 1 93  ? -5.870  0.330   -0.055  1.00 6.64   ? 93  HIS B CA  1 
ATOM   2859 C  C   . HIS B 1 93  ? -5.357  -0.901  -0.743  1.00 5.92   ? 93  HIS B C   1 
ATOM   2860 O  O   . HIS B 1 93  ? -5.814  -2.005  -0.374  1.00 7.93   ? 93  HIS B O   1 
ATOM   2861 C  CB  . HIS B 1 93  ? -5.216  0.552   1.315   1.00 7.26   ? 93  HIS B CB  1 
ATOM   2862 C  CG  . HIS B 1 93  ? -5.752  1.717   2.059   1.00 7.11   ? 93  HIS B CG  1 
ATOM   2863 N  ND1 . HIS B 1 93  ? -5.182  2.938   2.003   1.00 6.71   ? 93  HIS B ND1 1 
ATOM   2864 C  CD2 . HIS B 1 93  ? -6.766  1.783   2.895   1.00 7.88   ? 93  HIS B CD2 1 
ATOM   2865 C  CE1 . HIS B 1 93  ? -5.884  3.737   2.790   1.00 7.83   ? 93  HIS B CE1 1 
ATOM   2866 N  NE2 . HIS B 1 93  ? -6.860  3.103   3.341   1.00 6.42   ? 93  HIS B NE2 1 
ATOM   2867 N  N   . TRP B 1 94  ? -4.403  -0.760  -1.704  1.00 6.18   ? 94  TRP B N   1 
ATOM   2868 C  CA  . TRP B 1 94  ? -3.913  -1.915  -2.456  1.00 6.10   ? 94  TRP B CA  1 
ATOM   2869 C  C   . TRP B 1 94  ? -2.506  -1.625  -2.964  1.00 6.58   ? 94  TRP B C   1 
ATOM   2870 O  O   . TRP B 1 94  ? -1.930  -0.550  -2.718  1.00 7.12   ? 94  TRP B O   1 
ATOM   2871 C  CB  . TRP B 1 94  ? -4.851  -2.206  -3.631  1.00 7.40   ? 94  TRP B CB  1 
ATOM   2872 C  CG  . TRP B 1 94  ? -5.005  -1.018  -4.545  1.00 7.24   ? 94  TRP B CG  1 
ATOM   2873 C  CD1 . TRP B 1 94  ? -4.180  -0.690  -5.591  1.00 7.33   ? 94  TRP B CD1 1 
ATOM   2874 C  CD2 . TRP B 1 94  ? -6.043  0.020   -4.482  1.00 6.55   ? 94  TRP B CD2 1 
ATOM   2875 N  NE1 . TRP B 1 94  ? -4.651  0.501   -6.175  1.00 7.91   ? 94  TRP B NE1 1 
ATOM   2876 C  CE2 . TRP B 1 94  ? -5.818  0.912   -5.570  1.00 6.91   ? 94  TRP B CE2 1 
ATOM   2877 C  CE3 . TRP B 1 94  ? -7.175  0.253   -3.657  1.00 7.28   ? 94  TRP B CE3 1 
ATOM   2878 C  CZ2 . TRP B 1 94  ? -6.615  2.044   -5.804  1.00 8.47   ? 94  TRP B CZ2 1 
ATOM   2879 C  CZ3 . TRP B 1 94  ? -7.951  1.398   -3.846  1.00 8.03   ? 94  TRP B CZ3 1 
ATOM   2880 C  CH2 . TRP B 1 94  ? -7.709  2.221   -4.975  1.00 8.41   ? 94  TRP B CH2 1 
ATOM   2881 N  N   . GLY B 1 95  ? -1.913  -2.614  -3.623  1.00 8.04   ? 95  GLY B N   1 
ATOM   2882 C  CA  . GLY B 1 95  ? -0.547  -2.617  -4.067  1.00 8.63   ? 95  GLY B CA  1 
ATOM   2883 C  C   . GLY B 1 95  ? -0.446  -2.228  -5.532  1.00 8.16   ? 95  GLY B C   1 
ATOM   2884 O  O   . GLY B 1 95  ? -0.975  -1.220  -5.962  1.00 9.16   ? 95  GLY B O   1 
ATOM   2885 N  N   . ASN B 1 96  ? 0.113   -3.134  -6.336  1.00 8.66   ? 96  ASN B N   1 
ATOM   2886 C  CA  . ASN B 1 96  ? 0.249   -2.820  -7.738  1.00 9.65   ? 96  ASN B CA  1 
ATOM   2887 C  C   . ASN B 1 96  ? 0.278   -4.119  -8.517  1.00 10.89  ? 96  ASN B C   1 
ATOM   2888 O  O   . ASN B 1 96  ? 0.366   -5.200  -7.916  1.00 10.56  ? 96  ASN B O   1 
ATOM   2889 C  CB  . ASN B 1 96  ? 1.489   -1.982  -8.034  1.00 11.63  ? 96  ASN B CB  1 
ATOM   2890 C  CG  . ASN B 1 96  ? 2.792   -2.745  -7.863  1.00 12.98  ? 96  ASN B CG  1 
ATOM   2891 O  OD1 . ASN B 1 96  ? 3.226   -3.488  -8.745  1.00 20.22  ? 96  ASN B OD1 1 
ATOM   2892 N  ND2 . ASN B 1 96  ? 3.403   -2.620  -6.707  1.00 16.50  ? 96  ASN B ND2 1 
ATOM   2893 N  N   . PRO B 1 97  ? 0.152   -4.070  -9.858  1.00 11.33  ? 97  PRO B N   1 
ATOM   2894 C  CA  . PRO B 1 97  ? 0.004   -5.321  -10.613 1.00 12.88  ? 97  PRO B CA  1 
ATOM   2895 C  C   . PRO B 1 97  ? 1.110   -6.340  -10.363 1.00 11.36  ? 97  PRO B C   1 
ATOM   2896 O  O   . PRO B 1 97  ? 0.833   -7.530  -10.486 1.00 15.76  ? 97  PRO B O   1 
ATOM   2897 C  CB  . PRO B 1 97  ? 0.001   -4.848  -12.058 1.00 16.61  ? 97  PRO B CB  1 
ATOM   2898 C  CG  . PRO B 1 97  ? -0.664  -3.445  -11.922 1.00 15.95  ? 97  PRO B CG  1 
ATOM   2899 C  CD  . PRO B 1 97  ? -0.009  -2.857  -10.688 1.00 14.84  ? 97  PRO B CD  1 
ATOM   2900 N  N   . ASN B 1 98  ? 2.342   -5.879  -10.183 1.00 10.99  ? 98  ASN B N   1 
ATOM   2901 C  CA  . ASN B 1 98  ? 3.488   -6.777  -10.046 1.00 11.37  ? 98  ASN B CA  1 
ATOM   2902 C  C   . ASN B 1 98  ? 3.738   -7.110  -8.569  1.00 12.47  ? 98  ASN B C   1 
ATOM   2903 O  O   . ASN B 1 98  ? 4.653   -7.842  -8.255  1.00 19.60  ? 98  ASN B O   1 
ATOM   2904 C  CB  . ASN B 1 98  ? 4.729   -6.232  -10.752 1.00 10.98  ? 98  ASN B CB  1 
ATOM   2905 C  CG  . ASN B 1 98  ? 4.469   -6.009  -12.222 1.00 12.05  ? 98  ASN B CG  1 
ATOM   2906 O  OD1 . ASN B 1 98  ? 4.331   -6.979  -12.960 1.00 14.75  ? 98  ASN B OD1 1 
ATOM   2907 N  ND2 . ASN B 1 98  ? 4.374   -4.764  -12.689 1.00 15.58  ? 98  ASN B ND2 1 
ATOM   2908 N  N   . ASP B 1 99  ? 2.954   -6.563  -7.655  1.00 11.99  ? 99  ASP B N   1 
ATOM   2909 C  CA  . ASP B 1 99  ? 3.145   -6.853  -6.237  1.00 11.81  ? 99  ASP B CA  1 
ATOM   2910 C  C   . ASP B 1 99  ? 1.801   -6.621  -5.568  1.00 12.29  ? 99  ASP B C   1 
ATOM   2911 O  O   . ASP B 1 99  ? 1.534   -5.565  -5.009  1.00 9.32   ? 99  ASP B O   1 
ATOM   2912 C  CB  . ASP B 1 99  ? 4.136   -5.878  -5.580  1.00 14.18  ? 99  ASP B CB  1 
ATOM   2913 C  CG  . ASP B 1 99  ? 4.433   -6.142  -4.094  1.00 17.39  ? 99  ASP B CG  1 
ATOM   2914 O  OD1 . ASP B 1 99  ? 3.988   -7.164  -3.565  1.00 21.45  ? 99  ASP B OD1 1 
ATOM   2915 O  OD2 . ASP B 1 99  ? 4.986   -5.222  -3.436  1.00 26.63  ? 99  ASP B OD2 1 
ATOM   2916 N  N   . PRO B 1 100 ? 0.870   -7.608  -5.630  1.00 9.21   ? 100 PRO B N   1 
ATOM   2917 C  CA  . PRO B 1 100 ? -0.489  -7.414  -5.075  1.00 9.06   ? 100 PRO B CA  1 
ATOM   2918 C  C   . PRO B 1 100 ? -0.437  -7.658  -3.560  1.00 10.58  ? 100 PRO B C   1 
ATOM   2919 O  O   . PRO B 1 100 ? -1.033  -8.596  -3.068  1.00 11.39  ? 100 PRO B O   1 
ATOM   2920 C  CB  . PRO B 1 100 ? -1.301  -8.472  -5.849  1.00 11.20  ? 100 PRO B CB  1 
ATOM   2921 C  CG  . PRO B 1 100 ? -0.268  -9.592  -6.157  1.00 10.80  ? 100 PRO B CG  1 
ATOM   2922 C  CD  . PRO B 1 100 ? 1.060   -8.865  -6.381  1.00 10.16  ? 100 PRO B CD  1 
ATOM   2923 N  N   . HIS B 1 101 ? 0.253   -6.797  -2.803  1.00 10.11  ? 101 HIS B N   1 
ATOM   2924 C  CA  . HIS B 1 101 ? 0.404   -6.966  -1.371  1.00 10.02  ? 101 HIS B CA  1 
ATOM   2925 C  C   . HIS B 1 101 ? 0.363   -5.612  -0.684  1.00 8.81   ? 101 HIS B C   1 
ATOM   2926 O  O   . HIS B 1 101 ? 1.365   -5.169  -0.092  1.00 16.45  ? 101 HIS B O   1 
ATOM   2927 C  CB  . HIS B 1 101 ? 1.686   -7.739  -1.018  1.00 12.18  ? 101 HIS B CB  1 
ATOM   2928 C  CG  . HIS B 1 101 ? 1.757   -9.087  -1.653  1.00 13.82  ? 101 HIS B CG  1 
ATOM   2929 N  ND1 . HIS B 1 101 ? 1.083   -10.207 -1.146  1.00 17.59  ? 101 HIS B ND1 1 
ATOM   2930 C  CD2 . HIS B 1 101 ? 2.319   -9.458  -2.826  1.00 12.23  ? 101 HIS B CD2 1 
ATOM   2931 C  CE1 . HIS B 1 101 ? 1.346   -11.294 -1.905  1.00 21.48  ? 101 HIS B CE1 1 
ATOM   2932 N  NE2 . HIS B 1 101 ? 2.076   -10.825 -3.004  1.00 21.95  ? 101 HIS B NE2 1 
ATOM   2933 N  N   . GLY B 1 102 ? -0.817  -5.014  -0.700  1.00 9.73   ? 102 GLY B N   1 
ATOM   2934 C  CA  . GLY B 1 102 ? -0.929  -3.638  -0.317  1.00 7.86   ? 102 GLY B CA  1 
ATOM   2935 C  C   . GLY B 1 102 ? -1.921  -3.422  0.833   1.00 7.98   ? 102 GLY B C   1 
ATOM   2936 O  O   . GLY B 1 102 ? -2.436  -2.331  0.973   1.00 8.44   ? 102 GLY B O   1 
ATOM   2937 N  N   . SER B 1 103 ? -2.204  -4.383  1.726   1.00 7.22   ? 103 SER B N   1 
ATOM   2938 C  CA  . SER B 1 103 ? -2.914  -4.106  2.982   1.00 7.10   ? 103 SER B CA  1 
ATOM   2939 C  C   . SER B 1 103 ? -2.105  -3.020  3.756   1.00 8.42   ? 103 SER B C   1 
ATOM   2940 O  O   . SER B 1 103 ? -0.873  -2.925  3.619   1.00 9.33   ? 103 SER B O   1 
ATOM   2941 C  CB  . SER B 1 103 ? -3.225  -5.387  3.784   1.00 7.64   ? 103 SER B CB  1 
ATOM   2942 O  OG  . SER B 1 103 ? -2.013  -5.901  4.345   1.00 7.82   ? 103 SER B OG  1 
ATOM   2943 N  N   . GLU B 1 104 ? -2.823  -2.347  4.663   1.00 7.64   ? 104 GLU B N   1 
ATOM   2944 C  CA  . GLU B 1 104 ? -2.159  -1.392  5.543   1.00 8.00   ? 104 GLU B CA  1 
ATOM   2945 C  C   . GLU B 1 104 ? -1.729  -2.129  6.823   1.00 8.34   ? 104 GLU B C   1 
ATOM   2946 O  O   . GLU B 1 104 ? -0.542  -2.175  7.162   1.00 8.32   ? 104 GLU B O   1 
ATOM   2947 C  CB  . GLU B 1 104 ? -3.066  -0.218  5.884   1.00 8.82   ? 104 GLU B CB  1 
ATOM   2948 C  CG  . GLU B 1 104 ? -3.482  0.504   4.598   1.00 9.46   ? 104 GLU B CG  1 
ATOM   2949 C  CD  . GLU B 1 104 ? -3.641  2.010   4.866   1.00 6.37   ? 104 GLU B CD  1 
ATOM   2950 O  OE1 . GLU B 1 104 ? -4.640  2.337   5.493   1.00 8.66   ? 104 GLU B OE1 1 
ATOM   2951 O  OE2 . GLU B 1 104 ? -2.670  2.716   4.532   1.00 7.66   ? 104 GLU B OE2 1 
ATOM   2952 N  N   . HIS B 1 105 ? -2.687  -2.757  7.535   1.00 8.39   ? 105 HIS B N   1 
ATOM   2953 C  CA  . HIS B 1 105 ? -2.266  -3.605  8.652   1.00 7.82   ? 105 HIS B CA  1 
ATOM   2954 C  C   . HIS B 1 105 ? -1.646  -4.886  8.115   1.00 8.82   ? 105 HIS B C   1 
ATOM   2955 O  O   . HIS B 1 105 ? -1.953  -5.349  7.023   1.00 9.09   ? 105 HIS B O   1 
ATOM   2956 C  CB  . HIS B 1 105 ? -3.519  -3.980  9.514   1.00 8.54   ? 105 HIS B CB  1 
ATOM   2957 C  CG  . HIS B 1 105 ? -4.030  -2.724  10.145  1.00 7.77   ? 105 HIS B CG  1 
ATOM   2958 N  ND1 . HIS B 1 105 ? -5.021  -1.954  9.576   1.00 7.99   ? 105 HIS B ND1 1 
ATOM   2959 C  CD2 . HIS B 1 105 ? -3.776  -2.282  11.397  1.00 8.07   ? 105 HIS B CD2 1 
ATOM   2960 C  CE1 . HIS B 1 105 ? -5.206  -0.940  10.424  1.00 7.38   ? 105 HIS B CE1 1 
ATOM   2961 N  NE2 . HIS B 1 105 ? -4.468  -1.068  11.530  1.00 8.77   ? 105 HIS B NE2 1 
ATOM   2962 N  N   . THR B 1 106 ? -0.644  -5.372  8.872   1.00 8.72   ? 106 THR B N   1 
ATOM   2963 C  CA  . THR B 1 106 ? -0.015  -6.659  8.574   1.00 9.88   ? 106 THR B CA  1 
ATOM   2964 C  C   . THR B 1 106 ? -0.242  -7.587  9.747   1.00 8.71   ? 106 THR B C   1 
ATOM   2965 O  O   . THR B 1 106 ? -0.584  -7.161  10.810  1.00 9.56   ? 106 THR B O   1 
ATOM   2966 C  CB  . THR B 1 106 ? 1.461   -6.398  8.270   1.00 9.84   ? 106 THR B CB  1 
ATOM   2967 O  OG1 . THR B 1 106 ? 2.140   -5.856  9.409   1.00 10.04  ? 106 THR B OG1 1 
ATOM   2968 C  CG2 . THR B 1 106 ? 1.627   -5.511  7.046   1.00 10.86  ? 106 THR B CG2 1 
ATOM   2969 N  N   . VAL B 1 107 ? -0.122  -8.902  9.460   1.00 11.98  ? 107 VAL B N   1 
ATOM   2970 C  CA  . VAL B 1 107 ? -0.309  -9.866  10.541  1.00 14.12  ? 107 VAL B CA  1 
ATOM   2971 C  C   . VAL B 1 107 ? 0.971   -10.688 10.601  1.00 13.27  ? 107 VAL B C   1 
ATOM   2972 O  O   . VAL B 1 107 ? 1.327   -11.318 9.604   1.00 13.51  ? 107 VAL B O   1 
ATOM   2973 C  CB  . VAL B 1 107 ? -1.553  -10.761 10.336  1.00 13.76  ? 107 VAL B CB  1 
ATOM   2974 C  CG1 . VAL B 1 107 ? -1.679  -11.837 11.418  1.00 18.42  ? 107 VAL B CG1 1 
ATOM   2975 C  CG2 . VAL B 1 107 ? -2.844  -9.940  10.288  1.00 17.15  ? 107 VAL B CG2 1 
ATOM   2976 N  N   . SER B 1 108 ? 1.599   -10.731 11.774  1.00 14.10  ? 108 SER B N   1 
ATOM   2977 C  CA  . SER B 1 108 ? 2.872   -11.446 11.954  1.00 14.25  ? 108 SER B CA  1 
ATOM   2978 C  C   . SER B 1 108 ? 3.834   -11.113 10.790  1.00 14.93  ? 108 SER B C   1 
ATOM   2979 O  O   . SER B 1 108 ? 4.413   -12.001 10.167  1.00 16.97  ? 108 SER B O   1 
ATOM   2980 C  CB  . SER B 1 108 ? 2.671   -12.948 12.099  1.00 20.05  ? 108 SER B CB  1 
ATOM   2981 O  OG  . SER B 1 108 ? 1.794   -13.192 13.199  1.00 21.98  ? 108 SER B OG  1 
ATOM   2982 N  N   . GLY B 1 109 ? 3.954   -9.826  10.458  1.00 14.72  ? 109 GLY B N   1 
ATOM   2983 C  CA  . GLY B 1 109 ? 4.889   -9.296  9.466   1.00 14.06  ? 109 GLY B CA  1 
ATOM   2984 C  C   . GLY B 1 109 ? 4.489   -9.441  7.995   1.00 18.87  ? 109 GLY B C   1 
ATOM   2985 O  O   . GLY B 1 109 ? 5.245   -9.003  7.109   1.00 23.28  ? 109 GLY B O   1 
ATOM   2986 N  N   . GLN B 1 110 ? 3.323   -10.045 7.711   1.00 16.58  ? 110 GLN B N   1 
ATOM   2987 C  CA  . GLN B 1 110 ? 2.902   -10.282 6.327   1.00 16.43  ? 110 GLN B CA  1 
ATOM   2988 C  C   . GLN B 1 110 ? 1.756   -9.363  5.888   1.00 11.52  ? 110 GLN B C   1 
ATOM   2989 O  O   . GLN B 1 110 ? 0.782   -9.196  6.604   1.00 10.07  ? 110 GLN B O   1 
ATOM   2990 C  CB  . GLN B 1 110 ? 2.360   -11.713 6.234   1.00 22.79  ? 110 GLN B CB  1 
ATOM   2991 C  CG  . GLN B 1 110 ? 3.194   -12.829 6.888   1.00 21.87  ? 110 GLN B CG  1 
ATOM   2992 C  CD  . GLN B 1 110 ? 4.583   -12.845 6.314   1.00 29.24  ? 110 GLN B CD  1 
ATOM   2993 O  OE1 . GLN B 1 110 ? 4.764   -13.072 5.111   1.00 41.77  ? 110 GLN B OE1 1 
ATOM   2994 N  NE2 . GLN B 1 110 ? 5.566   -12.662 7.196   1.00 30.95  ? 110 GLN B NE2 1 
ATOM   2995 N  N   . HIS B 1 111 ? 1.922   -8.772  4.693   1.00 11.60  ? 111 HIS B N   1 
ATOM   2996 C  CA  . HIS B 1 111 ? 0.832   -8.034  4.047   1.00 11.79  ? 111 HIS B CA  1 
ATOM   2997 C  C   . HIS B 1 111 ? -0.207  -8.934  3.427   1.00 8.24   ? 111 HIS B C   1 
ATOM   2998 O  O   . HIS B 1 111 ? 0.115   -9.978  2.816   1.00 14.82  ? 111 HIS B O   1 
ATOM   2999 C  CB  . HIS B 1 111 ? 1.283   -7.179  2.854   1.00 12.35  ? 111 HIS B CB  1 
ATOM   3000 C  CG  . HIS B 1 111 ? 1.957   -5.905  3.217   1.00 10.06  ? 111 HIS B CG  1 
ATOM   3001 N  ND1 . HIS B 1 111 ? 1.305   -4.721  3.424   1.00 12.06  ? 111 HIS B ND1 1 
ATOM   3002 C  CD2 . HIS B 1 111 ? 3.274   -5.693  3.514   1.00 13.63  ? 111 HIS B CD2 1 
ATOM   3003 C  CE1 . HIS B 1 111 ? 2.143   -3.828  3.830   1.00 14.84  ? 111 HIS B CE1 1 
ATOM   3004 N  NE2 . HIS B 1 111 ? 3.368   -4.367  3.833   1.00 14.41  ? 111 HIS B NE2 1 
ATOM   3005 N  N   . PHE B 1 112 ? -1.463  -8.549  3.545   1.00 9.13   ? 112 PHE B N   1 
ATOM   3006 C  CA  . PHE B 1 112 ? -2.536  -9.055  2.721   1.00 9.01   ? 112 PHE B CA  1 
ATOM   3007 C  C   . PHE B 1 112 ? -2.561  -8.356  1.375   1.00 7.67   ? 112 PHE B C   1 
ATOM   3008 O  O   . PHE B 1 112 ? -1.843  -7.356  1.177   1.00 8.26   ? 112 PHE B O   1 
ATOM   3009 C  CB  . PHE B 1 112 ? -3.873  -8.995  3.464   1.00 9.83   ? 112 PHE B CB  1 
ATOM   3010 C  CG  . PHE B 1 112 ? -3.966  -10.053 4.534   1.00 11.51  ? 112 PHE B CG  1 
ATOM   3011 C  CD1 . PHE B 1 112 ? -3.308  -9.908  5.751   1.00 14.19  ? 112 PHE B CD1 1 
ATOM   3012 C  CD2 . PHE B 1 112 ? -4.634  -11.246 4.233   1.00 13.61  ? 112 PHE B CD2 1 
ATOM   3013 C  CE1 . PHE B 1 112 ? -3.396  -10.914 6.693   1.00 20.30  ? 112 PHE B CE1 1 
ATOM   3014 C  CE2 . PHE B 1 112 ? -4.692  -12.258 5.183   1.00 19.44  ? 112 PHE B CE2 1 
ATOM   3015 C  CZ  . PHE B 1 112 ? -4.098  -12.049 6.403   1.00 17.37  ? 112 PHE B CZ  1 
ATOM   3016 N  N   . ALA B 1 113 ? -3.359  -8.818  0.423   1.00 7.85   ? 113 ALA B N   1 
ATOM   3017 C  CA  . ALA B 1 113 ? -3.394  -8.211  -0.898  1.00 7.94   ? 113 ALA B CA  1 
ATOM   3018 C  C   . ALA B 1 113 ? -3.923  -6.779  -0.851  1.00 6.94   ? 113 ALA B C   1 
ATOM   3019 O  O   . ALA B 1 113 ? -3.456  -5.934  -1.626  1.00 8.81   ? 113 ALA B O   1 
ATOM   3020 C  CB  . ALA B 1 113 ? -4.242  -9.063  -1.837  1.00 9.76   ? 113 ALA B CB  1 
ATOM   3021 N  N   . ALA B 1 114 ? -4.938  -6.539  -0.018  1.00 7.87   ? 114 ALA B N   1 
ATOM   3022 C  CA  . ALA B 1 114 ? -5.536  -5.192  0.044   1.00 7.00   ? 114 ALA B CA  1 
ATOM   3023 C  C   . ALA B 1 114 ? -6.306  -5.111  1.342   1.00 7.47   ? 114 ALA B C   1 
ATOM   3024 O  O   . ALA B 1 114 ? -6.319  -6.047  2.159   1.00 7.82   ? 114 ALA B O   1 
ATOM   3025 C  CB  . ALA B 1 114 ? -6.482  -5.127  -1.181  1.00 8.75   ? 114 ALA B CB  1 
ATOM   3026 N  N   . GLU B 1 115 ? -6.957  -3.960  1.569   1.00 7.33   ? 115 GLU B N   1 
ATOM   3027 C  CA  . GLU B 1 115 ? -7.727  -3.766  2.800   1.00 7.05   ? 115 GLU B CA  1 
ATOM   3028 C  C   . GLU B 1 115 ? -8.884  -2.810  2.547   1.00 7.26   ? 115 GLU B C   1 
ATOM   3029 O  O   . GLU B 1 115 ? -8.703  -1.797  1.848   1.00 8.17   ? 115 GLU B O   1 
ATOM   3030 C  CB  . GLU B 1 115 ? -6.742  -3.224  3.853   1.00 6.62   ? 115 GLU B CB  1 
ATOM   3031 C  CG  . GLU B 1 115 ? -7.319  -2.989  5.246   1.00 8.55   ? 115 GLU B CG  1 
ATOM   3032 C  CD  . GLU B 1 115 ? -6.218  -2.773  6.277   1.00 7.66   ? 115 GLU B CD  1 
ATOM   3033 O  OE1 . GLU B 1 115 ? -5.101  -3.224  6.070   1.00 7.94   ? 115 GLU B OE1 1 
ATOM   3034 O  OE2 . GLU B 1 115 ? -6.519  -2.172  7.333   1.00 8.26   ? 115 GLU B OE2 1 
ATOM   3035 N  N   . LEU B 1 116 ? -10.026 -3.134  3.100   1.00 6.49   ? 116 LEU B N   1 
ATOM   3036 C  CA  . LEU B 1 116 ? -11.222 -2.300  3.026   1.00 6.14   ? 116 LEU B CA  1 
ATOM   3037 C  C   . LEU B 1 116 ? -11.369 -1.562  4.356   1.00 6.37   ? 116 LEU B C   1 
ATOM   3038 O  O   . LEU B 1 116 ? -11.245 -2.178  5.409   1.00 6.89   ? 116 LEU B O   1 
ATOM   3039 C  CB  . LEU B 1 116 ? -12.482 -3.153  2.837   1.00 7.23   ? 116 LEU B CB  1 
ATOM   3040 C  CG  . LEU B 1 116 ? -13.824 -2.408  2.976   1.00 8.13   ? 116 LEU B CG  1 
ATOM   3041 C  CD1 . LEU B 1 116 ? -14.096 -1.540  1.780   1.00 8.88   ? 116 LEU B CD1 1 
ATOM   3042 C  CD2 . LEU B 1 116 ? -14.959 -3.407  3.087   1.00 10.25  ? 116 LEU B CD2 1 
ATOM   3043 N  N   . HIS B 1 117 ? -11.610 -0.220  4.290   1.00 6.97   ? 117 HIS B N   1 
ATOM   3044 C  CA  . HIS B 1 117 ? -11.943 0.503   5.515   1.00 7.70   ? 117 HIS B CA  1 
ATOM   3045 C  C   . HIS B 1 117 ? -13.351 1.094   5.433   1.00 6.76   ? 117 HIS B C   1 
ATOM   3046 O  O   . HIS B 1 117 ? -13.673 1.744   4.413   1.00 7.53   ? 117 HIS B O   1 
ATOM   3047 C  CB  . HIS B 1 117 ? -11.043 1.705   5.637   1.00 9.13   ? 117 HIS B CB  1 
ATOM   3048 C  CG  . HIS B 1 117 ? -9.663  1.235   6.008   1.00 7.27   ? 117 HIS B CG  1 
ATOM   3049 N  ND1 . HIS B 1 117 ? -8.484  2.002   5.746   1.00 9.62   ? 117 HIS B ND1 1 
ATOM   3050 C  CD2 . HIS B 1 117 ? -9.246  0.054   6.579   1.00 7.33   ? 117 HIS B CD2 1 
ATOM   3051 C  CE1 . HIS B 1 117 ? -7.424  1.354   6.287   1.00 9.37   ? 117 HIS B CE1 1 
ATOM   3052 N  NE2 . HIS B 1 117 ? -7.903  0.106   6.717   1.00 6.38   ? 117 HIS B NE2 1 
ATOM   3053 N  N   . ILE B 1 118 ? -14.211 0.799   6.433   1.00 7.47   ? 118 ILE B N   1 
ATOM   3054 C  CA  . ILE B 1 118 ? -15.566 1.388   6.465   1.00 6.62   ? 118 ILE B CA  1 
ATOM   3055 C  C   . ILE B 1 118 ? -15.569 2.406   7.609   1.00 7.25   ? 118 ILE B C   1 
ATOM   3056 O  O   . ILE B 1 118 ? -15.406 2.050   8.793   1.00 8.28   ? 118 ILE B O   1 
ATOM   3057 C  CB  . ILE B 1 118 ? -16.680 0.349   6.678   1.00 7.17   ? 118 ILE B CB  1 
ATOM   3058 C  CG1 . ILE B 1 118 ? -16.549 -0.816  5.692   1.00 9.87   ? 118 ILE B CG1 1 
ATOM   3059 C  CG2 . ILE B 1 118 ? -18.050 1.043   6.597   1.00 8.84   ? 118 ILE B CG2 1 
ATOM   3060 C  CD1 . ILE B 1 118 ? -17.524 -1.975  5.990   1.00 10.17  ? 118 ILE B CD1 1 
ATOM   3061 N  N   . VAL B 1 119 ? -15.508 3.698   7.213   1.00 6.97   ? 119 VAL B N   1 
ATOM   3062 C  CA  . VAL B 1 119 ? -15.323 4.785   8.179   1.00 8.16   ? 119 VAL B CA  1 
ATOM   3063 C  C   . VAL B 1 119 ? -16.682 5.222   8.774   1.00 7.82   ? 119 VAL B C   1 
ATOM   3064 O  O   . VAL B 1 119 ? -17.634 5.481   8.019   1.00 9.03   ? 119 VAL B O   1 
ATOM   3065 C  CB  . VAL B 1 119 ? -14.688 5.995   7.479   1.00 7.47   ? 119 VAL B CB  1 
ATOM   3066 C  CG1 . VAL B 1 119 ? -14.430 7.137   8.461   1.00 9.86   ? 119 VAL B CG1 1 
ATOM   3067 C  CG2 . VAL B 1 119 ? -13.344 5.652   6.788   1.00 9.80   ? 119 VAL B CG2 1 
ATOM   3068 N  N   . HIS B 1 120 ? -16.744 5.321   10.143  1.00 8.29   ? 120 HIS B N   1 
ATOM   3069 C  CA  . HIS B 1 120 ? -17.922 5.786   10.870  1.00 8.74   ? 120 HIS B CA  1 
ATOM   3070 C  C   . HIS B 1 120 ? -17.513 6.927   11.802  1.00 9.61   ? 120 HIS B C   1 
ATOM   3071 O  O   . HIS B 1 120 ? -16.327 7.037   12.148  1.00 10.23  ? 120 HIS B O   1 
ATOM   3072 C  CB  . HIS B 1 120 ? -18.493 4.641   11.704  1.00 12.21  ? 120 HIS B CB  1 
ATOM   3073 C  CG  . HIS B 1 120 ? -18.902 3.434   10.935  1.00 9.35   ? 120 HIS B CG  1 
ATOM   3074 N  ND1 . HIS B 1 120 ? -17.947 2.537   10.414  1.00 8.27   ? 120 HIS B ND1 1 
ATOM   3075 C  CD2 . HIS B 1 120 ? -20.105 2.809   10.786  1.00 9.13   ? 120 HIS B CD2 1 
ATOM   3076 C  CE1 . HIS B 1 120 ? -18.591 1.487   9.879   1.00 9.09   ? 120 HIS B CE1 1 
ATOM   3077 N  NE2 . HIS B 1 120 ? -19.935 1.597   10.092  1.00 8.67   ? 120 HIS B NE2 1 
ATOM   3078 N  N   . TYR B 1 121 ? -18.498 7.726   12.237  1.00 11.24  ? 121 TYR B N   1 
ATOM   3079 C  CA  . TYR B 1 121 ? -18.241 8.819   13.169  1.00 11.40  ? 121 TYR B CA  1 
ATOM   3080 C  C   . TYR B 1 121 ? -19.278 8.798   14.284  1.00 12.93  ? 121 TYR B C   1 
ATOM   3081 O  O   . TYR B 1 121 ? -20.399 8.207   14.137  1.00 13.96  ? 121 TYR B O   1 
ATOM   3082 C  CB  . TYR B 1 121 ? -18.206 10.155  12.432  1.00 12.13  ? 121 TYR B CB  1 
ATOM   3083 C  CG  . TYR B 1 121 ? -19.596 10.577  11.974  1.00 13.07  ? 121 TYR B CG  1 
ATOM   3084 C  CD1 . TYR B 1 121 ? -20.155 10.013  10.839  1.00 14.06  ? 121 TYR B CD1 1 
ATOM   3085 C  CD2 . TYR B 1 121 ? -20.399 11.475  12.691  1.00 14.65  ? 121 TYR B CD2 1 
ATOM   3086 C  CE1 . TYR B 1 121 ? -21.401 10.401  10.365  1.00 14.36  ? 121 TYR B CE1 1 
ATOM   3087 C  CE2 . TYR B 1 121 ? -21.658 11.856  12.214  1.00 18.30  ? 121 TYR B CE2 1 
ATOM   3088 C  CZ  . TYR B 1 121 ? -22.184 11.279  11.063  1.00 16.72  ? 121 TYR B CZ  1 
ATOM   3089 O  OH  . TYR B 1 121 ? -23.418 11.584  10.510  1.00 23.08  ? 121 TYR B OH  1 
ATOM   3090 N  N   . ASN B 1 122 ? -18.831 9.351   15.434  1.00 11.48  ? 122 ASN B N   1 
ATOM   3091 C  CA  . ASN B 1 122 ? -19.694 9.399   16.587  1.00 14.39  ? 122 ASN B CA  1 
ATOM   3092 C  C   . ASN B 1 122 ? -20.850 10.397  16.343  1.00 15.24  ? 122 ASN B C   1 
ATOM   3093 O  O   . ASN B 1 122 ? -20.686 11.637  16.495  1.00 14.56  ? 122 ASN B O   1 
ATOM   3094 C  CB  . ASN B 1 122 ? -18.897 9.612   17.876  1.00 15.08  ? 122 ASN B CB  1 
ATOM   3095 C  CG  . ASN B 1 122 ? -19.825 9.566   19.079  1.00 14.32  ? 122 ASN B CG  1 
ATOM   3096 O  OD1 . ASN B 1 122 ? -21.031 9.763   18.958  1.00 16.63  ? 122 ASN B OD1 1 
ATOM   3097 N  ND2 . ASN B 1 122 ? -19.279 9.399   20.255  1.00 17.40  ? 122 ASN B ND2 1 
ATOM   3098 N  N   . SER B 1 123 ? -22.012 9.910   15.856  1.00 12.72  ? 123 SER B N   1 
ATOM   3099 C  CA  . SER B 1 123 ? -23.150 10.800  15.498  1.00 12.87  ? 123 SER B CA  1 
ATOM   3100 C  C   . SER B 1 123 ? -23.987 11.150  16.749  1.00 13.87  ? 123 SER B C   1 
ATOM   3101 O  O   . SER B 1 123 ? -24.853 12.015  16.727  1.00 19.00  ? 123 SER B O   1 
ATOM   3102 C  CB  . SER B 1 123 ? -24.002 10.111  14.428  1.00 16.93  ? 123 SER B CB  1 
ATOM   3103 O  OG  . SER B 1 123 ? -24.303 8.787   14.881  1.00 15.41  ? 123 SER B OG  1 
ATOM   3104 N  N   . ASP B 1 124 ? -23.678 10.531  17.903  1.00 17.03  ? 124 ASP B N   1 
ATOM   3105 C  CA  . ASP B 1 124 ? -24.348 10.927  19.141  1.00 16.57  ? 124 ASP B CA  1 
ATOM   3106 C  C   . ASP B 1 124 ? -23.771 12.264  19.584  1.00 19.21  ? 124 ASP B C   1 
ATOM   3107 O  O   . ASP B 1 124 ? -24.505 13.092  20.070  1.00 20.30  ? 124 ASP B O   1 
ATOM   3108 C  CB  . ASP B 1 124 ? -24.102 9.863   20.211  1.00 19.64  ? 124 ASP B CB  1 
ATOM   3109 C  CG  . ASP B 1 124 ? -24.964 8.616   20.055  1.00 21.06  ? 124 ASP B CG  1 
ATOM   3110 O  OD1 . ASP B 1 124 ? -25.920 8.631   19.222  1.00 18.55  ? 124 ASP B OD1 1 
ATOM   3111 O  OD2 . ASP B 1 124 ? -24.698 7.641   20.802  1.00 21.95  ? 124 ASP B OD2 1 
ATOM   3112 N  N   . LEU B 1 125 ? -22.510 12.557  19.236  1.00 20.45  ? 125 LEU B N   1 
ATOM   3113 C  CA  . LEU B 1 125 ? -21.808 13.710  19.791  1.00 20.34  ? 125 LEU B CA  1 
ATOM   3114 C  C   . LEU B 1 125 ? -21.567 14.779  18.743  1.00 21.25  ? 125 LEU B C   1 
ATOM   3115 O  O   . LEU B 1 125 ? -21.429 15.930  19.117  1.00 26.53  ? 125 LEU B O   1 
ATOM   3116 C  CB  . LEU B 1 125 ? -20.451 13.297  20.380  1.00 20.22  ? 125 LEU B CB  1 
ATOM   3117 C  CG  . LEU B 1 125 ? -20.538 12.377  21.583  1.00 18.72  ? 125 LEU B CG  1 
ATOM   3118 C  CD1 . LEU B 1 125 ? -19.159 12.156  22.192  1.00 23.62  ? 125 LEU B CD1 1 
ATOM   3119 C  CD2 . LEU B 1 125 ? -21.461 13.019  22.601  1.00 21.34  ? 125 LEU B CD2 1 
ATOM   3120 N  N   . TYR B 1 126 ? -21.487 14.360  17.474  1.00 20.77  ? 126 TYR B N   1 
ATOM   3121 C  CA  . TYR B 1 126 ? -21.014 15.224  16.396  1.00 20.81  ? 126 TYR B CA  1 
ATOM   3122 C  C   . TYR B 1 126 ? -21.936 15.184  15.190  1.00 21.86  ? 126 TYR B C   1 
ATOM   3123 O  O   . TYR B 1 126 ? -22.481 14.129  14.837  1.00 22.88  ? 126 TYR B O   1 
ATOM   3124 C  CB  . TYR B 1 126 ? -19.625 14.733  15.990  1.00 19.39  ? 126 TYR B CB  1 
ATOM   3125 C  CG  . TYR B 1 126 ? -18.693 14.691  17.164  1.00 18.97  ? 126 TYR B CG  1 
ATOM   3126 C  CD1 . TYR B 1 126 ? -18.554 15.788  18.000  1.00 22.77  ? 126 TYR B CD1 1 
ATOM   3127 C  CD2 . TYR B 1 126 ? -17.969 13.536  17.445  1.00 20.84  ? 126 TYR B CD2 1 
ATOM   3128 C  CE1 . TYR B 1 126 ? -17.768 15.733  19.134  1.00 25.55  ? 126 TYR B CE1 1 
ATOM   3129 C  CE2 . TYR B 1 126 ? -17.165 13.466  18.563  1.00 25.88  ? 126 TYR B CE2 1 
ATOM   3130 C  CZ  . TYR B 1 126 ? -17.032 14.583  19.388  1.00 27.93  ? 126 TYR B CZ  1 
ATOM   3131 O  OH  . TYR B 1 126 ? -16.226 14.524  20.502  1.00 26.81  ? 126 TYR B OH  1 
ATOM   3132 N  N   . PRO B 1 127 ? -22.014 16.316  14.449  1.00 27.40  ? 127 PRO B N   1 
ATOM   3133 C  CA  . PRO B 1 127 ? -22.931 16.432  13.300  1.00 28.29  ? 127 PRO B CA  1 
ATOM   3134 C  C   . PRO B 1 127 ? -22.485 15.737  12.015  1.00 25.68  ? 127 PRO B C   1 
ATOM   3135 O  O   . PRO B 1 127 ? -23.306 15.426  11.136  1.00 34.94  ? 127 PRO B O   1 
ATOM   3136 C  CB  . PRO B 1 127 ? -22.995 17.965  13.090  1.00 33.70  ? 127 PRO B CB  1 
ATOM   3137 C  CG  . PRO B 1 127 ? -21.668 18.484  13.596  1.00 28.66  ? 127 PRO B CG  1 
ATOM   3138 C  CD  . PRO B 1 127 ? -21.347 17.592  14.791  1.00 27.27  ? 127 PRO B CD  1 
ATOM   3139 N  N   . ASP B 1 128 ? -21.173 15.460  11.926  1.00 25.10  ? 128 ASP B N   1 
ATOM   3140 C  CA  . ASP B 1 128 ? -20.603 14.956  10.689  1.00 21.43  ? 128 ASP B CA  1 
ATOM   3141 C  C   . ASP B 1 128 ? -19.243 14.356  11.016  1.00 21.52  ? 128 ASP B C   1 
ATOM   3142 O  O   . ASP B 1 128 ? -18.729 14.561  12.106  1.00 22.78  ? 128 ASP B O   1 
ATOM   3143 C  CB  . ASP B 1 128 ? -20.617 16.008  9.574   1.00 28.49  ? 128 ASP B CB  1 
ATOM   3144 C  CG  . ASP B 1 128 ? -19.690 17.157  9.872   1.00 27.96  ? 128 ASP B CG  1 
ATOM   3145 O  OD1 . ASP B 1 128 ? -19.518 17.457  11.043  1.00 40.88  ? 128 ASP B OD1 1 
ATOM   3146 O  OD2 . ASP B 1 128 ? -19.236 17.770  8.929   1.00 36.20  ? 128 ASP B OD2 1 
ATOM   3147 N  N   . ALA B 1 129 ? -18.702 13.539  10.118  1.00 24.23  ? 129 ALA B N   1 
ATOM   3148 C  CA  . ALA B 1 129 ? -17.379 12.959  10.304  1.00 20.86  ? 129 ALA B CA  1 
ATOM   3149 C  C   . ALA B 1 129 ? -16.289 14.031  10.346  1.00 19.43  ? 129 ALA B C   1 
ATOM   3150 O  O   . ALA B 1 129 ? -15.284 13.884  11.034  1.00 20.39  ? 129 ALA B O   1 
ATOM   3151 C  CB  . ALA B 1 129 ? -17.086 12.011  9.172   1.00 24.76  ? 129 ALA B CB  1 
ATOM   3152 N  N   A SER B 1 130 ? -16.453 15.119  9.590   0.50 19.52  ? 130 SER B N   1 
ATOM   3153 N  N   B SER B 1 130 ? -16.494 15.124  9.607   0.50 19.68  ? 130 SER B N   1 
ATOM   3154 C  CA  A SER B 1 130 ? -15.355 16.080  9.623   0.50 18.40  ? 130 SER B CA  1 
ATOM   3155 C  CA  B SER B 1 130 ? -15.411 16.098  9.550   0.50 19.76  ? 130 SER B CA  1 
ATOM   3156 C  C   A SER B 1 130 ? -15.185 16.612  11.039  0.50 18.77  ? 130 SER B C   1 
ATOM   3157 C  C   B SER B 1 130 ? -15.204 16.761  10.918  0.50 21.29  ? 130 SER B C   1 
ATOM   3158 O  O   A SER B 1 130 ? -14.057 16.656  11.555  0.50 22.54  ? 130 SER B O   1 
ATOM   3159 O  O   B SER B 1 130 ? -14.053 16.974  11.324  0.50 24.87  ? 130 SER B O   1 
ATOM   3160 C  CB  A SER B 1 130 ? -15.546 17.230  8.695   0.50 18.08  ? 130 SER B CB  1 
ATOM   3161 C  CB  B SER B 1 130 ? -15.525 17.079  8.385   0.50 26.25  ? 130 SER B CB  1 
ATOM   3162 O  OG  A SER B 1 130 ? -14.458 18.140  8.774   0.50 22.86  ? 130 SER B OG  1 
ATOM   3163 O  OG  B SER B 1 130 ? -16.858 17.541  8.242   0.50 34.74  ? 130 SER B OG  1 
ATOM   3164 N  N   . THR B 1 131 ? -16.298 17.051  11.652  1.00 20.75  ? 131 THR B N   1 
ATOM   3165 C  CA  . THR B 1 131 ? -16.182 17.583  13.019  1.00 24.98  ? 131 THR B CA  1 
ATOM   3166 C  C   . THR B 1 131 ? -15.564 16.545  13.982  1.00 18.74  ? 131 THR B C   1 
ATOM   3167 O  O   . THR B 1 131 ? -14.755 16.851  14.846  1.00 21.12  ? 131 THR B O   1 
ATOM   3168 C  CB  . THR B 1 131 ? -17.570 17.951  13.582  1.00 25.79  ? 131 THR B CB  1 
ATOM   3169 O  OG1 . THR B 1 131 ? -18.076 19.079  12.856  1.00 27.38  ? 131 THR B OG1 1 
ATOM   3170 C  CG2 . THR B 1 131 ? -17.580 18.189  15.090  1.00 23.01  ? 131 THR B CG2 1 
ATOM   3171 N  N   . ALA B 1 132 ? -16.000 15.287  13.845  1.00 19.18  ? 132 ALA B N   1 
ATOM   3172 C  CA  . ALA B 1 132 ? -15.700 14.150  14.720  1.00 18.77  ? 132 ALA B CA  1 
ATOM   3173 C  C   . ALA B 1 132 ? -14.213 13.823  14.637  1.00 19.24  ? 132 ALA B C   1 
ATOM   3174 O  O   . ALA B 1 132 ? -13.636 13.267  15.601  1.00 18.10  ? 132 ALA B O   1 
ATOM   3175 C  CB  . ALA B 1 132 ? -16.539 12.944  14.289  1.00 15.26  ? 132 ALA B CB  1 
ATOM   3176 N  N   . SER B 1 133 ? -13.669 14.055  13.424  1.00 18.65  ? 133 SER B N   1 
ATOM   3177 C  CA  . SER B 1 133 ? -12.316 13.598  13.078  1.00 16.53  ? 133 SER B CA  1 
ATOM   3178 C  C   . SER B 1 133 ? -11.278 14.308  13.954  1.00 23.27  ? 133 SER B C   1 
ATOM   3179 O  O   . SER B 1 133 ? -10.145 13.812  14.019  1.00 21.22  ? 133 SER B O   1 
ATOM   3180 C  CB  . SER B 1 133 ? -11.963 13.801  11.596  1.00 20.09  ? 133 SER B CB  1 
ATOM   3181 O  OG  . SER B 1 133 ? -11.837 15.186  11.249  1.00 24.27  ? 133 SER B OG  1 
ATOM   3182 N  N   . ASN B 1 134 ? -11.640 15.457  14.608  1.00 24.45  ? 134 ASN B N   1 
ATOM   3183 C  CA  . ASN B 1 134 ? -10.735 16.191  15.491  1.00 26.20  ? 134 ASN B CA  1 
ATOM   3184 C  C   . ASN B 1 134 ? -10.871 15.823  16.957  1.00 23.97  ? 134 ASN B C   1 
ATOM   3185 O  O   . ASN B 1 134 ? -10.315 16.518  17.785  1.00 32.90  ? 134 ASN B O   1 
ATOM   3186 C  CB  . ASN B 1 134 ? -11.020 17.698  15.350  1.00 31.06  ? 134 ASN B CB  1 
ATOM   3187 C  CG  . ASN B 1 134 ? -10.704 18.021  13.918  1.00 27.75  ? 134 ASN B CG  1 
ATOM   3188 O  OD1 . ASN B 1 134 ? -9.677  17.564  13.452  1.00 28.64  ? 134 ASN B OD1 1 
ATOM   3189 N  ND2 . ASN B 1 134 ? -11.626 18.639  13.196  1.00 41.04  ? 134 ASN B ND2 1 
ATOM   3190 N  N   . LYS B 1 135 ? -11.647 14.796  17.289  1.00 23.86  ? 135 LYS B N   1 
ATOM   3191 C  CA  . LYS B 1 135 ? -11.938 14.557  18.701  1.00 24.86  ? 135 LYS B CA  1 
ATOM   3192 C  C   . LYS B 1 135 ? -11.535 13.136  19.032  1.00 20.78  ? 135 LYS B C   1 
ATOM   3193 O  O   . LYS B 1 135 ? -11.514 12.297  18.123  1.00 19.09  ? 135 LYS B O   1 
ATOM   3194 C  CB  . LYS B 1 135 ? -13.423 14.645  19.077  1.00 34.07  ? 135 LYS B CB  1 
ATOM   3195 N  N   . SER B 1 136 ? -11.235 12.907  20.329  1.00 25.18  ? 136 SER B N   1 
ATOM   3196 C  CA  . SER B 1 136 ? -10.710 11.614  20.747  1.00 26.03  ? 136 SER B CA  1 
ATOM   3197 C  C   . SER B 1 136 ? -11.802 10.592  20.444  1.00 20.83  ? 136 SER B C   1 
ATOM   3198 O  O   . SER B 1 136 ? -12.969 10.863  20.754  1.00 26.85  ? 136 SER B O   1 
ATOM   3199 C  CB  . SER B 1 136 ? -10.331 11.577  22.213  1.00 34.55  ? 136 SER B CB  1 
ATOM   3200 O  OG  . SER B 1 136 ? -11.490 11.454  23.058  1.00 48.92  ? 136 SER B OG  1 
ATOM   3201 N  N   . GLU B 1 137 ? -11.447 9.491   19.740  1.00 20.75  ? 137 GLU B N   1 
ATOM   3202 C  CA  . GLU B 1 137 ? -12.428 8.448   19.427  1.00 20.29  ? 137 GLU B CA  1 
ATOM   3203 C  C   . GLU B 1 137 ? -13.627 9.009   18.661  1.00 17.41  ? 137 GLU B C   1 
ATOM   3204 O  O   . GLU B 1 137 ? -14.743 8.466   18.756  1.00 21.18  ? 137 GLU B O   1 
ATOM   3205 C  CB  . GLU B 1 137 ? -12.972 7.781   20.707  1.00 23.84  ? 137 GLU B CB  1 
ATOM   3206 C  CG  . GLU B 1 137 ? -11.911 7.299   21.711  1.00 29.00  ? 137 GLU B CG  1 
ATOM   3207 N  N   . GLY B 1 138 ? -13.444 10.100  17.905  1.00 17.92  ? 138 GLY B N   1 
ATOM   3208 C  CA  . GLY B 1 138 ? -14.533 10.660  17.112  1.00 14.75  ? 138 GLY B CA  1 
ATOM   3209 C  C   . GLY B 1 138 ? -14.871 9.702   15.959  1.00 13.24  ? 138 GLY B C   1 
ATOM   3210 O  O   . GLY B 1 138 ? -15.961 9.775   15.410  1.00 14.95  ? 138 GLY B O   1 
ATOM   3211 N  N   . LEU B 1 139 ? -13.900 8.852   15.510  1.00 10.95  ? 139 LEU B N   1 
ATOM   3212 C  CA  . LEU B 1 139 ? -14.082 7.982   14.359  1.00 7.57   ? 139 LEU B CA  1 
ATOM   3213 C  C   . LEU B 1 139 ? -13.912 6.546   14.799  1.00 9.14   ? 139 LEU B C   1 
ATOM   3214 O  O   . LEU B 1 139 ? -13.167 6.264   15.713  1.00 11.33  ? 139 LEU B O   1 
ATOM   3215 C  CB  . LEU B 1 139 ? -13.065 8.317   13.256  1.00 10.50  ? 139 LEU B CB  1 
ATOM   3216 C  CG  . LEU B 1 139 ? -13.093 9.761   12.766  1.00 12.46  ? 139 LEU B CG  1 
ATOM   3217 C  CD1 . LEU B 1 139 ? -12.023 9.919   11.716  1.00 14.50  ? 139 LEU B CD1 1 
ATOM   3218 C  CD2 . LEU B 1 139 ? -14.462 10.047  12.153  1.00 14.36  ? 139 LEU B CD2 1 
ATOM   3219 N  N   . ALA B 1 140 ? -14.647 5.684   14.120  1.00 10.16  ? 140 ALA B N   1 
ATOM   3220 C  CA  . ALA B 1 140 ? -14.418 4.231   14.258  1.00 9.69   ? 140 ALA B CA  1 
ATOM   3221 C  C   . ALA B 1 140 ? -14.340 3.641   12.868  1.00 8.40   ? 140 ALA B C   1 
ATOM   3222 O  O   . ALA B 1 140 ? -15.251 3.909   12.059  1.00 10.37  ? 140 ALA B O   1 
ATOM   3223 C  CB  . ALA B 1 140 ? -15.567 3.593   15.008  1.00 10.82  ? 140 ALA B CB  1 
ATOM   3224 N  N   . VAL B 1 141 ? -13.283 2.821   12.608  1.00 8.46   ? 141 VAL B N   1 
ATOM   3225 C  CA  . VAL B 1 141 ? -13.182 2.239   11.290  1.00 7.69   ? 141 VAL B CA  1 
ATOM   3226 C  C   . VAL B 1 141 ? -13.304 0.727   11.467  1.00 7.81   ? 141 VAL B C   1 
ATOM   3227 O  O   . VAL B 1 141 ? -12.690 0.169   12.405  1.00 8.26   ? 141 VAL B O   1 
ATOM   3228 C  CB  . VAL B 1 141 ? -11.836 2.642   10.665  1.00 7.96   ? 141 VAL B CB  1 
ATOM   3229 C  CG1 . VAL B 1 141 ? -11.647 1.986   9.293   1.00 10.73  ? 141 VAL B CG1 1 
ATOM   3230 C  CG2 . VAL B 1 141 ? -11.705 4.160   10.514  1.00 11.41  ? 141 VAL B CG2 1 
ATOM   3231 N  N   . LEU B 1 142 ? -14.029 0.118   10.536  1.00 7.77   ? 142 LEU B N   1 
ATOM   3232 C  CA  . LEU B 1 142 ? -13.937 -1.346  10.424  1.00 7.00   ? 142 LEU B CA  1 
ATOM   3233 C  C   . LEU B 1 142 ? -13.030 -1.672  9.259   1.00 7.18   ? 142 LEU B C   1 
ATOM   3234 O  O   . LEU B 1 142 ? -13.167 -1.148  8.141   1.00 8.85   ? 142 LEU B O   1 
ATOM   3235 C  CB  . LEU B 1 142 ? -15.319 -1.925  10.096  1.00 8.72   ? 142 LEU B CB  1 
ATOM   3236 C  CG  . LEU B 1 142 ? -16.462 -1.630  11.066  1.00 9.41   ? 142 LEU B CG  1 
ATOM   3237 C  CD1 . LEU B 1 142 ? -17.767 -2.268  10.581  1.00 11.38  ? 142 LEU B CD1 1 
ATOM   3238 C  CD2 . LEU B 1 142 ? -16.140 -2.068  12.491  1.00 11.84  ? 142 LEU B CD2 1 
ATOM   3239 N  N   . ALA B 1 143 ? -12.007 -2.515  9.540   1.00 7.57   ? 143 ALA B N   1 
ATOM   3240 C  CA  . ALA B 1 143 ? -10.996 -2.884  8.549   1.00 8.29   ? 143 ALA B CA  1 
ATOM   3241 C  C   . ALA B 1 143 ? -11.190 -4.364  8.200   1.00 7.89   ? 143 ALA B C   1 
ATOM   3242 O  O   . ALA B 1 143 ? -11.242 -5.213  9.116   1.00 8.12   ? 143 ALA B O   1 
ATOM   3243 C  CB  . ALA B 1 143 ? -9.559  -2.682  9.033   1.00 8.40   ? 143 ALA B CB  1 
ATOM   3244 N  N   . VAL B 1 144 ? -11.268 -4.599  6.898   1.00 6.57   ? 144 VAL B N   1 
ATOM   3245 C  CA  . VAL B 1 144 ? -11.339 -6.010  6.411   1.00 7.22   ? 144 VAL B CA  1 
ATOM   3246 C  C   . VAL B 1 144 ? -10.083 -6.233  5.604   1.00 7.54   ? 144 VAL B C   1 
ATOM   3247 O  O   . VAL B 1 144 ? -9.770  -5.575  4.601   1.00 7.63   ? 144 VAL B O   1 
ATOM   3248 C  CB  . VAL B 1 144 ? -12.582 -6.218  5.521   1.00 7.35   ? 144 VAL B CB  1 
ATOM   3249 C  CG1 . VAL B 1 144 ? -12.631 -7.723  5.027   1.00 10.26  ? 144 VAL B CG1 1 
ATOM   3250 C  CG2 . VAL B 1 144 ? -13.902 -5.873  6.209   1.00 9.07   ? 144 VAL B CG2 1 
ATOM   3251 N  N   . LEU B 1 145 ? -9.353  -7.295  6.013   1.00 8.27   ? 145 LEU B N   1 
ATOM   3252 C  CA  . LEU B 1 145 ? -8.170  -7.721  5.264   1.00 7.87   ? 145 LEU B CA  1 
ATOM   3253 C  C   . LEU B 1 145 ? -8.620  -8.549  4.042   1.00 7.17   ? 145 LEU B C   1 
ATOM   3254 O  O   . LEU B 1 145 ? -9.571  -9.327  4.137   1.00 8.02   ? 145 LEU B O   1 
ATOM   3255 C  CB  . LEU B 1 145 ? -7.291  -8.581  6.187   1.00 8.59   ? 145 LEU B CB  1 
ATOM   3256 C  CG  . LEU B 1 145 ? -6.750  -7.869  7.423   1.00 9.68   ? 145 LEU B CG  1 
ATOM   3257 C  CD1 . LEU B 1 145 ? -6.142  -8.854  8.436   1.00 12.10  ? 145 LEU B CD1 1 
ATOM   3258 C  CD2 . LEU B 1 145 ? -5.715  -6.822  7.010   1.00 15.22  ? 145 LEU B CD2 1 
ATOM   3259 N  N   . ILE B 1 146 ? -7.954  -8.363  2.899   1.00 8.10   ? 146 ILE B N   1 
ATOM   3260 C  CA  . ILE B 1 146 ? -8.385  -8.958  1.633   1.00 8.22   ? 146 ILE B CA  1 
ATOM   3261 C  C   . ILE B 1 146 ? -7.229  -9.791  1.111   1.00 7.21   ? 146 ILE B C   1 
ATOM   3262 O  O   . ILE B 1 146 ? -6.102  -9.282  0.966   1.00 8.92   ? 146 ILE B O   1 
ATOM   3263 C  CB  . ILE B 1 146 ? -8.769  -7.854  0.598   1.00 8.25   ? 146 ILE B CB  1 
ATOM   3264 C  CG1 . ILE B 1 146 ? -9.967  -7.077  1.115   1.00 10.01  ? 146 ILE B CG1 1 
ATOM   3265 C  CG2 . ILE B 1 146 ? -9.145  -8.574  -0.730  1.00 10.13  ? 146 ILE B CG2 1 
ATOM   3266 C  CD1 . ILE B 1 146 ? -10.242 -5.790  0.304   1.00 11.04  ? 146 ILE B CD1 1 
ATOM   3267 N  N   . GLU B 1 147 ? -7.499  -11.075 0.825   1.00 8.46   ? 147 GLU B N   1 
ATOM   3268 C  CA  . GLU B 1 147 ? -6.471  -11.962 0.273   1.00 9.59   ? 147 GLU B CA  1 
ATOM   3269 C  C   . GLU B 1 147 ? -6.892  -12.368 -1.144  1.00 8.48   ? 147 GLU B C   1 
ATOM   3270 O  O   . GLU B 1 147 ? -8.076  -12.382 -1.481  1.00 8.92   ? 147 GLU B O   1 
ATOM   3271 C  CB  . GLU B 1 147 ? -6.231  -13.176 1.200   1.00 14.13  ? 147 GLU B CB  1 
ATOM   3272 C  CG  . GLU B 1 147 ? -7.379  -14.140 1.250   1.00 21.91  ? 147 GLU B CG  1 
ATOM   3273 C  CD  . GLU B 1 147 ? -7.142  -15.313 2.217   1.00 29.25  ? 147 GLU B CD  1 
ATOM   3274 O  OE1 . GLU B 1 147 ? -6.126  -15.262 2.937   1.00 23.78  ? 147 GLU B OE1 1 
ATOM   3275 O  OE2 . GLU B 1 147 ? -7.964  -16.309 2.224   1.00 31.95  ? 147 GLU B OE2 1 
ATOM   3276 N  N   . MET B 1 148 ? -5.905  -12.690 -1.979  1.00 10.12  ? 148 MET B N   1 
ATOM   3277 C  CA  . MET B 1 148 ? -6.192  -13.232 -3.321  1.00 9.52   ? 148 MET B CA  1 
ATOM   3278 C  C   . MET B 1 148 ? -6.821  -14.627 -3.181  1.00 9.00   ? 148 MET B C   1 
ATOM   3279 O  O   . MET B 1 148 ? -6.231  -15.511 -2.542  1.00 10.57  ? 148 MET B O   1 
ATOM   3280 C  CB  . MET B 1 148 ? -4.889  -13.343 -4.114  1.00 9.06   ? 148 MET B CB  1 
ATOM   3281 C  CG  . MET B 1 148 ? -5.134  -13.775 -5.529  1.00 11.33  ? 148 MET B CG  1 
ATOM   3282 S  SD  . MET B 1 148 ? -3.558  -13.862 -6.485  1.00 12.99  ? 148 MET B SD  1 
ATOM   3283 C  CE  . MET B 1 148 ? -3.190  -12.138 -6.526  1.00 18.66  ? 148 MET B CE  1 
ATOM   3284 N  N   . GLY B 1 149 ? -7.966  -14.798 -3.833  1.00 8.97   ? 149 GLY B N   1 
ATOM   3285 C  CA  . GLY B 1 149 ? -8.654  -16.103 -3.712  1.00 10.05  ? 149 GLY B CA  1 
ATOM   3286 C  C   . GLY B 1 149 ? -9.760  -16.161 -4.737  1.00 9.01   ? 149 GLY B C   1 
ATOM   3287 O  O   . GLY B 1 149 ? -9.546  -15.865 -5.922  1.00 9.04   ? 149 GLY B O   1 
ATOM   3288 N  N   . SER B 1 150 ? -10.949 -16.523 -4.269  1.00 10.25  ? 150 SER B N   1 
ATOM   3289 C  CA  . SER B 1 150 ? -12.102 -16.647 -5.128  1.00 8.60   ? 150 SER B CA  1 
ATOM   3290 C  C   . SER B 1 150 ? -12.628 -15.276 -5.576  1.00 9.13   ? 150 SER B C   1 
ATOM   3291 O  O   . SER B 1 150 ? -12.561 -14.258 -4.843  1.00 8.81   ? 150 SER B O   1 
ATOM   3292 C  CB  . SER B 1 150 ? -13.249 -17.393 -4.428  1.00 8.04   ? 150 SER B CB  1 
ATOM   3293 O  OG  . SER B 1 150 ? -12.847 -18.785 -4.273  1.00 10.22  ? 150 SER B OG  1 
ATOM   3294 N  N   . PHE B 1 151 ? -13.242 -15.251 -6.769  1.00 9.45   ? 151 PHE B N   1 
ATOM   3295 C  CA  . PHE B 1 151 ? -13.975 -14.050 -7.219  1.00 9.96   ? 151 PHE B CA  1 
ATOM   3296 C  C   . PHE B 1 151 ? -15.030 -13.733 -6.200  1.00 11.16  ? 151 PHE B C   1 
ATOM   3297 O  O   . PHE B 1 151 ? -15.746 -14.588 -5.679  1.00 11.61  ? 151 PHE B O   1 
ATOM   3298 C  CB  . PHE B 1 151 ? -14.650 -14.387 -8.558  1.00 10.83  ? 151 PHE B CB  1 
ATOM   3299 C  CG  . PHE B 1 151 ? -15.458 -13.241 -9.122  1.00 10.70  ? 151 PHE B CG  1 
ATOM   3300 C  CD1 . PHE B 1 151 ? -14.809 -12.211 -9.791  1.00 10.98  ? 151 PHE B CD1 1 
ATOM   3301 C  CD2 . PHE B 1 151 ? -16.847 -13.216 -9.011  1.00 10.57  ? 151 PHE B CD2 1 
ATOM   3302 C  CE1 . PHE B 1 151 ? -15.530 -11.117 -10.260 1.00 13.35  ? 151 PHE B CE1 1 
ATOM   3303 C  CE2 . PHE B 1 151 ? -17.556 -12.103 -9.440  1.00 12.65  ? 151 PHE B CE2 1 
ATOM   3304 C  CZ  . PHE B 1 151 ? -16.901 -11.086 -10.105 1.00 12.57  ? 151 PHE B CZ  1 
ATOM   3305 N  N   . ASN B 1 152 ? -15.206 -12.412 -5.930  1.00 8.92   ? 152 ASN B N   1 
ATOM   3306 C  CA  . ASN B 1 152 ? -16.136 -11.984 -4.935  1.00 8.67   ? 152 ASN B CA  1 
ATOM   3307 C  C   . ASN B 1 152 ? -17.203 -11.115 -5.605  1.00 9.37   ? 152 ASN B C   1 
ATOM   3308 O  O   . ASN B 1 152 ? -16.972 -9.888  -5.853  1.00 9.65   ? 152 ASN B O   1 
ATOM   3309 C  CB  . ASN B 1 152 ? -15.379 -11.261 -3.802  1.00 8.76   ? 152 ASN B CB  1 
ATOM   3310 C  CG  . ASN B 1 152 ? -16.198 -10.973 -2.579  1.00 8.20   ? 152 ASN B CG  1 
ATOM   3311 O  OD1 . ASN B 1 152 ? -17.329 -10.478 -2.674  1.00 9.22   ? 152 ASN B OD1 1 
ATOM   3312 N  ND2 . ASN B 1 152 ? -15.648 -11.253 -1.412  1.00 9.65   ? 152 ASN B ND2 1 
ATOM   3313 N  N   . PRO B 1 153 ? -18.424 -11.590 -5.824  1.00 10.34  ? 153 PRO B N   1 
ATOM   3314 C  CA  . PRO B 1 153 ? -19.469 -10.807 -6.485  1.00 10.01  ? 153 PRO B CA  1 
ATOM   3315 C  C   . PRO B 1 153 ? -19.815 -9.568  -5.663  1.00 11.40  ? 153 PRO B C   1 
ATOM   3316 O  O   . PRO B 1 153 ? -20.170 -8.572  -6.273  1.00 12.85  ? 153 PRO B O   1 
ATOM   3317 C  CB  . PRO B 1 153 ? -20.631 -11.785 -6.522  1.00 12.07  ? 153 PRO B CB  1 
ATOM   3318 C  CG  . PRO B 1 153 ? -20.004 -13.131 -6.556  1.00 15.42  ? 153 PRO B CG  1 
ATOM   3319 C  CD  . PRO B 1 153 ? -18.816 -13.019 -5.627  1.00 11.76  ? 153 PRO B CD  1 
ATOM   3320 N  N   . SER B 1 154 ? -19.726 -9.612  -4.332  1.00 10.25  ? 154 SER B N   1 
ATOM   3321 C  CA  . SER B 1 154 ? -20.118 -8.410  -3.560  1.00 8.90   ? 154 SER B CA  1 
ATOM   3322 C  C   . SER B 1 154 ? -19.123 -7.287  -3.778  1.00 9.81   ? 154 SER B C   1 
ATOM   3323 O  O   . SER B 1 154 ? -19.503 -6.109  -3.898  1.00 10.57  ? 154 SER B O   1 
ATOM   3324 C  CB  . SER B 1 154 ? -20.317 -8.723  -2.071  1.00 12.09  ? 154 SER B CB  1 
ATOM   3325 O  OG  . SER B 1 154 ? -21.225 -9.817  -1.958  1.00 15.37  ? 154 SER B OG  1 
ATOM   3326 N  N   . TYR B 1 155 ? -17.818 -7.573  -3.634  1.00 8.61   ? 155 TYR B N   1 
ATOM   3327 C  CA  . TYR B 1 155 ? -16.843 -6.521  -3.919  1.00 8.39   ? 155 TYR B CA  1 
ATOM   3328 C  C   . TYR B 1 155 ? -16.970 -6.021  -5.340  1.00 8.66   ? 155 TYR B C   1 
ATOM   3329 O  O   . TYR B 1 155 ? -16.734 -4.834  -5.586  1.00 9.78   ? 155 TYR B O   1 
ATOM   3330 C  CB  . TYR B 1 155 ? -15.391 -6.941  -3.578  1.00 8.70   ? 155 TYR B CB  1 
ATOM   3331 C  CG  . TYR B 1 155 ? -15.067 -6.881  -2.121  1.00 8.50   ? 155 TYR B CG  1 
ATOM   3332 C  CD1 . TYR B 1 155 ? -15.524 -7.829  -1.221  1.00 9.55   ? 155 TYR B CD1 1 
ATOM   3333 C  CD2 . TYR B 1 155 ? -14.349 -5.786  -1.619  1.00 10.25  ? 155 TYR B CD2 1 
ATOM   3334 C  CE1 . TYR B 1 155 ? -15.252 -7.750  0.144   1.00 10.18  ? 155 TYR B CE1 1 
ATOM   3335 C  CE2 . TYR B 1 155 ? -14.041 -5.707  -0.264  1.00 9.19   ? 155 TYR B CE2 1 
ATOM   3336 C  CZ  . TYR B 1 155 ? -14.571 -6.643  0.635   1.00 10.14  ? 155 TYR B CZ  1 
ATOM   3337 O  OH  . TYR B 1 155 ? -14.230 -6.551  1.950   1.00 8.74   ? 155 TYR B OH  1 
ATOM   3338 N  N   . ASP B 1 156 ? -17.391 -6.842  -6.288  1.00 8.42   ? 156 ASP B N   1 
ATOM   3339 C  CA  . ASP B 1 156 ? -17.543 -6.421  -7.671  1.00 9.33   ? 156 ASP B CA  1 
ATOM   3340 C  C   . ASP B 1 156 ? -18.621 -5.353  -7.798  1.00 8.64   ? 156 ASP B C   1 
ATOM   3341 O  O   . ASP B 1 156 ? -18.618 -4.677  -8.817  1.00 10.35  ? 156 ASP B O   1 
ATOM   3342 C  CB  . ASP B 1 156 ? -17.679 -7.582  -8.677  1.00 10.86  ? 156 ASP B CB  1 
ATOM   3343 C  CG  . ASP B 1 156 ? -16.684 -7.406  -9.832  1.00 12.69  ? 156 ASP B CG  1 
ATOM   3344 O  OD1 . ASP B 1 156 ? -15.437 -7.228  -9.550  1.00 10.99  ? 156 ASP B OD1 1 
ATOM   3345 O  OD2 . ASP B 1 156 ? -17.154 -7.338  -10.965 1.00 16.14  ? 156 ASP B OD2 1 
ATOM   3346 N  N   . LYS B 1 157 ? -19.567 -5.261  -6.849  1.00 9.74   ? 157 LYS B N   1 
ATOM   3347 C  CA  . LYS B 1 157 ? -20.582 -4.226  -6.865  1.00 11.29  ? 157 LYS B CA  1 
ATOM   3348 C  C   . LYS B 1 157 ? -19.920 -2.859  -6.686  1.00 11.36  ? 157 LYS B C   1 
ATOM   3349 O  O   . LYS B 1 157 ? -20.461 -1.871  -7.218  1.00 15.46  ? 157 LYS B O   1 
ATOM   3350 C  CB  . LYS B 1 157 ? -21.593 -4.509  -5.749  1.00 10.09  ? 157 LYS B CB  1 
ATOM   3351 C  CG  . LYS B 1 157 ? -22.485 -5.714  -6.063  1.00 12.19  ? 157 LYS B CG  1 
ATOM   3352 C  CD  . LYS B 1 157 ? -23.487 -6.095  -4.960  1.00 13.78  ? 157 LYS B CD  1 
ATOM   3353 C  CE  . LYS B 1 157 ? -23.952 -7.532  -5.165  1.00 16.70  ? 157 LYS B CE  1 
ATOM   3354 N  NZ  . LYS B 1 157 ? -24.898 -7.992  -4.095  1.00 18.44  ? 157 LYS B NZ  1 
ATOM   3355 N  N   . ILE B 1 158 ? -18.707 -2.780  -6.080  1.00 9.69   ? 158 ILE B N   1 
ATOM   3356 C  CA  . ILE B 1 158 ? -17.911 -1.544  -6.116  1.00 10.67  ? 158 ILE B CA  1 
ATOM   3357 C  C   . ILE B 1 158 ? -16.971 -1.492  -7.313  1.00 10.50  ? 158 ILE B C   1 
ATOM   3358 O  O   . ILE B 1 158 ? -16.965 -0.526  -8.064  1.00 11.63  ? 158 ILE B O   1 
ATOM   3359 C  CB  . ILE B 1 158 ? -17.050 -1.448  -4.843  1.00 9.78   ? 158 ILE B CB  1 
ATOM   3360 C  CG1 . ILE B 1 158 ? -17.966 -1.392  -3.619  1.00 12.77  ? 158 ILE B CG1 1 
ATOM   3361 C  CG2 . ILE B 1 158 ? -16.151 -0.211  -4.917  1.00 14.37  ? 158 ILE B CG2 1 
ATOM   3362 C  CD1 . ILE B 1 158 ? -17.254 -1.728  -2.298  1.00 14.56  ? 158 ILE B CD1 1 
ATOM   3363 N  N   . PHE B 1 159 ? -16.249 -2.602  -7.578  1.00 10.48  ? 159 PHE B N   1 
ATOM   3364 C  CA  . PHE B 1 159 ? -15.152 -2.548  -8.543  1.00 11.48  ? 159 PHE B CA  1 
ATOM   3365 C  C   . PHE B 1 159 ? -15.687 -2.280  -9.966  1.00 11.14  ? 159 PHE B C   1 
ATOM   3366 O  O   . PHE B 1 159 ? -15.030 -1.639  -10.790 1.00 17.00  ? 159 PHE B O   1 
ATOM   3367 C  CB  . PHE B 1 159 ? -14.387 -3.874  -8.586  1.00 12.43  ? 159 PHE B CB  1 
ATOM   3368 C  CG  . PHE B 1 159 ? -13.704 -4.255  -7.273  1.00 10.75  ? 159 PHE B CG  1 
ATOM   3369 C  CD1 . PHE B 1 159 ? -13.367 -3.244  -6.346  1.00 13.99  ? 159 PHE B CD1 1 
ATOM   3370 C  CD2 . PHE B 1 159 ? -13.351 -5.589  -7.000  1.00 12.07  ? 159 PHE B CD2 1 
ATOM   3371 C  CE1 . PHE B 1 159 ? -12.672 -3.562  -5.159  1.00 11.92  ? 159 PHE B CE1 1 
ATOM   3372 C  CE2 . PHE B 1 159 ? -12.658 -5.872  -5.831  1.00 13.07  ? 159 PHE B CE2 1 
ATOM   3373 C  CZ  . PHE B 1 159 ? -12.359 -4.889  -4.921  1.00 13.99  ? 159 PHE B CZ  1 
ATOM   3374 N  N   . SER B 1 160 ? -16.901 -2.742  -10.274 1.00 11.72  ? 160 SER B N   1 
ATOM   3375 C  CA  . SER B 1 160 ? -17.500 -2.590  -11.604 1.00 15.73  ? 160 SER B CA  1 
ATOM   3376 C  C   . SER B 1 160 ? -17.754 -1.133  -11.981 1.00 14.37  ? 160 SER B C   1 
ATOM   3377 O  O   . SER B 1 160 ? -17.967 -0.862  -13.167 1.00 18.40  ? 160 SER B O   1 
ATOM   3378 C  CB  . SER B 1 160 ? -18.736 -3.500  -11.764 1.00 18.28  ? 160 SER B CB  1 
ATOM   3379 O  OG  . SER B 1 160 ? -19.787 -3.100  -10.886 1.00 19.80  ? 160 SER B OG  1 
ATOM   3380 N  N   . HIS B 1 161 ? -17.686 -0.201  -10.997 1.00 14.08  ? 161 HIS B N   1 
ATOM   3381 C  CA  . HIS B 1 161 ? -17.951 1.214   -11.267 1.00 15.58  ? 161 HIS B CA  1 
ATOM   3382 C  C   . HIS B 1 161 ? -16.735 2.112   -11.325 1.00 16.47  ? 161 HIS B C   1 
ATOM   3383 O  O   . HIS B 1 161 ? -16.843 3.327   -11.610 1.00 16.70  ? 161 HIS B O   1 
ATOM   3384 C  CB  . HIS B 1 161 ? -18.864 1.824   -10.217 1.00 15.52  ? 161 HIS B CB  1 
ATOM   3385 C  CG  . HIS B 1 161 ? -20.215 1.256   -10.321 1.00 15.51  ? 161 HIS B CG  1 
ATOM   3386 N  ND1 . HIS B 1 161 ? -21.092 1.699   -11.273 1.00 20.63  ? 161 HIS B ND1 1 
ATOM   3387 C  CD2 . HIS B 1 161 ? -20.797 0.233   -9.680  1.00 18.01  ? 161 HIS B CD2 1 
ATOM   3388 C  CE1 . HIS B 1 161 ? -22.186 0.973   -11.221 1.00 21.98  ? 161 HIS B CE1 1 
ATOM   3389 N  NE2 . HIS B 1 161 ? -22.026 0.090   -10.228 1.00 19.17  ? 161 HIS B NE2 1 
ATOM   3390 N  N   . LEU B 1 162 ? -15.571 1.546   -11.026 1.00 15.13  ? 162 LEU B N   1 
ATOM   3391 C  CA  . LEU B 1 162 ? -14.430 2.462   -10.949 1.00 15.08  ? 162 LEU B CA  1 
ATOM   3392 C  C   . LEU B 1 162 ? -14.124 3.213   -12.251 1.00 18.03  ? 162 LEU B C   1 
ATOM   3393 O  O   . LEU B 1 162 ? -13.480 4.250   -12.194 1.00 16.73  ? 162 LEU B O   1 
ATOM   3394 C  CB  . LEU B 1 162 ? -13.183 1.747   -10.398 1.00 20.01  ? 162 LEU B CB  1 
ATOM   3395 C  CG  . LEU B 1 162 ? -13.361 1.101   -9.015  1.00 16.45  ? 162 LEU B CG  1 
ATOM   3396 C  CD1 . LEU B 1 162 ? -12.223 0.179   -8.624  1.00 21.05  ? 162 LEU B CD1 1 
ATOM   3397 C  CD2 . LEU B 1 162 ? -13.681 2.125   -7.912  1.00 17.40  ? 162 LEU B CD2 1 
ATOM   3398 N  N   . GLN B 1 163 ? -14.522 2.764   -13.445 1.00 19.94  ? 163 GLN B N   1 
ATOM   3399 C  CA  . GLN B 1 163 ? -14.090 3.525   -14.625 1.00 16.66  ? 163 GLN B CA  1 
ATOM   3400 C  C   . GLN B 1 163 ? -14.733 4.911   -14.718 1.00 18.29  ? 163 GLN B C   1 
ATOM   3401 O  O   . GLN B 1 163 ? -14.203 5.806   -15.397 1.00 22.21  ? 163 GLN B O   1 
ATOM   3402 C  CB  . GLN B 1 163 ? -14.328 2.725   -15.918 1.00 22.25  ? 163 GLN B CB  1 
ATOM   3403 C  CG  . GLN B 1 163 ? -15.782 2.351   -16.167 1.00 25.55  ? 163 GLN B CG  1 
ATOM   3404 C  CD  . GLN B 1 163 ? -16.007 1.646   -17.492 1.00 30.01  ? 163 GLN B CD  1 
ATOM   3405 O  OE1 . GLN B 1 163 ? -15.976 0.404   -17.592 1.00 31.21  ? 163 GLN B OE1 1 
ATOM   3406 N  NE2 . GLN B 1 163 ? -16.232 2.456   -18.526 1.00 31.89  ? 163 GLN B NE2 1 
ATOM   3407 N  N   . HIS B 1 164 ? -15.834 5.106   -14.031 1.00 14.58  ? 164 HIS B N   1 
ATOM   3408 C  CA  . HIS B 1 164 ? -16.561 6.370   -14.119 1.00 19.60  ? 164 HIS B CA  1 
ATOM   3409 C  C   . HIS B 1 164 ? -15.872 7.253   -13.136 1.00 17.32  ? 164 HIS B C   1 
ATOM   3410 O  O   . HIS B 1 164 ? -16.254 8.418   -13.043 1.00 18.75  ? 164 HIS B O   1 
ATOM   3411 C  CB  . HIS B 1 164 ? -18.046 6.181   -13.758 1.00 15.75  ? 164 HIS B CB  1 
ATOM   3412 C  CG  . HIS B 1 164 ? -18.663 5.233   -14.721 1.00 18.02  ? 164 HIS B CG  1 
ATOM   3413 N  ND1 . HIS B 1 164 ? -18.720 5.516   -16.088 1.00 22.25  ? 164 HIS B ND1 1 
ATOM   3414 C  CD2 . HIS B 1 164 ? -19.245 4.024   -14.553 1.00 23.29  ? 164 HIS B CD2 1 
ATOM   3415 C  CE1 . HIS B 1 164 ? -19.355 4.539   -16.707 1.00 26.93  ? 164 HIS B CE1 1 
ATOM   3416 N  NE2 . HIS B 1 164 ? -19.656 3.599   -15.799 1.00 26.17  ? 164 HIS B NE2 1 
ATOM   3417 N  N   . VAL B 1 165 ? -14.951 6.632   -12.327 1.00 16.30  ? 165 VAL B N   1 
ATOM   3418 C  CA  . VAL B 1 165 ? -14.218 7.551   -11.484 1.00 14.94  ? 165 VAL B CA  1 
ATOM   3419 C  C   . VAL B 1 165 ? -12.717 7.420   -11.665 1.00 10.13  ? 165 VAL B C   1 
ATOM   3420 O  O   . VAL B 1 165 ? -11.953 7.601   -10.697 1.00 10.69  ? 165 VAL B O   1 
ATOM   3421 C  CB  . VAL B 1 165 ? -14.633 7.402   -10.005 1.00 14.13  ? 165 VAL B CB  1 
ATOM   3422 C  CG1 . VAL B 1 165 ? -16.106 7.747   -9.898  1.00 15.21  ? 165 VAL B CG1 1 
ATOM   3423 C  CG2 . VAL B 1 165 ? -14.362 5.983   -9.448  1.00 12.95  ? 165 VAL B CG2 1 
ATOM   3424 N  N   . LYS B 1 166 ? -12.303 7.096   -12.897 1.00 11.12  ? 166 LYS B N   1 
ATOM   3425 C  CA  . LYS B 1 166 ? -10.905 6.808   -13.160 1.00 11.22  ? 166 LYS B CA  1 
ATOM   3426 C  C   . LYS B 1 166 ? -9.962  7.944   -12.741 1.00 9.78   ? 166 LYS B C   1 
ATOM   3427 O  O   . LYS B 1 166 ? -8.827  7.679   -12.289 1.00 11.97  ? 166 LYS B O   1 
ATOM   3428 C  CB  . LYS B 1 166 ? -10.747 6.556   -14.649 1.00 14.05  ? 166 LYS B CB  1 
ATOM   3429 C  CG  . LYS B 1 166 ? -9.343  6.289   -15.113 1.00 12.33  ? 166 LYS B CG  1 
ATOM   3430 C  CD  . LYS B 1 166 ? -9.303  5.741   -16.538 1.00 18.80  ? 166 LYS B CD  1 
ATOM   3431 C  CE  . LYS B 1 166 ? -7.883  5.396   -16.897 1.00 26.65  ? 166 LYS B CE  1 
ATOM   3432 N  N   . TYR B 1 167 ? -10.403 9.210   -12.875 1.00 9.14   ? 167 TYR B N   1 
ATOM   3433 C  CA  . TYR B 1 167 ? -9.543  10.346  -12.662 1.00 9.57   ? 167 TYR B CA  1 
ATOM   3434 C  C   . TYR B 1 167 ? -10.013 11.155  -11.447 1.00 8.54   ? 167 TYR B C   1 
ATOM   3435 O  O   . TYR B 1 167 ? -11.204 11.226  -11.118 1.00 10.74  ? 167 TYR B O   1 
ATOM   3436 C  CB  . TYR B 1 167 ? -9.493  11.193  -13.944 1.00 10.06  ? 167 TYR B CB  1 
ATOM   3437 C  CG  . TYR B 1 167 ? -9.067  10.423  -15.161 1.00 10.31  ? 167 TYR B CG  1 
ATOM   3438 C  CD1 . TYR B 1 167 ? -7.729  10.073  -15.358 1.00 11.35  ? 167 TYR B CD1 1 
ATOM   3439 C  CD2 . TYR B 1 167 ? -10.010 10.046  -16.129 1.00 11.29  ? 167 TYR B CD2 1 
ATOM   3440 C  CE1 . TYR B 1 167 ? -7.366  9.330   -16.484 1.00 12.49  ? 167 TYR B CE1 1 
ATOM   3441 C  CE2 . TYR B 1 167 ? -9.666  9.269   -17.233 1.00 13.94  ? 167 TYR B CE2 1 
ATOM   3442 C  CZ  . TYR B 1 167 ? -8.326  8.941   -17.426 1.00 13.86  ? 167 TYR B CZ  1 
ATOM   3443 O  OH  . TYR B 1 167 ? -8.011  8.175   -18.527 1.00 15.56  ? 167 TYR B OH  1 
ATOM   3444 N  N   . LYS B 1 168 ? -9.059  11.949  -10.920 1.00 11.33  ? 168 LYS B N   1 
ATOM   3445 C  CA  . LYS B 1 168 ? -9.361  12.954  -9.873  1.00 11.61  ? 168 LYS B CA  1 
ATOM   3446 C  C   . LYS B 1 168 ? -10.491 13.886  -10.313 1.00 12.10  ? 168 LYS B C   1 
ATOM   3447 O  O   . LYS B 1 168 ? -10.499 14.351  -11.454 1.00 14.35  ? 168 LYS B O   1 
ATOM   3448 C  CB  . LYS B 1 168 ? -8.121  13.804  -9.602  1.00 12.66  ? 168 LYS B CB  1 
ATOM   3449 C  CG  . LYS B 1 168 ? -8.258  14.739  -8.432  1.00 14.38  ? 168 LYS B CG  1 
ATOM   3450 C  CD  . LYS B 1 168 ? -7.028  15.607  -8.264  1.00 18.25  ? 168 LYS B CD  1 
ATOM   3451 C  CE  . LYS B 1 168 ? -7.261  16.713  -7.236  1.00 20.49  ? 168 LYS B CE  1 
ATOM   3452 N  NZ  . LYS B 1 168 ? -6.086  17.567  -6.995  1.00 31.11  ? 168 LYS B NZ  1 
ATOM   3453 N  N   . GLY B 1 169 ? -11.436 14.098  -9.410  1.00 14.23  ? 169 GLY B N   1 
ATOM   3454 C  CA  . GLY B 1 169 ? -12.527 15.039  -9.640  1.00 16.64  ? 169 GLY B CA  1 
ATOM   3455 C  C   . GLY B 1 169 ? -13.733 14.416  -10.313 1.00 15.23  ? 169 GLY B C   1 
ATOM   3456 O  O   . GLY B 1 169 ? -14.786 15.041  -10.393 1.00 21.99  ? 169 GLY B O   1 
ATOM   3457 N  N   . GLN B 1 170 ? -13.624 13.117  -10.600 1.00 13.06  ? 170 GLN B N   1 
ATOM   3458 C  CA  . GLN B 1 170 ? -14.764 12.382  -11.126 1.00 13.10  ? 170 GLN B CA  1 
ATOM   3459 C  C   . GLN B 1 170 ? -15.670 11.787  -10.038 1.00 11.71  ? 170 GLN B C   1 
ATOM   3460 O  O   . GLN B 1 170 ? -15.180 11.415  -8.982  1.00 15.64  ? 170 GLN B O   1 
ATOM   3461 C  CB  . GLN B 1 170 ? -14.319 11.385  -12.190 1.00 12.74  ? 170 GLN B CB  1 
ATOM   3462 C  CG  . GLN B 1 170 ? -13.650 12.043  -13.379 1.00 14.35  ? 170 GLN B CG  1 
ATOM   3463 C  CD  . GLN B 1 170 ? -13.283 11.130  -14.522 1.00 14.60  ? 170 GLN B CD  1 
ATOM   3464 O  OE1 . GLN B 1 170 ? -12.929 9.975   -14.330 1.00 15.05  ? 170 GLN B OE1 1 
ATOM   3465 N  NE2 . GLN B 1 170 ? -13.417 11.625  -15.746 1.00 20.16  ? 170 GLN B NE2 1 
ATOM   3466 N  N   . GLU B 1 171 ? -16.950 11.650  -10.377 1.00 14.67  ? 171 GLU B N   1 
ATOM   3467 C  CA  . GLU B 1 171 ? -17.979 11.093  -9.509  1.00 17.50  ? 171 GLU B CA  1 
ATOM   3468 C  C   . GLU B 1 171 ? -18.929 10.192  -10.300 1.00 16.94  ? 171 GLU B C   1 
ATOM   3469 O  O   . GLU B 1 171 ? -19.093 10.326  -11.528 1.00 19.85  ? 171 GLU B O   1 
ATOM   3470 C  CB  . GLU B 1 171 ? -18.771 12.222  -8.840  1.00 24.49  ? 171 GLU B CB  1 
ATOM   3471 C  CG  . GLU B 1 171 ? -17.899 13.116  -7.981  1.00 26.19  ? 171 GLU B CG  1 
ATOM   3472 C  CD  . GLU B 1 171 ? -18.534 14.343  -7.347  1.00 35.08  ? 171 GLU B CD  1 
ATOM   3473 O  OE1 . GLU B 1 171 ? -19.762 14.545  -7.551  1.00 32.54  ? 171 GLU B OE1 1 
ATOM   3474 O  OE2 . GLU B 1 171 ? -17.799 15.090  -6.652  1.00 35.39  ? 171 GLU B OE2 1 
ATOM   3475 N  N   . ALA B 1 172 ? -19.499 9.205   -9.619  1.00 15.37  ? 172 ALA B N   1 
ATOM   3476 C  CA  . ALA B 1 172 ? -20.455 8.320   -10.241 1.00 15.88  ? 172 ALA B CA  1 
ATOM   3477 C  C   . ALA B 1 172 ? -21.382 7.776   -9.158  1.00 13.22  ? 172 ALA B C   1 
ATOM   3478 O  O   . ALA B 1 172 ? -21.078 7.856   -7.976  1.00 17.93  ? 172 ALA B O   1 
ATOM   3479 C  CB  . ALA B 1 172 ? -19.681 7.207   -10.877 1.00 19.02  ? 172 ALA B CB  1 
ATOM   3480 N  N   . PHE B 1 173 ? -22.504 7.221   -9.582  1.00 16.94  ? 173 PHE B N   1 
ATOM   3481 C  CA  . PHE B 1 173 ? -23.461 6.616   -8.667  1.00 15.74  ? 173 PHE B CA  1 
ATOM   3482 C  C   . PHE B 1 173 ? -23.388 5.090   -8.713  1.00 14.91  ? 173 PHE B C   1 
ATOM   3483 O  O   . PHE B 1 173 ? -23.356 4.499   -9.803  1.00 21.01  ? 173 PHE B O   1 
ATOM   3484 C  CB  . PHE B 1 173 ? -24.875 7.151   -8.941  1.00 20.51  ? 173 PHE B CB  1 
ATOM   3485 C  CG  . PHE B 1 173 ? -25.089 8.540   -8.372  1.00 18.18  ? 173 PHE B CG  1 
ATOM   3486 C  CD1 . PHE B 1 173 ? -25.083 8.737   -6.993  1.00 20.69  ? 173 PHE B CD1 1 
ATOM   3487 C  CD2 . PHE B 1 173 ? -25.310 9.644   -9.178  1.00 27.62  ? 173 PHE B CD2 1 
ATOM   3488 C  CE1 . PHE B 1 173 ? -25.270 9.986   -6.426  1.00 23.80  ? 173 PHE B CE1 1 
ATOM   3489 C  CE2 . PHE B 1 173 ? -25.507 10.902  -8.621  1.00 32.79  ? 173 PHE B CE2 1 
ATOM   3490 C  CZ  . PHE B 1 173 ? -25.475 11.071  -7.248  1.00 32.39  ? 173 PHE B CZ  1 
ATOM   3491 N  N   . VAL B 1 174 ? -23.423 4.505   -7.503  1.00 12.61  ? 174 VAL B N   1 
ATOM   3492 C  CA  . VAL B 1 174 ? -23.430 3.061   -7.308  1.00 14.62  ? 174 VAL B CA  1 
ATOM   3493 C  C   . VAL B 1 174 ? -24.792 2.702   -6.719  1.00 16.53  ? 174 VAL B C   1 
ATOM   3494 O  O   . VAL B 1 174 ? -25.158 3.269   -5.696  1.00 17.05  ? 174 VAL B O   1 
ATOM   3495 C  CB  . VAL B 1 174 ? -22.298 2.616   -6.339  1.00 12.71  ? 174 VAL B CB  1 
ATOM   3496 C  CG1 . VAL B 1 174 ? -22.366 1.071   -6.113  1.00 15.20  ? 174 VAL B CG1 1 
ATOM   3497 C  CG2 . VAL B 1 174 ? -20.939 2.939   -6.983  1.00 15.62  ? 174 VAL B CG2 1 
ATOM   3498 N  N   . PRO B 1 175 ? -25.536 1.720   -7.274  1.00 12.83  ? 175 PRO B N   1 
ATOM   3499 C  CA  . PRO B 1 175 ? -26.766 1.298   -6.618  1.00 12.47  ? 175 PRO B CA  1 
ATOM   3500 C  C   . PRO B 1 175 ? -26.466 0.642   -5.253  1.00 11.49  ? 175 PRO B C   1 
ATOM   3501 O  O   . PRO B 1 175 ? -25.421 -0.016  -5.036  1.00 13.00  ? 175 PRO B O   1 
ATOM   3502 C  CB  . PRO B 1 175 ? -27.305 0.184   -7.522  1.00 15.45  ? 175 PRO B CB  1 
ATOM   3503 C  CG  . PRO B 1 175 ? -26.727 0.494   -8.864  1.00 16.22  ? 175 PRO B CG  1 
ATOM   3504 C  CD  . PRO B 1 175 ? -25.313 1.009   -8.538  1.00 15.15  ? 175 PRO B CD  1 
ATOM   3505 N  N   . GLY B 1 176 ? -27.384 0.847   -4.299  1.00 11.98  ? 176 GLY B N   1 
ATOM   3506 C  CA  . GLY B 1 176 ? -27.326 0.248   -2.980  1.00 10.77  ? 176 GLY B CA  1 
ATOM   3507 C  C   . GLY B 1 176 ? -27.135 -1.268  -3.050  1.00 10.32  ? 176 GLY B C   1 
ATOM   3508 O  O   . GLY B 1 176 ? -27.719 -1.915  -3.929  1.00 13.39  ? 176 GLY B O   1 
ATOM   3509 N  N   . PHE B 1 177 ? -26.325 -1.778  -2.116  1.00 10.90  ? 177 PHE B N   1 
ATOM   3510 C  CA  . PHE B 1 177 ? -26.309 -3.212  -1.894  1.00 11.69  ? 177 PHE B CA  1 
ATOM   3511 C  C   . PHE B 1 177 ? -26.034 -3.410  -0.404  1.00 10.17  ? 177 PHE B C   1 
ATOM   3512 O  O   . PHE B 1 177 ? -25.880 -2.481  0.407   1.00 10.27  ? 177 PHE B O   1 
ATOM   3513 C  CB  . PHE B 1 177 ? -25.257 -3.916  -2.775  1.00 11.17  ? 177 PHE B CB  1 
ATOM   3514 C  CG  . PHE B 1 177 ? -23.808 -3.536  -2.500  1.00 11.84  ? 177 PHE B CG  1 
ATOM   3515 C  CD1 . PHE B 1 177 ? -23.290 -2.301  -2.962  1.00 11.62  ? 177 PHE B CD1 1 
ATOM   3516 C  CD2 . PHE B 1 177 ? -22.963 -4.354  -1.746  1.00 14.05  ? 177 PHE B CD2 1 
ATOM   3517 C  CE1 . PHE B 1 177 ? -21.961 -1.930  -2.736  1.00 12.46  ? 177 PHE B CE1 1 
ATOM   3518 C  CE2 . PHE B 1 177 ? -21.666 -3.949  -1.476  1.00 12.43  ? 177 PHE B CE2 1 
ATOM   3519 C  CZ  . PHE B 1 177 ? -21.150 -2.788  -2.028  1.00 15.47  ? 177 PHE B CZ  1 
ATOM   3520 N  N   . ASN B 1 178 ? -26.039 -4.681  0.007   1.00 11.91  ? 178 ASN B N   1 
ATOM   3521 C  CA  . ASN B 1 178 ? -25.867 -5.022  1.411   1.00 11.72  ? 178 ASN B CA  1 
ATOM   3522 C  C   . ASN B 1 178 ? -24.390 -4.973  1.793   1.00 9.56   ? 178 ASN B C   1 
ATOM   3523 O  O   . ASN B 1 178 ? -23.607 -5.861  1.449   1.00 11.58  ? 178 ASN B O   1 
ATOM   3524 C  CB  . ASN B 1 178 ? -26.537 -6.364  1.720   1.00 13.70  ? 178 ASN B CB  1 
ATOM   3525 C  CG  . ASN B 1 178 ? -26.375 -6.686  3.184   1.00 13.30  ? 178 ASN B CG  1 
ATOM   3526 O  OD1 . ASN B 1 178 ? -25.949 -5.851  4.031   1.00 12.93  ? 178 ASN B OD1 1 
ATOM   3527 N  ND2 . ASN B 1 178 ? -26.667 -7.938  3.496   1.00 17.73  ? 178 ASN B ND2 1 
ATOM   3528 N  N   . ILE B 1 179 ? -23.947 -3.841  2.382   1.00 8.34   ? 179 ILE B N   1 
ATOM   3529 C  CA  . ILE B 1 179 ? -22.550 -3.645  2.761   1.00 9.74   ? 179 ILE B CA  1 
ATOM   3530 C  C   . ILE B 1 179 ? -22.037 -4.830  3.637   1.00 9.96   ? 179 ILE B C   1 
ATOM   3531 O  O   . ILE B 1 179 ? -20.820 -5.090  3.712   1.00 10.64  ? 179 ILE B O   1 
ATOM   3532 C  CB  . ILE B 1 179 ? -22.328 -2.266  3.440   1.00 9.26   ? 179 ILE B CB  1 
ATOM   3533 C  CG1 . ILE B 1 179 ? -22.878 -1.196  2.494   1.00 9.65   ? 179 ILE B CG1 1 
ATOM   3534 C  CG2 . ILE B 1 179 ? -20.863 -2.080  3.845   1.00 11.83  ? 179 ILE B CG2 1 
ATOM   3535 C  CD1 . ILE B 1 179 ? -22.251 -1.193  1.059   1.00 12.17  ? 179 ILE B CD1 1 
ATOM   3536 N  N   . GLU B 1 180 ? -22.920 -5.489  4.374   1.00 10.76  ? 180 GLU B N   1 
ATOM   3537 C  CA  . GLU B 1 180 ? -22.494 -6.556  5.260   1.00 10.87  ? 180 GLU B CA  1 
ATOM   3538 C  C   . GLU B 1 180 ? -21.880 -7.708  4.450   1.00 9.87   ? 180 GLU B C   1 
ATOM   3539 O  O   . GLU B 1 180 ? -21.071 -8.505  4.984   1.00 12.06  ? 180 GLU B O   1 
ATOM   3540 C  CB  . GLU B 1 180 ? -23.662 -7.055  6.125   1.00 14.19  ? 180 GLU B CB  1 
ATOM   3541 C  CG  . GLU B 1 180 ? -23.180 -7.937  7.285   1.00 19.72  ? 180 GLU B CG  1 
ATOM   3542 C  CD  . GLU B 1 180 ? -24.214 -8.167  8.380   1.00 20.40  ? 180 GLU B CD  1 
ATOM   3543 O  OE1 . GLU B 1 180 ? -25.388 -7.760  8.224   1.00 22.28  ? 180 GLU B OE1 1 
ATOM   3544 O  OE2 . GLU B 1 180 ? -23.848 -8.792  9.381   1.00 30.47  ? 180 GLU B OE2 1 
ATOM   3545 N  N   . GLU B 1 181 ? -22.178 -7.749  3.145   1.00 9.80   ? 181 GLU B N   1 
ATOM   3546 C  CA  . GLU B 1 181 ? -21.615 -8.770  2.280   1.00 9.94   ? 181 GLU B CA  1 
ATOM   3547 C  C   . GLU B 1 181 ? -20.099 -8.601  2.131   1.00 9.33   ? 181 GLU B C   1 
ATOM   3548 O  O   . GLU B 1 181 ? -19.437 -9.536  1.677   1.00 12.67  ? 181 GLU B O   1 
ATOM   3549 C  CB  . GLU B 1 181 ? -22.275 -8.775  0.908   1.00 11.08  ? 181 GLU B CB  1 
ATOM   3550 C  CG  . GLU B 1 181 ? -23.745 -9.090  0.873   1.00 13.96  ? 181 GLU B CG  1 
ATOM   3551 C  CD  . GLU B 1 181 ? -24.388 -8.880  -0.514  1.00 14.31  ? 181 GLU B CD  1 
ATOM   3552 O  OE1 . GLU B 1 181 ? -23.663 -8.599  -1.519  1.00 17.73  ? 181 GLU B OE1 1 
ATOM   3553 O  OE2 . GLU B 1 181 ? -25.633 -9.002  -0.589  1.00 18.96  ? 181 GLU B OE2 1 
ATOM   3554 N  N   . LEU B 1 182 ? -19.569 -7.420  2.437   1.00 7.60   ? 182 LEU B N   1 
ATOM   3555 C  CA  . LEU B 1 182 ? -18.144 -7.140  2.353   1.00 9.20   ? 182 LEU B CA  1 
ATOM   3556 C  C   . LEU B 1 182 ? -17.400 -7.627  3.591   1.00 8.20   ? 182 LEU B C   1 
ATOM   3557 O  O   . LEU B 1 182 ? -16.163 -7.626  3.588   1.00 9.56   ? 182 LEU B O   1 
ATOM   3558 C  CB  . LEU B 1 182 ? -17.929 -5.610  2.202   1.00 9.52   ? 182 LEU B CB  1 
ATOM   3559 C  CG  . LEU B 1 182 ? -18.625 -4.968  0.979   1.00 10.43  ? 182 LEU B CG  1 
ATOM   3560 C  CD1 . LEU B 1 182 ? -18.330 -3.466  0.954   1.00 10.79  ? 182 LEU B CD1 1 
ATOM   3561 C  CD2 . LEU B 1 182 ? -18.239 -5.656  -0.338  1.00 10.57  ? 182 LEU B CD2 1 
ATOM   3562 N  N   . LEU B 1 183 ? -18.133 -7.976  4.674   1.00 8.54   ? 183 LEU B N   1 
ATOM   3563 C  CA  . LEU B 1 183 ? -17.526 -8.409  5.929   1.00 8.49   ? 183 LEU B CA  1 
ATOM   3564 C  C   . LEU B 1 183 ? -17.157 -9.894  5.863   1.00 9.21   ? 183 LEU B C   1 
ATOM   3565 O  O   . LEU B 1 183 ? -17.826 -10.684 5.159   1.00 12.30  ? 183 LEU B O   1 
ATOM   3566 C  CB  . LEU B 1 183 ? -18.362 -8.041  7.144   1.00 10.20  ? 183 LEU B CB  1 
ATOM   3567 C  CG  . LEU B 1 183 ? -18.777 -6.577  7.222   1.00 10.95  ? 183 LEU B CG  1 
ATOM   3568 C  CD1 . LEU B 1 183 ? -19.605 -6.442  8.500   1.00 15.49  ? 183 LEU B CD1 1 
ATOM   3569 C  CD2 . LEU B 1 183 ? -17.582 -5.664  7.158   1.00 14.85  ? 183 LEU B CD2 1 
ATOM   3570 N  N   . PRO B 1 184 ? -16.129 -10.298 6.665   1.00 10.01  ? 184 PRO B N   1 
ATOM   3571 C  CA  . PRO B 1 184 ? -15.709 -11.714 6.664   1.00 11.05  ? 184 PRO B CA  1 
ATOM   3572 C  C   . PRO B 1 184 ? -16.572 -12.514 7.589   1.00 11.94  ? 184 PRO B C   1 
ATOM   3573 O  O   . PRO B 1 184 ? -17.497 -12.026 8.208   1.00 14.43  ? 184 PRO B O   1 
ATOM   3574 C  CB  . PRO B 1 184 ? -14.260 -11.592 7.211   1.00 12.01  ? 184 PRO B CB  1 
ATOM   3575 C  CG  . PRO B 1 184 ? -14.335 -10.394 8.150   1.00 9.95   ? 184 PRO B CG  1 
ATOM   3576 C  CD  . PRO B 1 184 ? -15.253 -9.409  7.457   1.00 10.22  ? 184 PRO B CD  1 
ATOM   3577 N  N   . GLU B 1 185 ? -16.211 -13.808 7.632   1.00 13.13  ? 185 GLU B N   1 
ATOM   3578 C  CA  . GLU B 1 185 ? -16.825 -14.752 8.538   1.00 14.00  ? 185 GLU B CA  1 
ATOM   3579 C  C   . GLU B 1 185 ? -16.430 -14.384 9.974   1.00 12.67  ? 185 GLU B C   1 
ATOM   3580 O  O   . GLU B 1 185 ? -15.311 -13.898 10.230  1.00 14.01  ? 185 GLU B O   1 
ATOM   3581 C  CB  . GLU B 1 185 ? -16.375 -16.192 8.208   1.00 18.40  ? 185 GLU B CB  1 
ATOM   3582 C  CG  . GLU B 1 185 ? -16.906 -16.769 6.895   1.00 20.12  ? 185 GLU B CG  1 
ATOM   3583 C  CD  . GLU B 1 185 ? -16.695 -18.271 6.748   1.00 30.47  ? 185 GLU B CD  1 
ATOM   3584 O  OE1 . GLU B 1 185 ? -15.524 -18.691 6.647   1.00 42.08  ? 185 GLU B OE1 1 
ATOM   3585 O  OE2 . GLU B 1 185 ? -17.696 -19.029 6.800   1.00 48.58  ? 185 GLU B OE2 1 
ATOM   3586 N  N   . ARG B 1 186 ? -17.347 -14.673 10.910  1.00 12.32  ? 186 ARG B N   1 
ATOM   3587 C  CA  . ARG B 1 186 ? -17.086 -14.643 12.356  1.00 14.23  ? 186 ARG B CA  1 
ATOM   3588 C  C   . ARG B 1 186 ? -16.670 -13.214 12.744  1.00 12.70  ? 186 ARG B C   1 
ATOM   3589 O  O   . ARG B 1 186 ? -15.555 -12.976 13.252  1.00 13.10  ? 186 ARG B O   1 
ATOM   3590 C  CB  . ARG B 1 186 ? -16.094 -15.703 12.824  1.00 15.68  ? 186 ARG B CB  1 
ATOM   3591 C  CG  . ARG B 1 186 ? -16.723 -17.086 12.710  1.00 21.87  ? 186 ARG B CG  1 
ATOM   3592 C  CD  . ARG B 1 186 ? -15.843 -18.205 13.257  1.00 21.56  ? 186 ARG B CD  1 
ATOM   3593 N  NE  . ARG B 1 186 ? -14.552 -18.253 12.556  1.00 24.76  ? 186 ARG B NE  1 
ATOM   3594 C  CZ  . ARG B 1 186 ? -14.295 -18.782 11.349  1.00 32.53  ? 186 ARG B CZ  1 
ATOM   3595 N  NH1 . ARG B 1 186 ? -15.243 -19.353 10.620  1.00 34.81  ? 186 ARG B NH1 1 
ATOM   3596 N  NH2 . ARG B 1 186 ? -13.059 -18.760 10.873  1.00 41.52  ? 186 ARG B NH2 1 
ATOM   3597 N  N   . THR B 1 187 ? -17.487 -12.220 12.354  1.00 12.44  ? 187 THR B N   1 
ATOM   3598 C  CA  . THR B 1 187 ? -17.184 -10.829 12.715  1.00 11.03  ? 187 THR B CA  1 
ATOM   3599 C  C   . THR B 1 187 ? -17.033 -10.643 14.210  1.00 11.00  ? 187 THR B C   1 
ATOM   3600 O  O   . THR B 1 187 ? -16.441 -9.627  14.627  1.00 11.86  ? 187 THR B O   1 
ATOM   3601 C  CB  . THR B 1 187 ? -18.201 -9.859  12.102  1.00 12.62  ? 187 THR B CB  1 
ATOM   3602 O  OG1 . THR B 1 187 ? -19.526 -10.279 12.460  1.00 13.78  ? 187 THR B OG1 1 
ATOM   3603 C  CG2 . THR B 1 187 ? -18.010 -9.771  10.597  1.00 12.79  ? 187 THR B CG2 1 
ATOM   3604 N  N   . ALA B 1 188 ? -17.545 -11.568 15.053  1.00 11.87  ? 188 ALA B N   1 
ATOM   3605 C  CA  . ALA B 1 188 ? -17.324 -11.460 16.490  1.00 11.41  ? 188 ALA B CA  1 
ATOM   3606 C  C   . ALA B 1 188 ? -15.847 -11.509 16.850  1.00 11.92  ? 188 ALA B C   1 
ATOM   3607 O  O   . ALA B 1 188 ? -15.538 -11.103 17.965  1.00 12.11  ? 188 ALA B O   1 
ATOM   3608 C  CB  . ALA B 1 188 ? -18.101 -12.506 17.296  1.00 14.20  ? 188 ALA B CB  1 
ATOM   3609 N  N   A GLU B 1 189 ? -14.984 -12.045 15.959  0.50 11.13  ? 189 GLU B N   1 
ATOM   3610 N  N   B GLU B 1 189 ? -14.997 -12.068 15.973  0.50 11.16  ? 189 GLU B N   1 
ATOM   3611 C  CA  A GLU B 1 189 ? -13.557 -12.172 16.252  0.50 10.63  ? 189 GLU B CA  1 
ATOM   3612 C  CA  B GLU B 1 189 ? -13.565 -12.175 16.261  0.50 10.62  ? 189 GLU B CA  1 
ATOM   3613 C  C   A GLU B 1 189 ? -12.818 -11.014 15.583  0.50 10.59  ? 189 GLU B C   1 
ATOM   3614 C  C   B GLU B 1 189 ? -12.836 -11.002 15.602  0.50 10.63  ? 189 GLU B C   1 
ATOM   3615 O  O   A GLU B 1 189 ? -12.843 -10.886 14.333  0.50 10.87  ? 189 GLU B O   1 
ATOM   3616 O  O   B GLU B 1 189 ? -12.829 -10.883 14.364  0.50 10.93  ? 189 GLU B O   1 
ATOM   3617 C  CB  A GLU B 1 189 ? -13.086 -13.526 15.736  0.50 13.35  ? 189 GLU B CB  1 
ATOM   3618 C  CB  B GLU B 1 189 ? -13.026 -13.475 15.678  0.50 13.56  ? 189 GLU B CB  1 
ATOM   3619 C  CG  A GLU B 1 189 ? -13.885 -14.670 16.351  0.50 13.04  ? 189 GLU B CG  1 
ATOM   3620 C  CG  B GLU B 1 189 ? -13.693 -14.745 16.184  0.50 13.80  ? 189 GLU B CG  1 
ATOM   3621 C  CD  A GLU B 1 189 ? -13.419 -16.049 15.910  0.50 17.42  ? 189 GLU B CD  1 
ATOM   3622 C  CD  B GLU B 1 189 ? -12.890 -15.861 15.506  0.50 19.44  ? 189 GLU B CD  1 
ATOM   3623 O  OE1 A GLU B 1 189 ? -12.229 -16.188 15.501  0.50 21.59  ? 189 GLU B OE1 1 
ATOM   3624 O  OE1 B GLU B 1 189 ? -11.981 -16.376 16.112  0.50 23.46  ? 189 GLU B OE1 1 
ATOM   3625 O  OE2 A GLU B 1 189 ? -14.270 -16.968 15.968  0.50 23.68  ? 189 GLU B OE2 1 
ATOM   3626 O  OE2 B GLU B 1 189 ? -13.051 -16.024 14.268  0.50 28.37  ? 189 GLU B OE2 1 
ATOM   3627 N  N   . TYR B 1 190 ? -12.258 -10.129 16.436  1.00 9.93   ? 190 TYR B N   1 
ATOM   3628 C  CA  . TYR B 1 190 ? -11.616 -8.923  15.903  1.00 11.51  ? 190 TYR B CA  1 
ATOM   3629 C  C   . TYR B 1 190 ? -10.478 -8.481  16.828  1.00 9.52   ? 190 TYR B C   1 
ATOM   3630 O  O   . TYR B 1 190 ? -10.424 -8.823  18.020  1.00 9.51   ? 190 TYR B O   1 
ATOM   3631 C  CB  . TYR B 1 190 ? -12.637 -7.778  15.643  1.00 9.58   ? 190 TYR B CB  1 
ATOM   3632 C  CG  . TYR B 1 190 ? -13.460 -7.391  16.853  1.00 8.58   ? 190 TYR B CG  1 
ATOM   3633 C  CD1 . TYR B 1 190 ? -12.929 -6.533  17.843  1.00 9.69   ? 190 TYR B CD1 1 
ATOM   3634 C  CD2 . TYR B 1 190 ? -14.719 -7.909  17.070  1.00 10.65  ? 190 TYR B CD2 1 
ATOM   3635 C  CE1 . TYR B 1 190 ? -13.707 -6.181  18.951  1.00 9.65   ? 190 TYR B CE1 1 
ATOM   3636 C  CE2 . TYR B 1 190 ? -15.498 -7.563  18.181  1.00 10.22  ? 190 TYR B CE2 1 
ATOM   3637 C  CZ  . TYR B 1 190 ? -14.995 -6.687  19.120  1.00 10.51  ? 190 TYR B CZ  1 
ATOM   3638 O  OH  . TYR B 1 190 ? -15.736 -6.263  20.192  1.00 10.29  ? 190 TYR B OH  1 
ATOM   3639 N  N   . TYR B 1 191 ? -9.621  -7.604  16.266  1.00 8.36   ? 191 TYR B N   1 
ATOM   3640 C  CA  . TYR B 1 191 ? -8.570  -6.877  16.976  1.00 8.28   ? 191 TYR B CA  1 
ATOM   3641 C  C   . TYR B 1 191 ? -9.103  -5.458  17.175  1.00 7.76   ? 191 TYR B C   1 
ATOM   3642 O  O   . TYR B 1 191 ? -9.717  -4.927  16.286  1.00 8.96   ? 191 TYR B O   1 
ATOM   3643 C  CB  . TYR B 1 191 ? -7.298  -6.747  16.134  1.00 8.31   ? 191 TYR B CB  1 
ATOM   3644 C  CG  . TYR B 1 191 ? -6.730  -8.049  15.589  1.00 8.59   ? 191 TYR B CG  1 
ATOM   3645 C  CD1 . TYR B 1 191 ? -5.691  -8.667  16.269  1.00 9.89   ? 191 TYR B CD1 1 
ATOM   3646 C  CD2 . TYR B 1 191 ? -7.067  -8.515  14.318  1.00 8.87   ? 191 TYR B CD2 1 
ATOM   3647 C  CE1 . TYR B 1 191 ? -5.109  -9.829  15.783  1.00 9.53   ? 191 TYR B CE1 1 
ATOM   3648 C  CE2 . TYR B 1 191 ? -6.475  -9.685  13.804  1.00 9.84   ? 191 TYR B CE2 1 
ATOM   3649 C  CZ  . TYR B 1 191 ? -5.477  -10.313 14.541  1.00 10.08  ? 191 TYR B CZ  1 
ATOM   3650 O  OH  . TYR B 1 191 ? -4.926  -11.455 14.004  1.00 13.47  ? 191 TYR B OH  1 
ATOM   3651 N  N   . ARG B 1 192 ? -8.829  -4.870  18.341  1.00 8.81   ? 192 ARG B N   1 
ATOM   3652 C  CA  . ARG B 1 192 ? -9.293  -3.527  18.689  1.00 8.32   ? 192 ARG B CA  1 
ATOM   3653 C  C   . ARG B 1 192 ? -8.118  -2.749  19.235  1.00 7.84   ? 192 ARG B C   1 
ATOM   3654 O  O   . ARG B 1 192 ? -7.410  -3.179  20.162  1.00 9.89   ? 192 ARG B O   1 
ATOM   3655 C  CB  . ARG B 1 192 ? -10.371 -3.617  19.795  1.00 9.33   ? 192 ARG B CB  1 
ATOM   3656 C  CG  . ARG B 1 192 ? -10.697 -2.299  20.493  1.00 11.62  ? 192 ARG B CG  1 
ATOM   3657 C  CD  . ARG B 1 192 ? -11.452 -1.305  19.601  1.00 11.53  ? 192 ARG B CD  1 
ATOM   3658 N  NE  . ARG B 1 192 ? -12.555 -1.816  18.795  1.00 11.63  ? 192 ARG B NE  1 
ATOM   3659 C  CZ  . ARG B 1 192 ? -13.747 -2.213  19.298  1.00 11.04  ? 192 ARG B CZ  1 
ATOM   3660 N  NH1 . ARG B 1 192 ? -14.012 -2.052  20.592  1.00 13.37  ? 192 ARG B NH1 1 
ATOM   3661 N  NH2 . ARG B 1 192 ? -14.665 -2.738  18.490  1.00 12.00  ? 192 ARG B NH2 1 
ATOM   3662 N  N   . TYR B 1 193 ? -7.935  -1.557  18.736  1.00 9.04   ? 193 TYR B N   1 
ATOM   3663 C  CA  . TYR B 1 193 ? -6.917  -0.701  19.317  1.00 11.11  ? 193 TYR B CA  1 
ATOM   3664 C  C   . TYR B 1 193 ? -7.233  0.763   19.027  1.00 7.47   ? 193 TYR B C   1 
ATOM   3665 O  O   . TYR B 1 193 ? -7.980  1.067   18.097  1.00 8.72   ? 193 TYR B O   1 
ATOM   3666 C  CB  . TYR B 1 193 ? -5.493  -1.089  18.820  1.00 9.65   ? 193 TYR B CB  1 
ATOM   3667 C  CG  . TYR B 1 193 ? -5.131  -0.678  17.410  1.00 7.83   ? 193 TYR B CG  1 
ATOM   3668 C  CD1 . TYR B 1 193 ? -5.540  -1.411  16.280  1.00 8.34   ? 193 TYR B CD1 1 
ATOM   3669 C  CD2 . TYR B 1 193 ? -4.430  0.507   17.193  1.00 8.82   ? 193 TYR B CD2 1 
ATOM   3670 C  CE1 . TYR B 1 193 ? -5.226  -1.009  14.981  1.00 8.21   ? 193 TYR B CE1 1 
ATOM   3671 C  CE2 . TYR B 1 193 ? -4.036  0.870   15.918  1.00 8.27   ? 193 TYR B CE2 1 
ATOM   3672 C  CZ  . TYR B 1 193 ? -4.482  0.188   14.818  1.00 6.65   ? 193 TYR B CZ  1 
ATOM   3673 O  OH  . TYR B 1 193 ? -4.094  0.594   13.586  1.00 8.31   ? 193 TYR B OH  1 
ATOM   3674 N  N   . ARG B 1 194 ? -6.496  1.630   19.714  1.00 9.83   ? 194 ARG B N   1 
ATOM   3675 C  CA  . ARG B 1 194 ? -6.610  3.093   19.513  1.00 10.98  ? 194 ARG B CA  1 
ATOM   3676 C  C   . ARG B 1 194 ? -5.525  3.573   18.583  1.00 10.16  ? 194 ARG B C   1 
ATOM   3677 O  O   . ARG B 1 194 ? -4.369  3.368   18.819  1.00 11.82  ? 194 ARG B O   1 
ATOM   3678 C  CB  . ARG B 1 194 ? -6.572  3.823   20.854  1.00 16.00  ? 194 ARG B CB  1 
ATOM   3679 C  CG  . ARG B 1 194 ? -7.860  3.698   21.675  1.00 24.38  ? 194 ARG B CG  1 
ATOM   3680 C  CD  . ARG B 1 194 ? -7.928  4.275   23.090  1.00 31.06  ? 194 ARG B CD  1 
ATOM   3681 N  NE  . ARG B 1 194 ? -9.252  4.058   23.699  1.00 41.95  ? 194 ARG B NE  1 
ATOM   3682 C  CZ  . ARG B 1 194 ? -10.045 3.008   23.531  1.00 48.05  ? 194 ARG B CZ  1 
ATOM   3683 N  NH1 . ARG B 1 194 ? -9.670  1.974   22.786  1.00 58.26  ? 194 ARG B NH1 1 
ATOM   3684 N  NH2 . ARG B 1 194 ? -11.223 2.983   24.136  1.00 44.08  ? 194 ARG B NH2 1 
ATOM   3685 N  N   . GLY B 1 195 ? -5.940  4.233   17.498  1.00 9.56   ? 195 GLY B N   1 
ATOM   3686 C  CA  . GLY B 1 195 ? -4.975  4.688   16.508  1.00 10.04  ? 195 GLY B CA  1 
ATOM   3687 C  C   . GLY B 1 195 ? -5.440  5.949   15.777  1.00 9.02   ? 195 GLY B C   1 
ATOM   3688 O  O   . GLY B 1 195 ? -6.086  6.819   16.349  1.00 9.98   ? 195 GLY B O   1 
ATOM   3689 N  N   . SER B 1 196 ? -5.099  5.997   14.516  1.00 9.39   ? 196 SER B N   1 
ATOM   3690 C  CA  . SER B 1 196 ? -5.134  7.264   13.796  1.00 9.15   ? 196 SER B CA  1 
ATOM   3691 C  C   . SER B 1 196 ? -5.636  7.031   12.380  1.00 8.60   ? 196 SER B C   1 
ATOM   3692 O  O   . SER B 1 196 ? -5.764  5.876   11.886  1.00 8.70   ? 196 SER B O   1 
ATOM   3693 C  CB  . SER B 1 196 ? -3.790  7.947   13.646  1.00 8.88   ? 196 SER B CB  1 
ATOM   3694 O  OG  . SER B 1 196 ? -2.956  7.215   12.695  1.00 10.32  ? 196 SER B OG  1 
ATOM   3695 N  N   . LEU B 1 197 ? -5.924  8.088   11.673  1.00 8.18   ? 197 LEU B N   1 
ATOM   3696 C  CA  . LEU B 1 197 ? -6.096  8.015   10.232  1.00 7.42   ? 197 LEU B CA  1 
ATOM   3697 C  C   . LEU B 1 197 ? -4.767  7.514   9.667   1.00 8.97   ? 197 LEU B C   1 
ATOM   3698 O  O   . LEU B 1 197 ? -3.688  7.881   10.165  1.00 8.51   ? 197 LEU B O   1 
ATOM   3699 C  CB  . LEU B 1 197 ? -6.248  9.449   9.669   1.00 10.20  ? 197 LEU B CB  1 
ATOM   3700 C  CG  . LEU B 1 197 ? -7.666  9.900   9.346   1.00 12.92  ? 197 LEU B CG  1 
ATOM   3701 C  CD1 . LEU B 1 197 ? -8.555  10.014  10.569  1.00 15.01  ? 197 LEU B CD1 1 
ATOM   3702 C  CD2 . LEU B 1 197 ? -7.592  11.287  8.667   1.00 16.14  ? 197 LEU B CD2 1 
ATOM   3703 N  N   . THR B 1 198 ? -4.838  6.670   8.628   1.00 7.14   ? 198 THR B N   1 
ATOM   3704 C  CA  . THR B 1 198 ? -3.620  6.179   7.987   1.00 6.49   ? 198 THR B CA  1 
ATOM   3705 C  C   . THR B 1 198 ? -3.192  7.066   6.826   1.00 8.04   ? 198 THR B C   1 
ATOM   3706 O  O   . THR B 1 198 ? -2.205  6.775   6.158   1.00 8.83   ? 198 THR B O   1 
ATOM   3707 C  CB  . THR B 1 198 ? -3.817  4.734   7.472   1.00 8.52   ? 198 THR B CB  1 
ATOM   3708 O  OG1 . THR B 1 198 ? -4.765  4.737   6.390   1.00 8.74   ? 198 THR B OG1 1 
ATOM   3709 C  CG2 . THR B 1 198 ? -4.169  3.721   8.575   1.00 8.16   ? 198 THR B CG2 1 
ATOM   3710 N  N   . THR B 1 199 ? -3.993  8.167   6.562   1.00 8.61   ? 199 THR B N   1 
ATOM   3711 C  CA  . THR B 1 199 ? -3.644  9.125   5.525   1.00 7.72   ? 199 THR B CA  1 
ATOM   3712 C  C   . THR B 1 199 ? -3.464  10.432  6.263   1.00 7.80   ? 199 THR B C   1 
ATOM   3713 O  O   . THR B 1 199 ? -4.136  10.648  7.278   1.00 9.72   ? 199 THR B O   1 
ATOM   3714 C  CB  . THR B 1 199 ? -4.783  9.325   4.500   1.00 7.62   ? 199 THR B CB  1 
ATOM   3715 O  OG1 . THR B 1 199 ? -5.991  9.671   5.190   1.00 9.54   ? 199 THR B OG1 1 
ATOM   3716 C  CG2 . THR B 1 199 ? -5.101  8.022   3.783   1.00 9.36   ? 199 THR B CG2 1 
ATOM   3717 N  N   . PRO B 1 200 ? -2.770  11.420  5.670   1.00 7.37   ? 200 PRO B N   1 
ATOM   3718 C  CA  . PRO B 1 200 ? -2.889  12.796  6.145   1.00 7.96   ? 200 PRO B CA  1 
ATOM   3719 C  C   . PRO B 1 200 ? -4.374  13.169  6.267   1.00 10.31  ? 200 PRO B C   1 
ATOM   3720 O  O   . PRO B 1 200 ? -5.174  12.804  5.393   1.00 10.46  ? 200 PRO B O   1 
ATOM   3721 C  CB  . PRO B 1 200 ? -2.175  13.608  5.093   1.00 10.32  ? 200 PRO B CB  1 
ATOM   3722 C  CG  . PRO B 1 200 ? -1.180  12.670  4.474   1.00 8.17   ? 200 PRO B CG  1 
ATOM   3723 C  CD  . PRO B 1 200 ? -1.948  11.360  4.455   1.00 8.50   ? 200 PRO B CD  1 
ATOM   3724 N  N   A PRO B 1 201 ? -4.779  13.961  7.289   0.50 10.44  ? 201 PRO B N   1 
ATOM   3725 N  N   B PRO B 1 201 ? -4.821  13.930  7.294   0.50 9.91   ? 201 PRO B N   1 
ATOM   3726 C  CA  A PRO B 1 201 ? -3.857  14.565  8.259   0.50 10.20  ? 201 PRO B CA  1 
ATOM   3727 C  CA  B PRO B 1 201 ? -3.948  14.580  8.279   0.50 9.44   ? 201 PRO B CA  1 
ATOM   3728 C  C   A PRO B 1 201 ? -3.475  13.728  9.475   0.50 9.90   ? 201 PRO B C   1 
ATOM   3729 C  C   B PRO B 1 201 ? -3.425  13.726  9.431   0.50 9.17   ? 201 PRO B C   1 
ATOM   3730 O  O   A PRO B 1 201 ? -3.011  14.230  10.472  0.50 9.87   ? 201 PRO B O   1 
ATOM   3731 O  O   B PRO B 1 201 ? -2.752  14.211  10.315  0.50 9.09   ? 201 PRO B O   1 
ATOM   3732 C  CB  A PRO B 1 201 ? -4.659  15.758  8.818   0.50 13.17  ? 201 PRO B CB  1 
ATOM   3733 C  CB  B PRO B 1 201 ? -4.880  15.682  8.843   0.50 10.09  ? 201 PRO B CB  1 
ATOM   3734 C  CG  A PRO B 1 201 ? -5.822  15.970  7.872   0.50 12.10  ? 201 PRO B CG  1 
ATOM   3735 C  CG  B PRO B 1 201 ? -6.263  15.068  8.734   0.50 9.38   ? 201 PRO B CG  1 
ATOM   3736 C  CD  A PRO B 1 201 ? -6.121  14.568  7.360   0.50 9.82   ? 201 PRO B CD  1 
ATOM   3737 C  CD  B PRO B 1 201 ? -6.208  14.435  7.361   0.50 10.10  ? 201 PRO B CD  1 
ATOM   3738 N  N   . CYS B 1 202 ? -3.774  12.410  9.441   1.00 8.73   ? 202 CYS B N   1 
ATOM   3739 C  CA  . CYS B 1 202 ? -3.236  11.419  10.428  1.00 8.91   ? 202 CYS B CA  1 
ATOM   3740 C  C   . CYS B 1 202 ? -3.735  11.632  11.882  1.00 9.20   ? 202 CYS B C   1 
ATOM   3741 O  O   . CYS B 1 202 ? -3.075  11.266  12.868  1.00 10.05  ? 202 CYS B O   1 
ATOM   3742 C  CB  . CYS B 1 202 ? -1.698  11.372  10.509  1.00 10.05  ? 202 CYS B CB  1 
ATOM   3743 S  SG  . CYS B 1 202 ? -0.844  11.045  8.936   1.00 9.25   ? 202 CYS B SG  1 
ATOM   3744 N  N   A ASN B 1 203 ? -4.916  12.231  12.047  0.50 10.23  ? 203 ASN B N   1 
ATOM   3745 N  N   B ASN B 1 203 ? -4.906  12.262  12.030  0.50 9.88   ? 203 ASN B N   1 
ATOM   3746 C  CA  A ASN B 1 203 ? -5.366  12.549  13.388  0.50 11.10  ? 203 ASN B CA  1 
ATOM   3747 C  CA  B ASN B 1 203 ? -5.527  12.552  13.313  0.50 10.02  ? 203 ASN B CA  1 
ATOM   3748 C  C   A ASN B 1 203 ? -5.499  11.300  14.195  0.50 8.91   ? 203 ASN B C   1 
ATOM   3749 C  C   B ASN B 1 203 ? -5.550  11.322  14.195  0.50 8.90   ? 203 ASN B C   1 
ATOM   3750 O  O   A ASN B 1 203 ? -6.030  10.310  13.688  0.50 11.04  ? 203 ASN B O   1 
ATOM   3751 O  O   B ASN B 1 203 ? -6.078  10.310  13.734  0.50 11.06  ? 203 ASN B O   1 
ATOM   3752 C  CB  A ASN B 1 203 ? -6.722  13.238  13.417  0.50 14.34  ? 203 ASN B CB  1 
ATOM   3753 C  CB  B ASN B 1 203 ? -6.956  13.083  13.115  0.50 11.59  ? 203 ASN B CB  1 
ATOM   3754 C  CG  A ASN B 1 203 ? -6.622  14.440  12.519  0.50 17.87  ? 203 ASN B CG  1 
ATOM   3755 C  CG  B ASN B 1 203 ? -7.065  14.371  12.309  0.50 13.71  ? 203 ASN B CG  1 
ATOM   3756 O  OD1 A ASN B 1 203 ? -6.748  14.282  11.307  0.50 21.43  ? 203 ASN B OD1 1 
ATOM   3757 O  OD1 B ASN B 1 203 ? -6.052  14.955  11.892  0.50 16.55  ? 203 ASN B OD1 1 
ATOM   3758 N  ND2 A ASN B 1 203 ? -6.249  15.571  13.096  0.50 21.70  ? 203 ASN B ND2 1 
ATOM   3759 N  ND2 B ASN B 1 203 ? -8.297  14.851  12.159  0.50 13.40  ? 203 ASN B ND2 1 
ATOM   3760 N  N   . PRO B 1 204 ? -5.064  11.356  15.460  1.00 10.69  ? 204 PRO B N   1 
ATOM   3761 C  CA  . PRO B 1 204 ? -5.107  10.175  16.348  1.00 11.31  ? 204 PRO B CA  1 
ATOM   3762 C  C   . PRO B 1 204 ? -6.473  9.995   17.017  1.00 10.74  ? 204 PRO B C   1 
ATOM   3763 O  O   . PRO B 1 204 ? -6.585  9.958   18.245  1.00 14.32  ? 204 PRO B O   1 
ATOM   3764 C  CB  . PRO B 1 204 ? -4.023  10.490  17.389  1.00 12.44  ? 204 PRO B CB  1 
ATOM   3765 C  CG  . PRO B 1 204 ? -4.019  12.048  17.453  1.00 12.75  ? 204 PRO B CG  1 
ATOM   3766 C  CD  . PRO B 1 204 ? -4.385  12.525  16.031  1.00 12.28  ? 204 PRO B CD  1 
ATOM   3767 N  N   . THR B 1 205 ? -7.514  9.809   16.175  1.00 10.80  ? 205 THR B N   1 
ATOM   3768 C  CA  . THR B 1 205 ? -8.831  9.931   16.666  1.00 10.59  ? 205 THR B CA  1 
ATOM   3769 C  C   . THR B 1 205 ? -9.687  8.738   16.229  1.00 12.68  ? 205 THR B C   1 
ATOM   3770 O  O   . THR B 1 205 ? -10.926 8.798   16.254  1.00 13.28  ? 205 THR B O   1 
ATOM   3771 C  CB  . THR B 1 205 ? -9.489  11.183  16.117  1.00 12.14  ? 205 THR B CB  1 
ATOM   3772 O  OG1 . THR B 1 205 ? -9.291  11.206  14.698  1.00 12.82  ? 205 THR B OG1 1 
ATOM   3773 C  CG2 . THR B 1 205 ? -8.737  12.419  16.653  1.00 13.38  ? 205 THR B CG2 1 
ATOM   3774 N  N   . VAL B 1 206 ? -9.039  7.612   15.929  1.00 10.06  ? 206 VAL B N   1 
ATOM   3775 C  CA  . VAL B 1 206 ? -9.738  6.439   15.388  1.00 9.69   ? 206 VAL B CA  1 
ATOM   3776 C  C   . VAL B 1 206 ? -9.710  5.272   16.382  1.00 8.69   ? 206 VAL B C   1 
ATOM   3777 O  O   . VAL B 1 206 ? -8.649  4.871   16.837  1.00 11.53  ? 206 VAL B O   1 
ATOM   3778 C  CB  . VAL B 1 206 ? -9.163  5.962   14.008  1.00 8.67   ? 206 VAL B CB  1 
ATOM   3779 C  CG1 . VAL B 1 206 ? -9.886  4.678   13.516  1.00 10.83  ? 206 VAL B CG1 1 
ATOM   3780 C  CG2 . VAL B 1 206 ? -9.180  7.067   12.983  1.00 10.28  ? 206 VAL B CG2 1 
ATOM   3781 N  N   A LEU B 1 207 ? -10.881 4.694   16.590  0.50 10.29  ? 207 LEU B N   1 
ATOM   3782 N  N   B LEU B 1 207 ? -10.887 4.717   16.647  0.50 10.11  ? 207 LEU B N   1 
ATOM   3783 C  CA  A LEU B 1 207 ? -11.022 3.441   17.308  0.50 9.07   ? 207 LEU B CA  1 
ATOM   3784 C  CA  B LEU B 1 207 ? -11.021 3.415   17.281  0.50 9.56   ? 207 LEU B CA  1 
ATOM   3785 C  C   A LEU B 1 207 ? -11.094 2.347   16.225  0.50 8.60   ? 207 LEU B C   1 
ATOM   3786 C  C   B LEU B 1 207 ? -11.052 2.395   16.138  0.50 8.50   ? 207 LEU B C   1 
ATOM   3787 O  O   A LEU B 1 207 ? -12.079 2.263   15.475  0.50 10.56  ? 207 LEU B O   1 
ATOM   3788 O  O   B LEU B 1 207 ? -11.953 2.397   15.289  0.50 9.37   ? 207 LEU B O   1 
ATOM   3789 C  CB  A LEU B 1 207 ? -12.313 3.480   18.109  0.50 11.09  ? 207 LEU B CB  1 
ATOM   3790 C  CB  B LEU B 1 207 ? -12.325 3.326   18.055  0.50 12.49  ? 207 LEU B CB  1 
ATOM   3791 C  CG  A LEU B 1 207 ? -12.482 2.280   19.031  0.50 10.45  ? 207 LEU B CG  1 
ATOM   3792 C  CG  B LEU B 1 207 ? -12.337 4.162   19.324  0.50 13.80  ? 207 LEU B CG  1 
ATOM   3793 C  CD1 A LEU B 1 207 ? -11.376 2.260   20.082  0.50 12.73  ? 207 LEU B CD1 1 
ATOM   3794 C  CD1 B LEU B 1 207 ? -13.686 4.039   20.007  0.50 18.18  ? 207 LEU B CD1 1 
ATOM   3795 C  CD2 A LEU B 1 207 ? -13.860 2.319   19.662  0.50 12.68  ? 207 LEU B CD2 1 
ATOM   3796 C  CD2 B LEU B 1 207 ? -11.219 3.778   20.290  0.50 16.68  ? 207 LEU B CD2 1 
ATOM   3797 N  N   . TRP B 1 208 ? -9.997  1.588   16.078  1.00 7.62   ? 208 TRP B N   1 
ATOM   3798 C  CA  . TRP B 1 208 ? -9.896  0.586   15.018  1.00 8.02   ? 208 TRP B CA  1 
ATOM   3799 C  C   . TRP B 1 208 ? -10.467 -0.768  15.447  1.00 8.38   ? 208 TRP B C   1 
ATOM   3800 O  O   . TRP B 1 208 ? -10.219 -1.207  16.581  1.00 9.64   ? 208 TRP B O   1 
ATOM   3801 C  CB  . TRP B 1 208 ? -8.380  0.390   14.724  1.00 9.03   ? 208 TRP B CB  1 
ATOM   3802 C  CG  . TRP B 1 208 ? -7.834  1.450   13.807  1.00 8.41   ? 208 TRP B CG  1 
ATOM   3803 C  CD1 . TRP B 1 208 ? -7.264  2.660   14.211  1.00 8.67   ? 208 TRP B CD1 1 
ATOM   3804 C  CD2 . TRP B 1 208 ? -7.990  1.490   12.368  1.00 8.02   ? 208 TRP B CD2 1 
ATOM   3805 N  NE1 . TRP B 1 208 ? -6.987  3.352   13.064  1.00 9.15   ? 208 TRP B NE1 1 
ATOM   3806 C  CE2 . TRP B 1 208 ? -7.487  2.741   11.949  1.00 7.59   ? 208 TRP B CE2 1 
ATOM   3807 C  CE3 . TRP B 1 208 ? -8.542  0.651   11.388  1.00 7.98   ? 208 TRP B CE3 1 
ATOM   3808 C  CZ2 . TRP B 1 208 ? -7.449  3.116   10.595  1.00 7.26   ? 208 TRP B CZ2 1 
ATOM   3809 C  CZ3 . TRP B 1 208 ? -8.480  1.018   10.059  1.00 8.07   ? 208 TRP B CZ3 1 
ATOM   3810 C  CH2 . TRP B 1 208 ? -7.955  2.271   9.656   1.00 7.35   ? 208 TRP B CH2 1 
ATOM   3811 N  N   . THR B 1 209 ? -11.179 -1.342  14.510  1.00 7.98   ? 209 THR B N   1 
ATOM   3812 C  CA  . THR B 1 209 ? -11.609 -2.732  14.654  1.00 8.69   ? 209 THR B CA  1 
ATOM   3813 C  C   . THR B 1 209 ? -11.144 -3.442  13.379  1.00 8.99   ? 209 THR B C   1 
ATOM   3814 O  O   . THR B 1 209 ? -11.570 -3.097  12.281  1.00 9.03   ? 209 THR B O   1 
ATOM   3815 C  CB  . THR B 1 209 ? -13.123 -2.832  14.764  1.00 8.60   ? 209 THR B CB  1 
ATOM   3816 O  OG1 . THR B 1 209 ? -13.513 -2.141  15.912  1.00 9.21   ? 209 THR B OG1 1 
ATOM   3817 C  CG2 . THR B 1 209 ? -13.594 -4.264  14.857  1.00 10.91  ? 209 THR B CG2 1 
ATOM   3818 N  N   . VAL B 1 210 ? -10.176 -4.407  13.508  1.00 7.86   ? 210 VAL B N   1 
ATOM   3819 C  CA  . VAL B 1 210 ? -9.702  -5.138  12.356  1.00 7.37   ? 210 VAL B CA  1 
ATOM   3820 C  C   . VAL B 1 210 ? -10.250 -6.555  12.529  1.00 7.81   ? 210 VAL B C   1 
ATOM   3821 O  O   . VAL B 1 210 ? -9.982  -7.200  13.542  1.00 8.58   ? 210 VAL B O   1 
ATOM   3822 C  CB  . VAL B 1 210 ? -8.166  -5.185  12.297  1.00 7.61   ? 210 VAL B CB  1 
ATOM   3823 C  CG1 . VAL B 1 210 ? -7.710  -5.913  11.046  1.00 8.00   ? 210 VAL B CG1 1 
ATOM   3824 C  CG2 . VAL B 1 210 ? -7.585  -3.737  12.274  1.00 8.36   ? 210 VAL B CG2 1 
ATOM   3825 N  N   . PHE B 1 211 ? -11.092 -6.993  11.591  1.00 8.59   ? 211 PHE B N   1 
ATOM   3826 C  CA  . PHE B 1 211 ? -11.609 -8.346  11.711  1.00 8.66   ? 211 PHE B CA  1 
ATOM   3827 C  C   . PHE B 1 211 ? -10.483 -9.358  11.586  1.00 9.45   ? 211 PHE B C   1 
ATOM   3828 O  O   . PHE B 1 211 ? -9.517  -9.209  10.844  1.00 9.58   ? 211 PHE B O   1 
ATOM   3829 C  CB  . PHE B 1 211 ? -12.708 -8.561  10.656  1.00 9.00   ? 211 PHE B CB  1 
ATOM   3830 C  CG  . PHE B 1 211 ? -13.932 -7.761  10.973  1.00 8.59   ? 211 PHE B CG  1 
ATOM   3831 C  CD1 . PHE B 1 211 ? -14.723 -7.963  12.096  1.00 10.43  ? 211 PHE B CD1 1 
ATOM   3832 C  CD2 . PHE B 1 211 ? -14.260 -6.714  10.111  1.00 8.78   ? 211 PHE B CD2 1 
ATOM   3833 C  CE1 . PHE B 1 211 ? -15.813 -7.149  12.397  1.00 10.96  ? 211 PHE B CE1 1 
ATOM   3834 C  CE2 . PHE B 1 211 ? -15.375 -5.914  10.397  1.00 9.56   ? 211 PHE B CE2 1 
ATOM   3835 C  CZ  . PHE B 1 211 ? -16.132 -6.109  11.525  1.00 10.19  ? 211 PHE B CZ  1 
ATOM   3836 N  N   . ARG B 1 212 ? -10.662 -10.451 12.364  1.00 9.92   ? 212 ARG B N   1 
ATOM   3837 C  CA  . ARG B 1 212 ? -9.608  -11.471 12.405  1.00 9.89   ? 212 ARG B CA  1 
ATOM   3838 C  C   . ARG B 1 212 ? -9.475  -12.189 11.058  1.00 9.61   ? 212 ARG B C   1 
ATOM   3839 O  O   . ARG B 1 212 ? -8.351  -12.506 10.663  1.00 10.97  ? 212 ARG B O   1 
ATOM   3840 C  CB  . ARG B 1 212 ? -9.981  -12.537 13.442  1.00 10.16  ? 212 ARG B CB  1 
ATOM   3841 C  CG  . ARG B 1 212 ? -8.903  -13.615 13.587  1.00 10.03  ? 212 ARG B CG  1 
ATOM   3842 C  CD  . ARG B 1 212 ? -9.362  -14.716 14.584  1.00 12.84  ? 212 ARG B CD  1 
ATOM   3843 N  NE  . ARG B 1 212 ? -8.236  -15.638 14.865  1.00 14.01  ? 212 ARG B NE  1 
ATOM   3844 C  CZ  . ARG B 1 212 ? -8.251  -16.563 15.808  1.00 14.11  ? 212 ARG B CZ  1 
ATOM   3845 N  NH1 . ARG B 1 212 ? -9.377  -16.832 16.446  1.00 17.15  ? 212 ARG B NH1 1 
ATOM   3846 N  NH2 . ARG B 1 212 ? -7.151  -17.235 16.064  1.00 19.18  ? 212 ARG B NH2 1 
ATOM   3847 N  N   . ASN B 1 213 ? -10.582 -12.415 10.376  1.00 9.43   ? 213 ASN B N   1 
ATOM   3848 C  CA  . ASN B 1 213 ? -10.574 -13.307 9.226   1.00 9.00   ? 213 ASN B CA  1 
ATOM   3849 C  C   . ASN B 1 213 ? -10.596 -12.440 7.977   1.00 9.38   ? 213 ASN B C   1 
ATOM   3850 O  O   . ASN B 1 213 ? -11.362 -11.452 7.916   1.00 9.84   ? 213 ASN B O   1 
ATOM   3851 C  CB  . ASN B 1 213 ? -11.809 -14.213 9.258   1.00 12.53  ? 213 ASN B CB  1 
ATOM   3852 C  CG  . ASN B 1 213 ? -11.731 -15.136 10.478  1.00 14.77  ? 213 ASN B CG  1 
ATOM   3853 O  OD1 . ASN B 1 213 ? -10.701 -15.769 10.695  1.00 19.58  ? 213 ASN B OD1 1 
ATOM   3854 N  ND2 . ASN B 1 213 ? -12.766 -15.217 11.290  1.00 17.80  ? 213 ASN B ND2 1 
ATOM   3855 N  N   . PRO B 1 214 ? -9.794  -12.748 6.961   1.00 10.04  ? 214 PRO B N   1 
ATOM   3856 C  CA  . PRO B 1 214 ? -9.859  -12.048 5.682   1.00 8.63   ? 214 PRO B CA  1 
ATOM   3857 C  C   . PRO B 1 214 ? -11.047 -12.495 4.837   1.00 8.37   ? 214 PRO B C   1 
ATOM   3858 O  O   . PRO B 1 214 ? -11.647 -13.596 5.051   1.00 10.16  ? 214 PRO B O   1 
ATOM   3859 C  CB  . PRO B 1 214 ? -8.543  -12.422 5.016   1.00 10.77  ? 214 PRO B CB  1 
ATOM   3860 C  CG  . PRO B 1 214 ? -8.332  -13.887 5.472   1.00 12.48  ? 214 PRO B CG  1 
ATOM   3861 C  CD  . PRO B 1 214 ? -8.848  -13.899 6.910   1.00 12.07  ? 214 PRO B CD  1 
ATOM   3862 N  N   . VAL B 1 215 ? -11.311 -11.711 3.800   1.00 8.04   ? 215 VAL B N   1 
ATOM   3863 C  CA  . VAL B 1 215 ? -12.173 -12.086 2.691   1.00 7.99   ? 215 VAL B CA  1 
ATOM   3864 C  C   . VAL B 1 215 ? -11.273 -12.317 1.477   1.00 8.20   ? 215 VAL B C   1 
ATOM   3865 O  O   . VAL B 1 215 ? -10.087 -12.006 1.500   1.00 9.03   ? 215 VAL B O   1 
ATOM   3866 C  CB  . VAL B 1 215 ? -13.243 -11.014 2.358   1.00 9.32   ? 215 VAL B CB  1 
ATOM   3867 C  CG1 . VAL B 1 215 ? -14.194 -10.762 3.537   1.00 9.74   ? 215 VAL B CG1 1 
ATOM   3868 C  CG2 . VAL B 1 215 ? -12.631 -9.671  1.824   1.00 11.23  ? 215 VAL B CG2 1 
ATOM   3869 N  N   . GLN B 1 216 ? -11.841 -12.929 0.411   1.00 9.12   ? 216 GLN B N   1 
ATOM   3870 C  CA  . GLN B 1 216 ? -11.111 -13.181 -0.824  1.00 7.96   ? 216 GLN B CA  1 
ATOM   3871 C  C   . GLN B 1 216 ? -11.721 -12.408 -1.985  1.00 7.09   ? 216 GLN B C   1 
ATOM   3872 O  O   . GLN B 1 216 ? -12.939 -12.274 -2.073  1.00 8.77   ? 216 GLN B O   1 
ATOM   3873 C  CB  . GLN B 1 216 ? -11.146 -14.683 -1.220  1.00 9.14   ? 216 GLN B CB  1 
ATOM   3874 C  CG  . GLN B 1 216 ? -10.493 -15.579 -0.178  1.00 11.42  ? 216 GLN B CG  1 
ATOM   3875 C  CD  . GLN B 1 216 ? -10.422 -17.022 -0.634  1.00 12.77  ? 216 GLN B CD  1 
ATOM   3876 O  OE1 . GLN B 1 216 ? -11.027 -17.454 -1.640  1.00 13.22  ? 216 GLN B OE1 1 
ATOM   3877 N  NE2 . GLN B 1 216 ? -9.635  -17.750 0.142   1.00 20.27  ? 216 GLN B NE2 1 
ATOM   3878 N  N   . ILE B 1 217 ? -10.813 -11.852 -2.789  1.00 7.82   ? 217 ILE B N   1 
ATOM   3879 C  CA  . ILE B 1 217 ? -11.158 -11.386 -4.126  1.00 8.36   ? 217 ILE B CA  1 
ATOM   3880 C  C   . ILE B 1 217 ? -10.209 -12.062 -5.137  1.00 8.13   ? 217 ILE B C   1 
ATOM   3881 O  O   . ILE B 1 217 ? -9.148  -12.547 -4.710  1.00 8.90   ? 217 ILE B O   1 
ATOM   3882 C  CB  . ILE B 1 217 ? -11.159 -9.840  -4.191  1.00 6.86   ? 217 ILE B CB  1 
ATOM   3883 C  CG1 . ILE B 1 217 ? -9.763  -9.292  -4.190  1.00 7.53   ? 217 ILE B CG1 1 
ATOM   3884 C  CG2 . ILE B 1 217 ? -12.118 -9.220  -3.177  1.00 8.96   ? 217 ILE B CG2 1 
ATOM   3885 C  CD1 . ILE B 1 217 ? -9.732  -7.746  -4.240  1.00 9.29   ? 217 ILE B CD1 1 
ATOM   3886 N  N   . SER B 1 218 ? -10.549 -12.092 -6.422  1.00 7.68   ? 218 SER B N   1 
ATOM   3887 C  CA  . SER B 1 218 ? -9.697  -12.885 -7.302  1.00 7.57   ? 218 SER B CA  1 
ATOM   3888 C  C   . SER B 1 218 ? -8.482  -12.098 -7.789  1.00 6.90   ? 218 SER B C   1 
ATOM   3889 O  O   . SER B 1 218 ? -8.446  -10.890 -7.688  1.00 8.98   ? 218 SER B O   1 
ATOM   3890 C  CB  . SER B 1 218 ? -10.504 -13.372 -8.478  1.00 9.59   ? 218 SER B CB  1 
ATOM   3891 O  OG  . SER B 1 218 ? -10.933 -12.277 -9.298  1.00 9.27   ? 218 SER B OG  1 
ATOM   3892 N  N   . GLN B 1 219 ? -7.532  -12.799 -8.370  1.00 8.79   ? 219 GLN B N   1 
ATOM   3893 C  CA  . GLN B 1 219 ? -6.408  -12.221 -9.096  1.00 8.74   ? 219 GLN B CA  1 
ATOM   3894 C  C   . GLN B 1 219 ? -6.939  -11.196 -10.097 1.00 9.16   ? 219 GLN B C   1 
ATOM   3895 O  O   . GLN B 1 219 ? -6.364  -10.111 -10.235 1.00 10.12  ? 219 GLN B O   1 
ATOM   3896 C  CB  . GLN B 1 219 ? -5.622  -13.343 -9.810  1.00 12.30  ? 219 GLN B CB  1 
ATOM   3897 C  CG  . GLN B 1 219 ? -4.327  -12.822 -10.453 1.00 17.54  ? 219 GLN B CG  1 
ATOM   3898 C  CD  . GLN B 1 219 ? -4.376  -12.091 -11.771 1.00 21.63  ? 219 GLN B CD  1 
ATOM   3899 O  OE1 . GLN B 1 219 ? -3.641  -11.103 -12.001 1.00 28.17  ? 219 GLN B OE1 1 
ATOM   3900 N  NE2 . GLN B 1 219 ? -5.288  -12.531 -12.632 1.00 32.61  ? 219 GLN B NE2 1 
ATOM   3901 N  N   . GLU B 1 220 ? -7.966  -11.550 -10.836 1.00 8.87   ? 220 GLU B N   1 
ATOM   3902 C  CA  . GLU B 1 220 ? -8.470  -10.650 -11.870 1.00 9.44   ? 220 GLU B CA  1 
ATOM   3903 C  C   . GLU B 1 220 ? -9.038  -9.362  -11.242 1.00 8.34   ? 220 GLU B C   1 
ATOM   3904 O  O   . GLU B 1 220 ? -8.904  -8.274  -11.821 1.00 10.31  ? 220 GLU B O   1 
ATOM   3905 C  CB  . GLU B 1 220 ? -9.465  -11.328 -12.809 1.00 10.31  ? 220 GLU B CB  1 
ATOM   3906 C  CG  . GLU B 1 220 ? -8.895  -12.519 -13.595 1.00 11.04  ? 220 GLU B CG  1 
ATOM   3907 C  CD  . GLU B 1 220 ? -8.665  -13.840 -12.877 1.00 12.29  ? 220 GLU B CD  1 
ATOM   3908 O  OE1 . GLU B 1 220 ? -9.096  -14.004 -11.692 1.00 13.42  ? 220 GLU B OE1 1 
ATOM   3909 O  OE2 . GLU B 1 220 ? -8.081  -14.713 -13.558 1.00 21.00  ? 220 GLU B OE2 1 
ATOM   3910 N  N   . GLN B 1 221 ? -9.746  -9.492  -10.119 1.00 8.03   ? 221 GLN B N   1 
ATOM   3911 C  CA  . GLN B 1 221 ? -10.344 -8.317  -9.506  1.00 7.38   ? 221 GLN B CA  1 
ATOM   3912 C  C   . GLN B 1 221 ? -9.223  -7.467  -8.937  1.00 9.68   ? 221 GLN B C   1 
ATOM   3913 O  O   . GLN B 1 221 ? -9.301  -6.236  -9.037  1.00 9.42   ? 221 GLN B O   1 
ATOM   3914 C  CB  . GLN B 1 221 ? -11.225 -8.778  -8.341  1.00 8.75   ? 221 GLN B CB  1 
ATOM   3915 C  CG  . GLN B 1 221 ? -12.578 -9.284  -8.765  1.00 9.54   ? 221 GLN B CG  1 
ATOM   3916 C  CD  . GLN B 1 221 ? -13.460 -9.737  -7.636  1.00 8.97   ? 221 GLN B CD  1 
ATOM   3917 O  OE1 . GLN B 1 221 ? -13.139 -10.710 -6.887  1.00 9.60   ? 221 GLN B OE1 1 
ATOM   3918 N  NE2 . GLN B 1 221 ? -14.601 -9.058  -7.473  1.00 10.71  ? 221 GLN B NE2 1 
ATOM   3919 N  N   . LEU B 1 222 ? -8.169  -8.063  -8.378  1.00 7.97   ? 222 LEU B N   1 
ATOM   3920 C  CA  . LEU B 1 222 ? -7.019  -7.302  -7.903  1.00 8.39   ? 222 LEU B CA  1 
ATOM   3921 C  C   . LEU B 1 222 ? -6.393  -6.529  -9.048  1.00 8.38   ? 222 LEU B C   1 
ATOM   3922 O  O   . LEU B 1 222 ? -6.093  -5.333  -8.899  1.00 8.47   ? 222 LEU B O   1 
ATOM   3923 C  CB  . LEU B 1 222 ? -6.000  -8.185  -7.155  1.00 9.45   ? 222 LEU B CB  1 
ATOM   3924 C  CG  . LEU B 1 222 ? -6.426  -8.501  -5.713  1.00 9.40   ? 222 LEU B CG  1 
ATOM   3925 C  CD1 . LEU B 1 222 ? -5.747  -9.798  -5.219  1.00 10.45  ? 222 LEU B CD1 1 
ATOM   3926 C  CD2 . LEU B 1 222 ? -6.073  -7.335  -4.792  1.00 8.39   ? 222 LEU B CD2 1 
ATOM   3927 N  N   . LEU B 1 223 ? -6.144  -7.170  -10.176 1.00 8.28   ? 223 LEU B N   1 
ATOM   3928 C  CA  . LEU B 1 223 ? -5.497  -6.554  -11.330 1.00 7.82   ? 223 LEU B CA  1 
ATOM   3929 C  C   . LEU B 1 223 ? -6.374  -5.414  -11.788 1.00 9.73   ? 223 LEU B C   1 
ATOM   3930 O  O   . LEU B 1 223 ? -5.850  -4.382  -12.151 1.00 10.22  ? 223 LEU B O   1 
ATOM   3931 C  CB  . LEU B 1 223 ? -5.240  -7.588  -12.461 1.00 9.86   ? 223 LEU B CB  1 
ATOM   3932 C  CG  . LEU B 1 223 ? -4.589  -6.994  -13.721 1.00 11.34  ? 223 LEU B CG  1 
ATOM   3933 C  CD1 . LEU B 1 223 ? -3.200  -6.480  -13.394 1.00 13.08  ? 223 LEU B CD1 1 
ATOM   3934 C  CD2 . LEU B 1 223 ? -4.504  -8.027  -14.779 1.00 13.34  ? 223 LEU B CD2 1 
ATOM   3935 N  N   . ALA B 1 224 ? -7.663  -5.594  -11.829 1.00 9.68   ? 224 ALA B N   1 
ATOM   3936 C  CA  . ALA B 1 224 ? -8.592  -4.561  -12.283 1.00 11.03  ? 224 ALA B CA  1 
ATOM   3937 C  C   . ALA B 1 224 ? -8.489  -3.396  -11.320 1.00 9.23   ? 224 ALA B C   1 
ATOM   3938 O  O   . ALA B 1 224 ? -8.360  -2.234  -11.760 1.00 10.22  ? 224 ALA B O   1 
ATOM   3939 C  CB  . ALA B 1 224 ? -10.044 -5.017  -12.415 1.00 11.93  ? 224 ALA B CB  1 
ATOM   3940 N  N   . LEU B 1 225 ? -8.516  -3.643  -10.016 1.00 9.56   ? 225 LEU B N   1 
ATOM   3941 C  CA  . LEU B 1 225 ? -8.484  -2.519  -9.087  1.00 8.91   ? 225 LEU B CA  1 
ATOM   3942 C  C   . LEU B 1 225 ? -7.141  -1.797  -9.188  1.00 10.22  ? 225 LEU B C   1 
ATOM   3943 O  O   . LEU B 1 225 ? -7.131  -0.561  -9.073  1.00 9.83   ? 225 LEU B O   1 
ATOM   3944 C  CB  . LEU B 1 225 ? -8.612  -3.117  -7.685  1.00 9.54   ? 225 LEU B CB  1 
ATOM   3945 C  CG  . LEU B 1 225 ? -8.405  -2.181  -6.513  1.00 9.40   ? 225 LEU B CG  1 
ATOM   3946 C  CD1 . LEU B 1 225 ? -9.449  -1.089  -6.477  1.00 10.66  ? 225 LEU B CD1 1 
ATOM   3947 C  CD2 . LEU B 1 225 ? -8.434  -3.018  -5.218  1.00 13.08  ? 225 LEU B CD2 1 
ATOM   3948 N  N   . GLU B 1 226 ? -6.026  -2.474  -9.365  1.00 9.05   ? 226 GLU B N   1 
ATOM   3949 C  CA  . GLU B 1 226 ? -4.675  -1.892  -9.376  1.00 10.03  ? 226 GLU B CA  1 
ATOM   3950 C  C   . GLU B 1 226 ? -4.404  -1.121  -10.693 1.00 9.77   ? 226 GLU B C   1 
ATOM   3951 O  O   . GLU B 1 226 ? -3.376  -0.444  -10.747 1.00 13.93  ? 226 GLU B O   1 
ATOM   3952 C  CB  . GLU B 1 226 ? -3.652  -3.040  -9.262  1.00 10.40  ? 226 GLU B CB  1 
ATOM   3953 C  CG  . GLU B 1 226 ? -3.676  -3.740  -7.891  1.00 9.74   ? 226 GLU B CG  1 
ATOM   3954 C  CD  . GLU B 1 226 ? -3.236  -5.183  -7.902  1.00 9.15   ? 226 GLU B CD  1 
ATOM   3955 O  OE1 . GLU B 1 226 ? -2.875  -5.619  -8.981  1.00 13.28  ? 226 GLU B OE1 1 
ATOM   3956 O  OE2 . GLU B 1 226 ? -3.302  -5.799  -6.830  1.00 10.08  ? 226 GLU B OE2 1 
ATOM   3957 N  N   . THR B 1 227 ? -5.266  -1.261  -11.715 1.00 9.62   ? 227 THR B N   1 
ATOM   3958 C  CA  . THR B 1 227 ? -5.078  -0.575  -13.011 1.00 9.12   ? 227 THR B CA  1 
ATOM   3959 C  C   . THR B 1 227 ? -6.225  0.397   -13.311 1.00 9.25   ? 227 THR B C   1 
ATOM   3960 O  O   . THR B 1 227 ? -6.249  0.974   -14.384 1.00 14.04  ? 227 THR B O   1 
ATOM   3961 C  CB  . THR B 1 227 ? -4.937  -1.598  -14.165 1.00 10.83  ? 227 THR B CB  1 
ATOM   3962 O  OG1 . THR B 1 227 ? -6.063  -2.489  -14.181 1.00 10.82  ? 227 THR B OG1 1 
ATOM   3963 C  CG2 . THR B 1 227 ? -3.645  -2.379  -13.986 1.00 11.85  ? 227 THR B CG2 1 
ATOM   3964 N  N   . ALA B 1 228 ? -7.209  0.487   -12.429 1.00 9.51   ? 228 ALA B N   1 
ATOM   3965 C  CA  . ALA B 1 228 ? -8.442  1.203   -12.781 1.00 11.36  ? 228 ALA B CA  1 
ATOM   3966 C  C   . ALA B 1 228 ? -8.312  2.729   -12.597 1.00 10.38  ? 228 ALA B C   1 
ATOM   3967 O  O   . ALA B 1 228 ? -9.082  3.489   -13.207 1.00 16.18  ? 228 ALA B O   1 
ATOM   3968 C  CB  . ALA B 1 228 ? -9.613  0.764   -11.904 1.00 13.57  ? 228 ALA B CB  1 
ATOM   3969 N  N   . LEU B 1 229 ? -7.414  3.170   -11.688 1.00 10.81  ? 229 LEU B N   1 
ATOM   3970 C  CA  . LEU B 1 229 ? -7.581  4.500   -11.128 1.00 8.77   ? 229 LEU B CA  1 
ATOM   3971 C  C   . LEU B 1 229 ? -6.281  5.268   -11.162 1.00 9.69   ? 229 LEU B C   1 
ATOM   3972 O  O   . LEU B 1 229 ? -5.181  4.747   -11.141 1.00 9.91   ? 229 LEU B O   1 
ATOM   3973 C  CB  . LEU B 1 229 ? -8.004  4.418   -9.660  1.00 10.79  ? 229 LEU B CB  1 
ATOM   3974 C  CG  . LEU B 1 229 ? -9.373  3.796   -9.377  1.00 9.78   ? 229 LEU B CG  1 
ATOM   3975 C  CD1 . LEU B 1 229 ? -9.460  3.372   -7.917  1.00 12.13  ? 229 LEU B CD1 1 
ATOM   3976 C  CD2 . LEU B 1 229 ? -10.519 4.730   -9.776  1.00 14.38  ? 229 LEU B CD2 1 
ATOM   3977 N  N   . TYR B 1 230 ? -6.451  6.604   -11.250 1.00 8.70   ? 230 TYR B N   1 
ATOM   3978 C  CA  . TYR B 1 230 ? -5.405  7.647   -11.312 1.00 10.21  ? 230 TYR B CA  1 
ATOM   3979 C  C   . TYR B 1 230 ? -5.558  8.622   -10.159 1.00 8.27   ? 230 TYR B C   1 
ATOM   3980 O  O   . TYR B 1 230 ? -6.701  8.901   -9.738  1.00 10.72  ? 230 TYR B O   1 
ATOM   3981 C  CB  . TYR B 1 230 ? -5.363  8.347   -12.679 1.00 11.59  ? 230 TYR B CB  1 
ATOM   3982 C  CG  . TYR B 1 230 ? -4.795  7.460   -13.761 1.00 9.12   ? 230 TYR B CG  1 
ATOM   3983 C  CD1 . TYR B 1 230 ? -5.552  6.429   -14.308 1.00 10.97  ? 230 TYR B CD1 1 
ATOM   3984 C  CD2 . TYR B 1 230 ? -3.433  7.541   -14.095 1.00 11.16  ? 230 TYR B CD2 1 
ATOM   3985 C  CE1 . TYR B 1 230 ? -4.982  5.495   -15.159 1.00 14.21  ? 230 TYR B CE1 1 
ATOM   3986 C  CE2 . TYR B 1 230 ? -2.848  6.625   -14.957 1.00 12.70  ? 230 TYR B CE2 1 
ATOM   3987 C  CZ  . TYR B 1 230 ? -3.630  5.579   -15.479 1.00 14.41  ? 230 TYR B CZ  1 
ATOM   3988 O  OH  . TYR B 1 230 ? -3.123  4.642   -16.321 1.00 18.91  ? 230 TYR B OH  1 
ATOM   3989 N  N   . CYS B 1 231 ? -4.401  9.138   -9.682  1.00 10.10  ? 231 CYS B N   1 
ATOM   3990 C  CA  . CYS B 1 231 ? -4.347  10.199  -8.672  1.00 10.27  ? 231 CYS B CA  1 
ATOM   3991 C  C   . CYS B 1 231 ? -4.625  11.571  -9.290  1.00 9.31   ? 231 CYS B C   1 
ATOM   3992 O  O   . CYS B 1 231 ? -4.811  12.568  -8.569  1.00 12.98  ? 231 CYS B O   1 
ATOM   3993 C  CB  . CYS B 1 231 ? -2.992  10.185  -7.957  1.00 11.57  ? 231 CYS B CB  1 
ATOM   3994 S  SG  . CYS B 1 231 ? -2.643  8.680   -7.030  1.00 12.83  ? 231 CYS B SG  1 
ATOM   3995 N  N   . THR B 1 232 ? -4.527  11.612  -10.615 1.00 10.36  ? 232 THR B N   1 
ATOM   3996 C  CA  . THR B 1 232 ? -4.445  12.866  -11.345 1.00 10.50  ? 232 THR B CA  1 
ATOM   3997 C  C   . THR B 1 232 ? -5.744  13.107  -12.139 1.00 8.66   ? 232 THR B C   1 
ATOM   3998 O  O   . THR B 1 232 ? -6.522  12.218  -12.463 1.00 10.49  ? 232 THR B O   1 
ATOM   3999 C  CB  . THR B 1 232 ? -3.162  12.883  -12.234 1.00 8.95   ? 232 THR B CB  1 
ATOM   4000 O  OG1 . THR B 1 232 ? -3.072  11.575  -12.850 1.00 9.58   ? 232 THR B OG1 1 
ATOM   4001 C  CG2 . THR B 1 232 ? -1.950  13.112  -11.375 1.00 10.89  ? 232 THR B CG2 1 
ATOM   4002 N  N   . HIS B 1 233 ? -5.943  14.389  -12.490 1.00 11.43  ? 233 HIS B N   1 
ATOM   4003 C  CA  . HIS B 1 233 ? -7.031  14.737  -13.395 1.00 11.93  ? 233 HIS B CA  1 
ATOM   4004 C  C   . HIS B 1 233 ? -6.920  14.083  -14.771 1.00 10.95  ? 233 HIS B C   1 
ATOM   4005 O  O   . HIS B 1 233 ? -5.841  13.815  -15.261 1.00 11.23  ? 233 HIS B O   1 
ATOM   4006 C  CB  . HIS B 1 233 ? -7.138  16.264  -13.575 1.00 14.51  ? 233 HIS B CB  1 
ATOM   4007 C  CG  . HIS B 1 233 ? -7.530  16.972  -12.349 1.00 15.44  ? 233 HIS B CG  1 
ATOM   4008 N  ND1 . HIS B 1 233 ? -6.753  17.991  -11.866 1.00 22.62  ? 233 HIS B ND1 1 
ATOM   4009 C  CD2 . HIS B 1 233 ? -8.667  16.979  -11.634 1.00 17.82  ? 233 HIS B CD2 1 
ATOM   4010 C  CE1 . HIS B 1 233 ? -7.330  18.550  -10.805 1.00 26.01  ? 233 HIS B CE1 1 
ATOM   4011 N  NE2 . HIS B 1 233 ? -8.513  17.930  -10.629 1.00 23.69  ? 233 HIS B NE2 1 
ATOM   4012 N  N   . MET B 1 234 ? -8.065  13.936  -15.450 1.00 10.23  ? 234 MET B N   1 
ATOM   4013 C  CA  . MET B 1 234 ? -8.077  13.408  -16.802 1.00 11.54  ? 234 MET B CA  1 
ATOM   4014 C  C   . MET B 1 234 ? -7.133  14.158  -17.735 1.00 11.16  ? 234 MET B C   1 
ATOM   4015 O  O   . MET B 1 234 ? -6.633  13.588  -18.690 1.00 11.13  ? 234 MET B O   1 
ATOM   4016 C  CB  . MET B 1 234 ? -9.516  13.433  -17.325 1.00 11.78  ? 234 MET B CB  1 
ATOM   4017 C  CG  . MET B 1 234 ? -9.743  12.771  -18.685 1.00 14.71  ? 234 MET B CG  1 
ATOM   4018 S  SD  . MET B 1 234 ? -11.561 12.642  -18.963 1.00 19.80  ? 234 MET B SD  1 
ATOM   4019 C  CE  . MET B 1 234 ? -11.601 11.772  -20.544 1.00 20.21  ? 234 MET B CE  1 
ATOM   4020 N  N   . ASP B 1 235 ? -7.001  15.490  -17.550 1.00 12.53  ? 235 ASP B N   1 
ATOM   4021 C  CA  . ASP B 1 235 ? -6.209  16.278  -18.487 1.00 14.60  ? 235 ASP B CA  1 
ATOM   4022 C  C   . ASP B 1 235 ? -4.810  16.580  -17.974 1.00 13.72  ? 235 ASP B C   1 
ATOM   4023 O  O   . ASP B 1 235 ? -4.109  17.449  -18.508 1.00 16.33  ? 235 ASP B O   1 
ATOM   4024 C  CB  . ASP B 1 235 ? -6.942  17.554  -18.924 1.00 18.50  ? 235 ASP B CB  1 
ATOM   4025 C  CG  . ASP B 1 235 ? -7.052  18.488  -17.755 1.00 22.45  ? 235 ASP B CG  1 
ATOM   4026 O  OD1 . ASP B 1 235 ? -6.680  18.092  -16.632 1.00 28.25  ? 235 ASP B OD1 1 
ATOM   4027 O  OD2 . ASP B 1 235 ? -7.568  19.610  -17.966 1.00 36.79  ? 235 ASP B OD2 1 
ATOM   4028 N  N   . ASP B 1 236 ? -4.363  15.887  -16.933 1.00 13.07  ? 236 ASP B N   1 
ATOM   4029 C  CA  . ASP B 1 236 ? -3.078  16.206  -16.348 1.00 11.43  ? 236 ASP B CA  1 
ATOM   4030 C  C   . ASP B 1 236 ? -1.958  15.699  -17.259 1.00 11.58  ? 236 ASP B C   1 
ATOM   4031 O  O   . ASP B 1 236 ? -1.921  14.510  -17.605 1.00 11.85  ? 236 ASP B O   1 
ATOM   4032 C  CB  . ASP B 1 236 ? -2.940  15.542  -14.966 1.00 11.81  ? 236 ASP B CB  1 
ATOM   4033 C  CG  . ASP B 1 236 ? -1.806  16.126  -14.124 1.00 12.13  ? 236 ASP B CG  1 
ATOM   4034 O  OD1 . ASP B 1 236 ? -0.725  16.275  -14.665 1.00 13.55  ? 236 ASP B OD1 1 
ATOM   4035 O  OD2 . ASP B 1 236 ? -1.993  16.391  -12.898 1.00 16.09  ? 236 ASP B OD2 1 
ATOM   4036 N  N   . PRO B 1 237 ? -0.973  16.522  -17.645 1.00 10.47  ? 237 PRO B N   1 
ATOM   4037 C  CA  . PRO B 1 237 ? 0.132   16.034  -18.484 1.00 11.74  ? 237 PRO B CA  1 
ATOM   4038 C  C   . PRO B 1 237 ? 1.178   15.165  -17.772 1.00 11.23  ? 237 PRO B C   1 
ATOM   4039 O  O   . PRO B 1 237 ? 2.110   14.641  -18.425 1.00 12.04  ? 237 PRO B O   1 
ATOM   4040 C  CB  . PRO B 1 237 ? 0.756   17.364  -18.999 1.00 11.82  ? 237 PRO B CB  1 
ATOM   4041 C  CG  . PRO B 1 237 ? 0.526   18.240  -17.795 1.00 13.23  ? 237 PRO B CG  1 
ATOM   4042 C  CD  . PRO B 1 237 ? -0.905  17.977  -17.362 1.00 10.85  ? 237 PRO B CD  1 
ATOM   4043 N  N   A SER B 1 238 ? 1.028   15.022  -16.448 0.50 10.86  ? 238 SER B N   1 
ATOM   4044 N  N   B SER B 1 238 ? 1.052   15.018  -16.448 0.50 10.76  ? 238 SER B N   1 
ATOM   4045 C  CA  A SER B 1 238 ? 1.900   14.172  -15.637 0.50 10.57  ? 238 SER B CA  1 
ATOM   4046 C  CA  B SER B 1 238 ? 1.944   14.133  -15.698 0.50 10.76  ? 238 SER B CA  1 
ATOM   4047 C  C   A SER B 1 238 ? 1.035   13.169  -14.890 0.50 10.43  ? 238 SER B C   1 
ATOM   4048 C  C   B SER B 1 238 ? 1.091   13.154  -14.911 0.50 10.59  ? 238 SER B C   1 
ATOM   4049 O  O   A SER B 1 238 ? 0.870   13.226  -13.672 0.50 11.61  ? 238 SER B O   1 
ATOM   4050 O  O   B SER B 1 238 ? 1.026   13.223  -13.688 0.50 11.02  ? 238 SER B O   1 
ATOM   4051 C  CB  A SER B 1 238 ? 2.709   15.027  -14.685 0.50 12.65  ? 238 SER B CB  1 
ATOM   4052 C  CB  B SER B 1 238 ? 2.821   14.948  -14.776 0.50 14.57  ? 238 SER B CB  1 
ATOM   4053 O  OG  A SER B 1 238 ? 3.635   15.852  -15.390 0.50 14.59  ? 238 SER B OG  1 
ATOM   4054 O  OG  B SER B 1 238 ? 3.791   14.150  -14.109 0.50 21.34  ? 238 SER B OG  1 
ATOM   4055 N  N   . PRO B 1 239 ? 0.436   12.196  -15.599 1.00 9.56   ? 239 PRO B N   1 
ATOM   4056 C  CA  . PRO B 1 239 ? -0.445  11.240  -14.919 1.00 9.88   ? 239 PRO B CA  1 
ATOM   4057 C  C   . PRO B 1 239 ? 0.306   10.406  -13.865 1.00 9.05   ? 239 PRO B C   1 
ATOM   4058 O  O   . PRO B 1 239 ? 1.498   10.086  -14.038 1.00 11.30  ? 239 PRO B O   1 
ATOM   4059 C  CB  . PRO B 1 239 ? -0.932  10.330  -16.056 1.00 12.09  ? 239 PRO B CB  1 
ATOM   4060 C  CG  . PRO B 1 239 ? -0.099  10.653  -17.243 1.00 15.73  ? 239 PRO B CG  1 
ATOM   4061 C  CD  . PRO B 1 239 ? 0.549   11.988  -17.050 1.00 10.02  ? 239 PRO B CD  1 
ATOM   4062 N  N   . ARG B 1 240 ? -0.398  10.065  -12.780 1.00 9.08   ? 240 ARG B N   1 
ATOM   4063 C  CA  . ARG B 1 240 ? 0.121   9.189   -11.752 1.00 10.43  ? 240 ARG B CA  1 
ATOM   4064 C  C   . ARG B 1 240 ? -0.922  8.138   -11.425 1.00 8.50   ? 240 ARG B C   1 
ATOM   4065 O  O   . ARG B 1 240 ? -2.054  8.457   -11.053 1.00 10.56  ? 240 ARG B O   1 
ATOM   4066 C  CB  . ARG B 1 240 ? 0.433   9.980   -10.486 1.00 11.41  ? 240 ARG B CB  1 
ATOM   4067 C  CG  . ARG B 1 240 ? 1.628   10.917  -10.646 1.00 12.90  ? 240 ARG B CG  1 
ATOM   4068 C  CD  . ARG B 1 240 ? 1.966   11.723  -9.381  1.00 13.39  ? 240 ARG B CD  1 
ATOM   4069 N  NE  . ARG B 1 240 ? 0.923   12.732  -9.117  1.00 14.32  ? 240 ARG B NE  1 
ATOM   4070 C  CZ  . ARG B 1 240 ? 0.039   12.643  -8.102  1.00 13.91  ? 240 ARG B CZ  1 
ATOM   4071 N  NH1 . ARG B 1 240 ? 0.059   11.592  -7.295  1.00 13.25  ? 240 ARG B NH1 1 
ATOM   4072 N  NH2 . ARG B 1 240 ? -0.885  13.570  -7.903  1.00 17.32  ? 240 ARG B NH2 1 
ATOM   4073 N  N   . GLU B 1 241 ? -0.550  6.867   -11.540 1.00 9.09   ? 241 GLU B N   1 
ATOM   4074 C  CA  . GLU B 1 241 ? -1.450  5.776   -11.223 1.00 9.72   ? 241 GLU B CA  1 
ATOM   4075 C  C   . GLU B 1 241 ? -1.730  5.717   -9.726  1.00 8.91   ? 241 GLU B C   1 
ATOM   4076 O  O   . GLU B 1 241 ? -0.823  5.911   -8.896  1.00 10.02  ? 241 GLU B O   1 
ATOM   4077 C  CB  . GLU B 1 241 ? -0.753  4.458   -11.634 1.00 12.28  ? 241 GLU B CB  1 
ATOM   4078 C  CG  . GLU B 1 241 ? -0.620  4.333   -13.113 1.00 13.52  ? 241 GLU B CG  1 
ATOM   4079 C  CD  . GLU B 1 241 ? 0.442   3.386   -13.616 1.00 16.78  ? 241 GLU B CD  1 
ATOM   4080 O  OE1 . GLU B 1 241 ? 1.541   3.409   -13.081 1.00 27.02  ? 241 GLU B OE1 1 
ATOM   4081 O  OE2 . GLU B 1 241 ? 0.165   2.628   -14.512 1.00 26.40  ? 241 GLU B OE2 1 
ATOM   4082 N  N   . MET B 1 242 ? -2.987  5.366   -9.380  1.00 8.97   ? 242 MET B N   1 
ATOM   4083 C  CA  . MET B 1 242 ? -3.332  5.159   -7.977  1.00 9.30   ? 242 MET B CA  1 
ATOM   4084 C  C   . MET B 1 242 ? -2.981  3.703   -7.634  1.00 8.19   ? 242 MET B C   1 
ATOM   4085 O  O   . MET B 1 242 ? -3.812  2.808   -7.836  1.00 10.20  ? 242 MET B O   1 
ATOM   4086 C  CB  . MET B 1 242 ? -4.815  5.459   -7.701  1.00 9.18   ? 242 MET B CB  1 
ATOM   4087 C  CG  . MET B 1 242 ? -5.082  5.508   -6.167  1.00 9.81   ? 242 MET B CG  1 
ATOM   4088 S  SD  . MET B 1 242 ? -6.823  5.828   -5.877  1.00 10.33  ? 242 MET B SD  1 
ATOM   4089 C  CE  . MET B 1 242 ? -6.771  7.560   -6.029  1.00 8.83   ? 242 MET B CE  1 
ATOM   4090 N  N   . ILE B 1 243 ? -1.712  3.494   -7.165  1.00 8.05   ? 243 ILE B N   1 
ATOM   4091 C  CA  . ILE B 1 243 ? -1.166  2.199   -6.789  1.00 8.96   ? 243 ILE B CA  1 
ATOM   4092 C  C   . ILE B 1 243 ? -0.410  2.384   -5.483  1.00 8.65   ? 243 ILE B C   1 
ATOM   4093 O  O   . ILE B 1 243 ? 0.005   3.501   -5.153  1.00 8.46   ? 243 ILE B O   1 
ATOM   4094 C  CB  . ILE B 1 243 ? -0.244  1.639   -7.889  1.00 9.57   ? 243 ILE B CB  1 
ATOM   4095 C  CG1 . ILE B 1 243 ? 0.827   2.679   -8.239  1.00 10.55  ? 243 ILE B CG1 1 
ATOM   4096 C  CG2 . ILE B 1 243 ? -1.061  1.235   -9.102  1.00 11.77  ? 243 ILE B CG2 1 
ATOM   4097 C  CD1 . ILE B 1 243 ? 1.910   2.214   -9.226  1.00 13.36  ? 243 ILE B CD1 1 
ATOM   4098 N  N   . ASN B 1 244 ? -0.181  1.297   -4.763  1.00 8.20   ? 244 ASN B N   1 
ATOM   4099 C  CA  . ASN B 1 244 ? 0.658   1.291   -3.567  1.00 7.73   ? 244 ASN B CA  1 
ATOM   4100 C  C   . ASN B 1 244 ? 0.142   2.340   -2.592  1.00 6.35   ? 244 ASN B C   1 
ATOM   4101 O  O   . ASN B 1 244 ? 0.956   2.965   -1.892  1.00 9.04   ? 244 ASN B O   1 
ATOM   4102 C  CB  . ASN B 1 244 ? 2.139   1.439   -3.948  1.00 9.07   ? 244 ASN B CB  1 
ATOM   4103 C  CG  . ASN B 1 244 ? 2.597   0.409   -4.935  1.00 8.27   ? 244 ASN B CG  1 
ATOM   4104 O  OD1 . ASN B 1 244 ? 2.194   -0.750  -4.826  1.00 11.86  ? 244 ASN B OD1 1 
ATOM   4105 N  ND2 . ASN B 1 244 ? 3.357   0.837   -5.956  1.00 14.31  ? 244 ASN B ND2 1 
ATOM   4106 N  N   . ASN B 1 245 ? -1.185  2.462   -2.481  1.00 7.21   ? 245 ASN B N   1 
ATOM   4107 C  CA  . ASN B 1 245 ? -1.719  3.520   -1.643  1.00 7.02   ? 245 ASN B CA  1 
ATOM   4108 C  C   . ASN B 1 245 ? -1.938  2.930   -0.239  1.00 6.95   ? 245 ASN B C   1 
ATOM   4109 O  O   . ASN B 1 245 ? -3.013  2.994   0.309   1.00 8.35   ? 245 ASN B O   1 
ATOM   4110 C  CB  . ASN B 1 245 ? -3.039  4.069   -2.208  1.00 7.66   ? 245 ASN B CB  1 
ATOM   4111 C  CG  . ASN B 1 245 ? -4.127  3.072   -2.425  1.00 6.48   ? 245 ASN B CG  1 
ATOM   4112 O  OD1 . ASN B 1 245 ? -3.842  1.865   -2.655  1.00 9.37   ? 245 ASN B OD1 1 
ATOM   4113 N  ND2 . ASN B 1 245 ? -5.390  3.448   -2.410  1.00 8.57   ? 245 ASN B ND2 1 
ATOM   4114 N  N   . PHE B 1 246 ? -0.871  2.416   0.373   1.00 6.86   ? 246 PHE B N   1 
ATOM   4115 C  CA  . PHE B 1 246 ? -0.879  1.938   1.765   1.00 6.19   ? 246 PHE B CA  1 
ATOM   4116 C  C   . PHE B 1 246 ? 0.289   2.606   2.514   1.00 7.31   ? 246 PHE B C   1 
ATOM   4117 O  O   . PHE B 1 246 ? 1.353   2.798   1.901   1.00 7.72   ? 246 PHE B O   1 
ATOM   4118 C  CB  . PHE B 1 246 ? -0.810  0.376   1.823   1.00 7.28   ? 246 PHE B CB  1 
ATOM   4119 C  CG  . PHE B 1 246 ? 0.426   -0.223  1.190   1.00 8.44   ? 246 PHE B CG  1 
ATOM   4120 C  CD1 . PHE B 1 246 ? 0.500   -0.427  -0.184  1.00 8.01   ? 246 PHE B CD1 1 
ATOM   4121 C  CD2 . PHE B 1 246 ? 1.528   -0.519  1.992   1.00 8.84   ? 246 PHE B CD2 1 
ATOM   4122 C  CE1 . PHE B 1 246 ? 1.658   -0.934  -0.767  1.00 8.37   ? 246 PHE B CE1 1 
ATOM   4123 C  CE2 . PHE B 1 246 ? 2.694   -1.029  1.446   1.00 8.56   ? 246 PHE B CE2 1 
ATOM   4124 C  CZ  . PHE B 1 246 ? 2.725   -1.278  0.058   1.00 8.75   ? 246 PHE B CZ  1 
ATOM   4125 N  N   . ARG B 1 247 ? 0.061   2.903   3.819   1.00 7.85   ? 247 ARG B N   1 
ATOM   4126 C  CA  . ARG B 1 247 ? 1.147   3.405   4.658   1.00 8.02   ? 247 ARG B CA  1 
ATOM   4127 C  C   . ARG B 1 247 ? 1.909   2.285   5.322   1.00 6.25   ? 247 ARG B C   1 
ATOM   4128 O  O   . ARG B 1 247 ? 1.290   1.265   5.601   1.00 7.62   ? 247 ARG B O   1 
ATOM   4129 C  CB  . ARG B 1 247 ? 0.512   4.316   5.726   1.00 7.87   ? 247 ARG B CB  1 
ATOM   4130 C  CG  . ARG B 1 247 ? 1.481   5.171   6.508   1.00 8.57   ? 247 ARG B CG  1 
ATOM   4131 C  CD  . ARG B 1 247 ? 0.785   5.813   7.697   1.00 7.85   ? 247 ARG B CD  1 
ATOM   4132 N  NE  . ARG B 1 247 ? 1.632   6.938   8.201   1.00 8.59   ? 247 ARG B NE  1 
ATOM   4133 C  CZ  . ARG B 1 247 ? 1.353   7.608   9.327   1.00 8.17   ? 247 ARG B CZ  1 
ATOM   4134 N  NH1 . ARG B 1 247 ? 0.268   7.377   10.022  1.00 8.88   ? 247 ARG B NH1 1 
ATOM   4135 N  NH2 . ARG B 1 247 ? 2.088   8.687   9.632   1.00 8.99   ? 247 ARG B NH2 1 
ATOM   4136 N  N   . GLN B 1 248 ? 3.255   2.379   5.441   1.00 7.15   ? 248 GLN B N   1 
ATOM   4137 C  CA  . GLN B 1 248 ? 4.011   1.390   6.250   1.00 6.66   ? 248 GLN B CA  1 
ATOM   4138 C  C   . GLN B 1 248 ? 3.505   1.349   7.688   1.00 7.25   ? 248 GLN B C   1 
ATOM   4139 O  O   . GLN B 1 248 ? 2.918   2.319   8.187   1.00 8.52   ? 248 GLN B O   1 
ATOM   4140 C  CB  . GLN B 1 248 ? 5.497   1.766   6.259   1.00 8.20   ? 248 GLN B CB  1 
ATOM   4141 C  CG  . GLN B 1 248 ? 6.219   1.778   4.879   1.00 7.77   ? 248 GLN B CG  1 
ATOM   4142 C  CD  . GLN B 1 248 ? 6.191   0.405   4.244   1.00 9.50   ? 248 GLN B CD  1 
ATOM   4143 O  OE1 . GLN B 1 248 ? 5.295   0.104   3.475   1.00 8.76   ? 248 GLN B OE1 1 
ATOM   4144 N  NE2 . GLN B 1 248 ? 7.205   -0.346  4.600   1.00 10.89  ? 248 GLN B NE2 1 
ATOM   4145 N  N   . VAL B 1 249 ? 3.638   0.161   8.319   1.00 7.39   ? 249 VAL B N   1 
ATOM   4146 C  CA  . VAL B 1 249 ? 3.246   0.047   9.706   1.00 7.32   ? 249 VAL B CA  1 
ATOM   4147 C  C   . VAL B 1 249 ? 4.080   0.968   10.585  1.00 8.38   ? 249 VAL B C   1 
ATOM   4148 O  O   . VAL B 1 249 ? 5.264   1.246   10.285  1.00 7.47   ? 249 VAL B O   1 
ATOM   4149 C  CB  . VAL B 1 249 ? 3.299   -1.422  10.181  1.00 8.97   ? 249 VAL B CB  1 
ATOM   4150 C  CG1 . VAL B 1 249 ? 2.247   -2.233  9.394   1.00 8.56   ? 249 VAL B CG1 1 
ATOM   4151 C  CG2 . VAL B 1 249 ? 4.715   -2.029  10.044  1.00 10.61  ? 249 VAL B CG2 1 
ATOM   4152 N  N   . GLN B 1 250 ? 3.494   1.334   11.723  1.00 7.34   ? 250 GLN B N   1 
ATOM   4153 C  CA  . GLN B 1 250 ? 4.064   2.347   12.578  1.00 7.61   ? 250 GLN B CA  1 
ATOM   4154 C  C   . GLN B 1 250 ? 4.587   1.720   13.889  1.00 8.26   ? 250 GLN B C   1 
ATOM   4155 O  O   . GLN B 1 250 ? 4.174   0.600   14.272  1.00 10.13  ? 250 GLN B O   1 
ATOM   4156 C  CB  . GLN B 1 250 ? 2.961   3.294   13.020  1.00 8.97   ? 250 GLN B CB  1 
ATOM   4157 C  CG  . GLN B 1 250 ? 2.262   3.983   11.818  1.00 8.66   ? 250 GLN B CG  1 
ATOM   4158 C  CD  . GLN B 1 250 ? 3.182   4.921   11.075  1.00 7.37   ? 250 GLN B CD  1 
ATOM   4159 O  OE1 . GLN B 1 250 ? 3.608   5.977   11.613  1.00 10.17  ? 250 GLN B OE1 1 
ATOM   4160 N  NE2 . GLN B 1 250 ? 3.463   4.594   9.825   1.00 8.56   ? 250 GLN B NE2 1 
ATOM   4161 N  N   . LYS B 1 251 ? 5.494   2.400   14.550  1.00 9.46   ? 251 LYS B N   1 
ATOM   4162 C  CA  . LYS B 1 251 ? 5.948   2.007   15.887  1.00 9.90   ? 251 LYS B CA  1 
ATOM   4163 C  C   . LYS B 1 251 ? 4.758   1.909   16.850  1.00 10.45  ? 251 LYS B C   1 
ATOM   4164 O  O   . LYS B 1 251 ? 3.773   2.666   16.761  1.00 10.69  ? 251 LYS B O   1 
ATOM   4165 C  CB  . LYS B 1 251 ? 6.923   3.028   16.466  1.00 10.96  ? 251 LYS B CB  1 
ATOM   4166 C  CG  . LYS B 1 251 ? 8.357   3.006   15.938  1.00 11.97  ? 251 LYS B CG  1 
ATOM   4167 C  CD  . LYS B 1 251 ? 9.198   1.830   16.320  1.00 12.47  ? 251 LYS B CD  1 
ATOM   4168 C  CE  . LYS B 1 251 ? 10.680  1.911   15.979  1.00 10.51  ? 251 LYS B CE  1 
ATOM   4169 N  NZ  . LYS B 1 251 ? 10.900  1.930   14.517  1.00 8.40   ? 251 LYS B NZ  1 
ATOM   4170 N  N   . PHE B 1 252 ? 4.748   0.933   17.797  1.00 12.01  ? 252 PHE B N   1 
ATOM   4171 C  CA  . PHE B 1 252 ? 3.636   0.807   18.722  1.00 11.63  ? 252 PHE B CA  1 
ATOM   4172 C  C   . PHE B 1 252 ? 3.531   1.771   19.911  1.00 30.26  ? 252 PHE B C   1 
ATOM   4173 O  O   . PHE B 1 252 ? 2.408   1.965   20.415  1.00 31.76  ? 252 PHE B O   1 
ATOM   4174 C  CB  . PHE B 1 252 ? 3.032   -0.569  18.492  1.00 20.22  ? 252 PHE B CB  1 
ATOM   4175 C  CG  . PHE B 1 252 ? 1.572   -0.674  18.844  1.00 20.56  ? 252 PHE B CG  1 
ATOM   4176 C  CD1 . PHE B 1 252 ? 0.638   0.275   18.433  1.00 20.22  ? 252 PHE B CD1 1 
ATOM   4177 C  CD2 . PHE B 1 252 ? 1.133   -1.706  19.662  1.00 19.24  ? 252 PHE B CD2 1 
ATOM   4178 C  CE1 . PHE B 1 252 ? -0.705  0.161   18.791  1.00 19.92  ? 252 PHE B CE1 1 
ATOM   4179 C  CE2 . PHE B 1 252 ? -0.221  -1.832  19.991  1.00 18.20  ? 252 PHE B CE2 1 
ATOM   4180 C  CZ  . PHE B 1 252 ? -1.139  -0.872  19.583  1.00 24.32  ? 252 PHE B CZ  1 
ATOM   4181 N  N   . ASP B 1 253 ? 4.645   2.350   20.337  1.00 29.47  ? 253 ASP B N   1 
ATOM   4182 C  CA  . ASP B 1 253 ? 4.614   3.429   21.327  1.00 32.13  ? 253 ASP B CA  1 
ATOM   4183 C  C   . ASP B 1 253 ? 3.934   2.909   22.607  1.00 38.49  ? 253 ASP B C   1 
ATOM   4184 O  O   . ASP B 1 253 ? 3.117   3.626   23.173  1.00 35.05  ? 253 ASP B O   1 
ATOM   4185 C  CB  . ASP B 1 253 ? 3.835   4.611   20.769  1.00 35.40  ? 253 ASP B CB  1 
ATOM   4186 C  CG  . ASP B 1 253 ? 4.655   5.713   20.131  1.00 49.94  ? 253 ASP B CG  1 
ATOM   4187 O  OD1 . ASP B 1 253 ? 5.488   5.408   19.227  1.00 46.56  ? 253 ASP B OD1 1 
ATOM   4188 O  OD2 . ASP B 1 253 ? 4.423   6.890   20.524  1.00 48.11  ? 253 ASP B OD2 1 
ATOM   4189 N  N   . GLU B 1 254 ? 4.212   1.652   23.031  1.00 29.80  ? 254 GLU B N   1 
ATOM   4190 C  CA  . GLU B 1 254 ? 3.748   1.048   24.290  1.00 34.65  ? 254 GLU B CA  1 
ATOM   4191 C  C   . GLU B 1 254 ? 2.295   0.529   24.242  1.00 32.22  ? 254 GLU B C   1 
ATOM   4192 O  O   . GLU B 1 254 ? 1.794   -0.028  25.213  1.00 27.73  ? 254 GLU B O   1 
ATOM   4193 C  CB  . GLU B 1 254 ? 4.097   1.944   25.495  1.00 37.61  ? 254 GLU B CB  1 
ATOM   4194 C  CG  . GLU B 1 254 ? 5.546   1.773   25.937  1.00 51.56  ? 254 GLU B CG  1 
ATOM   4195 C  CD  . GLU B 1 254 ? 6.253   2.959   26.569  1.00 58.18  ? 254 GLU B CD  1 
ATOM   4196 O  OE1 . GLU B 1 254 ? 6.059   4.090   26.101  1.00 51.43  ? 254 GLU B OE1 1 
ATOM   4197 O  OE2 . GLU B 1 254 ? 7.026   2.736   27.523  1.00 72.16  ? 254 GLU B OE2 1 
ATOM   4198 N  N   . ARG B 1 255 ? 1.611   0.653   23.103  1.00 22.38  ? 255 ARG B N   1 
ATOM   4199 C  CA  . ARG B 1 255 ? 0.212   0.305   23.033  1.00 15.90  ? 255 ARG B CA  1 
ATOM   4200 C  C   . ARG B 1 255 ? 0.109   -1.265  23.046  1.00 19.05  ? 255 ARG B C   1 
ATOM   4201 O  O   . ARG B 1 255 ? 1.019   -2.066  22.681  1.00 20.00  ? 255 ARG B O   1 
ATOM   4202 C  CB  . ARG B 1 255 ? -0.334  0.842   21.692  1.00 20.65  ? 255 ARG B CB  1 
ATOM   4203 C  CG  . ARG B 1 255 ? -0.498  2.360   21.568  1.00 23.66  ? 255 ARG B CG  1 
ATOM   4204 C  CD  . ARG B 1 255 ? -1.149  2.981   20.293  1.00 24.34  ? 255 ARG B CD  1 
ATOM   4205 N  NE  . ARG B 1 255 ? -0.133  3.090   19.275  1.00 35.84  ? 255 ARG B NE  1 
ATOM   4206 C  CZ  . ARG B 1 255 ? -0.335  3.230   17.954  1.00 27.63  ? 255 ARG B CZ  1 
ATOM   4207 N  NH1 . ARG B 1 255 ? -1.605  3.291   17.491  1.00 15.76  ? 255 ARG B NH1 1 
ATOM   4208 N  NH2 . ARG B 1 255 ? 0.752   3.277   17.138  1.00 24.08  ? 255 ARG B NH2 1 
ATOM   4209 N  N   . LEU B 1 256 ? -1.052  -1.778  23.454  1.00 18.86  ? 256 LEU B N   1 
ATOM   4210 C  CA  . LEU B 1 256 ? -1.421  -3.150  23.132  1.00 17.22  ? 256 LEU B CA  1 
ATOM   4211 C  C   . LEU B 1 256 ? -2.601  -3.156  22.163  1.00 14.25  ? 256 LEU B C   1 
ATOM   4212 O  O   . LEU B 1 256 ? -3.311  -2.177  22.019  1.00 16.13  ? 256 LEU B O   1 
ATOM   4213 C  CB  . LEU B 1 256 ? -1.822  -3.867  24.415  1.00 22.70  ? 256 LEU B CB  1 
ATOM   4214 C  CG  . LEU B 1 256 ? -0.749  -3.877  25.477  1.00 19.99  ? 256 LEU B CG  1 
ATOM   4215 C  CD1 . LEU B 1 256 ? -1.399  -4.465  26.727  1.00 23.68  ? 256 LEU B CD1 1 
ATOM   4216 C  CD2 . LEU B 1 256 ? 0.437   -4.717  24.987  1.00 26.17  ? 256 LEU B CD2 1 
ATOM   4217 N  N   . VAL B 1 257 ? -2.863  -4.306  21.559  1.00 12.05  ? 257 VAL B N   1 
ATOM   4218 C  CA  . VAL B 1 257 ? -4.029  -4.549  20.725  1.00 11.14  ? 257 VAL B CA  1 
ATOM   4219 C  C   . VAL B 1 257 ? -4.830  -5.593  21.504  1.00 10.51  ? 257 VAL B C   1 
ATOM   4220 O  O   . VAL B 1 257 ? -4.304  -6.639  21.899  1.00 13.18  ? 257 VAL B O   1 
ATOM   4221 C  CB  . VAL B 1 257 ? -3.596  -5.119  19.348  1.00 10.77  ? 257 VAL B CB  1 
ATOM   4222 C  CG1 . VAL B 1 257 ? -4.792  -5.572  18.526  1.00 11.99  ? 257 VAL B CG1 1 
ATOM   4223 C  CG2 . VAL B 1 257 ? -2.794  -4.065  18.569  1.00 12.80  ? 257 VAL B CG2 1 
ATOM   4224 N  N   . TYR B 1 258 ? -6.122  -5.349  21.647  1.00 9.82   ? 258 TYR B N   1 
ATOM   4225 C  CA  . TYR B 1 258 ? -7.052  -6.187  22.395  1.00 9.02   ? 258 TYR B CA  1 
ATOM   4226 C  C   . TYR B 1 258 ? -7.858  -7.029  21.464  1.00 8.56   ? 258 TYR B C   1 
ATOM   4227 O  O   . TYR B 1 258 ? -8.250  -6.593  20.409  1.00 11.89  ? 258 TYR B O   1 
ATOM   4228 C  CB  . TYR B 1 258 ? -7.981  -5.357  23.266  1.00 10.75  ? 258 TYR B CB  1 
ATOM   4229 C  CG  . TYR B 1 258 ? -7.187  -4.435  24.166  1.00 13.49  ? 258 TYR B CG  1 
ATOM   4230 C  CD1 . TYR B 1 258 ? -6.637  -4.909  25.366  1.00 15.25  ? 258 TYR B CD1 1 
ATOM   4231 C  CD2 . TYR B 1 258 ? -6.906  -3.111  23.779  1.00 12.83  ? 258 TYR B CD2 1 
ATOM   4232 C  CE1 . TYR B 1 258 ? -5.862  -4.072  26.170  1.00 17.85  ? 258 TYR B CE1 1 
ATOM   4233 C  CE2 . TYR B 1 258 ? -6.143  -2.290  24.583  1.00 14.83  ? 258 TYR B CE2 1 
ATOM   4234 C  CZ  . TYR B 1 258 ? -5.607  -2.756  25.766  1.00 15.91  ? 258 TYR B CZ  1 
ATOM   4235 O  OH  . TYR B 1 258 ? -4.830  -1.950  26.565  1.00 20.66  ? 258 TYR B OH  1 
ATOM   4236 N  N   . THR B 1 259 ? -7.895  -8.341  21.769  1.00 10.75  ? 259 THR B N   1 
ATOM   4237 C  CA  . THR B 1 259 ? -8.557  -9.301  20.889  1.00 8.52   ? 259 THR B CA  1 
ATOM   4238 C  C   . THR B 1 259 ? -9.844  -9.813  21.542  1.00 9.96   ? 259 THR B C   1 
ATOM   4239 O  O   . THR B 1 259 ? -9.924  -10.051 22.737  1.00 11.58  ? 259 THR B O   1 
ATOM   4240 C  CB  . THR B 1 259 ? -7.641  -10.489 20.507  1.00 10.19  ? 259 THR B CB  1 
ATOM   4241 O  OG1 . THR B 1 259 ? -7.240  -11.173 21.694  1.00 13.18  ? 259 THR B OG1 1 
ATOM   4242 C  CG2 . THR B 1 259 ? -6.409  -9.995  19.799  1.00 11.51  ? 259 THR B CG2 1 
ATOM   4243 N  N   . SER B 1 260 ? -10.860 -10.020 20.700  1.00 10.03  ? 260 SER B N   1 
ATOM   4244 C  CA  . SER B 1 260 ? -12.136 -10.545 21.202  1.00 10.14  ? 260 SER B CA  1 
ATOM   4245 C  C   . SER B 1 260 ? -12.113 -12.085 21.213  1.00 11.10  ? 260 SER B C   1 
ATOM   4246 O  O   . SER B 1 260 ? -13.107 -12.739 21.621  1.00 14.71  ? 260 SER B O   1 
ATOM   4247 C  CB  . SER B 1 260 ? -13.304 -10.109 20.327  1.00 11.68  ? 260 SER B CB  1 
ATOM   4248 O  OG  . SER B 1 260 ? -13.197 -10.692 19.037  1.00 11.06  ? 260 SER B OG  1 
ATOM   4249 N  N   . PHE B 1 261 ? -11.008 -12.658 20.725  1.00 12.29  ? 261 PHE B N   1 
ATOM   4250 C  CA  . PHE B 1 261 ? -10.806 -14.113 20.684  1.00 11.03  ? 261 PHE B CA  1 
ATOM   4251 C  C   . PHE B 1 261 ? -9.616  -14.442 21.551  1.00 11.05  ? 261 PHE B C   1 
ATOM   4252 O  O   . PHE B 1 261 ? -8.699  -13.651 21.647  1.00 12.59  ? 261 PHE B O   1 
ATOM   4253 C  CB  . PHE B 1 261 ? -10.635 -14.564 19.225  1.00 12.11  ? 261 PHE B CB  1 
ATOM   4254 C  CG  . PHE B 1 261 ? -9.577  -13.808 18.461  1.00 12.43  ? 261 PHE B CG  1 
ATOM   4255 C  CD1 . PHE B 1 261 ? -9.886  -12.608 17.838  1.00 11.31  ? 261 PHE B CD1 1 
ATOM   4256 C  CD2 . PHE B 1 261 ? -8.262  -14.251 18.423  1.00 14.33  ? 261 PHE B CD2 1 
ATOM   4257 C  CE1 . PHE B 1 261 ? -8.910  -11.927 17.125  1.00 12.74  ? 261 PHE B CE1 1 
ATOM   4258 C  CE2 . PHE B 1 261 ? -7.290  -13.567 17.707  1.00 14.53  ? 261 PHE B CE2 1 
ATOM   4259 C  CZ  . PHE B 1 261 ? -7.627  -12.375 17.093  1.00 12.68  ? 261 PHE B CZ  1 
ATOM   4260 N  N   . SER B 1 262 ? -9.668  -15.606 22.216  1.00 14.31  ? 262 SER B N   1 
ATOM   4261 C  CA  . SER B 1 262 ? -8.547  -15.908 23.108  1.00 16.10  ? 262 SER B CA  1 
ATOM   4262 C  C   . SER B 1 262 ? -7.420  -16.638 22.377  1.00 27.23  ? 262 SER B C   1 
ATOM   4263 O  O   . SER B 1 262 ? -6.274  -16.632 22.833  1.00 36.76  ? 262 SER B O   1 
ATOM   4264 C  CB  . SER B 1 262 ? -9.026  -16.675 24.332  1.00 22.91  ? 262 SER B CB  1 
ATOM   4265 O  OG  . SER B 1 262 ? -9.773  -17.764 23.878  1.00 27.60  ? 262 SER B OG  1 
ATOM   4266 N  N   . GLN B 1 263 ? -7.767  -17.265 21.254  1.00 30.00  ? 263 GLN B N   1 
ATOM   4267 C  CA  . GLN B 1 263 ? -7.010  -18.357 20.645  1.00 24.43  ? 263 GLN B CA  1 
ATOM   4268 C  C   . GLN B 1 263 ? -7.607  -18.540 19.249  1.00 32.24  ? 263 GLN B C   1 
ATOM   4269 O  O   . GLN B 1 263 ? -6.955  -19.047 18.285  1.00 30.40  ? 263 GLN B O   1 
ATOM   4270 C  CB  . GLN B 1 263 ? -6.995  -19.629 21.517  1.00 32.41  ? 263 GLN B CB  1 
ATOM   4271 C  CG  . GLN B 1 263 ? -8.288  -20.443 21.532  1.00 40.63  ? 263 GLN B CG  1 
ATOM   4272 C  CD  . GLN B 1 263 ? -8.072  -21.826 22.115  1.00 48.60  ? 263 GLN B CD  1 
ATOM   4273 O  OE1 . GLN B 1 263 ? -7.613  -22.739 21.431  1.00 57.21  ? 263 GLN B OE1 1 
ATOM   4274 N  NE2 . GLN B 1 263 ? -8.364  -21.992 23.389  1.00 32.23  ? 263 GLN B NE2 1 
ATOM   4275 O  OXT . GLN B 1 263 ? -8.776  -18.087 19.129  1.00 21.08  ? 263 GLN B OXT 1 
ATOM   4276 N  N   . LYS C 1 3   ? 34.034  18.549  -27.686 1.00 56.25  ? 3   LYS C N   1 
ATOM   4277 C  CA  . LYS C 1 3   ? 33.608  17.673  -26.559 1.00 95.29  ? 3   LYS C CA  1 
ATOM   4278 C  C   . LYS C 1 3   ? 32.348  16.937  -26.972 1.00 117.02 ? 3   LYS C C   1 
ATOM   4279 O  O   . LYS C 1 3   ? 31.451  17.463  -27.631 1.00 97.94  ? 3   LYS C O   1 
ATOM   4280 C  CB  . LYS C 1 3   ? 33.368  18.519  -25.306 1.00 63.87  ? 3   LYS C CB  1 
ATOM   4281 C  CG  . LYS C 1 3   ? 32.713  17.782  -24.153 1.00 64.72  ? 3   LYS C CG  1 
ATOM   4282 C  CD  . LYS C 1 3   ? 31.230  18.053  -24.053 1.00 82.09  ? 3   LYS C CD  1 
ATOM   4283 N  N   . TRP C 1 4   ? 32.319  15.688  -26.528 1.00 17.72  ? 4   TRP C N   1 
ATOM   4284 C  CA  . TRP C 1 4   ? 31.423  14.684  -27.046 1.00 16.95  ? 4   TRP C CA  1 
ATOM   4285 C  C   . TRP C 1 4   ? 31.335  13.522  -26.055 1.00 15.87  ? 4   TRP C C   1 
ATOM   4286 O  O   . TRP C 1 4   ? 32.291  13.265  -25.314 1.00 19.24  ? 4   TRP C O   1 
ATOM   4287 C  CB  . TRP C 1 4   ? 31.912  14.247  -28.452 1.00 15.09  ? 4   TRP C CB  1 
ATOM   4288 C  CG  . TRP C 1 4   ? 33.285  13.626  -28.490 1.00 15.84  ? 4   TRP C CG  1 
ATOM   4289 C  CD1 . TRP C 1 4   ? 34.515  14.214  -28.634 1.00 16.46  ? 4   TRP C CD1 1 
ATOM   4290 C  CD2 . TRP C 1 4   ? 33.550  12.226  -28.305 1.00 14.73  ? 4   TRP C CD2 1 
ATOM   4291 N  NE1 . TRP C 1 4   ? 35.518  13.268  -28.618 1.00 18.14  ? 4   TRP C NE1 1 
ATOM   4292 C  CE2 . TRP C 1 4   ? 34.942  12.029  -28.422 1.00 15.00  ? 4   TRP C CE2 1 
ATOM   4293 C  CE3 . TRP C 1 4   ? 32.724  11.112  -28.168 1.00 14.52  ? 4   TRP C CE3 1 
ATOM   4294 C  CZ2 . TRP C 1 4   ? 35.542  10.775  -28.383 1.00 18.33  ? 4   TRP C CZ2 1 
ATOM   4295 C  CZ3 . TRP C 1 4   ? 33.319  9.875   -28.108 1.00 16.18  ? 4   TRP C CZ3 1 
ATOM   4296 C  CH2 . TRP C 1 4   ? 34.709  9.699   -28.203 1.00 17.18  ? 4   TRP C CH2 1 
ATOM   4297 N  N   . THR C 1 5   ? 30.235  12.765  -26.135 1.00 16.28  ? 5   THR C N   1 
ATOM   4298 C  CA  . THR C 1 5   ? 29.974  11.669  -25.214 1.00 15.98  ? 5   THR C CA  1 
ATOM   4299 C  C   . THR C 1 5   ? 29.260  10.565  -25.989 1.00 14.39  ? 5   THR C C   1 
ATOM   4300 O  O   . THR C 1 5   ? 29.053  10.662  -27.199 1.00 12.88  ? 5   THR C O   1 
ATOM   4301 C  CB  . THR C 1 5   ? 29.092  12.101  -24.026 1.00 17.33  ? 5   THR C CB  1 
ATOM   4302 O  OG1 . THR C 1 5   ? 27.805  12.326  -24.625 1.00 21.74  ? 5   THR C OG1 1 
ATOM   4303 C  CG2 . THR C 1 5   ? 29.546  13.357  -23.280 1.00 23.53  ? 5   THR C CG2 1 
ATOM   4304 N  N   . TYR C 1 6   ? 28.897  9.508   -25.257 1.00 15.73  ? 6   TYR C N   1 
ATOM   4305 C  CA  . TYR C 1 6   ? 27.980  8.484   -25.763 1.00 19.73  ? 6   TYR C CA  1 
ATOM   4306 C  C   . TYR C 1 6   ? 26.534  8.521   -25.225 1.00 18.34  ? 6   TYR C C   1 
ATOM   4307 O  O   . TYR C 1 6   ? 25.875  7.465   -25.279 1.00 20.79  ? 6   TYR C O   1 
ATOM   4308 C  CB  . TYR C 1 6   ? 28.560  7.094   -25.530 1.00 18.28  ? 6   TYR C CB  1 
ATOM   4309 C  CG  . TYR C 1 6   ? 29.829  6.849   -26.312 1.00 14.68  ? 6   TYR C CG  1 
ATOM   4310 C  CD1 . TYR C 1 6   ? 31.074  7.171   -25.786 1.00 14.56  ? 6   TYR C CD1 1 
ATOM   4311 C  CD2 . TYR C 1 6   ? 29.805  6.247   -27.571 1.00 14.80  ? 6   TYR C CD2 1 
ATOM   4312 C  CE1 . TYR C 1 6   ? 32.240  6.846   -26.467 1.00 16.04  ? 6   TYR C CE1 1 
ATOM   4313 C  CE2 . TYR C 1 6   ? 30.950  6.004   -28.311 1.00 14.60  ? 6   TYR C CE2 1 
ATOM   4314 C  CZ  . TYR C 1 6   ? 32.188  6.302   -27.755 1.00 14.65  ? 6   TYR C CZ  1 
ATOM   4315 O  OH  . TYR C 1 6   ? 33.346  5.977   -28.394 1.00 16.91  ? 6   TYR C OH  1 
ATOM   4316 N  N   . PHE C 1 7   ? 25.986  9.676   -24.771 1.00 24.75  ? 7   PHE C N   1 
ATOM   4317 C  CA  . PHE C 1 7   ? 24.590  9.756   -24.293 1.00 34.97  ? 7   PHE C CA  1 
ATOM   4318 C  C   . PHE C 1 7   ? 24.062  11.199  -24.332 1.00 38.58  ? 7   PHE C C   1 
ATOM   4319 O  O   . PHE C 1 7   ? 24.746  12.087  -24.865 1.00 32.96  ? 7   PHE C O   1 
ATOM   4320 C  CB  . PHE C 1 7   ? 24.474  9.266   -22.847 1.00 43.12  ? 7   PHE C CB  1 
ATOM   4321 C  CG  . PHE C 1 7   ? 25.108  10.235  -21.879 1.00 48.68  ? 7   PHE C CG  1 
ATOM   4322 C  CD1 . PHE C 1 7   ? 26.466  10.162  -21.594 1.00 44.57  ? 7   PHE C CD1 1 
ATOM   4323 C  CD2 . PHE C 1 7   ? 24.382  11.272  -21.276 1.00 48.11  ? 7   PHE C CD2 1 
ATOM   4324 C  CE1 . PHE C 1 7   ? 27.072  11.067  -20.724 1.00 42.93  ? 7   PHE C CE1 1 
ATOM   4325 C  CE2 . PHE C 1 7   ? 24.985  12.176  -20.411 1.00 52.96  ? 7   PHE C CE2 1 
ATOM   4326 C  CZ  . PHE C 1 7   ? 26.338  12.085  -20.148 1.00 41.83  ? 7   PHE C CZ  1 
ATOM   4327 N  N   . GLY C 1 8   ? 22.888  11.450  -23.706 1.00 39.19  ? 8   GLY C N   1 
ATOM   4328 C  CA  . GLY C 1 8   ? 22.451  12.794  -23.310 1.00 28.42  ? 8   GLY C CA  1 
ATOM   4329 C  C   . GLY C 1 8   ? 22.473  13.648  -24.562 1.00 25.39  ? 8   GLY C C   1 
ATOM   4330 O  O   . GLY C 1 8   ? 22.391  13.035  -25.647 1.00 34.96  ? 8   GLY C O   1 
ATOM   4331 N  N   . PRO C 1 9   ? 22.630  15.002  -24.503 1.00 24.33  ? 9   PRO C N   1 
ATOM   4332 C  CA  . PRO C 1 9   ? 22.702  15.782  -25.737 1.00 26.65  ? 9   PRO C CA  1 
ATOM   4333 C  C   . PRO C 1 9   ? 24.012  15.854  -26.508 1.00 23.84  ? 9   PRO C C   1 
ATOM   4334 O  O   . PRO C 1 9   ? 24.007  16.387  -27.610 1.00 22.32  ? 9   PRO C O   1 
ATOM   4335 C  CB  . PRO C 1 9   ? 22.421  17.226  -25.251 1.00 32.41  ? 9   PRO C CB  1 
ATOM   4336 C  CG  . PRO C 1 9   ? 23.048  17.209  -23.878 1.00 36.33  ? 9   PRO C CG  1 
ATOM   4337 C  CD  . PRO C 1 9   ? 22.651  15.863  -23.296 1.00 29.68  ? 9   PRO C CD  1 
ATOM   4338 N  N   . ASP C 1 10  ? 25.134  15.399  -25.921 1.00 20.75  ? 10  ASP C N   1 
ATOM   4339 C  CA  . ASP C 1 10  ? 26.423  15.476  -26.614 1.00 19.78  ? 10  ASP C CA  1 
ATOM   4340 C  C   . ASP C 1 10  ? 26.835  14.137  -27.226 1.00 18.33  ? 10  ASP C C   1 
ATOM   4341 O  O   . ASP C 1 10  ? 27.997  13.919  -27.627 1.00 18.82  ? 10  ASP C O   1 
ATOM   4342 C  CB  . ASP C 1 10  ? 27.495  16.047  -25.688 1.00 22.88  ? 10  ASP C CB  1 
ATOM   4343 C  CG  . ASP C 1 10  ? 27.170  17.467  -25.253 1.00 29.30  ? 10  ASP C CG  1 
ATOM   4344 O  OD1 . ASP C 1 10  ? 26.754  18.262  -26.114 1.00 28.01  ? 10  ASP C OD1 1 
ATOM   4345 O  OD2 . ASP C 1 10  ? 27.308  17.760  -24.042 1.00 39.17  ? 10  ASP C OD2 1 
ATOM   4346 N  N   . GLY C 1 11  ? 25.862  13.237  -27.248 1.00 16.99  ? 11  GLY C N   1 
ATOM   4347 C  CA  . GLY C 1 11  ? 26.016  11.878  -27.747 1.00 13.70  ? 11  GLY C CA  1 
ATOM   4348 C  C   . GLY C 1 11  ? 25.998  11.773  -29.280 1.00 10.76  ? 11  GLY C C   1 
ATOM   4349 O  O   . GLY C 1 11  ? 26.081  12.733  -30.052 1.00 13.85  ? 11  GLY C O   1 
ATOM   4350 N  N   . GLU C 1 12  ? 26.050  10.520  -29.760 1.00 10.20  ? 12  GLU C N   1 
ATOM   4351 C  CA  . GLU C 1 12  ? 26.531  10.257  -31.111 1.00 10.23  ? 12  GLU C CA  1 
ATOM   4352 C  C   . GLU C 1 12  ? 25.638  10.876  -32.204 1.00 9.74   ? 12  GLU C C   1 
ATOM   4353 O  O   . GLU C 1 12  ? 26.155  11.215  -33.277 1.00 9.56   ? 12  GLU C O   1 
ATOM   4354 C  CB  . GLU C 1 12  ? 26.673  8.735   -31.335 1.00 10.79  ? 12  GLU C CB  1 
ATOM   4355 C  CG  . GLU C 1 12  ? 25.350  7.972   -31.455 1.00 10.80  ? 12  GLU C CG  1 
ATOM   4356 C  CD  . GLU C 1 12  ? 25.595  6.495   -31.289 1.00 9.07   ? 12  GLU C CD  1 
ATOM   4357 O  OE1 . GLU C 1 12  ? 25.872  5.799   -32.287 1.00 9.74   ? 12  GLU C OE1 1 
ATOM   4358 O  OE2 . GLU C 1 12  ? 25.638  6.134   -30.112 1.00 11.14  ? 12  GLU C OE2 1 
ATOM   4359 N  N   . ASN C 1 13  ? 24.340  11.113  -31.964 1.00 11.29  ? 13  ASN C N   1 
ATOM   4360 C  CA  . ASN C 1 13  ? 23.480  11.714  -33.003 1.00 10.13  ? 13  ASN C CA  1 
ATOM   4361 C  C   . ASN C 1 13  ? 23.882  13.194  -33.181 1.00 10.99  ? 13  ASN C C   1 
ATOM   4362 O  O   . ASN C 1 13  ? 23.494  13.756  -34.196 1.00 11.93  ? 13  ASN C O   1 
ATOM   4363 C  CB  . ASN C 1 13  ? 22.000  11.552  -32.638 1.00 10.05  ? 13  ASN C CB  1 
ATOM   4364 C  CG  . ASN C 1 13  ? 21.532  10.117  -32.754 1.00 9.09   ? 13  ASN C CG  1 
ATOM   4365 O  OD1 . ASN C 1 13  ? 22.210  9.268   -33.352 1.00 10.95  ? 13  ASN C OD1 1 
ATOM   4366 N  ND2 . ASN C 1 13  ? 20.337  9.925   -32.301 1.00 10.76  ? 13  ASN C ND2 1 
ATOM   4367 N  N   . SER C 1 14  ? 24.582  13.790  -32.179 1.00 10.29  ? 14  SER C N   1 
ATOM   4368 C  CA  . SER C 1 14  ? 24.965  15.213  -32.220 1.00 11.15  ? 14  SER C CA  1 
ATOM   4369 C  C   . SER C 1 14  ? 26.400  15.370  -32.593 1.00 9.81   ? 14  SER C C   1 
ATOM   4370 O  O   . SER C 1 14  ? 26.796  16.554  -32.852 1.00 13.55  ? 14  SER C O   1 
ATOM   4371 C  CB  . SER C 1 14  ? 24.777  15.838  -30.838 1.00 13.99  ? 14  SER C CB  1 
ATOM   4372 O  OG  . SER C 1 14  ? 23.387  15.950  -30.571 1.00 18.97  ? 14  SER C OG  1 
ATOM   4373 N  N   . TRP C 1 15  ? 27.188  14.354  -32.801 1.00 12.21  ? 15  TRP C N   1 
ATOM   4374 C  CA  . TRP C 1 15  ? 28.604  14.514  -33.155 1.00 10.75  ? 15  TRP C CA  1 
ATOM   4375 C  C   . TRP C 1 15  ? 28.791  15.328  -34.429 1.00 10.13  ? 15  TRP C C   1 
ATOM   4376 O  O   . TRP C 1 15  ? 29.722  16.154  -34.494 1.00 11.42  ? 15  TRP C O   1 
ATOM   4377 C  CB  . TRP C 1 15  ? 29.286  13.156  -33.349 1.00 12.23  ? 15  TRP C CB  1 
ATOM   4378 C  CG  . TRP C 1 15  ? 29.426  12.362  -32.092 1.00 10.81  ? 15  TRP C CG  1 
ATOM   4379 C  CD1 . TRP C 1 15  ? 29.203  12.732  -30.799 1.00 11.79  ? 15  TRP C CD1 1 
ATOM   4380 C  CD2 . TRP C 1 15  ? 29.876  11.009  -32.065 1.00 11.06  ? 15  TRP C CD2 1 
ATOM   4381 N  NE1 . TRP C 1 15  ? 29.472  11.685  -29.940 1.00 10.58  ? 15  TRP C NE1 1 
ATOM   4382 C  CE2 . TRP C 1 15  ? 29.923  10.625  -30.696 1.00 11.19  ? 15  TRP C CE2 1 
ATOM   4383 C  CE3 . TRP C 1 15  ? 30.267  10.113  -33.084 1.00 9.77   ? 15  TRP C CE3 1 
ATOM   4384 C  CZ2 . TRP C 1 15  ? 30.271  9.319   -30.335 1.00 10.85  ? 15  TRP C CZ2 1 
ATOM   4385 C  CZ3 . TRP C 1 15  ? 30.642  8.837   -32.710 1.00 9.24   ? 15  TRP C CZ3 1 
ATOM   4386 C  CH2 . TRP C 1 15  ? 30.688  8.474   -31.355 1.00 10.66  ? 15  TRP C CH2 1 
ATOM   4387 N  N   . SER C 1 16  ? 27.876  15.190  -35.421 1.00 10.99  ? 16  SER C N   1 
ATOM   4388 C  CA  . SER C 1 16  ? 27.996  15.880  -36.724 1.00 9.83   ? 16  SER C CA  1 
ATOM   4389 C  C   . SER C 1 16  ? 27.940  17.390  -36.617 1.00 10.47  ? 16  SER C C   1 
ATOM   4390 O  O   . SER C 1 16  ? 28.394  18.039  -37.541 1.00 10.70  ? 16  SER C O   1 
ATOM   4391 C  CB  . SER C 1 16  ? 26.950  15.423  -37.695 1.00 10.14  ? 16  SER C CB  1 
ATOM   4392 O  OG  . SER C 1 16  ? 25.690  15.793  -37.169 1.00 10.93  ? 16  SER C OG  1 
ATOM   4393 N  N   A LYS C 1 17  ? 27.437  17.929  -35.495 0.50 11.66  ? 17  LYS C N   1 
ATOM   4394 N  N   B LYS C 1 17  ? 27.446  17.928  -35.490 0.50 11.70  ? 17  LYS C N   1 
ATOM   4395 C  CA  A LYS C 1 17  ? 27.408  19.388  -35.383 0.50 13.51  ? 17  LYS C CA  1 
ATOM   4396 C  CA  B LYS C 1 17  ? 27.405  19.389  -35.374 0.50 13.35  ? 17  LYS C CA  1 
ATOM   4397 C  C   A LYS C 1 17  ? 28.825  19.953  -35.396 0.50 11.50  ? 17  LYS C C   1 
ATOM   4398 C  C   B LYS C 1 17  ? 28.816  19.970  -35.380 0.50 11.39  ? 17  LYS C C   1 
ATOM   4399 O  O   A LYS C 1 17  ? 29.111  20.916  -36.115 0.50 14.72  ? 17  LYS C O   1 
ATOM   4400 O  O   B LYS C 1 17  ? 29.087  20.949  -36.096 0.50 14.36  ? 17  LYS C O   1 
ATOM   4401 C  CB  A LYS C 1 17  ? 26.690  19.794  -34.095 0.50 13.76  ? 17  LYS C CB  1 
ATOM   4402 C  CB  B LYS C 1 17  ? 26.591  19.793  -34.138 0.50 14.40  ? 17  LYS C CB  1 
ATOM   4403 C  CG  A LYS C 1 17  ? 25.214  19.433  -34.038 0.50 16.99  ? 17  LYS C CG  1 
ATOM   4404 C  CG  B LYS C 1 17  ? 25.097  19.509  -34.281 0.50 18.22  ? 17  LYS C CG  1 
ATOM   4405 C  CD  A LYS C 1 17  ? 24.657  19.568  -32.626 0.50 16.14  ? 17  LYS C CD  1 
ATOM   4406 C  CD  B LYS C 1 17  ? 24.200  20.064  -33.170 0.50 19.52  ? 17  LYS C CD  1 
ATOM   4407 C  CE  A LYS C 1 17  ? 23.270  18.987  -32.471 0.50 14.48  ? 17  LYS C CE  1 
ATOM   4408 C  CE  B LYS C 1 17  ? 24.379  21.559  -32.998 0.50 23.97  ? 17  LYS C CE  1 
ATOM   4409 N  NZ  A LYS C 1 17  ? 22.711  19.312  -31.147 0.50 11.04  ? 17  LYS C NZ  1 
ATOM   4410 N  NZ  B LYS C 1 17  ? 23.023  22.295  -32.920 0.50 31.30  ? 17  LYS C NZ  1 
ATOM   4411 N  N   . LYS C 1 18  ? 29.709  19.434  -34.550 1.00 13.11  ? 18  LYS C N   1 
ATOM   4412 C  CA  . LYS C 1 18  ? 31.053  19.966  -34.393 1.00 12.68  ? 18  LYS C CA  1 
ATOM   4413 C  C   . LYS C 1 18  ? 32.057  19.168  -35.227 1.00 12.81  ? 18  LYS C C   1 
ATOM   4414 O  O   . LYS C 1 18  ? 33.150  19.628  -35.518 1.00 16.16  ? 18  LYS C O   1 
ATOM   4415 C  CB  . LYS C 1 18  ? 31.427  19.976  -32.898 1.00 15.68  ? 18  LYS C CB  1 
ATOM   4416 C  CG  . LYS C 1 18  ? 30.765  21.053  -32.032 1.00 29.00  ? 18  LYS C CG  1 
ATOM   4417 C  CD  . LYS C 1 18  ? 31.047  22.497  -32.464 1.00 34.62  ? 18  LYS C CD  1 
ATOM   4418 C  CE  . LYS C 1 18  ? 30.468  23.599  -31.594 1.00 35.25  ? 18  LYS C CE  1 
ATOM   4419 N  NZ  . LYS C 1 18  ? 31.526  24.269  -30.808 1.00 48.29  ? 18  LYS C NZ  1 
ATOM   4420 N  N   . TYR C 1 19  ? 31.682  17.942  -35.589 1.00 12.85  ? 19  TYR C N   1 
ATOM   4421 C  CA  . TYR C 1 19  ? 32.573  17.111  -36.395 1.00 10.85  ? 19  TYR C CA  1 
ATOM   4422 C  C   . TYR C 1 19  ? 31.892  16.640  -37.673 1.00 12.00  ? 19  TYR C C   1 
ATOM   4423 O  O   . TYR C 1 19  ? 31.259  15.560  -37.680 1.00 10.15  ? 19  TYR C O   1 
ATOM   4424 C  CB  . TYR C 1 19  ? 32.905  15.866  -35.555 1.00 11.45  ? 19  TYR C CB  1 
ATOM   4425 C  CG  . TYR C 1 19  ? 33.572  16.237  -34.247 1.00 12.19  ? 19  TYR C CG  1 
ATOM   4426 C  CD1 . TYR C 1 19  ? 34.947  16.532  -34.169 1.00 12.93  ? 19  TYR C CD1 1 
ATOM   4427 C  CD2 . TYR C 1 19  ? 32.840  16.312  -33.078 1.00 12.59  ? 19  TYR C CD2 1 
ATOM   4428 C  CE1 . TYR C 1 19  ? 35.564  16.857  -32.957 1.00 15.22  ? 19  TYR C CE1 1 
ATOM   4429 C  CE2 . TYR C 1 19  ? 33.435  16.638  -31.862 1.00 14.35  ? 19  TYR C CE2 1 
ATOM   4430 C  CZ  . TYR C 1 19  ? 34.795  16.938  -31.789 1.00 14.57  ? 19  TYR C CZ  1 
ATOM   4431 O  OH  . TYR C 1 19  ? 35.321  17.190  -30.540 1.00 19.88  ? 19  TYR C OH  1 
ATOM   4432 N  N   . PRO C 1 20  ? 31.899  17.431  -38.755 1.00 10.97  ? 20  PRO C N   1 
ATOM   4433 C  CA  . PRO C 1 20  ? 30.993  17.172  -39.892 1.00 10.04  ? 20  PRO C CA  1 
ATOM   4434 C  C   . PRO C 1 20  ? 31.202  15.774  -40.494 1.00 9.53   ? 20  PRO C C   1 
ATOM   4435 O  O   . PRO C 1 20  ? 30.281  15.222  -41.117 1.00 11.36  ? 20  PRO C O   1 
ATOM   4436 C  CB  . PRO C 1 20  ? 31.305  18.285  -40.880 1.00 13.60  ? 20  PRO C CB  1 
ATOM   4437 C  CG  . PRO C 1 20  ? 32.034  19.341  -40.086 1.00 18.26  ? 20  PRO C CG  1 
ATOM   4438 C  CD  . PRO C 1 20  ? 32.645  18.704  -38.861 1.00 12.68  ? 20  PRO C CD  1 
ATOM   4439 N  N   . SER C 1 21  ? 32.421  15.219  -40.409 1.00 9.49   ? 21  SER C N   1 
ATOM   4440 C  CA  . SER C 1 21  ? 32.626  13.890  -41.033 1.00 9.85   ? 21  SER C CA  1 
ATOM   4441 C  C   . SER C 1 21  ? 31.750  12.836  -40.389 1.00 9.00   ? 21  SER C C   1 
ATOM   4442 O  O   . SER C 1 21  ? 31.491  11.804  -41.011 1.00 9.35   ? 21  SER C O   1 
ATOM   4443 C  CB  . SER C 1 21  ? 34.100  13.412  -41.063 1.00 11.29  ? 21  SER C CB  1 
ATOM   4444 O  OG  . SER C 1 21  ? 34.831  14.241  -41.918 1.00 13.81  ? 21  SER C OG  1 
ATOM   4445 N  N   . CYS C 1 22  ? 31.289  13.057  -39.152 1.00 8.92   ? 22  CYS C N   1 
ATOM   4446 C  CA  . CYS C 1 22  ? 30.467  12.022  -38.537 1.00 9.55   ? 22  CYS C CA  1 
ATOM   4447 C  C   . CYS C 1 22  ? 29.097  11.845  -39.224 1.00 9.99   ? 22  CYS C C   1 
ATOM   4448 O  O   . CYS C 1 22  ? 28.393  10.842  -38.972 1.00 10.31  ? 22  CYS C O   1 
ATOM   4449 C  CB  . CYS C 1 22  ? 30.234  12.352  -37.055 1.00 9.57   ? 22  CYS C CB  1 
ATOM   4450 S  SG  . CYS C 1 22  ? 31.769  12.456  -36.090 1.00 10.76  ? 22  CYS C SG  1 
ATOM   4451 N  N   . GLY C 1 23  ? 28.677  12.823  -40.028 1.00 9.47   ? 23  GLY C N   1 
ATOM   4452 C  CA  . GLY C 1 23  ? 27.504  12.764  -40.884 1.00 10.07  ? 23  GLY C CA  1 
ATOM   4453 C  C   . GLY C 1 23  ? 27.835  12.541  -42.345 1.00 11.41  ? 23  GLY C C   1 
ATOM   4454 O  O   . GLY C 1 23  ? 26.917  12.583  -43.174 1.00 11.42  ? 23  GLY C O   1 
ATOM   4455 N  N   . GLY C 1 24  ? 29.105  12.193  -42.625 1.00 11.02  ? 24  GLY C N   1 
ATOM   4456 C  CA  . GLY C 1 24  ? 29.532  12.002  -44.001 1.00 11.96  ? 24  GLY C CA  1 
ATOM   4457 C  C   . GLY C 1 24  ? 29.516  10.541  -44.432 1.00 10.40  ? 24  GLY C C   1 
ATOM   4458 O  O   . GLY C 1 24  ? 28.847  9.684   -43.858 1.00 12.62  ? 24  GLY C O   1 
ATOM   4459 N  N   . LEU C 1 25  ? 30.277  10.284  -45.472 1.00 11.61  ? 25  LEU C N   1 
ATOM   4460 C  CA  . LEU C 1 25  ? 30.336  8.938   -46.036 1.00 12.18  ? 25  LEU C CA  1 
ATOM   4461 C  C   . LEU C 1 25  ? 31.251  7.990   -45.275 1.00 14.00  ? 25  LEU C C   1 
ATOM   4462 O  O   . LEU C 1 25  ? 32.049  8.444   -44.457 1.00 12.03  ? 25  LEU C O   1 
ATOM   4463 C  CB  . LEU C 1 25  ? 30.842  9.059   -47.470 1.00 16.45  ? 25  LEU C CB  1 
ATOM   4464 C  CG  . LEU C 1 25  ? 29.925  9.860   -48.397 1.00 20.12  ? 25  LEU C CG  1 
ATOM   4465 C  CD1 . LEU C 1 25  ? 30.543  9.986   -49.769 1.00 26.12  ? 25  LEU C CD1 1 
ATOM   4466 C  CD2 . LEU C 1 25  ? 28.505  9.298   -48.454 1.00 26.32  ? 25  LEU C CD2 1 
ATOM   4467 N  N   . LEU C 1 26  ? 31.104  6.679   -45.585 1.00 11.77  ? 26  LEU C N   1 
ATOM   4468 C  CA  . LEU C 1 26  ? 32.021  5.602   -45.209 1.00 12.13  ? 26  LEU C CA  1 
ATOM   4469 C  C   . LEU C 1 26  ? 32.140  5.487   -43.684 1.00 8.66   ? 26  LEU C C   1 
ATOM   4470 O  O   . LEU C 1 26  ? 33.158  5.031   -43.126 1.00 11.98  ? 26  LEU C O   1 
ATOM   4471 C  CB  . LEU C 1 26  ? 33.408  5.917   -45.772 1.00 15.06  ? 26  LEU C CB  1 
ATOM   4472 C  CG  . LEU C 1 26  ? 33.750  5.555   -47.219 1.00 24.23  ? 26  LEU C CG  1 
ATOM   4473 C  CD1 . LEU C 1 26  ? 35.185  5.018   -47.285 1.00 26.21  ? 26  LEU C CD1 1 
ATOM   4474 C  CD2 . LEU C 1 26  ? 32.774  4.611   -47.885 1.00 25.28  ? 26  LEU C CD2 1 
ATOM   4475 N  N   . GLN C 1 27  ? 31.030  5.774   -42.982 1.00 8.94   ? 27  GLN C N   1 
ATOM   4476 C  CA  . GLN C 1 27  ? 31.049  5.643   -41.534 1.00 8.16   ? 27  GLN C CA  1 
ATOM   4477 C  C   . GLN C 1 27  ? 31.106  4.200   -41.027 1.00 7.07   ? 27  GLN C C   1 
ATOM   4478 O  O   . GLN C 1 27  ? 30.440  3.269   -41.501 1.00 10.45  ? 27  GLN C O   1 
ATOM   4479 C  CB  . GLN C 1 27  ? 29.868  6.416   -40.931 1.00 8.15   ? 27  GLN C CB  1 
ATOM   4480 C  CG  . GLN C 1 27  ? 29.940  7.911   -41.251 1.00 8.92   ? 27  GLN C CG  1 
ATOM   4481 C  CD  . GLN C 1 27  ? 31.136  8.549   -40.569 1.00 7.86   ? 27  GLN C CD  1 
ATOM   4482 O  OE1 . GLN C 1 27  ? 31.156  8.738   -39.332 1.00 8.92   ? 27  GLN C OE1 1 
ATOM   4483 N  NE2 . GLN C 1 27  ? 32.207  8.808   -41.353 1.00 9.61   ? 27  GLN C NE2 1 
ATOM   4484 N  N   . SER C 1 28  ? 31.855  4.059   -39.935 1.00 7.29   ? 28  SER C N   1 
ATOM   4485 C  CA  . SER C 1 28  ? 32.000  2.822   -39.212 1.00 7.15   ? 28  SER C CA  1 
ATOM   4486 C  C   . SER C 1 28  ? 31.408  2.999   -37.822 1.00 8.29   ? 28  SER C C   1 
ATOM   4487 O  O   . SER C 1 28  ? 31.290  4.116   -37.340 1.00 8.71   ? 28  SER C O   1 
ATOM   4488 C  CB  . SER C 1 28  ? 33.480  2.513   -39.071 1.00 7.23   ? 28  SER C CB  1 
ATOM   4489 O  OG  . SER C 1 28  ? 34.050  2.173   -40.294 1.00 9.22   ? 28  SER C OG  1 
ATOM   4490 N  N   . PRO C 1 29  ? 31.043  1.978   -37.057 1.00 7.68   ? 29  PRO C N   1 
ATOM   4491 C  CA  . PRO C 1 29  ? 31.111  0.549   -37.416 1.00 7.65   ? 29  PRO C CA  1 
ATOM   4492 C  C   . PRO C 1 29  ? 29.931  0.054   -38.229 1.00 10.11  ? 29  PRO C C   1 
ATOM   4493 O  O   . PRO C 1 29  ? 29.026  0.809   -38.452 1.00 8.62   ? 29  PRO C O   1 
ATOM   4494 C  CB  . PRO C 1 29  ? 31.161  -0.111  -36.061 1.00 9.31   ? 29  PRO C CB  1 
ATOM   4495 C  CG  . PRO C 1 29  ? 30.183  0.712   -35.299 1.00 7.60   ? 29  PRO C CG  1 
ATOM   4496 C  CD  . PRO C 1 29  ? 30.438  2.160   -35.730 1.00 7.86   ? 29  PRO C CD  1 
ATOM   4497 N  N   . ILE C 1 30  ? 29.958  -1.210  -38.657 1.00 8.35   ? 30  ILE C N   1 
ATOM   4498 C  CA  . ILE C 1 30  ? 28.957  -1.772  -39.553 1.00 8.86   ? 30  ILE C CA  1 
ATOM   4499 C  C   . ILE C 1 30  ? 28.661  -3.192  -39.095 1.00 7.29   ? 30  ILE C C   1 
ATOM   4500 O  O   . ILE C 1 30  ? 29.423  -3.785  -38.276 1.00 9.20   ? 30  ILE C O   1 
ATOM   4501 C  CB  . ILE C 1 30  ? 29.437  -1.755  -41.044 1.00 7.70   ? 30  ILE C CB  1 
ATOM   4502 C  CG1 . ILE C 1 30  ? 30.625  -2.735  -41.197 1.00 9.94   ? 30  ILE C CG1 1 
ATOM   4503 C  CG2 . ILE C 1 30  ? 29.690  -0.272  -41.518 1.00 11.21  ? 30  ILE C CG2 1 
ATOM   4504 C  CD1 . ILE C 1 30  ? 30.993  -2.954  -42.667 1.00 10.93  ? 30  ILE C CD1 1 
ATOM   4505 N  N   . ASP C 1 31  ? 27.508  -3.658  -39.537 1.00 9.86   ? 31  ASP C N   1 
ATOM   4506 C  CA  . ASP C 1 31  ? 27.176  -5.077  -39.356 1.00 6.84   ? 31  ASP C CA  1 
ATOM   4507 C  C   . ASP C 1 31  ? 27.835  -5.947  -40.429 1.00 10.20  ? 31  ASP C C   1 
ATOM   4508 O  O   . ASP C 1 31  ? 27.678  -5.732  -41.640 1.00 12.03  ? 31  ASP C O   1 
ATOM   4509 C  CB  . ASP C 1 31  ? 25.649  -5.299  -39.481 1.00 9.50   ? 31  ASP C CB  1 
ATOM   4510 C  CG  . ASP C 1 31  ? 25.229  -6.729  -39.203 1.00 8.94   ? 31  ASP C CG  1 
ATOM   4511 O  OD1 . ASP C 1 31  ? 25.798  -7.352  -38.233 1.00 10.72  ? 31  ASP C OD1 1 
ATOM   4512 O  OD2 . ASP C 1 31  ? 24.263  -7.181  -39.865 1.00 16.80  ? 31  ASP C OD2 1 
ATOM   4513 N  N   . LEU C 1 32  ? 28.614  -6.934  -39.980 1.00 10.64  ? 32  LEU C N   1 
ATOM   4514 C  CA  . LEU C 1 32  ? 29.252  -7.918  -40.861 1.00 10.47  ? 32  LEU C CA  1 
ATOM   4515 C  C   . LEU C 1 32  ? 28.305  -9.109  -41.090 1.00 9.68   ? 32  LEU C C   1 
ATOM   4516 O  O   . LEU C 1 32  ? 28.178  -9.958  -40.254 1.00 13.53  ? 32  LEU C O   1 
ATOM   4517 C  CB  . LEU C 1 32  ? 30.609  -8.336  -40.272 1.00 10.47  ? 32  LEU C CB  1 
ATOM   4518 C  CG  . LEU C 1 32  ? 31.519  -7.201  -39.809 1.00 9.79   ? 32  LEU C CG  1 
ATOM   4519 C  CD1 . LEU C 1 32  ? 32.677  -7.719  -38.962 1.00 13.14  ? 32  LEU C CD1 1 
ATOM   4520 C  CD2 . LEU C 1 32  ? 32.053  -6.420  -41.010 1.00 16.50  ? 32  LEU C CD2 1 
ATOM   4521 N  N   . HIS C 1 33  ? 27.655  -9.206  -42.234 1.00 15.78  ? 33  HIS C N   1 
ATOM   4522 C  CA  . HIS C 1 33  ? 26.761  -10.345 -42.403 1.00 21.17  ? 33  HIS C CA  1 
ATOM   4523 C  C   . HIS C 1 33  ? 26.943  -10.987 -43.763 1.00 19.47  ? 33  HIS C C   1 
ATOM   4524 O  O   . HIS C 1 33  ? 27.439  -10.305 -44.636 1.00 18.74  ? 33  HIS C O   1 
ATOM   4525 C  CB  . HIS C 1 33  ? 25.308  -9.984  -42.129 1.00 27.26  ? 33  HIS C CB  1 
ATOM   4526 C  CG  . HIS C 1 33  ? 24.775  -8.991  -43.094 1.00 27.42  ? 33  HIS C CG  1 
ATOM   4527 N  ND1 . HIS C 1 33  ? 24.006  -9.381  -44.184 1.00 34.95  ? 33  HIS C ND1 1 
ATOM   4528 C  CD2 . HIS C 1 33  ? 24.981  -7.659  -43.195 1.00 26.69  ? 33  HIS C CD2 1 
ATOM   4529 C  CE1 . HIS C 1 33  ? 23.683  -8.307  -44.887 1.00 41.22  ? 33  HIS C CE1 1 
ATOM   4530 N  NE2 . HIS C 1 33  ? 24.260  -7.228  -44.293 1.00 33.59  ? 33  HIS C NE2 1 
ATOM   4531 N  N   . SER C 1 34  ? 26.465  -12.244 -43.943 1.00 24.56  ? 34  SER C N   1 
ATOM   4532 C  CA  . SER C 1 34  ? 26.917  -13.100 -45.043 1.00 27.82  ? 34  SER C CA  1 
ATOM   4533 C  C   . SER C 1 34  ? 26.583  -12.488 -46.403 1.00 27.36  ? 34  SER C C   1 
ATOM   4534 O  O   . SER C 1 34  ? 27.379  -12.535 -47.358 1.00 27.04  ? 34  SER C O   1 
ATOM   4535 C  CB  . SER C 1 34  ? 26.379  -14.486 -44.862 1.00 42.62  ? 34  SER C CB  1 
ATOM   4536 O  OG  . SER C 1 34  ? 25.555  -14.489 -43.710 1.00 61.47  ? 34  SER C OG  1 
ATOM   4537 N  N   . ASP C 1 35  ? 25.431  -11.816 -46.456 1.00 25.17  ? 35  ASP C N   1 
ATOM   4538 C  CA  . ASP C 1 35  ? 24.908  -11.352 -47.737 1.00 32.48  ? 35  ASP C CA  1 
ATOM   4539 C  C   . ASP C 1 35  ? 25.885  -10.361 -48.369 1.00 27.41  ? 35  ASP C C   1 
ATOM   4540 O  O   . ASP C 1 35  ? 25.857  -10.150 -49.574 1.00 34.90  ? 35  ASP C O   1 
ATOM   4541 C  CB  . ASP C 1 35  ? 23.463  -10.829 -47.626 1.00 34.03  ? 35  ASP C CB  1 
ATOM   4542 C  CG  . ASP C 1 35  ? 22.435  -11.905 -47.289 1.00 38.22  ? 35  ASP C CG  1 
ATOM   4543 O  OD1 . ASP C 1 35  ? 22.786  -13.093 -47.365 1.00 46.34  ? 35  ASP C OD1 1 
ATOM   4544 O  OD2 . ASP C 1 35  ? 21.273  -11.542 -46.940 1.00 43.93  ? 35  ASP C OD2 1 
ATOM   4545 N  N   . ILE C 1 36  ? 26.750  -9.747  -47.552 1.00 20.56  ? 36  ILE C N   1 
ATOM   4546 C  CA  . ILE C 1 36  ? 27.616  -8.695  -48.069 1.00 18.77  ? 36  ILE C CA  1 
ATOM   4547 C  C   . ILE C 1 36  ? 29.079  -9.113  -48.109 1.00 16.72  ? 36  ILE C C   1 
ATOM   4548 O  O   . ILE C 1 36  ? 29.941  -8.295  -48.426 1.00 18.82  ? 36  ILE C O   1 
ATOM   4549 C  CB  . ILE C 1 36  ? 27.430  -7.325  -47.349 1.00 17.85  ? 36  ILE C CB  1 
ATOM   4550 C  CG1 . ILE C 1 36  ? 27.893  -7.394  -45.876 1.00 15.84  ? 36  ILE C CG1 1 
ATOM   4551 C  CG2 . ILE C 1 36  ? 26.005  -6.776  -47.481 1.00 21.44  ? 36  ILE C CG2 1 
ATOM   4552 C  CD1 . ILE C 1 36  ? 27.998  -6.064  -45.184 1.00 18.42  ? 36  ILE C CD1 1 
ATOM   4553 N  N   . LEU C 1 37  ? 29.350  -10.374 -47.757 1.00 17.84  ? 37  LEU C N   1 
ATOM   4554 C  CA  . LEU C 1 37  ? 30.747  -10.829 -47.670 1.00 18.64  ? 37  LEU C CA  1 
ATOM   4555 C  C   . LEU C 1 37  ? 31.182  -11.309 -49.052 1.00 15.73  ? 37  LEU C C   1 
ATOM   4556 O  O   . LEU C 1 37  ? 30.413  -11.946 -49.760 1.00 24.27  ? 37  LEU C O   1 
ATOM   4557 C  CB  . LEU C 1 37  ? 30.903  -11.989 -46.692 1.00 20.77  ? 37  LEU C CB  1 
ATOM   4558 C  CG  . LEU C 1 37  ? 30.397  -11.723 -45.286 1.00 19.82  ? 37  LEU C CG  1 
ATOM   4559 C  CD1 . LEU C 1 37  ? 30.642  -12.958 -44.450 1.00 23.66  ? 37  LEU C CD1 1 
ATOM   4560 C  CD2 . LEU C 1 37  ? 31.116  -10.523 -44.695 1.00 18.58  ? 37  LEU C CD2 1 
ATOM   4561 N  N   . GLN C 1 38  ? 32.456  -11.144 -49.369 1.00 17.70  ? 38  GLN C N   1 
ATOM   4562 C  CA  . GLN C 1 38  ? 33.024  -11.611 -50.629 1.00 21.01  ? 38  GLN C CA  1 
ATOM   4563 C  C   . GLN C 1 38  ? 34.500  -11.933 -50.397 1.00 17.34  ? 38  GLN C C   1 
ATOM   4564 O  O   . GLN C 1 38  ? 35.283  -11.078 -49.987 1.00 19.31  ? 38  GLN C O   1 
ATOM   4565 C  CB  . GLN C 1 38  ? 32.913  -10.521 -51.716 1.00 21.67  ? 38  GLN C CB  1 
ATOM   4566 C  CG  . GLN C 1 38  ? 33.431  -10.988 -53.094 1.00 25.18  ? 38  GLN C CG  1 
ATOM   4567 C  CD  . GLN C 1 38  ? 33.069  -10.051 -54.228 1.00 27.67  ? 38  GLN C CD  1 
ATOM   4568 O  OE1 . GLN C 1 38  ? 31.912  -9.963  -54.646 1.00 40.48  ? 38  GLN C OE1 1 
ATOM   4569 N  NE2 . GLN C 1 38  ? 34.050  -9.310  -54.725 1.00 25.16  ? 38  GLN C NE2 1 
ATOM   4570 N  N   . TYR C 1 39  ? 34.912  -13.167 -50.696 1.00 21.06  ? 39  TYR C N   1 
ATOM   4571 C  CA  . TYR C 1 39  ? 36.332  -13.556 -50.699 1.00 22.56  ? 39  TYR C CA  1 
ATOM   4572 C  C   . TYR C 1 39  ? 37.160  -12.673 -51.658 1.00 24.78  ? 39  TYR C C   1 
ATOM   4573 O  O   . TYR C 1 39  ? 36.693  -12.394 -52.756 1.00 33.14  ? 39  TYR C O   1 
ATOM   4574 C  CB  . TYR C 1 39  ? 36.343  -15.017 -51.130 1.00 24.68  ? 39  TYR C CB  1 
ATOM   4575 C  CG  . TYR C 1 39  ? 37.605  -15.831 -51.000 1.00 32.91  ? 39  TYR C CG  1 
ATOM   4576 C  CD1 . TYR C 1 39  ? 38.607  -15.487 -50.123 1.00 28.64  ? 39  TYR C CD1 1 
ATOM   4577 C  CD2 . TYR C 1 39  ? 37.739  -17.017 -51.708 1.00 29.21  ? 39  TYR C CD2 1 
ATOM   4578 C  CE1 . TYR C 1 39  ? 39.754  -16.246 -49.993 1.00 35.69  ? 39  TYR C CE1 1 
ATOM   4579 C  CE2 . TYR C 1 39  ? 38.862  -17.816 -51.575 1.00 42.15  ? 39  TYR C CE2 1 
ATOM   4580 C  CZ  . TYR C 1 39  ? 39.869  -17.426 -50.707 1.00 31.74  ? 39  TYR C CZ  1 
ATOM   4581 O  OH  . TYR C 1 39  ? 40.979  -18.214 -50.588 1.00 36.12  ? 39  TYR C OH  1 
ATOM   4582 N  N   A ASP C 1 40  ? 38.345  -12.214 -51.213 0.50 28.01  ? 40  ASP C N   1 
ATOM   4583 N  N   B ASP C 1 40  ? 38.315  -12.215 -51.175 0.50 28.06  ? 40  ASP C N   1 
ATOM   4584 C  CA  A ASP C 1 40  ? 39.298  -11.342 -51.974 0.50 24.09  ? 40  ASP C CA  1 
ATOM   4585 C  CA  B ASP C 1 40  ? 39.310  -11.412 -51.934 0.50 25.10  ? 40  ASP C CA  1 
ATOM   4586 C  C   A ASP C 1 40  ? 40.687  -11.974 -51.834 0.50 24.90  ? 40  ASP C C   1 
ATOM   4587 C  C   B ASP C 1 40  ? 40.628  -12.198 -51.739 0.50 28.89  ? 40  ASP C C   1 
ATOM   4588 O  O   A ASP C 1 40  ? 41.135  -12.163 -50.685 0.50 23.87  ? 40  ASP C O   1 
ATOM   4589 O  O   B ASP C 1 40  ? 41.456  -11.764 -50.914 0.50 24.04  ? 40  ASP C O   1 
ATOM   4590 C  CB  A ASP C 1 40  ? 39.161  -9.886  -51.483 0.50 24.73  ? 40  ASP C CB  1 
ATOM   4591 C  CB  B ASP C 1 40  ? 39.292  -9.959  -51.416 0.50 25.22  ? 40  ASP C CB  1 
ATOM   4592 C  CG  A ASP C 1 40  ? 40.102  -8.815  -52.049 0.50 22.99  ? 40  ASP C CG  1 
ATOM   4593 C  CG  B ASP C 1 40  ? 40.158  -8.901  -52.096 0.50 22.88  ? 40  ASP C CG  1 
ATOM   4594 O  OD1 A ASP C 1 40  ? 41.045  -9.143  -52.763 0.50 22.29  ? 40  ASP C OD1 1 
ATOM   4595 O  OD1 B ASP C 1 40  ? 41.023  -9.259  -52.882 0.50 24.43  ? 40  ASP C OD1 1 
ATOM   4596 O  OD2 A ASP C 1 40  ? 39.910  -7.619  -51.719 0.50 28.83  ? 40  ASP C OD2 1 
ATOM   4597 O  OD2 B ASP C 1 40  ? 39.993  -7.700  -51.774 0.50 28.55  ? 40  ASP C OD2 1 
ATOM   4598 N  N   A ALA C 1 41  ? 41.312  -12.320 -52.964 0.50 17.13  ? 41  ALA C N   1 
ATOM   4599 N  N   B ALA C 1 41  ? 40.726  -13.373 -52.368 0.50 26.19  ? 41  ALA C N   1 
ATOM   4600 C  CA  A ALA C 1 41  ? 42.627  -13.005 -52.982 0.50 14.15  ? 41  ALA C CA  1 
ATOM   4601 C  CA  B ALA C 1 41  ? 41.873  -14.308 -52.245 0.50 22.59  ? 41  ALA C CA  1 
ATOM   4602 C  C   A ALA C 1 41  ? 43.754  -12.081 -52.505 0.50 16.25  ? 41  ALA C C   1 
ATOM   4603 C  C   B ALA C 1 41  ? 43.152  -13.624 -51.740 0.50 23.53  ? 41  ALA C C   1 
ATOM   4604 O  O   A ALA C 1 41  ? 44.789  -12.611 -52.054 0.50 18.39  ? 41  ALA C O   1 
ATOM   4605 O  O   B ALA C 1 41  ? 43.749  -14.130 -50.768 0.50 26.39  ? 41  ALA C O   1 
ATOM   4606 C  CB  A ALA C 1 41  ? 42.905  -13.541 -54.365 0.50 20.14  ? 41  ALA C CB  1 
ATOM   4607 C  CB  B ALA C 1 41  ? 42.107  -15.003 -53.564 0.50 27.85  ? 41  ALA C CB  1 
ATOM   4608 N  N   A SER C 1 42  ? 43.568  -10.761 -52.598 0.50 17.24  ? 42  SER C N   1 
ATOM   4609 N  N   B SER C 1 42  ? 43.548  -12.523 -52.381 0.50 22.46  ? 42  SER C N   1 
ATOM   4610 C  CA  A SER C 1 42  ? 44.622  -9.845  -52.187 0.50 18.16  ? 42  SER C CA  1 
ATOM   4611 C  CA  B SER C 1 42  ? 44.798  -11.806 -52.094 0.50 24.34  ? 42  SER C CA  1 
ATOM   4612 C  C   A SER C 1 42  ? 44.866  -9.906  -50.676 0.50 24.52  ? 42  SER C C   1 
ATOM   4613 C  C   B SER C 1 42  ? 44.750  -11.019 -50.775 0.50 26.20  ? 42  SER C C   1 
ATOM   4614 O  O   A SER C 1 42  ? 45.849  -9.322  -50.201 0.50 18.13  ? 42  SER C O   1 
ATOM   4615 O  O   B SER C 1 42  ? 45.439  -9.982  -50.620 0.50 25.95  ? 42  SER C O   1 
ATOM   4616 C  CB  A SER C 1 42  ? 44.375  -8.411  -52.659 0.50 18.20  ? 42  SER C CB  1 
ATOM   4617 C  CB  B SER C 1 42  ? 44.856  -10.740 -53.108 0.50 26.82  ? 42  SER C CB  1 
ATOM   4618 O  OG  A SER C 1 42  ? 43.489  -7.700  -51.791 0.50 20.59  ? 42  SER C OG  1 
ATOM   4619 O  OG  B SER C 1 42  ? 43.634  -10.042 -53.000 0.50 29.19  ? 42  SER C OG  1 
ATOM   4620 N  N   A LEU C 1 43  ? 43.965  -10.580 -49.935 0.50 22.91  ? 43  LEU C N   1 
ATOM   4621 N  N   B LEU C 1 43  ? 43.810  -11.346 -49.890 0.50 27.63  ? 43  LEU C N   1 
ATOM   4622 C  CA  A LEU C 1 43  ? 43.971  -10.538 -48.476 0.50 20.31  ? 43  LEU C CA  1 
ATOM   4623 C  CA  B LEU C 1 43  ? 43.904  -10.718 -48.578 0.50 21.94  ? 43  LEU C CA  1 
ATOM   4624 C  C   A LEU C 1 43  ? 44.784  -11.678 -47.873 0.50 18.64  ? 43  LEU C C   1 
ATOM   4625 C  C   B LEU C 1 43  ? 44.788  -11.655 -47.775 0.50 18.59  ? 43  LEU C C   1 
ATOM   4626 O  O   A LEU C 1 43  ? 44.275  -12.621 -47.246 0.50 24.37  ? 43  LEU C O   1 
ATOM   4627 O  O   B LEU C 1 43  ? 44.309  -12.615 -47.162 0.50 24.46  ? 43  LEU C O   1 
ATOM   4628 C  CB  A LEU C 1 43  ? 42.559  -10.493 -47.919 0.50 18.63  ? 43  LEU C CB  1 
ATOM   4629 C  CB  B LEU C 1 43  ? 42.528  -10.547 -47.949 0.50 18.92  ? 43  LEU C CB  1 
ATOM   4630 C  CG  A LEU C 1 43  ? 41.744  -9.331  -48.480 0.50 16.18  ? 43  LEU C CG  1 
ATOM   4631 C  CG  B LEU C 1 43  ? 41.739  -9.355  -48.494 0.50 16.40  ? 43  LEU C CG  1 
ATOM   4632 C  CD1 A LEU C 1 43  ? 40.348  -9.378  -47.852 0.50 18.17  ? 43  LEU C CD1 1 
ATOM   4633 C  CD1 B LEU C 1 43  ? 40.357  -9.349  -47.843 0.50 18.21  ? 43  LEU C CD1 1 
ATOM   4634 C  CD2 A LEU C 1 43  ? 42.416  -7.975  -48.241 0.50 19.41  ? 43  LEU C CD2 1 
ATOM   4635 C  CD2 B LEU C 1 43  ? 42.456  -8.025  -48.263 0.50 19.65  ? 43  LEU C CD2 1 
ATOM   4636 N  N   . THR C 1 44  ? 46.080  -11.487 -48.005 1.00 20.01  ? 44  THR C N   1 
ATOM   4637 C  CA  . THR C 1 44  ? 47.098  -12.376 -47.494 1.00 19.80  ? 44  THR C CA  1 
ATOM   4638 C  C   . THR C 1 44  ? 47.280  -12.112 -45.991 1.00 18.72  ? 44  THR C C   1 
ATOM   4639 O  O   . THR C 1 44  ? 46.793  -11.122 -45.415 1.00 19.34  ? 44  THR C O   1 
ATOM   4640 C  CB  . THR C 1 44  ? 48.357  -12.211 -48.351 1.00 21.43  ? 44  THR C CB  1 
ATOM   4641 O  OG1 . THR C 1 44  ? 48.680  -10.818 -48.412 1.00 27.04  ? 44  THR C OG1 1 
ATOM   4642 C  CG2 . THR C 1 44  ? 48.199  -12.743 -49.761 1.00 21.97  ? 44  THR C CG2 1 
ATOM   4643 N  N   . PRO C 1 45  ? 48.026  -12.977 -45.287 1.00 20.34  ? 45  PRO C N   1 
ATOM   4644 C  CA  . PRO C 1 45  ? 48.227  -12.825 -43.834 1.00 20.27  ? 45  PRO C CA  1 
ATOM   4645 C  C   . PRO C 1 45  ? 49.094  -11.618 -43.519 1.00 22.85  ? 45  PRO C C   1 
ATOM   4646 O  O   . PRO C 1 45  ? 50.086  -11.370 -44.184 1.00 25.52  ? 45  PRO C O   1 
ATOM   4647 C  CB  . PRO C 1 45  ? 48.918  -14.119 -43.395 1.00 24.15  ? 45  PRO C CB  1 
ATOM   4648 C  CG  . PRO C 1 45  ? 48.623  -15.045 -44.509 1.00 19.17  ? 45  PRO C CG  1 
ATOM   4649 C  CD  . PRO C 1 45  ? 48.571  -14.240 -45.789 1.00 21.05  ? 45  PRO C CD  1 
ATOM   4650 N  N   . LEU C 1 46  ? 48.649  -10.827 -42.545 1.00 19.68  ? 46  LEU C N   1 
ATOM   4651 C  CA  . LEU C 1 46  ? 49.400  -9.665  -42.117 1.00 19.10  ? 46  LEU C CA  1 
ATOM   4652 C  C   . LEU C 1 46  ? 50.566  -10.131 -41.266 1.00 20.24  ? 46  LEU C C   1 
ATOM   4653 O  O   . LEU C 1 46  ? 50.477  -11.168 -40.631 1.00 22.76  ? 46  LEU C O   1 
ATOM   4654 C  CB  . LEU C 1 46  ? 48.501  -8.711  -41.330 1.00 17.36  ? 46  LEU C CB  1 
ATOM   4655 C  CG  . LEU C 1 46  ? 47.401  -8.002  -42.135 1.00 19.46  ? 46  LEU C CG  1 
ATOM   4656 C  CD1 . LEU C 1 46  ? 46.551  -7.170  -41.207 1.00 19.11  ? 46  LEU C CD1 1 
ATOM   4657 C  CD2 . LEU C 1 46  ? 47.976  -7.093  -43.223 1.00 22.57  ? 46  LEU C CD2 1 
ATOM   4658 N  N   . GLU C 1 47  ? 51.661  -9.372  -41.298 1.00 19.79  ? 47  GLU C N   1 
ATOM   4659 C  CA  . GLU C 1 47  ? 52.750  -9.644  -40.383 1.00 22.23  ? 47  GLU C CA  1 
ATOM   4660 C  C   . GLU C 1 47  ? 52.811  -8.552  -39.330 1.00 16.80  ? 47  GLU C C   1 
ATOM   4661 O  O   . GLU C 1 47  ? 52.718  -7.354  -39.630 1.00 21.06  ? 47  GLU C O   1 
ATOM   4662 C  CB  . GLU C 1 47  ? 54.042  -9.875  -41.169 1.00 29.20  ? 47  GLU C CB  1 
ATOM   4663 C  CG  . GLU C 1 47  ? 54.073  -11.250 -41.827 1.00 36.82  ? 47  GLU C CG  1 
ATOM   4664 N  N   . PHE C 1 48  ? 52.969  -8.979  -38.083 1.00 20.44  ? 48  PHE C N   1 
ATOM   4665 C  CA  . PHE C 1 48  ? 52.942  -8.114  -36.928 1.00 19.50  ? 48  PHE C CA  1 
ATOM   4666 C  C   . PHE C 1 48  ? 54.382  -7.978  -36.449 1.00 20.50  ? 48  PHE C C   1 
ATOM   4667 O  O   . PHE C 1 48  ? 54.905  -8.892  -35.851 1.00 27.57  ? 48  PHE C O   1 
ATOM   4668 C  CB  . PHE C 1 48  ? 51.934  -8.623  -35.888 1.00 20.53  ? 48  PHE C CB  1 
ATOM   4669 C  CG  . PHE C 1 48  ? 50.603  -8.996  -36.484 1.00 19.46  ? 48  PHE C CG  1 
ATOM   4670 C  CD1 . PHE C 1 48  ? 49.712  -8.023  -36.975 1.00 19.41  ? 48  PHE C CD1 1 
ATOM   4671 C  CD2 . PHE C 1 48  ? 50.277  -10.338 -36.603 1.00 18.77  ? 48  PHE C CD2 1 
ATOM   4672 C  CE1 . PHE C 1 48  ? 48.539  -8.425  -37.588 1.00 21.28  ? 48  PHE C CE1 1 
ATOM   4673 C  CE2 . PHE C 1 48  ? 49.076  -10.722 -37.182 1.00 21.18  ? 48  PHE C CE2 1 
ATOM   4674 C  CZ  . PHE C 1 48  ? 48.206  -9.762  -37.641 1.00 22.61  ? 48  PHE C CZ  1 
ATOM   4675 N  N   . GLN C 1 49  ? 54.991  -6.826  -36.727 1.00 20.27  ? 49  GLN C N   1 
ATOM   4676 C  CA  . GLN C 1 49  ? 56.406  -6.594  -36.564 1.00 20.64  ? 49  GLN C CA  1 
ATOM   4677 C  C   . GLN C 1 49  ? 56.587  -5.700  -35.341 1.00 17.99  ? 49  GLN C C   1 
ATOM   4678 O  O   . GLN C 1 49  ? 55.931  -4.659  -35.184 1.00 20.73  ? 49  GLN C O   1 
ATOM   4679 C  CB  . GLN C 1 49  ? 56.962  -5.968  -37.854 1.00 23.85  ? 49  GLN C CB  1 
ATOM   4680 C  CG  . GLN C 1 49  ? 56.744  -6.818  -39.115 1.00 29.96  ? 49  GLN C CG  1 
ATOM   4681 C  CD  . GLN C 1 49  ? 57.661  -8.016  -39.291 1.00 40.28  ? 49  GLN C CD  1 
ATOM   4682 O  OE1 . GLN C 1 49  ? 57.711  -8.647  -40.351 1.00 52.05  ? 49  GLN C OE1 1 
ATOM   4683 N  NE2 . GLN C 1 49  ? 58.423  -8.358  -38.264 1.00 38.20  ? 49  GLN C NE2 1 
ATOM   4684 N  N   . GLY C 1 50  ? 57.501  -6.101  -34.474 1.00 22.21  ? 50  GLY C N   1 
ATOM   4685 C  CA  . GLY C 1 50  ? 57.767  -5.277  -33.315 1.00 22.48  ? 50  GLY C CA  1 
ATOM   4686 C  C   . GLY C 1 50  ? 56.661  -5.318  -32.268 1.00 25.06  ? 50  GLY C C   1 
ATOM   4687 O  O   . GLY C 1 50  ? 56.610  -4.444  -31.409 1.00 23.17  ? 50  GLY C O   1 
ATOM   4688 N  N   . TYR C 1 51  ? 55.787  -6.336  -32.345 1.00 24.21  ? 51  TYR C N   1 
ATOM   4689 C  CA  . TYR C 1 51  ? 54.725  -6.492  -31.365 1.00 22.44  ? 51  TYR C CA  1 
ATOM   4690 C  C   . TYR C 1 51  ? 55.230  -7.027  -30.024 1.00 23.60  ? 51  TYR C C   1 
ATOM   4691 O  O   . TYR C 1 51  ? 54.560  -6.805  -29.024 1.00 26.19  ? 51  TYR C O   1 
ATOM   4692 C  CB  . TYR C 1 51  ? 53.606  -7.390  -31.897 1.00 20.36  ? 51  TYR C CB  1 
ATOM   4693 C  CG  . TYR C 1 51  ? 52.572  -6.651  -32.725 1.00 19.20  ? 51  TYR C CG  1 
ATOM   4694 C  CD1 . TYR C 1 51  ? 52.953  -5.772  -33.742 1.00 20.44  ? 51  TYR C CD1 1 
ATOM   4695 C  CD2 . TYR C 1 51  ? 51.211  -6.827  -32.513 1.00 19.05  ? 51  TYR C CD2 1 
ATOM   4696 C  CE1 . TYR C 1 51  ? 52.002  -5.067  -34.485 1.00 18.17  ? 51  TYR C CE1 1 
ATOM   4697 C  CE2 . TYR C 1 51  ? 50.240  -6.178  -33.295 1.00 17.40  ? 51  TYR C CE2 1 
ATOM   4698 C  CZ  . TYR C 1 51  ? 50.637  -5.278  -34.273 1.00 16.94  ? 51  TYR C CZ  1 
ATOM   4699 O  OH  . TYR C 1 51  ? 49.645  -4.612  -34.924 1.00 17.83  ? 51  TYR C OH  1 
ATOM   4700 N  N   . ASN C 1 52  ? 56.356  -7.767  -30.020 1.00 25.35  ? 52  ASN C N   1 
ATOM   4701 C  CA  . ASN C 1 52  ? 56.877  -8.388  -28.805 1.00 29.33  ? 52  ASN C CA  1 
ATOM   4702 C  C   . ASN C 1 52  ? 57.667  -7.327  -28.051 1.00 32.40  ? 52  ASN C C   1 
ATOM   4703 O  O   . ASN C 1 52  ? 58.886  -7.194  -28.244 1.00 34.41  ? 52  ASN C O   1 
ATOM   4704 C  CB  . ASN C 1 52  ? 57.765  -9.606  -29.056 1.00 27.47  ? 52  ASN C CB  1 
ATOM   4705 C  CG  . ASN C 1 52  ? 57.984  -10.410 -27.793 1.00 30.98  ? 52  ASN C CG  1 
ATOM   4706 O  OD1 . ASN C 1 52  ? 57.541  -10.032 -26.698 1.00 33.76  ? 52  ASN C OD1 1 
ATOM   4707 N  ND2 . ASN C 1 52  ? 58.688  -11.522 -27.938 1.00 42.66  ? 52  ASN C ND2 1 
ATOM   4708 N  N   . LEU C 1 53  ? 56.931  -6.549  -27.247 1.00 28.17  ? 53  LEU C N   1 
ATOM   4709 C  CA  . LEU C 1 53  ? 57.513  -5.374  -26.634 1.00 34.72  ? 53  LEU C CA  1 
ATOM   4710 C  C   . LEU C 1 53  ? 58.437  -5.838  -25.518 1.00 32.62  ? 53  LEU C C   1 
ATOM   4711 O  O   . LEU C 1 53  ? 58.123  -6.752  -24.747 1.00 32.06  ? 53  LEU C O   1 
ATOM   4712 C  CB  . LEU C 1 53  ? 56.452  -4.404  -26.107 1.00 30.30  ? 53  LEU C CB  1 
ATOM   4713 C  CG  . LEU C 1 53  ? 55.459  -3.815  -27.130 1.00 27.48  ? 53  LEU C CG  1 
ATOM   4714 C  CD1 . LEU C 1 53  ? 54.448  -2.965  -26.414 1.00 25.22  ? 53  LEU C CD1 1 
ATOM   4715 C  CD2 . LEU C 1 53  ? 56.107  -3.040  -28.283 1.00 27.40  ? 53  LEU C CD2 1 
ATOM   4716 N  N   . SER C 1 54  ? 59.603  -5.196  -25.514 1.00 35.13  ? 54  SER C N   1 
ATOM   4717 C  CA  . SER C 1 54  ? 60.625  -5.354  -24.496 1.00 32.06  ? 54  SER C CA  1 
ATOM   4718 C  C   . SER C 1 54  ? 60.018  -5.248  -23.088 1.00 28.74  ? 54  SER C C   1 
ATOM   4719 O  O   . SER C 1 54  ? 59.323  -4.272  -22.808 1.00 38.67  ? 54  SER C O   1 
ATOM   4720 C  CB  . SER C 1 54  ? 61.655  -4.300  -24.730 1.00 34.34  ? 54  SER C CB  1 
ATOM   4721 O  OG  . SER C 1 54  ? 62.669  -4.381  -23.749 1.00 35.56  ? 54  SER C OG  1 
ATOM   4722 N  N   . ALA C 1 55  ? 60.195  -6.291  -22.272 1.00 28.05  ? 55  ALA C N   1 
ATOM   4723 C  CA  . ALA C 1 55  ? 59.710  -6.337  -20.893 1.00 40.55  ? 55  ALA C CA  1 
ATOM   4724 C  C   . ALA C 1 55  ? 60.308  -5.202  -20.047 1.00 44.61  ? 55  ALA C C   1 
ATOM   4725 O  O   . ALA C 1 55  ? 59.829  -4.877  -18.956 1.00 46.87  ? 55  ALA C O   1 
ATOM   4726 C  CB  . ALA C 1 55  ? 59.993  -7.703  -20.298 1.00 40.00  ? 55  ALA C CB  1 
ATOM   4727 N  N   . ASN C 1 56  ? 61.366  -4.560  -20.535 1.00 44.08  ? 56  ASN C N   1 
ATOM   4728 C  CA  . ASN C 1 56  ? 61.951  -3.564  -19.648 1.00 46.52  ? 56  ASN C CA  1 
ATOM   4729 C  C   . ASN C 1 56  ? 61.737  -2.163  -20.203 1.00 33.46  ? 56  ASN C C   1 
ATOM   4730 O  O   . ASN C 1 56  ? 62.215  -1.193  -19.614 1.00 33.70  ? 56  ASN C O   1 
ATOM   4731 C  CB  . ASN C 1 56  ? 63.333  -3.947  -19.105 1.00 62.15  ? 56  ASN C CB  1 
ATOM   4732 C  CG  . ASN C 1 56  ? 64.283  -4.473  -20.157 1.00 73.55  ? 56  ASN C CG  1 
ATOM   4733 O  OD1 . ASN C 1 56  ? 64.457  -3.868  -21.208 1.00 56.44  ? 56  ASN C OD1 1 
ATOM   4734 N  ND2 . ASN C 1 56  ? 64.925  -5.588  -19.864 1.00 57.89  ? 56  ASN C ND2 1 
ATOM   4735 N  N   . LYS C 1 57  ? 60.981  -2.068  -21.313 1.00 32.64  ? 57  LYS C N   1 
ATOM   4736 C  CA  . LYS C 1 57  ? 60.329  -0.824  -21.696 1.00 33.15  ? 57  LYS C CA  1 
ATOM   4737 C  C   . LYS C 1 57  ? 58.968  -0.790  -20.988 1.00 36.65  ? 57  LYS C C   1 
ATOM   4738 O  O   . LYS C 1 57  ? 58.399  -1.857  -20.699 1.00 29.59  ? 57  LYS C O   1 
ATOM   4739 C  CB  . LYS C 1 57  ? 60.210  -0.738  -23.228 1.00 33.68  ? 57  LYS C CB  1 
ATOM   4740 C  CG  . LYS C 1 57  ? 61.475  -0.386  -23.995 1.00 39.17  ? 57  LYS C CG  1 
ATOM   4741 C  CD  . LYS C 1 57  ? 61.203  -0.265  -25.471 1.00 41.52  ? 57  LYS C CD  1 
ATOM   4742 N  N   . GLN C 1 58  ? 58.449  0.424   -20.713 1.00 27.03  ? 58  GLN C N   1 
ATOM   4743 C  CA  . GLN C 1 58  ? 57.082  0.592   -20.221 1.00 28.32  ? 58  GLN C CA  1 
ATOM   4744 C  C   . GLN C 1 58  ? 56.241  1.586   -21.028 1.00 25.88  ? 58  GLN C C   1 
ATOM   4745 O  O   . GLN C 1 58  ? 56.708  2.592   -21.573 1.00 29.51  ? 58  GLN C O   1 
ATOM   4746 C  CB  . GLN C 1 58  ? 57.034  0.818   -18.716 1.00 26.27  ? 58  GLN C CB  1 
ATOM   4747 C  CG  . GLN C 1 58  ? 57.855  -0.251  -17.983 1.00 26.33  ? 58  GLN C CG  1 
ATOM   4748 C  CD  . GLN C 1 58  ? 57.810  -0.177  -16.487 1.00 24.88  ? 58  GLN C CD  1 
ATOM   4749 O  OE1 . GLN C 1 58  ? 58.335  -1.060  -15.810 1.00 27.32  ? 58  GLN C OE1 1 
ATOM   4750 N  NE2 . GLN C 1 58  ? 57.207  0.881   -15.976 1.00 23.99  ? 58  GLN C NE2 1 
ATOM   4751 N  N   . PHE C 1 59  ? 54.939  1.309   -21.048 1.00 25.38  ? 59  PHE C N   1 
ATOM   4752 C  CA  . PHE C 1 59  ? 54.036  1.993   -21.956 1.00 23.26  ? 59  PHE C CA  1 
ATOM   4753 C  C   . PHE C 1 59  ? 52.884  2.629   -21.211 1.00 25.93  ? 59  PHE C C   1 
ATOM   4754 O  O   . PHE C 1 59  ? 52.316  2.026   -20.294 1.00 25.98  ? 59  PHE C O   1 
ATOM   4755 C  CB  . PHE C 1 59  ? 53.577  1.029   -23.036 1.00 21.06  ? 59  PHE C CB  1 
ATOM   4756 C  CG  . PHE C 1 59  ? 54.776  0.456   -23.745 1.00 24.33  ? 59  PHE C CG  1 
ATOM   4757 C  CD1 . PHE C 1 59  ? 55.311  1.119   -24.836 1.00 25.80  ? 59  PHE C CD1 1 
ATOM   4758 C  CD2 . PHE C 1 59  ? 55.452  -0.650  -23.238 1.00 26.17  ? 59  PHE C CD2 1 
ATOM   4759 C  CE1 . PHE C 1 59  ? 56.442  0.638   -25.478 1.00 26.18  ? 59  PHE C CE1 1 
ATOM   4760 C  CE2 . PHE C 1 59  ? 56.576  -1.137  -23.884 1.00 29.52  ? 59  PHE C CE2 1 
ATOM   4761 C  CZ  . PHE C 1 59  ? 57.058  -0.496  -25.010 1.00 31.85  ? 59  PHE C CZ  1 
ATOM   4762 N  N   . LEU C 1 60  ? 52.558  3.849   -21.647 1.00 24.55  ? 60  LEU C N   1 
ATOM   4763 C  CA  . LEU C 1 60  ? 51.625  4.704   -20.930 1.00 24.11  ? 60  LEU C CA  1 
ATOM   4764 C  C   . LEU C 1 60  ? 50.184  4.264   -21.160 1.00 19.72  ? 60  LEU C C   1 
ATOM   4765 O  O   . LEU C 1 60  ? 49.687  4.328   -22.280 1.00 25.97  ? 60  LEU C O   1 
ATOM   4766 C  CB  . LEU C 1 60  ? 51.836  6.153   -21.372 1.00 30.75  ? 60  LEU C CB  1 
ATOM   4767 C  CG  . LEU C 1 60  ? 51.142  7.242   -20.540 1.00 30.95  ? 60  LEU C CG  1 
ATOM   4768 C  CD1 . LEU C 1 60  ? 51.628  7.246   -19.084 1.00 34.46  ? 60  LEU C CD1 1 
ATOM   4769 C  CD2 . LEU C 1 60  ? 51.403  8.608   -21.167 1.00 38.81  ? 60  LEU C CD2 1 
ATOM   4770 N  N   . LEU C 1 61  ? 49.457  4.045   -20.056 1.00 26.88  ? 61  LEU C N   1 
ATOM   4771 C  CA  . LEU C 1 61  ? 48.027  3.781   -20.019 1.00 26.20  ? 61  LEU C CA  1 
ATOM   4772 C  C   . LEU C 1 61  ? 47.326  5.064   -19.573 1.00 30.85  ? 61  LEU C C   1 
ATOM   4773 O  O   . LEU C 1 61  ? 47.719  5.624   -18.536 1.00 37.43  ? 61  LEU C O   1 
ATOM   4774 C  CB  . LEU C 1 61  ? 47.800  2.749   -18.918 1.00 31.46  ? 61  LEU C CB  1 
ATOM   4775 C  CG  . LEU C 1 61  ? 47.000  1.491   -19.190 1.00 34.33  ? 61  LEU C CG  1 
ATOM   4776 C  CD1 . LEU C 1 61  ? 46.230  1.066   -17.948 1.00 35.73  ? 61  LEU C CD1 1 
ATOM   4777 C  CD2 . LEU C 1 61  ? 46.101  1.577   -20.402 1.00 30.68  ? 61  LEU C CD2 1 
ATOM   4778 N  N   . THR C 1 62  ? 46.258  5.468   -20.288 1.00 32.97  ? 62  THR C N   1 
ATOM   4779 C  CA  . THR C 1 62  ? 45.542  6.717   -20.031 1.00 28.57  ? 62  THR C CA  1 
ATOM   4780 C  C   . THR C 1 62  ? 44.022  6.539   -20.054 1.00 31.17  ? 62  THR C C   1 
ATOM   4781 O  O   . THR C 1 62  ? 43.488  5.926   -20.981 1.00 35.00  ? 62  THR C O   1 
ATOM   4782 C  CB  . THR C 1 62  ? 45.886  7.749   -21.116 1.00 39.39  ? 62  THR C CB  1 
ATOM   4783 O  OG1 . THR C 1 62  ? 47.271  8.043   -20.992 1.00 43.01  ? 62  THR C OG1 1 
ATOM   4784 C  CG2 . THR C 1 62  ? 45.114  9.040   -20.992 1.00 40.10  ? 62  THR C CG2 1 
ATOM   4785 N  N   . ASN C 1 63  ? 43.321  7.118   -19.060 1.00 27.99  ? 63  ASN C N   1 
ATOM   4786 C  CA  . ASN C 1 63  ? 41.871  7.326   -19.114 1.00 27.52  ? 63  ASN C CA  1 
ATOM   4787 C  C   . ASN C 1 63  ? 41.596  8.660   -19.785 1.00 30.00  ? 63  ASN C C   1 
ATOM   4788 O  O   . ASN C 1 63  ? 41.896  9.695   -19.217 1.00 33.95  ? 63  ASN C O   1 
ATOM   4789 C  CB  . ASN C 1 63  ? 41.199  7.275   -17.738 1.00 25.11  ? 63  ASN C CB  1 
ATOM   4790 C  CG  . ASN C 1 63  ? 39.710  7.585   -17.710 1.00 22.60  ? 63  ASN C CG  1 
ATOM   4791 O  OD1 . ASN C 1 63  ? 39.152  8.216   -18.608 1.00 28.18  ? 63  ASN C OD1 1 
ATOM   4792 N  ND2 . ASN C 1 63  ? 39.034  7.175   -16.645 1.00 29.89  ? 63  ASN C ND2 1 
ATOM   4793 N  N   . ASN C 1 64  ? 41.021  8.664   -20.996 1.00 28.93  ? 64  ASN C N   1 
ATOM   4794 C  CA  . ASN C 1 64  ? 40.799  9.937   -21.664 1.00 34.31  ? 64  ASN C CA  1 
ATOM   4795 C  C   . ASN C 1 64  ? 39.347  10.402  -21.568 1.00 32.27  ? 64  ASN C C   1 
ATOM   4796 O  O   . ASN C 1 64  ? 38.948  11.294  -22.324 1.00 38.58  ? 64  ASN C O   1 
ATOM   4797 C  CB  . ASN C 1 64  ? 41.162  9.933   -23.157 1.00 27.08  ? 64  ASN C CB  1 
ATOM   4798 C  CG  . ASN C 1 64  ? 40.419  8.884   -23.970 1.00 28.06  ? 64  ASN C CG  1 
ATOM   4799 O  OD1 . ASN C 1 64  ? 39.333  8.424   -23.588 1.00 26.94  ? 64  ASN C OD1 1 
ATOM   4800 N  ND2 . ASN C 1 64  ? 40.990  8.517   -25.109 1.00 30.76  ? 64  ASN C ND2 1 
ATOM   4801 N  N   . GLY C 1 65  ? 38.546  9.753   -20.727 1.00 30.83  ? 65  GLY C N   1 
ATOM   4802 C  CA  . GLY C 1 65  ? 37.168  10.184  -20.584 1.00 28.80  ? 65  GLY C CA  1 
ATOM   4803 C  C   . GLY C 1 65  ? 36.214  9.466   -21.538 1.00 29.36  ? 65  GLY C C   1 
ATOM   4804 O  O   . GLY C 1 65  ? 35.027  9.449   -21.261 1.00 32.77  ? 65  GLY C O   1 
ATOM   4805 N  N   . HIS C 1 66  ? 36.740  8.882   -22.636 1.00 27.60  ? 66  HIS C N   1 
ATOM   4806 C  CA  . HIS C 1 66  ? 35.966  8.217   -23.669 1.00 26.75  ? 66  HIS C CA  1 
ATOM   4807 C  C   . HIS C 1 66  ? 36.241  6.715   -23.670 1.00 20.21  ? 66  HIS C C   1 
ATOM   4808 O  O   . HIS C 1 66  ? 35.386  5.927   -24.080 1.00 24.09  ? 66  HIS C O   1 
ATOM   4809 C  CB  . HIS C 1 66  ? 36.211  8.856   -25.043 1.00 28.28  ? 66  HIS C CB  1 
ATOM   4810 C  CG  . HIS C 1 66  ? 35.942  10.321  -25.053 1.00 24.27  ? 66  HIS C CG  1 
ATOM   4811 N  ND1 . HIS C 1 66  ? 36.961  11.263  -25.202 1.00 28.72  ? 66  HIS C ND1 1 
ATOM   4812 C  CD2 . HIS C 1 66  ? 34.767  11.012  -24.950 1.00 28.64  ? 66  HIS C CD2 1 
ATOM   4813 C  CE1 . HIS C 1 66  ? 36.424  12.475  -25.168 1.00 32.25  ? 66  HIS C CE1 1 
ATOM   4814 N  NE2 . HIS C 1 66  ? 35.070  12.355  -25.020 1.00 27.25  ? 66  HIS C NE2 1 
ATOM   4815 N  N   . SER C 1 67  ? 37.449  6.318   -23.238 1.00 23.90  ? 67  SER C N   1 
ATOM   4816 C  CA  . SER C 1 67  ? 37.900  4.932   -23.279 1.00 21.16  ? 67  SER C CA  1 
ATOM   4817 C  C   . SER C 1 67  ? 39.142  4.840   -22.393 1.00 20.47  ? 67  SER C C   1 
ATOM   4818 O  O   . SER C 1 67  ? 39.563  5.869   -21.803 1.00 28.70  ? 67  SER C O   1 
ATOM   4819 C  CB  . SER C 1 67  ? 38.246  4.577   -24.692 1.00 25.53  ? 67  SER C CB  1 
ATOM   4820 O  OG  . SER C 1 67  ? 38.667  3.228   -24.778 1.00 24.16  ? 67  SER C OG  1 
ATOM   4821 N  N   . VAL C 1 68  ? 39.778  3.667   -22.327 1.00 23.35  ? 68  VAL C N   1 
ATOM   4822 C  CA  . VAL C 1 68  ? 41.140  3.618   -21.789 1.00 24.69  ? 68  VAL C CA  1 
ATOM   4823 C  C   . VAL C 1 68  ? 42.091  3.260   -22.935 1.00 24.60  ? 68  VAL C C   1 
ATOM   4824 O  O   . VAL C 1 68  ? 41.756  2.343   -23.685 1.00 22.68  ? 68  VAL C O   1 
ATOM   4825 C  CB  . VAL C 1 68  ? 41.232  2.610   -20.626 1.00 27.21  ? 68  VAL C CB  1 
ATOM   4826 C  CG1 . VAL C 1 68  ? 40.712  1.207   -20.942 1.00 25.65  ? 68  VAL C CG1 1 
ATOM   4827 C  CG2 . VAL C 1 68  ? 42.621  2.536   -20.031 1.00 32.91  ? 68  VAL C CG2 1 
ATOM   4828 N  N   . LYS C 1 69  ? 43.205  4.020   -23.094 1.00 25.74  ? 69  LYS C N   1 
ATOM   4829 C  CA  . LYS C 1 69  ? 44.184  3.801   -24.163 1.00 21.81  ? 69  LYS C CA  1 
ATOM   4830 C  C   . LYS C 1 69  ? 45.577  3.424   -23.620 1.00 18.83  ? 69  LYS C C   1 
ATOM   4831 O  O   . LYS C 1 69  ? 46.015  3.937   -22.588 1.00 28.59  ? 69  LYS C O   1 
ATOM   4832 C  CB  . LYS C 1 69  ? 44.237  4.937   -25.193 1.00 27.15  ? 69  LYS C CB  1 
ATOM   4833 C  CG  . LYS C 1 69  ? 44.674  6.304   -24.692 1.00 31.60  ? 69  LYS C CG  1 
ATOM   4834 C  CD  . LYS C 1 69  ? 44.228  7.413   -25.635 1.00 37.33  ? 69  LYS C CD  1 
ATOM   4835 C  CE  . LYS C 1 69  ? 45.356  8.085   -26.375 1.00 39.70  ? 69  LYS C CE  1 
ATOM   4836 N  NZ  . LYS C 1 69  ? 45.572  9.462   -25.869 1.00 49.33  ? 69  LYS C NZ  1 
ATOM   4837 N  N   . LEU C 1 70  ? 46.226  2.472   -24.302 1.00 21.10  ? 70  LEU C N   1 
ATOM   4838 C  CA  . LEU C 1 70  ? 47.619  2.129   -24.114 1.00 20.84  ? 70  LEU C CA  1 
ATOM   4839 C  C   . LEU C 1 70  ? 48.435  2.699   -25.285 1.00 23.60  ? 70  LEU C C   1 
ATOM   4840 O  O   . LEU C 1 70  ? 48.161  2.369   -26.446 1.00 22.08  ? 70  LEU C O   1 
ATOM   4841 C  CB  . LEU C 1 70  ? 47.776  0.607   -23.994 1.00 22.95  ? 70  LEU C CB  1 
ATOM   4842 C  CG  . LEU C 1 70  ? 49.229  0.120   -23.749 1.00 22.60  ? 70  LEU C CG  1 
ATOM   4843 C  CD1 . LEU C 1 70  ? 49.832  0.638   -22.427 1.00 26.30  ? 70  LEU C CD1 1 
ATOM   4844 C  CD2 . LEU C 1 70  ? 49.398  -1.382  -23.910 1.00 25.36  ? 70  LEU C CD2 1 
ATOM   4845 N  N   . ASN C 1 71  ? 49.439  3.547   -24.986 1.00 23.23  ? 71  ASN C N   1 
ATOM   4846 C  CA  . ASN C 1 71  ? 50.310  4.171   -25.986 1.00 21.07  ? 71  ASN C CA  1 
ATOM   4847 C  C   . ASN C 1 71  ? 51.273  3.108   -26.481 1.00 22.47  ? 71  ASN C C   1 
ATOM   4848 O  O   . ASN C 1 71  ? 51.751  2.291   -25.712 1.00 22.50  ? 71  ASN C O   1 
ATOM   4849 C  CB  . ASN C 1 71  ? 51.058  5.425   -25.492 1.00 22.37  ? 71  ASN C CB  1 
ATOM   4850 C  CG  . ASN C 1 71  ? 50.230  6.689   -25.381 1.00 26.45  ? 71  ASN C CG  1 
ATOM   4851 O  OD1 . ASN C 1 71  ? 49.061  6.729   -25.784 1.00 35.17  ? 71  ASN C OD1 1 
ATOM   4852 N  ND2 . ASN C 1 71  ? 50.824  7.743   -24.822 1.00 37.98  ? 71  ASN C ND2 1 
ATOM   4853 N  N   . LEU C 1 72  ? 51.476  3.084   -27.786 1.00 18.61  ? 72  LEU C N   1 
ATOM   4854 C  CA  . LEU C 1 72  ? 52.297  2.078   -28.411 1.00 20.85  ? 72  LEU C CA  1 
ATOM   4855 C  C   . LEU C 1 72  ? 53.406  2.800   -29.161 1.00 19.17  ? 72  LEU C C   1 
ATOM   4856 O  O   . LEU C 1 72  ? 53.221  3.933   -29.620 1.00 20.98  ? 72  LEU C O   1 
ATOM   4857 C  CB  . LEU C 1 72  ? 51.410  1.236   -29.335 1.00 16.49  ? 72  LEU C CB  1 
ATOM   4858 C  CG  . LEU C 1 72  ? 50.368  0.323   -28.680 1.00 17.14  ? 72  LEU C CG  1 
ATOM   4859 C  CD1 . LEU C 1 72  ? 49.495  -0.323  -29.753 1.00 16.89  ? 72  LEU C CD1 1 
ATOM   4860 C  CD2 . LEU C 1 72  ? 50.981  -0.764  -27.775 1.00 18.21  ? 72  LEU C CD2 1 
ATOM   4861 N  N   . PRO C 1 73  ? 54.596  2.163   -29.291 1.00 23.13  ? 73  PRO C N   1 
ATOM   4862 C  CA  . PRO C 1 73  ? 55.743  2.815   -29.922 1.00 23.56  ? 73  PRO C CA  1 
ATOM   4863 C  C   . PRO C 1 73  ? 55.661  2.674   -31.437 1.00 23.65  ? 73  PRO C C   1 
ATOM   4864 O  O   . PRO C 1 73  ? 55.185  1.663   -31.939 1.00 22.99  ? 73  PRO C O   1 
ATOM   4865 C  CB  . PRO C 1 73  ? 56.944  2.007   -29.403 1.00 23.81  ? 73  PRO C CB  1 
ATOM   4866 C  CG  . PRO C 1 73  ? 56.381  0.629   -29.178 1.00 22.88  ? 73  PRO C CG  1 
ATOM   4867 C  CD  . PRO C 1 73  ? 54.914  0.813   -28.812 1.00 23.70  ? 73  PRO C CD  1 
ATOM   4868 N  N   . SER C 1 74  ? 56.173  3.677   -32.157 1.00 26.26  ? 74  SER C N   1 
ATOM   4869 C  CA  . SER C 1 74  ? 56.058  3.723   -33.611 1.00 26.42  ? 74  SER C CA  1 
ATOM   4870 C  C   . SER C 1 74  ? 56.917  2.670   -34.337 1.00 28.00  ? 74  SER C C   1 
ATOM   4871 O  O   . SER C 1 74  ? 56.722  2.491   -35.532 1.00 31.61  ? 74  SER C O   1 
ATOM   4872 C  CB  . SER C 1 74  ? 56.267  5.129   -34.114 1.00 30.51  ? 74  SER C CB  1 
ATOM   4873 O  OG  . SER C 1 74  ? 57.565  5.584   -33.765 1.00 33.80  ? 74  SER C OG  1 
ATOM   4874 N  N   . ASP C 1 75  ? 57.878  1.980   -33.673 1.00 28.52  ? 75  ASP C N   1 
ATOM   4875 C  CA  . ASP C 1 75  ? 58.609  0.894   -34.349 1.00 28.19  ? 75  ASP C CA  1 
ATOM   4876 C  C   . ASP C 1 75  ? 57.737  -0.366  -34.437 1.00 22.77  ? 75  ASP C C   1 
ATOM   4877 O  O   . ASP C 1 75  ? 58.036  -1.297  -35.189 1.00 27.78  ? 75  ASP C O   1 
ATOM   4878 C  CB  . ASP C 1 75  ? 59.991  0.567   -33.754 1.00 34.70  ? 75  ASP C CB  1 
ATOM   4879 C  CG  . ASP C 1 75  ? 59.829  0.028   -32.347 1.00 37.26  ? 75  ASP C CG  1 
ATOM   4880 O  OD1 . ASP C 1 75  ? 59.476  0.847   -31.465 1.00 33.01  ? 75  ASP C OD1 1 
ATOM   4881 O  OD2 . ASP C 1 75  ? 60.004  -1.213  -32.144 1.00 33.52  ? 75  ASP C OD2 1 
ATOM   4882 N  N   . MET C 1 76  ? 56.619  -0.391  -33.710 1.00 22.59  ? 76  MET C N   1 
ATOM   4883 C  CA  . MET C 1 76  ? 55.633  -1.461  -33.846 1.00 20.77  ? 76  MET C CA  1 
ATOM   4884 C  C   . MET C 1 76  ? 54.798  -1.194  -35.110 1.00 18.53  ? 76  MET C C   1 
ATOM   4885 O  O   . MET C 1 76  ? 54.336  -0.062  -35.328 1.00 20.23  ? 76  MET C O   1 
ATOM   4886 C  CB  . MET C 1 76  ? 54.674  -1.400  -32.657 1.00 21.41  ? 76  MET C CB  1 
ATOM   4887 C  CG  . MET C 1 76  ? 53.626  -2.434  -32.657 1.00 22.97  ? 76  MET C CG  1 
ATOM   4888 S  SD  . MET C 1 76  ? 52.871  -2.363  -30.987 1.00 23.82  ? 76  MET C SD  1 
ATOM   4889 C  CE  . MET C 1 76  ? 51.314  -3.081  -31.443 1.00 24.71  ? 76  MET C CE  1 
ATOM   4890 N  N   . HIS C 1 77  ? 54.658  -2.196  -35.985 1.00 17.37  ? 77  HIS C N   1 
ATOM   4891 C  CA  . HIS C 1 77  ? 53.971  -1.967  -37.262 1.00 16.92  ? 77  HIS C CA  1 
ATOM   4892 C  C   . HIS C 1 77  ? 53.357  -3.219  -37.899 1.00 17.67  ? 77  HIS C C   1 
ATOM   4893 O  O   . HIS C 1 77  ? 53.680  -4.351  -37.554 1.00 18.59  ? 77  HIS C O   1 
ATOM   4894 C  CB  . HIS C 1 77  ? 54.847  -1.180  -38.226 1.00 18.38  ? 77  HIS C CB  1 
ATOM   4895 C  CG  . HIS C 1 77  ? 56.077  -1.902  -38.661 1.00 19.13  ? 77  HIS C CG  1 
ATOM   4896 N  ND1 . HIS C 1 77  ? 57.280  -1.792  -37.986 1.00 21.51  ? 77  HIS C ND1 1 
ATOM   4897 C  CD2 . HIS C 1 77  ? 56.319  -2.638  -39.769 1.00 20.06  ? 77  HIS C CD2 1 
ATOM   4898 C  CE1 . HIS C 1 77  ? 58.193  -2.498  -38.629 1.00 23.40  ? 77  HIS C CE1 1 
ATOM   4899 N  NE2 . HIS C 1 77  ? 57.635  -3.006  -39.742 1.00 21.66  ? 77  HIS C NE2 1 
ATOM   4900 N  N   . ILE C 1 78  ? 52.447  -2.965  -38.850 1.00 16.94  ? 78  ILE C N   1 
ATOM   4901 C  CA  . ILE C 1 78  ? 51.870  -3.974  -39.719 1.00 16.94  ? 78  ILE C CA  1 
ATOM   4902 C  C   . ILE C 1 78  ? 52.684  -3.957  -41.013 1.00 17.01  ? 78  ILE C C   1 
ATOM   4903 O  O   . ILE C 1 78  ? 52.896  -2.868  -41.565 1.00 18.41  ? 78  ILE C O   1 
ATOM   4904 C  CB  . ILE C 1 78  ? 50.400  -3.696  -40.037 1.00 16.24  ? 78  ILE C CB  1 
ATOM   4905 C  CG1 . ILE C 1 78  ? 49.530  -3.664  -38.774 1.00 19.67  ? 78  ILE C CG1 1 
ATOM   4906 C  CG2 . ILE C 1 78  ? 49.912  -4.699  -41.067 1.00 21.44  ? 78  ILE C CG2 1 
ATOM   4907 C  CD1 . ILE C 1 78  ? 48.180  -2.908  -39.013 1.00 17.29  ? 78  ILE C CD1 1 
ATOM   4908 N  N   . GLN C 1 79  ? 53.163  -5.133  -41.435 1.00 21.36  ? 79  GLN C N   1 
ATOM   4909 C  CA  . GLN C 1 79  ? 53.687  -5.380  -42.778 1.00 25.68  ? 79  GLN C CA  1 
ATOM   4910 C  C   . GLN C 1 79  ? 52.678  -6.222  -43.573 1.00 23.49  ? 79  GLN C C   1 
ATOM   4911 O  O   . GLN C 1 79  ? 52.048  -7.150  -43.021 1.00 25.61  ? 79  GLN C O   1 
ATOM   4912 C  CB  . GLN C 1 79  ? 55.062  -6.066  -42.711 1.00 35.42  ? 79  GLN C CB  1 
ATOM   4913 C  CG  . GLN C 1 79  ? 55.491  -6.721  -44.024 1.00 43.04  ? 79  GLN C CG  1 
ATOM   4914 C  CD  . GLN C 1 79  ? 56.678  -7.634  -43.851 1.00 52.76  ? 79  GLN C CD  1 
ATOM   4915 O  OE1 . GLN C 1 79  ? 57.818  -7.228  -44.050 1.00 66.51  ? 79  GLN C OE1 1 
ATOM   4916 N  NE2 . GLN C 1 79  ? 56.416  -8.870  -43.447 1.00 55.08  ? 79  GLN C NE2 1 
ATOM   4917 N  N   . GLY C 1 80  ? 52.536  -5.883  -44.862 1.00 21.49  ? 80  GLY C N   1 
ATOM   4918 C  CA  . GLY C 1 80  ? 51.648  -6.601  -45.769 1.00 23.86  ? 80  GLY C CA  1 
ATOM   4919 C  C   . GLY C 1 80  ? 50.547  -5.761  -46.416 1.00 19.70  ? 80  GLY C C   1 
ATOM   4920 O  O   . GLY C 1 80  ? 49.903  -6.200  -47.361 1.00 23.77  ? 80  GLY C O   1 
ATOM   4921 N  N   . LEU C 1 81  ? 50.339  -4.540  -45.932 1.00 19.31  ? 81  LEU C N   1 
ATOM   4922 C  CA  . LEU C 1 81  ? 49.455  -3.593  -46.613 1.00 21.24  ? 81  LEU C CA  1 
ATOM   4923 C  C   . LEU C 1 81  ? 50.275  -2.805  -47.636 1.00 22.25  ? 81  LEU C C   1 
ATOM   4924 O  O   . LEU C 1 81  ? 51.469  -3.023  -47.781 1.00 25.04  ? 81  LEU C O   1 
ATOM   4925 C  CB  . LEU C 1 81  ? 48.808  -2.662  -45.582 1.00 20.73  ? 81  LEU C CB  1 
ATOM   4926 C  CG  . LEU C 1 81  ? 47.936  -3.346  -44.539 1.00 20.25  ? 81  LEU C CG  1 
ATOM   4927 C  CD1 . LEU C 1 81  ? 47.511  -2.393  -43.425 1.00 18.44  ? 81  LEU C CD1 1 
ATOM   4928 C  CD2 . LEU C 1 81  ? 46.689  -3.927  -45.168 1.00 18.87  ? 81  LEU C CD2 1 
ATOM   4929 N  N   . GLN C 1 82  ? 49.634  -1.874  -48.345 1.00 22.23  ? 82  GLN C N   1 
ATOM   4930 C  CA  . GLN C 1 82  ? 50.247  -1.154  -49.461 1.00 26.63  ? 82  GLN C CA  1 
ATOM   4931 C  C   . GLN C 1 82  ? 51.244  -0.083  -48.981 1.00 26.52  ? 82  GLN C C   1 
ATOM   4932 O  O   . GLN C 1 82  ? 52.068  0.396   -49.758 1.00 25.86  ? 82  GLN C O   1 
ATOM   4933 C  CB  . GLN C 1 82  ? 49.152  -0.677  -50.422 1.00 27.43  ? 82  GLN C CB  1 
ATOM   4934 C  CG  . GLN C 1 82  ? 48.547  -1.799  -51.294 1.00 30.75  ? 82  GLN C CG  1 
ATOM   4935 C  CD  . GLN C 1 82  ? 49.370  -2.345  -52.449 1.00 42.74  ? 82  GLN C CD  1 
ATOM   4936 O  OE1 . GLN C 1 82  ? 50.364  -1.762  -52.888 1.00 42.88  ? 82  GLN C OE1 1 
ATOM   4937 N  NE2 . GLN C 1 82  ? 48.959  -3.493  -52.980 1.00 43.58  ? 82  GLN C NE2 1 
ATOM   4938 N  N   . SER C 1 83  ? 51.194  0.288   -47.693 1.00 18.19  ? 83  SER C N   1 
ATOM   4939 C  CA  . SER C 1 83  ? 52.202  1.101   -47.036 1.00 19.23  ? 83  SER C CA  1 
ATOM   4940 C  C   . SER C 1 83  ? 52.485  0.474   -45.671 1.00 17.75  ? 83  SER C C   1 
ATOM   4941 O  O   . SER C 1 83  ? 51.671  -0.306  -45.186 1.00 16.99  ? 83  SER C O   1 
ATOM   4942 C  CB  . SER C 1 83  ? 51.685  2.521   -46.803 1.00 17.82  ? 83  SER C CB  1 
ATOM   4943 O  OG  . SER C 1 83  ? 51.342  3.173   -48.019 1.00 24.42  ? 83  SER C OG  1 
ATOM   4944 N  N   . ARG C 1 84  ? 53.559  0.904   -45.013 1.00 16.17  ? 84  ARG C N   1 
ATOM   4945 C  CA  . ARG C 1 84  ? 53.752  0.540   -43.619 1.00 15.33  ? 84  ARG C CA  1 
ATOM   4946 C  C   . ARG C 1 84  ? 52.786  1.347   -42.775 1.00 12.58  ? 84  ARG C C   1 
ATOM   4947 O  O   . ARG C 1 84  ? 52.724  2.585   -42.888 1.00 16.40  ? 84  ARG C O   1 
ATOM   4948 C  CB  . ARG C 1 84  ? 55.195  0.803   -43.165 1.00 16.11  ? 84  ARG C CB  1 
ATOM   4949 C  CG  . ARG C 1 84  ? 55.403  0.456   -41.695 1.00 16.39  ? 84  ARG C CG  1 
ATOM   4950 C  CD  . ARG C 1 84  ? 56.865  0.705   -41.256 1.00 16.18  ? 84  ARG C CD  1 
ATOM   4951 N  NE  . ARG C 1 84  ? 57.773  -0.256  -41.850 1.00 18.90  ? 84  ARG C NE  1 
ATOM   4952 C  CZ  . ARG C 1 84  ? 59.055  -0.424  -41.442 1.00 19.43  ? 84  ARG C CZ  1 
ATOM   4953 N  NH1 . ARG C 1 84  ? 59.557  0.346   -40.500 1.00 21.52  ? 84  ARG C NH1 1 
ATOM   4954 N  NH2 . ARG C 1 84  ? 59.843  -1.342  -41.976 1.00 24.81  ? 84  ARG C NH2 1 
ATOM   4955 N  N   . TYR C 1 85  ? 52.137  0.682   -41.830 1.00 13.22  ? 85  TYR C N   1 
ATOM   4956 C  CA  . TYR C 1 85  ? 51.277  1.328   -40.859 1.00 13.50  ? 85  TYR C CA  1 
ATOM   4957 C  C   . TYR C 1 85  ? 51.876  1.062   -39.481 1.00 13.26  ? 85  TYR C C   1 
ATOM   4958 O  O   . TYR C 1 85  ? 51.930  -0.095  -39.067 1.00 14.94  ? 85  TYR C O   1 
ATOM   4959 C  CB  . TYR C 1 85  ? 49.823  0.836   -40.924 1.00 12.70  ? 85  TYR C CB  1 
ATOM   4960 C  CG  . TYR C 1 85  ? 49.077  1.377   -42.117 1.00 13.01  ? 85  TYR C CG  1 
ATOM   4961 C  CD1 . TYR C 1 85  ? 49.176  0.791   -43.377 1.00 13.97  ? 85  TYR C CD1 1 
ATOM   4962 C  CD2 . TYR C 1 85  ? 48.240  2.470   -41.957 1.00 13.16  ? 85  TYR C CD2 1 
ATOM   4963 C  CE1 . TYR C 1 85  ? 48.458  1.302   -44.448 1.00 14.83  ? 85  TYR C CE1 1 
ATOM   4964 C  CE2 . TYR C 1 85  ? 47.555  2.989   -43.034 1.00 12.56  ? 85  TYR C CE2 1 
ATOM   4965 C  CZ  . TYR C 1 85  ? 47.668  2.417   -44.279 1.00 12.92  ? 85  TYR C CZ  1 
ATOM   4966 O  OH  . TYR C 1 85  ? 46.993  2.940   -45.335 1.00 15.22  ? 85  TYR C OH  1 
ATOM   4967 N  N   . SER C 1 86  ? 52.238  2.135   -38.764 1.00 14.38  ? 86  SER C N   1 
ATOM   4968 C  CA  . SER C 1 86  ? 52.886  2.048   -37.480 1.00 14.83  ? 86  SER C CA  1 
ATOM   4969 C  C   . SER C 1 86  ? 51.878  2.298   -36.363 1.00 16.10  ? 86  SER C C   1 
ATOM   4970 O  O   . SER C 1 86  ? 50.967  3.129   -36.487 1.00 16.29  ? 86  SER C O   1 
ATOM   4971 C  CB  . SER C 1 86  ? 54.003  3.096   -37.401 1.00 18.83  ? 86  SER C CB  1 
ATOM   4972 O  OG  . SER C 1 86  ? 55.023  2.828   -38.332 1.00 20.22  ? 86  SER C OG  1 
ATOM   4973 N  N   . ALA C 1 87  ? 52.103  1.602   -35.248 1.00 16.52  ? 87  ALA C N   1 
ATOM   4974 C  CA  . ALA C 1 87  ? 51.207  1.663   -34.096 1.00 16.15  ? 87  ALA C CA  1 
ATOM   4975 C  C   . ALA C 1 87  ? 51.258  3.043   -33.443 1.00 16.18  ? 87  ALA C C   1 
ATOM   4976 O  O   . ALA C 1 87  ? 52.314  3.698   -33.441 1.00 18.86  ? 87  ALA C O   1 
ATOM   4977 C  CB  . ALA C 1 87  ? 51.461  0.502   -33.155 1.00 19.75  ? 87  ALA C CB  1 
ATOM   4978 N  N   . THR C 1 88  ? 50.092  3.460   -32.923 1.00 16.42  ? 88  THR C N   1 
ATOM   4979 C  CA  . THR C 1 88  ? 50.011  4.651   -32.080 1.00 18.15  ? 88  THR C CA  1 
ATOM   4980 C  C   . THR C 1 88  ? 49.410  4.320   -30.713 1.00 18.46  ? 88  THR C C   1 
ATOM   4981 O  O   . THR C 1 88  ? 49.814  4.883   -29.699 1.00 17.44  ? 88  THR C O   1 
ATOM   4982 C  CB  . THR C 1 88  ? 49.331  5.849   -32.771 1.00 20.68  ? 88  THR C CB  1 
ATOM   4983 O  OG1 . THR C 1 88  ? 49.385  7.028   -31.959 1.00 24.00  ? 88  THR C OG1 1 
ATOM   4984 C  CG2 . THR C 1 88  ? 47.878  5.587   -33.097 1.00 19.48  ? 88  THR C CG2 1 
ATOM   4985 N  N   . GLN C 1 89  ? 48.358  3.491   -30.700 1.00 17.20  ? 89  GLN C N   1 
ATOM   4986 C  CA  . GLN C 1 89  ? 47.739  3.181   -29.416 1.00 16.58  ? 89  GLN C CA  1 
ATOM   4987 C  C   . GLN C 1 89  ? 46.772  2.040   -29.606 1.00 13.71  ? 89  GLN C C   1 
ATOM   4988 O  O   . GLN C 1 89  ? 46.317  1.801   -30.707 1.00 15.66  ? 89  GLN C O   1 
ATOM   4989 C  CB  . GLN C 1 89  ? 46.946  4.362   -28.845 1.00 17.24  ? 89  GLN C CB  1 
ATOM   4990 C  CG  . GLN C 1 89  ? 45.917  4.957   -29.820 1.00 21.79  ? 89  GLN C CG  1 
ATOM   4991 C  CD  . GLN C 1 89  ? 44.506  4.701   -29.365 1.00 23.24  ? 89  GLN C CD  1 
ATOM   4992 O  OE1 . GLN C 1 89  ? 44.144  3.586   -29.076 1.00 20.91  ? 89  GLN C OE1 1 
ATOM   4993 N  NE2 . GLN C 1 89  ? 43.692  5.726   -29.297 1.00 22.47  ? 89  GLN C NE2 1 
ATOM   4994 N  N   . LEU C 1 90  ? 46.402  1.407   -28.489 1.00 16.33  ? 90  LEU C N   1 
ATOM   4995 C  CA  . LEU C 1 90  ? 45.223  0.572   -28.474 1.00 15.40  ? 90  LEU C CA  1 
ATOM   4996 C  C   . LEU C 1 90  ? 44.224  1.064   -27.423 1.00 15.50  ? 90  LEU C C   1 
ATOM   4997 O  O   . LEU C 1 90  ? 44.594  1.715   -26.442 1.00 18.24  ? 90  LEU C O   1 
ATOM   4998 C  CB  . LEU C 1 90  ? 45.571  -0.915  -28.354 1.00 16.23  ? 90  LEU C CB  1 
ATOM   4999 C  CG  . LEU C 1 90  ? 46.343  -1.365  -27.100 1.00 18.15  ? 90  LEU C CG  1 
ATOM   5000 C  CD1 . LEU C 1 90  ? 45.437  -1.500  -25.867 1.00 21.33  ? 90  LEU C CD1 1 
ATOM   5001 C  CD2 . LEU C 1 90  ? 47.043  -2.715  -27.319 1.00 24.26  ? 90  LEU C CD2 1 
ATOM   5002 N  N   . HIS C 1 91  ? 42.942  0.721   -27.631 1.00 14.13  ? 91  HIS C N   1 
ATOM   5003 C  CA  . HIS C 1 91  ? 41.872  1.074   -26.712 1.00 13.59  ? 91  HIS C CA  1 
ATOM   5004 C  C   . HIS C 1 91  ? 40.773  0.024   -26.803 1.00 13.98  ? 91  HIS C C   1 
ATOM   5005 O  O   . HIS C 1 91  ? 40.788  -0.819  -27.698 1.00 13.83  ? 91  HIS C O   1 
ATOM   5006 C  CB  . HIS C 1 91  ? 41.410  2.534   -26.903 1.00 16.11  ? 91  HIS C CB  1 
ATOM   5007 C  CG  . HIS C 1 91  ? 40.786  2.667   -28.250 1.00 16.05  ? 91  HIS C CG  1 
ATOM   5008 N  ND1 . HIS C 1 91  ? 41.502  3.106   -29.354 1.00 14.75  ? 91  HIS C ND1 1 
ATOM   5009 C  CD2 . HIS C 1 91  ? 39.544  2.365   -28.700 1.00 15.05  ? 91  HIS C CD2 1 
ATOM   5010 C  CE1 . HIS C 1 91  ? 40.709  3.013   -30.426 1.00 12.20  ? 91  HIS C CE1 1 
ATOM   5011 N  NE2 . HIS C 1 91  ? 39.533  2.563   -30.034 1.00 14.18  ? 91  HIS C NE2 1 
ATOM   5012 N  N   . LEU C 1 92  ? 39.758  0.166   -25.959 1.00 15.09  ? 92  LEU C N   1 
ATOM   5013 C  CA  . LEU C 1 92  ? 38.673  -0.796  -25.976 1.00 14.01  ? 92  LEU C CA  1 
ATOM   5014 C  C   . LEU C 1 92  ? 37.303  -0.111  -25.967 1.00 12.15  ? 92  LEU C C   1 
ATOM   5015 O  O   . LEU C 1 92  ? 37.161  1.066   -25.630 1.00 15.56  ? 92  LEU C O   1 
ATOM   5016 C  CB  . LEU C 1 92  ? 38.739  -1.751  -24.778 1.00 19.14  ? 92  LEU C CB  1 
ATOM   5017 C  CG  . LEU C 1 92  ? 39.916  -2.723  -24.865 1.00 19.58  ? 92  LEU C CG  1 
ATOM   5018 C  CD1 . LEU C 1 92  ? 41.080  -2.296  -23.975 1.00 22.82  ? 92  LEU C CD1 1 
ATOM   5019 C  CD2 . LEU C 1 92  ? 39.503  -4.154  -24.519 1.00 21.11  ? 92  LEU C CD2 1 
ATOM   5020 N  N   . HIS C 1 93  ? 36.283  -0.884  -26.352 1.00 14.06  ? 93  HIS C N   1 
ATOM   5021 C  CA  . HIS C 1 93  ? 34.903  -0.433  -26.331 1.00 12.70  ? 93  HIS C CA  1 
ATOM   5022 C  C   . HIS C 1 93  ? 34.078  -1.499  -25.636 1.00 12.07  ? 93  HIS C C   1 
ATOM   5023 O  O   . HIS C 1 93  ? 34.288  -2.709  -25.902 1.00 12.61  ? 93  HIS C O   1 
ATOM   5024 C  CB  . HIS C 1 93  ? 34.355  -0.232  -27.791 1.00 12.68  ? 93  HIS C CB  1 
ATOM   5025 C  CG  . HIS C 1 93  ? 35.052  0.816   -28.615 1.00 9.86   ? 93  HIS C CG  1 
ATOM   5026 N  ND1 . HIS C 1 93  ? 34.723  2.168   -28.565 1.00 10.98  ? 93  HIS C ND1 1 
ATOM   5027 C  CD2 . HIS C 1 93  ? 36.188  0.750   -29.378 1.00 9.46   ? 93  HIS C CD2 1 
ATOM   5028 C  CE1 . HIS C 1 93  ? 35.551  2.828   -29.361 1.00 10.52  ? 93  HIS C CE1 1 
ATOM   5029 N  NE2 . HIS C 1 93  ? 36.440  2.026   -29.861 1.00 9.91   ? 93  HIS C NE2 1 
ATOM   5030 N  N   . TRP C 1 94  ? 33.142  -1.080  -24.780 1.00 11.86  ? 94  TRP C N   1 
ATOM   5031 C  CA  . TRP C 1 94  ? 32.384  -2.097  -24.044 1.00 12.54  ? 94  TRP C CA  1 
ATOM   5032 C  C   . TRP C 1 94  ? 30.950  -1.595  -23.737 1.00 13.03  ? 94  TRP C C   1 
ATOM   5033 O  O   . TRP C 1 94  ? 30.596  -0.420  -23.979 1.00 13.50  ? 94  TRP C O   1 
ATOM   5034 C  CB  . TRP C 1 94  ? 33.140  -2.573  -22.765 1.00 13.64  ? 94  TRP C CB  1 
ATOM   5035 C  CG  . TRP C 1 94  ? 33.408  -1.466  -21.805 1.00 15.39  ? 94  TRP C CG  1 
ATOM   5036 C  CD1 . TRP C 1 94  ? 32.596  -0.995  -20.799 1.00 13.93  ? 94  TRP C CD1 1 
ATOM   5037 C  CD2 . TRP C 1 94  ? 34.581  -0.645  -21.797 1.00 14.70  ? 94  TRP C CD2 1 
ATOM   5038 N  NE1 . TRP C 1 94  ? 33.175  0.097   -20.211 1.00 17.70  ? 94  TRP C NE1 1 
ATOM   5039 C  CE2 . TRP C 1 94  ? 34.425  0.283   -20.736 1.00 16.94  ? 94  TRP C CE2 1 
ATOM   5040 C  CE3 . TRP C 1 94  ? 35.776  -0.642  -22.532 1.00 15.14  ? 94  TRP C CE3 1 
ATOM   5041 C  CZ2 . TRP C 1 94  ? 35.372  1.272   -20.443 1.00 16.54  ? 94  TRP C CZ2 1 
ATOM   5042 C  CZ3 . TRP C 1 94  ? 36.715  0.319   -22.237 1.00 17.15  ? 94  TRP C CZ3 1 
ATOM   5043 C  CH2 . TRP C 1 94  ? 36.531  1.236   -21.185 1.00 20.03  ? 94  TRP C CH2 1 
ATOM   5044 N  N   . GLY C 1 95  ? 30.123  -2.465  -23.183 1.00 12.86  ? 95  GLY C N   1 
ATOM   5045 C  CA  . GLY C 1 95  ? 28.755  -2.150  -22.781 1.00 13.11  ? 95  GLY C CA  1 
ATOM   5046 C  C   . GLY C 1 95  ? 28.646  -1.897  -21.279 1.00 14.15  ? 95  GLY C C   1 
ATOM   5047 O  O   . GLY C 1 95  ? 29.255  -0.973  -20.743 1.00 15.80  ? 95  GLY C O   1 
ATOM   5048 N  N   . ASN C 1 96  ? 27.781  -2.659  -20.614 1.00 17.97  ? 96  ASN C N   1 
ATOM   5049 C  CA  . ASN C 1 96  ? 27.568  -2.440  -19.190 1.00 18.20  ? 96  ASN C CA  1 
ATOM   5050 C  C   . ASN C 1 96  ? 27.077  -3.741  -18.571 1.00 17.84  ? 96  ASN C C   1 
ATOM   5051 O  O   . ASN C 1 96  ? 26.697  -4.674  -19.306 1.00 17.02  ? 96  ASN C O   1 
ATOM   5052 C  CB  . ASN C 1 96  ? 26.601  -1.278  -18.940 1.00 21.04  ? 96  ASN C CB  1 
ATOM   5053 C  CG  . ASN C 1 96  ? 25.160  -1.634  -19.238 1.00 22.68  ? 96  ASN C CG  1 
ATOM   5054 O  OD1 . ASN C 1 96  ? 24.476  -2.120  -18.355 1.00 25.92  ? 96  ASN C OD1 1 
ATOM   5055 N  ND2 . ASN C 1 96  ? 24.706  -1.454  -20.468 1.00 26.40  ? 96  ASN C ND2 1 
ATOM   5056 N  N   . PRO C 1 97  ? 27.156  -3.916  -17.231 1.00 19.03  ? 97  PRO C N   1 
ATOM   5057 C  CA  . PRO C 1 97  ? 26.820  -5.211  -16.673 1.00 20.38  ? 97  PRO C CA  1 
ATOM   5058 C  C   . PRO C 1 97  ? 25.381  -5.686  -16.909 1.00 23.18  ? 97  PRO C C   1 
ATOM   5059 O  O   . PRO C 1 97  ? 25.144  -6.903  -16.968 1.00 24.20  ? 97  PRO C O   1 
ATOM   5060 C  CB  . PRO C 1 97  ? 27.146  -5.087  -15.158 1.00 25.45  ? 97  PRO C CB  1 
ATOM   5061 C  CG  . PRO C 1 97  ? 28.055  -3.848  -15.066 1.00 23.38  ? 97  PRO C CG  1 
ATOM   5062 C  CD  . PRO C 1 97  ? 27.641  -2.964  -16.223 1.00 21.06  ? 97  PRO C CD  1 
ATOM   5063 N  N   . ASN C 1 98  ? 24.415  -4.764  -17.055 1.00 19.93  ? 98  ASN C N   1 
ATOM   5064 C  CA  . ASN C 1 98  ? 23.037  -5.154  -17.345 1.00 22.95  ? 98  ASN C CA  1 
ATOM   5065 C  C   . ASN C 1 98  ? 22.821  -5.530  -18.824 1.00 20.55  ? 98  ASN C C   1 
ATOM   5066 O  O   . ASN C 1 98  ? 21.812  -6.189  -19.136 1.00 25.94  ? 98  ASN C O   1 
ATOM   5067 C  CB  . ASN C 1 98  ? 22.003  -4.089  -16.969 1.00 28.02  ? 98  ASN C CB  1 
ATOM   5068 C  CG  . ASN C 1 98  ? 21.847  -3.852  -15.482 1.00 34.71  ? 98  ASN C CG  1 
ATOM   5069 O  OD1 . ASN C 1 98  ? 21.875  -4.783  -14.672 1.00 42.45  ? 98  ASN C OD1 1 
ATOM   5070 N  ND2 . ASN C 1 98  ? 21.658  -2.596  -15.113 1.00 42.95  ? 98  ASN C ND2 1 
ATOM   5071 N  N   . ASP C 1 99  ? 23.733  -5.108  -19.723 1.00 20.39  ? 99  ASP C N   1 
ATOM   5072 C  CA  . ASP C 1 99  ? 23.612  -5.364  -21.156 1.00 17.55  ? 99  ASP C CA  1 
ATOM   5073 C  C   . ASP C 1 99  ? 25.020  -5.510  -21.721 1.00 18.94  ? 99  ASP C C   1 
ATOM   5074 O  O   . ASP C 1 99  ? 25.547  -4.557  -22.308 1.00 16.40  ? 99  ASP C O   1 
ATOM   5075 C  CB  . ASP C 1 99  ? 22.764  -4.309  -21.896 1.00 17.80  ? 99  ASP C CB  1 
ATOM   5076 C  CG  . ASP C 1 99  ? 22.214  -4.746  -23.239 1.00 17.68  ? 99  ASP C CG  1 
ATOM   5077 O  OD1 . ASP C 1 99  ? 22.453  -5.908  -23.634 1.00 20.41  ? 99  ASP C OD1 1 
ATOM   5078 O  OD2 . ASP C 1 99  ? 21.622  -3.884  -23.952 1.00 24.31  ? 99  ASP C OD2 1 
ATOM   5079 N  N   . PRO C 1 100 ? 25.692  -6.643  -21.435 1.00 16.23  ? 100 PRO C N   1 
ATOM   5080 C  CA  . PRO C 1 100 ? 27.138  -6.770  -21.640 1.00 15.04  ? 100 PRO C CA  1 
ATOM   5081 C  C   . PRO C 1 100 ? 27.435  -7.126  -23.091 1.00 14.17  ? 100 PRO C C   1 
ATOM   5082 O  O   . PRO C 1 100 ? 28.017  -8.174  -23.367 1.00 16.39  ? 100 PRO C O   1 
ATOM   5083 C  CB  . PRO C 1 100 ? 27.521  -7.898  -20.664 1.00 16.04  ? 100 PRO C CB  1 
ATOM   5084 C  CG  . PRO C 1 100 ? 26.325  -8.780  -20.647 1.00 20.11  ? 100 PRO C CG  1 
ATOM   5085 C  CD  . PRO C 1 100 ? 25.171  -7.792  -20.677 1.00 18.96  ? 100 PRO C CD  1 
ATOM   5086 N  N   . HIS C 1 101 ? 27.092  -6.211  -24.028 1.00 12.59  ? 101 HIS C N   1 
ATOM   5087 C  CA  . HIS C 1 101 ? 27.191  -6.479  -25.462 1.00 13.56  ? 101 HIS C CA  1 
ATOM   5088 C  C   . HIS C 1 101 ? 27.584  -5.185  -26.180 1.00 15.52  ? 101 HIS C C   1 
ATOM   5089 O  O   . HIS C 1 101 ? 26.815  -4.698  -26.988 1.00 17.85  ? 101 HIS C O   1 
ATOM   5090 C  CB  . HIS C 1 101 ? 25.855  -7.013  -26.058 1.00 14.82  ? 101 HIS C CB  1 
ATOM   5091 C  CG  . HIS C 1 101 ? 25.251  -8.110  -25.282 1.00 14.91  ? 101 HIS C CG  1 
ATOM   5092 N  ND1 . HIS C 1 101 ? 25.729  -9.439  -25.282 1.00 15.54  ? 101 HIS C ND1 1 
ATOM   5093 C  CD2 . HIS C 1 101 ? 24.278  -8.049  -24.347 1.00 16.28  ? 101 HIS C CD2 1 
ATOM   5094 C  CE1 . HIS C 1 101 ? 25.038  -10.138 -24.401 1.00 18.07  ? 101 HIS C CE1 1 
ATOM   5095 N  NE2 . HIS C 1 101 ? 24.155  -9.325  -23.838 1.00 15.76  ? 101 HIS C NE2 1 
ATOM   5096 N  N   . GLY C 1 102 ? 28.843  -4.770  -25.992 1.00 10.77  ? 102 GLY C N   1 
ATOM   5097 C  CA  . GLY C 1 102 ? 29.251  -3.428  -26.376 1.00 10.66  ? 102 GLY C CA  1 
ATOM   5098 C  C   . GLY C 1 102 ? 30.467  -3.426  -27.300 1.00 8.71   ? 102 GLY C C   1 
ATOM   5099 O  O   . GLY C 1 102 ? 31.118  -2.392  -27.451 1.00 11.04  ? 102 GLY C O   1 
ATOM   5100 N  N   . SER C 1 103 ? 30.543  -4.436  -28.154 1.00 9.92   ? 103 SER C N   1 
ATOM   5101 C  CA  . SER C 1 103 ? 31.361  -4.329  -29.344 1.00 10.00  ? 103 SER C CA  1 
ATOM   5102 C  C   . SER C 1 103 ? 30.825  -3.217  -30.247 1.00 10.31  ? 103 SER C C   1 
ATOM   5103 O  O   . SER C 1 103 ? 29.642  -2.876  -30.197 1.00 11.33  ? 103 SER C O   1 
ATOM   5104 C  CB  . SER C 1 103 ? 31.487  -5.648  -30.093 1.00 10.37  ? 103 SER C CB  1 
ATOM   5105 O  OG  . SER C 1 103 ? 30.296  -6.027  -30.753 1.00 9.87   ? 103 SER C OG  1 
ATOM   5106 N  N   . GLU C 1 104 ? 31.648  -2.731  -31.170 1.00 9.06   ? 104 GLU C N   1 
ATOM   5107 C  CA  . GLU C 1 104 ? 31.240  -1.753  -32.191 1.00 8.70   ? 104 GLU C CA  1 
ATOM   5108 C  C   . GLU C 1 104 ? 30.712  -2.481  -33.435 1.00 8.04   ? 104 GLU C C   1 
ATOM   5109 O  O   . GLU C 1 104 ? 29.575  -2.292  -33.823 1.00 8.97   ? 104 GLU C O   1 
ATOM   5110 C  CB  . GLU C 1 104 ? 32.399  -0.819  -32.494 1.00 9.08   ? 104 GLU C CB  1 
ATOM   5111 C  CG  . GLU C 1 104 ? 32.867  -0.025  -31.279 1.00 8.85   ? 104 GLU C CG  1 
ATOM   5112 C  CD  . GLU C 1 104 ? 33.296  1.398   -31.578 1.00 10.12  ? 104 GLU C CD  1 
ATOM   5113 O  OE1 . GLU C 1 104 ? 34.353  1.504   -32.201 1.00 10.65  ? 104 GLU C OE1 1 
ATOM   5114 O  OE2 . GLU C 1 104 ? 32.501  2.280   -31.261 1.00 11.58  ? 104 GLU C OE2 1 
ATOM   5115 N  N   . HIS C 1 105 ? 31.588  -3.291  -34.055 1.00 8.23   ? 105 HIS C N   1 
ATOM   5116 C  CA  . HIS C 1 105 ? 31.181  -4.198  -35.141 1.00 8.49   ? 105 HIS C CA  1 
ATOM   5117 C  C   . HIS C 1 105 ? 30.221  -5.282  -34.628 1.00 7.88   ? 105 HIS C C   1 
ATOM   5118 O  O   . HIS C 1 105 ? 30.317  -5.677  -33.456 1.00 9.78   ? 105 HIS C O   1 
ATOM   5119 C  CB  . HIS C 1 105 ? 32.348  -4.814  -35.922 1.00 8.88   ? 105 HIS C CB  1 
ATOM   5120 C  CG  . HIS C 1 105 ? 33.092  -3.712  -36.614 1.00 8.16   ? 105 HIS C CG  1 
ATOM   5121 N  ND1 . HIS C 1 105 ? 34.165  -3.036  -36.056 1.00 9.42   ? 105 HIS C ND1 1 
ATOM   5122 C  CD2 . HIS C 1 105 ? 32.923  -3.184  -37.856 1.00 7.67   ? 105 HIS C CD2 1 
ATOM   5123 C  CE1 . HIS C 1 105 ? 34.592  -2.115  -36.929 1.00 9.02   ? 105 HIS C CE1 1 
ATOM   5124 N  NE2 . HIS C 1 105 ? 33.846  -2.183  -38.039 1.00 8.06   ? 105 HIS C NE2 1 
ATOM   5125 N  N   . THR C 1 106 ? 29.219  -5.615  -35.437 1.00 8.59   ? 106 THR C N   1 
ATOM   5126 C  CA  . THR C 1 106 ? 28.418  -6.781  -35.135 1.00 8.33   ? 106 THR C CA  1 
ATOM   5127 C  C   . THR C 1 106 ? 28.597  -7.800  -36.255 1.00 9.44   ? 106 THR C C   1 
ATOM   5128 O  O   . THR C 1 106 ? 29.103  -7.465  -37.314 1.00 9.47   ? 106 THR C O   1 
ATOM   5129 C  CB  . THR C 1 106 ? 26.934  -6.352  -35.015 1.00 9.01   ? 106 THR C CB  1 
ATOM   5130 O  OG1 . THR C 1 106 ? 26.471  -5.749  -36.246 1.00 9.46   ? 106 THR C OG1 1 
ATOM   5131 C  CG2 . THR C 1 106 ? 26.693  -5.376  -33.886 1.00 10.33  ? 106 THR C CG2 1 
ATOM   5132 N  N   . VAL C 1 107 ? 28.275  -9.081  -35.932 1.00 8.81   ? 107 VAL C N   1 
ATOM   5133 C  CA  . VAL C 1 107 ? 28.330  -10.183 -36.886 1.00 10.41  ? 107 VAL C CA  1 
ATOM   5134 C  C   . VAL C 1 107 ? 26.918  -10.756 -36.974 1.00 9.73   ? 107 VAL C C   1 
ATOM   5135 O  O   . VAL C 1 107 ? 26.376  -11.224 -35.974 1.00 10.76  ? 107 VAL C O   1 
ATOM   5136 C  CB  . VAL C 1 107 ? 29.401  -11.216 -36.535 1.00 11.71  ? 107 VAL C CB  1 
ATOM   5137 C  CG1 . VAL C 1 107 ? 29.376  -12.403 -37.476 1.00 15.05  ? 107 VAL C CG1 1 
ATOM   5138 C  CG2 . VAL C 1 107 ? 30.777  -10.555 -36.479 1.00 12.43  ? 107 VAL C CG2 1 
ATOM   5139 N  N   . SER C 1 108 ? 26.312  -10.683 -38.172 1.00 10.32  ? 108 SER C N   1 
ATOM   5140 C  CA  . SER C 1 108 ? 24.950  -11.171 -38.372 1.00 12.92  ? 108 SER C CA  1 
ATOM   5141 C  C   . SER C 1 108 ? 24.048  -10.615 -37.267 1.00 10.25  ? 108 SER C C   1 
ATOM   5142 O  O   . SER C 1 108 ? 23.164  -11.270 -36.717 1.00 14.25  ? 108 SER C O   1 
ATOM   5143 C  CB  . SER C 1 108 ? 24.865  -12.713 -38.404 1.00 12.72  ? 108 SER C CB  1 
ATOM   5144 O  OG  . SER C 1 108 ? 25.718  -13.271 -39.385 1.00 18.97  ? 108 SER C OG  1 
ATOM   5145 N  N   . GLY C 1 109 ? 24.217  -9.314  -37.015 1.00 10.88  ? 109 GLY C N   1 
ATOM   5146 C  CA  . GLY C 1 109 ? 23.331  -8.529  -36.181 1.00 11.72  ? 109 GLY C CA  1 
ATOM   5147 C  C   . GLY C 1 109 ? 23.674  -8.660  -34.709 1.00 12.38  ? 109 GLY C C   1 
ATOM   5148 O  O   . GLY C 1 109 ? 23.068  -7.982  -33.891 1.00 14.89  ? 109 GLY C O   1 
ATOM   5149 N  N   . GLN C 1 110 ? 24.707  -9.443  -34.374 1.00 12.03  ? 110 GLN C N   1 
ATOM   5150 C  CA  . GLN C 1 110 ? 24.946  -9.707  -32.972 1.00 10.38  ? 110 GLN C CA  1 
ATOM   5151 C  C   . GLN C 1 110 ? 26.181  -8.932  -32.492 1.00 9.42   ? 110 GLN C C   1 
ATOM   5152 O  O   . GLN C 1 110 ? 27.269  -8.969  -33.108 1.00 8.96   ? 110 GLN C O   1 
ATOM   5153 C  CB  . GLN C 1 110 ? 25.190  -11.198 -32.776 1.00 11.78  ? 110 GLN C CB  1 
ATOM   5154 C  CG  . GLN C 1 110 ? 24.121  -12.084 -33.408 1.00 16.02  ? 110 GLN C CG  1 
ATOM   5155 C  CD  . GLN C 1 110 ? 22.729  -11.668 -32.976 1.00 14.78  ? 110 GLN C CD  1 
ATOM   5156 O  OE1 . GLN C 1 110 ? 21.877  -11.379 -33.838 1.00 20.95  ? 110 GLN C OE1 1 
ATOM   5157 N  NE2 . GLN C 1 110 ? 22.493  -11.575 -31.659 1.00 15.28  ? 110 GLN C NE2 1 
ATOM   5158 N  N   . HIS C 1 111 ? 26.006  -8.233  -31.366 1.00 11.82  ? 111 HIS C N   1 
ATOM   5159 C  CA  . HIS C 1 111 ? 27.168  -7.658  -30.702 1.00 11.68  ? 111 HIS C CA  1 
ATOM   5160 C  C   . HIS C 1 111 ? 27.997  -8.722  -29.973 1.00 14.58  ? 111 HIS C C   1 
ATOM   5161 O  O   . HIS C 1 111 ? 27.464  -9.730  -29.483 1.00 19.87  ? 111 HIS C O   1 
ATOM   5162 C  CB  . HIS C 1 111 ? 26.772  -6.639  -29.650 1.00 13.25  ? 111 HIS C CB  1 
ATOM   5163 C  CG  . HIS C 1 111 ? 26.288  -5.353  -30.189 1.00 12.85  ? 111 HIS C CG  1 
ATOM   5164 N  ND1 . HIS C 1 111 ? 27.084  -4.281  -30.321 1.00 16.17  ? 111 HIS C ND1 1 
ATOM   5165 C  CD2 . HIS C 1 111 ? 25.081  -5.046  -30.709 1.00 13.90  ? 111 HIS C CD2 1 
ATOM   5166 C  CE1 . HIS C 1 111 ? 26.376  -3.268  -30.851 1.00 17.53  ? 111 HIS C CE1 1 
ATOM   5167 N  NE2 . HIS C 1 111 ? 25.111  -3.730  -31.088 1.00 18.49  ? 111 HIS C NE2 1 
ATOM   5168 N  N   . PHE C 1 112 ? 29.303  -8.476  -29.850 1.00 12.41  ? 112 PHE C N   1 
ATOM   5169 C  CA  . PHE C 1 112 ? 30.175  -9.163  -28.894 1.00 12.26  ? 112 PHE C CA  1 
ATOM   5170 C  C   . PHE C 1 112 ? 30.140  -8.414  -27.581 1.00 10.63  ? 112 PHE C C   1 
ATOM   5171 O  O   . PHE C 1 112 ? 29.711  -7.256  -27.541 1.00 12.87  ? 112 PHE C O   1 
ATOM   5172 C  CB  . PHE C 1 112 ? 31.552  -9.435  -29.509 1.00 12.40  ? 112 PHE C CB  1 
ATOM   5173 C  CG  . PHE C 1 112 ? 31.500  -10.576 -30.500 1.00 13.90  ? 112 PHE C CG  1 
ATOM   5174 C  CD1 . PHE C 1 112 ? 30.974  -10.418 -31.775 1.00 17.78  ? 112 PHE C CD1 1 
ATOM   5175 C  CD2 . PHE C 1 112 ? 31.936  -11.843 -30.148 1.00 16.21  ? 112 PHE C CD2 1 
ATOM   5176 C  CE1 . PHE C 1 112 ? 30.896  -11.502 -32.659 1.00 18.64  ? 112 PHE C CE1 1 
ATOM   5177 C  CE2 . PHE C 1 112 ? 31.863  -12.918 -31.024 1.00 20.03  ? 112 PHE C CE2 1 
ATOM   5178 C  CZ  . PHE C 1 112 ? 31.356  -12.746 -32.298 1.00 19.91  ? 112 PHE C CZ  1 
ATOM   5179 N  N   . ALA C 1 113 ? 30.835  -8.914  -26.569 1.00 12.56  ? 113 ALA C N   1 
ATOM   5180 C  CA  . ALA C 1 113 ? 30.909  -8.293  -25.249 1.00 12.91  ? 113 ALA C CA  1 
ATOM   5181 C  C   . ALA C 1 113 ? 31.677  -7.000  -25.300 1.00 13.97  ? 113 ALA C C   1 
ATOM   5182 O  O   . ALA C 1 113 ? 31.244  -6.026  -24.681 1.00 14.57  ? 113 ALA C O   1 
ATOM   5183 C  CB  . ALA C 1 113 ? 31.520  -9.211  -24.231 1.00 15.46  ? 113 ALA C CB  1 
ATOM   5184 N  N   . ALA C 1 114 ? 32.790  -7.011  -26.081 1.00 12.06  ? 114 ALA C N   1 
ATOM   5185 C  CA  . ALA C 1 114 ? 33.631  -5.827  -26.136 1.00 11.99  ? 114 ALA C CA  1 
ATOM   5186 C  C   . ALA C 1 114 ? 34.462  -5.922  -27.404 1.00 11.33  ? 114 ALA C C   1 
ATOM   5187 O  O   . ALA C 1 114 ? 34.371  -6.874  -28.167 1.00 12.62  ? 114 ALA C O   1 
ATOM   5188 C  CB  . ALA C 1 114 ? 34.521  -5.848  -24.879 1.00 12.94  ? 114 ALA C CB  1 
ATOM   5189 N  N   . GLU C 1 115 ? 35.192  -4.844  -27.710 1.00 11.25  ? 115 GLU C N   1 
ATOM   5190 C  CA  . GLU C 1 115 ? 36.042  -4.869  -28.882 1.00 11.29  ? 115 GLU C CA  1 
ATOM   5191 C  C   . GLU C 1 115 ? 37.332  -4.150  -28.527 1.00 10.17  ? 115 GLU C C   1 
ATOM   5192 O  O   . GLU C 1 115 ? 37.282  -3.021  -27.945 1.00 12.70  ? 115 GLU C O   1 
ATOM   5193 C  CB  . GLU C 1 115 ? 35.298  -4.186  -30.036 1.00 10.07  ? 115 GLU C CB  1 
ATOM   5194 C  CG  . GLU C 1 115 ? 35.936  -4.237  -31.408 1.00 10.17  ? 115 GLU C CG  1 
ATOM   5195 C  CD  . GLU C 1 115 ? 34.974  -3.878  -32.542 1.00 8.08   ? 115 GLU C CD  1 
ATOM   5196 O  OE1 . GLU C 1 115 ? 35.471  -3.404  -33.615 1.00 9.42   ? 115 GLU C OE1 1 
ATOM   5197 O  OE2 . GLU C 1 115 ? 33.762  -4.085  -32.372 1.00 9.37   ? 115 GLU C OE2 1 
ATOM   5198 N  N   . LEU C 1 116 ? 38.450  -4.679  -29.042 1.00 11.00  ? 116 LEU C N   1 
ATOM   5199 C  CA  . LEU C 1 116 ? 39.756  -4.014  -28.880 1.00 12.08  ? 116 LEU C CA  1 
ATOM   5200 C  C   . LEU C 1 116 ? 40.181  -3.453  -30.224 1.00 10.87  ? 116 LEU C C   1 
ATOM   5201 O  O   . LEU C 1 116 ? 40.021  -4.124  -31.216 1.00 13.18  ? 116 LEU C O   1 
ATOM   5202 C  CB  . LEU C 1 116 ? 40.811  -5.025  -28.427 1.00 14.37  ? 116 LEU C CB  1 
ATOM   5203 C  CG  . LEU C 1 116 ? 42.256  -4.515  -28.485 1.00 16.74  ? 116 LEU C CG  1 
ATOM   5204 C  CD1 . LEU C 1 116 ? 42.532  -3.588  -27.310 1.00 20.75  ? 116 LEU C CD1 1 
ATOM   5205 C  CD2 . LEU C 1 116 ? 43.250  -5.663  -28.546 1.00 20.72  ? 116 LEU C CD2 1 
ATOM   5206 N  N   . HIS C 1 117 ? 40.665  -2.200  -30.279 1.00 11.64  ? 117 HIS C N   1 
ATOM   5207 C  CA  . HIS C 1 117 ? 41.179  -1.575  -31.496 1.00 11.59  ? 117 HIS C CA  1 
ATOM   5208 C  C   . HIS C 1 117 ? 42.666  -1.255  -31.283 1.00 10.86  ? 117 HIS C C   1 
ATOM   5209 O  O   . HIS C 1 117 ? 43.021  -0.594  -30.290 1.00 12.28  ? 117 HIS C O   1 
ATOM   5210 C  CB  . HIS C 1 117 ? 40.405  -0.261  -31.683 1.00 11.11  ? 117 HIS C CB  1 
ATOM   5211 C  CG  . HIS C 1 117 ? 38.987  -0.455  -32.106 1.00 8.85   ? 117 HIS C CG  1 
ATOM   5212 N  ND1 . HIS C 1 117 ? 38.012  0.498   -31.880 1.00 14.48  ? 117 HIS C ND1 1 
ATOM   5213 C  CD2 . HIS C 1 117 ? 38.376  -1.481  -32.736 1.00 8.01   ? 117 HIS C CD2 1 
ATOM   5214 C  CE1 . HIS C 1 117 ? 36.861  0.067   -32.354 1.00 9.65   ? 117 HIS C CE1 1 
ATOM   5215 N  NE2 . HIS C 1 117 ? 37.058  -1.146  -32.885 1.00 8.22   ? 117 HIS C NE2 1 
ATOM   5216 N  N   . ILE C 1 118 ? 43.510  -1.687  -32.225 1.00 11.63  ? 118 ILE C N   1 
ATOM   5217 C  CA  . ILE C 1 118 ? 44.897  -1.293  -32.295 1.00 12.61  ? 118 ILE C CA  1 
ATOM   5218 C  C   . ILE C 1 118 ? 45.057  -0.315  -33.468 1.00 10.09  ? 118 ILE C C   1 
ATOM   5219 O  O   . ILE C 1 118 ? 44.918  -0.733  -34.621 1.00 11.65  ? 118 ILE C O   1 
ATOM   5220 C  CB  . ILE C 1 118 ? 45.850  -2.501  -32.390 1.00 13.92  ? 118 ILE C CB  1 
ATOM   5221 C  CG1 . ILE C 1 118 ? 45.468  -3.628  -31.413 1.00 15.56  ? 118 ILE C CG1 1 
ATOM   5222 C  CG2 . ILE C 1 118 ? 47.321  -2.041  -32.235 1.00 16.97  ? 118 ILE C CG2 1 
ATOM   5223 C  CD1 . ILE C 1 118 ? 46.348  -4.873  -31.500 1.00 18.77  ? 118 ILE C CD1 1 
ATOM   5224 N  N   . VAL C 1 119 ? 45.302  0.971   -33.158 1.00 12.17  ? 119 VAL C N   1 
ATOM   5225 C  CA  . VAL C 1 119 ? 45.251  2.043   -34.150 1.00 11.43  ? 119 VAL C CA  1 
ATOM   5226 C  C   . VAL C 1 119 ? 46.679  2.250   -34.674 1.00 12.14  ? 119 VAL C C   1 
ATOM   5227 O  O   . VAL C 1 119 ? 47.616  2.395   -33.892 1.00 13.70  ? 119 VAL C O   1 
ATOM   5228 C  CB  . VAL C 1 119 ? 44.760  3.349   -33.473 1.00 11.40  ? 119 VAL C CB  1 
ATOM   5229 C  CG1 . VAL C 1 119 ? 44.736  4.489   -34.518 1.00 14.02  ? 119 VAL C CG1 1 
ATOM   5230 C  CG2 . VAL C 1 119 ? 43.392  3.198   -32.776 1.00 11.74  ? 119 VAL C CG2 1 
ATOM   5231 N  N   . HIS C 1 120 ? 46.784  2.243   -36.005 1.00 13.53  ? 120 HIS C N   1 
ATOM   5232 C  CA  . HIS C 1 120 ? 48.022  2.466   -36.710 1.00 11.96  ? 120 HIS C CA  1 
ATOM   5233 C  C   . HIS C 1 120 ? 47.825  3.605   -37.722 1.00 11.09  ? 120 HIS C C   1 
ATOM   5234 O  O   . HIS C 1 120 ? 46.730  3.884   -38.155 1.00 11.96  ? 120 HIS C O   1 
ATOM   5235 C  CB  . HIS C 1 120 ? 48.489  1.207   -37.474 1.00 12.29  ? 120 HIS C CB  1 
ATOM   5236 C  CG  . HIS C 1 120 ? 48.633  -0.074  -36.710 1.00 12.79  ? 120 HIS C CG  1 
ATOM   5237 N  ND1 . HIS C 1 120 ? 47.575  -0.770  -36.171 1.00 13.55  ? 120 HIS C ND1 1 
ATOM   5238 C  CD2 . HIS C 1 120 ? 49.754  -0.767  -36.425 1.00 15.58  ? 120 HIS C CD2 1 
ATOM   5239 C  CE1 . HIS C 1 120 ? 48.062  -1.862  -35.589 1.00 14.86  ? 120 HIS C CE1 1 
ATOM   5240 N  NE2 . HIS C 1 120 ? 49.394  -1.886  -35.721 1.00 14.91  ? 120 HIS C NE2 1 
ATOM   5241 N  N   . TYR C 1 121 ? 48.928  4.273   -38.078 1.00 14.63  ? 121 TYR C N   1 
ATOM   5242 C  CA  . TYR C 1 121 ? 48.866  5.328   -39.063 1.00 14.30  ? 121 TYR C CA  1 
ATOM   5243 C  C   . TYR C 1 121 ? 49.893  5.045   -40.164 1.00 13.78  ? 121 TYR C C   1 
ATOM   5244 O  O   . TYR C 1 121 ? 50.909  4.352   -39.946 1.00 14.43  ? 121 TYR C O   1 
ATOM   5245 C  CB  . TYR C 1 121 ? 49.141  6.725   -38.464 1.00 18.09  ? 121 TYR C CB  1 
ATOM   5246 C  CG  . TYR C 1 121 ? 50.534  6.895   -37.933 1.00 17.00  ? 121 TYR C CG  1 
ATOM   5247 C  CD1 . TYR C 1 121 ? 50.868  6.316   -36.710 1.00 18.22  ? 121 TYR C CD1 1 
ATOM   5248 C  CD2 . TYR C 1 121 ? 51.498  7.585   -38.657 1.00 18.99  ? 121 TYR C CD2 1 
ATOM   5249 C  CE1 . TYR C 1 121 ? 52.168  6.392   -36.232 1.00 18.87  ? 121 TYR C CE1 1 
ATOM   5250 C  CE2 . TYR C 1 121 ? 52.793  7.709   -38.167 1.00 19.04  ? 121 TYR C CE2 1 
ATOM   5251 C  CZ  . TYR C 1 121 ? 53.118  7.087   -36.970 1.00 19.61  ? 121 TYR C CZ  1 
ATOM   5252 O  OH  . TYR C 1 121 ? 54.352  7.208   -36.449 1.00 24.66  ? 121 TYR C OH  1 
ATOM   5253 N  N   . ASN C 1 122 ? 49.667  5.662   -41.329 1.00 14.57  ? 122 ASN C N   1 
ATOM   5254 C  CA  . ASN C 1 122 ? 50.531  5.406   -42.467 1.00 14.67  ? 122 ASN C CA  1 
ATOM   5255 C  C   . ASN C 1 122 ? 51.806  6.227   -42.287 1.00 14.82  ? 122 ASN C C   1 
ATOM   5256 O  O   . ASN C 1 122 ? 51.791  7.433   -42.569 1.00 16.39  ? 122 ASN C O   1 
ATOM   5257 C  CB  . ASN C 1 122 ? 49.833  5.916   -43.732 1.00 17.80  ? 122 ASN C CB  1 
ATOM   5258 C  CG  . ASN C 1 122 ? 50.577  5.599   -45.004 1.00 15.94  ? 122 ASN C CG  1 
ATOM   5259 O  OD1 . ASN C 1 122 ? 51.808  5.446   -44.970 1.00 15.69  ? 122 ASN C OD1 1 
ATOM   5260 N  ND2 . ASN C 1 122 ? 49.853  5.425   -46.103 1.00 21.96  ? 122 ASN C ND2 1 
ATOM   5261 N  N   . SER C 1 123 ? 52.863  5.574   -41.802 1.00 14.85  ? 123 SER C N   1 
ATOM   5262 C  CA  . SER C 1 123 ? 54.092  6.249   -41.441 1.00 16.27  ? 123 SER C CA  1 
ATOM   5263 C  C   . SER C 1 123 ? 54.982  6.491   -42.669 1.00 15.97  ? 123 SER C C   1 
ATOM   5264 O  O   . SER C 1 123 ? 55.945  7.247   -42.594 1.00 18.40  ? 123 SER C O   1 
ATOM   5265 C  CB  . SER C 1 123 ? 54.787  5.474   -40.336 1.00 18.06  ? 123 SER C CB  1 
ATOM   5266 O  OG  . SER C 1 123 ? 54.913  4.090   -40.671 1.00 16.43  ? 123 SER C OG  1 
ATOM   5267 N  N   . ASP C 1 124 ? 54.640  5.886   -43.810 1.00 17.02  ? 124 ASP C N   1 
ATOM   5268 C  CA  . ASP C 1 124 ? 55.357  6.161   -45.041 1.00 14.74  ? 124 ASP C CA  1 
ATOM   5269 C  C   . ASP C 1 124 ? 54.977  7.559   -45.549 1.00 16.53  ? 124 ASP C C   1 
ATOM   5270 O  O   . ASP C 1 124 ? 55.849  8.203   -46.133 1.00 22.12  ? 124 ASP C O   1 
ATOM   5271 C  CB  . ASP C 1 124 ? 55.100  5.076   -46.097 1.00 15.56  ? 124 ASP C CB  1 
ATOM   5272 C  CG  . ASP C 1 124 ? 55.750  3.734   -45.789 1.00 16.21  ? 124 ASP C CG  1 
ATOM   5273 O  OD1 . ASP C 1 124 ? 56.746  3.727   -45.041 1.00 19.17  ? 124 ASP C OD1 1 
ATOM   5274 O  OD2 . ASP C 1 124 ? 55.295  2.730   -46.363 1.00 16.55  ? 124 ASP C OD2 1 
ATOM   5275 N  N   . LEU C 1 125 ? 53.710  7.989   -45.343 1.00 16.09  ? 125 LEU C N   1 
ATOM   5276 C  CA  . LEU C 1 125 ? 53.167  9.253   -45.858 1.00 17.94  ? 125 LEU C CA  1 
ATOM   5277 C  C   . LEU C 1 125 ? 53.170  10.365  -44.797 1.00 18.17  ? 125 LEU C C   1 
ATOM   5278 O  O   . LEU C 1 125 ? 53.282  11.558  -45.152 1.00 23.32  ? 125 LEU C O   1 
ATOM   5279 C  CB  . LEU C 1 125 ? 51.726  9.003   -46.345 1.00 21.09  ? 125 LEU C CB  1 
ATOM   5280 C  CG  . LEU C 1 125 ? 51.504  8.603   -47.813 1.00 26.55  ? 125 LEU C CG  1 
ATOM   5281 C  CD1 . LEU C 1 125 ? 52.627  7.818   -48.446 1.00 31.77  ? 125 LEU C CD1 1 
ATOM   5282 C  CD2 . LEU C 1 125 ? 50.098  8.095   -48.093 1.00 21.28  ? 125 LEU C CD2 1 
ATOM   5283 N  N   . TYR C 1 126 ? 52.980  9.998   -43.513 1.00 18.44  ? 126 TYR C N   1 
ATOM   5284 C  CA  . TYR C 1 126 ? 52.715  11.001  -42.483 1.00 18.48  ? 126 TYR C CA  1 
ATOM   5285 C  C   . TYR C 1 126 ? 53.549  10.800  -41.236 1.00 19.23  ? 126 TYR C C   1 
ATOM   5286 O  O   . TYR C 1 126 ? 53.921  9.692   -40.931 1.00 19.50  ? 126 TYR C O   1 
ATOM   5287 C  CB  . TYR C 1 126 ? 51.236  10.925  -42.109 1.00 18.41  ? 126 TYR C CB  1 
ATOM   5288 C  CG  . TYR C 1 126 ? 50.335  10.943  -43.315 1.00 19.08  ? 126 TYR C CG  1 
ATOM   5289 C  CD1 . TYR C 1 126 ? 50.341  12.030  -44.176 1.00 21.36  ? 126 TYR C CD1 1 
ATOM   5290 C  CD2 . TYR C 1 126 ? 49.538  9.850   -43.630 1.00 20.53  ? 126 TYR C CD2 1 
ATOM   5291 C  CE1 . TYR C 1 126 ? 49.538  12.046  -45.297 1.00 17.03  ? 126 TYR C CE1 1 
ATOM   5292 C  CE2 . TYR C 1 126 ? 48.727  9.850   -44.758 1.00 19.18  ? 126 TYR C CE2 1 
ATOM   5293 C  CZ  . TYR C 1 126 ? 48.722  10.961  -45.579 1.00 20.58  ? 126 TYR C CZ  1 
ATOM   5294 O  OH  . TYR C 1 126 ? 47.952  11.039  -46.703 1.00 23.62  ? 126 TYR C OH  1 
ATOM   5295 N  N   . PRO C 1 127 ? 53.903  11.875  -40.494 1.00 22.12  ? 127 PRO C N   1 
ATOM   5296 C  CA  . PRO C 1 127 ? 54.747  11.726  -39.306 1.00 23.64  ? 127 PRO C CA  1 
ATOM   5297 C  C   . PRO C 1 127 ? 54.087  11.207  -38.029 1.00 24.22  ? 127 PRO C C   1 
ATOM   5298 O  O   . PRO C 1 127 ? 54.797  10.768  -37.122 1.00 27.39  ? 127 PRO C O   1 
ATOM   5299 C  CB  . PRO C 1 127 ? 55.335  13.129  -39.067 1.00 28.98  ? 127 PRO C CB  1 
ATOM   5300 C  CG  . PRO C 1 127 ? 54.354  14.084  -39.735 1.00 24.60  ? 127 PRO C CG  1 
ATOM   5301 C  CD  . PRO C 1 127 ? 53.657  13.295  -40.828 1.00 24.15  ? 127 PRO C CD  1 
ATOM   5302 N  N   . ASP C 1 128 ? 52.745  11.244  -37.953 1.00 25.47  ? 128 ASP C N   1 
ATOM   5303 C  CA  . ASP C 1 128 ? 52.049  10.845  -36.725 1.00 24.51  ? 128 ASP C CA  1 
ATOM   5304 C  C   . ASP C 1 128 ? 50.570  10.622  -37.043 1.00 21.56  ? 128 ASP C C   1 
ATOM   5305 O  O   . ASP C 1 128 ? 50.132  10.999  -38.127 1.00 22.51  ? 128 ASP C O   1 
ATOM   5306 C  CB  . ASP C 1 128 ? 52.305  11.808  -35.542 1.00 33.21  ? 128 ASP C CB  1 
ATOM   5307 C  CG  . ASP C 1 128 ? 52.099  13.274  -35.903 1.00 38.39  ? 128 ASP C CG  1 
ATOM   5308 O  OD1 . ASP C 1 128 ? 51.047  13.613  -36.491 1.00 29.60  ? 128 ASP C OD1 1 
ATOM   5309 O  OD2 . ASP C 1 128 ? 52.996  14.058  -35.638 1.00 46.52  ? 128 ASP C OD2 1 
ATOM   5310 N  N   . ALA C 1 129 ? 49.818  10.019  -36.091 1.00 23.76  ? 129 ALA C N   1 
ATOM   5311 C  CA  . ALA C 1 129 ? 48.442  9.627   -36.361 1.00 24.29  ? 129 ALA C CA  1 
ATOM   5312 C  C   . ALA C 1 129 ? 47.544  10.851  -36.518 1.00 21.20  ? 129 ALA C C   1 
ATOM   5313 O  O   . ALA C 1 129 ? 46.606  10.833  -37.300 1.00 24.52  ? 129 ALA C O   1 
ATOM   5314 C  CB  . ALA C 1 129 ? 47.901  8.691   -35.302 1.00 26.59  ? 129 ALA C CB  1 
ATOM   5315 N  N   . SER C 1 130 ? 47.806  11.894  -35.742 1.00 24.67  ? 130 SER C N   1 
ATOM   5316 C  CA  . SER C 1 130 ? 46.891  13.017  -35.823 1.00 30.35  ? 130 SER C CA  1 
ATOM   5317 C  C   . SER C 1 130 ? 46.990  13.630  -37.220 1.00 30.89  ? 130 SER C C   1 
ATOM   5318 O  O   . SER C 1 130 ? 45.953  13.810  -37.874 1.00 25.52  ? 130 SER C O   1 
ATOM   5319 C  CB  . SER C 1 130 ? 47.025  14.015  -34.679 1.00 41.64  ? 130 SER C CB  1 
ATOM   5320 O  OG  . SER C 1 130 ? 48.297  14.635  -34.674 1.00 45.47  ? 130 SER C OG  1 
ATOM   5321 N  N   . THR C 1 131 ? 48.223  13.842  -37.724 1.00 27.45  ? 131 THR C N   1 
ATOM   5322 C  CA  . THR C 1 131 ? 48.373  14.365  -39.080 1.00 23.25  ? 131 THR C CA  1 
ATOM   5323 C  C   . THR C 1 131 ? 47.772  13.390  -40.102 1.00 22.43  ? 131 THR C C   1 
ATOM   5324 O  O   . THR C 1 131 ? 47.152  13.822  -41.059 1.00 23.63  ? 131 THR C O   1 
ATOM   5325 C  CB  . THR C 1 131 ? 49.835  14.640  -39.478 1.00 22.57  ? 131 THR C CB  1 
ATOM   5326 O  OG1 . THR C 1 131 ? 50.575  15.466  -38.570 1.00 28.66  ? 131 THR C OG1 1 
ATOM   5327 C  CG2 . THR C 1 131 ? 49.950  15.303  -40.835 1.00 21.56  ? 131 THR C CG2 1 
ATOM   5328 N  N   . ALA C 1 132 ? 47.996  12.073  -39.933 1.00 21.12  ? 132 ALA C N   1 
ATOM   5329 C  CA  . ALA C 1 132 ? 47.440  11.081  -40.849 1.00 19.14  ? 132 ALA C CA  1 
ATOM   5330 C  C   . ALA C 1 132 ? 45.920  11.071  -40.827 1.00 19.16  ? 132 ALA C C   1 
ATOM   5331 O  O   . ALA C 1 132 ? 45.328  10.628  -41.819 1.00 21.50  ? 132 ALA C O   1 
ATOM   5332 C  CB  . ALA C 1 132 ? 47.924  9.657   -40.554 1.00 18.06  ? 132 ALA C CB  1 
ATOM   5333 N  N   . SER C 1 133 ? 45.314  11.516  -39.712 1.00 20.17  ? 133 SER C N   1 
ATOM   5334 C  CA  . SER C 1 133 ? 43.975  11.006  -39.402 1.00 19.69  ? 133 SER C CA  1 
ATOM   5335 C  C   . SER C 1 133 ? 42.940  11.585  -40.379 1.00 17.73  ? 133 SER C C   1 
ATOM   5336 O  O   . SER C 1 133 ? 41.852  11.062  -40.553 1.00 18.84  ? 133 SER C O   1 
ATOM   5337 C  CB  . SER C 1 133 ? 43.549  11.354  -37.958 1.00 21.32  ? 133 SER C CB  1 
ATOM   5338 O  OG  . SER C 1 133 ? 43.442  12.776  -37.804 1.00 22.12  ? 133 SER C OG  1 
ATOM   5339 N  N   . ASN C 1 134 ? 43.229  12.755  -40.936 1.00 21.79  ? 134 ASN C N   1 
ATOM   5340 C  CA  . ASN C 1 134 ? 42.210  13.396  -41.768 1.00 23.34  ? 134 ASN C CA  1 
ATOM   5341 C  C   . ASN C 1 134 ? 42.689  13.337  -43.216 1.00 25.33  ? 134 ASN C C   1 
ATOM   5342 O  O   . ASN C 1 134 ? 42.280  14.142  -44.045 1.00 29.24  ? 134 ASN C O   1 
ATOM   5343 C  CB  . ASN C 1 134 ? 41.827  14.820  -41.332 1.00 27.77  ? 134 ASN C CB  1 
ATOM   5344 C  CG  . ASN C 1 134 ? 42.965  15.811  -41.438 1.00 29.59  ? 134 ASN C CG  1 
ATOM   5345 O  OD1 . ASN C 1 134 ? 44.144  15.447  -41.567 1.00 30.01  ? 134 ASN C OD1 1 
ATOM   5346 N  ND2 . ASN C 1 134 ? 42.603  17.079  -41.386 1.00 31.74  ? 134 ASN C ND2 1 
ATOM   5347 N  N   . LYS C 1 135 ? 43.578  12.376  -43.501 1.00 24.02  ? 135 LYS C N   1 
ATOM   5348 C  CA  . LYS C 1 135 ? 44.249  12.360  -44.778 1.00 24.21  ? 135 LYS C CA  1 
ATOM   5349 C  C   . LYS C 1 135 ? 44.099  10.994  -45.436 1.00 20.44  ? 135 LYS C C   1 
ATOM   5350 O  O   . LYS C 1 135 ? 43.757  10.001  -44.786 1.00 21.14  ? 135 LYS C O   1 
ATOM   5351 C  CB  . LYS C 1 135 ? 45.725  12.789  -44.634 1.00 26.69  ? 135 LYS C CB  1 
ATOM   5352 C  CG  . LYS C 1 135 ? 45.929  14.227  -44.146 1.00 33.24  ? 135 LYS C CG  1 
ATOM   5353 C  CD  . LYS C 1 135 ? 47.328  14.802  -44.390 1.00 28.55  ? 135 LYS C CD  1 
ATOM   5354 C  CE  . LYS C 1 135 ? 47.638  16.081  -43.658 1.00 28.16  ? 135 LYS C CE  1 
ATOM   5355 N  NZ  . LYS C 1 135 ? 46.848  16.305  -42.424 1.00 34.21  ? 135 LYS C NZ  1 
ATOM   5356 N  N   . SER C 1 136 ? 44.222  10.986  -46.752 1.00 25.49  ? 136 SER C N   1 
ATOM   5357 C  CA  . SER C 1 136 ? 43.969  9.807   -47.560 1.00 23.39  ? 136 SER C CA  1 
ATOM   5358 C  C   . SER C 1 136 ? 44.846  8.666   -47.057 1.00 24.11  ? 136 SER C C   1 
ATOM   5359 O  O   . SER C 1 136 ? 46.060  8.827   -46.806 1.00 21.42  ? 136 SER C O   1 
ATOM   5360 C  CB  . SER C 1 136 ? 44.269  10.063  -49.013 1.00 35.25  ? 136 SER C CB  1 
ATOM   5361 O  OG  . SER C 1 136 ? 44.032  8.883   -49.773 1.00 38.63  ? 136 SER C OG  1 
ATOM   5362 N  N   . GLU C 1 137 ? 44.221  7.494   -47.013 1.00 22.18  ? 137 GLU C N   1 
ATOM   5363 C  CA  . GLU C 1 137 ? 44.897  6.272   -46.599 1.00 22.18  ? 137 GLU C CA  1 
ATOM   5364 C  C   . GLU C 1 137 ? 45.601  6.409   -45.247 1.00 21.20  ? 137 GLU C C   1 
ATOM   5365 O  O   . GLU C 1 137 ? 46.595  5.719   -44.965 1.00 23.17  ? 137 GLU C O   1 
ATOM   5366 C  CB  . GLU C 1 137 ? 45.849  5.803   -47.702 1.00 22.26  ? 137 GLU C CB  1 
ATOM   5367 C  CG  . GLU C 1 137 ? 45.065  5.377   -48.929 1.00 31.96  ? 137 GLU C CG  1 
ATOM   5368 N  N   . GLY C 1 138 ? 45.063  7.249   -44.367 1.00 14.82  ? 138 GLY C N   1 
ATOM   5369 C  CA  . GLY C 1 138 ? 45.835  7.663   -43.214 1.00 15.53  ? 138 GLY C CA  1 
ATOM   5370 C  C   . GLY C 1 138 ? 45.996  6.607   -42.117 1.00 13.55  ? 138 GLY C C   1 
ATOM   5371 O  O   . GLY C 1 138 ? 47.049  6.590   -41.457 1.00 16.02  ? 138 GLY C O   1 
ATOM   5372 N  N   . LEU C 1 139 ? 44.941  5.805   -41.860 1.00 11.48  ? 139 LEU C N   1 
ATOM   5373 C  CA  . LEU C 1 139 ? 44.900  5.002   -40.667 1.00 11.69  ? 139 LEU C CA  1 
ATOM   5374 C  C   . LEU C 1 139 ? 44.530  3.571   -41.031 1.00 11.27  ? 139 LEU C C   1 
ATOM   5375 O  O   . LEU C 1 139 ? 43.872  3.317   -42.033 1.00 12.50  ? 139 LEU C O   1 
ATOM   5376 C  CB  . LEU C 1 139 ? 43.890  5.513   -39.644 1.00 11.81  ? 139 LEU C CB  1 
ATOM   5377 C  CG  . LEU C 1 139 ? 44.090  6.945   -39.151 1.00 12.32  ? 139 LEU C CG  1 
ATOM   5378 C  CD1 . LEU C 1 139 ? 42.890  7.370   -38.336 1.00 14.31  ? 139 LEU C CD1 1 
ATOM   5379 C  CD2 . LEU C 1 139 ? 45.349  7.028   -38.318 1.00 17.23  ? 139 LEU C CD2 1 
ATOM   5380 N  N   . ALA C 1 140 ? 44.997  2.630   -40.187 1.00 11.56  ? 140 ALA C N   1 
ATOM   5381 C  CA  . ALA C 1 140 ? 44.600  1.230   -40.271 1.00 9.43   ? 140 ALA C CA  1 
ATOM   5382 C  C   . ALA C 1 140 ? 44.340  0.751   -38.853 1.00 9.67   ? 140 ALA C C   1 
ATOM   5383 O  O   . ALA C 1 140 ? 45.183  0.942   -37.972 1.00 11.74  ? 140 ALA C O   1 
ATOM   5384 C  CB  . ALA C 1 140 ? 45.700  0.459   -40.931 1.00 11.22  ? 140 ALA C CB  1 
ATOM   5385 N  N   . VAL C 1 141 ? 43.200  0.058   -38.641 1.00 10.07  ? 141 VAL C N   1 
ATOM   5386 C  CA  . VAL C 1 141 ? 42.909  -0.424  -37.307 1.00 9.65   ? 141 VAL C CA  1 
ATOM   5387 C  C   . VAL C 1 141 ? 42.799  -1.940  -37.362 1.00 8.05   ? 141 VAL C C   1 
ATOM   5388 O  O   . VAL C 1 141 ? 42.186  -2.481  -38.280 1.00 10.89  ? 141 VAL C O   1 
ATOM   5389 C  CB  . VAL C 1 141 ? 41.619  0.196   -36.728 1.00 8.24   ? 141 VAL C CB  1 
ATOM   5390 C  CG1 . VAL C 1 141 ? 41.256  -0.441  -35.370 1.00 13.35  ? 141 VAL C CG1 1 
ATOM   5391 C  CG2 . VAL C 1 141 ? 41.798  1.690   -36.624 1.00 11.15  ? 141 VAL C CG2 1 
ATOM   5392 N  N   . LEU C 1 142 ? 43.359  -2.606  -36.346 1.00 10.44  ? 142 LEU C N   1 
ATOM   5393 C  CA  . LEU C 1 142 ? 43.095  -4.032  -36.153 1.00 9.15   ? 142 LEU C CA  1 
ATOM   5394 C  C   . LEU C 1 142 ? 42.035  -4.116  -35.051 1.00 10.99  ? 142 LEU C C   1 
ATOM   5395 O  O   . LEU C 1 142 ? 42.208  -3.539  -33.951 1.00 11.56  ? 142 LEU C O   1 
ATOM   5396 C  CB  . LEU C 1 142 ? 44.355  -4.776  -35.664 1.00 13.31  ? 142 LEU C CB  1 
ATOM   5397 C  CG  . LEU C 1 142 ? 45.595  -4.652  -36.534 1.00 12.45  ? 142 LEU C CG  1 
ATOM   5398 C  CD1 . LEU C 1 142 ? 46.735  -5.453  -35.913 1.00 14.20  ? 142 LEU C CD1 1 
ATOM   5399 C  CD2 . LEU C 1 142 ? 45.270  -5.102  -37.964 1.00 13.51  ? 142 LEU C CD2 1 
ATOM   5400 N  N   . ALA C 1 143 ? 40.916  -4.750  -35.359 1.00 10.97  ? 143 ALA C N   1 
ATOM   5401 C  CA  . ALA C 1 143 ? 39.820  -4.984  -34.426 1.00 9.99   ? 143 ALA C CA  1 
ATOM   5402 C  C   . ALA C 1 143 ? 39.744  -6.434  -33.972 1.00 7.86   ? 143 ALA C C   1 
ATOM   5403 O  O   . ALA C 1 143 ? 39.676  -7.375  -34.778 1.00 11.66  ? 143 ALA C O   1 
ATOM   5404 C  CB  . ALA C 1 143 ? 38.506  -4.503  -35.022 1.00 11.40  ? 143 ALA C CB  1 
ATOM   5405 N  N   . VAL C 1 144 ? 39.644  -6.590  -32.656 1.00 10.19  ? 144 VAL C N   1 
ATOM   5406 C  CA  . VAL C 1 144 ? 39.492  -7.914  -32.088 1.00 9.61   ? 144 VAL C CA  1 
ATOM   5407 C  C   . VAL C 1 144 ? 38.164  -7.949  -31.317 1.00 12.34  ? 144 VAL C C   1 
ATOM   5408 O  O   . VAL C 1 144 ? 37.890  -7.133  -30.432 1.00 11.62  ? 144 VAL C O   1 
ATOM   5409 C  CB  . VAL C 1 144 ? 40.622  -8.223  -31.090 1.00 11.95  ? 144 VAL C CB  1 
ATOM   5410 C  CG1 . VAL C 1 144 ? 40.382  -9.622  -30.483 1.00 14.01  ? 144 VAL C CG1 1 
ATOM   5411 C  CG2 . VAL C 1 144 ? 41.980  -8.186  -31.756 1.00 13.84  ? 144 VAL C CG2 1 
ATOM   5412 N  N   . LEU C 1 145 ? 37.287  -8.871  -31.705 1.00 11.98  ? 145 LEU C N   1 
ATOM   5413 C  CA  . LEU C 1 145 ? 36.024  -9.096  -31.011 1.00 12.55  ? 145 LEU C CA  1 
ATOM   5414 C  C   . LEU C 1 145 ? 36.254  -9.922  -29.747 1.00 14.16  ? 145 LEU C C   1 
ATOM   5415 O  O   . LEU C 1 145 ? 37.045  -10.878 -29.774 1.00 15.65  ? 145 LEU C O   1 
ATOM   5416 C  CB  . LEU C 1 145 ? 35.041  -9.830  -31.936 1.00 13.80  ? 145 LEU C CB  1 
ATOM   5417 C  CG  . LEU C 1 145 ? 34.720  -9.067  -33.228 1.00 13.35  ? 145 LEU C CG  1 
ATOM   5418 C  CD1 . LEU C 1 145 ? 34.109  -10.097 -34.216 1.00 17.34  ? 145 LEU C CD1 1 
ATOM   5419 C  CD2 . LEU C 1 145 ? 33.817  -7.816  -32.972 1.00 16.38  ? 145 LEU C CD2 1 
ATOM   5420 N  N   . ILE C 1 146 ? 35.566  -9.540  -28.653 1.00 13.01  ? 146 ILE C N   1 
ATOM   5421 C  CA  . ILE C 1 146 ? 35.819  -10.138 -27.333 1.00 14.86  ? 146 ILE C CA  1 
ATOM   5422 C  C   . ILE C 1 146 ? 34.507  -10.708 -26.820 1.00 13.48  ? 146 ILE C C   1 
ATOM   5423 O  O   . ILE C 1 146 ? 33.501  -10.037 -26.807 1.00 15.20  ? 146 ILE C O   1 
ATOM   5424 C  CB  . ILE C 1 146 ? 36.368  -9.093  -26.334 1.00 14.33  ? 146 ILE C CB  1 
ATOM   5425 C  CG1 . ILE C 1 146 ? 37.680  -8.464  -26.813 1.00 14.96  ? 146 ILE C CG1 1 
ATOM   5426 C  CG2 . ILE C 1 146 ? 36.533  -9.719  -24.939 1.00 15.12  ? 146 ILE C CG2 1 
ATOM   5427 C  CD1 . ILE C 1 146 ? 38.025  -7.165  -26.083 1.00 15.78  ? 146 ILE C CD1 1 
ATOM   5428 N  N   . GLU C 1 147 ? 34.529  -12.007 -26.453 1.00 13.66  ? 147 GLU C N   1 
ATOM   5429 C  CA  . GLU C 1 147 ? 33.423  -12.655 -25.753 1.00 16.91  ? 147 GLU C CA  1 
ATOM   5430 C  C   . GLU C 1 147 ? 33.813  -13.176 -24.377 1.00 15.97  ? 147 GLU C C   1 
ATOM   5431 O  O   . GLU C 1 147 ? 34.974  -13.371 -24.078 1.00 19.84  ? 147 GLU C O   1 
ATOM   5432 C  CB  . GLU C 1 147 ? 32.808  -13.748 -26.609 1.00 19.02  ? 147 GLU C CB  1 
ATOM   5433 C  CG  . GLU C 1 147 ? 33.757  -14.900 -26.849 1.00 19.87  ? 147 GLU C CG  1 
ATOM   5434 C  CD  . GLU C 1 147 ? 33.222  -15.920 -27.841 1.00 23.08  ? 147 GLU C CD  1 
ATOM   5435 O  OE1 . GLU C 1 147 ? 32.288  -15.603 -28.595 1.00 23.40  ? 147 GLU C OE1 1 
ATOM   5436 O  OE2 . GLU C 1 147 ? 33.735  -17.018 -27.885 1.00 27.37  ? 147 GLU C OE2 1 
ATOM   5437 N  N   . MET C 1 148 ? 32.790  -13.546 -23.600 1.00 18.67  ? 148 MET C N   1 
ATOM   5438 C  CA  . MET C 1 148 ? 33.043  -14.046 -22.272 1.00 19.69  ? 148 MET C CA  1 
ATOM   5439 C  C   . MET C 1 148 ? 33.380  -15.539 -22.389 1.00 22.23  ? 148 MET C C   1 
ATOM   5440 O  O   . MET C 1 148 ? 32.734  -16.277 -23.121 1.00 25.36  ? 148 MET C O   1 
ATOM   5441 C  CB  . MET C 1 148 ? 31.773  -13.888 -21.415 1.00 25.80  ? 148 MET C CB  1 
ATOM   5442 C  CG  . MET C 1 148 ? 32.059  -14.192 -19.955 1.00 30.39  ? 148 MET C CG  1 
ATOM   5443 S  SD  . MET C 1 148 ? 31.841  -15.926 -19.589 1.00 33.96  ? 148 MET C SD  1 
ATOM   5444 N  N   . GLY C 1 149 ? 34.426  -15.967 -21.680 1.00 22.10  ? 149 GLY C N   1 
ATOM   5445 C  CA  . GLY C 1 149 ? 34.792  -17.382 -21.649 1.00 18.52  ? 149 GLY C CA  1 
ATOM   5446 C  C   . GLY C 1 149 ? 35.962  -17.594 -20.680 1.00 23.91  ? 149 GLY C C   1 
ATOM   5447 O  O   . GLY C 1 149 ? 35.910  -17.118 -19.544 1.00 23.45  ? 149 GLY C O   1 
ATOM   5448 N  N   . SER C 1 150 ? 37.017  -18.279 -21.165 1.00 25.36  ? 150 SER C N   1 
ATOM   5449 C  CA  . SER C 1 150 ? 38.242  -18.568 -20.432 1.00 25.88  ? 150 SER C CA  1 
ATOM   5450 C  C   . SER C 1 150 ? 38.888  -17.279 -19.939 1.00 21.78  ? 150 SER C C   1 
ATOM   5451 O  O   . SER C 1 150 ? 38.880  -16.260 -20.650 1.00 22.05  ? 150 SER C O   1 
ATOM   5452 C  CB  . SER C 1 150 ? 39.235  -19.284 -21.326 1.00 30.99  ? 150 SER C CB  1 
ATOM   5453 O  OG  . SER C 1 150 ? 39.070  -20.678 -21.193 1.00 43.05  ? 150 SER C OG  1 
ATOM   5454 N  N   . PHE C 1 151 ? 39.445  -17.350 -18.710 1.00 26.90  ? 151 PHE C N   1 
ATOM   5455 C  CA  . PHE C 1 151 ? 40.369  -16.330 -18.240 1.00 23.25  ? 151 PHE C CA  1 
ATOM   5456 C  C   . PHE C 1 151 ? 41.524  -16.143 -19.217 1.00 23.65  ? 151 PHE C C   1 
ATOM   5457 O  O   . PHE C 1 151 ? 42.103  -17.110 -19.687 1.00 26.49  ? 151 PHE C O   1 
ATOM   5458 C  CB  . PHE C 1 151 ? 40.974  -16.720 -16.895 1.00 22.76  ? 151 PHE C CB  1 
ATOM   5459 C  CG  . PHE C 1 151 ? 41.957  -15.719 -16.363 1.00 24.56  ? 151 PHE C CG  1 
ATOM   5460 C  CD1 . PHE C 1 151 ? 41.506  -14.532 -15.812 1.00 26.88  ? 151 PHE C CD1 1 
ATOM   5461 C  CD2 . PHE C 1 151 ? 43.317  -15.975 -16.401 1.00 26.65  ? 151 PHE C CD2 1 
ATOM   5462 C  CE1 . PHE C 1 151 ? 42.405  -13.602 -15.312 1.00 28.79  ? 151 PHE C CE1 1 
ATOM   5463 C  CE2 . PHE C 1 151 ? 44.217  -15.040 -15.917 1.00 29.26  ? 151 PHE C CE2 1 
ATOM   5464 C  CZ  . PHE C 1 151 ? 43.758  -13.858 -15.363 1.00 30.50  ? 151 PHE C CZ  1 
ATOM   5465 N  N   . ASN C 1 152 ? 41.839  -14.873 -19.514 1.00 23.09  ? 152 ASN C N   1 
ATOM   5466 C  CA  . ASN C 1 152 ? 42.850  -14.534 -20.492 1.00 23.88  ? 152 ASN C CA  1 
ATOM   5467 C  C   . ASN C 1 152 ? 44.024  -13.850 -19.793 1.00 27.17  ? 152 ASN C C   1 
ATOM   5468 O  O   . ASN C 1 152 ? 43.950  -12.652 -19.548 1.00 24.99  ? 152 ASN C O   1 
ATOM   5469 C  CB  . ASN C 1 152 ? 42.237  -13.584 -21.529 1.00 23.38  ? 152 ASN C CB  1 
ATOM   5470 C  CG  . ASN C 1 152 ? 43.144  -13.423 -22.722 1.00 23.55  ? 152 ASN C CG  1 
ATOM   5471 O  OD1 . ASN C 1 152 ? 44.302  -13.024 -22.579 1.00 24.59  ? 152 ASN C OD1 1 
ATOM   5472 N  ND2 . ASN C 1 152 ? 42.581  -13.616 -23.918 1.00 20.37  ? 152 ASN C ND2 1 
ATOM   5473 N  N   . PRO C 1 153 ? 45.153  -14.546 -19.501 1.00 29.20  ? 153 PRO C N   1 
ATOM   5474 C  CA  . PRO C 1 153 ? 46.318  -13.899 -18.886 1.00 28.87  ? 153 PRO C CA  1 
ATOM   5475 C  C   . PRO C 1 153 ? 46.833  -12.672 -19.641 1.00 30.21  ? 153 PRO C C   1 
ATOM   5476 O  O   . PRO C 1 153 ? 47.252  -11.676 -19.032 1.00 30.04  ? 153 PRO C O   1 
ATOM   5477 C  CB  . PRO C 1 153 ? 47.372  -15.021 -18.863 1.00 29.92  ? 153 PRO C CB  1 
ATOM   5478 C  CG  . PRO C 1 153 ? 46.567  -16.294 -18.805 1.00 29.63  ? 153 PRO C CG  1 
ATOM   5479 C  CD  . PRO C 1 153 ? 45.349  -15.999 -19.671 1.00 29.06  ? 153 PRO C CD  1 
ATOM   5480 N  N   . SER C 1 154 ? 46.797  -12.760 -20.975 1.00 23.46  ? 154 SER C N   1 
ATOM   5481 C  CA  . SER C 1 154 ? 47.383  -11.714 -21.764 1.00 23.42  ? 154 SER C CA  1 
ATOM   5482 C  C   . SER C 1 154 ? 46.574  -10.422 -21.624 1.00 22.52  ? 154 SER C C   1 
ATOM   5483 O  O   . SER C 1 154 ? 47.168  -9.344  -21.453 1.00 27.15  ? 154 SER C O   1 
ATOM   5484 C  CB  . SER C 1 154 ? 47.442  -12.178 -23.193 1.00 25.67  ? 154 SER C CB  1 
ATOM   5485 O  OG  . SER C 1 154 ? 48.391  -13.222 -23.343 1.00 30.00  ? 154 SER C OG  1 
ATOM   5486 N  N   . TYR C 1 155 ? 45.227  -10.529 -21.717 1.00 22.83  ? 155 TYR C N   1 
ATOM   5487 C  CA  . TYR C 1 155 ? 44.382  -9.370  -21.500 1.00 21.86  ? 155 TYR C CA  1 
ATOM   5488 C  C   . TYR C 1 155 ? 44.558  -8.834  -20.087 1.00 24.38  ? 155 TYR C C   1 
ATOM   5489 O  O   . TYR C 1 155 ? 44.425  -7.638  -19.840 1.00 26.42  ? 155 TYR C O   1 
ATOM   5490 C  CB  . TYR C 1 155 ? 42.896  -9.618  -21.847 1.00 19.86  ? 155 TYR C CB  1 
ATOM   5491 C  CG  . TYR C 1 155 ? 42.618  -9.404  -23.315 1.00 19.86  ? 155 TYR C CG  1 
ATOM   5492 C  CD1 . TYR C 1 155 ? 42.990  -10.345 -24.267 1.00 19.81  ? 155 TYR C CD1 1 
ATOM   5493 C  CD2 . TYR C 1 155 ? 42.098  -8.192  -23.779 1.00 21.60  ? 155 TYR C CD2 1 
ATOM   5494 C  CE1 . TYR C 1 155 ? 42.802  -10.113 -25.630 1.00 16.43  ? 155 TYR C CE1 1 
ATOM   5495 C  CE2 . TYR C 1 155 ? 41.900  -7.955  -25.136 1.00 17.42  ? 155 TYR C CE2 1 
ATOM   5496 C  CZ  . TYR C 1 155 ? 42.254  -8.911  -26.069 1.00 17.49  ? 155 TYR C CZ  1 
ATOM   5497 O  OH  . TYR C 1 155 ? 42.097  -8.678  -27.398 1.00 18.44  ? 155 TYR C OH  1 
ATOM   5498 N  N   . ASP C 1 156 ? 44.895  -9.719  -19.156 1.00 26.07  ? 156 ASP C N   1 
ATOM   5499 C  CA  . ASP C 1 156 ? 45.041  -9.276  -17.776 1.00 26.21  ? 156 ASP C CA  1 
ATOM   5500 C  C   . ASP C 1 156 ? 46.281  -8.382  -17.631 1.00 29.40  ? 156 ASP C C   1 
ATOM   5501 O  O   . ASP C 1 156 ? 46.332  -7.570  -16.696 1.00 32.92  ? 156 ASP C O   1 
ATOM   5502 C  CB  . ASP C 1 156 ? 44.908  -10.425 -16.787 1.00 28.85  ? 156 ASP C CB  1 
ATOM   5503 C  CG  . ASP C 1 156 ? 43.974  -10.049 -15.642 1.00 30.60  ? 156 ASP C CG  1 
ATOM   5504 O  OD1 . ASP C 1 156 ? 42.823  -9.568  -15.943 1.00 27.11  ? 156 ASP C OD1 1 
ATOM   5505 O  OD2 . ASP C 1 156 ? 44.403  -10.204 -14.469 1.00 32.43  ? 156 ASP C OD2 1 
ATOM   5506 N  N   . LYS C 1 157 ? 47.230  -8.478  -18.579 1.00 22.39  ? 157 LYS C N   1 
ATOM   5507 C  CA  . LYS C 1 157 ? 48.432  -7.659  -18.539 1.00 27.37  ? 157 LYS C CA  1 
ATOM   5508 C  C   . LYS C 1 157 ? 47.985  -6.211  -18.683 1.00 29.12  ? 157 LYS C C   1 
ATOM   5509 O  O   . LYS C 1 157 ? 48.694  -5.319  -18.210 1.00 31.23  ? 157 LYS C O   1 
ATOM   5510 C  CB  . LYS C 1 157 ? 49.463  -8.126  -19.579 1.00 28.09  ? 157 LYS C CB  1 
ATOM   5511 C  CG  . LYS C 1 157 ? 50.064  -9.501  -19.265 1.00 29.26  ? 157 LYS C CG  1 
ATOM   5512 C  CD  . LYS C 1 157 ? 50.942  -10.069 -20.360 1.00 27.08  ? 157 LYS C CD  1 
ATOM   5513 C  CE  . LYS C 1 157 ? 51.365  -11.503 -20.114 1.00 29.63  ? 157 LYS C CE  1 
ATOM   5514 N  NZ  . LYS C 1 157 ? 52.217  -12.020 -21.210 1.00 31.34  ? 157 LYS C NZ  1 
ATOM   5515 N  N   . ILE C 1 158 ? 46.783  -6.005  -19.268 1.00 26.52  ? 158 ILE C N   1 
ATOM   5516 C  CA  . ILE C 1 158 ? 46.199  -4.675  -19.349 1.00 24.66  ? 158 ILE C CA  1 
ATOM   5517 C  C   . ILE C 1 158 ? 45.257  -4.403  -18.178 1.00 25.10  ? 158 ILE C C   1 
ATOM   5518 O  O   . ILE C 1 158 ? 45.335  -3.372  -17.511 1.00 25.68  ? 158 ILE C O   1 
ATOM   5519 C  CB  . ILE C 1 158 ? 45.479  -4.411  -20.692 1.00 28.59  ? 158 ILE C CB  1 
ATOM   5520 C  CG1 . ILE C 1 158 ? 46.452  -4.501  -21.877 1.00 32.47  ? 158 ILE C CG1 1 
ATOM   5521 C  CG2 . ILE C 1 158 ? 44.813  -3.053  -20.606 1.00 23.54  ? 158 ILE C CG2 1 
ATOM   5522 C  CD1 . ILE C 1 158 ? 45.809  -4.385  -23.236 1.00 29.76  ? 158 ILE C CD1 1 
ATOM   5523 N  N   . PHE C 1 159 ? 44.315  -5.306  -17.962 1.00 28.73  ? 159 PHE C N   1 
ATOM   5524 C  CA  . PHE C 1 159 ? 43.206  -5.002  -17.063 1.00 28.94  ? 159 PHE C CA  1 
ATOM   5525 C  C   . PHE C 1 159 ? 43.647  -4.884  -15.595 1.00 30.12  ? 159 PHE C C   1 
ATOM   5526 O  O   . PHE C 1 159 ? 42.943  -4.283  -14.767 1.00 31.45  ? 159 PHE C O   1 
ATOM   5527 C  CB  . PHE C 1 159 ? 42.124  -6.083  -17.112 1.00 27.43  ? 159 PHE C CB  1 
ATOM   5528 C  CG  . PHE C 1 159 ? 41.449  -6.317  -18.450 1.00 25.18  ? 159 PHE C CG  1 
ATOM   5529 C  CD1 . PHE C 1 159 ? 41.310  -5.310  -19.406 1.00 22.35  ? 159 PHE C CD1 1 
ATOM   5530 C  CD2 . PHE C 1 159 ? 40.874  -7.555  -18.751 1.00 22.07  ? 159 PHE C CD2 1 
ATOM   5531 C  CE1 . PHE C 1 159 ? 40.655  -5.554  -20.615 1.00 25.30  ? 159 PHE C CE1 1 
ATOM   5532 C  CE2 . PHE C 1 159 ? 40.199  -7.795  -19.947 1.00 24.81  ? 159 PHE C CE2 1 
ATOM   5533 C  CZ  . PHE C 1 159 ? 40.093  -6.791  -20.896 1.00 22.87  ? 159 PHE C CZ  1 
ATOM   5534 N  N   . SER C 1 160 ? 44.786  -5.512  -15.256 1.00 31.95  ? 160 SER C N   1 
ATOM   5535 C  CA  . SER C 1 160 ? 45.298  -5.519  -13.895 1.00 30.90  ? 160 SER C CA  1 
ATOM   5536 C  C   . SER C 1 160 ? 45.724  -4.112  -13.484 1.00 34.84  ? 160 SER C C   1 
ATOM   5537 O  O   . SER C 1 160 ? 46.029  -3.883  -12.317 1.00 32.91  ? 160 SER C O   1 
ATOM   5538 C  CB  . SER C 1 160 ? 46.420  -6.520  -13.752 1.00 33.66  ? 160 SER C CB  1 
ATOM   5539 O  OG  . SER C 1 160 ? 47.588  -6.111  -14.478 1.00 33.40  ? 160 SER C OG  1 
ATOM   5540 N  N   . HIS C 1 161 ? 45.724  -3.184  -14.460 1.00 32.30  ? 161 HIS C N   1 
ATOM   5541 C  CA  . HIS C 1 161 ? 46.102  -1.804  -14.228 1.00 29.82  ? 161 HIS C CA  1 
ATOM   5542 C  C   . HIS C 1 161 ? 44.919  -0.829  -14.222 1.00 31.73  ? 161 HIS C C   1 
ATOM   5543 O  O   . HIS C 1 161 ? 45.109  0.351   -13.949 1.00 36.75  ? 161 HIS C O   1 
ATOM   5544 C  CB  . HIS C 1 161 ? 47.192  -1.362  -15.225 1.00 33.11  ? 161 HIS C CB  1 
ATOM   5545 C  CG  . HIS C 1 161 ? 48.486  -2.105  -15.113 1.00 27.88  ? 161 HIS C CG  1 
ATOM   5546 N  ND1 . HIS C 1 161 ? 49.503  -1.721  -14.252 1.00 27.80  ? 161 HIS C ND1 1 
ATOM   5547 C  CD2 . HIS C 1 161 ? 48.926  -3.212  -15.737 1.00 31.41  ? 161 HIS C CD2 1 
ATOM   5548 C  CE1 . HIS C 1 161 ? 50.515  -2.556  -14.371 1.00 28.40  ? 161 HIS C CE1 1 
ATOM   5549 N  NE2 . HIS C 1 161 ? 50.180  -3.480  -15.282 1.00 33.62  ? 161 HIS C NE2 1 
ATOM   5550 N  N   . LEU C 1 162 ? 43.690  -1.276  -14.505 1.00 34.60  ? 162 LEU C N   1 
ATOM   5551 C  CA  . LEU C 1 162 ? 42.577  -0.339  -14.689 1.00 41.63  ? 162 LEU C CA  1 
ATOM   5552 C  C   . LEU C 1 162 ? 42.288  0.517   -13.449 1.00 45.22  ? 162 LEU C C   1 
ATOM   5553 O  O   . LEU C 1 162 ? 41.842  1.651   -13.557 1.00 43.58  ? 162 LEU C O   1 
ATOM   5554 C  CB  . LEU C 1 162 ? 41.316  -1.070  -15.170 1.00 40.92  ? 162 LEU C CB  1 
ATOM   5555 C  CG  . LEU C 1 162 ? 41.439  -1.770  -16.523 1.00 43.99  ? 162 LEU C CG  1 
ATOM   5556 C  CD1 . LEU C 1 162 ? 40.168  -2.503  -16.863 1.00 38.64  ? 162 LEU C CD1 1 
ATOM   5557 C  CD2 . LEU C 1 162 ? 41.800  -0.796  -17.639 1.00 43.64  ? 162 LEU C CD2 1 
ATOM   5558 N  N   . GLN C 1 163 ? 42.560  -0.014  -12.255 1.00 44.52  ? 163 GLN C N   1 
ATOM   5559 C  CA  . GLN C 1 163 ? 42.323  0.658   -10.985 1.00 42.46  ? 163 GLN C CA  1 
ATOM   5560 C  C   . GLN C 1 163 ? 43.128  1.958   -10.873 1.00 40.72  ? 163 GLN C C   1 
ATOM   5561 O  O   . GLN C 1 163 ? 42.691  2.925   -10.236 1.00 38.67  ? 163 GLN C O   1 
ATOM   5562 C  CB  . GLN C 1 163 ? 42.729  -0.364  -9.927  1.00 52.23  ? 163 GLN C CB  1 
ATOM   5563 C  CG  . GLN C 1 163 ? 43.602  -1.469  -10.527 1.00 49.55  ? 163 GLN C CG  1 
ATOM   5564 C  CD  . GLN C 1 163 ? 43.958  -2.585  -9.571  1.00 52.88  ? 163 GLN C CD  1 
ATOM   5565 O  OE1 . GLN C 1 163 ? 43.622  -3.753  -9.779  1.00 57.84  ? 163 GLN C OE1 1 
ATOM   5566 N  NE2 . GLN C 1 163 ? 44.667  -2.236  -8.507  1.00 48.47  ? 163 GLN C NE2 1 
ATOM   5567 N  N   . HIS C 1 164 ? 44.288  1.990   -11.549 1.00 36.14  ? 164 HIS C N   1 
ATOM   5568 C  CA  . HIS C 1 164 ? 45.203  3.129   -11.510 1.00 36.46  ? 164 HIS C CA  1 
ATOM   5569 C  C   . HIS C 1 164 ? 44.789  4.228   -12.483 1.00 35.99  ? 164 HIS C C   1 
ATOM   5570 O  O   . HIS C 1 164 ? 45.334  5.329   -12.428 1.00 41.00  ? 164 HIS C O   1 
ATOM   5571 C  CB  . HIS C 1 164 ? 46.662  2.681   -11.660 1.00 33.59  ? 164 HIS C CB  1 
ATOM   5572 C  CG  . HIS C 1 164 ? 47.035  1.494   -10.829 1.00 32.90  ? 164 HIS C CG  1 
ATOM   5573 N  ND1 . HIS C 1 164 ? 46.741  1.391   -9.483  1.00 41.92  ? 164 HIS C ND1 1 
ATOM   5574 C  CD2 . HIS C 1 164 ? 47.706  0.365   -11.159 1.00 40.26  ? 164 HIS C CD2 1 
ATOM   5575 C  CE1 . HIS C 1 164 ? 47.194  0.239   -9.025  1.00 48.42  ? 164 HIS C CE1 1 
ATOM   5576 N  NE2 . HIS C 1 164 ? 47.797  -0.414  -10.035 1.00 45.21  ? 164 HIS C NE2 1 
ATOM   5577 N  N   . VAL C 1 165 ? 43.809  3.931   -13.359 1.00 41.78  ? 165 VAL C N   1 
ATOM   5578 C  CA  . VAL C 1 165 ? 43.401  4.860   -14.410 1.00 35.37  ? 165 VAL C CA  1 
ATOM   5579 C  C   . VAL C 1 165 ? 41.888  5.058   -14.352 1.00 31.14  ? 165 VAL C C   1 
ATOM   5580 O  O   . VAL C 1 165 ? 41.229  5.485   -15.318 1.00 31.99  ? 165 VAL C O   1 
ATOM   5581 C  CB  . VAL C 1 165 ? 43.956  4.449   -15.793 1.00 31.99  ? 165 VAL C CB  1 
ATOM   5582 C  CG1 . VAL C 1 165 ? 45.476  4.454   -15.786 1.00 33.45  ? 165 VAL C CG1 1 
ATOM   5583 C  CG2 . VAL C 1 165 ? 43.434  3.096   -16.277 1.00 30.93  ? 165 VAL C CG2 1 
ATOM   5584 N  N   . LYS C 1 166 ? 41.387  4.828   -13.131 1.00 36.25  ? 166 LYS C N   1 
ATOM   5585 C  CA  . LYS C 1 166 ? 39.971  4.688   -12.823 1.00 37.84  ? 166 LYS C CA  1 
ATOM   5586 C  C   . LYS C 1 166 ? 39.239  5.946   -13.265 1.00 29.71  ? 166 LYS C C   1 
ATOM   5587 O  O   . LYS C 1 166 ? 38.151  5.850   -13.849 1.00 36.09  ? 166 LYS C O   1 
ATOM   5588 C  CB  . LYS C 1 166 ? 39.764  4.427   -11.322 1.00 42.72  ? 166 LYS C CB  1 
ATOM   5589 C  CG  . LYS C 1 166 ? 38.728  3.366   -10.982 1.00 52.58  ? 166 LYS C CG  1 
ATOM   5590 C  CD  . LYS C 1 166 ? 38.437  3.167   -9.506  1.00 60.77  ? 166 LYS C CD  1 
ATOM   5591 C  CE  . LYS C 1 166 ? 36.976  2.869   -9.242  1.00 76.39  ? 166 LYS C CE  1 
ATOM   5592 N  NZ  . LYS C 1 166 ? 36.499  1.679   -9.989  1.00 66.03  ? 166 LYS C NZ  1 
ATOM   5593 N  N   . TYR C 1 167 ? 39.893  7.095   -13.060 1.00 29.80  ? 167 TYR C N   1 
ATOM   5594 C  CA  . TYR C 1 167 ? 39.263  8.375   -13.367 1.00 25.98  ? 167 TYR C CA  1 
ATOM   5595 C  C   . TYR C 1 167 ? 40.026  9.076   -14.497 1.00 27.09  ? 167 TYR C C   1 
ATOM   5596 O  O   . TYR C 1 167 ? 41.132  8.677   -14.843 1.00 29.78  ? 167 TYR C O   1 
ATOM   5597 C  CB  . TYR C 1 167 ? 39.243  9.253   -12.117 1.00 32.28  ? 167 TYR C CB  1 
ATOM   5598 C  CG  . TYR C 1 167 ? 38.417  8.655   -11.015 1.00 38.48  ? 167 TYR C CG  1 
ATOM   5599 C  CD1 . TYR C 1 167 ? 37.036  8.732   -11.062 1.00 43.66  ? 167 TYR C CD1 1 
ATOM   5600 C  CD2 . TYR C 1 167 ? 39.008  7.938   -9.985  1.00 37.67  ? 167 TYR C CD2 1 
ATOM   5601 C  CE1 . TYR C 1 167 ? 36.262  8.164   -10.064 1.00 50.08  ? 167 TYR C CE1 1 
ATOM   5602 C  CE2 . TYR C 1 167 ? 38.251  7.364   -8.978  1.00 44.10  ? 167 TYR C CE2 1 
ATOM   5603 C  CZ  . TYR C 1 167 ? 36.872  7.489   -9.018  1.00 47.35  ? 167 TYR C CZ  1 
ATOM   5604 O  OH  . TYR C 1 167 ? 36.100  6.931   -8.042  1.00 50.90  ? 167 TYR C OH  1 
ATOM   5605 N  N   . LYS C 1 168 ? 39.446  10.159  -15.020 1.00 23.75  ? 168 LYS C N   1 
ATOM   5606 C  CA  . LYS C 1 168 ? 39.906  10.823  -16.217 1.00 26.47  ? 168 LYS C CA  1 
ATOM   5607 C  C   . LYS C 1 168 ? 41.152  11.654  -15.906 1.00 40.87  ? 168 LYS C C   1 
ATOM   5608 O  O   . LYS C 1 168 ? 41.252  12.257  -14.840 1.00 41.79  ? 168 LYS C O   1 
ATOM   5609 C  CB  . LYS C 1 168 ? 38.777  11.750  -16.675 1.00 25.76  ? 168 LYS C CB  1 
ATOM   5610 C  CG  . LYS C 1 168 ? 38.981  12.327  -18.069 1.00 40.30  ? 168 LYS C CG  1 
ATOM   5611 C  CD  . LYS C 1 168 ? 38.094  13.512  -18.407 1.00 31.62  ? 168 LYS C CD  1 
ATOM   5612 C  CE  . LYS C 1 168 ? 38.583  14.238  -19.640 1.00 40.10  ? 168 LYS C CE  1 
ATOM   5613 N  NZ  . LYS C 1 168 ? 37.549  15.152  -20.189 1.00 55.29  ? 168 LYS C NZ  1 
ATOM   5614 N  N   . GLY C 1 169 ? 42.106  11.674  -16.843 1.00 42.87  ? 169 GLY C N   1 
ATOM   5615 C  CA  . GLY C 1 169 ? 43.354  12.391  -16.650 1.00 44.32  ? 169 GLY C CA  1 
ATOM   5616 C  C   . GLY C 1 169 ? 44.428  11.491  -16.041 1.00 43.49  ? 169 GLY C C   1 
ATOM   5617 O  O   . GLY C 1 169 ? 45.603  11.841  -16.036 1.00 59.55  ? 169 GLY C O   1 
ATOM   5618 N  N   . GLN C 1 170 ? 44.018  10.300  -15.591 1.00 39.21  ? 170 GLN C N   1 
ATOM   5619 C  CA  . GLN C 1 170 ? 44.900  9.429   -14.829 1.00 39.17  ? 170 GLN C CA  1 
ATOM   5620 C  C   . GLN C 1 170 ? 45.692  8.531   -15.783 1.00 33.61  ? 170 GLN C C   1 
ATOM   5621 O  O   . GLN C 1 170 ? 45.162  8.131   -16.826 1.00 28.79  ? 170 GLN C O   1 
ATOM   5622 C  CB  . GLN C 1 170 ? 44.079  8.652   -13.792 1.00 56.03  ? 170 GLN C CB  1 
ATOM   5623 C  CG  . GLN C 1 170 ? 43.301  9.550   -12.830 1.00 48.75  ? 170 GLN C CG  1 
ATOM   5624 C  CD  . GLN C 1 170 ? 42.841  8.835   -11.582 1.00 61.63  ? 170 GLN C CD  1 
ATOM   5625 O  OE1 . GLN C 1 170 ? 42.464  7.670   -11.596 1.00 50.47  ? 170 GLN C OE1 1 
ATOM   5626 N  NE2 . GLN C 1 170 ? 42.887  9.537   -10.460 1.00 58.29  ? 170 GLN C NE2 1 
ATOM   5627 N  N   . GLU C 1 171 ? 46.923  8.163   -15.359 1.00 35.38  ? 171 GLU C N   1 
ATOM   5628 C  CA  . GLU C 1 171 ? 47.988  7.528   -16.148 1.00 27.47  ? 171 GLU C CA  1 
ATOM   5629 C  C   . GLU C 1 171 ? 48.711  6.427   -15.360 1.00 27.08  ? 171 GLU C C   1 
ATOM   5630 O  O   . GLU C 1 171 ? 48.824  6.463   -14.121 1.00 38.17  ? 171 GLU C O   1 
ATOM   5631 C  CB  . GLU C 1 171 ? 48.981  8.580   -16.681 1.00 35.20  ? 171 GLU C CB  1 
ATOM   5632 C  CG  . GLU C 1 171 ? 48.349  9.825   -17.324 1.00 36.49  ? 171 GLU C CG  1 
ATOM   5633 C  CD  . GLU C 1 171 ? 49.266  10.868  -17.975 1.00 42.91  ? 171 GLU C CD  1 
ATOM   5634 O  OE1 . GLU C 1 171 ? 50.493  10.629  -18.063 1.00 42.38  ? 171 GLU C OE1 1 
ATOM   5635 O  OE2 . GLU C 1 171 ? 48.760  11.959  -18.371 1.00 46.92  ? 171 GLU C OE2 1 
ATOM   5636 N  N   . ALA C 1 172 ? 49.223  5.412   -16.061 1.00 27.07  ? 172 ALA C N   1 
ATOM   5637 C  CA  . ALA C 1 172 ? 50.025  4.395   -15.405 1.00 28.22  ? 172 ALA C CA  1 
ATOM   5638 C  C   . ALA C 1 172 ? 50.884  3.650   -16.415 1.00 26.13  ? 172 ALA C C   1 
ATOM   5639 O  O   . ALA C 1 172 ? 50.537  3.552   -17.583 1.00 29.35  ? 172 ALA C O   1 
ATOM   5640 C  CB  . ALA C 1 172 ? 49.147  3.408   -14.664 1.00 29.94  ? 172 ALA C CB  1 
ATOM   5641 N  N   . PHE C 1 173 ? 51.929  2.996   -15.930 1.00 30.84  ? 173 PHE C N   1 
ATOM   5642 C  CA  . PHE C 1 173 ? 52.879  2.355   -16.825 1.00 26.55  ? 173 PHE C CA  1 
ATOM   5643 C  C   . PHE C 1 173 ? 52.658  0.836   -16.854 1.00 26.27  ? 173 PHE C C   1 
ATOM   5644 O  O   . PHE C 1 173 ? 52.433  0.218   -15.824 1.00 28.13  ? 173 PHE C O   1 
ATOM   5645 C  CB  . PHE C 1 173 ? 54.306  2.802   -16.505 1.00 25.86  ? 173 PHE C CB  1 
ATOM   5646 C  CG  . PHE C 1 173 ? 54.687  4.185   -16.992 1.00 30.06  ? 173 PHE C CG  1 
ATOM   5647 C  CD1 . PHE C 1 173 ? 54.903  4.438   -18.343 1.00 25.93  ? 173 PHE C CD1 1 
ATOM   5648 C  CD2 . PHE C 1 173 ? 54.898  5.222   -16.080 1.00 30.29  ? 173 PHE C CD2 1 
ATOM   5649 C  CE1 . PHE C 1 173 ? 55.266  5.710   -18.774 1.00 33.65  ? 173 PHE C CE1 1 
ATOM   5650 C  CE2 . PHE C 1 173 ? 55.269  6.490   -16.512 1.00 38.55  ? 173 PHE C CE2 1 
ATOM   5651 C  CZ  . PHE C 1 173 ? 55.452  6.732   -17.860 1.00 33.11  ? 173 PHE C CZ  1 
ATOM   5652 N  N   . VAL C 1 174 ? 52.729  0.248   -18.059 1.00 21.28  ? 174 VAL C N   1 
ATOM   5653 C  CA  . VAL C 1 174 ? 52.516  -1.175  -18.205 1.00 20.30  ? 174 VAL C CA  1 
ATOM   5654 C  C   . VAL C 1 174 ? 53.786  -1.758  -18.825 1.00 25.01  ? 174 VAL C C   1 
ATOM   5655 O  O   . VAL C 1 174 ? 54.238  -1.262  -19.854 1.00 32.69  ? 174 VAL C O   1 
ATOM   5656 C  CB  . VAL C 1 174 ? 51.296  -1.386  -19.122 1.00 26.43  ? 174 VAL C CB  1 
ATOM   5657 C  CG1 . VAL C 1 174 ? 51.071  -2.862  -19.385 1.00 29.18  ? 174 VAL C CG1 1 
ATOM   5658 C  CG2 . VAL C 1 174 ? 50.028  -0.689  -18.589 1.00 24.09  ? 174 VAL C CG2 1 
ATOM   5659 N  N   . PRO C 1 175 ? 54.491  -2.712  -18.187 1.00 24.16  ? 175 PRO C N   1 
ATOM   5660 C  CA  . PRO C 1 175 ? 55.709  -3.272  -18.777 1.00 24.56  ? 175 PRO C CA  1 
ATOM   5661 C  C   . PRO C 1 175 ? 55.403  -3.923  -20.124 1.00 28.09  ? 175 PRO C C   1 
ATOM   5662 O  O   . PRO C 1 175 ? 54.340  -4.500  -20.294 1.00 30.76  ? 175 PRO C O   1 
ATOM   5663 C  CB  . PRO C 1 175 ? 56.122  -4.390  -17.808 1.00 23.10  ? 175 PRO C CB  1 
ATOM   5664 C  CG  . PRO C 1 175 ? 55.451  -4.023  -16.508 1.00 27.32  ? 175 PRO C CG  1 
ATOM   5665 C  CD  . PRO C 1 175 ? 54.169  -3.309  -16.878 1.00 25.68  ? 175 PRO C CD  1 
ATOM   5666 N  N   . GLY C 1 176 ? 56.340  -3.833  -21.073 1.00 28.23  ? 176 GLY C N   1 
ATOM   5667 C  CA  . GLY C 1 176 ? 56.184  -4.477  -22.364 1.00 21.73  ? 176 GLY C CA  1 
ATOM   5668 C  C   . GLY C 1 176 ? 55.774  -5.943  -22.245 1.00 20.87  ? 176 GLY C C   1 
ATOM   5669 O  O   . GLY C 1 176 ? 56.243  -6.687  -21.383 1.00 25.55  ? 176 GLY C O   1 
ATOM   5670 N  N   . PHE C 1 177 ? 54.858  -6.339  -23.123 1.00 26.16  ? 177 PHE C N   1 
ATOM   5671 C  CA  . PHE C 1 177 ? 54.573  -7.742  -23.366 1.00 23.76  ? 177 PHE C CA  1 
ATOM   5672 C  C   . PHE C 1 177 ? 54.234  -7.877  -24.842 1.00 22.89  ? 177 PHE C C   1 
ATOM   5673 O  O   . PHE C 1 177 ? 54.289  -6.906  -25.596 1.00 27.21  ? 177 PHE C O   1 
ATOM   5674 C  CB  . PHE C 1 177 ? 53.421  -8.255  -22.505 1.00 23.57  ? 177 PHE C CB  1 
ATOM   5675 C  CG  . PHE C 1 177 ? 52.069  -7.628  -22.801 1.00 24.13  ? 177 PHE C CG  1 
ATOM   5676 C  CD1 . PHE C 1 177 ? 51.752  -6.367  -22.297 1.00 22.91  ? 177 PHE C CD1 1 
ATOM   5677 C  CD2 . PHE C 1 177 ? 51.113  -8.285  -23.573 1.00 24.85  ? 177 PHE C CD2 1 
ATOM   5678 C  CE1 . PHE C 1 177 ? 50.506  -5.789  -22.535 1.00 30.70  ? 177 PHE C CE1 1 
ATOM   5679 C  CE2 . PHE C 1 177 ? 49.876  -7.700  -23.817 1.00 27.97  ? 177 PHE C CE2 1 
ATOM   5680 C  CZ  . PHE C 1 177 ? 49.566  -6.458  -23.290 1.00 27.64  ? 177 PHE C CZ  1 
ATOM   5681 N  N   . ASN C 1 178 ? 54.029  -9.120  -25.262 1.00 24.16  ? 178 ASN C N   1 
ATOM   5682 C  CA  . ASN C 1 178 ? 53.887  -9.409  -26.658 1.00 22.66  ? 178 ASN C CA  1 
ATOM   5683 C  C   . ASN C 1 178 ? 52.437  -9.064  -27.048 1.00 23.74  ? 178 ASN C C   1 
ATOM   5684 O  O   . ASN C 1 178 ? 51.532  -9.812  -26.718 1.00 23.73  ? 178 ASN C O   1 
ATOM   5685 C  CB  . ASN C 1 178 ? 54.269  -10.866 -26.922 1.00 25.33  ? 178 ASN C CB  1 
ATOM   5686 C  CG  . ASN C 1 178 ? 54.120  -11.183 -28.393 1.00 19.76  ? 178 ASN C CG  1 
ATOM   5687 O  OD1 . ASN C 1 178 ? 53.813  -10.273 -29.169 1.00 28.27  ? 178 ASN C OD1 1 
ATOM   5688 N  ND2 . ASN C 1 178 ? 54.246  -12.446 -28.761 1.00 24.79  ? 178 ASN C ND2 1 
ATOM   5689 N  N   . ILE C 1 179 ? 52.197  -7.902  -27.696 1.00 23.22  ? 179 ILE C N   1 
ATOM   5690 C  CA  . ILE C 1 179 ? 50.860  -7.418  -28.020 1.00 22.75  ? 179 ILE C CA  1 
ATOM   5691 C  C   . ILE C 1 179 ? 50.164  -8.435  -28.919 1.00 19.30  ? 179 ILE C C   1 
ATOM   5692 O  O   . ILE C 1 179 ? 48.927  -8.434  -29.017 1.00 18.93  ? 179 ILE C O   1 
ATOM   5693 C  CB  . ILE C 1 179 ? 50.909  -5.994  -28.648 1.00 21.03  ? 179 ILE C CB  1 
ATOM   5694 C  CG1 . ILE C 1 179 ? 51.544  -4.948  -27.729 1.00 24.04  ? 179 ILE C CG1 1 
ATOM   5695 C  CG2 . ILE C 1 179 ? 49.531  -5.515  -29.108 1.00 21.05  ? 179 ILE C CG2 1 
ATOM   5696 C  CD1 . ILE C 1 179 ? 50.845  -4.723  -26.410 1.00 26.95  ? 179 ILE C CD1 1 
ATOM   5697 N  N   . GLU C 1 180 ? 50.939  -9.249  -29.633 1.00 21.52  ? 180 GLU C N   1 
ATOM   5698 C  CA  . GLU C 1 180 ? 50.338  -10.242 -30.511 1.00 23.02  ? 180 GLU C CA  1 
ATOM   5699 C  C   . GLU C 1 180 ? 49.530  -11.225 -29.667 1.00 22.11  ? 180 GLU C C   1 
ATOM   5700 O  O   . GLU C 1 180 ? 48.633  -11.884 -30.196 1.00 21.99  ? 180 GLU C O   1 
ATOM   5701 C  CB  . GLU C 1 180 ? 51.410  -10.954 -31.332 1.00 26.11  ? 180 GLU C CB  1 
ATOM   5702 C  CG  . GLU C 1 180 ? 50.862  -11.834 -32.436 1.00 27.00  ? 180 GLU C CG  1 
ATOM   5703 C  CD  . GLU C 1 180 ? 51.849  -12.298 -33.487 1.00 26.03  ? 180 GLU C CD  1 
ATOM   5704 O  OE1 . GLU C 1 180 ? 53.055  -12.044 -33.357 1.00 29.42  ? 180 GLU C OE1 1 
ATOM   5705 O  OE2 . GLU C 1 180 ? 51.393  -12.916 -34.440 1.00 31.34  ? 180 GLU C OE2 1 
ATOM   5706 N  N   . GLU C 1 181 ? 49.786  -11.248 -28.343 1.00 22.69  ? 181 GLU C N   1 
ATOM   5707 C  CA  . GLU C 1 181 ? 49.053  -12.179 -27.506 1.00 22.81  ? 181 GLU C CA  1 
ATOM   5708 C  C   . GLU C 1 181 ? 47.588  -11.719 -27.374 1.00 20.32  ? 181 GLU C C   1 
ATOM   5709 O  O   . GLU C 1 181 ? 46.756  -12.552 -26.976 1.00 22.21  ? 181 GLU C O   1 
ATOM   5710 C  CB  . GLU C 1 181 ? 49.676  -12.313 -26.112 1.00 24.34  ? 181 GLU C CB  1 
ATOM   5711 C  CG  . GLU C 1 181 ? 51.023  -13.061 -26.014 1.00 28.96  ? 181 GLU C CG  1 
ATOM   5712 C  CD  . GLU C 1 181 ? 51.700  -12.865 -24.656 1.00 37.60  ? 181 GLU C CD  1 
ATOM   5713 O  OE1 . GLU C 1 181 ? 50.987  -12.482 -23.718 1.00 35.05  ? 181 GLU C OE1 1 
ATOM   5714 O  OE2 . GLU C 1 181 ? 52.949  -13.078 -24.523 1.00 34.76  ? 181 GLU C OE2 1 
ATOM   5715 N  N   . LEU C 1 182 ? 47.273  -10.440 -27.726 1.00 19.71  ? 182 LEU C N   1 
ATOM   5716 C  CA  . LEU C 1 182 ? 45.912  -9.914  -27.622 1.00 17.12  ? 182 LEU C CA  1 
ATOM   5717 C  C   . LEU C 1 182 ? 45.089  -10.301 -28.861 1.00 17.94  ? 182 LEU C C   1 
ATOM   5718 O  O   . LEU C 1 182 ? 43.869  -10.077 -28.864 1.00 17.47  ? 182 LEU C O   1 
ATOM   5719 C  CB  . LEU C 1 182 ? 45.870  -8.378  -27.506 1.00 17.83  ? 182 LEU C CB  1 
ATOM   5720 C  CG  . LEU C 1 182 ? 46.561  -7.773  -26.284 1.00 17.95  ? 182 LEU C CG  1 
ATOM   5721 C  CD1 . LEU C 1 182 ? 46.427  -6.254  -26.308 1.00 21.79  ? 182 LEU C CD1 1 
ATOM   5722 C  CD2 . LEU C 1 182 ? 46.106  -8.391  -24.953 1.00 19.04  ? 182 LEU C CD2 1 
ATOM   5723 N  N   . LEU C 1 183 ? 45.770  -10.808 -29.910 1.00 18.13  ? 183 LEU C N   1 
ATOM   5724 C  CA  . LEU C 1 183 ? 45.145  -11.164 -31.176 1.00 15.92  ? 183 LEU C CA  1 
ATOM   5725 C  C   . LEU C 1 183 ? 44.570  -12.579 -31.035 1.00 16.09  ? 183 LEU C C   1 
ATOM   5726 O  O   . LEU C 1 183 ? 45.037  -13.370 -30.217 1.00 20.87  ? 183 LEU C O   1 
ATOM   5727 C  CB  . LEU C 1 183 ? 46.177  -11.076 -32.309 1.00 18.21  ? 183 LEU C CB  1 
ATOM   5728 C  CG  . LEU C 1 183 ? 46.783  -9.697  -32.542 1.00 18.41  ? 183 LEU C CG  1 
ATOM   5729 C  CD1 . LEU C 1 183 ? 47.588  -9.681  -33.842 1.00 20.41  ? 183 LEU C CD1 1 
ATOM   5730 C  CD2 . LEU C 1 183 ? 45.716  -8.612  -32.528 1.00 17.57  ? 183 LEU C CD2 1 
ATOM   5731 N  N   . PRO C 1 184 ? 43.490  -12.884 -31.777 1.00 16.06  ? 184 PRO C N   1 
ATOM   5732 C  CA  . PRO C 1 184 ? 42.887  -14.220 -31.706 1.00 17.67  ? 184 PRO C CA  1 
ATOM   5733 C  C   . PRO C 1 184 ? 43.680  -15.254 -32.460 1.00 20.48  ? 184 PRO C C   1 
ATOM   5734 O  O   . PRO C 1 184 ? 44.658  -14.933 -33.101 1.00 20.37  ? 184 PRO C O   1 
ATOM   5735 C  CB  . PRO C 1 184 ? 41.536  -14.002 -32.411 1.00 19.70  ? 184 PRO C CB  1 
ATOM   5736 C  CG  . PRO C 1 184 ? 41.840  -12.860 -33.376 1.00 18.36  ? 184 PRO C CG  1 
ATOM   5737 C  CD  . PRO C 1 184 ? 42.756  -11.931 -32.627 1.00 16.38  ? 184 PRO C CD  1 
ATOM   5738 N  N   . GLU C 1 185 ? 43.204  -16.504 -32.387 1.00 23.64  ? 185 GLU C N   1 
ATOM   5739 C  CA  . GLU C 1 185 ? 43.646  -17.575 -33.261 1.00 24.04  ? 185 GLU C CA  1 
ATOM   5740 C  C   . GLU C 1 185 ? 43.357  -17.293 -34.739 1.00 22.10  ? 185 GLU C C   1 
ATOM   5741 O  O   . GLU C 1 185 ? 42.382  -16.597 -35.088 1.00 23.77  ? 185 GLU C O   1 
ATOM   5742 C  CB  . GLU C 1 185 ? 42.866  -18.825 -32.904 1.00 24.47  ? 185 GLU C CB  1 
ATOM   5743 C  CG  . GLU C 1 185 ? 43.088  -19.247 -31.465 1.00 29.21  ? 185 GLU C CG  1 
ATOM   5744 C  CD  . GLU C 1 185 ? 44.216  -20.235 -31.202 1.00 42.55  ? 185 GLU C CD  1 
ATOM   5745 O  OE1 . GLU C 1 185 ? 44.138  -20.937 -30.176 1.00 58.33  ? 185 GLU C OE1 1 
ATOM   5746 O  OE2 . GLU C 1 185 ? 45.166  -20.327 -32.033 1.00 39.97  ? 185 GLU C OE2 1 
ATOM   5747 N  N   . ARG C 1 186 ? 44.251  -17.784 -35.614 1.00 22.56  ? 186 ARG C N   1 
ATOM   5748 C  CA  . ARG C 1 186 ? 44.043  -17.731 -37.055 1.00 23.41  ? 186 ARG C CA  1 
ATOM   5749 C  C   . ARG C 1 186 ? 43.820  -16.278 -37.507 1.00 21.75  ? 186 ARG C C   1 
ATOM   5750 O  O   . ARG C 1 186 ? 42.835  -15.936 -38.184 1.00 18.55  ? 186 ARG C O   1 
ATOM   5751 C  CB  . ARG C 1 186 ? 42.937  -18.701 -37.503 1.00 26.03  ? 186 ARG C CB  1 
ATOM   5752 C  CG  . ARG C 1 186 ? 43.262  -20.185 -37.328 1.00 28.15  ? 186 ARG C CG  1 
ATOM   5753 C  CD  . ARG C 1 186 ? 41.965  -20.976 -37.409 1.00 39.95  ? 186 ARG C CD  1 
ATOM   5754 N  NE  . ARG C 1 186 ? 41.371  -21.168 -36.092 1.00 45.21  ? 186 ARG C NE  1 
ATOM   5755 C  CZ  . ARG C 1 186 ? 40.087  -21.006 -35.748 1.00 57.73  ? 186 ARG C CZ  1 
ATOM   5756 N  NH1 . ARG C 1 186 ? 39.183  -20.556 -36.610 1.00 45.13  ? 186 ARG C NH1 1 
ATOM   5757 N  NH2 . ARG C 1 186 ? 39.716  -21.271 -34.505 1.00 69.69  ? 186 ARG C NH2 1 
ATOM   5758 N  N   . THR C 1 187 ? 44.806  -15.429 -37.218 1.00 16.42  ? 187 THR C N   1 
ATOM   5759 C  CA  . THR C 1 187 ? 44.763  -14.055 -37.696 1.00 16.52  ? 187 THR C CA  1 
ATOM   5760 C  C   . THR C 1 187 ? 44.733  -13.990 -39.209 1.00 16.90  ? 187 THR C C   1 
ATOM   5761 O  O   . THR C 1 187 ? 44.457  -12.940 -39.751 1.00 17.66  ? 187 THR C O   1 
ATOM   5762 C  CB  . THR C 1 187 ? 45.924  -13.246 -37.109 1.00 20.26  ? 187 THR C CB  1 
ATOM   5763 O  OG1 . THR C 1 187 ? 47.170  -13.930 -37.298 1.00 22.73  ? 187 THR C OG1 1 
ATOM   5764 C  CG2 . THR C 1 187 ? 45.722  -12.982 -35.638 1.00 17.96  ? 187 THR C CG2 1 
ATOM   5765 N  N   . ALA C 1 188 ? 45.052  -15.110 -39.878 1.00 17.22  ? 188 ALA C N   1 
ATOM   5766 C  CA  . ALA C 1 188 ? 44.958  -15.115 -41.328 1.00 19.07  ? 188 ALA C CA  1 
ATOM   5767 C  C   . ALA C 1 188 ? 43.522  -14.849 -41.786 1.00 16.27  ? 188 ALA C C   1 
ATOM   5768 O  O   . ALA C 1 188 ? 43.319  -14.463 -42.942 1.00 15.99  ? 188 ALA C O   1 
ATOM   5769 C  CB  . ALA C 1 188 ? 45.481  -16.416 -41.892 1.00 20.07  ? 188 ALA C CB  1 
ATOM   5770 N  N   . GLU C 1 189 ? 42.525  -15.092 -40.901 1.00 14.90  ? 189 GLU C N   1 
ATOM   5771 C  CA  . GLU C 1 189 ? 41.101  -15.027 -41.237 1.00 13.75  ? 189 GLU C CA  1 
ATOM   5772 C  C   . GLU C 1 189 ? 40.558  -13.678 -40.723 1.00 14.84  ? 189 GLU C C   1 
ATOM   5773 O  O   . GLU C 1 189 ? 40.549  -13.432 -39.504 1.00 14.65  ? 189 GLU C O   1 
ATOM   5774 C  CB  . GLU C 1 189 ? 40.336  -16.232 -40.668 1.00 16.61  ? 189 GLU C CB  1 
ATOM   5775 C  CG  . GLU C 1 189 ? 40.812  -17.584 -41.139 1.00 21.22  ? 189 GLU C CG  1 
ATOM   5776 C  CD  . GLU C 1 189 ? 40.236  -18.751 -40.334 1.00 28.79  ? 189 GLU C CD  1 
ATOM   5777 O  OE1 . GLU C 1 189 ? 39.296  -18.552 -39.588 1.00 29.11  ? 189 GLU C OE1 1 
ATOM   5778 O  OE2 . GLU C 1 189 ? 40.767  -19.851 -40.413 1.00 33.18  ? 189 GLU C OE2 1 
ATOM   5779 N  N   . TYR C 1 190 ? 40.134  -12.825 -41.652 1.00 11.82  ? 190 TYR C N   1 
ATOM   5780 C  CA  . TYR C 1 190 ? 39.695  -11.486 -41.263 1.00 11.34  ? 190 TYR C CA  1 
ATOM   5781 C  C   . TYR C 1 190 ? 38.696  -10.954 -42.299 1.00 11.53  ? 190 TYR C C   1 
ATOM   5782 O  O   . TYR C 1 190 ? 38.692  -11.328 -43.491 1.00 13.84  ? 190 TYR C O   1 
ATOM   5783 C  CB  . TYR C 1 190 ? 40.874  -10.499 -41.075 1.00 11.20  ? 190 TYR C CB  1 
ATOM   5784 C  CG  . TYR C 1 190 ? 41.838  -10.374 -42.240 1.00 10.82  ? 190 TYR C CG  1 
ATOM   5785 C  CD1 . TYR C 1 190 ? 41.620  -9.435  -43.253 1.00 12.23  ? 190 TYR C CD1 1 
ATOM   5786 C  CD2 . TYR C 1 190 ? 43.012  -11.123 -42.271 1.00 14.29  ? 190 TYR C CD2 1 
ATOM   5787 C  CE1 . TYR C 1 190 ? 42.534  -9.267  -44.273 1.00 12.83  ? 190 TYR C CE1 1 
ATOM   5788 C  CE2 . TYR C 1 190 ? 43.941  -10.943 -43.282 1.00 14.57  ? 190 TYR C CE2 1 
ATOM   5789 C  CZ  . TYR C 1 190 ? 43.689  -10.047 -44.313 1.00 15.72  ? 190 TYR C CZ  1 
ATOM   5790 O  OH  . TYR C 1 190 ? 44.534  -9.841  -45.371 1.00 17.19  ? 190 TYR C OH  1 
ATOM   5791 N  N   . TYR C 1 191 ? 37.955  -9.946  -41.832 1.00 10.98  ? 191 TYR C N   1 
ATOM   5792 C  CA  . TYR C 1 191 ? 37.159  -9.089  -42.690 1.00 10.98  ? 191 TYR C CA  1 
ATOM   5793 C  C   . TYR C 1 191 ? 37.946  -7.805  -42.964 1.00 11.01  ? 191 TYR C C   1 
ATOM   5794 O  O   . TYR C 1 191 ? 38.644  -7.321  -42.068 1.00 11.49  ? 191 TYR C O   1 
ATOM   5795 C  CB  . TYR C 1 191 ? 35.887  -8.675  -41.948 1.00 11.01  ? 191 TYR C CB  1 
ATOM   5796 C  CG  . TYR C 1 191 ? 35.051  -9.814  -41.391 1.00 10.86  ? 191 TYR C CG  1 
ATOM   5797 C  CD1 . TYR C 1 191 ? 33.982  -10.361 -42.107 1.00 12.29  ? 191 TYR C CD1 1 
ATOM   5798 C  CD2 . TYR C 1 191 ? 35.199  -10.198 -40.061 1.00 12.16  ? 191 TYR C CD2 1 
ATOM   5799 C  CE1 . TYR C 1 191 ? 33.211  -11.376 -41.562 1.00 13.38  ? 191 TYR C CE1 1 
ATOM   5800 C  CE2 . TYR C 1 191 ? 34.428  -11.204 -39.508 1.00 11.54  ? 191 TYR C CE2 1 
ATOM   5801 C  CZ  . TYR C 1 191 ? 33.393  -11.766 -40.250 1.00 12.74  ? 191 TYR C CZ  1 
ATOM   5802 O  OH  . TYR C 1 191 ? 32.588  -12.737 -39.689 1.00 14.95  ? 191 TYR C OH  1 
ATOM   5803 N  N   . ARG C 1 192 ? 37.718  -7.203  -44.146 1.00 10.27  ? 192 ARG C N   1 
ATOM   5804 C  CA  . ARG C 1 192 ? 38.447  -6.013  -44.545 1.00 10.54  ? 192 ARG C CA  1 
ATOM   5805 C  C   . ARG C 1 192 ? 37.442  -5.080  -45.222 1.00 9.90   ? 192 ARG C C   1 
ATOM   5806 O  O   . ARG C 1 192 ? 36.736  -5.474  -46.158 1.00 10.71  ? 192 ARG C O   1 
ATOM   5807 C  CB  . ARG C 1 192 ? 39.533  -6.419  -45.544 1.00 14.22  ? 192 ARG C CB  1 
ATOM   5808 C  CG  . ARG C 1 192 ? 40.187  -5.273  -46.319 1.00 14.12  ? 192 ARG C CG  1 
ATOM   5809 C  CD  . ARG C 1 192 ? 40.958  -4.291  -45.444 1.00 14.00  ? 192 ARG C CD  1 
ATOM   5810 N  NE  . ARG C 1 192 ? 41.937  -4.894  -44.560 1.00 16.01  ? 192 ARG C NE  1 
ATOM   5811 C  CZ  . ARG C 1 192 ? 43.104  -5.413  -44.983 1.00 15.08  ? 192 ARG C CZ  1 
ATOM   5812 N  NH1 . ARG C 1 192 ? 43.406  -5.373  -46.269 1.00 19.12  ? 192 ARG C NH1 1 
ATOM   5813 N  NH2 . ARG C 1 192 ? 43.951  -5.941  -44.118 1.00 15.92  ? 192 ARG C NH2 1 
ATOM   5814 N  N   . TYR C 1 193 ? 37.420  -3.803  -44.797 1.00 11.14  ? 193 TYR C N   1 
ATOM   5815 C  CA  . TYR C 1 193 ? 36.648  -2.783  -45.516 1.00 10.54  ? 193 TYR C CA  1 
ATOM   5816 C  C   . TYR C 1 193 ? 37.269  -1.415  -45.259 1.00 10.11  ? 193 TYR C C   1 
ATOM   5817 O  O   . TYR C 1 193 ? 37.958  -1.213  -44.274 1.00 10.71  ? 193 TYR C O   1 
ATOM   5818 C  CB  . TYR C 1 193 ? 35.125  -2.865  -45.250 1.00 10.81  ? 193 TYR C CB  1 
ATOM   5819 C  CG  . TYR C 1 193 ? 34.741  -2.325  -43.890 1.00 10.91  ? 193 TYR C CG  1 
ATOM   5820 C  CD1 . TYR C 1 193 ? 34.973  -3.029  -42.705 1.00 11.11  ? 193 TYR C CD1 1 
ATOM   5821 C  CD2 . TYR C 1 193 ? 34.176  -1.049  -43.801 1.00 11.09  ? 193 TYR C CD2 1 
ATOM   5822 C  CE1 . TYR C 1 193 ? 34.615  -2.471  -41.485 1.00 8.40   ? 193 TYR C CE1 1 
ATOM   5823 C  CE2 . TYR C 1 193 ? 33.856  -0.495  -42.574 1.00 9.66   ? 193 TYR C CE2 1 
ATOM   5824 C  CZ  . TYR C 1 193 ? 34.095  -1.190  -41.406 1.00 8.42   ? 193 TYR C CZ  1 
ATOM   5825 O  OH  . TYR C 1 193 ? 33.765  -0.622  -40.185 1.00 8.71   ? 193 TYR C OH  1 
ATOM   5826 N  N   . ARG C 1 194 ? 36.910  -0.461  -46.115 1.00 9.07   ? 194 ARG C N   1 
ATOM   5827 C  CA  . ARG C 1 194 ? 37.279  0.952   -45.945 1.00 11.01  ? 194 ARG C CA  1 
ATOM   5828 C  C   . ARG C 1 194 ? 36.172  1.693   -45.194 1.00 10.45  ? 194 ARG C C   1 
ATOM   5829 O  O   . ARG C 1 194 ? 35.007  1.672   -45.576 1.00 10.87  ? 194 ARG C O   1 
ATOM   5830 C  CB  . ARG C 1 194 ? 37.461  1.650   -47.295 1.00 13.01  ? 194 ARG C CB  1 
ATOM   5831 C  CG  . ARG C 1 194 ? 38.684  1.138   -48.037 1.00 17.20  ? 194 ARG C CG  1 
ATOM   5832 C  CD  . ARG C 1 194 ? 38.996  1.942   -49.289 1.00 28.58  ? 194 ARG C CD  1 
ATOM   5833 N  NE  . ARG C 1 194 ? 40.151  1.308   -49.933 1.00 39.21  ? 194 ARG C NE  1 
ATOM   5834 C  CZ  . ARG C 1 194 ? 41.274  0.942   -49.307 1.00 42.82  ? 194 ARG C CZ  1 
ATOM   5835 N  NH1 . ARG C 1 194 ? 41.410  1.165   -48.011 1.00 47.34  ? 194 ARG C NH1 1 
ATOM   5836 N  NH2 . ARG C 1 194 ? 42.262  0.360   -49.973 1.00 46.27  ? 194 ARG C NH2 1 
ATOM   5837 N  N   . GLY C 1 195 ? 36.543  2.262   -44.059 1.00 10.03  ? 195 GLY C N   1 
ATOM   5838 C  CA  . GLY C 1 195 ? 35.566  2.994   -43.252 1.00 9.71   ? 195 GLY C CA  1 
ATOM   5839 C  C   . GLY C 1 195 ? 36.181  4.173   -42.533 1.00 8.24   ? 195 GLY C C   1 
ATOM   5840 O  O   . GLY C 1 195 ? 36.987  4.915   -43.126 1.00 9.18   ? 195 GLY C O   1 
ATOM   5841 N  N   . SER C 1 196 ? 35.736  4.418   -41.282 1.00 8.54   ? 196 SER C N   1 
ATOM   5842 C  CA  . SER C 1 196 ? 36.018  5.683   -40.615 1.00 8.65   ? 196 SER C CA  1 
ATOM   5843 C  C   . SER C 1 196 ? 36.489  5.423   -39.190 1.00 9.79   ? 196 SER C C   1 
ATOM   5844 O  O   . SER C 1 196 ? 36.337  4.342   -38.675 1.00 9.56   ? 196 SER C O   1 
ATOM   5845 C  CB  . SER C 1 196 ? 34.775  6.630   -40.565 1.00 9.35   ? 196 SER C CB  1 
ATOM   5846 O  OG  . SER C 1 196 ? 33.843  6.127   -39.625 1.00 9.38   ? 196 SER C OG  1 
ATOM   5847 N  N   . LEU C 1 197 ? 36.945  6.485   -38.533 1.00 9.66   ? 197 LEU C N   1 
ATOM   5848 C  CA  . LEU C 1 197 ? 37.046  6.436   -37.081 1.00 9.69   ? 197 LEU C CA  1 
ATOM   5849 C  C   . LEU C 1 197 ? 35.614  6.248   -36.571 1.00 9.64   ? 197 LEU C C   1 
ATOM   5850 O  O   . LEU C 1 197 ? 34.651  6.815   -37.118 1.00 9.28   ? 197 LEU C O   1 
ATOM   5851 C  CB  . LEU C 1 197 ? 37.518  7.768   -36.506 1.00 13.16  ? 197 LEU C CB  1 
ATOM   5852 C  CG  . LEU C 1 197 ? 39.017  8.010   -36.590 1.00 12.45  ? 197 LEU C CG  1 
ATOM   5853 C  CD1 . LEU C 1 197 ? 39.380  8.597   -37.964 1.00 16.46  ? 197 LEU C CD1 1 
ATOM   5854 C  CD2 . LEU C 1 197 ? 39.396  9.002   -35.489 1.00 17.62  ? 197 LEU C CD2 1 
ATOM   5855 N  N   . THR C 1 198 ? 35.473  5.493   -35.478 1.00 8.75   ? 198 THR C N   1 
ATOM   5856 C  CA  . THR C 1 198 ? 34.153  5.320   -34.883 1.00 9.44   ? 198 THR C CA  1 
ATOM   5857 C  C   . THR C 1 198 ? 33.920  6.327   -33.758 1.00 10.82  ? 198 THR C C   1 
ATOM   5858 O  O   . THR C 1 198 ? 32.822  6.338   -33.166 1.00 10.70  ? 198 THR C O   1 
ATOM   5859 C  CB  . THR C 1 198 ? 33.947  3.924   -34.304 1.00 7.75   ? 198 THR C CB  1 
ATOM   5860 O  OG1 . THR C 1 198 ? 34.874  3.823   -33.226 1.00 9.64   ? 198 THR C OG1 1 
ATOM   5861 C  CG2 . THR C 1 198 ? 34.141  2.735   -35.247 1.00 9.22   ? 198 THR C CG2 1 
ATOM   5862 N  N   . THR C 1 199 ? 34.841  7.286   -33.608 1.00 11.18  ? 199 THR C N   1 
ATOM   5863 C  CA  . THR C 1 199 ? 34.649  8.393   -32.690 1.00 10.92  ? 199 THR C CA  1 
ATOM   5864 C  C   . THR C 1 199 ? 34.884  9.646   -33.472 1.00 11.10  ? 199 THR C C   1 
ATOM   5865 O  O   . THR C 1 199 ? 35.504  9.569   -34.528 1.00 11.26  ? 199 THR C O   1 
ATOM   5866 C  CB  . THR C 1 199 ? 35.736  8.435   -31.589 1.00 11.04  ? 199 THR C CB  1 
ATOM   5867 O  OG1 . THR C 1 199 ? 37.020  8.436   -32.206 1.00 12.02  ? 199 THR C OG1 1 
ATOM   5868 C  CG2 . THR C 1 199 ? 35.691  7.101   -30.863 1.00 11.50  ? 199 THR C CG2 1 
ATOM   5869 N  N   . PRO C 1 200 ? 34.423  10.810  -32.963 1.00 9.63   ? 200 PRO C N   1 
ATOM   5870 C  CA  . PRO C 1 200 ? 34.904  12.060  -33.564 1.00 10.59  ? 200 PRO C CA  1 
ATOM   5871 C  C   . PRO C 1 200 ? 36.410  12.035  -33.711 1.00 11.17  ? 200 PRO C C   1 
ATOM   5872 O  O   . PRO C 1 200 ? 37.091  11.581  -32.812 1.00 12.94  ? 200 PRO C O   1 
ATOM   5873 C  CB  . PRO C 1 200 ? 34.417  13.098  -32.503 1.00 11.93  ? 200 PRO C CB  1 
ATOM   5874 C  CG  . PRO C 1 200 ? 33.156  12.474  -31.985 1.00 11.49  ? 200 PRO C CG  1 
ATOM   5875 C  CD  . PRO C 1 200 ? 33.553  11.046  -31.790 1.00 11.71  ? 200 PRO C CD  1 
ATOM   5876 N  N   . PRO C 1 201 ? 36.994  12.653  -34.771 1.00 12.98  ? 201 PRO C N   1 
ATOM   5877 C  CA  . PRO C 1 201 ? 36.226  13.348  -35.785 1.00 11.96  ? 201 PRO C CA  1 
ATOM   5878 C  C   . PRO C 1 201 ? 35.580  12.528  -36.912 1.00 12.51  ? 201 PRO C C   1 
ATOM   5879 O  O   . PRO C 1 201 ? 35.122  13.075  -37.883 1.00 11.72  ? 201 PRO C O   1 
ATOM   5880 C  CB  . PRO C 1 201 ? 37.208  14.355  -36.392 1.00 12.86  ? 201 PRO C CB  1 
ATOM   5881 C  CG  . PRO C 1 201 ? 38.373  14.333  -35.411 1.00 18.02  ? 201 PRO C CG  1 
ATOM   5882 C  CD  . PRO C 1 201 ? 38.433  12.890  -34.921 1.00 14.18  ? 201 PRO C CD  1 
ATOM   5883 N  N   . CYS C 1 202 ? 35.549  11.198  -36.763 1.00 10.12  ? 202 CYS C N   1 
ATOM   5884 C  CA  . CYS C 1 202 ? 34.845  10.330  -37.705 1.00 11.18  ? 202 CYS C CA  1 
ATOM   5885 C  C   . CYS C 1 202 ? 35.415  10.379  -39.123 1.00 10.60  ? 202 CYS C C   1 
ATOM   5886 O  O   . CYS C 1 202 ? 34.705  10.049  -40.063 1.00 10.15  ? 202 CYS C O   1 
ATOM   5887 C  CB  . CYS C 1 202 ? 33.330  10.572  -37.809 1.00 10.78  ? 202 CYS C CB  1 
ATOM   5888 S  SG  . CYS C 1 202 ? 32.462  10.584  -36.210 1.00 11.12  ? 202 CYS C SG  1 
ATOM   5889 N  N   . ASN C 1 203 ? 36.693  10.737  -39.288 1.00 10.50  ? 203 ASN C N   1 
ATOM   5890 C  CA  . ASN C 1 203 ? 37.193  10.829  -40.650 1.00 11.65  ? 203 ASN C CA  1 
ATOM   5891 C  C   . ASN C 1 203 ? 37.109  9.501   -41.398 1.00 10.62  ? 203 ASN C C   1 
ATOM   5892 O  O   . ASN C 1 203 ? 37.360  8.451   -40.814 1.00 12.10  ? 203 ASN C O   1 
ATOM   5893 C  CB  . ASN C 1 203 ? 38.643  11.344  -40.675 1.00 14.03  ? 203 ASN C CB  1 
ATOM   5894 C  CG  . ASN C 1 203 ? 38.795  12.595  -39.833 1.00 14.39  ? 203 ASN C CG  1 
ATOM   5895 O  OD1 . ASN C 1 203 ? 38.928  12.489  -38.601 1.00 16.15  ? 203 ASN C OD1 1 
ATOM   5896 N  ND2 . ASN C 1 203 ? 38.797  13.757  -40.488 1.00 20.81  ? 203 ASN C ND2 1 
ATOM   5897 N  N   . PRO C 1 204 ? 36.717  9.520   -42.685 1.00 11.14  ? 204 PRO C N   1 
ATOM   5898 C  CA  . PRO C 1 204 ? 36.615  8.276   -43.473 1.00 11.59  ? 204 PRO C CA  1 
ATOM   5899 C  C   . PRO C 1 204 ? 37.964  7.846   -44.024 1.00 10.46  ? 204 PRO C C   1 
ATOM   5900 O  O   . PRO C 1 204 ? 38.113  7.651   -45.245 1.00 13.95  ? 204 PRO C O   1 
ATOM   5901 C  CB  . PRO C 1 204 ? 35.677  8.767   -44.610 1.00 11.62  ? 204 PRO C CB  1 
ATOM   5902 C  CG  . PRO C 1 204 ? 36.095  10.196  -44.834 1.00 13.69  ? 204 PRO C CG  1 
ATOM   5903 C  CD  . PRO C 1 204 ? 36.264  10.718  -43.415 1.00 13.81  ? 204 PRO C CD  1 
ATOM   5904 N  N   . THR C 1 205 ? 38.913  7.624   -43.105 1.00 11.40  ? 205 THR C N   1 
ATOM   5905 C  CA  . THR C 1 205 ? 40.309  7.384   -43.478 1.00 10.99  ? 205 THR C CA  1 
ATOM   5906 C  C   . THR C 1 205 ? 40.884  6.062   -42.959 1.00 12.45  ? 205 THR C C   1 
ATOM   5907 O  O   . THR C 1 205 ? 42.090  5.952   -42.904 1.00 12.71  ? 205 THR C O   1 
ATOM   5908 C  CB  . THR C 1 205 ? 41.102  8.632   -43.025 1.00 13.40  ? 205 THR C CB  1 
ATOM   5909 O  OG1 . THR C 1 205 ? 40.890  8.653   -41.620 1.00 13.42  ? 205 THR C OG1 1 
ATOM   5910 C  CG2 . THR C 1 205 ? 40.721  9.906   -43.762 1.00 15.40  ? 205 THR C CG2 1 
ATOM   5911 N  N   . VAL C 1 206 ? 40.010  5.172   -42.486 1.00 11.54  ? 206 VAL C N   1 
ATOM   5912 C  CA  . VAL C 1 206 ? 40.444  3.944   -41.827 1.00 9.92   ? 206 VAL C CA  1 
ATOM   5913 C  C   . VAL C 1 206 ? 40.276  2.686   -42.678 1.00 9.74   ? 206 VAL C C   1 
ATOM   5914 O  O   . VAL C 1 206 ? 39.185  2.374   -43.158 1.00 11.19  ? 206 VAL C O   1 
ATOM   5915 C  CB  . VAL C 1 206 ? 39.731  3.735   -40.464 1.00 9.70   ? 206 VAL C CB  1 
ATOM   5916 C  CG1 . VAL C 1 206 ? 40.113  2.360   -39.850 1.00 10.86  ? 206 VAL C CG1 1 
ATOM   5917 C  CG2 . VAL C 1 206 ? 39.928  4.867   -39.488 1.00 11.04  ? 206 VAL C CG2 1 
ATOM   5918 N  N   . LEU C 1 207 ? 41.381  2.008   -42.873 1.00 11.31  ? 207 LEU C N   1 
ATOM   5919 C  CA  . LEU C 1 207 ? 41.337  0.652   -43.416 1.00 10.21  ? 207 LEU C CA  1 
ATOM   5920 C  C   . LEU C 1 207 ? 41.101  -0.303  -42.250 1.00 9.33   ? 207 LEU C C   1 
ATOM   5921 O  O   . LEU C 1 207 ? 41.979  -0.460  -41.384 1.00 10.12  ? 207 LEU C O   1 
ATOM   5922 C  CB  . LEU C 1 207 ? 42.678  0.333   -44.100 1.00 13.46  ? 207 LEU C CB  1 
ATOM   5923 C  CG  . LEU C 1 207 ? 42.650  -0.873  -45.026 1.00 15.91  ? 207 LEU C CG  1 
ATOM   5924 C  CD1 . LEU C 1 207 ? 41.623  -0.753  -46.167 1.00 20.90  ? 207 LEU C CD1 1 
ATOM   5925 C  CD2 . LEU C 1 207 ? 44.036  -1.141  -45.583 1.00 24.56  ? 207 LEU C CD2 1 
ATOM   5926 N  N   . TRP C 1 208 ? 39.914  -0.905  -42.223 1.00 9.37   ? 208 TRP C N   1 
ATOM   5927 C  CA  . TRP C 1 208 ? 39.526  -1.800  -41.127 1.00 8.20   ? 208 TRP C CA  1 
ATOM   5928 C  C   . TRP C 1 208 ? 39.903  -3.252  -41.397 1.00 8.54   ? 208 TRP C C   1 
ATOM   5929 O  O   . TRP C 1 208 ? 39.681  -3.738  -42.514 1.00 11.49  ? 208 TRP C O   1 
ATOM   5930 C  CB  . TRP C 1 208 ? 38.027  -1.761  -40.841 1.00 9.15   ? 208 TRP C CB  1 
ATOM   5931 C  CG  . TRP C 1 208 ? 37.598  -0.533  -40.102 1.00 9.16   ? 208 TRP C CG  1 
ATOM   5932 C  CD1 . TRP C 1 208 ? 37.136  0.658   -40.606 1.00 9.77   ? 208 TRP C CD1 1 
ATOM   5933 C  CD2 . TRP C 1 208 ? 37.697  -0.377  -38.687 1.00 7.96   ? 208 TRP C CD2 1 
ATOM   5934 N  NE1 . TRP C 1 208 ? 36.996  1.555   -39.579 1.00 9.31   ? 208 TRP C NE1 1 
ATOM   5935 C  CE2 . TRP C 1 208 ? 37.312  0.959   -38.377 1.00 8.79   ? 208 TRP C CE2 1 
ATOM   5936 C  CE3 . TRP C 1 208 ? 38.062  -1.240  -37.636 1.00 9.26   ? 208 TRP C CE3 1 
ATOM   5937 C  CZ2 . TRP C 1 208 ? 37.324  1.432   -37.069 1.00 8.59   ? 208 TRP C CZ2 1 
ATOM   5938 C  CZ3 . TRP C 1 208 ? 38.014  -0.761  -36.323 1.00 8.51   ? 208 TRP C CZ3 1 
ATOM   5939 C  CH2 . TRP C 1 208 ? 37.688  0.573   -36.079 1.00 9.07   ? 208 TRP C CH2 1 
ATOM   5940 N  N   . THR C 1 209 ? 40.503  -3.854  -40.372 1.00 10.96  ? 209 THR C N   1 
ATOM   5941 C  CA  . THR C 1 209 ? 40.697  -5.272  -40.405 1.00 9.21   ? 209 THR C CA  1 
ATOM   5942 C  C   . THR C 1 209 ? 40.092  -5.838  -39.131 1.00 11.48  ? 209 THR C C   1 
ATOM   5943 O  O   . THR C 1 209 ? 40.573  -5.505  -38.061 1.00 9.78   ? 209 THR C O   1 
ATOM   5944 C  CB  . THR C 1 209 ? 42.201  -5.602  -40.398 1.00 10.47  ? 209 THR C CB  1 
ATOM   5945 O  OG1 . THR C 1 209 ? 42.806  -5.113  -41.580 1.00 10.77  ? 209 THR C OG1 1 
ATOM   5946 C  CG2 . THR C 1 209 ? 42.429  -7.109  -40.385 1.00 11.53  ? 209 THR C CG2 1 
ATOM   5947 N  N   . VAL C 1 210 ? 38.994  -6.597  -39.262 1.00 10.40  ? 210 VAL C N   1 
ATOM   5948 C  CA  . VAL C 1 210 ? 38.293  -7.168  -38.123 1.00 9.08   ? 210 VAL C CA  1 
ATOM   5949 C  C   . VAL C 1 210 ? 38.582  -8.672  -38.118 1.00 9.53   ? 210 VAL C C   1 
ATOM   5950 O  O   . VAL C 1 210 ? 38.269  -9.352  -39.084 1.00 12.15  ? 210 VAL C O   1 
ATOM   5951 C  CB  . VAL C 1 210 ? 36.778  -6.909  -38.169 1.00 8.26   ? 210 VAL C CB  1 
ATOM   5952 C  CG1 . VAL C 1 210 ? 36.130  -7.496  -36.884 1.00 10.91  ? 210 VAL C CG1 1 
ATOM   5953 C  CG2 . VAL C 1 210 ? 36.467  -5.420  -38.293 1.00 11.15  ? 210 VAL C CG2 1 
ATOM   5954 N  N   . PHE C 1 211 ? 39.280  -9.178  -37.107 1.00 10.58  ? 211 PHE C N   1 
ATOM   5955 C  CA  . PHE C 1 211 ? 39.581  -10.602 -37.188 1.00 8.94   ? 211 PHE C CA  1 
ATOM   5956 C  C   . PHE C 1 211 ? 38.305  -11.425 -37.073 1.00 11.73  ? 211 PHE C C   1 
ATOM   5957 O  O   . PHE C 1 211 ? 37.380  -11.101 -36.321 1.00 12.10  ? 211 PHE C O   1 
ATOM   5958 C  CB  . PHE C 1 211 ? 40.592  -10.998 -36.091 1.00 11.40  ? 211 PHE C CB  1 
ATOM   5959 C  CG  . PHE C 1 211 ? 41.940  -10.398 -36.372 1.00 11.72  ? 211 PHE C CG  1 
ATOM   5960 C  CD1 . PHE C 1 211 ? 42.720  -10.868 -37.435 1.00 15.42  ? 211 PHE C CD1 1 
ATOM   5961 C  CD2 . PHE C 1 211 ? 42.401  -9.344  -35.605 1.00 12.59  ? 211 PHE C CD2 1 
ATOM   5962 C  CE1 . PHE C 1 211 ? 43.929  -10.271 -37.744 1.00 14.63  ? 211 PHE C CE1 1 
ATOM   5963 C  CE2 . PHE C 1 211 ? 43.602  -8.729  -35.929 1.00 14.30  ? 211 PHE C CE2 1 
ATOM   5964 C  CZ  . PHE C 1 211 ? 44.388  -9.236  -36.941 1.00 15.80  ? 211 PHE C CZ  1 
ATOM   5965 N  N   . ARG C 1 212 ? 38.299  -12.564 -37.784 1.00 10.60  ? 212 ARG C N   1 
ATOM   5966 C  CA  . ARG C 1 212 ? 37.088  -13.407 -37.860 1.00 11.76  ? 212 ARG C CA  1 
ATOM   5967 C  C   . ARG C 1 212 ? 36.788  -14.020 -36.492 1.00 12.31  ? 212 ARG C C   1 
ATOM   5968 O  O   . ARG C 1 212 ? 35.618  -14.024 -36.056 1.00 14.22  ? 212 ARG C O   1 
ATOM   5969 C  CB  . ARG C 1 212 ? 37.244  -14.611 -38.819 1.00 13.35  ? 212 ARG C CB  1 
ATOM   5970 C  CG  . ARG C 1 212 ? 36.034  -15.538 -39.039 1.00 17.25  ? 212 ARG C CG  1 
ATOM   5971 C  CD  . ARG C 1 212 ? 36.398  -16.882 -39.702 1.00 21.52  ? 212 ARG C CD  1 
ATOM   5972 N  NE  . ARG C 1 212 ? 35.227  -17.591 -40.202 1.00 27.45  ? 212 ARG C NE  1 
ATOM   5973 C  CZ  . ARG C 1 212 ? 35.258  -18.606 -41.085 1.00 37.51  ? 212 ARG C CZ  1 
ATOM   5974 N  NH1 . ARG C 1 212 ? 36.404  -19.072 -41.573 1.00 38.92  ? 212 ARG C NH1 1 
ATOM   5975 N  NH2 . ARG C 1 212 ? 34.126  -19.157 -41.479 1.00 53.65  ? 212 ARG C NH2 1 
ATOM   5976 N  N   . ASN C 1 213 ? 37.858  -14.473 -35.817 1.00 13.65  ? 213 ASN C N   1 
ATOM   5977 C  CA  . ASN C 1 213 ? 37.618  -15.182 -34.559 1.00 15.54  ? 213 ASN C CA  1 
ATOM   5978 C  C   . ASN C 1 213 ? 37.757  -14.275 -33.331 1.00 15.15  ? 213 ASN C C   1 
ATOM   5979 O  O   . ASN C 1 213 ? 38.676  -13.465 -33.256 1.00 15.42  ? 213 ASN C O   1 
ATOM   5980 C  CB  . ASN C 1 213 ? 38.558  -16.374 -34.421 1.00 19.25  ? 213 ASN C CB  1 
ATOM   5981 C  CG  . ASN C 1 213 ? 38.514  -17.230 -35.659 1.00 22.31  ? 213 ASN C CG  1 
ATOM   5982 O  OD1 . ASN C 1 213 ? 39.548  -17.442 -36.302 1.00 25.65  ? 213 ASN C OD1 1 
ATOM   5983 N  ND2 . ASN C 1 213 ? 37.326  -17.673 -36.023 1.00 20.76  ? 213 ASN C ND2 1 
ATOM   5984 N  N   . PRO C 1 214 ? 36.862  -14.406 -32.333 1.00 14.94  ? 214 PRO C N   1 
ATOM   5985 C  CA  . PRO C 1 214 ? 36.934  -13.606 -31.109 1.00 15.99  ? 214 PRO C CA  1 
ATOM   5986 C  C   . PRO C 1 214 ? 37.976  -14.173 -30.149 1.00 17.58  ? 214 PRO C C   1 
ATOM   5987 O  O   . PRO C 1 214 ? 38.357  -15.340 -30.274 1.00 18.08  ? 214 PRO C O   1 
ATOM   5988 C  CB  . PRO C 1 214 ? 35.526  -13.758 -30.511 1.00 16.87  ? 214 PRO C CB  1 
ATOM   5989 C  CG  . PRO C 1 214 ? 35.173  -15.148 -30.922 1.00 16.97  ? 214 PRO C CG  1 
ATOM   5990 C  CD  . PRO C 1 214 ? 35.658  -15.235 -32.373 1.00 17.92  ? 214 PRO C CD  1 
ATOM   5991 N  N   . VAL C 1 215 ? 38.442  -13.348 -29.211 1.00 15.70  ? 215 VAL C N   1 
ATOM   5992 C  CA  . VAL C 1 215 ? 39.162  -13.834 -28.033 1.00 16.80  ? 215 VAL C CA  1 
ATOM   5993 C  C   . VAL C 1 215 ? 38.160  -13.964 -26.894 1.00 16.99  ? 215 VAL C C   1 
ATOM   5994 O  O   . VAL C 1 215 ? 37.049  -13.409 -26.933 1.00 16.53  ? 215 VAL C O   1 
ATOM   5995 C  CB  . VAL C 1 215 ? 40.309  -12.887 -27.608 1.00 17.65  ? 215 VAL C CB  1 
ATOM   5996 C  CG1 . VAL C 1 215 ? 41.379  -12.739 -28.719 1.00 15.15  ? 215 VAL C CG1 1 
ATOM   5997 C  CG2 . VAL C 1 215 ? 39.783  -11.498 -27.224 1.00 20.50  ? 215 VAL C CG2 1 
ATOM   5998 N  N   . GLN C 1 216 ? 38.610  -14.652 -25.847 1.00 16.92  ? 216 GLN C N   1 
ATOM   5999 C  CA  . GLN C 1 216 ? 37.803  -14.791 -24.661 1.00 19.53  ? 216 GLN C CA  1 
ATOM   6000 C  C   . GLN C 1 216 ? 38.466  -14.120 -23.467 1.00 22.32  ? 216 GLN C C   1 
ATOM   6001 O  O   . GLN C 1 216 ? 39.685  -14.189 -23.309 1.00 22.28  ? 216 GLN C O   1 
ATOM   6002 C  CB  . GLN C 1 216 ? 37.582  -16.271 -24.350 1.00 24.47  ? 216 GLN C CB  1 
ATOM   6003 C  CG  . GLN C 1 216 ? 36.768  -16.965 -25.427 1.00 26.58  ? 216 GLN C CG  1 
ATOM   6004 C  CD  . GLN C 1 216 ? 36.223  -18.308 -25.006 1.00 35.05  ? 216 GLN C CD  1 
ATOM   6005 O  OE1 . GLN C 1 216 ? 36.701  -18.970 -24.066 1.00 35.46  ? 216 GLN C OE1 1 
ATOM   6006 N  NE2 . GLN C 1 216 ? 35.168  -18.727 -25.689 1.00 41.03  ? 216 GLN C NE2 1 
ATOM   6007 N  N   . ILE C 1 217 ? 37.625  -13.484 -22.634 1.00 18.79  ? 217 ILE C N   1 
ATOM   6008 C  CA  . ILE C 1 217 ? 38.031  -13.053 -21.300 1.00 17.94  ? 217 ILE C CA  1 
ATOM   6009 C  C   . ILE C 1 217 ? 37.042  -13.624 -20.284 1.00 19.82  ? 217 ILE C C   1 
ATOM   6010 O  O   . ILE C 1 217 ? 35.890  -13.859 -20.625 1.00 20.18  ? 217 ILE C O   1 
ATOM   6011 C  CB  . ILE C 1 217 ? 38.163  -11.513 -21.242 1.00 18.95  ? 217 ILE C CB  1 
ATOM   6012 C  CG1 . ILE C 1 217 ? 36.803  -10.786 -21.389 1.00 15.93  ? 217 ILE C CG1 1 
ATOM   6013 C  CG2 . ILE C 1 217 ? 39.186  -11.089 -22.282 1.00 18.09  ? 217 ILE C CG2 1 
ATOM   6014 C  CD1 . ILE C 1 217 ? 36.892  -9.285  -21.156 1.00 19.10  ? 217 ILE C CD1 1 
ATOM   6015 N  N   . SER C 1 218 ? 37.458  -13.828 -19.030 1.00 21.06  ? 218 SER C N   1 
ATOM   6016 C  CA  . SER C 1 218 ? 36.511  -14.466 -18.118 1.00 22.18  ? 218 SER C CA  1 
ATOM   6017 C  C   . SER C 1 218 ? 35.378  -13.512 -17.765 1.00 19.52  ? 218 SER C C   1 
ATOM   6018 O  O   . SER C 1 218 ? 35.427  -12.299 -18.038 1.00 18.34  ? 218 SER C O   1 
ATOM   6019 C  CB  . SER C 1 218 ? 37.186  -14.888 -16.829 1.00 24.22  ? 218 SER C CB  1 
ATOM   6020 O  OG  . SER C 1 218 ? 37.665  -13.743 -16.135 1.00 24.76  ? 218 SER C OG  1 
ATOM   6021 N  N   . GLN C 1 219 ? 34.315  -14.065 -17.181 1.00 26.27  ? 219 GLN C N   1 
ATOM   6022 C  CA  . GLN C 1 219 ? 33.206  -13.231 -16.724 1.00 22.66  ? 219 GLN C CA  1 
ATOM   6023 C  C   . GLN C 1 219 ? 33.752  -12.195 -15.748 1.00 21.46  ? 219 GLN C C   1 
ATOM   6024 O  O   . GLN C 1 219 ? 33.342  -11.033 -15.774 1.00 22.97  ? 219 GLN C O   1 
ATOM   6025 C  CB  . GLN C 1 219 ? 32.102  -14.098 -16.091 1.00 31.66  ? 219 GLN C CB  1 
ATOM   6026 C  CG  . GLN C 1 219 ? 32.516  -14.884 -14.843 1.00 35.35  ? 219 GLN C CG  1 
ATOM   6027 C  CD  . GLN C 1 219 ? 31.724  -16.153 -14.605 1.00 35.26  ? 219 GLN C CD  1 
ATOM   6028 O  OE1 . GLN C 1 219 ? 30.756  -16.443 -15.301 1.00 40.14  ? 219 GLN C OE1 1 
ATOM   6029 N  NE2 . GLN C 1 219 ? 32.107  -16.915 -13.598 1.00 36.58  ? 219 GLN C NE2 1 
ATOM   6030 N  N   . GLU C 1 220 ? 34.738  -12.600 -14.925 1.00 26.92  ? 220 GLU C N   1 
ATOM   6031 C  CA  . GLU C 1 220 ? 35.335  -11.694 -13.974 1.00 24.27  ? 220 GLU C CA  1 
ATOM   6032 C  C   . GLU C 1 220 ? 36.079  -10.550 -14.660 1.00 19.37  ? 220 GLU C C   1 
ATOM   6033 O  O   . GLU C 1 220 ? 35.933  -9.395  -14.233 1.00 20.67  ? 220 GLU C O   1 
ATOM   6034 C  CB  . GLU C 1 220 ? 36.208  -12.490 -13.001 1.00 28.35  ? 220 GLU C CB  1 
ATOM   6035 C  CG  . GLU C 1 220 ? 35.436  -13.544 -12.193 1.00 28.97  ? 220 GLU C CG  1 
ATOM   6036 C  CD  . GLU C 1 220 ? 35.251  -14.957 -12.767 1.00 32.51  ? 220 GLU C CD  1 
ATOM   6037 O  OE1 . GLU C 1 220 ? 35.735  -15.212 -13.875 1.00 28.83  ? 220 GLU C OE1 1 
ATOM   6038 O  OE2 . GLU C 1 220 ? 34.635  -15.831 -12.078 1.00 29.89  ? 220 GLU C OE2 1 
ATOM   6039 N  N   . GLN C 1 221 ? 36.866  -10.848 -15.715 1.00 18.92  ? 221 GLN C N   1 
ATOM   6040 C  CA  . GLN C 1 221 ? 37.583  -9.821  -16.471 1.00 20.04  ? 221 GLN C CA  1 
ATOM   6041 C  C   . GLN C 1 221 ? 36.582  -8.831  -17.075 1.00 19.74  ? 221 GLN C C   1 
ATOM   6042 O  O   . GLN C 1 221 ? 36.794  -7.600  -17.012 1.00 20.16  ? 221 GLN C O   1 
ATOM   6043 C  CB  . GLN C 1 221 ? 38.505  -10.482 -17.490 1.00 20.64  ? 221 GLN C CB  1 
ATOM   6044 C  CG  . GLN C 1 221 ? 39.754  -11.056 -16.850 1.00 23.89  ? 221 GLN C CG  1 
ATOM   6045 C  CD  . GLN C 1 221 ? 40.573  -11.740 -17.910 1.00 18.38  ? 221 GLN C CD  1 
ATOM   6046 O  OE1 . GLN C 1 221 ? 40.126  -12.726 -18.533 1.00 20.78  ? 221 GLN C OE1 1 
ATOM   6047 N  NE2 . GLN C 1 221 ? 41.787  -11.229 -18.055 1.00 21.49  ? 221 GLN C NE2 1 
ATOM   6048 N  N   . LEU C 1 222 ? 35.493  -9.354  -17.667 1.00 21.42  ? 222 LEU C N   1 
ATOM   6049 C  CA  . LEU C 1 222 ? 34.561  -8.482  -18.373 1.00 20.49  ? 222 LEU C CA  1 
ATOM   6050 C  C   . LEU C 1 222 ? 33.879  -7.535  -17.388 1.00 20.17  ? 222 LEU C C   1 
ATOM   6051 O  O   . LEU C 1 222 ? 33.737  -6.334  -17.637 1.00 21.56  ? 222 LEU C O   1 
ATOM   6052 C  CB  . LEU C 1 222 ? 33.529  -9.334  -19.111 1.00 20.43  ? 222 LEU C CB  1 
ATOM   6053 C  CG  . LEU C 1 222 ? 32.411  -8.593  -19.836 1.00 21.61  ? 222 LEU C CG  1 
ATOM   6054 C  CD1 . LEU C 1 222 ? 33.016  -7.717  -20.911 1.00 20.16  ? 222 LEU C CD1 1 
ATOM   6055 C  CD2 . LEU C 1 222 ? 31.444  -9.561  -20.477 1.00 21.75  ? 222 LEU C CD2 1 
ATOM   6056 N  N   . LEU C 1 223 ? 33.525  -8.093  -16.219 1.00 23.87  ? 223 LEU C N   1 
ATOM   6057 C  CA  . LEU C 1 223 ? 32.798  -7.296  -15.251 1.00 22.77  ? 223 LEU C CA  1 
ATOM   6058 C  C   . LEU C 1 223 ? 33.734  -6.227  -14.710 1.00 20.50  ? 223 LEU C C   1 
ATOM   6059 O  O   . LEU C 1 223 ? 33.292  -5.094  -14.513 1.00 22.89  ? 223 LEU C O   1 
ATOM   6060 C  CB  . LEU C 1 223 ? 32.374  -8.229  -14.124 1.00 23.85  ? 223 LEU C CB  1 
ATOM   6061 C  CG  . LEU C 1 223 ? 31.592  -7.545  -13.017 1.00 28.71  ? 223 LEU C CG  1 
ATOM   6062 C  CD1 . LEU C 1 223 ? 30.313  -6.978  -13.616 1.00 26.98  ? 223 LEU C CD1 1 
ATOM   6063 C  CD2 . LEU C 1 223 ? 31.248  -8.574  -11.951 1.00 25.30  ? 223 LEU C CD2 1 
ATOM   6064 N  N   . ALA C 1 224 ? 35.026  -6.566  -14.558 1.00 21.31  ? 224 ALA C N   1 
ATOM   6065 C  CA  . ALA C 1 224 ? 36.017  -5.591  -14.111 1.00 22.08  ? 224 ALA C CA  1 
ATOM   6066 C  C   . ALA C 1 224 ? 36.115  -4.418  -15.092 1.00 18.44  ? 224 ALA C C   1 
ATOM   6067 O  O   . ALA C 1 224 ? 36.101  -3.256  -14.676 1.00 25.46  ? 224 ALA C O   1 
ATOM   6068 C  CB  . ALA C 1 224 ? 37.345  -6.248  -13.799 1.00 24.45  ? 224 ALA C CB  1 
ATOM   6069 N  N   . LEU C 1 225 ? 36.250  -4.704  -16.391 1.00 20.14  ? 225 LEU C N   1 
ATOM   6070 C  CA  . LEU C 1 225 ? 36.381  -3.661  -17.408 1.00 18.51  ? 225 LEU C CA  1 
ATOM   6071 C  C   . LEU C 1 225 ? 35.132  -2.771  -17.401 1.00 13.47  ? 225 LEU C C   1 
ATOM   6072 O  O   . LEU C 1 225 ? 35.217  -1.525  -17.454 1.00 21.81  ? 225 LEU C O   1 
ATOM   6073 C  CB  . LEU C 1 225 ? 36.486  -4.349  -18.770 1.00 18.73  ? 225 LEU C CB  1 
ATOM   6074 C  CG  . LEU C 1 225 ? 36.510  -3.399  -19.970 1.00 18.61  ? 225 LEU C CG  1 
ATOM   6075 C  CD1 . LEU C 1 225 ? 37.784  -2.552  -19.887 1.00 16.40  ? 225 LEU C CD1 1 
ATOM   6076 C  CD2 . LEU C 1 225 ? 36.536  -4.213  -21.247 1.00 18.38  ? 225 LEU C CD2 1 
ATOM   6077 N  N   . GLU C 1 226 ? 33.966  -3.393  -17.252 1.00 20.47  ? 226 GLU C N   1 
ATOM   6078 C  CA  . GLU C 1 226 ? 32.696  -2.670  -17.287 1.00 18.36  ? 226 GLU C CA  1 
ATOM   6079 C  C   . GLU C 1 226 ? 32.458  -1.769  -16.069 1.00 24.18  ? 226 GLU C C   1 
ATOM   6080 O  O   . GLU C 1 226 ? 31.636  -0.863  -16.127 1.00 21.73  ? 226 GLU C O   1 
ATOM   6081 C  CB  . GLU C 1 226 ? 31.552  -3.673  -17.394 1.00 20.69  ? 226 GLU C CB  1 
ATOM   6082 C  CG  . GLU C 1 226 ? 31.459  -4.332  -18.749 1.00 16.20  ? 226 GLU C CG  1 
ATOM   6083 C  CD  . GLU C 1 226 ? 30.487  -5.499  -18.693 1.00 19.59  ? 226 GLU C CD  1 
ATOM   6084 O  OE1 . GLU C 1 226 ? 30.169  -5.964  -17.529 1.00 22.33  ? 226 GLU C OE1 1 
ATOM   6085 O  OE2 . GLU C 1 226 ? 30.108  -5.973  -19.770 1.00 20.64  ? 226 GLU C OE2 1 
ATOM   6086 N  N   . THR C 1 227 ? 33.197  -1.988  -14.979 1.00 20.55  ? 227 THR C N   1 
ATOM   6087 C  CA  . THR C 1 227 ? 32.882  -1.330  -13.718 1.00 23.98  ? 227 THR C CA  1 
ATOM   6088 C  C   . THR C 1 227 ? 34.045  -0.483  -13.217 1.00 26.82  ? 227 THR C C   1 
ATOM   6089 O  O   . THR C 1 227 ? 33.897  0.226   -12.222 1.00 28.63  ? 227 THR C O   1 
ATOM   6090 C  CB  . THR C 1 227 ? 32.425  -2.328  -12.634 1.00 22.07  ? 227 THR C CB  1 
ATOM   6091 O  OG1 . THR C 1 227 ? 33.477  -3.271  -12.383 1.00 25.69  ? 227 THR C OG1 1 
ATOM   6092 C  CG2 . THR C 1 227 ? 31.114  -3.023  -12.951 1.00 24.98  ? 227 THR C CG2 1 
ATOM   6093 N  N   . ALA C 1 228 ? 35.207  -0.547  -13.883 1.00 26.87  ? 228 ALA C N   1 
ATOM   6094 C  CA  . ALA C 1 228 ? 36.421  0.018   -13.289 1.00 28.19  ? 228 ALA C CA  1 
ATOM   6095 C  C   . ALA C 1 228 ? 36.534  1.519   -13.546 1.00 30.65  ? 228 ALA C C   1 
ATOM   6096 O  O   . ALA C 1 228 ? 37.167  2.239   -12.778 1.00 35.26  ? 228 ALA C O   1 
ATOM   6097 C  CB  . ALA C 1 228 ? 37.631  -0.686  -13.833 1.00 34.38  ? 228 ALA C CB  1 
ATOM   6098 N  N   . LEU C 1 229 ? 35.961  1.987   -14.676 1.00 22.45  ? 229 LEU C N   1 
ATOM   6099 C  CA  . LEU C 1 229 ? 36.363  3.313   -15.126 1.00 25.34  ? 229 LEU C CA  1 
ATOM   6100 C  C   . LEU C 1 229 ? 35.203  4.299   -15.074 1.00 24.71  ? 229 LEU C C   1 
ATOM   6101 O  O   . LEU C 1 229 ? 34.027  3.937   -15.232 1.00 30.77  ? 229 LEU C O   1 
ATOM   6102 C  CB  . LEU C 1 229 ? 36.980  3.279   -16.533 1.00 26.59  ? 229 LEU C CB  1 
ATOM   6103 C  CG  . LEU C 1 229 ? 38.040  2.199   -16.727 1.00 31.49  ? 229 LEU C CG  1 
ATOM   6104 C  CD1 . LEU C 1 229 ? 38.306  1.927   -18.199 1.00 34.97  ? 229 LEU C CD1 1 
ATOM   6105 C  CD2 . LEU C 1 229 ? 39.308  2.559   -15.975 1.00 36.53  ? 229 LEU C CD2 1 
ATOM   6106 N  N   . TYR C 1 230 ? 35.586  5.566   -14.915 1.00 29.65  ? 230 TYR C N   1 
ATOM   6107 C  CA  . TYR C 1 230 ? 34.670  6.694   -14.979 1.00 27.11  ? 230 TYR C CA  1 
ATOM   6108 C  C   . TYR C 1 230 ? 35.088  7.635   -16.108 1.00 28.10  ? 230 TYR C C   1 
ATOM   6109 O  O   . TYR C 1 230 ? 36.270  7.729   -16.432 1.00 23.74  ? 230 TYR C O   1 
ATOM   6110 C  CB  . TYR C 1 230 ? 34.662  7.399   -13.622 1.00 27.79  ? 230 TYR C CB  1 
ATOM   6111 C  CG  . TYR C 1 230 ? 33.871  6.658   -12.572 1.00 30.54  ? 230 TYR C CG  1 
ATOM   6112 C  CD1 . TYR C 1 230 ? 34.303  5.426   -12.098 1.00 32.90  ? 230 TYR C CD1 1 
ATOM   6113 C  CD2 . TYR C 1 230 ? 32.677  7.177   -12.070 1.00 28.40  ? 230 TYR C CD2 1 
ATOM   6114 C  CE1 . TYR C 1 230 ? 33.583  4.724   -11.143 1.00 39.28  ? 230 TYR C CE1 1 
ATOM   6115 C  CE2 . TYR C 1 230 ? 31.934  6.478   -11.133 1.00 37.52  ? 230 TYR C CE2 1 
ATOM   6116 C  CZ  . TYR C 1 230 ? 32.381  5.240   -10.684 1.00 37.73  ? 230 TYR C CZ  1 
ATOM   6117 O  OH  . TYR C 1 230 ? 31.677  4.560   -9.728  1.00 63.43  ? 230 TYR C OH  1 
ATOM   6118 N  N   . CYS C 1 231 ? 34.116  8.377   -16.648 1.00 30.62  ? 231 CYS C N   1 
ATOM   6119 C  CA  . CYS C 1 231 ? 34.417  9.351   -17.679 1.00 28.72  ? 231 CYS C CA  1 
ATOM   6120 C  C   . CYS C 1 231 ? 34.860  10.674  -17.094 1.00 32.07  ? 231 CYS C C   1 
ATOM   6121 O  O   . CYS C 1 231 ? 35.407  11.511  -17.811 1.00 34.99  ? 231 CYS C O   1 
ATOM   6122 C  CB  . CYS C 1 231 ? 33.171  9.617   -18.507 1.00 31.82  ? 231 CYS C CB  1 
ATOM   6123 S  SG  . CYS C 1 231 ? 32.781  8.155   -19.489 1.00 30.69  ? 231 CYS C SG  1 
ATOM   6124 N  N   . THR C 1 232 ? 34.606  10.840  -15.791 1.00 30.99  ? 232 THR C N   1 
ATOM   6125 C  CA  . THR C 1 232 ? 34.694  12.131  -15.119 1.00 30.44  ? 232 THR C CA  1 
ATOM   6126 C  C   . THR C 1 232 ? 35.935  12.152  -14.244 1.00 31.04  ? 232 THR C C   1 
ATOM   6127 O  O   . THR C 1 232 ? 36.468  11.096  -13.931 1.00 31.25  ? 232 THR C O   1 
ATOM   6128 C  CB  . THR C 1 232 ? 33.441  12.298  -14.256 1.00 30.67  ? 232 THR C CB  1 
ATOM   6129 O  OG1 . THR C 1 232 ? 33.139  11.030  -13.653 1.00 28.89  ? 232 THR C OG1 1 
ATOM   6130 C  CG2 . THR C 1 232 ? 32.252  12.739  -15.081 1.00 31.46  ? 232 THR C CG2 1 
ATOM   6131 N  N   . HIS C 1 233 ? 36.370  13.375  -13.891 1.00 38.54  ? 233 HIS C N   1 
ATOM   6132 C  CA  . HIS C 1 233 ? 37.502  13.640  -13.016 1.00 43.28  ? 233 HIS C CA  1 
ATOM   6133 C  C   . HIS C 1 233 ? 37.236  13.059  -11.631 1.00 38.09  ? 233 HIS C C   1 
ATOM   6134 O  O   . HIS C 1 233 ? 36.087  12.910  -11.209 1.00 38.46  ? 233 HIS C O   1 
ATOM   6135 C  CB  . HIS C 1 233 ? 37.831  15.140  -12.993 1.00 51.20  ? 233 HIS C CB  1 
ATOM   6136 C  CG  . HIS C 1 233 ? 38.469  15.638  -14.251 1.00 73.17  ? 233 HIS C CG  1 
ATOM   6137 N  ND1 . HIS C 1 233 ? 37.725  16.020  -15.358 1.00 83.03  ? 233 HIS C ND1 1 
ATOM   6138 C  CD2 . HIS C 1 233 ? 39.768  15.817  -14.594 1.00 81.37  ? 233 HIS C CD2 1 
ATOM   6139 C  CE1 . HIS C 1 233 ? 38.536  16.408  -16.327 1.00 78.08  ? 233 HIS C CE1 1 
ATOM   6140 N  NE2 . HIS C 1 233 ? 39.801  16.296  -15.882 1.00 82.22  ? 233 HIS C NE2 1 
ATOM   6141 N  N   . MET C 1 234 ? 38.321  12.705  -10.939 1.00 40.26  ? 234 MET C N   1 
ATOM   6142 C  CA  . MET C 1 234 ? 38.256  12.037  -9.645  1.00 40.74  ? 234 MET C CA  1 
ATOM   6143 C  C   . MET C 1 234 ? 37.307  12.780  -8.699  1.00 45.22  ? 234 MET C C   1 
ATOM   6144 O  O   . MET C 1 234 ? 36.545  12.141  -7.964  1.00 41.85  ? 234 MET C O   1 
ATOM   6145 C  CB  . MET C 1 234 ? 39.665  11.850  -9.055  1.00 48.97  ? 234 MET C CB  1 
ATOM   6146 C  CG  . MET C 1 234 ? 39.684  11.347  -7.618  1.00 49.99  ? 234 MET C CG  1 
ATOM   6147 S  SD  . MET C 1 234 ? 41.306  10.826  -6.989  1.00 59.85  ? 234 MET C SD  1 
ATOM   6148 C  CE  . MET C 1 234 ? 41.421  9.134   -7.572  1.00 47.02  ? 234 MET C CE  1 
ATOM   6149 N  N   . ASP C 1 235 ? 37.294  14.120  -8.767  1.00 43.60  ? 235 ASP C N   1 
ATOM   6150 C  CA  . ASP C 1 235 ? 36.543  14.870  -7.767  1.00 48.58  ? 235 ASP C CA  1 
ATOM   6151 C  C   . ASP C 1 235 ? 35.291  15.531  -8.346  1.00 42.23  ? 235 ASP C C   1 
ATOM   6152 O  O   . ASP C 1 235 ? 34.727  16.428  -7.744  1.00 46.11  ? 235 ASP C O   1 
ATOM   6153 C  CB  . ASP C 1 235 ? 37.423  15.651  -6.773  1.00 60.23  ? 235 ASP C CB  1 
ATOM   6154 C  CG  . ASP C 1 235 ? 38.671  16.292  -7.358  1.00 57.23  ? 235 ASP C CG  1 
ATOM   6155 O  OD1 . ASP C 1 235 ? 38.518  17.251  -8.142  1.00 61.64  ? 235 ASP C OD1 1 
ATOM   6156 O  OD2 . ASP C 1 235 ? 39.788  15.836  -7.008  1.00 55.99  ? 235 ASP C OD2 1 
ATOM   6157 N  N   . ASP C 1 236 ? 34.796  15.024  -9.470  1.00 47.16  ? 236 ASP C N   1 
ATOM   6158 C  CA  . ASP C 1 236 ? 33.510  15.463  -9.990  1.00 44.92  ? 236 ASP C CA  1 
ATOM   6159 C  C   . ASP C 1 236 ? 32.406  14.955  -9.063  1.00 44.39  ? 236 ASP C C   1 
ATOM   6160 O  O   . ASP C 1 236 ? 32.323  13.744  -8.796  1.00 34.93  ? 236 ASP C O   1 
ATOM   6161 C  CB  . ASP C 1 236 ? 33.305  14.918  -11.403 1.00 40.87  ? 236 ASP C CB  1 
ATOM   6162 C  CG  . ASP C 1 236 ? 32.276  15.658  -12.253 1.00 52.30  ? 236 ASP C CG  1 
ATOM   6163 O  OD1 . ASP C 1 236 ? 31.242  16.090  -11.708 1.00 51.44  ? 236 ASP C OD1 1 
ATOM   6164 O  OD2 . ASP C 1 236 ? 32.520  15.790  -13.465 1.00 55.54  ? 236 ASP C OD2 1 
ATOM   6165 N  N   . PRO C 1 237 ? 31.524  15.854  -8.551  1.00 45.97  ? 237 PRO C N   1 
ATOM   6166 C  CA  . PRO C 1 237 ? 30.445  15.456  -7.642  1.00 51.22  ? 237 PRO C CA  1 
ATOM   6167 C  C   . PRO C 1 237 ? 29.251  14.856  -8.383  1.00 47.04  ? 237 PRO C C   1 
ATOM   6168 O  O   . PRO C 1 237 ? 28.230  14.533  -7.781  1.00 60.10  ? 237 PRO C O   1 
ATOM   6169 C  CB  . PRO C 1 237 ? 30.069  16.787  -6.964  1.00 57.06  ? 237 PRO C CB  1 
ATOM   6170 C  CG  . PRO C 1 237 ? 30.319  17.832  -8.039  1.00 55.36  ? 237 PRO C CG  1 
ATOM   6171 C  CD  . PRO C 1 237 ? 31.506  17.302  -8.827  1.00 59.04  ? 237 PRO C CD  1 
ATOM   6172 N  N   . SER C 1 238 ? 29.395  14.710  -9.702  1.00 50.85  ? 238 SER C N   1 
ATOM   6173 C  CA  . SER C 1 238 ? 28.390  14.050  -10.513 1.00 51.18  ? 238 SER C CA  1 
ATOM   6174 C  C   . SER C 1 238 ? 29.082  12.974  -11.344 1.00 41.03  ? 238 SER C C   1 
ATOM   6175 O  O   . SER C 1 238 ? 29.190  13.119  -12.553 1.00 45.15  ? 238 SER C O   1 
ATOM   6176 C  CB  . SER C 1 238 ? 27.698  15.076  -11.374 1.00 61.25  ? 238 SER C CB  1 
ATOM   6177 O  OG  . SER C 1 238 ? 26.598  14.507  -12.052 1.00 72.38  ? 238 SER C OG  1 
ATOM   6178 N  N   . PRO C 1 239 ? 29.611  11.885  -10.740 1.00 30.73  ? 239 PRO C N   1 
ATOM   6179 C  CA  . PRO C 1 239 ? 30.434  10.943  -11.493 1.00 35.40  ? 239 PRO C CA  1 
ATOM   6180 C  C   . PRO C 1 239 ? 29.575  10.268  -12.557 1.00 35.83  ? 239 PRO C C   1 
ATOM   6181 O  O   . PRO C 1 239 ? 28.397  10.001  -12.314 1.00 36.24  ? 239 PRO C O   1 
ATOM   6182 C  CB  . PRO C 1 239 ? 30.879  9.896   -10.464 1.00 32.90  ? 239 PRO C CB  1 
ATOM   6183 C  CG  . PRO C 1 239 ? 29.877  10.033  -9.337  1.00 41.25  ? 239 PRO C CG  1 
ATOM   6184 C  CD  . PRO C 1 239 ? 29.494  11.502  -9.324  1.00 38.64  ? 239 PRO C CD  1 
ATOM   6185 N  N   . ARG C 1 240 ? 30.171  10.037  -13.734 1.00 36.50  ? 240 ARG C N   1 
ATOM   6186 C  CA  . ARG C 1 240 ? 29.556  9.220   -14.772 1.00 39.77  ? 240 ARG C CA  1 
ATOM   6187 C  C   . ARG C 1 240 ? 30.452  8.005   -14.990 1.00 38.39  ? 240 ARG C C   1 
ATOM   6188 O  O   . ARG C 1 240 ? 31.645  8.183   -15.271 1.00 26.58  ? 240 ARG C O   1 
ATOM   6189 C  CB  . ARG C 1 240 ? 29.405  9.971   -16.111 1.00 44.03  ? 240 ARG C CB  1 
ATOM   6190 C  CG  . ARG C 1 240 ? 28.361  11.077  -16.143 1.00 42.55  ? 240 ARG C CG  1 
ATOM   6191 N  N   . GLU C 1 241 ? 29.855  6.804   -14.863 1.00 29.16  ? 241 GLU C N   1 
ATOM   6192 C  CA  . GLU C 1 241 ? 30.501  5.560   -15.249 1.00 29.29  ? 241 GLU C CA  1 
ATOM   6193 C  C   . GLU C 1 241 ? 30.886  5.621   -16.721 1.00 26.62  ? 241 GLU C C   1 
ATOM   6194 O  O   . GLU C 1 241 ? 30.158  6.192   -17.548 1.00 28.39  ? 241 GLU C O   1 
ATOM   6195 C  CB  . GLU C 1 241 ? 29.577  4.369   -15.065 1.00 26.54  ? 241 GLU C CB  1 
ATOM   6196 C  CG  . GLU C 1 241 ? 29.335  3.972   -13.630 1.00 32.60  ? 241 GLU C CG  1 
ATOM   6197 C  CD  . GLU C 1 241 ? 28.442  2.756   -13.441 1.00 42.26  ? 241 GLU C CD  1 
ATOM   6198 O  OE1 . GLU C 1 241 ? 27.592  2.482   -14.316 1.00 50.18  ? 241 GLU C OE1 1 
ATOM   6199 O  OE2 . GLU C 1 241 ? 28.609  2.069   -12.422 1.00 44.89  ? 241 GLU C OE2 1 
ATOM   6200 N  N   . MET C 1 242 ? 32.046  5.036   -17.035 1.00 26.57  ? 242 MET C N   1 
ATOM   6201 C  CA  . MET C 1 242 ? 32.442  4.793   -18.418 1.00 23.38  ? 242 MET C CA  1 
ATOM   6202 C  C   . MET C 1 242 ? 31.900  3.434   -18.856 1.00 16.57  ? 242 MET C C   1 
ATOM   6203 O  O   . MET C 1 242 ? 32.524  2.392   -18.651 1.00 22.73  ? 242 MET C O   1 
ATOM   6204 C  CB  . MET C 1 242 ? 33.964  4.782   -18.590 1.00 21.48  ? 242 MET C CB  1 
ATOM   6205 C  CG  . MET C 1 242 ? 34.370  4.863   -20.062 1.00 21.16  ? 242 MET C CG  1 
ATOM   6206 S  SD  . MET C 1 242 ? 36.153  4.840   -20.322 1.00 21.00  ? 242 MET C SD  1 
ATOM   6207 C  CE  . MET C 1 242 ? 36.656  6.456   -19.721 1.00 20.48  ? 242 MET C CE  1 
ATOM   6208 N  N   . ILE C 1 243 ? 30.734  3.510   -19.497 1.00 16.37  ? 243 ILE C N   1 
ATOM   6209 C  CA  . ILE C 1 243 ? 30.010  2.338   -19.960 1.00 17.40  ? 243 ILE C CA  1 
ATOM   6210 C  C   . ILE C 1 243 ? 29.383  2.683   -21.314 1.00 13.54  ? 243 ILE C C   1 
ATOM   6211 O  O   . ILE C 1 243 ? 29.169  3.863   -21.663 1.00 15.41  ? 243 ILE C O   1 
ATOM   6212 C  CB  . ILE C 1 243 ? 28.889  1.909   -18.979 1.00 18.28  ? 243 ILE C CB  1 
ATOM   6213 C  CG1 . ILE C 1 243 ? 27.974  3.091   -18.626 1.00 19.18  ? 243 ILE C CG1 1 
ATOM   6214 C  CG2 . ILE C 1 243 ? 29.470  1.216   -17.738 1.00 20.99  ? 243 ILE C CG2 1 
ATOM   6215 C  CD1 . ILE C 1 243 ? 26.720  2.751   -17.804 1.00 19.30  ? 243 ILE C CD1 1 
ATOM   6216 N  N   . ASN C 1 244 ? 29.079  1.654   -22.067 1.00 13.23  ? 244 ASN C N   1 
ATOM   6217 C  CA  . ASN C 1 244 ? 28.376  1.803   -23.347 1.00 14.41  ? 244 ASN C CA  1 
ATOM   6218 C  C   . ASN C 1 244 ? 29.113  2.781   -24.280 1.00 13.56  ? 244 ASN C C   1 
ATOM   6219 O  O   . ASN C 1 244 ? 28.508  3.613   -24.949 1.00 12.70  ? 244 ASN C O   1 
ATOM   6220 C  CB  . ASN C 1 244 ? 26.926  2.255   -23.141 1.00 16.74  ? 244 ASN C CB  1 
ATOM   6221 C  CG  . ASN C 1 244 ? 26.163  1.348   -22.197 1.00 20.77  ? 244 ASN C CG  1 
ATOM   6222 O  OD1 . ASN C 1 244 ? 26.320  0.128   -22.250 1.00 19.96  ? 244 ASN C OD1 1 
ATOM   6223 N  ND2 . ASN C 1 244 ? 25.338  1.938   -21.324 1.00 22.19  ? 244 ASN C ND2 1 
ATOM   6224 N  N   . ASN C 1 245 ? 30.442  2.657   -24.354 1.00 11.66  ? 245 ASN C N   1 
ATOM   6225 C  CA  . ASN C 1 245 ? 31.285  3.585   -25.089 1.00 10.93  ? 245 ASN C CA  1 
ATOM   6226 C  C   . ASN C 1 245 ? 31.537  3.042   -26.482 1.00 10.27  ? 245 ASN C C   1 
ATOM   6227 O  O   . ASN C 1 245 ? 32.676  2.863   -26.875 1.00 11.33  ? 245 ASN C O   1 
ATOM   6228 C  CB  . ASN C 1 245 ? 32.564  3.928   -24.325 1.00 13.95  ? 245 ASN C CB  1 
ATOM   6229 C  CG  . ASN C 1 245 ? 33.469  2.726   -24.075 1.00 16.95  ? 245 ASN C CG  1 
ATOM   6230 O  OD1 . ASN C 1 245 ? 33.004  1.609   -24.010 1.00 14.40  ? 245 ASN C OD1 1 
ATOM   6231 N  ND2 . ASN C 1 245 ? 34.733  2.956   -23.792 1.00 16.79  ? 245 ASN C ND2 1 
ATOM   6232 N  N   . PHE C 1 246 ? 30.444  2.718   -27.180 1.00 9.85   ? 246 PHE C N   1 
ATOM   6233 C  CA  . PHE C 1 246 ? 30.564  2.165   -28.522 1.00 10.53  ? 246 PHE C CA  1 
ATOM   6234 C  C   . PHE C 1 246 ? 29.609  2.996   -29.360 1.00 10.61  ? 246 PHE C C   1 
ATOM   6235 O  O   . PHE C 1 246 ? 28.544  3.429   -28.866 1.00 10.91  ? 246 PHE C O   1 
ATOM   6236 C  CB  . PHE C 1 246 ? 30.193  0.652   -28.551 1.00 9.43   ? 246 PHE C CB  1 
ATOM   6237 C  CG  . PHE C 1 246 ? 28.782  0.321   -28.075 1.00 9.23   ? 246 PHE C CG  1 
ATOM   6238 C  CD1 . PHE C 1 246 ? 28.517  0.099   -26.723 1.00 11.67  ? 246 PHE C CD1 1 
ATOM   6239 C  CD2 . PHE C 1 246 ? 27.715  0.211   -28.991 1.00 11.19  ? 246 PHE C CD2 1 
ATOM   6240 C  CE1 . PHE C 1 246 ? 27.220  -0.182  -26.298 1.00 13.89  ? 246 PHE C CE1 1 
ATOM   6241 C  CE2 . PHE C 1 246 ? 26.414  -0.006  -28.540 1.00 10.94  ? 246 PHE C CE2 1 
ATOM   6242 C  CZ  . PHE C 1 246 ? 26.161  -0.242  -27.191 1.00 11.49  ? 246 PHE C CZ  1 
ATOM   6243 N  N   . ARG C 1 247 ? 29.891  3.061   -30.656 1.00 9.02   ? 247 ARG C N   1 
ATOM   6244 C  CA  . ARG C 1 247 ? 28.950  3.679   -31.573 1.00 8.79   ? 247 ARG C CA  1 
ATOM   6245 C  C   . ARG C 1 247 ? 27.965  2.656   -32.057 1.00 8.13   ? 247 ARG C C   1 
ATOM   6246 O  O   . ARG C 1 247 ? 28.359  1.543   -32.365 1.00 9.19   ? 247 ARG C O   1 
ATOM   6247 C  CB  . ARG C 1 247 ? 29.747  4.351   -32.720 1.00 9.37   ? 247 ARG C CB  1 
ATOM   6248 C  CG  . ARG C 1 247 ? 28.977  5.340   -33.571 1.00 8.81   ? 247 ARG C CG  1 
ATOM   6249 C  CD  . ARG C 1 247 ? 29.711  5.806   -34.815 1.00 9.66   ? 247 ARG C CD  1 
ATOM   6250 N  NE  . ARG C 1 247 ? 29.162  7.027   -35.391 1.00 8.71   ? 247 ARG C NE  1 
ATOM   6251 C  CZ  . ARG C 1 247 ? 29.604  7.555   -36.537 1.00 8.00   ? 247 ARG C CZ  1 
ATOM   6252 N  NH1 . ARG C 1 247 ? 30.665  7.051   -37.146 1.00 8.40   ? 247 ARG C NH1 1 
ATOM   6253 N  NH2 . ARG C 1 247 ? 29.080  8.710   -36.994 1.00 9.49   ? 247 ARG C NH2 1 
ATOM   6254 N  N   . GLN C 1 248 ? 26.740  3.120   -32.315 1.00 8.25   ? 248 GLN C N   1 
ATOM   6255 C  CA  . GLN C 1 248 ? 25.802  2.274   -33.020 1.00 8.55   ? 248 GLN C CA  1 
ATOM   6256 C  C   . GLN C 1 248 ? 26.323  1.949   -34.432 1.00 8.02   ? 248 GLN C C   1 
ATOM   6257 O  O   . GLN C 1 248 ? 26.975  2.758   -35.070 1.00 9.23   ? 248 GLN C O   1 
ATOM   6258 C  CB  . GLN C 1 248 ? 24.451  2.988   -33.157 1.00 9.12   ? 248 GLN C CB  1 
ATOM   6259 C  CG  . GLN C 1 248 ? 23.720  3.286   -31.859 1.00 8.25   ? 248 GLN C CG  1 
ATOM   6260 C  CD  . GLN C 1 248 ? 23.348  2.074   -31.045 1.00 8.95   ? 248 GLN C CD  1 
ATOM   6261 O  OE1 . GLN C 1 248 ? 24.069  1.727   -30.106 1.00 11.15  ? 248 GLN C OE1 1 
ATOM   6262 N  NE2 . GLN C 1 248 ? 22.233  1.414   -31.345 1.00 13.09  ? 248 GLN C NE2 1 
ATOM   6263 N  N   . VAL C 1 249 ? 25.914  0.806   -34.979 1.00 8.71   ? 249 VAL C N   1 
ATOM   6264 C  CA  . VAL C 1 249 ? 26.224  0.489   -36.373 1.00 8.62   ? 249 VAL C CA  1 
ATOM   6265 C  C   . VAL C 1 249 ? 25.582  1.489   -37.353 1.00 10.13  ? 249 VAL C C   1 
ATOM   6266 O  O   . VAL C 1 249 ? 24.464  1.971   -37.195 1.00 9.53   ? 249 VAL C O   1 
ATOM   6267 C  CB  . VAL C 1 249 ? 25.845  -0.949  -36.703 1.00 10.56  ? 249 VAL C CB  1 
ATOM   6268 C  CG1 . VAL C 1 249 ? 26.690  -1.935  -35.937 1.00 12.12  ? 249 VAL C CG1 1 
ATOM   6269 C  CG2 . VAL C 1 249 ? 24.361  -1.179  -36.624 1.00 14.92  ? 249 VAL C CG2 1 
ATOM   6270 N  N   . GLN C 1 250 ? 26.261  1.685   -38.449 1.00 8.85   ? 250 GLN C N   1 
ATOM   6271 C  CA  . GLN C 1 250 ? 25.896  2.603   -39.503 1.00 8.97   ? 250 GLN C CA  1 
ATOM   6272 C  C   . GLN C 1 250 ? 25.317  1.867   -40.685 1.00 10.22  ? 250 GLN C C   1 
ATOM   6273 O  O   . GLN C 1 250 ? 25.678  0.720   -40.945 1.00 10.36  ? 250 GLN C O   1 
ATOM   6274 C  CB  . GLN C 1 250 ? 27.148  3.324   -39.994 1.00 8.14   ? 250 GLN C CB  1 
ATOM   6275 C  CG  . GLN C 1 250 ? 27.951  3.921   -38.828 1.00 10.12  ? 250 GLN C CG  1 
ATOM   6276 C  CD  . GLN C 1 250 ? 27.182  5.077   -38.227 1.00 8.67   ? 250 GLN C CD  1 
ATOM   6277 O  OE1 . GLN C 1 250 ? 26.977  6.115   -38.902 1.00 9.47   ? 250 GLN C OE1 1 
ATOM   6278 N  NE2 . GLN C 1 250 ? 26.946  5.016   -36.907 1.00 9.65   ? 250 GLN C NE2 1 
ATOM   6279 N  N   . LYS C 1 251 ? 24.445  2.527   -41.439 1.00 9.87   ? 251 LYS C N   1 
ATOM   6280 C  CA  . LYS C 1 251 ? 24.023  1.905   -42.685 1.00 10.70  ? 251 LYS C CA  1 
ATOM   6281 C  C   . LYS C 1 251 ? 25.242  1.706   -43.577 1.00 9.69   ? 251 LYS C C   1 
ATOM   6282 O  O   . LYS C 1 251 ? 26.151  2.537   -43.619 1.00 11.24  ? 251 LYS C O   1 
ATOM   6283 C  CB  . LYS C 1 251 ? 23.007  2.782   -43.399 1.00 11.58  ? 251 LYS C CB  1 
ATOM   6284 C  CG  . LYS C 1 251 ? 21.659  2.831   -42.699 1.00 10.54  ? 251 LYS C CG  1 
ATOM   6285 C  CD  . LYS C 1 251 ? 20.689  3.766   -43.309 1.00 13.23  ? 251 LYS C CD  1 
ATOM   6286 C  CE  . LYS C 1 251 ? 19.234  3.607   -42.901 1.00 9.68   ? 251 LYS C CE  1 
ATOM   6287 N  NZ  . LYS C 1 251 ? 19.096  3.694   -41.427 1.00 9.26   ? 251 LYS C NZ  1 
ATOM   6288 N  N   . PHE C 1 252 ? 25.193  0.639   -44.372 1.00 11.51  ? 252 PHE C N   1 
ATOM   6289 C  CA  . PHE C 1 252 ? 26.283  0.259   -45.268 1.00 14.14  ? 252 PHE C CA  1 
ATOM   6290 C  C   . PHE C 1 252 ? 25.611  -0.404  -46.482 1.00 22.61  ? 252 PHE C C   1 
ATOM   6291 O  O   . PHE C 1 252 ? 25.225  -1.577  -46.452 1.00 25.90  ? 252 PHE C O   1 
ATOM   6292 C  CB  . PHE C 1 252 ? 27.085  -0.862  -44.588 1.00 14.48  ? 252 PHE C CB  1 
ATOM   6293 C  CG  . PHE C 1 252 ? 28.392  -1.249  -45.213 1.00 14.27  ? 252 PHE C CG  1 
ATOM   6294 C  CD1 . PHE C 1 252 ? 29.515  -0.442  -45.184 1.00 14.32  ? 252 PHE C CD1 1 
ATOM   6295 C  CD2 . PHE C 1 252 ? 28.496  -2.490  -45.830 1.00 15.48  ? 252 PHE C CD2 1 
ATOM   6296 C  CE1 . PHE C 1 252 ? 30.725  -0.909  -45.700 1.00 16.33  ? 252 PHE C CE1 1 
ATOM   6297 C  CE2 . PHE C 1 252 ? 29.688  -2.930  -46.402 1.00 16.28  ? 252 PHE C CE2 1 
ATOM   6298 C  CZ  . PHE C 1 252 ? 30.815  -2.144  -46.336 1.00 16.53  ? 252 PHE C CZ  1 
ATOM   6299 N  N   . ASP C 1 253 ? 25.352  0.382   -47.506 1.00 27.31  ? 253 ASP C N   1 
ATOM   6300 C  CA  . ASP C 1 253 ? 24.517  -0.137  -48.592 1.00 30.37  ? 253 ASP C CA  1 
ATOM   6301 C  C   . ASP C 1 253 ? 25.264  -0.126  -49.919 1.00 22.96  ? 253 ASP C C   1 
ATOM   6302 O  O   . ASP C 1 253 ? 26.126  0.732   -50.176 1.00 26.58  ? 253 ASP C O   1 
ATOM   6303 C  CB  . ASP C 1 253 ? 23.152  0.549   -48.608 1.00 33.33  ? 253 ASP C CB  1 
ATOM   6304 C  CG  . ASP C 1 253 ? 22.138  -0.046  -49.580 1.00 40.98  ? 253 ASP C CG  1 
ATOM   6305 O  OD1 . ASP C 1 253 ? 21.753  -1.225  -49.408 1.00 43.16  ? 253 ASP C OD1 1 
ATOM   6306 O  OD2 . ASP C 1 253 ? 21.706  0.695   -50.488 1.00 46.60  ? 253 ASP C OD2 1 
ATOM   6307 N  N   A GLU C 1 254 ? 24.960  -1.141  -50.730 0.50 24.14  ? 254 GLU C N   1 
ATOM   6308 N  N   B GLU C 1 254 ? 24.976  -1.143  -50.732 0.50 24.22  ? 254 GLU C N   1 
ATOM   6309 C  CA  A GLU C 1 254 ? 25.578  -1.301  -52.027 0.50 23.48  ? 254 GLU C CA  1 
ATOM   6310 C  CA  B GLU C 1 254 ? 25.594  -1.276  -52.041 0.50 23.78  ? 254 GLU C CA  1 
ATOM   6311 C  C   A GLU C 1 254 ? 27.095  -1.342  -51.838 0.50 20.51  ? 254 GLU C C   1 
ATOM   6312 C  C   B GLU C 1 254 ? 27.108  -1.368  -51.854 0.50 20.77  ? 254 GLU C C   1 
ATOM   6313 O  O   A GLU C 1 254 ? 27.844  -0.805  -52.669 0.50 24.70  ? 254 GLU C O   1 
ATOM   6314 O  O   B GLU C 1 254 ? 27.857  -0.819  -52.669 0.50 24.77  ? 254 GLU C O   1 
ATOM   6315 C  CB  A GLU C 1 254 ? 25.149  -0.174  -52.969 0.50 25.22  ? 254 GLU C CB  1 
ATOM   6316 C  CB  B GLU C 1 254 ? 25.207  -0.096  -52.943 0.50 25.84  ? 254 GLU C CB  1 
ATOM   6317 C  CG  A GLU C 1 254 ? 23.670  -0.134  -53.305 0.50 30.88  ? 254 GLU C CG  1 
ATOM   6318 C  CG  B GLU C 1 254 ? 23.731  -0.055  -53.295 0.50 33.38  ? 254 GLU C CG  1 
ATOM   6319 C  CD  A GLU C 1 254 ? 23.501  0.799   -54.486 0.50 33.81  ? 254 GLU C CD  1 
ATOM   6320 C  CD  B GLU C 1 254 ? 23.239  -1.369  -53.873 0.50 38.98  ? 254 GLU C CD  1 
ATOM   6321 O  OE1 A GLU C 1 254 ? 23.879  0.396   -55.605 0.50 46.74  ? 254 GLU C OE1 1 
ATOM   6322 O  OE1 B GLU C 1 254 ? 24.073  -2.122  -54.426 0.50 54.19  ? 254 GLU C OE1 1 
ATOM   6323 O  OE2 A GLU C 1 254 ? 23.046  1.939   -54.287 0.50 39.00  ? 254 GLU C OE2 1 
ATOM   6324 O  OE2 B GLU C 1 254 ? 22.048  -1.661  -53.745 0.50 40.12  ? 254 GLU C OE2 1 
ATOM   6325 N  N   . ARG C 1 255 ? 27.551  -1.966  -50.736 1.00 22.03  ? 255 ARG C N   1 
ATOM   6326 C  CA  . ARG C 1 255 ? 28.984  -2.105  -50.517 1.00 22.60  ? 255 ARG C CA  1 
ATOM   6327 C  C   . ARG C 1 255 ? 29.287  -3.517  -50.034 1.00 22.92  ? 255 ARG C C   1 
ATOM   6328 O  O   . ARG C 1 255 ? 28.404  -4.200  -49.527 1.00 20.68  ? 255 ARG C O   1 
ATOM   6329 C  CB  . ARG C 1 255 ? 29.518  -1.064  -49.522 1.00 19.97  ? 255 ARG C CB  1 
ATOM   6330 C  CG  . ARG C 1 255 ? 29.352  0.381   -49.960 1.00 21.76  ? 255 ARG C CG  1 
ATOM   6331 C  CD  . ARG C 1 255 ? 29.920  1.290   -48.874 1.00 22.85  ? 255 ARG C CD  1 
ATOM   6332 N  NE  . ARG C 1 255 ? 31.338  0.964   -48.753 1.00 24.60  ? 255 ARG C NE  1 
ATOM   6333 C  CZ  . ARG C 1 255 ? 32.091  1.260   -47.686 1.00 22.05  ? 255 ARG C CZ  1 
ATOM   6334 N  NH1 . ARG C 1 255 ? 31.534  1.909   -46.658 1.00 20.42  ? 255 ARG C NH1 1 
ATOM   6335 N  NH2 . ARG C 1 255 ? 33.375  0.890   -47.641 1.00 14.72  ? 255 ARG C NH2 1 
ATOM   6336 N  N   . LEU C 1 256 ? 30.556  -3.934  -50.222 1.00 20.96  ? 256 LEU C N   1 
ATOM   6337 C  CA  . LEU C 1 256 ? 30.964  -5.245  -49.750 1.00 20.25  ? 256 LEU C CA  1 
ATOM   6338 C  C   . LEU C 1 256 ? 31.972  -5.140  -48.615 1.00 19.03  ? 256 LEU C C   1 
ATOM   6339 O  O   . LEU C 1 256 ? 32.653  -4.115  -48.396 1.00 22.41  ? 256 LEU C O   1 
ATOM   6340 C  CB  . LEU C 1 256 ? 31.557  -6.074  -50.902 1.00 20.59  ? 256 LEU C CB  1 
ATOM   6341 C  CG  . LEU C 1 256 ? 30.605  -6.394  -52.058 1.00 28.43  ? 256 LEU C CG  1 
ATOM   6342 C  CD1 . LEU C 1 256 ? 31.336  -7.061  -53.215 1.00 31.02  ? 256 LEU C CD1 1 
ATOM   6343 C  CD2 . LEU C 1 256 ? 29.471  -7.290  -51.573 1.00 31.90  ? 256 LEU C CD2 1 
ATOM   6344 N  N   . VAL C 1 257 ? 32.014  -6.246  -47.874 1.00 17.86  ? 257 VAL C N   1 
ATOM   6345 C  CA  . VAL C 1 257 ? 33.053  -6.500  -46.906 1.00 14.57  ? 257 VAL C CA  1 
ATOM   6346 C  C   . VAL C 1 257 ? 33.834  -7.685  -47.455 1.00 15.72  ? 257 VAL C C   1 
ATOM   6347 O  O   . VAL C 1 257 ? 33.281  -8.760  -47.771 1.00 16.55  ? 257 VAL C O   1 
ATOM   6348 C  CB  . VAL C 1 257 ? 32.490  -6.864  -45.523 1.00 14.63  ? 257 VAL C CB  1 
ATOM   6349 C  CG1 . VAL C 1 257 ? 33.644  -7.271  -44.619 1.00 16.11  ? 257 VAL C CG1 1 
ATOM   6350 C  CG2 . VAL C 1 257 ? 31.735  -5.692  -44.935 1.00 18.38  ? 257 VAL C CG2 1 
ATOM   6351 N  N   . TYR C 1 258 ? 35.123  -7.452  -47.672 1.00 14.16  ? 258 TYR C N   1 
ATOM   6352 C  CA  . TYR C 1 258 ? 35.944  -8.508  -48.247 1.00 15.60  ? 258 TYR C CA  1 
ATOM   6353 C  C   . TYR C 1 258 ? 36.448  -9.421  -47.133 1.00 16.42  ? 258 TYR C C   1 
ATOM   6354 O  O   . TYR C 1 258 ? 36.723  -8.969  -46.022 1.00 18.16  ? 258 TYR C O   1 
ATOM   6355 C  CB  . TYR C 1 258 ? 37.057  -7.884  -49.093 1.00 17.35  ? 258 TYR C CB  1 
ATOM   6356 C  CG  . TYR C 1 258 ? 36.482  -6.965  -50.131 1.00 19.13  ? 258 TYR C CG  1 
ATOM   6357 C  CD1 . TYR C 1 258 ? 35.974  -7.468  -51.322 1.00 21.82  ? 258 TYR C CD1 1 
ATOM   6358 C  CD2 . TYR C 1 258 ? 36.353  -5.613  -49.869 1.00 21.49  ? 258 TYR C CD2 1 
ATOM   6359 C  CE1 . TYR C 1 258 ? 35.381  -6.625  -52.252 1.00 25.05  ? 258 TYR C CE1 1 
ATOM   6360 C  CE2 . TYR C 1 258 ? 35.768  -4.752  -50.781 1.00 25.28  ? 258 TYR C CE2 1 
ATOM   6361 C  CZ  . TYR C 1 258 ? 35.295  -5.263  -51.984 1.00 23.22  ? 258 TYR C CZ  1 
ATOM   6362 O  OH  . TYR C 1 258 ? 34.669  -4.435  -52.862 1.00 36.08  ? 258 TYR C OH  1 
ATOM   6363 N  N   . THR C 1 259 ? 36.561  -10.722 -47.456 1.00 15.55  ? 259 THR C N   1 
ATOM   6364 C  CA  . THR C 1 259 ? 37.029  -11.694 -46.484 1.00 16.08  ? 259 THR C CA  1 
ATOM   6365 C  C   . THR C 1 259 ? 38.232  -12.451 -47.032 1.00 13.11  ? 259 THR C C   1 
ATOM   6366 O  O   . THR C 1 259 ? 38.362  -12.657 -48.244 1.00 17.34  ? 259 THR C O   1 
ATOM   6367 C  CB  . THR C 1 259 ? 35.932  -12.677 -46.069 1.00 16.49  ? 259 THR C CB  1 
ATOM   6368 O  OG1 . THR C 1 259 ? 35.553  -13.348 -47.273 1.00 19.42  ? 259 THR C OG1 1 
ATOM   6369 C  CG2 . THR C 1 259 ? 34.727  -11.990 -45.449 1.00 16.22  ? 259 THR C CG2 1 
ATOM   6370 N  N   . SER C 1 260 ? 39.178  -12.702 -46.104 1.00 13.80  ? 260 SER C N   1 
ATOM   6371 C  CA  . SER C 1 260 ? 40.366  -13.473 -46.500 1.00 14.53  ? 260 SER C CA  1 
ATOM   6372 C  C   . SER C 1 260 ? 40.070  -14.973 -46.476 1.00 16.19  ? 260 SER C C   1 
ATOM   6373 O  O   . SER C 1 260 ? 40.935  -15.831 -46.735 1.00 20.11  ? 260 SER C O   1 
ATOM   6374 C  CB  . SER C 1 260 ? 41.548  -13.204 -45.581 1.00 16.31  ? 260 SER C CB  1 
ATOM   6375 O  OG  . SER C 1 260 ? 41.181  -13.625 -44.275 1.00 14.14  ? 260 SER C OG  1 
ATOM   6376 N  N   . PHE C 1 261 ? 38.857  -15.290 -46.068 1.00 17.69  ? 261 PHE C N   1 
ATOM   6377 C  CA  . PHE C 1 261 ? 38.444  -16.674 -46.023 1.00 17.12  ? 261 PHE C CA  1 
ATOM   6378 C  C   . PHE C 1 261 ? 37.200  -16.871 -46.880 1.00 17.93  ? 261 PHE C C   1 
ATOM   6379 O  O   . PHE C 1 261 ? 36.478  -15.923 -47.148 1.00 20.99  ? 261 PHE C O   1 
ATOM   6380 C  CB  . PHE C 1 261 ? 38.125  -17.056 -44.563 1.00 19.08  ? 261 PHE C CB  1 
ATOM   6381 C  CG  . PHE C 1 261 ? 37.152  -16.152 -43.849 1.00 16.99  ? 261 PHE C CG  1 
ATOM   6382 C  CD1 . PHE C 1 261 ? 37.574  -14.987 -43.200 1.00 17.33  ? 261 PHE C CD1 1 
ATOM   6383 C  CD2 . PHE C 1 261 ? 35.788  -16.427 -43.895 1.00 19.48  ? 261 PHE C CD2 1 
ATOM   6384 C  CE1 . PHE C 1 261 ? 36.638  -14.166 -42.566 1.00 18.99  ? 261 PHE C CE1 1 
ATOM   6385 C  CE2 . PHE C 1 261 ? 34.880  -15.605 -43.233 1.00 21.65  ? 261 PHE C CE2 1 
ATOM   6386 C  CZ  . PHE C 1 261 ? 35.278  -14.449 -42.603 1.00 20.42  ? 261 PHE C CZ  1 
ATOM   6387 N  N   . SER C 1 262 ? 36.938  -18.127 -47.240 1.00 20.79  ? 262 SER C N   1 
ATOM   6388 C  CA  . SER C 1 262 ? 35.675  -18.570 -47.792 1.00 26.41  ? 262 SER C CA  1 
ATOM   6389 C  C   . SER C 1 262 ? 35.114  -19.629 -46.842 1.00 36.43  ? 262 SER C C   1 
ATOM   6390 O  O   . SER C 1 262 ? 33.998  -19.392 -46.357 1.00 45.77  ? 262 SER C O   1 
ATOM   6391 C  CB  . SER C 1 262 ? 35.905  -19.094 -49.162 1.00 38.52  ? 262 SER C CB  1 
ATOM   6392 O  OG  . SER C 1 262 ? 35.049  -20.197 -49.382 1.00 45.81  ? 262 SER C OG  1 
ATOM   6393 N  N   . LYS D 1 3   ? 14.311  19.233  -45.735 1.00 49.14  ? 3   LYS D N   1 
ATOM   6394 C  CA  . LYS D 1 3   ? 14.881  18.301  -46.749 1.00 41.56  ? 3   LYS D CA  1 
ATOM   6395 C  C   . LYS D 1 3   ? 15.724  17.230  -46.064 1.00 23.98  ? 3   LYS D C   1 
ATOM   6396 O  O   . LYS D 1 3   ? 16.627  16.650  -46.705 1.00 25.02  ? 3   LYS D O   1 
ATOM   6397 C  CB  . LYS D 1 3   ? 15.808  19.021  -47.718 1.00 38.26  ? 3   LYS D CB  1 
ATOM   6398 C  CG  . LYS D 1 3   ? 16.757  20.034  -47.103 1.00 43.63  ? 3   LYS D CG  1 
ATOM   6399 C  CD  . LYS D 1 3   ? 17.371  20.913  -48.182 1.00 48.80  ? 3   LYS D CD  1 
ATOM   6400 C  CE  . LYS D 1 3   ? 18.667  20.334  -48.701 1.00 46.91  ? 3   LYS D CE  1 
ATOM   6401 N  NZ  . LYS D 1 3   ? 19.729  20.490  -47.667 1.00 32.53  ? 3   LYS D NZ  1 
ATOM   6402 N  N   . TRP D 1 4   ? 15.409  16.956  -44.774 1.00 18.16  ? 4   TRP D N   1 
ATOM   6403 C  CA  . TRP D 1 4   ? 15.977  15.762  -44.136 1.00 13.48  ? 4   TRP D CA  1 
ATOM   6404 C  C   . TRP D 1 4   ? 15.713  14.514  -44.981 1.00 11.54  ? 4   TRP D C   1 
ATOM   6405 O  O   . TRP D 1 4   ? 14.730  14.491  -45.736 1.00 13.43  ? 4   TRP D O   1 
ATOM   6406 C  CB  . TRP D 1 4   ? 15.509  15.552  -42.692 1.00 13.80  ? 4   TRP D CB  1 
ATOM   6407 C  CG  . TRP D 1 4   ? 14.044  15.289  -42.514 1.00 12.39  ? 4   TRP D CG  1 
ATOM   6408 C  CD1 . TRP D 1 4   ? 13.060  16.207  -42.308 1.00 10.87  ? 4   TRP D CD1 1 
ATOM   6409 C  CD2 . TRP D 1 4   ? 13.386  13.992  -42.515 1.00 9.85   ? 4   TRP D CD2 1 
ATOM   6410 N  NE1 . TRP D 1 4   ? 11.860  15.599  -42.100 1.00 12.85  ? 4   TRP D NE1 1 
ATOM   6411 C  CE2 . TRP D 1 4   ? 12.024  14.221  -42.232 1.00 10.79  ? 4   TRP D CE2 1 
ATOM   6412 C  CE3 . TRP D 1 4   ? 13.843  12.667  -42.632 1.00 9.11   ? 4   TRP D CE3 1 
ATOM   6413 C  CZ2 . TRP D 1 4   ? 11.125  13.171  -42.086 1.00 12.43  ? 4   TRP D CZ2 1 
ATOM   6414 C  CZ3 . TRP D 1 4   ? 12.944  11.626  -42.522 1.00 10.83  ? 4   TRP D CZ3 1 
ATOM   6415 C  CH2 . TRP D 1 4   ? 11.592  11.875  -42.269 1.00 11.44  ? 4   TRP D CH2 1 
ATOM   6416 N  N   . THR D 1 5   ? 16.674  13.570  -44.954 1.00 12.25  ? 5   THR D N   1 
ATOM   6417 C  CA  . THR D 1 5   ? 16.567  12.349  -45.761 1.00 12.10  ? 5   THR D CA  1 
ATOM   6418 C  C   . THR D 1 5   ? 17.027  11.169  -44.921 1.00 11.38  ? 5   THR D C   1 
ATOM   6419 O  O   . THR D 1 5   ? 17.417  11.338  -43.741 1.00 10.51  ? 5   THR D O   1 
ATOM   6420 C  CB  . THR D 1 5   ? 17.468  12.465  -47.029 1.00 11.67  ? 5   THR D CB  1 
ATOM   6421 O  OG1 . THR D 1 5   ? 18.811  12.425  -46.507 1.00 12.64  ? 5   THR D OG1 1 
ATOM   6422 C  CG2 . THR D 1 5   ? 17.262  13.718  -47.872 1.00 12.45  ? 5   THR D CG2 1 
ATOM   6423 N  N   . TYR D 1 6   ? 17.085  9.987   -45.576 1.00 10.74  ? 6   TYR D N   1 
ATOM   6424 C  CA  . TYR D 1 6   ? 17.730  8.851   -44.988 1.00 10.98  ? 6   TYR D CA  1 
ATOM   6425 C  C   . TYR D 1 6   ? 19.059  8.481   -45.633 1.00 10.54  ? 6   TYR D C   1 
ATOM   6426 O  O   . TYR D 1 6   ? 19.561  7.413   -45.278 1.00 12.01  ? 6   TYR D O   1 
ATOM   6427 C  CB  . TYR D 1 6   ? 16.814  7.638   -45.088 1.00 10.27  ? 6   TYR D CB  1 
ATOM   6428 C  CG  . TYR D 1 6   ? 15.554  7.775   -44.260 1.00 8.95   ? 6   TYR D CG  1 
ATOM   6429 C  CD1 . TYR D 1 6   ? 14.396  8.375   -44.718 1.00 10.08  ? 6   TYR D CD1 1 
ATOM   6430 C  CD2 . TYR D 1 6   ? 15.537  7.239   -42.976 1.00 9.04   ? 6   TYR D CD2 1 
ATOM   6431 C  CE1 . TYR D 1 6   ? 13.233  8.398   -43.953 1.00 10.13  ? 6   TYR D CE1 1 
ATOM   6432 C  CE2 . TYR D 1 6   ? 14.389  7.243   -42.205 1.00 8.81   ? 6   TYR D CE2 1 
ATOM   6433 C  CZ  . TYR D 1 6   ? 13.239  7.896   -42.663 1.00 9.18   ? 6   TYR D CZ  1 
ATOM   6434 O  OH  . TYR D 1 6   ? 12.071  7.911   -41.950 1.00 10.30  ? 6   TYR D OH  1 
ATOM   6435 N  N   . PHE D 1 7   ? 19.671  9.337   -46.450 1.00 11.16  ? 7   PHE D N   1 
ATOM   6436 C  CA  . PHE D 1 7   ? 20.911  8.987   -47.124 1.00 13.64  ? 7   PHE D CA  1 
ATOM   6437 C  C   . PHE D 1 7   ? 21.644  10.237  -47.541 1.00 15.78  ? 7   PHE D C   1 
ATOM   6438 O  O   . PHE D 1 7   ? 21.008  11.090  -48.134 1.00 15.58  ? 7   PHE D O   1 
ATOM   6439 C  CB  . PHE D 1 7   ? 20.641  8.131   -48.376 1.00 18.94  ? 7   PHE D CB  1 
ATOM   6440 C  CG  . PHE D 1 7   ? 21.883  7.730   -49.143 1.00 27.23  ? 7   PHE D CG  1 
ATOM   6441 C  CD1 . PHE D 1 7   ? 22.620  6.626   -48.750 1.00 31.01  ? 7   PHE D CD1 1 
ATOM   6442 C  CD2 . PHE D 1 7   ? 22.314  8.460   -50.255 1.00 31.97  ? 7   PHE D CD2 1 
ATOM   6443 C  CE1 . PHE D 1 7   ? 23.749  6.225   -49.442 1.00 39.15  ? 7   PHE D CE1 1 
ATOM   6444 C  CE2 . PHE D 1 7   ? 23.449  8.064   -50.949 1.00 41.31  ? 7   PHE D CE2 1 
ATOM   6445 C  CZ  . PHE D 1 7   ? 24.167  6.956   -50.542 1.00 50.24  ? 7   PHE D CZ  1 
ATOM   6446 N  N   . GLY D 1 8   ? 22.942  10.325  -47.214 1.00 15.20  ? 8   GLY D N   1 
ATOM   6447 C  CA  . GLY D 1 8   ? 23.741  11.416  -47.721 1.00 17.39  ? 8   GLY D CA  1 
ATOM   6448 C  C   . GLY D 1 8   ? 23.847  12.494  -46.655 1.00 14.27  ? 8   GLY D C   1 
ATOM   6449 O  O   . GLY D 1 8   ? 23.598  12.234  -45.472 1.00 15.44  ? 8   GLY D O   1 
ATOM   6450 N  N   . PRO D 1 9   ? 24.213  13.730  -47.061 1.00 15.51  ? 9   PRO D N   1 
ATOM   6451 C  CA  . PRO D 1 9   ? 24.549  14.780  -46.115 1.00 17.82  ? 9   PRO D CA  1 
ATOM   6452 C  C   . PRO D 1 9   ? 23.436  15.190  -45.163 1.00 15.00  ? 9   PRO D C   1 
ATOM   6453 O  O   . PRO D 1 9   ? 23.728  15.678  -44.082 1.00 19.05  ? 9   PRO D O   1 
ATOM   6454 C  CB  . PRO D 1 9   ? 24.876  16.000  -47.016 1.00 21.77  ? 9   PRO D CB  1 
ATOM   6455 C  CG  . PRO D 1 9   ? 25.165  15.494  -48.396 1.00 26.84  ? 9   PRO D CG  1 
ATOM   6456 C  CD  . PRO D 1 9   ? 24.463  14.159  -48.454 1.00 16.59  ? 9   PRO D CD  1 
ATOM   6457 N  N   . ASP D 1 10  ? 22.186  14.977  -45.566 1.00 13.61  ? 10  ASP D N   1 
ATOM   6458 C  CA  . ASP D 1 10  ? 21.038  15.350  -44.730 1.00 13.36  ? 10  ASP D CA  1 
ATOM   6459 C  C   . ASP D 1 10  ? 20.394  14.139  -44.060 1.00 10.82  ? 10  ASP D C   1 
ATOM   6460 O  O   . ASP D 1 10  ? 19.283  14.222  -43.532 1.00 11.42  ? 10  ASP D O   1 
ATOM   6461 C  CB  . ASP D 1 10  ? 20.006  16.137  -45.533 1.00 14.84  ? 10  ASP D CB  1 
ATOM   6462 C  CG  . ASP D 1 10  ? 20.597  17.400  -46.115 1.00 24.11  ? 10  ASP D CG  1 
ATOM   6463 O  OD1 . ASP D 1 10  ? 21.204  18.154  -45.336 1.00 22.70  ? 10  ASP D OD1 1 
ATOM   6464 O  OD2 . ASP D 1 10  ? 20.475  17.578  -47.341 1.00 23.30  ? 10  ASP D OD2 1 
ATOM   6465 N  N   . GLY D 1 11  ? 21.129  13.037  -44.050 1.00 10.70  ? 11  GLY D N   1 
ATOM   6466 C  CA  . GLY D 1 11  ? 20.686  11.781  -43.476 1.00 8.53   ? 11  GLY D CA  1 
ATOM   6467 C  C   . GLY D 1 11  ? 20.727  11.813  -41.931 1.00 8.44   ? 11  GLY D C   1 
ATOM   6468 O  O   . GLY D 1 11  ? 20.969  12.834  -41.239 1.00 9.95   ? 11  GLY D O   1 
ATOM   6469 N  N   . GLU D 1 12  ? 20.508  10.655  -41.326 1.00 7.93   ? 12  GLU D N   1 
ATOM   6470 C  CA  . GLU D 1 12  ? 20.074  10.581  -39.944 1.00 7.59   ? 12  GLU D CA  1 
ATOM   6471 C  C   . GLU D 1 12  ? 21.138  11.061  -38.966 1.00 6.75   ? 12  GLU D C   1 
ATOM   6472 O  O   . GLU D 1 12  ? 20.775  11.529  -37.884 1.00 7.67   ? 12  GLU D O   1 
ATOM   6473 C  CB  . GLU D 1 12  ? 19.611  9.151   -39.537 1.00 7.35   ? 12  GLU D CB  1 
ATOM   6474 C  CG  . GLU D 1 12  ? 20.744  8.106   -39.438 1.00 7.69   ? 12  GLU D CG  1 
ATOM   6475 C  CD  . GLU D 1 12  ? 20.136  6.703   -39.438 1.00 7.44   ? 12  GLU D CD  1 
ATOM   6476 O  OE1 . GLU D 1 12  ? 19.713  6.274   -38.380 1.00 9.16   ? 12  GLU D OE1 1 
ATOM   6477 O  OE2 . GLU D 1 12  ? 20.031  6.183   -40.561 1.00 9.29   ? 12  GLU D OE2 1 
ATOM   6478 N  N   . ASN D 1 13  ? 22.435  10.945  -39.290 1.00 8.97   ? 13  ASN D N   1 
ATOM   6479 C  CA  . ASN D 1 13  ? 23.422  11.454  -38.351 1.00 8.96   ? 13  ASN D CA  1 
ATOM   6480 C  C   . ASN D 1 13  ? 23.469  12.991  -38.323 1.00 11.44  ? 13  ASN D C   1 
ATOM   6481 O  O   . ASN D 1 13  ? 24.077  13.529  -37.414 1.00 10.56  ? 13  ASN D O   1 
ATOM   6482 C  CB  . ASN D 1 13  ? 24.848  10.919  -38.631 1.00 9.98   ? 13  ASN D CB  1 
ATOM   6483 C  CG  . ASN D 1 13  ? 24.959  9.405   -38.442 1.00 8.14   ? 13  ASN D CG  1 
ATOM   6484 O  OD1 . ASN D 1 13  ? 24.047  8.772   -37.931 1.00 10.37  ? 13  ASN D OD1 1 
ATOM   6485 N  ND2 . ASN D 1 13  ? 26.171  8.937   -38.701 1.00 9.52   ? 13  ASN D ND2 1 
ATOM   6486 N  N   . SER D 1 14  ? 22.742  13.594  -39.237 1.00 9.30   ? 14  SER D N   1 
ATOM   6487 C  CA  . SER D 1 14  ? 22.733  15.081  -39.320 1.00 9.86   ? 14  SER D CA  1 
ATOM   6488 C  C   . SER D 1 14  ? 21.393  15.650  -38.869 1.00 9.28   ? 14  SER D C   1 
ATOM   6489 O  O   . SER D 1 14  ? 21.230  16.887  -38.799 1.00 10.96  ? 14  SER D O   1 
ATOM   6490 C  CB  . SER D 1 14  ? 23.032  15.526  -40.748 1.00 12.01  ? 14  SER D CB  1 
ATOM   6491 O  OG  . SER D 1 14  ? 24.392  15.279  -41.044 1.00 11.65  ? 14  SER D OG  1 
ATOM   6492 N  N   . TRP D 1 15  ? 20.409  14.855  -38.578 1.00 7.53   ? 15  TRP D N   1 
ATOM   6493 C  CA  . TRP D 1 15  ? 19.072  15.344  -38.270 1.00 8.45   ? 15  TRP D CA  1 
ATOM   6494 C  C   . TRP D 1 15  ? 19.141  16.279  -37.060 1.00 10.96  ? 15  TRP D C   1 
ATOM   6495 O  O   . TRP D 1 15  ? 18.409  17.283  -37.021 1.00 11.69  ? 15  TRP D O   1 
ATOM   6496 C  CB  . TRP D 1 15  ? 18.109  14.212  -37.919 1.00 9.30   ? 15  TRP D CB  1 
ATOM   6497 C  CG  . TRP D 1 15  ? 17.715  13.337  -39.076 1.00 8.88   ? 15  TRP D CG  1 
ATOM   6498 C  CD1 . TRP D 1 15  ? 17.984  13.479  -40.410 1.00 10.16  ? 15  TRP D CD1 1 
ATOM   6499 C  CD2 . TRP D 1 15  ? 16.974  12.102  -38.963 1.00 8.14   ? 15  TRP D CD2 1 
ATOM   6500 N  NE1 . TRP D 1 15  ? 17.428  12.450  -41.140 1.00 9.63   ? 15  TRP D NE1 1 
ATOM   6501 C  CE2 . TRP D 1 15  ? 16.791  11.614  -40.275 1.00 8.55   ? 15  TRP D CE2 1 
ATOM   6502 C  CE3 . TRP D 1 15  ? 16.364  11.418  -37.880 1.00 8.62   ? 15  TRP D CE3 1 
ATOM   6503 C  CZ2 . TRP D 1 15  ? 16.088  10.422  -40.505 1.00 8.93   ? 15  TRP D CZ2 1 
ATOM   6504 C  CZ3 . TRP D 1 15  ? 15.668  10.254  -38.093 1.00 9.01   ? 15  TRP D CZ3 1 
ATOM   6505 C  CH2 . TRP D 1 15  ? 15.532  9.791   -39.410 1.00 9.20   ? 15  TRP D CH2 1 
ATOM   6506 N  N   . SER D 1 16  ? 20.006  15.992  -36.070 1.00 9.07   ? 16  SER D N   1 
ATOM   6507 C  CA  . SER D 1 16  ? 20.127  16.799  -34.841 1.00 9.29   ? 16  SER D CA  1 
ATOM   6508 C  C   . SER D 1 16  ? 20.556  18.234  -35.138 1.00 11.47  ? 16  SER D C   1 
ATOM   6509 O  O   . SER D 1 16  ? 20.250  19.075  -34.264 1.00 10.95  ? 16  SER D O   1 
ATOM   6510 C  CB  . SER D 1 16  ? 21.097  16.215  -33.849 1.00 11.46  ? 16  SER D CB  1 
ATOM   6511 O  OG  . SER D 1 16  ? 22.397  16.232  -34.410 1.00 13.81  ? 16  SER D OG  1 
ATOM   6512 N  N   . LYS D 1 17  ? 21.216  18.504  -36.295 1.00 9.98   ? 17  LYS D N   1 
ATOM   6513 C  CA  . LYS D 1 17  ? 21.648  19.897  -36.569 1.00 10.65  ? 17  LYS D CA  1 
ATOM   6514 C  C   . LYS D 1 17  ? 20.389  20.744  -36.672 1.00 11.11  ? 17  LYS D C   1 
ATOM   6515 O  O   . LYS D 1 17  ? 20.486  21.973  -36.441 1.00 14.99  ? 17  LYS D O   1 
ATOM   6516 C  CB  . LYS D 1 17  ? 22.355  19.914  -37.906 1.00 10.82  ? 17  LYS D CB  1 
ATOM   6517 C  CG  . LYS D 1 17  ? 23.654  19.125  -37.938 1.00 11.87  ? 17  LYS D CG  1 
ATOM   6518 C  CD  . LYS D 1 17  ? 24.306  19.153  -39.288 1.00 11.83  ? 17  LYS D CD  1 
ATOM   6519 C  CE  . LYS D 1 17  ? 25.443  18.153  -39.455 1.00 12.14  ? 17  LYS D CE  1 
ATOM   6520 N  NZ  . LYS D 1 17  ? 26.114  18.254  -40.787 1.00 12.91  ? 17  LYS D NZ  1 
ATOM   6521 N  N   . LYS D 1 18  ? 19.269  20.254  -37.185 1.00 13.10  ? 18  LYS D N   1 
ATOM   6522 C  CA  . LYS D 1 18  ? 18.065  21.056  -37.410 1.00 11.89  ? 18  LYS D CA  1 
ATOM   6523 C  C   . LYS D 1 18  ? 16.947  20.764  -36.425 1.00 12.65  ? 18  LYS D C   1 
ATOM   6524 O  O   . LYS D 1 18  ? 15.972  21.484  -36.303 1.00 16.50  ? 18  LYS D O   1 
ATOM   6525 C  CB  . LYS D 1 18  ? 17.561  20.853  -38.865 1.00 13.83  ? 18  LYS D CB  1 
ATOM   6526 C  CG  . LYS D 1 18  ? 18.455  21.419  -39.989 1.00 18.28  ? 18  LYS D CG  1 
ATOM   6527 C  CD  . LYS D 1 18  ? 17.919  21.152  -41.415 1.00 22.17  ? 18  LYS D CD  1 
ATOM   6528 C  CE  . LYS D 1 18  ? 18.633  21.956  -42.479 1.00 26.19  ? 18  LYS D CE  1 
ATOM   6529 N  NZ  . LYS D 1 18  ? 18.039  21.700  -43.820 1.00 33.80  ? 18  LYS D NZ  1 
ATOM   6530 N  N   . TYR D 1 19  ? 17.006  19.578  -35.786 1.00 12.06  ? 19  TYR D N   1 
ATOM   6531 C  CA  . TYR D 1 19  ? 15.924  19.015  -35.017 1.00 10.57  ? 19  TYR D CA  1 
ATOM   6532 C  C   . TYR D 1 19  ? 16.518  18.570  -33.697 1.00 10.81  ? 19  TYR D C   1 
ATOM   6533 O  O   . TYR D 1 19  ? 16.970  17.426  -33.599 1.00 10.74  ? 19  TYR D O   1 
ATOM   6534 C  CB  . TYR D 1 19  ? 15.224  17.853  -35.720 1.00 10.99  ? 19  TYR D CB  1 
ATOM   6535 C  CG  . TYR D 1 19  ? 14.627  18.262  -37.038 1.00 10.95  ? 19  TYR D CG  1 
ATOM   6536 C  CD1 . TYR D 1 19  ? 13.413  18.960  -37.087 1.00 11.14  ? 19  TYR D CD1 1 
ATOM   6537 C  CD2 . TYR D 1 19  ? 15.322  18.061  -38.213 1.00 11.64  ? 19  TYR D CD2 1 
ATOM   6538 C  CE1 . TYR D 1 19  ? 12.848  19.326  -38.295 1.00 13.91  ? 19  TYR D CE1 1 
ATOM   6539 C  CE2 . TYR D 1 19  ? 14.780  18.437  -39.436 1.00 11.46  ? 19  TYR D CE2 1 
ATOM   6540 C  CZ  . TYR D 1 19  ? 13.553  19.075  -39.470 1.00 12.56  ? 19  TYR D CZ  1 
ATOM   6541 O  OH  . TYR D 1 19  ? 12.997  19.446  -40.668 1.00 15.86  ? 19  TYR D OH  1 
ATOM   6542 N  N   . PRO D 1 20  ? 16.623  19.452  -32.685 1.00 12.44  ? 20  PRO D N   1 
ATOM   6543 C  CA  . PRO D 1 20  ? 17.425  19.130  -31.510 1.00 13.12  ? 20  PRO D CA  1 
ATOM   6544 C  C   . PRO D 1 20  ? 17.001  17.847  -30.817 1.00 9.79   ? 20  PRO D C   1 
ATOM   6545 O  O   . PRO D 1 20  ? 17.883  17.191  -30.252 1.00 11.50  ? 20  PRO D O   1 
ATOM   6546 C  CB  . PRO D 1 20  ? 17.341  20.333  -30.553 1.00 16.47  ? 20  PRO D CB  1 
ATOM   6547 C  CG  . PRO D 1 20  ? 16.490  21.268  -31.310 1.00 17.73  ? 20  PRO D CG  1 
ATOM   6548 C  CD  . PRO D 1 20  ? 16.139  20.853  -32.701 1.00 13.87  ? 20  PRO D CD  1 
ATOM   6549 N  N   . SER D 1 21  ? 15.710  17.492  -30.832 1.00 11.24  ? 21  SER D N   1 
ATOM   6550 C  CA  . SER D 1 21  ? 15.285  16.278  -30.135 1.00 10.52  ? 21  SER D CA  1 
ATOM   6551 C  C   . SER D 1 21  ? 15.907  15.052  -30.764 1.00 10.10  ? 21  SER D C   1 
ATOM   6552 O  O   . SER D 1 21  ? 15.974  14.012  -30.057 1.00 12.09  ? 21  SER D O   1 
ATOM   6553 C  CB  . SER D 1 21  ? 13.806  16.188  -30.047 1.00 11.56  ? 21  SER D CB  1 
ATOM   6554 O  OG  . SER D 1 21  ? 13.262  17.158  -29.137 1.00 12.38  ? 21  SER D OG  1 
ATOM   6555 N  N   . CYS D 1 22  ? 16.337  15.105  -32.013 1.00 8.43   ? 22  CYS D N   1 
ATOM   6556 C  CA  . CYS D 1 22  ? 16.918  13.906  -32.616 1.00 9.09   ? 22  CYS D CA  1 
ATOM   6557 C  C   . CYS D 1 22  ? 18.244  13.525  -31.945 1.00 10.32  ? 22  CYS D C   1 
ATOM   6558 O  O   . CYS D 1 22  ? 18.756  12.446  -32.191 1.00 12.05  ? 22  CYS D O   1 
ATOM   6559 C  CB  . CYS D 1 22  ? 17.050  14.010  -34.110 1.00 10.51  ? 22  CYS D CB  1 
ATOM   6560 S  SG  . CYS D 1 22  ? 15.500  14.334  -35.006 1.00 10.25  ? 22  CYS D SG  1 
ATOM   6561 N  N   . GLY D 1 23  ? 18.892  14.486  -31.232 1.00 10.83  ? 23  GLY D N   1 
ATOM   6562 C  CA  . GLY D 1 23  ? 20.097  14.251  -30.468 1.00 12.58  ? 23  GLY D CA  1 
ATOM   6563 C  C   . GLY D 1 23  ? 19.866  14.211  -28.965 1.00 12.73  ? 23  GLY D C   1 
ATOM   6564 O  O   . GLY D 1 23  ? 20.827  14.256  -28.165 1.00 16.75  ? 23  GLY D O   1 
ATOM   6565 N  N   . GLY D 1 24  ? 18.590  14.114  -28.574 1.00 12.36  ? 24  GLY D N   1 
ATOM   6566 C  CA  . GLY D 1 24  ? 18.249  14.083  -27.152 1.00 13.79  ? 24  GLY D CA  1 
ATOM   6567 C  C   . GLY D 1 24  ? 18.044  12.645  -26.665 1.00 13.63  ? 24  GLY D C   1 
ATOM   6568 O  O   . GLY D 1 24  ? 18.538  11.671  -27.263 1.00 17.79  ? 24  GLY D O   1 
ATOM   6569 N  N   . LEU D 1 25  ? 17.391  12.555  -25.524 1.00 14.65  ? 25  LEU D N   1 
ATOM   6570 C  CA  . LEU D 1 25  ? 17.185  11.275  -24.890 1.00 14.19  ? 25  LEU D CA  1 
ATOM   6571 C  C   . LEU D 1 25  ? 15.937  10.576  -25.420 1.00 13.27  ? 25  LEU D C   1 
ATOM   6572 O  O   . LEU D 1 25  ? 15.132  11.105  -26.194 1.00 13.06  ? 25  LEU D O   1 
ATOM   6573 C  CB  . LEU D 1 25  ? 17.101  11.413  -23.375 1.00 21.67  ? 25  LEU D CB  1 
ATOM   6574 C  CG  . LEU D 1 25  ? 18.336  12.015  -22.697 1.00 21.40  ? 25  LEU D CG  1 
ATOM   6575 C  CD1 . LEU D 1 25  ? 18.044  12.328  -21.231 1.00 32.98  ? 25  LEU D CD1 1 
ATOM   6576 C  CD2 . LEU D 1 25  ? 19.530  11.075  -22.844 1.00 25.71  ? 25  LEU D CD2 1 
ATOM   6577 N  N   . LEU D 1 26  ? 15.841  9.291   -25.088 1.00 14.84  ? 26  LEU D N   1 
ATOM   6578 C  CA  . LEU D 1 26  ? 14.715  8.358   -25.261 1.00 12.27  ? 26  LEU D CA  1 
ATOM   6579 C  C   . LEU D 1 26  ? 14.311  8.242   -26.726 1.00 10.16  ? 26  LEU D C   1 
ATOM   6580 O  O   . LEU D 1 26  ? 13.117  8.314   -27.097 1.00 11.09  ? 26  LEU D O   1 
ATOM   6581 C  CB  . LEU D 1 26  ? 13.528  8.880   -24.447 1.00 15.04  ? 26  LEU D CB  1 
ATOM   6582 C  CG  . LEU D 1 26  ? 13.818  9.221   -22.987 1.00 22.81  ? 26  LEU D CG  1 
ATOM   6583 C  CD1 . LEU D 1 26  ? 12.514  9.553   -22.280 1.00 29.50  ? 26  LEU D CD1 1 
ATOM   6584 C  CD2 . LEU D 1 26  ? 14.564  8.113   -22.237 1.00 28.48  ? 26  LEU D CD2 1 
ATOM   6585 N  N   . GLN D 1 27  ? 15.313  8.091   -27.595 1.00 10.65  ? 27  GLN D N   1 
ATOM   6586 C  CA  . GLN D 1 27  ? 15.021  7.974   -29.012 1.00 9.68   ? 27  GLN D CA  1 
ATOM   6587 C  C   . GLN D 1 27  ? 14.590  6.554   -29.419 1.00 7.62   ? 27  GLN D C   1 
ATOM   6588 O  O   . GLN D 1 27  ? 14.973  5.527   -28.835 1.00 9.66   ? 27  GLN D O   1 
ATOM   6589 C  CB  . GLN D 1 27  ? 16.281  8.412   -29.746 1.00 8.40   ? 27  GLN D CB  1 
ATOM   6590 C  CG  . GLN D 1 27  ? 16.647  9.899   -29.564 1.00 11.33  ? 27  GLN D CG  1 
ATOM   6591 C  CD  . GLN D 1 27  ? 15.566  10.761  -30.198 1.00 9.75   ? 27  GLN D CD  1 
ATOM   6592 O  OE1 . GLN D 1 27  ? 15.538  10.910  -31.420 1.00 10.83  ? 27  GLN D OE1 1 
ATOM   6593 N  NE2 . GLN D 1 27  ? 14.645  11.296  -29.386 1.00 10.57  ? 27  GLN D NE2 1 
ATOM   6594 N  N   . SER D 1 28  ? 13.863  6.529   -30.510 1.00 7.10   ? 28  SER D N   1 
ATOM   6595 C  CA  . SER D 1 28  ? 13.410  5.271   -31.122 1.00 7.34   ? 28  SER D CA  1 
ATOM   6596 C  C   . SER D 1 28  ? 13.920  5.238   -32.578 1.00 7.50   ? 28  SER D C   1 
ATOM   6597 O  O   . SER D 1 28  ? 14.239  6.269   -33.196 1.00 8.99   ? 28  SER D O   1 
ATOM   6598 C  CB  . SER D 1 28  ? 11.909  5.269   -31.141 1.00 8.91   ? 28  SER D CB  1 
ATOM   6599 O  OG  . SER D 1 28  ? 11.423  5.188   -29.814 1.00 10.15  ? 28  SER D OG  1 
ATOM   6600 N  N   . PRO D 1 29  ? 14.014  4.099   -33.244 1.00 6.24   ? 29  PRO D N   1 
ATOM   6601 C  CA  . PRO D 1 29  ? 13.694  2.762   -32.714 1.00 6.41   ? 29  PRO D CA  1 
ATOM   6602 C  C   . PRO D 1 29  ? 14.854  2.177   -31.909 1.00 7.21   ? 29  PRO D C   1 
ATOM   6603 O  O   . PRO D 1 29  ? 15.922  2.736   -31.692 1.00 9.48   ? 29  PRO D O   1 
ATOM   6604 C  CB  . PRO D 1 29  ? 13.415  2.084   -34.029 1.00 8.12   ? 29  PRO D CB  1 
ATOM   6605 C  CG  . PRO D 1 29  ? 14.504  2.507   -34.919 1.00 7.24   ? 29  PRO D CG  1 
ATOM   6606 C  CD  . PRO D 1 29  ? 14.525  4.022   -34.618 1.00 8.12   ? 29  PRO D CD  1 
ATOM   6607 N  N   . ILE D 1 30  ? 14.632  0.916   -31.446 1.00 8.09   ? 30  ILE D N   1 
ATOM   6608 C  CA  . ILE D 1 30  ? 15.569  0.178   -30.558 1.00 7.95   ? 30  ILE D CA  1 
ATOM   6609 C  C   . ILE D 1 30  ? 15.525  -1.313  -30.925 1.00 7.39   ? 30  ILE D C   1 
ATOM   6610 O  O   . ILE D 1 30  ? 14.632  -1.758  -31.698 1.00 8.75   ? 30  ILE D O   1 
ATOM   6611 C  CB  . ILE D 1 30  ? 15.248  0.352   -29.052 1.00 8.17   ? 30  ILE D CB  1 
ATOM   6612 C  CG1 . ILE D 1 30  ? 13.834  -0.125  -28.721 1.00 10.83  ? 30  ILE D CG1 1 
ATOM   6613 C  CG2 . ILE D 1 30  ? 15.501  1.804   -28.623 1.00 12.28  ? 30  ILE D CG2 1 
ATOM   6614 C  CD1 . ILE D 1 30  ? 13.562  -0.369  -27.295 1.00 12.70  ? 30  ILE D CD1 1 
ATOM   6615 N  N   . ASP D 1 31  ? 16.616  -1.939  -30.515 1.00 8.57   ? 31  ASP D N   1 
ATOM   6616 C  CA  . ASP D 1 31  ? 16.657  -3.399  -30.702 1.00 6.97   ? 31  ASP D CA  1 
ATOM   6617 C  C   . ASP D 1 31  ? 16.022  -4.102  -29.515 1.00 8.66   ? 31  ASP D C   1 
ATOM   6618 O  O   . ASP D 1 31  ? 16.458  -3.929  -28.381 1.00 10.90  ? 31  ASP D O   1 
ATOM   6619 C  CB  . ASP D 1 31  ? 18.148  -3.824  -30.794 1.00 8.95   ? 31  ASP D CB  1 
ATOM   6620 C  CG  . ASP D 1 31  ? 18.274  -5.332  -30.883 1.00 9.23   ? 31  ASP D CG  1 
ATOM   6621 O  OD1 . ASP D 1 31  ? 17.759  -5.882  -31.831 1.00 11.29  ? 31  ASP D OD1 1 
ATOM   6622 O  OD2 . ASP D 1 31  ? 18.941  -5.882  -30.019 1.00 13.07  ? 31  ASP D OD2 1 
ATOM   6623 N  N   . LEU D 1 32  ? 15.054  -4.976  -29.803 1.00 10.48  ? 32  LEU D N   1 
ATOM   6624 C  CA  . LEU D 1 32  ? 14.380  -5.705  -28.733 1.00 11.74  ? 32  LEU D CA  1 
ATOM   6625 C  C   . LEU D 1 32  ? 15.158  -7.007  -28.497 1.00 10.93  ? 32  LEU D C   1 
ATOM   6626 O  O   . LEU D 1 32  ? 15.185  -7.842  -29.383 1.00 13.12  ? 32  LEU D O   1 
ATOM   6627 C  CB  . LEU D 1 32  ? 12.946  -6.007  -29.172 1.00 13.03  ? 32  LEU D CB  1 
ATOM   6628 C  CG  . LEU D 1 32  ? 12.168  -4.771  -29.610 1.00 12.46  ? 32  LEU D CG  1 
ATOM   6629 C  CD1 . LEU D 1 32  ? 10.874  -5.110  -30.330 1.00 14.78  ? 32  LEU D CD1 1 
ATOM   6630 C  CD2 . LEU D 1 32  ? 11.864  -3.895  -28.403 1.00 17.25  ? 32  LEU D CD2 1 
ATOM   6631 N  N   . HIS D 1 33  ? 15.836  -7.132  -27.335 1.00 10.42  ? 33  HIS D N   1 
ATOM   6632 C  CA  . HIS D 1 33  ? 16.667  -8.276  -27.049 1.00 11.29  ? 33  HIS D CA  1 
ATOM   6633 C  C   . HIS D 1 33  ? 16.528  -8.632  -25.566 1.00 11.43  ? 33  HIS D C   1 
ATOM   6634 O  O   . HIS D 1 33  ? 16.210  -7.786  -24.717 1.00 11.78  ? 33  HIS D O   1 
ATOM   6635 C  CB  . HIS D 1 33  ? 18.168  -8.095  -27.455 1.00 14.56  ? 33  HIS D CB  1 
ATOM   6636 C  CG  . HIS D 1 33  ? 18.886  -6.989  -26.788 1.00 12.13  ? 33  HIS D CG  1 
ATOM   6637 N  ND1 . HIS D 1 33  ? 18.692  -5.642  -27.096 1.00 18.30  ? 33  HIS D ND1 1 
ATOM   6638 C  CD2 . HIS D 1 33  ? 19.729  -7.012  -25.747 1.00 13.45  ? 33  HIS D CD2 1 
ATOM   6639 C  CE1 . HIS D 1 33  ? 19.453  -4.917  -26.280 1.00 17.64  ? 33  HIS D CE1 1 
ATOM   6640 N  NE2 . HIS D 1 33  ? 20.078  -5.718  -25.454 1.00 14.60  ? 33  HIS D NE2 1 
ATOM   6641 N  N   . SER D 1 34  ? 16.782  -9.912  -25.242 1.00 13.22  ? 34  SER D N   1 
ATOM   6642 C  CA  . SER D 1 34  ? 16.510  -10.491 -23.935 1.00 13.80  ? 34  SER D CA  1 
ATOM   6643 C  C   . SER D 1 34  ? 16.972  -9.619  -22.769 1.00 12.11  ? 34  SER D C   1 
ATOM   6644 O  O   . SER D 1 34  ? 16.270  -9.520  -21.775 1.00 13.84  ? 34  SER D O   1 
ATOM   6645 C  CB  . SER D 1 34  ? 17.035  -11.925 -23.868 1.00 14.38  ? 34  SER D CB  1 
ATOM   6646 O  OG  . SER D 1 34  ? 18.459  -11.876 -23.910 1.00 21.20  ? 34  SER D OG  1 
ATOM   6647 N  N   . ASP D 1 35  ? 18.185  -9.050  -22.841 1.00 11.46  ? 35  ASP D N   1 
ATOM   6648 C  CA  . ASP D 1 35  ? 18.775  -8.437  -21.651 1.00 10.86  ? 35  ASP D CA  1 
ATOM   6649 C  C   . ASP D 1 35  ? 17.960  -7.256  -21.120 1.00 12.65  ? 35  ASP D C   1 
ATOM   6650 O  O   . ASP D 1 35  ? 18.051  -6.944  -19.947 1.00 16.55  ? 35  ASP D O   1 
ATOM   6651 C  CB  . ASP D 1 35  ? 20.215  -7.928  -21.927 1.00 14.58  ? 35  ASP D CB  1 
ATOM   6652 C  CG  . ASP D 1 35  ? 21.106  -8.978  -22.568 1.00 16.26  ? 35  ASP D CG  1 
ATOM   6653 O  OD1 . ASP D 1 35  ? 20.802  -9.402  -23.744 1.00 18.85  ? 35  ASP D OD1 1 
ATOM   6654 O  OD2 . ASP D 1 35  ? 22.089  -9.389  -21.892 1.00 15.99  ? 35  ASP D OD2 1 
ATOM   6655 N  N   . ILE D 1 36  ? 17.144  -6.646  -21.985 1.00 12.66  ? 36  ILE D N   1 
ATOM   6656 C  CA  . ILE D 1 36  ? 16.446  -5.428  -21.619 1.00 13.51  ? 36  ILE D CA  1 
ATOM   6657 C  C   . ILE D 1 36  ? 14.935  -5.615  -21.510 1.00 11.78  ? 36  ILE D C   1 
ATOM   6658 O  O   . ILE D 1 36  ? 14.224  -4.646  -21.228 1.00 15.70  ? 36  ILE D O   1 
ATOM   6659 C  CB  . ILE D 1 36  ? 16.893  -4.195  -22.450 1.00 15.55  ? 36  ILE D CB  1 
ATOM   6660 C  CG1 . ILE D 1 36  ? 16.728  -4.413  -23.956 1.00 17.60  ? 36  ILE D CG1 1 
ATOM   6661 C  CG2 . ILE D 1 36  ? 18.326  -3.769  -22.105 1.00 20.39  ? 36  ILE D CG2 1 
ATOM   6662 C  CD1 . ILE D 1 36  ? 15.305  -4.541  -24.427 1.00 19.14  ? 36  ILE D CD1 1 
ATOM   6663 N  N   . LEU D 1 37  ? 14.464  -6.868  -21.631 1.00 9.94   ? 37  LEU D N   1 
ATOM   6664 C  CA  . LEU D 1 37  ? 13.049  -7.160  -21.478 1.00 11.69  ? 37  LEU D CA  1 
ATOM   6665 C  C   . LEU D 1 37  ? 12.675  -7.469  -20.047 1.00 11.77  ? 37  LEU D C   1 
ATOM   6666 O  O   . LEU D 1 37  ? 13.364  -8.198  -19.330 1.00 15.14  ? 37  LEU D O   1 
ATOM   6667 C  CB  . LEU D 1 37  ? 12.712  -8.389  -22.321 1.00 12.94  ? 37  LEU D CB  1 
ATOM   6668 C  CG  . LEU D 1 37  ? 12.980  -8.257  -23.839 1.00 13.13  ? 37  LEU D CG  1 
ATOM   6669 C  CD1 . LEU D 1 37  ? 12.582  -9.555  -24.549 1.00 16.64  ? 37  LEU D CD1 1 
ATOM   6670 C  CD2 . LEU D 1 37  ? 12.300  -7.076  -24.522 1.00 13.77  ? 37  LEU D CD2 1 
ATOM   6671 N  N   . GLN D 1 38  ? 11.514  -6.950  -19.646 1.00 12.14  ? 38  GLN D N   1 
ATOM   6672 C  CA  . GLN D 1 38  ? 11.004  -7.305  -18.329 1.00 11.20  ? 38  GLN D CA  1 
ATOM   6673 C  C   . GLN D 1 38  ? 9.489   -7.449  -18.407 1.00 11.68  ? 38  GLN D C   1 
ATOM   6674 O  O   . GLN D 1 38  ? 8.758   -6.530  -18.814 1.00 12.15  ? 38  GLN D O   1 
ATOM   6675 C  CB  . GLN D 1 38  ? 11.313  -6.165  -17.342 1.00 14.83  ? 38  GLN D CB  1 
ATOM   6676 C  CG  . GLN D 1 38  ? 11.019  -6.565  -15.897 1.00 17.70  ? 38  GLN D CG  1 
ATOM   6677 C  CD  . GLN D 1 38  ? 11.696  -5.601  -14.973 1.00 22.75  ? 38  GLN D CD  1 
ATOM   6678 O  OE1 . GLN D 1 38  ? 12.913  -5.696  -14.752 1.00 30.21  ? 38  GLN D OE1 1 
ATOM   6679 N  NE2 . GLN D 1 38  ? 10.896  -4.689  -14.445 1.00 21.97  ? 38  GLN D NE2 1 
ATOM   6680 N  N   . TYR D 1 39  ? 8.965   -8.582  -17.919 1.00 12.31  ? 39  TYR D N   1 
ATOM   6681 C  CA  . TYR D 1 39  ? 7.518   -8.799  -17.858 1.00 11.03  ? 39  TYR D CA  1 
ATOM   6682 C  C   . TYR D 1 39  ? 6.837   -7.786  -16.915 1.00 9.25   ? 39  TYR D C   1 
ATOM   6683 O  O   . TYR D 1 39  ? 7.421   -7.412  -15.854 1.00 12.97  ? 39  TYR D O   1 
ATOM   6684 C  CB  . TYR D 1 39  ? 7.224   -10.222 -17.339 1.00 13.57  ? 39  TYR D CB  1 
ATOM   6685 C  CG  . TYR D 1 39  ? 5.754   -10.472 -17.148 1.00 13.08  ? 39  TYR D CG  1 
ATOM   6686 C  CD1 . TYR D 1 39  ? 4.852   -10.549 -18.198 1.00 14.20  ? 39  TYR D CD1 1 
ATOM   6687 C  CD2 . TYR D 1 39  ? 5.237   -10.613 -15.864 1.00 12.46  ? 39  TYR D CD2 1 
ATOM   6688 C  CE1 . TYR D 1 39  ? 3.486   -10.778 -17.964 1.00 13.55  ? 39  TYR D CE1 1 
ATOM   6689 C  CE2 . TYR D 1 39  ? 3.885   -10.793 -15.617 1.00 13.17  ? 39  TYR D CE2 1 
ATOM   6690 C  CZ  . TYR D 1 39  ? 2.989   -10.855 -16.669 1.00 12.65  ? 39  TYR D CZ  1 
ATOM   6691 O  OH  . TYR D 1 39  ? 1.644   -11.007 -16.439 1.00 15.12  ? 39  TYR D OH  1 
ATOM   6692 N  N   . ASP D 1 40  ? 5.660   -7.266  -17.366 1.00 10.81  ? 40  ASP D N   1 
ATOM   6693 C  CA  . ASP D 1 40  ? 4.905   -6.321  -16.557 1.00 11.62  ? 40  ASP D CA  1 
ATOM   6694 C  C   . ASP D 1 40  ? 3.445   -6.729  -16.614 1.00 10.19  ? 40  ASP D C   1 
ATOM   6695 O  O   . ASP D 1 40  ? 2.818   -6.623  -17.683 1.00 13.03  ? 40  ASP D O   1 
ATOM   6696 C  CB  . ASP D 1 40  ? 5.147   -4.903  -17.071 1.00 13.96  ? 40  ASP D CB  1 
ATOM   6697 C  CG  . ASP D 1 40  ? 4.427   -3.789  -16.324 1.00 15.41  ? 40  ASP D CG  1 
ATOM   6698 O  OD1 . ASP D 1 40  ? 3.621   -4.080  -15.398 1.00 13.96  ? 40  ASP D OD1 1 
ATOM   6699 O  OD2 . ASP D 1 40  ? 4.599   -2.594  -16.771 1.00 22.37  ? 40  ASP D OD2 1 
ATOM   6700 N  N   . ALA D 1 41  ? 2.933   -7.182  -15.479 1.00 10.07  ? 41  ALA D N   1 
ATOM   6701 C  CA  . ALA D 1 41  ? 1.563   -7.665  -15.359 1.00 11.55  ? 41  ALA D CA  1 
ATOM   6702 C  C   . ALA D 1 41  ? 0.537   -6.537  -15.602 1.00 12.29  ? 41  ALA D C   1 
ATOM   6703 O  O   . ALA D 1 41  ? -0.618  -6.782  -15.825 1.00 13.28  ? 41  ALA D O   1 
ATOM   6704 C  CB  . ALA D 1 41  ? 1.367   -8.264  -13.980 1.00 14.01  ? 41  ALA D CB  1 
ATOM   6705 N  N   . SER D 1 42  ? 0.967   -5.266  -15.604 1.00 10.71  ? 42  SER D N   1 
ATOM   6706 C  CA  . SER D 1 42  ? 0.045   -4.158  -15.855 1.00 12.97  ? 42  SER D CA  1 
ATOM   6707 C  C   . SER D 1 42  ? -0.325  -4.072  -17.342 1.00 13.59  ? 42  SER D C   1 
ATOM   6708 O  O   . SER D 1 42  ? -1.209  -3.289  -17.734 1.00 16.99  ? 42  SER D O   1 
ATOM   6709 C  CB  . SER D 1 42  ? 0.602   -2.829  -15.328 1.00 18.30  ? 42  SER D CB  1 
ATOM   6710 O  OG  . SER D 1 42  ? 1.506   -2.308  -16.280 1.00 21.36  ? 42  SER D OG  1 
ATOM   6711 N  N   . LEU D 1 43  ? 0.432   -4.769  -18.198 1.00 14.50  ? 43  LEU D N   1 
ATOM   6712 C  CA  . LEU D 1 43  ? 0.267   -4.677  -19.649 1.00 13.95  ? 43  LEU D CA  1 
ATOM   6713 C  C   . LEU D 1 43  ? -0.893  -5.580  -20.091 1.00 14.87  ? 43  LEU D C   1 
ATOM   6714 O  O   . LEU D 1 43  ? -0.703  -6.637  -20.650 1.00 16.04  ? 43  LEU D O   1 
ATOM   6715 C  CB  . LEU D 1 43  ? 1.588   -4.937  -20.407 1.00 12.38  ? 43  LEU D CB  1 
ATOM   6716 C  CG  . LEU D 1 43  ? 2.708   -3.985  -20.083 1.00 13.48  ? 43  LEU D CG  1 
ATOM   6717 C  CD1 . LEU D 1 43  ? 3.945   -4.388  -20.883 1.00 12.79  ? 43  LEU D CD1 1 
ATOM   6718 C  CD2 . LEU D 1 43  ? 2.280   -2.539  -20.336 1.00 16.44  ? 43  LEU D CD2 1 
ATOM   6719 N  N   . THR D 1 44  ? -2.111  -5.064  -19.952 1.00 17.01  ? 44  THR D N   1 
ATOM   6720 C  CA  . THR D 1 44  ? -3.351  -5.753  -20.247 1.00 16.80  ? 44  THR D CA  1 
ATOM   6721 C  C   . THR D 1 44  ? -3.685  -5.500  -21.715 1.00 13.99  ? 44  THR D C   1 
ATOM   6722 O  O   . THR D 1 44  ? -3.040  -4.697  -22.390 1.00 14.21  ? 44  THR D O   1 
ATOM   6723 C  CB  . THR D 1 44  ? -4.457  -5.306  -19.274 1.00 20.63  ? 44  THR D CB  1 
ATOM   6724 O  OG1 . THR D 1 44  ? -4.538  -3.880  -19.367 1.00 23.57  ? 44  THR D OG1 1 
ATOM   6725 C  CG2 . THR D 1 44  ? -4.174  -5.718  -17.837 1.00 25.88  ? 44  THR D CG2 1 
ATOM   6726 N  N   . PRO D 1 45  ? -4.598  -6.267  -22.339 1.00 17.67  ? 45  PRO D N   1 
ATOM   6727 C  CA  . PRO D 1 45  ? -4.807  -6.092  -23.777 1.00 14.05  ? 45  PRO D CA  1 
ATOM   6728 C  C   . PRO D 1 45  ? -5.363  -4.709  -24.128 1.00 15.51  ? 45  PRO D C   1 
ATOM   6729 O  O   . PRO D 1 45  ? -6.276  -4.170  -23.470 1.00 19.43  ? 45  PRO D O   1 
ATOM   6730 C  CB  . PRO D 1 45  ? -5.817  -7.166  -24.114 1.00 17.14  ? 45  PRO D CB  1 
ATOM   6731 C  CG  . PRO D 1 45  ? -5.511  -8.253  -23.009 1.00 18.84  ? 45  PRO D CG  1 
ATOM   6732 C  CD  . PRO D 1 45  ? -5.366  -7.391  -21.769 1.00 17.90  ? 45  PRO D CD  1 
ATOM   6733 N  N   . LEU D 1 46  ? -4.849  -4.173  -25.244 1.00 12.84  ? 46  LEU D N   1 
ATOM   6734 C  CA  . LEU D 1 46  ? -5.473  -2.983  -25.842 1.00 12.40  ? 46  LEU D CA  1 
ATOM   6735 C  C   . LEU D 1 46  ? -6.827  -3.388  -26.455 1.00 14.29  ? 46  LEU D C   1 
ATOM   6736 O  O   . LEU D 1 46  ? -7.000  -4.510  -26.991 1.00 17.30  ? 46  LEU D O   1 
ATOM   6737 C  CB  . LEU D 1 46  ? -4.550  -2.388  -26.913 1.00 14.95  ? 46  LEU D CB  1 
ATOM   6738 C  CG  . LEU D 1 46  ? -3.290  -1.703  -26.395 1.00 13.79  ? 46  LEU D CG  1 
ATOM   6739 C  CD1 . LEU D 1 46  ? -2.366  -1.418  -27.602 1.00 16.93  ? 46  LEU D CD1 1 
ATOM   6740 C  CD2 . LEU D 1 46  ? -3.582  -0.426  -25.602 1.00 19.61  ? 46  LEU D CD2 1 
ATOM   6741 N  N   . GLU D 1 47  ? -7.757  -2.423  -26.442 1.00 15.47  ? 47  GLU D N   1 
ATOM   6742 C  CA  . GLU D 1 47  ? -8.948  -2.558  -27.268 1.00 12.93  ? 47  GLU D CA  1 
ATOM   6743 C  C   . GLU D 1 47  ? -8.863  -1.578  -28.438 1.00 10.57  ? 47  GLU D C   1 
ATOM   6744 O  O   . GLU D 1 47  ? -8.556  -0.371  -28.254 1.00 14.49  ? 47  GLU D O   1 
ATOM   6745 C  CB  . GLU D 1 47  ? -10.176 -2.371  -26.390 1.00 19.37  ? 47  GLU D CB  1 
ATOM   6746 C  CG  . GLU D 1 47  ? -10.272 -3.526  -25.377 1.00 29.19  ? 47  GLU D CG  1 
ATOM   6747 C  CD  . GLU D 1 47  ? -11.663 -3.789  -24.828 1.00 38.50  ? 47  GLU D CD  1 
ATOM   6748 O  OE1 . GLU D 1 47  ? -12.361 -2.784  -24.568 1.00 56.18  ? 47  GLU D OE1 1 
ATOM   6749 O  OE2 . GLU D 1 47  ? -12.036 -4.986  -24.650 1.00 51.89  ? 47  GLU D OE2 1 
ATOM   6750 N  N   . PHE D 1 48  ? -9.194  -2.112  -29.611 1.00 12.44  ? 48  PHE D N   1 
ATOM   6751 C  CA  . PHE D 1 48  ? -9.174  -1.364  -30.883 1.00 12.85  ? 48  PHE D CA  1 
ATOM   6752 C  C   . PHE D 1 48  ? -10.591 -0.949  -31.264 1.00 14.76  ? 48  PHE D C   1 
ATOM   6753 O  O   . PHE D 1 48  ? -11.386 -1.783  -31.682 1.00 18.81  ? 48  PHE D O   1 
ATOM   6754 C  CB  . PHE D 1 48  ? -8.481  -2.155  -32.006 1.00 13.63  ? 48  PHE D CB  1 
ATOM   6755 C  CG  . PHE D 1 48  ? -7.210  -2.804  -31.537 1.00 15.21  ? 48  PHE D CG  1 
ATOM   6756 C  CD1 . PHE D 1 48  ? -6.076  -2.037  -31.323 1.00 14.48  ? 48  PHE D CD1 1 
ATOM   6757 C  CD2 . PHE D 1 48  ? -7.150  -4.185  -31.286 1.00 15.81  ? 48  PHE D CD2 1 
ATOM   6758 C  CE1 . PHE D 1 48  ? -4.909  -2.620  -30.842 1.00 14.43  ? 48  PHE D CE1 1 
ATOM   6759 C  CE2 . PHE D 1 48  ? -5.956  -4.754  -30.854 1.00 18.98  ? 48  PHE D CE2 1 
ATOM   6760 C  CZ  . PHE D 1 48  ? -4.831  -3.988  -30.615 1.00 15.00  ? 48  PHE D CZ  1 
ATOM   6761 N  N   . GLN D 1 49  ? -10.873 0.374   -31.178 1.00 15.60  ? 49  GLN D N   1 
ATOM   6762 C  CA  . GLN D 1 49  ? -12.243 0.884   -31.345 1.00 16.40  ? 49  GLN D CA  1 
ATOM   6763 C  C   . GLN D 1 49  ? -12.348 1.662   -32.656 1.00 12.16  ? 49  GLN D C   1 
ATOM   6764 O  O   . GLN D 1 49  ? -11.522 2.529   -32.929 1.00 12.59  ? 49  GLN D O   1 
ATOM   6765 C  CB  . GLN D 1 49  ? -12.625 1.876   -30.245 1.00 18.64  ? 49  GLN D CB  1 
ATOM   6766 C  CG  . GLN D 1 49  ? -12.664 1.199   -28.880 1.00 23.34  ? 49  GLN D CG  1 
ATOM   6767 C  CD  . GLN D 1 49  ? -13.609 0.021   -28.776 1.00 26.60  ? 49  GLN D CD  1 
ATOM   6768 O  OE1 . GLN D 1 49  ? -13.203 -1.127  -28.675 1.00 42.63  ? 49  GLN D OE1 1 
ATOM   6769 N  NE2 . GLN D 1 49  ? -14.897 0.307   -28.688 1.00 43.77  ? 49  GLN D NE2 1 
ATOM   6770 N  N   . GLY D 1 50  ? -13.399 1.412   -33.439 1.00 12.26  ? 50  GLY D N   1 
ATOM   6771 C  CA  . GLY D 1 50  ? -13.610 2.180   -34.660 1.00 12.63  ? 50  GLY D CA  1 
ATOM   6772 C  C   . GLY D 1 50  ? -12.556 1.903   -35.732 1.00 9.97   ? 50  GLY D C   1 
ATOM   6773 O  O   . GLY D 1 50  ? -12.435 2.687   -36.670 1.00 11.15  ? 50  GLY D O   1 
ATOM   6774 N  N   . TYR D 1 51  ? -11.883 0.714   -35.672 1.00 11.13  ? 51  TYR D N   1 
ATOM   6775 C  CA  . TYR D 1 51  ? -10.906 0.331   -36.695 1.00 10.11  ? 51  TYR D CA  1 
ATOM   6776 C  C   . TYR D 1 51  ? -11.591 -0.172  -37.973 1.00 9.17   ? 51  TYR D C   1 
ATOM   6777 O  O   . TYR D 1 51  ? -10.989 -0.234  -39.061 1.00 10.93  ? 51  TYR D O   1 
ATOM   6778 C  CB  . TYR D 1 51  ? -9.959  -0.753  -36.147 1.00 9.19   ? 51  TYR D CB  1 
ATOM   6779 C  CG  . TYR D 1 51  ? -8.748  -0.225  -35.426 1.00 9.23   ? 51  TYR D CG  1 
ATOM   6780 C  CD1 . TYR D 1 51  ? -8.861  0.746   -34.435 1.00 9.81   ? 51  TYR D CD1 1 
ATOM   6781 C  CD2 . TYR D 1 51  ? -7.477  -0.748  -35.686 1.00 11.06  ? 51  TYR D CD2 1 
ATOM   6782 C  CE1 . TYR D 1 51  ? -7.737  1.244   -33.790 1.00 10.42  ? 51  TYR D CE1 1 
ATOM   6783 C  CE2 . TYR D 1 51  ? -6.346  -0.236  -35.056 1.00 10.10  ? 51  TYR D CE2 1 
ATOM   6784 C  CZ  . TYR D 1 51  ? -6.483  0.769   -34.105 1.00 9.31   ? 51  TYR D CZ  1 
ATOM   6785 O  OH  . TYR D 1 51  ? -5.335  1.277   -33.519 1.00 10.44  ? 51  TYR D OH  1 
ATOM   6786 N  N   . ASN D 1 52  ? -12.880 -0.564  -37.832 1.00 11.97  ? 52  ASN D N   1 
ATOM   6787 C  CA  . ASN D 1 52  ? -13.542 -1.126  -39.007 1.00 10.88  ? 52  ASN D CA  1 
ATOM   6788 C  C   . ASN D 1 52  ? -14.105 0.014   -39.873 1.00 12.34  ? 52  ASN D C   1 
ATOM   6789 O  O   . ASN D 1 52  ? -15.271 0.443   -39.684 1.00 14.49  ? 52  ASN D O   1 
ATOM   6790 C  CB  . ASN D 1 52  ? -14.680 -2.063  -38.595 1.00 11.96  ? 52  ASN D CB  1 
ATOM   6791 C  CG  . ASN D 1 52  ? -15.254 -2.852  -39.744 1.00 15.28  ? 52  ASN D CG  1 
ATOM   6792 O  OD1 . ASN D 1 52  ? -15.145 -2.424  -40.870 1.00 19.29  ? 52  ASN D OD1 1 
ATOM   6793 N  ND2 . ASN D 1 52  ? -15.969 -3.912  -39.436 1.00 20.75  ? 52  ASN D ND2 1 
ATOM   6794 N  N   . LEU D 1 53  ? -13.288 0.514   -40.822 1.00 11.82  ? 53  LEU D N   1 
ATOM   6795 C  CA  . LEU D 1 53  ? -13.710 1.657   -41.624 1.00 10.31  ? 53  LEU D CA  1 
ATOM   6796 C  C   . LEU D 1 53  ? -14.614 1.192   -42.770 1.00 11.23  ? 53  LEU D C   1 
ATOM   6797 O  O   . LEU D 1 53  ? -14.352 0.156   -43.395 1.00 16.32  ? 53  LEU D O   1 
ATOM   6798 C  CB  . LEU D 1 53  ? -12.495 2.401   -42.180 1.00 11.27  ? 53  LEU D CB  1 
ATOM   6799 C  CG  . LEU D 1 53  ? -11.461 2.754   -41.122 1.00 11.67  ? 53  LEU D CG  1 
ATOM   6800 C  CD1 . LEU D 1 53  ? -10.265 3.437   -41.775 1.00 13.99  ? 53  LEU D CD1 1 
ATOM   6801 C  CD2 . LEU D 1 53  ? -12.073 3.660   -40.018 1.00 15.23  ? 53  LEU D CD2 1 
ATOM   6802 N  N   . SER D 1 54  ? -15.661 1.942   -43.062 1.00 13.30  ? 54  SER D N   1 
ATOM   6803 C  CA  . SER D 1 54  ? -16.589 1.548   -44.112 1.00 13.03  ? 54  SER D CA  1 
ATOM   6804 C  C   . SER D 1 54  ? -15.915 1.618   -45.485 1.00 12.63  ? 54  SER D C   1 
ATOM   6805 O  O   . SER D 1 54  ? -15.269 2.617   -45.837 1.00 15.11  ? 54  SER D O   1 
ATOM   6806 C  CB  . SER D 1 54  ? -17.785 2.442   -44.152 1.00 14.48  ? 54  SER D CB  1 
ATOM   6807 O  OG  . SER D 1 54  ? -18.661 2.069   -45.232 1.00 19.00  ? 54  SER D OG  1 
ATOM   6808 N  N   . ALA D 1 55  ? -16.097 0.551   -46.238 1.00 14.76  ? 55  ALA D N   1 
ATOM   6809 C  CA  . ALA D 1 55  ? -15.701 0.502   -47.638 1.00 16.50  ? 55  ALA D CA  1 
ATOM   6810 C  C   . ALA D 1 55  ? -16.413 1.551   -48.512 1.00 18.67  ? 55  ALA D C   1 
ATOM   6811 O  O   . ALA D 1 55  ? -16.003 1.784   -49.665 1.00 24.61  ? 55  ALA D O   1 
ATOM   6812 C  CB  . ALA D 1 55  ? -15.845 -0.925  -48.186 1.00 21.72  ? 55  ALA D CB  1 
ATOM   6813 N  N   . ASN D 1 56  ? -17.479 2.206   -48.025 1.00 22.47  ? 56  ASN D N   1 
ATOM   6814 C  CA  . ASN D 1 56  ? -18.187 3.187   -48.831 1.00 20.22  ? 56  ASN D CA  1 
ATOM   6815 C  C   . ASN D 1 56  ? -17.727 4.587   -48.443 1.00 21.85  ? 56  ASN D C   1 
ATOM   6816 O  O   . ASN D 1 56  ? -18.245 5.589   -48.955 1.00 27.56  ? 56  ASN D O   1 
ATOM   6817 C  CB  . ASN D 1 56  ? -19.710 3.042   -48.659 1.00 22.38  ? 56  ASN D CB  1 
ATOM   6818 C  CG  . ASN D 1 56  ? -20.290 1.757   -49.213 1.00 28.29  ? 56  ASN D CG  1 
ATOM   6819 O  OD1 . ASN D 1 56  ? -19.666 1.042   -49.986 1.00 45.42  ? 56  ASN D OD1 1 
ATOM   6820 N  ND2 . ASN D 1 56  ? -21.512 1.458   -48.829 1.00 41.81  ? 56  ASN D ND2 1 
ATOM   6821 N  N   . LYS D 1 57  ? -16.774 4.646   -47.491 1.00 17.24  ? 57  LYS D N   1 
ATOM   6822 C  CA  . LYS D 1 57  ? -16.131 5.912   -47.191 1.00 17.97  ? 57  LYS D CA  1 
ATOM   6823 C  C   . LYS D 1 57  ? -14.741 5.861   -47.795 1.00 15.25  ? 57  LYS D C   1 
ATOM   6824 O  O   . LYS D 1 57  ? -14.261 4.795   -48.206 1.00 16.91  ? 57  LYS D O   1 
ATOM   6825 C  CB  . LYS D 1 57  ? -16.067 6.199   -45.676 1.00 16.99  ? 57  LYS D CB  1 
ATOM   6826 C  CG  . LYS D 1 57  ? -17.424 6.506   -45.061 1.00 22.36  ? 57  LYS D CG  1 
ATOM   6827 C  CD  . LYS D 1 57  ? -17.411 6.763   -43.584 1.00 28.94  ? 57  LYS D CD  1 
ATOM   6828 C  CE  . LYS D 1 57  ? -18.512 7.697   -43.115 1.00 34.77  ? 57  LYS D CE  1 
ATOM   6829 N  NZ  . LYS D 1 57  ? -18.355 7.956   -41.663 1.00 32.72  ? 57  LYS D NZ  1 
ATOM   6830 N  N   . GLN D 1 58  ? -14.108 7.030   -47.878 1.00 14.61  ? 58  GLN D N   1 
ATOM   6831 C  CA  . GLN D 1 58  ? -12.773 7.052   -48.432 1.00 17.15  ? 58  GLN D CA  1 
ATOM   6832 C  C   . GLN D 1 58  ? -11.830 7.890   -47.557 1.00 12.89  ? 58  GLN D C   1 
ATOM   6833 O  O   . GLN D 1 58  ? -12.249 8.776   -46.790 1.00 16.13  ? 58  GLN D O   1 
ATOM   6834 C  CB  . GLN D 1 58  ? -12.881 7.328   -49.929 1.00 24.13  ? 58  GLN D CB  1 
ATOM   6835 C  CG  . GLN D 1 58  ? -13.488 8.648   -50.255 1.00 28.13  ? 58  GLN D CG  1 
ATOM   6836 C  CD  . GLN D 1 58  ? -13.415 9.004   -51.720 1.00 31.77  ? 58  GLN D CD  1 
ATOM   6837 O  OE1 . GLN D 1 58  ? -13.133 8.178   -52.612 1.00 30.38  ? 58  GLN D OE1 1 
ATOM   6838 N  NE2 . GLN D 1 58  ? -13.645 10.283  -51.968 1.00 31.49  ? 58  GLN D NE2 1 
ATOM   6839 N  N   . PHE D 1 59  ? -10.555 7.509   -47.594 1.00 12.45  ? 59  PHE D N   1 
ATOM   6840 C  CA  . PHE D 1 59  ? -9.508  7.967   -46.682 1.00 12.07  ? 59  PHE D CA  1 
ATOM   6841 C  C   . PHE D 1 59  ? -8.305  8.370   -47.524 1.00 11.47  ? 59  PHE D C   1 
ATOM   6842 O  O   . PHE D 1 59  ? -7.964  7.771   -48.528 1.00 13.39  ? 59  PHE D O   1 
ATOM   6843 C  CB  . PHE D 1 59  ? -9.158  6.872   -45.666 1.00 11.66  ? 59  PHE D CB  1 
ATOM   6844 C  CG  . PHE D 1 59  ? -10.401 6.510   -44.901 1.00 10.47  ? 59  PHE D CG  1 
ATOM   6845 C  CD1 . PHE D 1 59  ? -11.306 5.534   -45.347 1.00 12.30  ? 59  PHE D CD1 1 
ATOM   6846 C  CD2 . PHE D 1 59  ? -10.727 7.244   -43.767 1.00 11.52  ? 59  PHE D CD2 1 
ATOM   6847 C  CE1 . PHE D 1 59  ? -12.476 5.300   -44.640 1.00 13.09  ? 59  PHE D CE1 1 
ATOM   6848 C  CE2 . PHE D 1 59  ? -11.928 7.024   -43.092 1.00 13.73  ? 59  PHE D CE2 1 
ATOM   6849 C  CZ  . PHE D 1 59  ? -12.797 6.049   -43.531 1.00 13.25  ? 59  PHE D CZ  1 
ATOM   6850 N  N   . LEU D 1 60  ? -7.718  9.502   -47.147 1.00 13.41  ? 60  LEU D N   1 
ATOM   6851 C  CA  . LEU D 1 60  ? -6.740  10.130  -48.014 1.00 13.39  ? 60  LEU D CA  1 
ATOM   6852 C  C   . LEU D 1 60  ? -5.365  9.519   -47.823 1.00 10.98  ? 60  LEU D C   1 
ATOM   6853 O  O   . LEU D 1 60  ? -4.827  9.493   -46.712 1.00 12.25  ? 60  LEU D O   1 
ATOM   6854 C  CB  . LEU D 1 60  ? -6.700  11.607  -47.643 1.00 14.09  ? 60  LEU D CB  1 
ATOM   6855 C  CG  . LEU D 1 60  ? -5.924  12.513  -48.608 1.00 16.48  ? 60  LEU D CG  1 
ATOM   6856 C  CD1 . LEU D 1 60  ? -6.613  12.651  -49.973 1.00 21.37  ? 60  LEU D CD1 1 
ATOM   6857 C  CD2 . LEU D 1 60  ? -5.671  13.914  -48.002 1.00 23.04  ? 60  LEU D CD2 1 
ATOM   6858 N  N   . LEU D 1 61  ? -4.819  9.000   -48.925 1.00 14.01  ? 61  LEU D N   1 
ATOM   6859 C  CA  . LEU D 1 61  ? -3.441  8.537   -48.987 1.00 12.65  ? 61  LEU D CA  1 
ATOM   6860 C  C   . LEU D 1 61  ? -2.590  9.684   -49.525 1.00 14.80  ? 61  LEU D C   1 
ATOM   6861 O  O   . LEU D 1 61  ? -2.975  10.276  -50.529 1.00 14.63  ? 61  LEU D O   1 
ATOM   6862 C  CB  . LEU D 1 61  ? -3.396  7.280   -49.884 1.00 15.55  ? 61  LEU D CB  1 
ATOM   6863 C  CG  . LEU D 1 61  ? -2.116  6.459   -49.980 1.00 15.56  ? 61  LEU D CG  1 
ATOM   6864 C  CD1 . LEU D 1 61  ? -1.987  5.686   -48.686 1.00 18.36  ? 61  LEU D CD1 1 
ATOM   6865 C  CD2 . LEU D 1 61  ? -2.264  5.434   -51.146 1.00 18.34  ? 61  LEU D CD2 1 
ATOM   6866 N  N   . THR D 1 62  ? -1.432  9.966   -48.903 1.00 14.14  ? 62  THR D N   1 
ATOM   6867 C  CA  . THR D 1 62  ? -0.623  11.098  -49.314 1.00 16.42  ? 62  THR D CA  1 
ATOM   6868 C  C   . THR D 1 62  ? 0.826   10.622  -49.302 1.00 18.02  ? 62  THR D C   1 
ATOM   6869 O  O   . THR D 1 62  ? 1.262   9.915   -48.399 1.00 20.84  ? 62  THR D O   1 
ATOM   6870 C  CB  . THR D 1 62  ? -0.830  12.346  -48.434 1.00 20.34  ? 62  THR D CB  1 
ATOM   6871 O  OG1 . THR D 1 62  ? -0.408  12.262  -47.078 1.00 20.08  ? 62  THR D OG1 1 
ATOM   6872 C  CG2 . THR D 1 62  ? -2.206  12.950  -48.413 1.00 19.86  ? 62  THR D CG2 1 
ATOM   6873 N  N   . ASN D 1 63  ? 1.562   10.938  -50.357 1.00 21.27  ? 63  ASN D N   1 
ATOM   6874 C  CA  . ASN D 1 63  ? 2.992   10.756  -50.331 1.00 20.82  ? 63  ASN D CA  1 
ATOM   6875 C  C   . ASN D 1 63  ? 3.562   12.020  -49.755 1.00 24.19  ? 63  ASN D C   1 
ATOM   6876 O  O   . ASN D 1 63  ? 3.500   13.109  -50.385 1.00 21.99  ? 63  ASN D O   1 
ATOM   6877 C  CB  . ASN D 1 63  ? 3.568   10.762  -51.731 1.00 16.57  ? 63  ASN D CB  1 
ATOM   6878 C  CG  . ASN D 1 63  ? 5.074   10.664  -51.801 1.00 13.97  ? 63  ASN D CG  1 
ATOM   6879 O  OD1 . ASN D 1 63  ? 5.785   11.134  -50.918 1.00 16.00  ? 63  ASN D OD1 1 
ATOM   6880 N  ND2 . ASN D 1 63  ? 5.555   9.952   -52.800 1.00 14.91  ? 63  ASN D ND2 1 
ATOM   6881 N  N   . ASN D 1 64  ? 4.206   11.800  -48.598 1.00 15.25  ? 64  ASN D N   1 
ATOM   6882 C  CA  . ASN D 1 64  ? 4.675   13.045  -48.006 1.00 19.23  ? 64  ASN D CA  1 
ATOM   6883 C  C   . ASN D 1 64  ? 6.145   13.360  -48.286 1.00 24.95  ? 64  ASN D C   1 
ATOM   6884 O  O   . ASN D 1 64  ? 6.656   14.374  -47.770 1.00 36.64  ? 64  ASN D O   1 
ATOM   6885 C  CB  . ASN D 1 64  ? 4.655   13.086  -46.470 1.00 23.36  ? 64  ASN D CB  1 
ATOM   6886 C  CG  . ASN D 1 64  ? 5.365   11.988  -45.686 1.00 24.89  ? 64  ASN D CG  1 
ATOM   6887 O  OD1 . ASN D 1 64  ? 6.204   11.230  -46.191 1.00 19.94  ? 64  ASN D OD1 1 
ATOM   6888 N  ND2 . ASN D 1 64  ? 5.023   11.887  -44.403 1.00 30.35  ? 64  ASN D ND2 1 
ATOM   6889 N  N   . GLY D 1 65  ? 6.761   12.579  -49.154 1.00 20.37  ? 65  GLY D N   1 
ATOM   6890 C  CA  . GLY D 1 65  ? 8.181   12.760  -49.374 1.00 20.21  ? 65  GLY D CA  1 
ATOM   6891 C  C   . GLY D 1 65  ? 9.055   11.896  -48.458 1.00 24.91  ? 65  GLY D C   1 
ATOM   6892 O  O   . GLY D 1 65  ? 10.247  11.881  -48.753 1.00 18.10  ? 65  GLY D O   1 
ATOM   6893 N  N   . HIS D 1 66  ? 8.492   11.203  -47.407 1.00 21.55  ? 66  HIS D N   1 
ATOM   6894 C  CA  . HIS D 1 66  ? 9.222   10.365  -46.427 1.00 19.28  ? 66  HIS D CA  1 
ATOM   6895 C  C   . HIS D 1 66  ? 8.663   8.996   -46.178 1.00 13.45  ? 66  HIS D C   1 
ATOM   6896 O  O   . HIS D 1 66  ? 9.445   8.015   -45.990 1.00 17.33  ? 66  HIS D O   1 
ATOM   6897 C  CB  . HIS D 1 66  ? 9.495   10.997  -45.064 1.00 20.00  ? 66  HIS D CB  1 
ATOM   6898 C  CG  . HIS D 1 66  ? 10.011  12.375  -45.208 1.00 18.64  ? 66  HIS D CG  1 
ATOM   6899 N  ND1 . HIS D 1 66  ? 11.376  12.638  -45.441 1.00 18.23  ? 66  HIS D ND1 1 
ATOM   6900 C  CD2 . HIS D 1 66  ? 9.376   13.548  -45.164 1.00 14.75  ? 66  HIS D CD2 1 
ATOM   6901 C  CE1 . HIS D 1 66  ? 11.524  13.951  -45.516 1.00 12.88  ? 66  HIS D CE1 1 
ATOM   6902 N  NE2 . HIS D 1 66  ? 10.295  14.515  -45.389 1.00 19.96  ? 66  HIS D NE2 1 
ATOM   6903 N  N   . SER D 1 67  ? 7.330   8.867   -46.269 1.00 24.62  ? 67  SER D N   1 
ATOM   6904 C  CA  . SER D 1 67  ? 6.692   7.562   -46.238 1.00 21.01  ? 67  SER D CA  1 
ATOM   6905 C  C   . SER D 1 67  ? 5.381   7.740   -46.996 1.00 20.57  ? 67  SER D C   1 
ATOM   6906 O  O   . SER D 1 67  ? 5.037   8.772   -47.482 1.00 28.61  ? 67  SER D O   1 
ATOM   6907 C  CB  . SER D 1 67  ? 6.489   7.116   -44.798 1.00 24.31  ? 67  SER D CB  1 
ATOM   6908 O  OG  . SER D 1 67  ? 5.774   5.891   -44.844 1.00 19.13  ? 67  SER D OG  1 
ATOM   6909 N  N   . VAL D 1 68  ? 4.645   6.657   -47.130 1.00 17.21  ? 68  VAL D N   1 
ATOM   6910 C  CA  . VAL D 1 68  ? 3.334   6.844   -47.707 1.00 20.36  ? 68  VAL D CA  1 
ATOM   6911 C  C   . VAL D 1 68  ? 2.424   6.880   -46.474 1.00 21.04  ? 68  VAL D C   1 
ATOM   6912 O  O   . VAL D 1 68  ? 2.578   5.943   -45.701 1.00 20.15  ? 68  VAL D O   1 
ATOM   6913 C  CB  . VAL D 1 68  ? 3.021   5.709   -48.726 1.00 18.78  ? 68  VAL D CB  1 
ATOM   6914 C  CG1 . VAL D 1 68  ? 3.286   4.261   -48.269 1.00 21.72  ? 68  VAL D CG1 1 
ATOM   6915 C  CG2 . VAL D 1 68  ? 1.606   5.852   -49.215 1.00 24.85  ? 68  VAL D CG2 1 
ATOM   6916 N  N   . LYS D 1 69  ? 1.487   7.862   -46.312 1.00 18.06  ? 69  LYS D N   1 
ATOM   6917 C  CA  . LYS D 1 69  ? 0.563   7.814   -45.170 1.00 17.05  ? 69  LYS D CA  1 
ATOM   6918 C  C   . LYS D 1 69  ? -0.917  7.782   -45.574 1.00 13.50  ? 69  LYS D C   1 
ATOM   6919 O  O   . LYS D 1 69  ? -1.341  8.313   -46.563 1.00 15.37  ? 69  LYS D O   1 
ATOM   6920 C  CB  . LYS D 1 69  ? 0.820   8.880   -44.125 1.00 22.21  ? 69  LYS D CB  1 
ATOM   6921 C  CG  . LYS D 1 69  ? 0.321   10.238  -44.552 1.00 20.09  ? 69  LYS D CG  1 
ATOM   6922 C  CD  . LYS D 1 69  ? 0.633   11.371  -43.546 1.00 25.75  ? 69  LYS D CD  1 
ATOM   6923 C  CE  . LYS D 1 69  ? 1.854   10.976  -42.745 1.00 34.49  ? 69  LYS D CE  1 
ATOM   6924 N  NZ  . LYS D 1 69  ? 2.721   12.124  -42.374 1.00 36.77  ? 69  LYS D NZ  1 
ATOM   6925 N  N   . LEU D 1 70  ? -1.665  7.018   -44.813 1.00 9.16   ? 70  LEU D N   1 
ATOM   6926 C  CA  . LEU D 1 70  ? -3.090  6.984   -44.946 1.00 8.84   ? 70  LEU D CA  1 
ATOM   6927 C  C   . LEU D 1 70  ? -3.684  7.674   -43.734 1.00 9.28   ? 70  LEU D C   1 
ATOM   6928 O  O   . LEU D 1 70  ? -3.409  7.284   -42.591 1.00 9.01   ? 70  LEU D O   1 
ATOM   6929 C  CB  . LEU D 1 70  ? -3.506  5.515   -44.929 1.00 8.41   ? 70  LEU D CB  1 
ATOM   6930 C  CG  . LEU D 1 70  ? -5.017  5.310   -45.106 1.00 9.18   ? 70  LEU D CG  1 
ATOM   6931 C  CD1 . LEU D 1 70  ? -5.500  5.826   -46.452 1.00 13.51  ? 70  LEU D CD1 1 
ATOM   6932 C  CD2 . LEU D 1 70  ? -5.330  3.800   -45.002 1.00 10.88  ? 70  LEU D CD2 1 
ATOM   6933 N  N   . ASN D 1 71  ? -4.478  8.698   -43.996 1.00 9.72   ? 71  ASN D N   1 
ATOM   6934 C  CA  . ASN D 1 71  ? -5.149  9.434   -42.933 1.00 10.43  ? 71  ASN D CA  1 
ATOM   6935 C  C   . ASN D 1 71  ? -6.260  8.580   -42.341 1.00 11.61  ? 71  ASN D C   1 
ATOM   6936 O  O   . ASN D 1 71  ? -6.944  7.845   -43.067 1.00 14.34  ? 71  ASN D O   1 
ATOM   6937 C  CB  . ASN D 1 71  ? -5.759  10.758  -43.440 1.00 11.94  ? 71  ASN D CB  1 
ATOM   6938 C  CG  . ASN D 1 71  ? -4.761  11.864  -43.595 1.00 16.06  ? 71  ASN D CG  1 
ATOM   6939 O  OD1 . ASN D 1 71  ? -3.578  11.692  -43.365 1.00 18.04  ? 71  ASN D OD1 1 
ATOM   6940 N  ND2 . ASN D 1 71  ? -5.250  13.045  -43.958 1.00 22.49  ? 71  ASN D ND2 1 
ATOM   6941 N  N   . LEU D 1 72  ? -6.416  8.716   -41.011 1.00 9.73   ? 72  LEU D N   1 
ATOM   6942 C  CA  . LEU D 1 72  ? -7.398  7.941   -40.276 1.00 10.07  ? 72  LEU D CA  1 
ATOM   6943 C  C   . LEU D 1 72  ? -8.317  8.856   -39.481 1.00 11.55  ? 72  LEU D C   1 
ATOM   6944 O  O   . LEU D 1 72  ? -7.917  9.964   -39.106 1.00 14.10  ? 72  LEU D O   1 
ATOM   6945 C  CB  . LEU D 1 72  ? -6.631  7.021   -39.317 1.00 9.78   ? 72  LEU D CB  1 
ATOM   6946 C  CG  . LEU D 1 72  ? -5.744  5.966   -40.007 1.00 9.02   ? 72  LEU D CG  1 
ATOM   6947 C  CD1 . LEU D 1 72  ? -4.857  5.242   -39.005 1.00 9.24   ? 72  LEU D CD1 1 
ATOM   6948 C  CD2 . LEU D 1 72  ? -6.517  4.931   -40.839 1.00 11.04  ? 72  LEU D CD2 1 
ATOM   6949 N  N   . PRO D 1 73  ? -9.569  8.447   -39.277 1.00 11.57  ? 73  PRO D N   1 
ATOM   6950 C  CA  . PRO D 1 73  ? -10.544 9.307   -38.613 1.00 12.15  ? 73  PRO D CA  1 
ATOM   6951 C  C   . PRO D 1 73  ? -10.382 9.283   -37.085 1.00 11.94  ? 73  PRO D C   1 
ATOM   6952 O  O   . PRO D 1 73  ? -9.998  8.268   -36.491 1.00 12.33  ? 73  PRO D O   1 
ATOM   6953 C  CB  . PRO D 1 73  ? -11.861 8.658   -39.043 1.00 12.54  ? 73  PRO D CB  1 
ATOM   6954 C  CG  . PRO D 1 73  ? -11.494 7.173   -39.083 1.00 12.07  ? 73  PRO D CG  1 
ATOM   6955 C  CD  . PRO D 1 73  ? -10.129 7.144   -39.770 1.00 10.65  ? 73  PRO D CD  1 
ATOM   6956 N  N   . SER D 1 74  ? -10.657 10.441  -36.429 1.00 14.60  ? 74  SER D N   1 
ATOM   6957 C  CA  . SER D 1 74  ? -10.392 10.571  -34.993 1.00 14.78  ? 74  SER D CA  1 
ATOM   6958 C  C   . SER D 1 74  ? -11.340 9.734   -34.141 1.00 17.33  ? 74  SER D C   1 
ATOM   6959 O  O   . SER D 1 74  ? -11.076 9.533   -32.945 1.00 19.69  ? 74  SER D O   1 
ATOM   6960 C  CB  . SER D 1 74  ? -10.261 12.021  -34.558 1.00 17.75  ? 74  SER D CB  1 
ATOM   6961 O  OG  . SER D 1 74  ? -11.462 12.728  -34.836 1.00 22.31  ? 74  SER D OG  1 
ATOM   6962 N  N   . ASP D 1 75  ? -12.413 9.222   -34.745 1.00 15.89  ? 75  ASP D N   1 
ATOM   6963 C  CA  . ASP D 1 75  ? -13.302 8.328   -33.998 1.00 17.20  ? 75  ASP D CA  1 
ATOM   6964 C  C   . ASP D 1 75  ? -12.645 6.958   -33.785 1.00 15.40  ? 75  ASP D C   1 
ATOM   6965 O  O   . ASP D 1 75  ? -13.095 6.189   -32.952 1.00 18.61  ? 75  ASP D O   1 
ATOM   6966 C  CB  . ASP D 1 75  ? -14.682 8.162   -34.641 1.00 22.07  ? 75  ASP D CB  1 
ATOM   6967 C  CG  . ASP D 1 75  ? -14.782 7.263   -35.867 1.00 38.79  ? 75  ASP D CG  1 
ATOM   6968 O  OD1 . ASP D 1 75  ? -14.344 7.685   -36.971 1.00 41.49  ? 75  ASP D OD1 1 
ATOM   6969 O  OD2 . ASP D 1 75  ? -15.327 6.123   -35.708 1.00 51.71  ? 75  ASP D OD2 1 
ATOM   6970 N  N   A MET D 1 76  ? -11.657 6.616   -34.607 0.50 11.59  ? 76  MET D N   1 
ATOM   6971 N  N   B MET D 1 76  ? -11.637 6.639   -34.608 0.50 12.90  ? 76  MET D N   1 
ATOM   6972 C  CA  A MET D 1 76  ? -10.955 5.356   -34.421 0.50 11.14  ? 76  MET D CA  1 
ATOM   6973 C  CA  B MET D 1 76  ? -10.840 5.421   -34.495 0.50 12.57  ? 76  MET D CA  1 
ATOM   6974 C  C   A MET D 1 76  ? -9.919  5.576   -33.321 0.50 11.14  ? 76  MET D C   1 
ATOM   6975 C  C   B MET D 1 76  ? -9.889  5.603   -33.307 0.50 11.29  ? 76  MET D C   1 
ATOM   6976 O  O   A MET D 1 76  ? -9.240  6.597   -33.309 0.50 11.63  ? 76  MET D O   1 
ATOM   6977 O  O   B MET D 1 76  ? -9.244  6.638   -33.198 0.50 12.16  ? 76  MET D O   1 
ATOM   6978 C  CB  A MET D 1 76  ? -10.281 4.940   -35.730 0.50 9.36   ? 76  MET D CB  1 
ATOM   6979 C  CB  B MET D 1 76  ? -10.073 5.195   -35.810 0.50 12.41  ? 76  MET D CB  1 
ATOM   6980 C  CG  A MET D 1 76  ? -9.065  4.040   -35.546 0.50 8.46   ? 76  MET D CG  1 
ATOM   6981 C  CG  B MET D 1 76  ? -9.433  3.801   -35.985 0.50 12.40  ? 76  MET D CG  1 
ATOM   6982 S  SD  A MET D 1 76  ? -8.466  3.826   -37.233 0.50 8.91   ? 76  MET D SD  1 
ATOM   6983 S  SD  B MET D 1 76  ? -8.675  3.610   -37.665 0.50 13.27  ? 76  MET D SD  1 
ATOM   6984 C  CE  A MET D 1 76  ? -7.059  2.744   -37.023 0.50 7.40   ? 76  MET D CE  1 
ATOM   6985 C  CE  B MET D 1 76  ? -8.672  1.837   -38.021 0.50 6.38   ? 76  MET D CE  1 
ATOM   6986 N  N   . HIS D 1 77  ? -9.871  4.678   -32.336 1.00 11.82  ? 77  HIS D N   1 
ATOM   6987 C  CA  . HIS D 1 77  ? -9.032  4.952   -31.185 1.00 11.56  ? 77  HIS D CA  1 
ATOM   6988 C  C   . HIS D 1 77  ? -8.604  3.686   -30.464 1.00 11.11  ? 77  HIS D C   1 
ATOM   6989 O  O   . HIS D 1 77  ? -9.212  2.633   -30.773 1.00 11.99  ? 77  HIS D O   1 
ATOM   6990 C  CB  . HIS D 1 77  ? -9.770  5.910   -30.223 1.00 13.79  ? 77  HIS D CB  1 
ATOM   6991 C  CG  . HIS D 1 77  ? -11.012 5.425   -29.560 1.00 14.33  ? 77  HIS D CG  1 
ATOM   6992 N  ND1 . HIS D 1 77  ? -12.278 5.400   -30.201 1.00 17.47  ? 77  HIS D ND1 1 
ATOM   6993 C  CD2 . HIS D 1 77  ? -11.220 4.988   -28.303 1.00 17.12  ? 77  HIS D CD2 1 
ATOM   6994 C  CE1 . HIS D 1 77  ? -13.194 4.996   -29.335 1.00 18.73  ? 77  HIS D CE1 1 
ATOM   6995 N  NE2 . HIS D 1 77  ? -12.551 4.691   -28.170 1.00 17.90  ? 77  HIS D NE2 1 
ATOM   6996 N  N   . ILE D 1 78  ? -7.655  3.829   -29.534 1.00 11.53  ? 78  ILE D N   1 
ATOM   6997 C  CA  . ILE D 1 78  ? -7.368  2.705   -28.656 1.00 11.67  ? 78  ILE D CA  1 
ATOM   6998 C  C   . ILE D 1 78  ? -7.788  3.018   -27.242 1.00 12.23  ? 78  ILE D C   1 
ATOM   6999 O  O   . ILE D 1 78  ? -7.579  4.183   -26.771 1.00 12.48  ? 78  ILE D O   1 
ATOM   7000 C  CB  . ILE D 1 78  ? -5.903  2.304   -28.739 1.00 15.46  ? 78  ILE D CB  1 
ATOM   7001 C  CG1 . ILE D 1 78  ? -4.919  3.435   -28.485 1.00 16.46  ? 78  ILE D CG1 1 
ATOM   7002 C  CG2 . ILE D 1 78  ? -5.600  1.672   -30.090 1.00 19.28  ? 78  ILE D CG2 1 
ATOM   7003 C  CD1 . ILE D 1 78  ? -3.524  3.024   -29.038 1.00 18.94  ? 78  ILE D CD1 1 
ATOM   7004 N  N   . GLN D 1 79  ? -8.266  1.978   -26.575 1.00 14.72  ? 79  GLN D N   1 
ATOM   7005 C  CA  . GLN D 1 79  ? -8.535  2.033   -25.137 1.00 16.10  ? 79  GLN D CA  1 
ATOM   7006 C  C   . GLN D 1 79  ? -7.577  1.091   -24.407 1.00 14.40  ? 79  GLN D C   1 
ATOM   7007 O  O   . GLN D 1 79  ? -7.183  0.046   -24.928 1.00 16.25  ? 79  GLN D O   1 
ATOM   7008 C  CB  . GLN D 1 79  ? -9.973  1.617   -24.799 1.00 22.03  ? 79  GLN D CB  1 
ATOM   7009 C  CG  . GLN D 1 79  ? -10.991 2.707   -25.163 1.00 25.07  ? 79  GLN D CG  1 
ATOM   7010 C  CD  . GLN D 1 79  ? -11.001 3.931   -24.276 1.00 35.00  ? 79  GLN D CD  1 
ATOM   7011 O  OE1 . GLN D 1 79  ? -10.765 3.874   -23.067 1.00 49.75  ? 79  GLN D OE1 1 
ATOM   7012 N  NE2 . GLN D 1 79  ? -11.336 5.070   -24.864 1.00 36.79  ? 79  GLN D NE2 1 
ATOM   7013 N  N   . GLY D 1 80  ? -7.225  1.457   -23.172 1.00 16.68  ? 80  GLY D N   1 
ATOM   7014 C  CA  . GLY D 1 80  ? -6.380  0.591   -22.383 1.00 15.50  ? 80  GLY D CA  1 
ATOM   7015 C  C   . GLY D 1 80  ? -5.195  1.349   -21.814 1.00 18.61  ? 80  GLY D C   1 
ATOM   7016 O  O   . GLY D 1 80  ? -4.638  0.933   -20.819 1.00 20.36  ? 80  GLY D O   1 
ATOM   7017 N  N   . LEU D 1 81  ? -4.846  2.501   -22.415 1.00 13.72  ? 81  LEU D N   1 
ATOM   7018 C  CA  . LEU D 1 81  ? -3.752  3.294   -21.857 1.00 14.34  ? 81  LEU D CA  1 
ATOM   7019 C  C   . LEU D 1 81  ? -4.256  4.258   -20.783 1.00 12.07  ? 81  LEU D C   1 
ATOM   7020 O  O   . LEU D 1 81  ? -5.400  4.189   -20.344 1.00 16.12  ? 81  LEU D O   1 
ATOM   7021 C  CB  . LEU D 1 81  ? -3.013  4.014   -23.005 1.00 14.73  ? 81  LEU D CB  1 
ATOM   7022 C  CG  . LEU D 1 81  ? -2.455  3.077   -24.080 1.00 13.88  ? 81  LEU D CG  1 
ATOM   7023 C  CD1 . LEU D 1 81  ? -1.885  3.862   -25.268 1.00 16.27  ? 81  LEU D CD1 1 
ATOM   7024 C  CD2 . LEU D 1 81  ? -1.349  2.254   -23.432 1.00 13.84  ? 81  LEU D CD2 1 
ATOM   7025 N  N   . GLN D 1 82  ? -3.401  5.233   -20.395 1.00 13.48  ? 82  GLN D N   1 
ATOM   7026 C  CA  . GLN D 1 82  ? -3.767  6.089   -19.269 1.00 12.14  ? 82  GLN D CA  1 
ATOM   7027 C  C   . GLN D 1 82  ? -4.744  7.187   -19.731 1.00 13.10  ? 82  GLN D C   1 
ATOM   7028 O  O   . GLN D 1 82  ? -5.415  7.827   -18.894 1.00 13.23  ? 82  GLN D O   1 
ATOM   7029 C  CB  . GLN D 1 82  ? -2.519  6.800   -18.693 1.00 13.00  ? 82  GLN D CB  1 
ATOM   7030 C  CG  . GLN D 1 82  ? -2.055  8.105   -19.333 1.00 15.93  ? 82  GLN D CG  1 
ATOM   7031 C  CD  . GLN D 1 82  ? -1.490  7.878   -20.722 1.00 14.76  ? 82  GLN D CD  1 
ATOM   7032 O  OE1 . GLN D 1 82  ? -1.308  6.749   -21.223 1.00 18.18  ? 82  GLN D OE1 1 
ATOM   7033 N  NE2 . GLN D 1 82  ? -1.179  8.982   -21.381 1.00 15.40  ? 82  GLN D NE2 1 
ATOM   7034 N  N   . SER D 1 83  ? -4.870  7.346   -21.056 1.00 12.05  ? 83  SER D N   1 
ATOM   7035 C  CA  . SER D 1 83  ? -5.742  8.301   -21.705 1.00 10.38  ? 83  SER D CA  1 
ATOM   7036 C  C   . SER D 1 83  ? -6.305  7.639   -22.946 1.00 10.89  ? 83  SER D C   1 
ATOM   7037 O  O   . SER D 1 83  ? -5.662  6.712   -23.459 1.00 12.16  ? 83  SER D O   1 
ATOM   7038 C  CB  . SER D 1 83  ? -4.956  9.555   -22.131 1.00 12.42  ? 83  SER D CB  1 
ATOM   7039 O  OG  . SER D 1 83  ? -4.424  10.241  -20.993 1.00 14.03  ? 83  SER D OG  1 
ATOM   7040 N  N   . ARG D 1 84  ? -7.390  8.178   -23.517 1.00 12.34  ? 84  ARG D N   1 
ATOM   7041 C  CA  . ARG D 1 84  ? -7.778  7.801   -24.879 1.00 11.33  ? 84  ARG D CA  1 
ATOM   7042 C  C   . ARG D 1 84  ? -6.766  8.358   -25.870 1.00 10.85  ? 84  ARG D C   1 
ATOM   7043 O  O   . ARG D 1 84  ? -6.413  9.549   -25.831 1.00 11.62  ? 84  ARG D O   1 
ATOM   7044 C  CB  . ARG D 1 84  ? -9.210  8.269   -25.211 1.00 11.08  ? 84  ARG D CB  1 
ATOM   7045 C  CG  . ARG D 1 84  ? -9.588  8.100   -26.675 1.00 11.94  ? 84  ARG D CG  1 
ATOM   7046 C  CD  . ARG D 1 84  ? -11.047 8.409   -26.993 1.00 13.38  ? 84  ARG D CD  1 
ATOM   7047 N  NE  . ARG D 1 84  ? -11.126 8.631   -28.430 1.00 14.02  ? 84  ARG D NE  1 
ATOM   7048 C  CZ  . ARG D 1 84  ? -12.298 8.676   -29.102 1.00 17.21  ? 84  ARG D CZ  1 
ATOM   7049 N  NH1 . ARG D 1 84  ? -13.436 8.512   -28.419 1.00 20.56  ? 84  ARG D NH1 1 
ATOM   7050 N  NH2 . ARG D 1 84  ? -12.323 8.858   -30.431 1.00 18.25  ? 84  ARG D NH2 1 
ATOM   7051 N  N   . TYR D 1 85  ? -6.317  7.491   -26.779 1.00 10.07  ? 85  TYR D N   1 
ATOM   7052 C  CA  . TYR D 1 85  ? -5.494  7.874   -27.914 1.00 9.33   ? 85  TYR D CA  1 
ATOM   7053 C  C   . TYR D 1 85  ? -6.243  7.633   -29.214 1.00 10.97  ? 85  TYR D C   1 
ATOM   7054 O  O   . TYR D 1 85  ? -6.724  6.495   -29.519 1.00 12.06  ? 85  TYR D O   1 
ATOM   7055 C  CB  . TYR D 1 85  ? -4.154  7.121   -27.924 1.00 9.24   ? 85  TYR D CB  1 
ATOM   7056 C  CG  . TYR D 1 85  ? -3.170  7.666   -26.919 1.00 9.20   ? 85  TYR D CG  1 
ATOM   7057 C  CD1 . TYR D 1 85  ? -3.207  7.264   -25.575 1.00 10.78  ? 85  TYR D CD1 1 
ATOM   7058 C  CD2 . TYR D 1 85  ? -2.178  8.570   -27.311 1.00 10.24  ? 85  TYR D CD2 1 
ATOM   7059 C  CE1 . TYR D 1 85  ? -2.270  7.722   -24.660 1.00 9.79   ? 85  TYR D CE1 1 
ATOM   7060 C  CE2 . TYR D 1 85  ? -1.268  9.062   -26.396 1.00 10.10  ? 85  TYR D CE2 1 
ATOM   7061 C  CZ  . TYR D 1 85  ? -1.344  8.676   -25.062 1.00 10.30  ? 85  TYR D CZ  1 
ATOM   7062 O  OH  . TYR D 1 85  ? -0.446  9.138   -24.158 1.00 12.05  ? 85  TYR D OH  1 
ATOM   7063 N  N   . SER D 1 86  ? -6.448  8.713   -29.968 1.00 10.80  ? 86  SER D N   1 
ATOM   7064 C  CA  . SER D 1 86  ? -7.231  8.640   -31.199 1.00 10.26  ? 86  SER D CA  1 
ATOM   7065 C  C   . SER D 1 86  ? -6.343  8.563   -32.440 1.00 8.31   ? 86  SER D C   1 
ATOM   7066 O  O   . SER D 1 86  ? -5.269  9.126   -32.462 1.00 9.24   ? 86  SER D O   1 
ATOM   7067 C  CB  . SER D 1 86  ? -8.155  9.862   -31.349 1.00 11.88  ? 86  SER D CB  1 
ATOM   7068 O  OG  . SER D 1 86  ? -9.126  9.890   -30.297 1.00 13.25  ? 86  SER D OG  1 
ATOM   7069 N  N   . ALA D 1 87  ? -6.757  7.786   -33.452 1.00 10.58  ? 87  ALA D N   1 
ATOM   7070 C  CA  . ALA D 1 87  ? -5.937  7.592   -34.628 1.00 9.47   ? 87  ALA D CA  1 
ATOM   7071 C  C   . ALA D 1 87  ? -5.761  8.909   -35.404 1.00 9.53   ? 87  ALA D C   1 
ATOM   7072 O  O   . ALA D 1 87  ? -6.698  9.744   -35.449 1.00 11.81  ? 87  ALA D O   1 
ATOM   7073 C  CB  . ALA D 1 87  ? -6.517  6.523   -35.515 1.00 11.01  ? 87  ALA D CB  1 
ATOM   7074 N  N   . THR D 1 88  ? -4.594  9.035   -36.084 1.00 8.49   ? 88  THR D N   1 
ATOM   7075 C  CA  . THR D 1 88  ? -4.382  10.152  -37.003 1.00 9.40   ? 88  THR D CA  1 
ATOM   7076 C  C   . THR D 1 88  ? -3.979  9.626   -38.383 1.00 9.07   ? 88  THR D C   1 
ATOM   7077 O  O   . THR D 1 88  ? -4.443  10.135  -39.411 1.00 10.38  ? 88  THR D O   1 
ATOM   7078 C  CB  . THR D 1 88  ? -3.449  11.206  -36.384 1.00 14.88  ? 88  THR D CB  1 
ATOM   7079 O  OG1 . THR D 1 88  ? -3.375  12.280  -37.333 1.00 19.72  ? 88  THR D OG1 1 
ATOM   7080 C  CG2 . THR D 1 88  ? -2.086  10.694  -36.020 1.00 16.67  ? 88  THR D CG2 1 
ATOM   7081 N  N   . GLN D 1 89  ? -3.070  8.621   -38.453 1.00 8.17   ? 89  GLN D N   1 
ATOM   7082 C  CA  . GLN D 1 89  ? -2.565  8.194   -39.754 1.00 8.71   ? 89  GLN D CA  1 
ATOM   7083 C  C   . GLN D 1 89  ? -1.821  6.871   -39.547 1.00 8.89   ? 89  GLN D C   1 
ATOM   7084 O  O   . GLN D 1 89  ? -1.408  6.583   -38.418 1.00 8.46   ? 89  GLN D O   1 
ATOM   7085 C  CB  . GLN D 1 89  ? -1.644  9.279   -40.360 1.00 8.90   ? 89  GLN D CB  1 
ATOM   7086 C  CG  . GLN D 1 89  ? -0.469  9.680   -39.479 1.00 11.55  ? 89  GLN D CG  1 
ATOM   7087 C  CD  . GLN D 1 89  ? 0.844   9.160   -39.987 1.00 10.99  ? 89  GLN D CD  1 
ATOM   7088 O  OE1 . GLN D 1 89  ? 0.968   7.975   -40.301 1.00 10.48  ? 89  GLN D OE1 1 
ATOM   7089 N  NE2 . GLN D 1 89  ? 1.885   9.938   -40.040 1.00 14.41  ? 89  GLN D NE2 1 
ATOM   7090 N  N   . LEU D 1 90  ? -1.647  6.106   -40.624 1.00 8.16   ? 90  LEU D N   1 
ATOM   7091 C  CA  . LEU D 1 90  ? -0.670  5.017   -40.645 1.00 8.03   ? 90  LEU D CA  1 
ATOM   7092 C  C   . LEU D 1 90  ? 0.274   5.203   -41.825 1.00 7.00   ? 90  LEU D C   1 
ATOM   7093 O  O   . LEU D 1 90  ? -0.009  5.877   -42.805 1.00 8.66   ? 90  LEU D O   1 
ATOM   7094 C  CB  . LEU D 1 90  ? -1.340  3.638   -40.655 1.00 8.09   ? 90  LEU D CB  1 
ATOM   7095 C  CG  . LEU D 1 90  ? -2.334  3.285   -41.768 1.00 8.24   ? 90  LEU D CG  1 
ATOM   7096 C  CD1 . LEU D 1 90  ? -1.676  2.910   -43.053 1.00 9.13   ? 90  LEU D CD1 1 
ATOM   7097 C  CD2 . LEU D 1 90  ? -3.248  2.126   -41.350 1.00 9.81   ? 90  LEU D CD2 1 
ATOM   7098 N  N   . HIS D 1 91  ? 1.450   4.580   -41.706 1.00 7.15   ? 91  HIS D N   1 
ATOM   7099 C  CA  . HIS D 1 91  ? 2.512   4.642   -42.701 1.00 6.85   ? 91  HIS D CA  1 
ATOM   7100 C  C   . HIS D 1 91  ? 3.403   3.415   -42.531 1.00 6.47   ? 91  HIS D C   1 
ATOM   7101 O  O   . HIS D 1 91  ? 3.317   2.753   -41.479 1.00 7.96   ? 91  HIS D O   1 
ATOM   7102 C  CB  . HIS D 1 91  ? 3.196   6.042   -42.625 1.00 7.59   ? 91  HIS D CB  1 
ATOM   7103 C  CG  . HIS D 1 91  ? 3.954   6.187   -41.338 1.00 7.46   ? 91  HIS D CG  1 
ATOM   7104 N  ND1 . HIS D 1 91  ? 3.386   6.760   -40.196 1.00 8.10   ? 91  HIS D ND1 1 
ATOM   7105 C  CD2 . HIS D 1 91  ? 5.192   5.750   -40.948 1.00 8.36   ? 91  HIS D CD2 1 
ATOM   7106 C  CE1 . HIS D 1 91  ? 4.256   6.702   -39.199 1.00 7.27   ? 91  HIS D CE1 1 
ATOM   7107 N  NE2 . HIS D 1 91  ? 5.368   6.038   -39.605 1.00 7.38   ? 91  HIS D NE2 1 
ATOM   7108 N  N   . LEU D 1 92  ? 4.369   3.314   -43.442 1.00 6.80   ? 92  LEU D N   1 
ATOM   7109 C  CA  . LEU D 1 92  ? 5.296   2.189   -43.398 1.00 7.70   ? 92  LEU D CA  1 
ATOM   7110 C  C   . LEU D 1 92  ? 6.746   2.610   -43.583 1.00 7.37   ? 92  LEU D C   1 
ATOM   7111 O  O   . LEU D 1 92  ? 7.066   3.784   -43.929 1.00 7.68   ? 92  LEU D O   1 
ATOM   7112 C  CB  . LEU D 1 92  ? 4.966   1.125   -44.439 1.00 10.28  ? 92  LEU D CB  1 
ATOM   7113 C  CG  . LEU D 1 92  ? 3.571   0.500   -44.324 1.00 9.46   ? 92  LEU D CG  1 
ATOM   7114 C  CD1 . LEU D 1 92  ? 2.602   1.211   -45.269 1.00 11.45  ? 92  LEU D CD1 1 
ATOM   7115 C  CD2 . LEU D 1 92  ? 3.591   -0.996  -44.613 1.00 9.62   ? 92  LEU D CD2 1 
ATOM   7116 N  N   . HIS D 1 93  ? 7.646   1.744   -43.139 1.00 8.51   ? 93  HIS D N   1 
ATOM   7117 C  CA  . HIS D 1 93  ? 9.073   1.893   -43.317 1.00 7.36   ? 93  HIS D CA  1 
ATOM   7118 C  C   . HIS D 1 93  ? 9.579   0.646   -44.021 1.00 5.84   ? 93  HIS D C   1 
ATOM   7119 O  O   . HIS D 1 93  ? 9.145   -0.464  -43.688 1.00 7.91   ? 93  HIS D O   1 
ATOM   7120 C  CB  . HIS D 1 93  ? 9.806   2.072   -41.976 1.00 8.40   ? 93  HIS D CB  1 
ATOM   7121 C  CG  . HIS D 1 93  ? 9.324   3.287   -41.243 1.00 6.78   ? 93  HIS D CG  1 
ATOM   7122 N  ND1 . HIS D 1 93  ? 9.972   4.524   -41.327 1.00 8.20   ? 93  HIS D ND1 1 
ATOM   7123 C  CD2 . HIS D 1 93  ? 8.291   3.408   -40.395 1.00 6.17   ? 93  HIS D CD2 1 
ATOM   7124 C  CE1 . HIS D 1 93  ? 9.252   5.338   -40.568 1.00 6.78   ? 93  HIS D CE1 1 
ATOM   7125 N  NE2 . HIS D 1 93  ? 8.286   4.747   -39.958 1.00 6.74   ? 93  HIS D NE2 1 
ATOM   7126 N  N   . TRP D 1 94  ? 10.541  0.779   -44.954 1.00 6.89   ? 94  TRP D N   1 
ATOM   7127 C  CA  . TRP D 1 94  ? 11.012  -0.391  -45.691 1.00 6.34   ? 94  TRP D CA  1 
ATOM   7128 C  C   . TRP D 1 94  ? 12.473  -0.206  -46.181 1.00 5.80   ? 94  TRP D C   1 
ATOM   7129 O  O   . TRP D 1 94  ? 13.083  0.878   -46.037 1.00 8.29   ? 94  TRP D O   1 
ATOM   7130 C  CB  . TRP D 1 94  ? 10.085  -0.665  -46.883 1.00 8.07   ? 94  TRP D CB  1 
ATOM   7131 C  CG  . TRP D 1 94  ? 9.937   0.499   -47.832 1.00 8.35   ? 94  TRP D CG  1 
ATOM   7132 C  CD1 . TRP D 1 94  ? 10.730  0.778   -48.917 1.00 8.84   ? 94  TRP D CD1 1 
ATOM   7133 C  CD2 . TRP D 1 94  ? 8.911   1.527   -47.791 1.00 6.96   ? 94  TRP D CD2 1 
ATOM   7134 N  NE1 . TRP D 1 94  ? 10.308  1.953   -49.525 1.00 8.52   ? 94  TRP D NE1 1 
ATOM   7135 C  CE2 . TRP D 1 94  ? 9.138   2.377   -48.916 1.00 8.00   ? 94  TRP D CE2 1 
ATOM   7136 C  CE3 . TRP D 1 94  ? 7.775   1.769   -46.993 1.00 7.28   ? 94  TRP D CE3 1 
ATOM   7137 C  CZ2 . TRP D 1 94  ? 8.375   3.571   -49.132 1.00 8.74   ? 94  TRP D CZ2 1 
ATOM   7138 C  CZ3 . TRP D 1 94  ? 7.061   2.940   -47.186 1.00 8.62   ? 94  TRP D CZ3 1 
ATOM   7139 C  CH2 . TRP D 1 94  ? 7.311   3.793   -48.288 1.00 8.37   ? 94  TRP D CH2 1 
ATOM   7140 N  N   . GLY D 1 95  ? 13.025  -1.225  -46.809 1.00 7.37   ? 95  GLY D N   1 
ATOM   7141 C  CA  . GLY D 1 95  ? 14.381  -1.206  -47.337 1.00 7.02   ? 95  GLY D CA  1 
ATOM   7142 C  C   . GLY D 1 95  ? 14.397  -1.001  -48.855 1.00 8.54   ? 95  GLY D C   1 
ATOM   7143 O  O   . GLY D 1 95  ? 14.007  0.079   -49.329 1.00 8.29   ? 95  GLY D O   1 
ATOM   7144 N  N   . ASN D 1 96  ? 15.009  -1.951  -49.585 1.00 10.72  ? 96  ASN D N   1 
ATOM   7145 C  CA  . ASN D 1 96  ? 15.198  -1.700  -51.001 1.00 9.90   ? 96  ASN D CA  1 
ATOM   7146 C  C   . ASN D 1 96  ? 15.276  -3.041  -51.712 1.00 9.50   ? 96  ASN D C   1 
ATOM   7147 O  O   . ASN D 1 96  ? 15.386  -4.032  -51.036 1.00 12.13  ? 96  ASN D O   1 
ATOM   7148 C  CB  . ASN D 1 96  ? 16.432  -0.844  -51.307 1.00 13.83  ? 96  ASN D CB  1 
ATOM   7149 C  CG  . ASN D 1 96  ? 17.754  -1.554  -51.007 1.00 16.24  ? 96  ASN D CG  1 
ATOM   7150 O  OD1 . ASN D 1 96  ? 18.185  -2.449  -51.735 1.00 22.91  ? 96  ASN D OD1 1 
ATOM   7151 N  ND2 . ASN D 1 96  ? 18.394  -1.210  -49.901 1.00 17.15  ? 96  ASN D ND2 1 
ATOM   7152 N  N   . PRO D 1 97  ? 15.161  -3.095  -53.047 1.00 11.67  ? 97  PRO D N   1 
ATOM   7153 C  CA  . PRO D 1 97  ? 15.047  -4.366  -53.742 1.00 13.79  ? 97  PRO D CA  1 
ATOM   7154 C  C   . PRO D 1 97  ? 16.179  -5.350  -53.436 1.00 16.78  ? 97  PRO D C   1 
ATOM   7155 O  O   . PRO D 1 97  ? 15.947  -6.553  -53.334 1.00 20.47  ? 97  PRO D O   1 
ATOM   7156 C  CB  . PRO D 1 97  ? 15.018  -3.924  -55.221 1.00 17.50  ? 97  PRO D CB  1 
ATOM   7157 C  CG  . PRO D 1 97  ? 14.406  -2.554  -55.211 1.00 17.87  ? 97  PRO D CG  1 
ATOM   7158 C  CD  . PRO D 1 97  ? 14.986  -1.945  -53.962 1.00 14.46  ? 97  PRO D CD  1 
ATOM   7159 N  N   . ASN D 1 98  ? 17.410  -4.867  -53.268 1.00 15.54  ? 98  ASN D N   1 
ATOM   7160 C  CA  . ASN D 1 98  ? 18.507  -5.770  -53.024 1.00 21.41  ? 98  ASN D CA  1 
ATOM   7161 C  C   . ASN D 1 98  ? 18.677  -6.070  -51.544 1.00 20.58  ? 98  ASN D C   1 
ATOM   7162 O  O   . ASN D 1 98  ? 19.386  -7.026  -51.226 1.00 28.99  ? 98  ASN D O   1 
ATOM   7163 C  CB  . ASN D 1 98  ? 19.765  -5.318  -53.742 1.00 27.03  ? 98  ASN D CB  1 
ATOM   7164 C  CG  . ASN D 1 98  ? 19.571  -5.436  -55.250 1.00 28.95  ? 98  ASN D CG  1 
ATOM   7165 O  OD1 . ASN D 1 98  ? 19.107  -6.446  -55.787 1.00 30.95  ? 98  ASN D OD1 1 
ATOM   7166 N  ND2 . ASN D 1 98  ? 19.800  -4.345  -55.929 1.00 40.31  ? 98  ASN D ND2 1 
ATOM   7167 N  N   . ASP D 1 99  ? 18.035  -5.299  -50.651 1.00 16.21  ? 99  ASP D N   1 
ATOM   7168 C  CA  . ASP D 1 99  ? 18.120  -5.483  -49.208 1.00 12.89  ? 99  ASP D CA  1 
ATOM   7169 C  C   . ASP D 1 99  ? 16.742  -5.291  -48.556 1.00 9.54   ? 99  ASP D C   1 
ATOM   7170 O  O   . ASP D 1 99  ? 16.428  -4.221  -47.983 1.00 11.87  ? 99  ASP D O   1 
ATOM   7171 C  CB  . ASP D 1 99  ? 19.136  -4.530  -48.549 1.00 16.03  ? 99  ASP D CB  1 
ATOM   7172 C  CG  . ASP D 1 99  ? 19.321  -4.795  -47.058 1.00 18.15  ? 99  ASP D CG  1 
ATOM   7173 O  OD1 . ASP D 1 99  ? 18.932  -5.890  -46.598 1.00 16.30  ? 99  ASP D OD1 1 
ATOM   7174 O  OD2 . ASP D 1 99  ? 19.759  -3.865  -46.339 1.00 22.79  ? 99  ASP D OD2 1 
ATOM   7175 N  N   . PRO D 1 100 ? 15.826  -6.243  -48.666 1.00 11.78  ? 100 PRO D N   1 
ATOM   7176 C  CA  . PRO D 1 100 ? 14.448  -6.062  -48.167 1.00 9.76   ? 100 PRO D CA  1 
ATOM   7177 C  C   . PRO D 1 100 ? 14.455  -6.368  -46.665 1.00 10.19  ? 100 PRO D C   1 
ATOM   7178 O  O   . PRO D 1 100 ? 13.734  -7.261  -46.195 1.00 12.36  ? 100 PRO D O   1 
ATOM   7179 C  CB  . PRO D 1 100 ? 13.634  -7.073  -48.984 1.00 12.59  ? 100 PRO D CB  1 
ATOM   7180 C  CG  . PRO D 1 100 ? 14.629  -8.183  -49.151 1.00 14.43  ? 100 PRO D CG  1 
ATOM   7181 C  CD  . PRO D 1 100 ? 15.978  -7.499  -49.429 1.00 11.23  ? 100 PRO D CD  1 
ATOM   7182 N  N   . HIS D 1 101 ? 15.127  -5.499  -45.893 1.00 9.26   ? 101 HIS D N   1 
ATOM   7183 C  CA  . HIS D 1 101 ? 15.279  -5.695  -44.441 1.00 9.13   ? 101 HIS D CA  1 
ATOM   7184 C  C   . HIS D 1 101 ? 15.245  -4.302  -43.806 1.00 10.02  ? 101 HIS D C   1 
ATOM   7185 O  O   . HIS D 1 101 ? 16.261  -3.917  -43.219 1.00 12.49  ? 101 HIS D O   1 
ATOM   7186 C  CB  . HIS D 1 101 ? 16.576  -6.486  -44.152 1.00 12.94  ? 101 HIS D CB  1 
ATOM   7187 C  CG  . HIS D 1 101 ? 16.639  -7.834  -44.805 1.00 12.88  ? 101 HIS D CG  1 
ATOM   7188 N  ND1 . HIS D 1 101 ? 15.901  -8.956  -44.382 1.00 14.81  ? 101 HIS D ND1 1 
ATOM   7189 C  CD2 . HIS D 1 101 ? 17.232  -8.167  -45.965 1.00 12.66  ? 101 HIS D CD2 1 
ATOM   7190 C  CE1 . HIS D 1 101 ? 16.170  -9.979  -45.174 1.00 15.14  ? 101 HIS D CE1 1 
ATOM   7191 N  NE2 . HIS D 1 101 ? 16.971  -9.499  -46.183 1.00 16.99  ? 101 HIS D NE2 1 
ATOM   7192 N  N   . GLY D 1 102 ? 14.062  -3.671  -43.913 1.00 7.04   ? 102 GLY D N   1 
ATOM   7193 C  CA  . GLY D 1 102 ? 13.972  -2.249  -43.601 1.00 9.10   ? 102 GLY D CA  1 
ATOM   7194 C  C   . GLY D 1 102 ? 12.977  -1.970  -42.472 1.00 7.45   ? 102 GLY D C   1 
ATOM   7195 O  O   . GLY D 1 102 ? 12.543  -0.818  -42.329 1.00 8.58   ? 102 GLY D O   1 
ATOM   7196 N  N   . SER D 1 103 ? 12.741  -2.896  -41.534 1.00 7.89   ? 103 SER D N   1 
ATOM   7197 C  CA  . SER D 1 103 ? 12.043  -2.553  -40.312 1.00 8.23   ? 103 SER D CA  1 
ATOM   7198 C  C   . SER D 1 103 ? 12.867  -1.517  -39.530 1.00 7.79   ? 103 SER D C   1 
ATOM   7199 O  O   . SER D 1 103 ? 14.084  -1.453  -39.648 1.00 8.53   ? 103 SER D O   1 
ATOM   7200 C  CB  . SER D 1 103 ? 11.724  -3.817  -39.480 1.00 7.94   ? 103 SER D CB  1 
ATOM   7201 O  OG  . SER D 1 103 ? 12.875  -4.336  -38.862 1.00 8.82   ? 103 SER D OG  1 
ATOM   7202 N  N   . GLU D 1 104 ? 12.197  -0.768  -38.636 1.00 7.54   ? 104 GLU D N   1 
ATOM   7203 C  CA  . GLU D 1 104 ? 12.882  0.167   -37.737 1.00 7.66   ? 104 GLU D CA  1 
ATOM   7204 C  C   . GLU D 1 104 ? 13.333  -0.548  -36.470 1.00 8.19   ? 104 GLU D C   1 
ATOM   7205 O  O   . GLU D 1 104 ? 14.501  -0.580  -36.146 1.00 9.27   ? 104 GLU D O   1 
ATOM   7206 C  CB  . GLU D 1 104 ? 11.973  1.370   -37.416 1.00 7.62   ? 104 GLU D CB  1 
ATOM   7207 C  CG  . GLU D 1 104 ? 11.612  2.167   -38.729 1.00 7.29   ? 104 GLU D CG  1 
ATOM   7208 C  CD  . GLU D 1 104 ? 11.510  3.667   -38.468 1.00 7.92   ? 104 GLU D CD  1 
ATOM   7209 O  OE1 . GLU D 1 104 ? 10.468  4.051   -37.887 1.00 8.42   ? 104 GLU D OE1 1 
ATOM   7210 O  OE2 . GLU D 1 104 ? 12.474  4.349   -38.862 1.00 9.04   ? 104 GLU D OE2 1 
ATOM   7211 N  N   . HIS D 1 105 ? 12.351  -1.128  -35.747 1.00 8.32   ? 105 HIS D N   1 
ATOM   7212 C  CA  . HIS D 1 105 ? 12.683  -1.962  -34.607 1.00 7.72   ? 105 HIS D CA  1 
ATOM   7213 C  C   . HIS D 1 105 ? 13.299  -3.300  -35.099 1.00 8.17   ? 105 HIS D C   1 
ATOM   7214 O  O   . HIS D 1 105 ? 12.981  -3.780  -36.204 1.00 8.89   ? 105 HIS D O   1 
ATOM   7215 C  CB  . HIS D 1 105 ? 11.425  -2.261  -33.768 1.00 8.35   ? 105 HIS D CB  1 
ATOM   7216 C  CG  . HIS D 1 105 ? 10.958  -1.020  -33.113 1.00 8.35   ? 105 HIS D CG  1 
ATOM   7217 N  ND1 . HIS D 1 105 ? 9.979   -0.189  -33.688 1.00 7.80   ? 105 HIS D ND1 1 
ATOM   7218 C  CD2 . HIS D 1 105 ? 11.225  -0.548  -31.887 1.00 9.07   ? 105 HIS D CD2 1 
ATOM   7219 C  CE1 . HIS D 1 105 ? 9.817   0.844   -32.836 1.00 8.47   ? 105 HIS D CE1 1 
ATOM   7220 N  NE2 . HIS D 1 105 ? 10.612  0.704   -31.778 1.00 8.87   ? 105 HIS D NE2 1 
ATOM   7221 N  N   . THR D 1 106 ? 14.302  -3.766  -34.360 1.00 9.16   ? 106 THR D N   1 
ATOM   7222 C  CA  . THR D 1 106 ? 14.877  -5.066  -34.692 1.00 8.97   ? 106 THR D CA  1 
ATOM   7223 C  C   . THR D 1 106 ? 14.652  -5.962  -33.475 1.00 10.13  ? 106 THR D C   1 
ATOM   7224 O  O   . THR D 1 106 ? 14.306  -5.513  -32.391 1.00 9.71   ? 106 THR D O   1 
ATOM   7225 C  CB  . THR D 1 106 ? 16.387  -4.910  -34.977 1.00 10.19  ? 106 THR D CB  1 
ATOM   7226 O  OG1 . THR D 1 106 ? 17.101  -4.301  -33.884 1.00 11.26  ? 106 THR D OG1 1 
ATOM   7227 C  CG2 . THR D 1 106 ? 16.651  -4.034  -36.192 1.00 10.12  ? 106 THR D CG2 1 
ATOM   7228 N  N   . VAL D 1 107 ? 14.710  -7.285  -33.730 1.00 9.62   ? 107 VAL D N   1 
ATOM   7229 C  CA  . VAL D 1 107 ? 14.545  -8.286  -32.698 1.00 12.66  ? 107 VAL D CA  1 
ATOM   7230 C  C   . VAL D 1 107 ? 15.814  -9.143  -32.648 1.00 10.45  ? 107 VAL D C   1 
ATOM   7231 O  O   . VAL D 1 107 ? 16.202  -9.724  -33.670 1.00 13.56  ? 107 VAL D O   1 
ATOM   7232 C  CB  . VAL D 1 107 ? 13.251  -9.117  -32.869 1.00 12.27  ? 107 VAL D CB  1 
ATOM   7233 C  CG1 . VAL D 1 107 ? 13.123  -10.150 -31.747 1.00 14.90  ? 107 VAL D CG1 1 
ATOM   7234 C  CG2 . VAL D 1 107 ? 11.999  -8.237  -32.936 1.00 12.48  ? 107 VAL D CG2 1 
ATOM   7235 N  N   . SER D 1 108 ? 16.467  -9.175  -31.478 1.00 11.79  ? 108 SER D N   1 
ATOM   7236 C  CA  . SER D 1 108 ? 17.728  -9.898  -31.307 1.00 12.13  ? 108 SER D CA  1 
ATOM   7237 C  C   . SER D 1 108 ? 18.677  -9.624  -32.461 1.00 12.04  ? 108 SER D C   1 
ATOM   7238 O  O   . SER D 1 108 ? 19.240  -10.522 -33.064 1.00 13.45  ? 108 SER D O   1 
ATOM   7239 C  CB  . SER D 1 108 ? 17.487  -11.380 -31.212 1.00 16.65  ? 108 SER D CB  1 
ATOM   7240 O  OG  . SER D 1 108 ? 16.594  -11.656 -30.141 1.00 17.69  ? 108 SER D OG  1 
ATOM   7241 N  N   . GLY D 1 109 ? 18.786  -8.343  -32.823 1.00 12.54  ? 109 GLY D N   1 
ATOM   7242 C  CA  . GLY D 1 109 ? 19.756  -7.849  -33.791 1.00 11.70  ? 109 GLY D CA  1 
ATOM   7243 C  C   . GLY D 1 109 ? 19.343  -7.959  -35.259 1.00 13.40  ? 109 GLY D C   1 
ATOM   7244 O  O   . GLY D 1 109 ? 20.129  -7.582  -36.156 1.00 19.69  ? 109 GLY D O   1 
ATOM   7245 N  N   . GLN D 1 110 ? 18.145  -8.498  -35.521 1.00 14.05  ? 110 GLN D N   1 
ATOM   7246 C  CA  . GLN D 1 110 ? 17.737  -8.763  -36.886 1.00 15.13  ? 110 GLN D CA  1 
ATOM   7247 C  C   . GLN D 1 110 ? 16.609  -7.803  -37.305 1.00 12.19  ? 110 GLN D C   1 
ATOM   7248 O  O   . GLN D 1 110 ? 15.619  -7.626  -36.591 1.00 11.99  ? 110 GLN D O   1 
ATOM   7249 C  CB  . GLN D 1 110 ? 17.219  -10.205 -37.044 1.00 20.57  ? 110 GLN D CB  1 
ATOM   7250 C  CG  . GLN D 1 110 ? 18.058  -11.256 -36.338 1.00 24.46  ? 110 GLN D CG  1 
ATOM   7251 C  CD  . GLN D 1 110 ? 19.421  -11.360 -36.961 1.00 23.28  ? 110 GLN D CD  1 
ATOM   7252 O  OE1 . GLN D 1 110 ? 19.566  -11.580 -38.170 1.00 35.26  ? 110 GLN D OE1 1 
ATOM   7253 N  NE2 . GLN D 1 110 ? 20.435  -11.317 -36.097 1.00 30.52  ? 110 GLN D NE2 1 
ATOM   7254 N  N   . HIS D 1 111 ? 16.727  -7.262  -38.519 1.00 11.07  ? 111 HIS D N   1 
ATOM   7255 C  CA  . HIS D 1 111 ? 15.644  -6.516  -39.129 1.00 9.69   ? 111 HIS D CA  1 
ATOM   7256 C  C   . HIS D 1 111 ? 14.586  -7.485  -39.671 1.00 9.56   ? 111 HIS D C   1 
ATOM   7257 O  O   . HIS D 1 111 ? 14.871  -8.602  -40.162 1.00 12.85  ? 111 HIS D O   1 
ATOM   7258 C  CB  . HIS D 1 111 ? 16.154  -5.695  -40.324 1.00 9.49   ? 111 HIS D CB  1 
ATOM   7259 C  CG  . HIS D 1 111 ? 16.858  -4.413  -39.966 1.00 7.74   ? 111 HIS D CG  1 
ATOM   7260 N  ND1 . HIS D 1 111 ? 16.250  -3.182  -39.808 1.00 9.76   ? 111 HIS D ND1 1 
ATOM   7261 C  CD2 . HIS D 1 111 ? 18.182  -4.242  -39.766 1.00 9.47   ? 111 HIS D CD2 1 
ATOM   7262 C  CE1 . HIS D 1 111 ? 17.184  -2.301  -39.474 1.00 12.08  ? 111 HIS D CE1 1 
ATOM   7263 N  NE2 . HIS D 1 111 ? 18.377  -2.885  -39.494 1.00 12.44  ? 111 HIS D NE2 1 
ATOM   7264 N  N   . PHE D 1 112 ? 13.342  -7.049  -39.568 1.00 9.38   ? 112 PHE D N   1 
ATOM   7265 C  CA  . PHE D 1 112 ? 12.269  -7.533  -40.392 1.00 8.59   ? 112 PHE D CA  1 
ATOM   7266 C  C   . PHE D 1 112 ? 12.312  -6.878  -41.776 1.00 9.27   ? 112 PHE D C   1 
ATOM   7267 O  O   . PHE D 1 112 ? 13.050  -5.933  -41.974 1.00 9.40   ? 112 PHE D O   1 
ATOM   7268 C  CB  . PHE D 1 112 ? 10.956  -7.450  -39.620 1.00 9.47   ? 112 PHE D CB  1 
ATOM   7269 C  CG  . PHE D 1 112 ? 10.827  -8.561  -38.604 1.00 12.31  ? 112 PHE D CG  1 
ATOM   7270 C  CD1 . PHE D 1 112 ? 11.447  -8.496  -37.369 1.00 14.19  ? 112 PHE D CD1 1 
ATOM   7271 C  CD2 . PHE D 1 112 ? 10.041  -9.660  -38.897 1.00 13.95  ? 112 PHE D CD2 1 
ATOM   7272 C  CE1 . PHE D 1 112 ? 11.346  -9.581  -36.497 1.00 17.98  ? 112 PHE D CE1 1 
ATOM   7273 C  CE2 . PHE D 1 112 ? 9.898   -10.706 -38.001 1.00 17.59  ? 112 PHE D CE2 1 
ATOM   7274 C  CZ  . PHE D 1 112 ? 10.569  -10.667 -36.810 1.00 18.06  ? 112 PHE D CZ  1 
ATOM   7275 N  N   . ALA D 1 113 ? 11.424  -7.313  -42.683 1.00 7.42   ? 113 ALA D N   1 
ATOM   7276 C  CA  . ALA D 1 113 ? 11.371  -6.793  -44.048 1.00 8.49   ? 113 ALA D CA  1 
ATOM   7277 C  C   . ALA D 1 113 ? 10.910  -5.338  -44.027 1.00 7.57   ? 113 ALA D C   1 
ATOM   7278 O  O   . ALA D 1 113 ? 11.436  -4.513  -44.795 1.00 8.05   ? 113 ALA D O   1 
ATOM   7279 C  CB  . ALA D 1 113 ? 10.500  -7.640  -44.938 1.00 9.99   ? 113 ALA D CB  1 
ATOM   7280 N  N   . ALA D 1 114 ? 9.831   -5.064  -43.272 1.00 7.47   ? 114 ALA D N   1 
ATOM   7281 C  CA  . ALA D 1 114 ? 9.259   -3.706  -43.257 1.00 7.16   ? 114 ALA D CA  1 
ATOM   7282 C  C   . ALA D 1 114 ? 8.518   -3.584  -41.932 1.00 6.83   ? 114 ALA D C   1 
ATOM   7283 O  O   . ALA D 1 114 ? 8.578   -4.435  -41.028 1.00 8.49   ? 114 ALA D O   1 
ATOM   7284 C  CB  . ALA D 1 114 ? 8.308   -3.546  -44.434 1.00 8.06   ? 114 ALA D CB  1 
ATOM   7285 N  N   . GLU D 1 115 ? 7.958   -2.387  -41.715 1.00 7.45   ? 115 GLU D N   1 
ATOM   7286 C  CA  . GLU D 1 115 ? 7.270   -2.104  -40.444 1.00 6.87   ? 115 GLU D CA  1 
ATOM   7287 C  C   . GLU D 1 115 ? 6.084   -1.170  -40.725 1.00 7.34   ? 115 GLU D C   1 
ATOM   7288 O  O   . GLU D 1 115 ? 6.278   -0.199  -41.468 1.00 7.89   ? 115 GLU D O   1 
ATOM   7289 C  CB  . GLU D 1 115 ? 8.284   -1.621  -39.411 1.00 7.23   ? 115 GLU D CB  1 
ATOM   7290 C  CG  . GLU D 1 115 ? 7.709   -1.388  -38.049 1.00 8.28   ? 115 GLU D CG  1 
ATOM   7291 C  CD  . GLU D 1 115 ? 8.798   -1.110  -37.015 1.00 7.61   ? 115 GLU D CD  1 
ATOM   7292 O  OE1 . GLU D 1 115 ? 9.948   -1.545  -37.215 1.00 6.75   ? 115 GLU D OE1 1 
ATOM   7293 O  OE2 . GLU D 1 115 ? 8.510   -0.475  -35.938 1.00 8.49   ? 115 GLU D OE2 1 
ATOM   7294 N  N   . LEU D 1 116 ? 4.928   -1.427  -40.101 1.00 7.30   ? 116 LEU D N   1 
ATOM   7295 C  CA  . LEU D 1 116 ? 3.743   -0.565  -40.148 1.00 7.45   ? 116 LEU D CA  1 
ATOM   7296 C  C   . LEU D 1 116 ? 3.598   0.150   -38.847 1.00 7.20   ? 116 LEU D C   1 
ATOM   7297 O  O   . LEU D 1 116 ? 3.771   -0.389  -37.756 1.00 7.79   ? 116 LEU D O   1 
ATOM   7298 C  CB  . LEU D 1 116 ? 2.506   -1.445  -40.304 1.00 8.81   ? 116 LEU D CB  1 
ATOM   7299 C  CG  . LEU D 1 116 ? 1.193   -0.647  -40.173 1.00 7.59   ? 116 LEU D CG  1 
ATOM   7300 C  CD1 . LEU D 1 116 ? 0.937   0.204   -41.385 1.00 9.37   ? 116 LEU D CD1 1 
ATOM   7301 C  CD2 . LEU D 1 116 ? 0.032   -1.627  -39.922 1.00 10.75  ? 116 LEU D CD2 1 
ATOM   7302 N  N   . HIS D 1 117 ? 3.413   1.510   -38.901 1.00 8.38   ? 117 HIS D N   1 
ATOM   7303 C  CA  . HIS D 1 117 ? 3.130   2.305   -37.709 1.00 6.86   ? 117 HIS D CA  1 
ATOM   7304 C  C   . HIS D 1 117 ? 1.720   2.885   -37.836 1.00 7.21   ? 117 HIS D C   1 
ATOM   7305 O  O   . HIS D 1 117 ? 1.417   3.550   -38.860 1.00 7.83   ? 117 HIS D O   1 
ATOM   7306 C  CB  . HIS D 1 117 ? 4.104   3.467   -37.635 1.00 7.00   ? 117 HIS D CB  1 
ATOM   7307 C  CG  . HIS D 1 117 ? 5.443   3.016   -37.342 1.00 6.03   ? 117 HIS D CG  1 
ATOM   7308 N  ND1 . HIS D 1 117 ? 6.562   3.744   -37.699 1.00 23.90  ? 117 HIS D ND1 1 
ATOM   7309 C  CD2 . HIS D 1 117 ? 5.895   1.905   -36.722 1.00 9.14   ? 117 HIS D CD2 1 
ATOM   7310 C  CE1 . HIS D 1 117 ? 7.645   3.100   -37.311 1.00 7.80   ? 117 HIS D CE1 1 
ATOM   7311 N  NE2 . HIS D 1 117 ? 7.262   1.968   -36.708 1.00 8.27   ? 117 HIS D NE2 1 
ATOM   7312 N  N   . ILE D 1 118 ? 0.890   2.660   -36.804 1.00 7.45   ? 118 ILE D N   1 
ATOM   7313 C  CA  . ILE D 1 118 ? -0.423  3.326   -36.665 1.00 6.73   ? 118 ILE D CA  1 
ATOM   7314 C  C   . ILE D 1 118 ? -0.358  4.386   -35.571 1.00 6.82   ? 118 ILE D C   1 
ATOM   7315 O  O   . ILE D 1 118 ? -0.168  4.036   -34.399 1.00 7.81   ? 118 ILE D O   1 
ATOM   7316 C  CB  . ILE D 1 118 ? -1.510  2.277   -36.384 1.00 8.23   ? 118 ILE D CB  1 
ATOM   7317 C  CG1 . ILE D 1 118 ? -1.385  1.043   -37.298 1.00 8.10   ? 118 ILE D CG1 1 
ATOM   7318 C  CG2 . ILE D 1 118 ? -2.883  2.991   -36.543 1.00 9.77   ? 118 ILE D CG2 1 
ATOM   7319 C  CD1 . ILE D 1 118 ? -2.450  0.007   -37.014 1.00 11.51  ? 118 ILE D CD1 1 
ATOM   7320 N  N   . VAL D 1 119 ? -0.277  5.681   -36.000 1.00 7.64   ? 119 VAL D N   1 
ATOM   7321 C  CA  . VAL D 1 119 ? -0.016  6.795   -35.085 1.00 7.31   ? 119 VAL D CA  1 
ATOM   7322 C  C   . VAL D 1 119 ? -1.347  7.290   -34.512 1.00 7.53   ? 119 VAL D C   1 
ATOM   7323 O  O   . VAL D 1 119 ? -2.342  7.520   -35.258 1.00 8.79   ? 119 VAL D O   1 
ATOM   7324 C  CB  . VAL D 1 119 ? 0.649   7.905   -35.889 1.00 8.79   ? 119 VAL D CB  1 
ATOM   7325 C  CG1 . VAL D 1 119 ? 0.961   9.150   -34.998 1.00 10.87  ? 119 VAL D CG1 1 
ATOM   7326 C  CG2 . VAL D 1 119 ? 1.879   7.442   -36.689 1.00 8.52   ? 119 VAL D CG2 1 
ATOM   7327 N  N   . HIS D 1 120 ? -1.326  7.440   -33.165 1.00 7.56   ? 120 HIS D N   1 
ATOM   7328 C  CA  . HIS D 1 120 ? -2.457  7.973   -32.450 1.00 8.76   ? 120 HIS D CA  1 
ATOM   7329 C  C   . HIS D 1 120 ? -1.976  9.109   -31.539 1.00 8.42   ? 120 HIS D C   1 
ATOM   7330 O  O   . HIS D 1 120 ? -0.781  9.177   -31.177 1.00 10.28  ? 120 HIS D O   1 
ATOM   7331 C  CB  . HIS D 1 120 ? -2.985  6.876   -31.506 1.00 9.17   ? 120 HIS D CB  1 
ATOM   7332 C  CG  . HIS D 1 120 ? -3.478  5.626   -32.191 1.00 8.34   ? 120 HIS D CG  1 
ATOM   7333 N  ND1 . HIS D 1 120 ? -2.595  4.712   -32.735 1.00 10.41  ? 120 HIS D ND1 1 
ATOM   7334 C  CD2 . HIS D 1 120 ? -4.716  5.054   -32.283 1.00 8.11   ? 120 HIS D CD2 1 
ATOM   7335 C  CE1 . HIS D 1 120 ? -3.300  3.640   -33.185 1.00 10.49  ? 120 HIS D CE1 1 
ATOM   7336 N  NE2 . HIS D 1 120 ? -4.580  3.806   -32.894 1.00 9.77   ? 120 HIS D NE2 1 
ATOM   7337 N  N   . TYR D 1 121 ? -2.946  10.035  -31.201 1.00 9.59   ? 121 TYR D N   1 
ATOM   7338 C  CA  . TYR D 1 121 ? -2.562  11.137  -30.340 1.00 10.07  ? 121 TYR D CA  1 
ATOM   7339 C  C   . TYR D 1 121 ? -3.489  11.206  -29.148 1.00 9.90   ? 121 TYR D C   1 
ATOM   7340 O  O   . TYR D 1 121 ? -4.593  10.665  -29.177 1.00 10.20  ? 121 TYR D O   1 
ATOM   7341 C  CB  . TYR D 1 121 ? -2.645  12.488  -31.093 1.00 9.99   ? 121 TYR D CB  1 
ATOM   7342 C  CG  . TYR D 1 121 ? -4.046  12.897  -31.467 1.00 9.71   ? 121 TYR D CG  1 
ATOM   7343 C  CD1 . TYR D 1 121 ? -4.629  12.431  -32.634 1.00 10.71  ? 121 TYR D CD1 1 
ATOM   7344 C  CD2 . TYR D 1 121 ? -4.772  13.845  -30.731 1.00 10.97  ? 121 TYR D CD2 1 
ATOM   7345 C  CE1 . TYR D 1 121 ? -5.941  12.736  -32.987 1.00 12.98  ? 121 TYR D CE1 1 
ATOM   7346 C  CE2 . TYR D 1 121 ? -6.073  14.197  -31.088 1.00 12.01  ? 121 TYR D CE2 1 
ATOM   7347 C  CZ  . TYR D 1 121 ? -6.660  13.640  -32.224 1.00 13.61  ? 121 TYR D CZ  1 
ATOM   7348 O  OH  . TYR D 1 121 ? -7.941  13.940  -32.577 1.00 16.05  ? 121 TYR D OH  1 
ATOM   7349 N  N   . ASN D 1 122 ? -3.003  11.860  -28.089 1.00 10.44  ? 122 ASN D N   1 
ATOM   7350 C  CA  . ASN D 1 122 ? -3.713  11.911  -26.819 1.00 9.82   ? 122 ASN D CA  1 
ATOM   7351 C  C   . ASN D 1 122 ? -4.865  12.920  -26.956 1.00 9.41   ? 122 ASN D C   1 
ATOM   7352 O  O   . ASN D 1 122 ? -4.626  14.112  -26.752 1.00 11.46  ? 122 ASN D O   1 
ATOM   7353 C  CB  . ASN D 1 122 ? -2.733  12.261  -25.685 1.00 9.51   ? 122 ASN D CB  1 
ATOM   7354 C  CG  . ASN D 1 122 ? -3.366  12.157  -24.317 1.00 10.06  ? 122 ASN D CG  1 
ATOM   7355 O  OD1 . ASN D 1 122 ? -4.575  12.347  -24.197 1.00 11.39  ? 122 ASN D OD1 1 
ATOM   7356 N  ND2 . ASN D 1 122 ? -2.562  11.910  -23.292 1.00 12.64  ? 122 ASN D ND2 1 
ATOM   7357 N  N   . SER D 1 123 ? -6.046  12.446  -27.265 1.00 9.33   ? 123 SER D N   1 
ATOM   7358 C  CA  . SER D 1 123 ? -7.179  13.353  -27.535 1.00 10.08  ? 123 SER D CA  1 
ATOM   7359 C  C   . SER D 1 123 ? -7.853  13.779  -26.231 1.00 10.53  ? 123 SER D C   1 
ATOM   7360 O  O   . SER D 1 123 ? -8.698  14.690  -26.255 1.00 12.67  ? 123 SER D O   1 
ATOM   7361 C  CB  . SER D 1 123 ? -8.170  12.690  -28.505 1.00 11.50  ? 123 SER D CB  1 
ATOM   7362 O  OG  . SER D 1 123 ? -8.459  11.357  -28.074 1.00 10.86  ? 123 SER D OG  1 
ATOM   7363 N  N   . ASP D 1 124 ? -7.446  13.169  -25.088 1.00 12.54  ? 124 ASP D N   1 
ATOM   7364 C  CA  . ASP D 1 124 ? -7.869  13.670  -23.799 1.00 12.14  ? 124 ASP D CA  1 
ATOM   7365 C  C   . ASP D 1 124 ? -7.221  15.027  -23.483 1.00 12.47  ? 124 ASP D C   1 
ATOM   7366 O  O   . ASP D 1 124 ? -7.811  15.827  -22.711 1.00 17.39  ? 124 ASP D O   1 
ATOM   7367 C  CB  . ASP D 1 124 ? -7.675  12.618  -22.702 1.00 13.14  ? 124 ASP D CB  1 
ATOM   7368 C  CG  . ASP D 1 124 ? -8.557  11.391  -22.876 1.00 11.25  ? 124 ASP D CG  1 
ATOM   7369 O  OD1 . ASP D 1 124 ? -9.597  11.499  -23.566 1.00 13.13  ? 124 ASP D OD1 1 
ATOM   7370 O  OD2 . ASP D 1 124 ? -8.199  10.334  -22.320 1.00 13.92  ? 124 ASP D OD2 1 
ATOM   7371 N  N   . LEU D 1 125 ? -6.019  15.259  -24.013 1.00 12.67  ? 125 LEU D N   1 
ATOM   7372 C  CA  . LEU D 1 125 ? -5.211  16.456  -23.695 1.00 12.27  ? 125 LEU D CA  1 
ATOM   7373 C  C   . LEU D 1 125 ? -5.122  17.435  -24.860 1.00 11.68  ? 125 LEU D C   1 
ATOM   7374 O  O   . LEU D 1 125 ? -5.043  18.639  -24.627 1.00 15.69  ? 125 LEU D O   1 
ATOM   7375 C  CB  . LEU D 1 125 ? -3.794  16.046  -23.236 1.00 13.81  ? 125 LEU D CB  1 
ATOM   7376 C  CG  . LEU D 1 125 ? -3.702  15.689  -21.747 1.00 16.10  ? 125 LEU D CG  1 
ATOM   7377 C  CD1 . LEU D 1 125 ? -4.542  14.457  -21.379 1.00 19.62  ? 125 LEU D CD1 1 
ATOM   7378 C  CD2 . LEU D 1 125 ? -2.238  15.463  -21.340 1.00 19.30  ? 125 LEU D CD2 1 
ATOM   7379 N  N   . TYR D 1 126 ? -5.144  16.923  -26.095 1.00 11.70  ? 126 TYR D N   1 
ATOM   7380 C  CA  . TYR D 1 126 ? -4.743  17.711  -27.255 1.00 11.97  ? 126 TYR D CA  1 
ATOM   7381 C  C   . TYR D 1 126 ? -5.801  17.588  -28.353 1.00 13.96  ? 126 TYR D C   1 
ATOM   7382 O  O   . TYR D 1 126 ? -6.433  16.535  -28.536 1.00 15.60  ? 126 TYR D O   1 
ATOM   7383 C  CB  . TYR D 1 126 ? -3.352  17.279  -27.757 1.00 11.91  ? 126 TYR D CB  1 
ATOM   7384 C  CG  . TYR D 1 126 ? -2.320  17.269  -26.657 1.00 12.89  ? 126 TYR D CG  1 
ATOM   7385 C  CD1 . TYR D 1 126 ? -2.002  18.428  -25.951 1.00 13.73  ? 126 TYR D CD1 1 
ATOM   7386 C  CD2 . TYR D 1 126 ? -1.731  16.086  -26.244 1.00 12.53  ? 126 TYR D CD2 1 
ATOM   7387 C  CE1 . TYR D 1 126 ? -1.108  18.413  -24.879 1.00 13.09  ? 126 TYR D CE1 1 
ATOM   7388 C  CE2 . TYR D 1 126 ? -0.828  16.028  -25.202 1.00 11.67  ? 126 TYR D CE2 1 
ATOM   7389 C  CZ  . TYR D 1 126 ? -0.533  17.193  -24.494 1.00 10.97  ? 126 TYR D CZ  1 
ATOM   7390 O  OH  . TYR D 1 126 ? 0.375   17.168  -23.479 1.00 11.69  ? 126 TYR D OH  1 
ATOM   7391 N  N   . PRO D 1 127 ? -5.935  18.631  -29.192 1.00 15.17  ? 127 PRO D N   1 
ATOM   7392 C  CA  . PRO D 1 127 ? -6.950  18.610  -30.253 1.00 18.00  ? 127 PRO D CA  1 
ATOM   7393 C  C   . PRO D 1 127 ? -6.543  17.800  -31.492 1.00 18.12  ? 127 PRO D C   1 
ATOM   7394 O  O   . PRO D 1 127 ? -7.392  17.385  -32.304 1.00 21.18  ? 127 PRO D O   1 
ATOM   7395 C  CB  . PRO D 1 127 ? -7.096  20.130  -30.610 1.00 20.21  ? 127 PRO D CB  1 
ATOM   7396 C  CG  . PRO D 1 127 ? -5.773  20.784  -30.165 1.00 21.33  ? 127 PRO D CG  1 
ATOM   7397 C  CD  . PRO D 1 127 ? -5.306  19.970  -28.979 1.00 17.15  ? 127 PRO D CD  1 
ATOM   7398 N  N   . ASP D 1 128 ? -5.235  17.663  -31.719 1.00 16.11  ? 128 ASP D N   1 
ATOM   7399 C  CA  . ASP D 1 128 ? -4.715  17.052  -32.931 1.00 15.85  ? 128 ASP D CA  1 
ATOM   7400 C  C   . ASP D 1 128 ? -3.287  16.538  -32.724 1.00 13.59  ? 128 ASP D C   1 
ATOM   7401 O  O   . ASP D 1 128 ? -2.662  16.825  -31.697 1.00 16.26  ? 128 ASP D O   1 
ATOM   7402 C  CB  . ASP D 1 128 ? -4.891  17.923  -34.163 1.00 18.04  ? 128 ASP D CB  1 
ATOM   7403 C  CG  . ASP D 1 128 ? -4.126  19.244  -34.162 1.00 20.18  ? 128 ASP D CG  1 
ATOM   7404 O  OD1 . ASP D 1 128 ? -3.156  19.401  -33.453 1.00 22.03  ? 128 ASP D OD1 1 
ATOM   7405 O  OD2 . ASP D 1 128 ? -4.436  20.070  -35.018 1.00 32.12  ? 128 ASP D OD2 1 
ATOM   7406 N  N   . ALA D 1 129 ? -2.844  15.640  -33.631 1.00 15.93  ? 129 ALA D N   1 
ATOM   7407 C  CA  . ALA D 1 129 ? -1.527  15.055  -33.507 1.00 15.87  ? 129 ALA D CA  1 
ATOM   7408 C  C   . ALA D 1 129 ? -0.462  16.127  -33.643 1.00 14.49  ? 129 ALA D C   1 
ATOM   7409 O  O   . ALA D 1 129 ? 0.546   16.024  -32.955 1.00 15.33  ? 129 ALA D O   1 
ATOM   7410 C  CB  . ALA D 1 129 ? -1.282  14.028  -34.581 1.00 16.23  ? 129 ALA D CB  1 
ATOM   7411 N  N   . SER D 1 130 ? -0.656  17.149  -34.525 1.00 15.24  ? 130 SER D N   1 
ATOM   7412 C  CA  . SER D 1 130 ? 0.365   18.180  -34.633 1.00 16.25  ? 130 SER D CA  1 
ATOM   7413 C  C   . SER D 1 130 ? 0.655   18.842  -33.275 1.00 15.86  ? 130 SER D C   1 
ATOM   7414 O  O   . SER D 1 130 ? 1.842   18.958  -32.845 1.00 16.87  ? 130 SER D O   1 
ATOM   7415 C  CB  . SER D 1 130 ? -0.022  19.217  -35.680 1.00 22.02  ? 130 SER D CB  1 
ATOM   7416 O  OG  . SER D 1 130 ? 0.970   20.213  -35.623 1.00 32.13  ? 130 SER D OG  1 
ATOM   7417 N  N   . THR D 1 131 ? -0.437  19.235  -32.576 1.00 15.96  ? 131 THR D N   1 
ATOM   7418 C  CA  . THR D 1 131 ? -0.328  19.916  -31.285 1.00 14.27  ? 131 THR D CA  1 
ATOM   7419 C  C   . THR D 1 131 ? 0.218   18.945  -30.238 1.00 14.75  ? 131 THR D C   1 
ATOM   7420 O  O   . THR D 1 131 ? 1.031   19.299  -29.396 1.00 12.92  ? 131 THR D O   1 
ATOM   7421 C  CB  . THR D 1 131 ? -1.699  20.454  -30.832 1.00 14.65  ? 131 THR D CB  1 
ATOM   7422 O  OG1 . THR D 1 131 ? -2.192  21.376  -31.810 1.00 19.65  ? 131 THR D OG1 1 
ATOM   7423 C  CG2 . THR D 1 131 ? -1.646  21.191  -29.509 1.00 16.37  ? 131 THR D CG2 1 
ATOM   7424 N  N   . ALA D 1 132 ? -0.214  17.684  -30.308 1.00 12.33  ? 132 ALA D N   1 
ATOM   7425 C  CA  . ALA D 1 132 ? 0.232   16.710  -29.313 1.00 10.45  ? 132 ALA D CA  1 
ATOM   7426 C  C   . ALA D 1 132 ? 1.724   16.335  -29.464 1.00 10.52  ? 132 ALA D C   1 
ATOM   7427 O  O   . ALA D 1 132 ? 2.357   15.873  -28.510 1.00 10.61  ? 132 ALA D O   1 
ATOM   7428 C  CB  . ALA D 1 132 ? -0.623  15.462  -29.519 1.00 11.20  ? 132 ALA D CB  1 
ATOM   7429 N  N   . SER D 1 133 ? 2.257   16.423  -30.690 1.00 12.05  ? 133 SER D N   1 
ATOM   7430 C  CA  . SER D 1 133 ? 3.478   15.710  -31.032 1.00 13.09  ? 133 SER D CA  1 
ATOM   7431 C  C   . SER D 1 133 ? 4.689   16.172  -30.219 1.00 13.63  ? 133 SER D C   1 
ATOM   7432 O  O   . SER D 1 133 ? 5.652   15.426  -30.077 1.00 13.22  ? 133 SER D O   1 
ATOM   7433 C  CB  . SER D 1 133 ? 3.744   15.814  -32.493 1.00 13.46  ? 133 SER D CB  1 
ATOM   7434 O  OG  . SER D 1 133 ? 4.091   17.169  -32.886 1.00 14.60  ? 133 SER D OG  1 
ATOM   7435 N  N   . ASN D 1 134 ? 4.708   17.442  -29.765 1.00 10.85  ? 134 ASN D N   1 
ATOM   7436 C  CA  . ASN D 1 134 ? 5.833   17.958  -28.981 1.00 12.30  ? 134 ASN D CA  1 
ATOM   7437 C  C   . ASN D 1 134 ? 5.463   18.173  -27.505 1.00 11.71  ? 134 ASN D C   1 
ATOM   7438 O  O   . ASN D 1 134 ? 6.180   18.888  -26.793 1.00 14.66  ? 134 ASN D O   1 
ATOM   7439 C  CB  . ASN D 1 134 ? 6.484   19.199  -29.587 1.00 13.33  ? 134 ASN D CB  1 
ATOM   7440 C  CG  . ASN D 1 134 ? 5.597   20.428  -29.520 1.00 16.39  ? 134 ASN D CG  1 
ATOM   7441 O  OD1 . ASN D 1 134 ? 4.375   20.288  -29.397 1.00 15.70  ? 134 ASN D OD1 1 
ATOM   7442 N  ND2 . ASN D 1 134 ? 6.218   21.601  -29.592 1.00 18.43  ? 134 ASN D ND2 1 
ATOM   7443 N  N   . LYS D 1 135 ? 4.414   17.477  -27.038 1.00 11.43  ? 135 LYS D N   1 
ATOM   7444 C  CA  . LYS D 1 135 ? 3.929   17.700  -25.673 1.00 12.00  ? 135 LYS D CA  1 
ATOM   7445 C  C   . LYS D 1 135 ? 3.866   16.391  -24.878 1.00 11.34  ? 135 LYS D C   1 
ATOM   7446 O  O   . LYS D 1 135 ? 3.780   15.303  -25.481 1.00 11.86  ? 135 LYS D O   1 
ATOM   7447 C  CB  . LYS D 1 135 ? 2.560   18.402  -25.696 1.00 12.56  ? 135 LYS D CB  1 
ATOM   7448 C  CG  . LYS D 1 135 ? 2.761   19.808  -26.271 1.00 12.54  ? 135 LYS D CG  1 
ATOM   7449 C  CD  . LYS D 1 135 ? 1.425   20.523  -26.399 1.00 15.05  ? 135 LYS D CD  1 
ATOM   7450 C  CE  . LYS D 1 135 ? 1.551   21.898  -27.069 1.00 14.72  ? 135 LYS D CE  1 
ATOM   7451 N  NZ  . LYS D 1 135 ? 2.051   21.742  -28.473 1.00 15.45  ? 135 LYS D NZ  1 
ATOM   7452 N  N   A SER D 1 136 ? 3.779   16.557  -23.566 0.50 11.80  ? 136 SER D N   1 
ATOM   7453 N  N   B SER D 1 136 ? 3.844   16.541  -23.540 0.50 12.60  ? 136 SER D N   1 
ATOM   7454 C  CA  A SER D 1 136 ? 3.815   15.438  -22.649 0.50 10.74  ? 136 SER D CA  1 
ATOM   7455 C  CA  B SER D 1 136 ? 3.788   15.423  -22.605 0.50 11.54  ? 136 SER D CA  1 
ATOM   7456 C  C   A SER D 1 136 ? 2.716   14.395  -22.931 0.50 11.76  ? 136 SER D C   1 
ATOM   7457 C  C   B SER D 1 136 ? 2.727   14.399  -23.021 0.50 11.78  ? 136 SER D C   1 
ATOM   7458 O  O   A SER D 1 136 ? 1.527   14.724  -23.078 0.50 11.25  ? 136 SER D O   1 
ATOM   7459 O  O   B SER D 1 136 ? 1.564   14.751  -23.275 0.50 12.04  ? 136 SER D O   1 
ATOM   7460 C  CB  A SER D 1 136 ? 3.749   15.955  -21.264 0.50 12.32  ? 136 SER D CB  1 
ATOM   7461 C  CB  B SER D 1 136 ? 3.478   15.831  -21.187 0.50 13.54  ? 136 SER D CB  1 
ATOM   7462 O  OG  A SER D 1 136 ? 3.771   14.904  -20.341 0.50 13.19  ? 136 SER D OG  1 
ATOM   7463 O  OG  B SER D 1 136 ? 4.307   16.873  -20.697 0.50 17.43  ? 136 SER D OG  1 
ATOM   7464 N  N   . GLU D 1 137 ? 3.127   13.125  -23.050 1.00 11.89  ? 137 GLU D N   1 
ATOM   7465 C  CA  . GLU D 1 137 ? 2.167   12.044  -23.267 1.00 10.81  ? 137 GLU D CA  1 
ATOM   7466 C  C   . GLU D 1 137 ? 1.438   12.187  -24.611 1.00 10.06  ? 137 GLU D C   1 
ATOM   7467 O  O   . GLU D 1 137 ? 0.328   11.719  -24.806 1.00 10.86  ? 137 GLU D O   1 
ATOM   7468 C  CB  . GLU D 1 137 ? 1.103   11.882  -22.180 1.00 11.60  ? 137 GLU D CB  1 
ATOM   7469 C  CG  . GLU D 1 137 ? 1.667   11.781  -20.787 1.00 14.18  ? 137 GLU D CG  1 
ATOM   7470 C  CD  . GLU D 1 137 ? 2.522   10.569  -20.502 1.00 20.59  ? 137 GLU D CD  1 
ATOM   7471 O  OE1 . GLU D 1 137 ? 2.429   9.595   -21.249 1.00 23.23  ? 137 GLU D OE1 1 
ATOM   7472 O  OE2 . GLU D 1 137 ? 3.208   10.583  -19.485 1.00 31.75  ? 137 GLU D OE2 1 
ATOM   7473 N  N   . GLY D 1 138 ? 2.038   12.860  -25.588 1.00 10.19  ? 138 GLY D N   1 
ATOM   7474 C  CA  . GLY D 1 138 ? 1.309   13.290  -26.790 1.00 10.63  ? 138 GLY D CA  1 
ATOM   7475 C  C   . GLY D 1 138 ? 0.843   12.143  -27.697 1.00 9.35   ? 138 GLY D C   1 
ATOM   7476 O  O   . GLY D 1 138 ? -0.244  12.256  -28.284 1.00 9.92   ? 138 GLY D O   1 
ATOM   7477 N  N   . LEU D 1 139 ? 1.710   11.101  -27.893 1.00 8.53   ? 139 LEU D N   1 
ATOM   7478 C  CA  . LEU D 1 139 ? 1.482   10.159  -28.984 1.00 9.84   ? 139 LEU D CA  1 
ATOM   7479 C  C   . LEU D 1 139 ? 1.546   8.707   -28.484 1.00 9.99   ? 139 LEU D C   1 
ATOM   7480 O  O   . LEU D 1 139 ? 2.285   8.408   -27.549 1.00 9.50   ? 139 LEU D O   1 
ATOM   7481 C  CB  . LEU D 1 139 ? 2.481   10.353  -30.120 1.00 11.58  ? 139 LEU D CB  1 
ATOM   7482 C  CG  . LEU D 1 139 ? 2.473   11.777  -30.733 1.00 10.03  ? 139 LEU D CG  1 
ATOM   7483 C  CD1 . LEU D 1 139 ? 3.713   11.935  -31.640 1.00 11.15  ? 139 LEU D CD1 1 
ATOM   7484 C  CD2 . LEU D 1 139 ? 1.206   11.974  -31.546 1.00 11.78  ? 139 LEU D CD2 1 
ATOM   7485 N  N   . ALA D 1 140 ? 0.832   7.861   -29.216 1.00 9.25   ? 140 ALA D N   1 
ATOM   7486 C  CA  . ALA D 1 140 ? 1.009   6.405   -29.013 1.00 8.46   ? 140 ALA D CA  1 
ATOM   7487 C  C   . ALA D 1 140 ? 1.051   5.767   -30.384 1.00 9.19   ? 140 ALA D C   1 
ATOM   7488 O  O   . ALA D 1 140 ? 0.207   6.038   -31.213 1.00 9.84   ? 140 ALA D O   1 
ATOM   7489 C  CB  . ALA D 1 140 ? -0.086  5.845   -28.173 1.00 10.50  ? 140 ALA D CB  1 
ATOM   7490 N  N   . VAL D 1 141 ? 2.065   4.915   -30.640 1.00 8.35   ? 141 VAL D N   1 
ATOM   7491 C  CA  . VAL D 1 141 ? 2.124   4.238   -31.933 1.00 8.05   ? 141 VAL D CA  1 
ATOM   7492 C  C   . VAL D 1 141 ? 1.959   2.726   -31.677 1.00 8.48   ? 141 VAL D C   1 
ATOM   7493 O  O   . VAL D 1 141 ? 2.588   2.175   -30.786 1.00 9.02   ? 141 VAL D O   1 
ATOM   7494 C  CB  . VAL D 1 141 ? 3.402   4.574   -32.701 1.00 7.65   ? 141 VAL D CB  1 
ATOM   7495 C  CG1 . VAL D 1 141 ? 3.541   3.894   -34.061 1.00 11.55  ? 141 VAL D CG1 1 
ATOM   7496 C  CG2 . VAL D 1 141 ? 3.453   6.131   -32.848 1.00 10.99  ? 141 VAL D CG2 1 
ATOM   7497 N  N   . LEU D 1 142 ? 1.213   2.123   -32.590 1.00 8.04   ? 142 LEU D N   1 
ATOM   7498 C  CA  . LEU D 1 142 ? 1.255   0.650   -32.707 1.00 7.37   ? 142 LEU D CA  1 
ATOM   7499 C  C   . LEU D 1 142 ? 2.148   0.268   -33.872 1.00 7.27   ? 142 LEU D C   1 
ATOM   7500 O  O   . LEU D 1 142 ? 1.983   0.760   -35.000 1.00 9.01   ? 142 LEU D O   1 
ATOM   7501 C  CB  . LEU D 1 142 ? -0.150  0.147   -33.005 1.00 9.25   ? 142 LEU D CB  1 
ATOM   7502 C  CG  . LEU D 1 142 ? -1.232  0.535   -32.010 1.00 9.95   ? 142 LEU D CG  1 
ATOM   7503 C  CD1 . LEU D 1 142 ? -2.547  -0.104  -32.428 1.00 12.49  ? 142 LEU D CD1 1 
ATOM   7504 C  CD2 . LEU D 1 142 ? -0.857  0.184   -30.554 1.00 11.12  ? 142 LEU D CD2 1 
ATOM   7505 N  N   . ALA D 1 143 ? 3.119   -0.632  -33.579 1.00 9.05   ? 143 ALA D N   1 
ATOM   7506 C  CA  . ALA D 1 143 ? 4.050   -1.069  -34.637 1.00 8.19   ? 143 ALA D CA  1 
ATOM   7507 C  C   . ALA D 1 143 ? 3.781   -2.561  -34.914 1.00 6.31   ? 143 ALA D C   1 
ATOM   7508 O  O   . ALA D 1 143 ? 3.745   -3.375  -33.988 1.00 9.09   ? 143 ALA D O   1 
ATOM   7509 C  CB  . ALA D 1 143 ? 5.507   -0.856  -34.220 1.00 8.30   ? 143 ALA D CB  1 
ATOM   7510 N  N   . VAL D 1 144 ? 3.720   -2.843  -36.176 1.00 7.78   ? 144 VAL D N   1 
ATOM   7511 C  CA  . VAL D 1 144 ? 3.628   -4.250  -36.664 1.00 7.80   ? 144 VAL D CA  1 
ATOM   7512 C  C   . VAL D 1 144 ? 4.868   -4.487  -37.488 1.00 8.35   ? 144 VAL D C   1 
ATOM   7513 O  O   . VAL D 1 144 ? 5.109   -3.896  -38.519 1.00 9.36   ? 144 VAL D O   1 
ATOM   7514 C  CB  . VAL D 1 144 ? 2.366   -4.438  -37.528 1.00 8.19   ? 144 VAL D CB  1 
ATOM   7515 C  CG1 . VAL D 1 144 ? 2.267   -5.913  -38.041 1.00 9.16   ? 144 VAL D CG1 1 
ATOM   7516 C  CG2 . VAL D 1 144 ? 1.074   -4.023  -36.840 1.00 9.21   ? 144 VAL D CG2 1 
ATOM   7517 N  N   . LEU D 1 145 ? 5.577   -5.589  -37.129 1.00 8.94   ? 145 LEU D N   1 
ATOM   7518 C  CA  . LEU D 1 145 ? 6.744   -6.068  -37.880 1.00 7.74   ? 145 LEU D CA  1 
ATOM   7519 C  C   . LEU D 1 145 ? 6.263   -6.902  -39.069 1.00 7.82   ? 145 LEU D C   1 
ATOM   7520 O  O   . LEU D 1 145 ? 5.287   -7.648  -38.917 1.00 9.33   ? 145 LEU D O   1 
ATOM   7521 C  CB  . LEU D 1 145 ? 7.624   -6.934  -36.971 1.00 8.71   ? 145 LEU D CB  1 
ATOM   7522 C  CG  . LEU D 1 145 ? 8.229   -6.171  -35.776 1.00 9.97   ? 145 LEU D CG  1 
ATOM   7523 C  CD1 . LEU D 1 145 ? 8.760   -7.157  -34.705 1.00 12.63  ? 145 LEU D CD1 1 
ATOM   7524 C  CD2 . LEU D 1 145 ? 9.307   -5.166  -36.234 1.00 11.92  ? 145 LEU D CD2 1 
ATOM   7525 N  N   . ILE D 1 146 ? 6.855   -6.681  -40.239 1.00 8.35   ? 146 ILE D N   1 
ATOM   7526 C  CA  . ILE D 1 146 ? 6.428   -7.339  -41.460 1.00 9.21   ? 146 ILE D CA  1 
ATOM   7527 C  C   . ILE D 1 146 ? 7.561   -8.180  -41.974 1.00 8.94   ? 146 ILE D C   1 
ATOM   7528 O  O   . ILE D 1 146 ? 8.655   -7.729  -42.176 1.00 8.59   ? 146 ILE D O   1 
ATOM   7529 C  CB  . ILE D 1 146 ? 6.033   -6.275  -42.510 1.00 9.34   ? 146 ILE D CB  1 
ATOM   7530 C  CG1 . ILE D 1 146 ? 4.860   -5.460  -41.989 1.00 10.89  ? 146 ILE D CG1 1 
ATOM   7531 C  CG2 . ILE D 1 146 ? 5.672   -6.936  -43.835 1.00 9.54   ? 146 ILE D CG2 1 
ATOM   7532 C  CD1 . ILE D 1 146 ? 4.579   -4.159  -42.794 1.00 9.21   ? 146 ILE D CD1 1 
ATOM   7533 N  N   A GLU D 1 147 ? 7.265   -9.502  -42.196 0.50 8.28   ? 147 GLU D N   1 
ATOM   7534 N  N   B GLU D 1 147 ? 7.195   -9.479  -42.257 0.50 8.28   ? 147 GLU D N   1 
ATOM   7535 C  CA  A GLU D 1 147 ? 8.240   -10.413 -42.794 0.50 10.47  ? 147 GLU D CA  1 
ATOM   7536 C  CA  B GLU D 1 147 ? 8.053   -10.516 -42.826 0.50 10.15  ? 147 GLU D CA  1 
ATOM   7537 C  C   A GLU D 1 147 ? 7.798   -10.843 -44.192 0.50 8.20   ? 147 GLU D C   1 
ATOM   7538 C  C   B GLU D 1 147 ? 7.744   -10.783 -44.298 0.50 8.92   ? 147 GLU D C   1 
ATOM   7539 O  O   A GLU D 1 147 ? 6.596   -10.888 -44.463 0.50 8.07   ? 147 GLU D O   1 
ATOM   7540 O  O   B GLU D 1 147 ? 6.593   -10.692 -44.728 0.50 9.28   ? 147 GLU D O   1 
ATOM   7541 C  CB  A GLU D 1 147 ? 8.551   -11.591 -41.851 0.50 12.90  ? 147 GLU D CB  1 
ATOM   7542 C  CB  B GLU D 1 147 ? 7.865   -11.795 -42.016 0.50 12.34  ? 147 GLU D CB  1 
ATOM   7543 C  CG  A GLU D 1 147 ? 7.389   -12.581 -41.696 0.50 14.84  ? 147 GLU D CG  1 
ATOM   7544 C  CG  B GLU D 1 147 ? 8.853   -12.918 -42.304 0.50 12.34  ? 147 GLU D CG  1 
ATOM   7545 C  CD  A GLU D 1 147 ? 7.606   -13.795 -40.797 0.50 19.89  ? 147 GLU D CD  1 
ATOM   7546 C  CD  B GLU D 1 147 ? 9.046   -13.788 -41.073 0.50 16.98  ? 147 GLU D CD  1 
ATOM   7547 O  OE1 A GLU D 1 147 ? 8.660   -13.824 -40.118 0.50 23.46  ? 147 GLU D OE1 1 
ATOM   7548 O  OE1 B GLU D 1 147 ? 8.345   -13.568 -40.058 0.50 20.72  ? 147 GLU D OE1 1 
ATOM   7549 O  OE2 A GLU D 1 147 ? 6.727   -14.725 -40.776 0.50 21.94  ? 147 GLU D OE2 1 
ATOM   7550 O  OE2 B GLU D 1 147 ? 9.923   -14.650 -41.126 0.50 23.50  ? 147 GLU D OE2 1 
ATOM   7551 N  N   . MET D 1 148 ? 8.761   -11.179 -45.076 1.00 9.85   ? 148 MET D N   1 
ATOM   7552 C  CA  . MET D 1 148 ? 8.483   -11.721 -46.403 1.00 10.14  ? 148 MET D CA  1 
ATOM   7553 C  C   . MET D 1 148 ? 7.848   -13.106 -46.297 1.00 9.49   ? 148 MET D C   1 
ATOM   7554 O  O   . MET D 1 148 ? 8.374   -14.019 -45.608 1.00 12.20  ? 148 MET D O   1 
ATOM   7555 C  CB  . MET D 1 148 ? 9.759   -11.799 -47.229 1.00 9.88   ? 148 MET D CB  1 
ATOM   7556 C  CG  . MET D 1 148 ? 9.499   -12.237 -48.634 1.00 13.50  ? 148 MET D CG  1 
ATOM   7557 S  SD  . MET D 1 148 ? 11.057  -12.324 -49.582 1.00 14.04  ? 148 MET D SD  1 
ATOM   7558 C  CE  . MET D 1 148 ? 11.575  -10.612 -49.561 1.00 14.91  ? 148 MET D CE  1 
ATOM   7559 N  N   . GLY D 1 149 ? 6.646   -13.257 -46.870 1.00 10.25  ? 149 GLY D N   1 
ATOM   7560 C  CA  . GLY D 1 149 ? 5.956   -14.553 -46.750 1.00 11.01  ? 149 GLY D CA  1 
ATOM   7561 C  C   . GLY D 1 149 ? 4.817   -14.608 -47.755 1.00 10.14  ? 149 GLY D C   1 
ATOM   7562 O  O   . GLY D 1 149 ? 5.032   -14.328 -48.925 1.00 10.32  ? 149 GLY D O   1 
ATOM   7563 N  N   . SER D 1 150 ? 3.613   -15.034 -47.339 1.00 9.73   ? 150 SER D N   1 
ATOM   7564 C  CA  . SER D 1 150 ? 2.473   -15.101 -48.251 1.00 9.14   ? 150 SER D CA  1 
ATOM   7565 C  C   . SER D 1 150 ? 1.967   -13.731 -48.642 1.00 9.05   ? 150 SER D C   1 
ATOM   7566 O  O   . SER D 1 150 ? 2.045   -12.754 -47.847 1.00 11.59  ? 150 SER D O   1 
ATOM   7567 C  CB  . SER D 1 150 ? 1.352   -15.908 -47.579 1.00 10.65  ? 150 SER D CB  1 
ATOM   7568 O  OG  . SER D 1 150 ? 1.728   -17.302 -47.485 1.00 11.12  ? 150 SER D OG  1 
ATOM   7569 N  N   . PHE D 1 151 ? 1.317   -13.692 -49.814 1.00 11.43  ? 151 PHE D N   1 
ATOM   7570 C  CA  . PHE D 1 151 ? 0.563   -12.516 -50.230 1.00 10.93  ? 151 PHE D CA  1 
ATOM   7571 C  C   . PHE D 1 151 ? -0.455  -12.185 -49.176 1.00 9.46   ? 151 PHE D C   1 
ATOM   7572 O  O   . PHE D 1 151 ? -1.156  -12.985 -48.574 1.00 13.39  ? 151 PHE D O   1 
ATOM   7573 C  CB  . PHE D 1 151 ? -0.124  -12.827 -51.558 1.00 11.02  ? 151 PHE D CB  1 
ATOM   7574 C  CG  . PHE D 1 151 ? -0.927  -11.660 -52.072 1.00 9.84   ? 151 PHE D CG  1 
ATOM   7575 C  CD1 . PHE D 1 151 ? -0.280  -10.610 -52.708 1.00 12.67  ? 151 PHE D CD1 1 
ATOM   7576 C  CD2 . PHE D 1 151 ? -2.309  -11.648 -51.978 1.00 13.24  ? 151 PHE D CD2 1 
ATOM   7577 C  CE1 . PHE D 1 151 ? -1.015  -9.512  -53.162 1.00 12.71  ? 151 PHE D CE1 1 
ATOM   7578 C  CE2 . PHE D 1 151 ? -3.057  -10.562 -52.412 1.00 14.18  ? 151 PHE D CE2 1 
ATOM   7579 C  CZ  . PHE D 1 151 ? -2.405  -9.479  -53.009 1.00 12.77  ? 151 PHE D CZ  1 
ATOM   7580 N  N   . ASN D 1 152 ? -0.568  -10.854 -48.897 1.00 11.33  ? 152 ASN D N   1 
ATOM   7581 C  CA  . ASN D 1 152 ? -1.465  -10.358 -47.883 1.00 9.97   ? 152 ASN D CA  1 
ATOM   7582 C  C   . ASN D 1 152 ? -2.512  -9.489  -48.557 1.00 11.42  ? 152 ASN D C   1 
ATOM   7583 O  O   . ASN D 1 152 ? -2.232  -8.291  -48.860 1.00 10.62  ? 152 ASN D O   1 
ATOM   7584 C  CB  . ASN D 1 152 ? -0.632  -9.621  -46.816 1.00 9.59   ? 152 ASN D CB  1 
ATOM   7585 C  CG  . ASN D 1 152 ? -1.442  -9.268  -45.576 1.00 10.30  ? 152 ASN D CG  1 
ATOM   7586 O  OD1 . ASN D 1 152 ? -2.582  -8.747  -45.700 1.00 10.19  ? 152 ASN D OD1 1 
ATOM   7587 N  ND2 . ASN D 1 152 ? -0.901  -9.555  -44.385 1.00 11.58  ? 152 ASN D ND2 1 
ATOM   7588 N  N   . PRO D 1 153 ? -3.772  -9.936  -48.687 1.00 11.54  ? 153 PRO D N   1 
ATOM   7589 C  CA  . PRO D 1 153 ? -4.805  -9.173  -49.388 1.00 11.00  ? 153 PRO D CA  1 
ATOM   7590 C  C   . PRO D 1 153 ? -5.144  -7.905  -48.594 1.00 11.66  ? 153 PRO D C   1 
ATOM   7591 O  O   . PRO D 1 153 ? -5.525  -6.915  -49.208 1.00 13.46  ? 153 PRO D O   1 
ATOM   7592 C  CB  . PRO D 1 153 ? -6.023  -10.134 -49.418 1.00 12.49  ? 153 PRO D CB  1 
ATOM   7593 C  CG  . PRO D 1 153 ? -5.365  -11.488 -49.455 1.00 15.49  ? 153 PRO D CG  1 
ATOM   7594 C  CD  . PRO D 1 153 ? -4.159  -11.387 -48.513 1.00 14.78  ? 153 PRO D CD  1 
ATOM   7595 N  N   . SER D 1 154 ? -5.001  -7.951  -47.253 1.00 9.93   ? 154 SER D N   1 
ATOM   7596 C  CA  . SER D 1 154 ? -5.358  -6.744  -46.498 1.00 12.09  ? 154 SER D CA  1 
ATOM   7597 C  C   . SER D 1 154 ? -4.350  -5.631  -46.774 1.00 10.59  ? 154 SER D C   1 
ATOM   7598 O  O   . SER D 1 154 ? -4.727  -4.442  -46.915 1.00 10.82  ? 154 SER D O   1 
ATOM   7599 C  CB  . SER D 1 154 ? -5.491  -7.059  -45.013 1.00 11.70  ? 154 SER D CB  1 
ATOM   7600 O  OG  . SER D 1 154 ? -6.588  -7.980  -44.844 1.00 13.95  ? 154 SER D OG  1 
ATOM   7601 N  N   . TYR D 1 155 ? -3.046  -5.931  -46.606 1.00 10.04  ? 155 TYR D N   1 
ATOM   7602 C  CA  . TYR D 1 155 ? -2.066  -4.884  -46.922 1.00 8.37   ? 155 TYR D CA  1 
ATOM   7603 C  C   . TYR D 1 155 ? -2.174  -4.440  -48.394 1.00 9.10   ? 155 TYR D C   1 
ATOM   7604 O  O   . TYR D 1 155 ? -1.901  -3.267  -48.677 1.00 10.02  ? 155 TYR D O   1 
ATOM   7605 C  CB  . TYR D 1 155 ? -0.640  -5.339  -46.612 1.00 8.91   ? 155 TYR D CB  1 
ATOM   7606 C  CG  . TYR D 1 155 ? -0.285  -5.253  -45.158 1.00 8.86   ? 155 TYR D CG  1 
ATOM   7607 C  CD1 . TYR D 1 155 ? -0.773  -6.159  -44.192 1.00 8.60   ? 155 TYR D CD1 1 
ATOM   7608 C  CD2 . TYR D 1 155 ? 0.462   -4.151  -44.716 1.00 10.34  ? 155 TYR D CD2 1 
ATOM   7609 C  CE1 . TYR D 1 155 ? -0.435  -6.023  -42.843 1.00 8.76   ? 155 TYR D CE1 1 
ATOM   7610 C  CE2 . TYR D 1 155 ? 0.809   -4.010  -43.377 1.00 9.79   ? 155 TYR D CE2 1 
ATOM   7611 C  CZ  . TYR D 1 155 ? 0.344   -4.930  -42.424 1.00 9.35   ? 155 TYR D CZ  1 
ATOM   7612 O  OH  . TYR D 1 155 ? 0.628   -4.724  -41.089 1.00 10.76  ? 155 TYR D OH  1 
ATOM   7613 N  N   . ASP D 1 156 ? -2.632  -5.261  -49.301 1.00 10.23  ? 156 ASP D N   1 
ATOM   7614 C  CA  . ASP D 1 156 ? -2.770  -4.864  -50.679 1.00 10.66  ? 156 ASP D CA  1 
ATOM   7615 C  C   . ASP D 1 156 ? -3.852  -3.772  -50.845 1.00 10.26  ? 156 ASP D C   1 
ATOM   7616 O  O   . ASP D 1 156 ? -3.881  -3.122  -51.893 1.00 11.89  ? 156 ASP D O   1 
ATOM   7617 C  CB  . ASP D 1 156 ? -2.991  -6.090  -51.601 1.00 11.86  ? 156 ASP D CB  1 
ATOM   7618 C  CG  . ASP D 1 156 ? -2.082  -5.957  -52.832 1.00 13.54  ? 156 ASP D CG  1 
ATOM   7619 O  OD1 . ASP D 1 156 ? -0.796  -5.697  -52.613 1.00 13.48  ? 156 ASP D OD1 1 
ATOM   7620 O  OD2 . ASP D 1 156 ? -2.609  -6.073  -53.965 1.00 17.98  ? 156 ASP D OD2 1 
ATOM   7621 N  N   . LYS D 1 157 ? -4.791  -3.651  -49.903 1.00 11.47  ? 157 LYS D N   1 
ATOM   7622 C  CA  . LYS D 1 157 ? -5.783  -2.601  -49.969 1.00 11.73  ? 157 LYS D CA  1 
ATOM   7623 C  C   . LYS D 1 157 ? -5.110  -1.232  -49.798 1.00 12.28  ? 157 LYS D C   1 
ATOM   7624 O  O   . LYS D 1 157 ? -5.677  -0.230  -50.176 1.00 17.71  ? 157 LYS D O   1 
ATOM   7625 C  CB  . LYS D 1 157 ? -6.809  -2.780  -48.868 1.00 12.48  ? 157 LYS D CB  1 
ATOM   7626 C  CG  . LYS D 1 157 ? -7.615  -4.071  -49.020 1.00 15.65  ? 157 LYS D CG  1 
ATOM   7627 C  CD  . LYS D 1 157 ? -8.579  -4.403  -47.840 1.00 15.06  ? 157 LYS D CD  1 
ATOM   7628 C  CE  . LYS D 1 157 ? -9.241  -5.754  -48.033 1.00 14.35  ? 157 LYS D CE  1 
ATOM   7629 N  NZ  . LYS D 1 157 ? -10.140 -6.125  -46.897 1.00 17.65  ? 157 LYS D NZ  1 
ATOM   7630 N  N   . ILE D 1 158 ? -3.870  -1.187  -49.259 1.00 11.56  ? 158 ILE D N   1 
ATOM   7631 C  CA  . ILE D 1 158 ? -3.037  0.018   -49.321 1.00 10.18  ? 158 ILE D CA  1 
ATOM   7632 C  C   . ILE D 1 158 ? -2.220  -0.069  -50.608 1.00 9.92   ? 158 ILE D C   1 
ATOM   7633 O  O   . ILE D 1 158 ? -2.121  0.941   -51.313 1.00 11.67  ? 158 ILE D O   1 
ATOM   7634 C  CB  . ILE D 1 158 ? -2.135  0.154   -48.075 1.00 11.05  ? 158 ILE D CB  1 
ATOM   7635 C  CG1 . ILE D 1 158 ? -3.011  0.305   -46.810 1.00 13.53  ? 158 ILE D CG1 1 
ATOM   7636 C  CG2 . ILE D 1 158 ? -1.206  1.371   -48.196 1.00 13.17  ? 158 ILE D CG2 1 
ATOM   7637 C  CD1 . ILE D 1 158 ? -2.315  0.053   -45.519 1.00 16.72  ? 158 ILE D CD1 1 
ATOM   7638 N  N   . PHE D 1 159 ? -1.473  -1.176  -50.796 1.00 9.87   ? 159 PHE D N   1 
ATOM   7639 C  CA  . PHE D 1 159 ? -0.404  -1.129  -51.771 1.00 9.69   ? 159 PHE D CA  1 
ATOM   7640 C  C   . PHE D 1 159 ? -0.936  -0.940  -53.190 1.00 10.60  ? 159 PHE D C   1 
ATOM   7641 O  O   . PHE D 1 159 ? -0.208  -0.458  -54.048 1.00 12.28  ? 159 PHE D O   1 
ATOM   7642 C  CB  . PHE D 1 159 ? 0.453   -2.396  -51.729 1.00 9.88   ? 159 PHE D CB  1 
ATOM   7643 C  CG  . PHE D 1 159 ? 1.118   -2.693  -50.384 1.00 10.77  ? 159 PHE D CG  1 
ATOM   7644 C  CD1 . PHE D 1 159 ? 1.490   -1.677  -49.468 1.00 12.34  ? 159 PHE D CD1 1 
ATOM   7645 C  CD2 . PHE D 1 159 ? 1.410   -4.023  -50.054 1.00 11.05  ? 159 PHE D CD2 1 
ATOM   7646 C  CE1 . PHE D 1 159 ? 2.183   -1.981  -48.298 1.00 10.59  ? 159 PHE D CE1 1 
ATOM   7647 C  CE2 . PHE D 1 159 ? 2.095   -4.310  -48.876 1.00 10.93  ? 159 PHE D CE2 1 
ATOM   7648 C  CZ  . PHE D 1 159 ? 2.465   -3.314  -48.002 1.00 10.55  ? 159 PHE D CZ  1 
ATOM   7649 N  N   . SER D 1 160 ? -2.160  -1.420  -53.485 1.00 11.90  ? 160 SER D N   1 
ATOM   7650 C  CA  . SER D 1 160 ? -2.703  -1.325  -54.834 1.00 12.40  ? 160 SER D CA  1 
ATOM   7651 C  C   . SER D 1 160 ? -2.862  0.131   -55.281 1.00 12.97  ? 160 SER D C   1 
ATOM   7652 O  O   . SER D 1 160 ? -2.976  0.363   -56.475 1.00 17.20  ? 160 SER D O   1 
ATOM   7653 C  CB  . SER D 1 160 ? -4.023  -2.103  -54.922 1.00 15.42  ? 160 SER D CB  1 
ATOM   7654 O  OG  . SER D 1 160 ? -5.024  -1.478  -54.152 1.00 16.08  ? 160 SER D OG  1 
ATOM   7655 N  N   . HIS D 1 161 ? -2.878  1.077   -54.337 1.00 12.36  ? 161 HIS D N   1 
ATOM   7656 C  CA  . HIS D 1 161 ? -3.046  2.485   -54.681 1.00 14.16  ? 161 HIS D CA  1 
ATOM   7657 C  C   . HIS D 1 161 ? -1.724  3.209   -54.835 1.00 12.50  ? 161 HIS D C   1 
ATOM   7658 O  O   . HIS D 1 161 ? -1.759  4.423   -55.120 1.00 16.17  ? 161 HIS D O   1 
ATOM   7659 C  CB  . HIS D 1 161 ? -3.877  3.191   -53.602 1.00 12.98  ? 161 HIS D CB  1 
ATOM   7660 C  CG  . HIS D 1 161 ? -5.267  2.699   -53.563 1.00 15.22  ? 161 HIS D CG  1 
ATOM   7661 N  ND1 . HIS D 1 161 ? -6.256  3.270   -54.356 1.00 19.75  ? 161 HIS D ND1 1 
ATOM   7662 C  CD2 . HIS D 1 161 ? -5.826  1.641   -52.929 1.00 17.07  ? 161 HIS D CD2 1 
ATOM   7663 C  CE1 . HIS D 1 161 ? -7.391  2.607   -54.180 1.00 23.67  ? 161 HIS D CE1 1 
ATOM   7664 N  NE2 . HIS D 1 161 ? -7.155  1.616   -53.290 1.00 21.65  ? 161 HIS D NE2 1 
ATOM   7665 N  N   . LEU D 1 162 ? -0.560  2.573   -54.553 1.00 16.89  ? 162 LEU D N   1 
ATOM   7666 C  CA  . LEU D 1 162 ? 0.697   3.330   -54.430 1.00 17.56  ? 162 LEU D CA  1 
ATOM   7667 C  C   . LEU D 1 162 ? 1.073   4.124   -55.687 1.00 12.72  ? 162 LEU D C   1 
ATOM   7668 O  O   . LEU D 1 162 ? 1.626   5.272   -55.586 1.00 16.01  ? 162 LEU D O   1 
ATOM   7669 C  CB  . LEU D 1 162 ? 1.824   2.379   -54.051 1.00 16.58  ? 162 LEU D CB  1 
ATOM   7670 C  CG  . LEU D 1 162 ? 1.677   1.744   -52.670 1.00 23.77  ? 162 LEU D CG  1 
ATOM   7671 C  CD1 . LEU D 1 162 ? 2.821   0.808   -52.387 1.00 27.98  ? 162 LEU D CD1 1 
ATOM   7672 C  CD2 . LEU D 1 162 ? 1.585   2.805   -51.582 1.00 24.83  ? 162 LEU D CD2 1 
ATOM   7673 N  N   . GLN D 1 163 ? 0.701   3.572   -56.849 1.00 18.65  ? 163 GLN D N   1 
ATOM   7674 C  CA  . GLN D 1 163 ? 1.036   4.233   -58.102 1.00 17.09  ? 163 GLN D CA  1 
ATOM   7675 C  C   . GLN D 1 163 ? 0.375   5.615   -58.200 1.00 16.39  ? 163 GLN D C   1 
ATOM   7676 O  O   . GLN D 1 163 ? 0.929   6.498   -58.876 1.00 20.22  ? 163 GLN D O   1 
ATOM   7677 C  CB  . GLN D 1 163 ? 0.741   3.385   -59.343 1.00 20.67  ? 163 GLN D CB  1 
ATOM   7678 C  CG  . GLN D 1 163 ? -0.730  3.070   -59.600 1.00 29.04  ? 163 GLN D CG  1 
ATOM   7679 C  CD  . GLN D 1 163 ? -0.982  2.271   -60.871 1.00 30.89  ? 163 GLN D CD  1 
ATOM   7680 O  OE1 . GLN D 1 163 ? -1.175  2.820   -61.969 1.00 39.55  ? 163 GLN D OE1 1 
ATOM   7681 N  NE2 . GLN D 1 163 ? -0.991  0.954   -60.741 1.00 28.59  ? 163 GLN D NE2 1 
ATOM   7682 N  N   . HIS D 1 164 ? -0.695  5.843   -57.423 1.00 15.13  ? 164 HIS D N   1 
ATOM   7683 C  CA  . HIS D 1 164 ? -1.459  7.099   -57.471 1.00 15.63  ? 164 HIS D CA  1 
ATOM   7684 C  C   . HIS D 1 164 ? -0.851  8.172   -56.561 1.00 12.76  ? 164 HIS D C   1 
ATOM   7685 O  O   . HIS D 1 164 ? -1.268  9.304   -56.614 1.00 15.20  ? 164 HIS D O   1 
ATOM   7686 C  CB  . HIS D 1 164 ? -2.942  6.826   -57.225 1.00 15.09  ? 164 HIS D CB  1 
ATOM   7687 C  CG  . HIS D 1 164 ? -3.496  5.863   -58.218 1.00 17.78  ? 164 HIS D CG  1 
ATOM   7688 N  ND1 . HIS D 1 164 ? -3.559  6.144   -59.575 1.00 20.83  ? 164 HIS D ND1 1 
ATOM   7689 C  CD2 . HIS D 1 164 ? -3.917  4.589   -58.085 1.00 18.96  ? 164 HIS D CD2 1 
ATOM   7690 C  CE1 . HIS D 1 164 ? -4.061  5.105   -60.223 1.00 23.98  ? 164 HIS D CE1 1 
ATOM   7691 N  NE2 . HIS D 1 164 ? -4.311  4.149   -59.330 1.00 22.66  ? 164 HIS D NE2 1 
ATOM   7692 N  N   . VAL D 1 165 ? 0.163   7.825   -55.740 1.00 13.30  ? 165 VAL D N   1 
ATOM   7693 C  CA  . VAL D 1 165 ? 0.878   8.748   -54.870 1.00 13.88  ? 165 VAL D CA  1 
ATOM   7694 C  C   . VAL D 1 165 ? 2.400   8.637   -55.061 1.00 13.87  ? 165 VAL D C   1 
ATOM   7695 O  O   . VAL D 1 165 ? 3.184   8.820   -54.117 1.00 14.07  ? 165 VAL D O   1 
ATOM   7696 C  CB  . VAL D 1 165 ? 0.451   8.570   -53.391 1.00 15.89  ? 165 VAL D CB  1 
ATOM   7697 C  CG1 . VAL D 1 165 ? -1.018  8.965   -53.184 1.00 19.14  ? 165 VAL D CG1 1 
ATOM   7698 C  CG2 . VAL D 1 165 ? 0.640   7.130   -52.933 1.00 15.80  ? 165 VAL D CG2 1 
ATOM   7699 N  N   . LYS D 1 166 ? 2.838   8.382   -56.304 1.00 13.87  ? 166 LYS D N   1 
ATOM   7700 C  CA  . LYS D 1 166 ? 4.241   8.141   -56.615 1.00 12.34  ? 166 LYS D CA  1 
ATOM   7701 C  C   . LYS D 1 166 ? 5.134   9.299   -56.157 1.00 10.55  ? 166 LYS D C   1 
ATOM   7702 O  O   . LYS D 1 166 ? 6.235   9.038   -55.655 1.00 12.66  ? 166 LYS D O   1 
ATOM   7703 C  CB  . LYS D 1 166 ? 4.294   7.969   -58.132 1.00 14.35  ? 166 LYS D CB  1 
ATOM   7704 C  CG  . LYS D 1 166 ? 5.667   7.675   -58.668 1.00 16.53  ? 166 LYS D CG  1 
ATOM   7705 C  CD  . LYS D 1 166 ? 5.575   7.388   -60.136 1.00 17.02  ? 166 LYS D CD  1 
ATOM   7706 C  CE  . LYS D 1 166 ? 6.871   6.939   -60.736 1.00 24.00  ? 166 LYS D CE  1 
ATOM   7707 N  NZ  . LYS D 1 166 ? 6.576   6.425   -62.097 1.00 29.70  ? 166 LYS D NZ  1 
ATOM   7708 N  N   . TYR D 1 167 ? 4.744   10.555  -56.377 1.00 12.08  ? 167 TYR D N   1 
ATOM   7709 C  CA  . TYR D 1 167 ? 5.681   11.660  -56.091 1.00 12.71  ? 167 TYR D CA  1 
ATOM   7710 C  C   . TYR D 1 167 ? 5.190   12.498  -54.914 1.00 12.22  ? 167 TYR D C   1 
ATOM   7711 O  O   . TYR D 1 167 ? 3.974   12.537  -54.575 1.00 12.60  ? 167 TYR D O   1 
ATOM   7712 C  CB  . TYR D 1 167 ? 5.721   12.619  -57.305 1.00 13.86  ? 167 TYR D CB  1 
ATOM   7713 C  CG  . TYR D 1 167 ? 6.341   11.881  -58.469 1.00 15.73  ? 167 TYR D CG  1 
ATOM   7714 C  CD1 . TYR D 1 167 ? 7.728   11.720  -58.555 1.00 15.63  ? 167 TYR D CD1 1 
ATOM   7715 C  CD2 . TYR D 1 167 ? 5.552   11.380  -59.502 1.00 18.04  ? 167 TYR D CD2 1 
ATOM   7716 C  CE1 . TYR D 1 167 ? 8.287   11.005  -59.605 1.00 17.32  ? 167 TYR D CE1 1 
ATOM   7717 C  CE2 . TYR D 1 167 ? 6.122   10.778  -60.614 1.00 19.67  ? 167 TYR D CE2 1 
ATOM   7718 C  CZ  . TYR D 1 167 ? 7.490   10.554  -60.649 1.00 22.85  ? 167 TYR D CZ  1 
ATOM   7719 O  OH  . TYR D 1 167 ? 8.073   9.951   -61.738 1.00 30.45  ? 167 TYR D OH  1 
ATOM   7720 N  N   . LYS D 1 168 ? 6.161   13.200  -54.336 1.00 12.98  ? 168 LYS D N   1 
ATOM   7721 C  CA  . LYS D 1 168 ? 5.838   14.088  -53.235 1.00 18.05  ? 168 LYS D CA  1 
ATOM   7722 C  C   . LYS D 1 168 ? 4.654   14.986  -53.620 1.00 21.48  ? 168 LYS D C   1 
ATOM   7723 O  O   . LYS D 1 168 ? 4.692   15.684  -54.651 1.00 19.13  ? 168 LYS D O   1 
ATOM   7724 C  CB  . LYS D 1 168 ? 7.027   15.017  -52.962 1.00 18.26  ? 168 LYS D CB  1 
ATOM   7725 C  CG  . LYS D 1 168 ? 6.858   15.892  -51.732 1.00 27.33  ? 168 LYS D CG  1 
ATOM   7726 C  CD  . LYS D 1 168 ? 8.073   16.715  -51.393 1.00 27.66  ? 168 LYS D CD  1 
ATOM   7727 C  CE  . LYS D 1 168 ? 7.660   18.018  -50.742 1.00 35.53  ? 168 LYS D CE  1 
ATOM   7728 N  NZ  . LYS D 1 168 ? 8.789   18.951  -50.564 1.00 45.72  ? 168 LYS D NZ  1 
ATOM   7729 N  N   . GLY D 1 169 ? 3.674   15.076  -52.706 1.00 24.22  ? 169 GLY D N   1 
ATOM   7730 C  CA  . GLY D 1 169 ? 2.568   16.000  -52.895 1.00 27.22  ? 169 GLY D CA  1 
ATOM   7731 C  C   . GLY D 1 169 ? 1.346   15.411  -53.597 1.00 21.46  ? 169 GLY D C   1 
ATOM   7732 O  O   . GLY D 1 169 ? 0.309   16.052  -53.693 1.00 29.49  ? 169 GLY D O   1 
ATOM   7733 N  N   . GLN D 1 170 ? 1.458   14.190  -54.099 1.00 16.05  ? 170 GLN D N   1 
ATOM   7734 C  CA  . GLN D 1 170 ? 0.331   13.491  -54.665 1.00 17.54  ? 170 GLN D CA  1 
ATOM   7735 C  C   . GLN D 1 170 ? -0.535  12.875  -53.565 1.00 14.86  ? 170 GLN D C   1 
ATOM   7736 O  O   . GLN D 1 170 ? -0.039  12.444  -52.514 1.00 19.94  ? 170 GLN D O   1 
ATOM   7737 C  CB  . GLN D 1 170 ? 0.893   12.492  -55.678 1.00 14.90  ? 170 GLN D CB  1 
ATOM   7738 C  CG  . GLN D 1 170 ? 1.478   13.193  -56.911 1.00 18.48  ? 170 GLN D CG  1 
ATOM   7739 C  CD  . GLN D 1 170 ? 1.826   12.226  -58.027 1.00 16.94  ? 170 GLN D CD  1 
ATOM   7740 O  OE1 . GLN D 1 170 ? 2.167   11.090  -57.776 1.00 16.69  ? 170 GLN D OE1 1 
ATOM   7741 N  NE2 . GLN D 1 170 ? 1.756   12.674  -59.280 1.00 19.62  ? 170 GLN D NE2 1 
ATOM   7742 N  N   . GLU D 1 171 ? -1.825  12.791  -53.863 1.00 17.13  ? 171 GLU D N   1 
ATOM   7743 C  CA  . GLU D 1 171 ? -2.841  12.330  -52.924 1.00 16.20  ? 171 GLU D CA  1 
ATOM   7744 C  C   . GLU D 1 171 ? -3.806  11.468  -53.710 1.00 17.44  ? 171 GLU D C   1 
ATOM   7745 O  O   . GLU D 1 171 ? -4.020  11.715  -54.896 1.00 19.65  ? 171 GLU D O   1 
ATOM   7746 C  CB  . GLU D 1 171 ? -3.587  13.485  -52.234 1.00 23.43  ? 171 GLU D CB  1 
ATOM   7747 C  CG  . GLU D 1 171 ? -2.718  14.289  -51.291 1.00 29.37  ? 171 GLU D CG  1 
ATOM   7748 C  CD  . GLU D 1 171 ? -3.317  15.558  -50.711 1.00 32.91  ? 171 GLU D CD  1 
ATOM   7749 O  OE1 . GLU D 1 171 ? -4.476  15.899  -51.046 1.00 29.11  ? 171 GLU D OE1 1 
ATOM   7750 O  OE2 . GLU D 1 171 ? -2.609  16.212  -49.921 1.00 37.07  ? 171 GLU D OE2 1 
ATOM   7751 N  N   . ALA D 1 172 ? -4.408  10.480  -53.036 1.00 15.79  ? 172 ALA D N   1 
ATOM   7752 C  CA  . ALA D 1 172 ? -5.400  9.602   -53.652 1.00 18.31  ? 172 ALA D CA  1 
ATOM   7753 C  C   . ALA D 1 172 ? -6.338  9.145   -52.546 1.00 17.12  ? 172 ALA D C   1 
ATOM   7754 O  O   . ALA D 1 172 ? -5.945  9.007   -51.380 1.00 20.79  ? 172 ALA D O   1 
ATOM   7755 C  CB  . ALA D 1 172 ? -4.738  8.402   -54.303 1.00 19.25  ? 172 ALA D CB  1 
ATOM   7756 N  N   . PHE D 1 173 ? -7.540  8.769   -52.927 1.00 17.84  ? 173 PHE D N   1 
ATOM   7757 C  CA  . PHE D 1 173 ? -8.502  8.225   -51.981 1.00 16.33  ? 173 PHE D CA  1 
ATOM   7758 C  C   . PHE D 1 173 ? -8.492  6.697   -52.031 1.00 15.25  ? 173 PHE D C   1 
ATOM   7759 O  O   . PHE D 1 173 ? -8.467  6.089   -53.099 1.00 26.24  ? 173 PHE D O   1 
ATOM   7760 C  CB  . PHE D 1 173 ? -9.900  8.806   -52.199 1.00 18.99  ? 173 PHE D CB  1 
ATOM   7761 C  CG  . PHE D 1 173 ? -10.088 10.182  -51.600 1.00 19.22  ? 173 PHE D CG  1 
ATOM   7762 C  CD1 . PHE D 1 173 ? -10.117 10.378  -50.217 1.00 21.48  ? 173 PHE D CD1 1 
ATOM   7763 C  CD2 . PHE D 1 173 ? -10.251 11.294  -52.406 1.00 26.85  ? 173 PHE D CD2 1 
ATOM   7764 C  CE1 . PHE D 1 173 ? -10.324 11.633  -49.662 1.00 26.40  ? 173 PHE D CE1 1 
ATOM   7765 C  CE2 . PHE D 1 173 ? -10.465 12.551  -51.845 1.00 32.42  ? 173 PHE D CE2 1 
ATOM   7766 C  CZ  . PHE D 1 173 ? -10.490 12.738  -50.475 1.00 25.92  ? 173 PHE D CZ  1 
ATOM   7767 N  N   . VAL D 1 174 ? -8.487  6.110   -50.844 1.00 15.69  ? 174 VAL D N   1 
ATOM   7768 C  CA  . VAL D 1 174 ? -8.501  4.646   -50.658 1.00 14.64  ? 174 VAL D CA  1 
ATOM   7769 C  C   . VAL D 1 174 ? -9.840  4.323   -49.976 1.00 15.90  ? 174 VAL D C   1 
ATOM   7770 O  O   . VAL D 1 174 ? -10.214 4.974   -48.977 1.00 15.34  ? 174 VAL D O   1 
ATOM   7771 C  CB  . VAL D 1 174 ? -7.361  4.211   -49.683 1.00 15.69  ? 174 VAL D CB  1 
ATOM   7772 C  CG1 . VAL D 1 174 ? -7.433  2.687   -49.382 1.00 15.11  ? 174 VAL D CG1 1 
ATOM   7773 C  CG2 . VAL D 1 174 ? -5.975  4.502   -50.257 1.00 19.15  ? 174 VAL D CG2 1 
ATOM   7774 N  N   . PRO D 1 175 ? -10.616 3.310   -50.450 1.00 14.01  ? 175 PRO D N   1 
ATOM   7775 C  CA  . PRO D 1 175 ? -11.824 2.905   -49.737 1.00 12.38  ? 175 PRO D CA  1 
ATOM   7776 C  C   . PRO D 1 175 ? -11.454 2.440   -48.324 1.00 13.60  ? 175 PRO D C   1 
ATOM   7777 O  O   . PRO D 1 175 ? -10.390 1.822   -48.102 1.00 14.05  ? 175 PRO D O   1 
ATOM   7778 C  CB  . PRO D 1 175 ? -12.376 1.752   -50.575 1.00 16.90  ? 175 PRO D CB  1 
ATOM   7779 C  CG  . PRO D 1 175 ? -11.807 1.951   -51.972 1.00 18.88  ? 175 PRO D CG  1 
ATOM   7780 C  CD  . PRO D 1 175 ? -10.426 2.531   -51.692 1.00 15.65  ? 175 PRO D CD  1 
ATOM   7781 N  N   . GLY D 1 176 ? -12.342 2.699   -47.347 1.00 12.75  ? 176 GLY D N   1 
ATOM   7782 C  CA  . GLY D 1 176 ? -12.129 2.116   -46.020 1.00 12.29  ? 176 GLY D CA  1 
ATOM   7783 C  C   . GLY D 1 176 ? -12.068 0.589   -46.043 1.00 11.74  ? 176 GLY D C   1 
ATOM   7784 O  O   . GLY D 1 176 ? -12.640 -0.102  -46.883 1.00 16.17  ? 176 GLY D O   1 
ATOM   7785 N  N   . PHE D 1 177 ? -11.355 0.085   -45.048 1.00 12.19  ? 177 PHE D N   1 
ATOM   7786 C  CA  . PHE D 1 177 ? -11.400 -1.336  -44.808 1.00 11.23  ? 177 PHE D CA  1 
ATOM   7787 C  C   . PHE D 1 177 ? -11.112 -1.501  -43.309 1.00 10.92  ? 177 PHE D C   1 
ATOM   7788 O  O   . PHE D 1 177 ? -10.825 -0.513  -42.572 1.00 12.48  ? 177 PHE D O   1 
ATOM   7789 C  CB  . PHE D 1 177 ? -10.388 -2.075  -45.679 1.00 15.27  ? 177 PHE D CB  1 
ATOM   7790 C  CG  . PHE D 1 177 ? -8.935  -1.707  -45.438 1.00 12.76  ? 177 PHE D CG  1 
ATOM   7791 C  CD1 . PHE D 1 177 ? -8.339  -0.568  -46.022 1.00 11.54  ? 177 PHE D CD1 1 
ATOM   7792 C  CD2 . PHE D 1 177 ? -8.149  -2.530  -44.617 1.00 12.04  ? 177 PHE D CD2 1 
ATOM   7793 C  CE1 . PHE D 1 177 ? -6.984  -0.333  -45.824 1.00 14.43  ? 177 PHE D CE1 1 
ATOM   7794 C  CE2 . PHE D 1 177 ? -6.800  -2.265  -44.420 1.00 14.00  ? 177 PHE D CE2 1 
ATOM   7795 C  CZ  . PHE D 1 177 ? -6.228  -1.150  -45.002 1.00 14.93  ? 177 PHE D CZ  1 
ATOM   7796 N  N   . ASN D 1 178 ? -11.206 -2.725  -42.856 1.00 10.49  ? 178 ASN D N   1 
ATOM   7797 C  CA  . ASN D 1 178 ? -10.997 -2.952  -41.433 1.00 11.18  ? 178 ASN D CA  1 
ATOM   7798 C  C   . ASN D 1 178 ? -9.513  -2.919  -41.079 1.00 9.76   ? 178 ASN D C   1 
ATOM   7799 O  O   . ASN D 1 178 ? -8.826  -3.857  -41.365 1.00 10.62  ? 178 ASN D O   1 
ATOM   7800 C  CB  . ASN D 1 178 ? -11.664 -4.254  -40.975 1.00 13.93  ? 178 ASN D CB  1 
ATOM   7801 C  CG  . ASN D 1 178 ? -11.374 -4.603  -39.555 1.00 14.89  ? 178 ASN D CG  1 
ATOM   7802 O  OD1 . ASN D 1 178 ? -11.028 -3.788  -38.704 1.00 13.38  ? 178 ASN D OD1 1 
ATOM   7803 N  ND2 . ASN D 1 178 ? -11.460 -5.911  -39.332 1.00 21.91  ? 178 ASN D ND2 1 
ATOM   7804 N  N   . ILE D 1 179 ? -9.031  -1.887  -40.387 1.00 10.15  ? 179 ILE D N   1 
ATOM   7805 C  CA  . ILE D 1 179 ? -7.618  -1.718  -40.103 1.00 8.85   ? 179 ILE D CA  1 
ATOM   7806 C  C   . ILE D 1 179 ? -7.076  -2.851  -39.208 1.00 10.36  ? 179 ILE D C   1 
ATOM   7807 O  O   . ILE D 1 179 ? -5.865  -3.154  -39.215 1.00 9.30   ? 179 ILE D O   1 
ATOM   7808 C  CB  . ILE D 1 179 ? -7.345  -0.305  -39.510 1.00 9.73   ? 179 ILE D CB  1 
ATOM   7809 C  CG1 . ILE D 1 179 ? -7.801  0.778   -40.525 1.00 11.06  ? 179 ILE D CG1 1 
ATOM   7810 C  CG2 . ILE D 1 179 ? -5.838  -0.198  -39.219 1.00 10.88  ? 179 ILE D CG2 1 
ATOM   7811 C  CD1 . ILE D 1 179 ? -7.221  0.655   -41.928 1.00 12.11  ? 179 ILE D CD1 1 
ATOM   7812 N  N   A GLU D 1 180 ? -7.968  -3.473  -38.445 0.50 9.99   ? 180 GLU D N   1 
ATOM   7813 N  N   B GLU D 1 180 ? -7.966  -3.460  -38.414 0.50 10.02  ? 180 GLU D N   1 
ATOM   7814 C  CA  A GLU D 1 180 ? -7.493  -4.550  -37.587 0.50 11.43  ? 180 GLU D CA  1 
ATOM   7815 C  CA  B GLU D 1 180 ? -7.537  -4.586  -37.584 0.50 11.27  ? 180 GLU D CA  1 
ATOM   7816 C  C   A GLU D 1 180 ? -7.033  -5.768  -38.407 0.50 11.66  ? 180 GLU D C   1 
ATOM   7817 C  C   B GLU D 1 180 ? -6.957  -5.723  -38.435 0.50 10.98  ? 180 GLU D C   1 
ATOM   7818 O  O   A GLU D 1 180 ? -6.326  -6.637  -37.882 0.50 14.51  ? 180 GLU D O   1 
ATOM   7819 O  O   B GLU D 1 180 ? -6.091  -6.470  -37.963 0.50 11.32  ? 180 GLU D O   1 
ATOM   7820 C  CB  A GLU D 1 180 ? -8.606  -4.959  -36.624 0.50 14.77  ? 180 GLU D CB  1 
ATOM   7821 C  CB  B GLU D 1 180 ? -8.704  -5.174  -36.783 0.50 14.17  ? 180 GLU D CB  1 
ATOM   7822 C  CG  A GLU D 1 180 ? -8.072  -5.643  -35.389 0.50 16.36  ? 180 GLU D CG  1 
ATOM   7823 C  CG  B GLU D 1 180 ? -9.128  -4.294  -35.604 0.50 14.52  ? 180 GLU D CG  1 
ATOM   7824 C  CD  A GLU D 1 180 ? -9.083  -6.029  -34.326 0.50 17.24  ? 180 GLU D CD  1 
ATOM   7825 C  CD  B GLU D 1 180 ? -9.935  -4.913  -34.460 0.50 15.55  ? 180 GLU D CD  1 
ATOM   7826 O  OE1 A GLU D 1 180 ? -10.284 -5.670  -34.464 0.50 19.77  ? 180 GLU D OE1 1 
ATOM   7827 O  OE1 B GLU D 1 180 ? -9.459  -5.899  -33.809 0.50 20.24  ? 180 GLU D OE1 1 
ATOM   7828 O  OE2 A GLU D 1 180 ? -8.669  -6.687  -33.367 0.50 20.05  ? 180 GLU D OE2 1 
ATOM   7829 O  OE2 B GLU D 1 180 ? -11.040 -4.371  -34.188 0.50 15.54  ? 180 GLU D OE2 1 
ATOM   7830 N  N   . GLU D 1 181 ? -7.365  -5.798  -39.708 1.00 10.71  ? 181 GLU D N   1 
ATOM   7831 C  CA  . GLU D 1 181 ? -6.832  -6.890  -40.547 1.00 9.95   ? 181 GLU D CA  1 
ATOM   7832 C  C   . GLU D 1 181 ? -5.323  -6.695  -40.781 1.00 9.18   ? 181 GLU D C   1 
ATOM   7833 O  O   . GLU D 1 181 ? -4.619  -7.570  -41.245 1.00 10.82  ? 181 GLU D O   1 
ATOM   7834 C  CB  . GLU D 1 181 ? -7.414  -6.842  -41.939 1.00 11.90  ? 181 GLU D CB  1 
ATOM   7835 C  CG  . GLU D 1 181 ? -8.900  -7.237  -41.980 1.00 12.62  ? 181 GLU D CG  1 
ATOM   7836 C  CD  . GLU D 1 181 ? -9.580  -6.955  -43.333 1.00 13.04  ? 181 GLU D CD  1 
ATOM   7837 O  OE1 . GLU D 1 181 ? -8.870  -6.631  -44.370 1.00 15.95  ? 181 GLU D OE1 1 
ATOM   7838 O  OE2 . GLU D 1 181 ? -10.830 -7.019  -43.384 1.00 16.14  ? 181 GLU D OE2 1 
ATOM   7839 N  N   . LEU D 1 182 ? -4.731  -5.525  -40.500 1.00 8.79   ? 182 LEU D N   1 
ATOM   7840 C  CA  . LEU D 1 182 ? -3.283  -5.287  -40.641 1.00 8.41   ? 182 LEU D CA  1 
ATOM   7841 C  C   . LEU D 1 182 ? -2.531  -5.768  -39.388 1.00 8.90   ? 182 LEU D C   1 
ATOM   7842 O  O   . LEU D 1 182 ? -1.304  -5.776  -39.368 1.00 10.16  ? 182 LEU D O   1 
ATOM   7843 C  CB  . LEU D 1 182 ? -2.970  -3.763  -40.803 1.00 10.18  ? 182 LEU D CB  1 
ATOM   7844 C  CG  . LEU D 1 182 ? -3.676  -3.146  -42.019 1.00 8.19   ? 182 LEU D CG  1 
ATOM   7845 C  CD1 . LEU D 1 182 ? -3.396  -1.635  -42.128 1.00 10.65  ? 182 LEU D CD1 1 
ATOM   7846 C  CD2 . LEU D 1 182 ? -3.330  -3.874  -43.286 1.00 9.06   ? 182 LEU D CD2 1 
ATOM   7847 N  N   . LEU D 1 183 ? -3.229  -6.019  -38.279 1.00 10.27  ? 183 LEU D N   1 
ATOM   7848 C  CA  . LEU D 1 183 ? -2.591  -6.418  -37.046 1.00 10.38  ? 183 LEU D CA  1 
ATOM   7849 C  C   . LEU D 1 183 ? -2.300  -7.930  -37.081 1.00 9.24   ? 183 LEU D C   1 
ATOM   7850 O  O   . LEU D 1 183 ? -2.979  -8.673  -37.767 1.00 11.68  ? 183 LEU D O   1 
ATOM   7851 C  CB  . LEU D 1 183 ? -3.547  -6.074  -35.901 1.00 12.54  ? 183 LEU D CB  1 
ATOM   7852 C  CG  . LEU D 1 183 ? -3.898  -4.594  -35.709 1.00 12.94  ? 183 LEU D CG  1 
ATOM   7853 C  CD1 . LEU D 1 183 ? -4.716  -4.380  -34.442 1.00 17.38  ? 183 LEU D CD1 1 
ATOM   7854 C  CD2 . LEU D 1 183 ? -2.639  -3.718  -35.686 1.00 16.31  ? 183 LEU D CD2 1 
ATOM   7855 N  N   . PRO D 1 184 ? -1.282  -8.350  -36.296 1.00 9.42   ? 184 PRO D N   1 
ATOM   7856 C  CA  . PRO D 1 184 ? -0.895  -9.755  -36.271 1.00 10.31  ? 184 PRO D CA  1 
ATOM   7857 C  C   . PRO D 1 184 ? -1.748  -10.583 -35.315 1.00 11.91  ? 184 PRO D C   1 
ATOM   7858 O  O   . PRO D 1 184 ? -2.635  -10.097 -34.629 1.00 12.58  ? 184 PRO D O   1 
ATOM   7859 C  CB  . PRO D 1 184 ? 0.551   -9.716  -35.706 1.00 10.95  ? 184 PRO D CB  1 
ATOM   7860 C  CG  . PRO D 1 184 ? 0.544   -8.505  -34.755 1.00 11.51  ? 184 PRO D CG  1 
ATOM   7861 C  CD  . PRO D 1 184 ? -0.386  -7.502  -35.483 1.00 10.00  ? 184 PRO D CD  1 
ATOM   7862 N  N   . GLU D 1 185 ? -1.467  -11.903 -35.333 1.00 12.88  ? 185 GLU D N   1 
ATOM   7863 C  CA  . GLU D 1 185 ? -2.054  -12.765 -34.303 1.00 14.16  ? 185 GLU D CA  1 
ATOM   7864 C  C   . GLU D 1 185 ? -1.619  -12.360 -32.887 1.00 12.59  ? 185 GLU D C   1 
ATOM   7865 O  O   . GLU D 1 185 ? -0.486  -11.875 -32.645 1.00 12.91  ? 185 GLU D O   1 
ATOM   7866 C  CB  . GLU D 1 185 ? -1.662  -14.243 -34.515 1.00 17.29  ? 185 GLU D CB  1 
ATOM   7867 C  CG  . GLU D 1 185 ? -2.067  -14.858 -35.857 1.00 20.84  ? 185 GLU D CG  1 
ATOM   7868 C  CD  . GLU D 1 185 ? -1.867  -16.362 -36.004 1.00 32.74  ? 185 GLU D CD  1 
ATOM   7869 O  OE1 . GLU D 1 185 ? -0.740  -16.783 -36.333 1.00 41.64  ? 185 GLU D OE1 1 
ATOM   7870 O  OE2 . GLU D 1 185 ? -2.835  -17.099 -35.767 1.00 45.69  ? 185 GLU D OE2 1 
ATOM   7871 N  N   . ARG D 1 186 ? -2.532  -12.627 -31.946 1.00 13.30  ? 186 ARG D N   1 
ATOM   7872 C  CA  . ARG D 1 186 ? -2.274  -12.520 -30.525 1.00 14.01  ? 186 ARG D CA  1 
ATOM   7873 C  C   . ARG D 1 186 ? -1.781  -11.135 -30.145 1.00 12.59  ? 186 ARG D C   1 
ATOM   7874 O  O   . ARG D 1 186 ? -0.698  -10.925 -29.555 1.00 13.63  ? 186 ARG D O   1 
ATOM   7875 C  CB  . ARG D 1 186 ? -1.284  -13.593 -30.096 1.00 16.59  ? 186 ARG D CB  1 
ATOM   7876 C  CG  . ARG D 1 186 ? -1.931  -14.979 -30.084 1.00 20.40  ? 186 ARG D CG  1 
ATOM   7877 C  CD  . ARG D 1 186 ? -1.092  -16.177 -29.687 1.00 24.08  ? 186 ARG D CD  1 
ATOM   7878 N  NE  . ARG D 1 186 ? 0.029   -16.353 -30.604 1.00 24.02  ? 186 ARG D NE  1 
ATOM   7879 C  CZ  . ARG D 1 186 ? -0.028  -16.923 -31.807 1.00 32.51  ? 186 ARG D CZ  1 
ATOM   7880 N  NH1 . ARG D 1 186 ? -1.179  -17.378 -32.285 1.00 33.00  ? 186 ARG D NH1 1 
ATOM   7881 N  NH2 . ARG D 1 186 ? 1.070   -16.983 -32.540 1.00 33.47  ? 186 ARG D NH2 1 
ATOM   7882 N  N   . THR D 1 187 ? -2.613  -10.171 -30.464 1.00 13.49  ? 187 THR D N   1 
ATOM   7883 C  CA  . THR D 1 187 ? -2.255  -8.773  -30.166 1.00 11.98  ? 187 THR D CA  1 
ATOM   7884 C  C   . THR D 1 187 ? -2.074  -8.546  -28.663 1.00 13.11  ? 187 THR D C   1 
ATOM   7885 O  O   . THR D 1 187 ? -1.514  -7.503  -28.283 1.00 11.22  ? 187 THR D O   1 
ATOM   7886 C  CB  . THR D 1 187 ? -3.257  -7.773  -30.768 1.00 12.98  ? 187 THR D CB  1 
ATOM   7887 O  OG1 . THR D 1 187 ? -4.576  -8.101  -30.333 1.00 14.92  ? 187 THR D OG1 1 
ATOM   7888 C  CG2 . THR D 1 187 ? -3.141  -7.729  -32.280 1.00 15.08  ? 187 THR D CG2 1 
ATOM   7889 N  N   . ALA D 1 188 ? -2.612  -9.412  -27.784 1.00 12.61  ? 188 ALA D N   1 
ATOM   7890 C  CA  . ALA D 1 188 ? -2.388  -9.253  -26.353 1.00 12.65  ? 188 ALA D CA  1 
ATOM   7891 C  C   . ALA D 1 188 ? -0.897  -9.368  -25.982 1.00 10.86  ? 188 ALA D C   1 
ATOM   7892 O  O   . ALA D 1 188 ? -0.526  -9.008  -24.867 1.00 11.99  ? 188 ALA D O   1 
ATOM   7893 C  CB  . ALA D 1 188 ? -3.228  -10.291 -25.612 1.00 15.97  ? 188 ALA D CB  1 
ATOM   7894 N  N   . GLU D 1 189 ? -0.071  -9.933  -26.875 1.00 11.38  ? 189 GLU D N   1 
ATOM   7895 C  CA  . GLU D 1 189 ? 1.350   -10.140 -26.636 1.00 11.02  ? 189 GLU D CA  1 
ATOM   7896 C  C   . GLU D 1 189 ? 2.118   -9.014  -27.345 1.00 10.80  ? 189 GLU D C   1 
ATOM   7897 O  O   . GLU D 1 189 ? 2.127   -8.955  -28.571 1.00 10.96  ? 189 GLU D O   1 
ATOM   7898 C  CB  . GLU D 1 189 ? 1.776   -11.457 -27.278 1.00 11.13  ? 189 GLU D CB  1 
ATOM   7899 C  CG  . GLU D 1 189 ? 1.073   -12.592 -26.521 1.00 16.12  ? 189 GLU D CG  1 
ATOM   7900 C  CD  . GLU D 1 189 ? 1.399   -13.993 -27.010 1.00 17.18  ? 189 GLU D CD  1 
ATOM   7901 O  OE1 . GLU D 1 189 ? 2.504   -14.227 -27.488 1.00 19.57  ? 189 GLU D OE1 1 
ATOM   7902 O  OE2 . GLU D 1 189 ? 0.561   -14.839 -26.764 1.00 22.18  ? 189 GLU D OE2 1 
ATOM   7903 N  N   . TYR D 1 190 ? 2.807   -8.180  -26.548 1.00 10.81  ? 190 TYR D N   1 
ATOM   7904 C  CA  . TYR D 1 190 ? 3.438   -6.997  -27.153 1.00 10.03  ? 190 TYR D CA  1 
ATOM   7905 C  C   . TYR D 1 190 ? 4.573   -6.527  -26.251 1.00 9.36   ? 190 TYR D C   1 
ATOM   7906 O  O   . TYR D 1 190 ? 4.681   -6.883  -25.060 1.00 10.44  ? 190 TYR D O   1 
ATOM   7907 C  CB  . TYR D 1 190 ? 2.421   -5.867  -27.414 1.00 10.02  ? 190 TYR D CB  1 
ATOM   7908 C  CG  . TYR D 1 190 ? 1.663   -5.429  -26.196 1.00 10.34  ? 190 TYR D CG  1 
ATOM   7909 C  CD1 . TYR D 1 190 ? 2.250   -4.529  -25.286 1.00 11.07  ? 190 TYR D CD1 1 
ATOM   7910 C  CD2 . TYR D 1 190 ? 0.348   -5.843  -25.982 1.00 10.44  ? 190 TYR D CD2 1 
ATOM   7911 C  CE1 . TYR D 1 190 ? 1.516   -4.047  -24.202 1.00 12.09  ? 190 TYR D CE1 1 
ATOM   7912 C  CE2 . TYR D 1 190 ? -0.361  -5.402  -24.867 1.00 9.83   ? 190 TYR D CE2 1 
ATOM   7913 C  CZ  . TYR D 1 190 ? 0.216   -4.497  -23.971 1.00 9.66   ? 190 TYR D CZ  1 
ATOM   7914 O  OH  . TYR D 1 190 ? -0.458  -4.052  -22.849 1.00 10.87  ? 190 TYR D OH  1 
ATOM   7915 N  N   . TYR D 1 191 ? 5.450   -5.712  -26.845 1.00 8.92   ? 191 TYR D N   1 
ATOM   7916 C  CA  . TYR D 1 191 ? 6.476   -4.970  -26.137 1.00 9.83   ? 191 TYR D CA  1 
ATOM   7917 C  C   . TYR D 1 191 ? 5.999   -3.532  -25.957 1.00 9.97   ? 191 TYR D C   1 
ATOM   7918 O  O   . TYR D 1 191 ? 5.357   -3.021  -26.863 1.00 10.28  ? 191 TYR D O   1 
ATOM   7919 C  CB  . TYR D 1 191 ? 7.691   -4.929  -27.082 1.00 8.75   ? 191 TYR D CB  1 
ATOM   7920 C  CG  . TYR D 1 191 ? 8.263   -6.244  -27.569 1.00 8.06   ? 191 TYR D CG  1 
ATOM   7921 C  CD1 . TYR D 1 191 ? 9.226   -6.922  -26.846 1.00 8.28   ? 191 TYR D CD1 1 
ATOM   7922 C  CD2 . TYR D 1 191 ? 7.916   -6.741  -28.821 1.00 9.67   ? 191 TYR D CD2 1 
ATOM   7923 C  CE1 . TYR D 1 191 ? 9.807   -8.086  -27.330 1.00 10.57  ? 191 TYR D CE1 1 
ATOM   7924 C  CE2 . TYR D 1 191 ? 8.439   -7.947  -29.287 1.00 9.91   ? 191 TYR D CE2 1 
ATOM   7925 C  CZ  . TYR D 1 191 ? 9.415   -8.597  -28.549 1.00 10.46  ? 191 TYR D CZ  1 
ATOM   7926 O  OH  . TYR D 1 191 ? 9.950   -9.792  -29.032 1.00 13.54  ? 191 TYR D OH  1 
ATOM   7927 N  N   . ARG D 1 192 ? 6.382   -2.908  -24.838 1.00 10.51  ? 192 ARG D N   1 
ATOM   7928 C  CA  . ARG D 1 192 ? 5.963   -1.543  -24.540 1.00 9.05   ? 192 ARG D CA  1 
ATOM   7929 C  C   . ARG D 1 192 ? 7.189   -0.772  -24.080 1.00 8.15   ? 192 ARG D C   1 
ATOM   7930 O  O   . ARG D 1 192 ? 7.824   -1.195  -23.115 1.00 9.68   ? 192 ARG D O   1 
ATOM   7931 C  CB  . ARG D 1 192 ? 4.859   -1.653  -23.447 1.00 10.67  ? 192 ARG D CB  1 
ATOM   7932 C  CG  . ARG D 1 192 ? 4.559   -0.340  -22.731 1.00 13.11  ? 192 ARG D CG  1 
ATOM   7933 C  CD  . ARG D 1 192 ? 3.833   0.675   -23.622 1.00 12.15  ? 192 ARG D CD  1 
ATOM   7934 N  NE  . ARG D 1 192 ? 2.660   0.161   -24.402 1.00 13.74  ? 192 ARG D NE  1 
ATOM   7935 C  CZ  . ARG D 1 192 ? 1.474   -0.165  -23.870 1.00 13.33  ? 192 ARG D CZ  1 
ATOM   7936 N  NH1 . ARG D 1 192 ? 1.229   0.044   -22.578 1.00 17.16  ? 192 ARG D NH1 1 
ATOM   7937 N  NH2 . ARG D 1 192 ? 0.508   -0.625  -24.658 1.00 15.69  ? 192 ARG D NH2 1 
ATOM   7938 N  N   . TYR D 1 193 ? 7.415   0.470   -24.586 1.00 7.94   ? 193 TYR D N   1 
ATOM   7939 C  CA  . TYR D 1 193 ? 8.439   1.295   -23.966 1.00 7.32   ? 193 TYR D CA  1 
ATOM   7940 C  C   . TYR D 1 193 ? 8.198   2.754   -24.300 1.00 7.96   ? 193 TYR D C   1 
ATOM   7941 O  O   . TYR D 1 193 ? 7.446   3.051   -25.204 1.00 9.24   ? 193 TYR D O   1 
ATOM   7942 C  CB  . TYR D 1 193 ? 9.812   0.785   -24.479 1.00 10.05  ? 193 TYR D CB  1 
ATOM   7943 C  CG  . TYR D 1 193 ? 10.165  1.176   -25.909 1.00 7.04   ? 193 TYR D CG  1 
ATOM   7944 C  CD1 . TYR D 1 193 ? 9.780   0.457   -27.007 1.00 10.17  ? 193 TYR D CD1 1 
ATOM   7945 C  CD2 . TYR D 1 193 ? 10.913  2.330   -26.188 1.00 8.95   ? 193 TYR D CD2 1 
ATOM   7946 C  CE1 . TYR D 1 193 ? 10.103  0.770   -28.311 1.00 9.29   ? 193 TYR D CE1 1 
ATOM   7947 C  CE2 . TYR D 1 193 ? 11.244  2.719   -27.466 1.00 8.83   ? 193 TYR D CE2 1 
ATOM   7948 C  CZ  . TYR D 1 193 ? 10.813  1.974   -28.540 1.00 8.45   ? 193 TYR D CZ  1 
ATOM   7949 O  OH  . TYR D 1 193 ? 11.108  2.389   -29.796 1.00 8.60   ? 193 TYR D OH  1 
ATOM   7950 N  N   . ARG D 1 194 ? 8.923   3.595   -23.588 1.00 10.47  ? 194 ARG D N   1 
ATOM   7951 C  CA  . ARG D 1 194 ? 8.828   5.042   -23.837 1.00 11.17  ? 194 ARG D CA  1 
ATOM   7952 C  C   . ARG D 1 194 ? 9.924   5.476   -24.796 1.00 10.38  ? 194 ARG D C   1 
ATOM   7953 O  O   . ARG D 1 194 ? 11.102  5.235   -24.622 1.00 11.99  ? 194 ARG D O   1 
ATOM   7954 C  CB  . ARG D 1 194 ? 9.166   5.760   -22.545 1.00 13.85  ? 194 ARG D CB  1 
ATOM   7955 C  CG  . ARG D 1 194 ? 8.133   5.520   -21.484 1.00 17.47  ? 194 ARG D CG  1 
ATOM   7956 C  CD  . ARG D 1 194 ? 6.985   6.412   -21.736 1.00 23.91  ? 194 ARG D CD  1 
ATOM   7957 N  NE  . ARG D 1 194 ? 6.068   6.145   -20.654 1.00 28.03  ? 194 ARG D NE  1 
ATOM   7958 C  CZ  . ARG D 1 194 ? 5.028   6.921   -20.434 1.00 30.42  ? 194 ARG D CZ  1 
ATOM   7959 N  NH1 . ARG D 1 194 ? 4.862   7.990   -21.209 1.00 31.07  ? 194 ARG D NH1 1 
ATOM   7960 N  NH2 . ARG D 1 194 ? 4.194   6.656   -19.440 1.00 30.96  ? 194 ARG D NH2 1 
ATOM   7961 N  N   . GLY D 1 195 ? 9.486   6.133   -25.873 1.00 8.74   ? 195 GLY D N   1 
ATOM   7962 C  CA  . GLY D 1 195 ? 10.450  6.593   -26.852 1.00 10.25  ? 195 GLY D CA  1 
ATOM   7963 C  C   . GLY D 1 195 ? 10.021  7.842   -27.623 1.00 9.79   ? 195 GLY D C   1 
ATOM   7964 O  O   . GLY D 1 195 ? 9.400   8.711   -27.005 1.00 9.77   ? 195 GLY D O   1 
ATOM   7965 N  N   . SER D 1 196 ? 10.336  7.855   -28.914 1.00 9.28   ? 196 SER D N   1 
ATOM   7966 C  CA  . SER D 1 196 ? 10.248  9.094   -29.685 1.00 8.90   ? 196 SER D CA  1 
ATOM   7967 C  C   . SER D 1 196 ? 9.586   8.864   -31.033 1.00 8.62   ? 196 SER D C   1 
ATOM   7968 O  O   . SER D 1 196 ? 9.466   7.692   -31.490 1.00 7.71   ? 196 SER D O   1 
ATOM   7969 C  CB  . SER D 1 196 ? 11.638  9.683   -29.892 1.00 9.77   ? 196 SER D CB  1 
ATOM   7970 O  OG  . SER D 1 196 ? 12.439  8.961   -30.835 1.00 9.21   ? 196 SER D OG  1 
ATOM   7971 N  N   . LEU D 1 197 ? 9.350   9.942   -31.812 1.00 8.43   ? 197 LEU D N   1 
ATOM   7972 C  CA  . LEU D 1 197 ? 9.162   9.767   -33.242 1.00 8.35   ? 197 LEU D CA  1 
ATOM   7973 C  C   . LEU D 1 197 ? 10.496  9.219   -33.759 1.00 8.76   ? 197 LEU D C   1 
ATOM   7974 O  O   . LEU D 1 197 ? 11.612  9.614   -33.339 1.00 9.28   ? 197 LEU D O   1 
ATOM   7975 C  CB  . LEU D 1 197 ? 8.956   11.155  -33.924 1.00 10.15  ? 197 LEU D CB  1 
ATOM   7976 C  CG  . LEU D 1 197 ? 7.525   11.707  -33.806 1.00 10.39  ? 197 LEU D CG  1 
ATOM   7977 C  CD1 . LEU D 1 197 ? 7.297   12.308  -32.397 1.00 14.86  ? 197 LEU D CD1 1 
ATOM   7978 C  CD2 . LEU D 1 197 ? 7.374   12.822  -34.852 1.00 14.25  ? 197 LEU D CD2 1 
ATOM   7979 N  N   . THR D 1 198 ? 10.376  8.348   -34.787 1.00 7.67   ? 198 THR D N   1 
ATOM   7980 C  CA  . THR D 1 198 ? 11.596  7.861   -35.432 1.00 7.82   ? 198 THR D CA  1 
ATOM   7981 C  C   . THR D 1 198 ? 12.012  8.701   -36.639 1.00 7.47   ? 198 THR D C   1 
ATOM   7982 O  O   . THR D 1 198 ? 13.001  8.404   -37.301 1.00 8.56   ? 198 THR D O   1 
ATOM   7983 C  CB  . THR D 1 198 ? 11.393  6.426   -35.904 1.00 7.12   ? 198 THR D CB  1 
ATOM   7984 O  OG1 . THR D 1 198 ? 10.449  6.451   -36.967 1.00 8.01   ? 198 THR D OG1 1 
ATOM   7985 C  CG2 . THR D 1 198 ? 10.983  5.437   -34.818 1.00 8.58   ? 198 THR D CG2 1 
ATOM   7986 N  N   . THR D 1 199 ? 11.257  9.809   -36.858 1.00 8.11   ? 199 THR D N   1 
ATOM   7987 C  CA  . THR D 1 199 ? 11.615  10.803  -37.857 1.00 7.63   ? 199 THR D CA  1 
ATOM   7988 C  C   . THR D 1 199 ? 11.767  12.153  -37.184 1.00 7.72   ? 199 THR D C   1 
ATOM   7989 O  O   . THR D 1 199 ? 11.138  12.348  -36.133 1.00 8.91   ? 199 THR D O   1 
ATOM   7990 C  CB  . THR D 1 199 ? 10.462  10.952  -38.872 1.00 8.94   ? 199 THR D CB  1 
ATOM   7991 O  OG1 . THR D 1 199 ? 9.250   11.308  -38.225 1.00 10.46  ? 199 THR D OG1 1 
ATOM   7992 C  CG2 . THR D 1 199 ? 10.069  9.609   -39.516 1.00 10.04  ? 199 THR D CG2 1 
ATOM   7993 N  N   . PRO D 1 200 ? 12.453  13.091  -37.826 1.00 7.65   ? 200 PRO D N   1 
ATOM   7994 C  CA  . PRO D 1 200 ? 12.324  14.458  -37.328 1.00 8.47   ? 200 PRO D CA  1 
ATOM   7995 C  C   . PRO D 1 200 ? 10.865  14.835  -37.151 1.00 8.87   ? 200 PRO D C   1 
ATOM   7996 O  O   . PRO D 1 200 ? 10.026  14.461  -37.988 1.00 9.30   ? 200 PRO D O   1 
ATOM   7997 C  CB  . PRO D 1 200 ? 13.020  15.233  -38.460 1.00 9.70   ? 200 PRO D CB  1 
ATOM   7998 C  CG  . PRO D 1 200 ? 14.090  14.306  -38.982 1.00 9.27   ? 200 PRO D CG  1 
ATOM   7999 C  CD  . PRO D 1 200 ? 13.329  12.972  -39.014 1.00 8.58   ? 200 PRO D CD  1 
ATOM   8000 N  N   . PRO D 1 201 ? 10.517  15.647  -36.112 1.00 9.85   ? 201 PRO D N   1 
ATOM   8001 C  CA  . PRO D 1 201 ? 11.482  16.225  -35.167 1.00 10.29  ? 201 PRO D CA  1 
ATOM   8002 C  C   . PRO D 1 201 ? 11.925  15.432  -33.947 1.00 10.44  ? 201 PRO D C   1 
ATOM   8003 O  O   . PRO D 1 201 ? 12.606  15.864  -33.033 1.00 10.78  ? 201 PRO D O   1 
ATOM   8004 C  CB  . PRO D 1 201 ? 10.712  17.445  -34.596 1.00 12.89  ? 201 PRO D CB  1 
ATOM   8005 C  CG  . PRO D 1 201 ? 9.508   17.613  -35.486 1.00 15.21  ? 201 PRO D CG  1 
ATOM   8006 C  CD  . PRO D 1 201 ? 9.166   16.221  -35.961 1.00 11.88  ? 201 PRO D CD  1 
ATOM   8007 N  N   . CYS D 1 202 ? 11.627  14.077  -33.978 1.00 9.42   ? 202 CYS D N   1 
ATOM   8008 C  CA  . CYS D 1 202 ? 12.199  13.082  -33.043 1.00 9.68   ? 202 CYS D CA  1 
ATOM   8009 C  C   . CYS D 1 202 ? 11.728  13.346  -31.612 1.00 9.17   ? 202 CYS D C   1 
ATOM   8010 O  O   . CYS D 1 202 ? 12.388  12.970  -30.641 1.00 10.23  ? 202 CYS D O   1 
ATOM   8011 C  CB  . CYS D 1 202 ? 13.734  13.032  -33.038 1.00 9.28   ? 202 CYS D CB  1 
ATOM   8012 S  SG  . CYS D 1 202 ? 14.541  12.669  -34.664 1.00 9.87   ? 202 CYS D SG  1 
ATOM   8013 N  N   . ASN D 1 203 ? 10.596  14.039  -31.412 1.00 8.79   ? 203 ASN D N   1 
ATOM   8014 C  CA  . ASN D 1 203 ? 10.178  14.366  -30.057 1.00 10.17  ? 203 ASN D CA  1 
ATOM   8015 C  C   . ASN D 1 203 ? 10.025  13.134  -29.180 1.00 8.91   ? 203 ASN D C   1 
ATOM   8016 O  O   . ASN D 1 203 ? 9.486   12.138  -29.701 1.00 9.52   ? 203 ASN D O   1 
ATOM   8017 C  CB  . ASN D 1 203 ? 8.817   15.076  -30.051 1.00 11.10  ? 203 ASN D CB  1 
ATOM   8018 C  CG  . ASN D 1 203 ? 8.932   16.293  -30.957 1.00 11.30  ? 203 ASN D CG  1 
ATOM   8019 O  OD1 . ASN D 1 203 ? 8.800   16.155  -32.153 1.00 11.88  ? 203 ASN D OD1 1 
ATOM   8020 N  ND2 . ASN D 1 203 ? 9.249   17.466  -30.399 1.00 13.09  ? 203 ASN D ND2 1 
ATOM   8021 N  N   . PRO D 1 204 ? 10.506  13.135  -27.923 1.00 10.16  ? 204 PRO D N   1 
ATOM   8022 C  CA  . PRO D 1 204 ? 10.400  11.990  -27.032 1.00 10.76  ? 204 PRO D CA  1 
ATOM   8023 C  C   . PRO D 1 204 ? 9.032   11.888  -26.354 1.00 10.75  ? 204 PRO D C   1 
ATOM   8024 O  O   . PRO D 1 204 ? 8.933   11.878  -25.124 1.00 12.53  ? 204 PRO D O   1 
ATOM   8025 C  CB  . PRO D 1 204 ? 11.532  12.190  -26.020 1.00 11.89  ? 204 PRO D CB  1 
ATOM   8026 C  CG  . PRO D 1 204 ? 11.554  13.720  -25.905 1.00 12.11  ? 204 PRO D CG  1 
ATOM   8027 C  CD  . PRO D 1 204 ? 11.289  14.240  -27.320 1.00 11.75  ? 204 PRO D CD  1 
ATOM   8028 N  N   . THR D 1 205 ? 7.991   11.752  -27.185 1.00 10.06  ? 205 THR D N   1 
ATOM   8029 C  CA  . THR D 1 205 ? 6.626   11.885  -26.739 1.00 9.12   ? 205 THR D CA  1 
ATOM   8030 C  C   . THR D 1 205 ? 5.803   10.684  -27.109 1.00 9.90   ? 205 THR D C   1 
ATOM   8031 O  O   . THR D 1 205 ? 4.601   10.779  -27.150 1.00 10.00  ? 205 THR D O   1 
ATOM   8032 C  CB  . THR D 1 205 ? 6.023   13.160  -27.343 1.00 9.30   ? 205 THR D CB  1 
ATOM   8033 O  OG1 . THR D 1 205 ? 6.173   13.030  -28.765 1.00 10.59  ? 205 THR D OG1 1 
ATOM   8034 C  CG2 . THR D 1 205 ? 6.727   14.422  -26.845 1.00 12.55  ? 205 THR D CG2 1 
ATOM   8035 N  N   . VAL D 1 206 ? 6.482   9.569   -27.468 1.00 11.10  ? 206 VAL D N   1 
ATOM   8036 C  CA  . VAL D 1 206 ? 5.708   8.417   -28.026 1.00 9.24   ? 206 VAL D CA  1 
ATOM   8037 C  C   . VAL D 1 206 ? 5.733   7.216   -27.108 1.00 8.56   ? 206 VAL D C   1 
ATOM   8038 O  O   . VAL D 1 206 ? 6.826   6.778   -26.736 1.00 10.32  ? 206 VAL D O   1 
ATOM   8039 C  CB  . VAL D 1 206 ? 6.288   7.935   -29.386 1.00 7.98   ? 206 VAL D CB  1 
ATOM   8040 C  CG1 . VAL D 1 206 ? 5.558   6.715   -29.926 1.00 9.40   ? 206 VAL D CG1 1 
ATOM   8041 C  CG2 . VAL D 1 206 ? 6.241   9.041   -30.449 1.00 9.37   ? 206 VAL D CG2 1 
ATOM   8042 N  N   . LEU D 1 207 ? 4.537   6.745   -26.736 1.00 9.73   ? 207 LEU D N   1 
ATOM   8043 C  CA  . LEU D 1 207 ? 4.450   5.469   -26.044 1.00 10.06  ? 207 LEU D CA  1 
ATOM   8044 C  C   . LEU D 1 207 ? 4.335   4.397   -27.125 1.00 8.22   ? 207 LEU D C   1 
ATOM   8045 O  O   . LEU D 1 207 ? 3.417   4.411   -27.918 1.00 9.36   ? 207 LEU D O   1 
ATOM   8046 C  CB  . LEU D 1 207 ? 3.198   5.448   -25.163 1.00 11.23  ? 207 LEU D CB  1 
ATOM   8047 C  CG  . LEU D 1 207 ? 3.097   4.217   -24.285 1.00 13.11  ? 207 LEU D CG  1 
ATOM   8048 C  CD1 . LEU D 1 207 ? 4.178   4.234   -23.226 1.00 14.78  ? 207 LEU D CD1 1 
ATOM   8049 C  CD2 . LEU D 1 207 ? 1.696   4.051   -23.731 1.00 19.38  ? 207 LEU D CD2 1 
ATOM   8050 N  N   . TRP D 1 208 ? 5.404   3.549   -27.233 1.00 8.45   ? 208 TRP D N   1 
ATOM   8051 C  CA  . TRP D 1 208 ? 5.494   2.506   -28.265 1.00 8.74   ? 208 TRP D CA  1 
ATOM   8052 C  C   . TRP D 1 208 ? 4.841   1.225   -27.796 1.00 7.57   ? 208 TRP D C   1 
ATOM   8053 O  O   . TRP D 1 208 ? 5.147   0.762   -26.705 1.00 8.99   ? 208 TRP D O   1 
ATOM   8054 C  CB  . TRP D 1 208 ? 6.977   2.232   -28.654 1.00 8.99   ? 208 TRP D CB  1 
ATOM   8055 C  CG  . TRP D 1 208 ? 7.535   3.292   -29.562 1.00 6.65   ? 208 TRP D CG  1 
ATOM   8056 C  CD1 . TRP D 1 208 ? 8.143   4.483   -29.166 1.00 9.65   ? 208 TRP D CD1 1 
ATOM   8057 C  CD2 . TRP D 1 208 ? 7.317   3.351   -30.975 1.00 7.05   ? 208 TRP D CD2 1 
ATOM   8058 N  NE1 . TRP D 1 208 ? 8.358   5.196   -30.323 1.00 7.77   ? 208 TRP D NE1 1 
ATOM   8059 C  CE2 . TRP D 1 208 ? 7.839   4.572   -31.443 1.00 7.35   ? 208 TRP D CE2 1 
ATOM   8060 C  CE3 . TRP D 1 208 ? 6.705   2.505   -31.895 1.00 8.92   ? 208 TRP D CE3 1 
ATOM   8061 C  CZ2 . TRP D 1 208 ? 7.795   4.944   -32.804 1.00 8.21   ? 208 TRP D CZ2 1 
ATOM   8062 C  CZ3 . TRP D 1 208 ? 6.728   2.801   -33.262 1.00 8.81   ? 208 TRP D CZ3 1 
ATOM   8063 C  CH2 . TRP D 1 208 ? 7.216   4.056   -33.703 1.00 9.00   ? 208 TRP D CH2 1 
ATOM   8064 N  N   . THR D 1 209 ? 4.127   0.614   -28.729 1.00 8.71   ? 209 THR D N   1 
ATOM   8065 C  CA  . THR D 1 209 ? 3.622   -0.781  -28.562 1.00 7.62   ? 209 THR D CA  1 
ATOM   8066 C  C   . THR D 1 209 ? 4.014   -1.498  -29.815 1.00 7.72   ? 209 THR D C   1 
ATOM   8067 O  O   . THR D 1 209 ? 3.540   -1.180  -30.881 1.00 10.05  ? 209 THR D O   1 
ATOM   8068 C  CB  . THR D 1 209 ? 2.098   -0.837  -28.384 1.00 9.01   ? 209 THR D CB  1 
ATOM   8069 O  OG1 . THR D 1 209 ? 1.762   -0.079  -27.209 1.00 9.56   ? 209 THR D OG1 1 
ATOM   8070 C  CG2 . THR D 1 209 ? 1.547   -2.251  -28.203 1.00 8.58   ? 209 THR D CG2 1 
ATOM   8071 N  N   . VAL D 1 210 ? 4.967   -2.458  -29.698 1.00 8.20   ? 210 VAL D N   1 
ATOM   8072 C  CA  . VAL D 1 210 ? 5.409   -3.271  -30.841 1.00 8.40   ? 210 VAL D CA  1 
ATOM   8073 C  C   . VAL D 1 210 ? 4.814   -4.660  -30.633 1.00 7.53   ? 210 VAL D C   1 
ATOM   8074 O  O   . VAL D 1 210 ? 5.113   -5.276  -29.614 1.00 8.85   ? 210 VAL D O   1 
ATOM   8075 C  CB  . VAL D 1 210 ? 6.946   -3.374  -30.922 1.00 7.83   ? 210 VAL D CB  1 
ATOM   8076 C  CG1 . VAL D 1 210 ? 7.397   -4.134  -32.146 1.00 10.46  ? 210 VAL D CG1 1 
ATOM   8077 C  CG2 . VAL D 1 210 ? 7.561   -1.955  -30.886 1.00 10.31  ? 210 VAL D CG2 1 
ATOM   8078 N  N   . PHE D 1 211 ? 3.926   -5.126  -31.548 1.00 8.37   ? 211 PHE D N   1 
ATOM   8079 C  CA  . PHE D 1 211 ? 3.388   -6.482  -31.340 1.00 9.57   ? 211 PHE D CA  1 
ATOM   8080 C  C   . PHE D 1 211 ? 4.483   -7.535  -31.428 1.00 10.23  ? 211 PHE D C   1 
ATOM   8081 O  O   . PHE D 1 211 ? 5.417   -7.435  -32.204 1.00 8.65   ? 211 PHE D O   1 
ATOM   8082 C  CB  . PHE D 1 211 ? 2.225   -6.735  -32.288 1.00 9.55   ? 211 PHE D CB  1 
ATOM   8083 C  CG  . PHE D 1 211 ? 1.082   -5.774  -31.991 1.00 8.67   ? 211 PHE D CG  1 
ATOM   8084 C  CD1 . PHE D 1 211 ? 0.328   -5.936  -30.843 1.00 10.68  ? 211 PHE D CD1 1 
ATOM   8085 C  CD2 . PHE D 1 211 ? 0.752   -4.724  -32.874 1.00 9.74   ? 211 PHE D CD2 1 
ATOM   8086 C  CE1 . PHE D 1 211 ? -0.727  -5.084  -30.548 1.00 10.67  ? 211 PHE D CE1 1 
ATOM   8087 C  CE2 . PHE D 1 211 ? -0.349  -3.910  -32.612 1.00 10.53  ? 211 PHE D CE2 1 
ATOM   8088 C  CZ  . PHE D 1 211 ? -1.082  -4.076  -31.443 1.00 11.21  ? 211 PHE D CZ  1 
ATOM   8089 N  N   . ARG D 1 212 ? 4.301   -8.597  -30.605 1.00 10.63  ? 212 ARG D N   1 
ATOM   8090 C  CA  . ARG D 1 212 ? 5.282   -9.677  -30.533 1.00 10.79  ? 212 ARG D CA  1 
ATOM   8091 C  C   . ARG D 1 212 ? 5.370   -10.423 -31.868 1.00 11.42  ? 212 ARG D C   1 
ATOM   8092 O  O   . ARG D 1 212 ? 6.470   -10.752 -32.326 1.00 11.19  ? 212 ARG D O   1 
ATOM   8093 C  CB  . ARG D 1 212 ? 4.909   -10.657 -29.418 1.00 10.00  ? 212 ARG D CB  1 
ATOM   8094 C  CG  . ARG D 1 212 ? 5.921   -11.792 -29.329 1.00 13.22  ? 212 ARG D CG  1 
ATOM   8095 C  CD  . ARG D 1 212 ? 5.448   -12.822 -28.319 1.00 13.04  ? 212 ARG D CD  1 
ATOM   8096 N  NE  . ARG D 1 212 ? 6.535   -13.771 -28.010 1.00 15.12  ? 212 ARG D NE  1 
ATOM   8097 C  CZ  . ARG D 1 212 ? 6.440   -14.738 -27.101 1.00 18.58  ? 212 ARG D CZ  1 
ATOM   8098 N  NH1 . ARG D 1 212 ? 5.275   -14.964 -26.540 1.00 16.65  ? 212 ARG D NH1 1 
ATOM   8099 N  NH2 . ARG D 1 212 ? 7.503   -15.479 -26.796 1.00 23.32  ? 212 ARG D NH2 1 
ATOM   8100 N  N   . ASN D 1 213 ? 4.213   -10.652 -32.508 1.00 11.55  ? 213 ASN D N   1 
ATOM   8101 C  CA  . ASN D 1 213 ? 4.191   -11.500 -33.701 1.00 9.54   ? 213 ASN D CA  1 
ATOM   8102 C  C   . ASN D 1 213 ? 4.191   -10.625 -34.979 1.00 10.26  ? 213 ASN D C   1 
ATOM   8103 O  O   . ASN D 1 213 ? 3.501   -9.599  -35.034 1.00 10.17  ? 213 ASN D O   1 
ATOM   8104 C  CB  . ASN D 1 213 ? 2.971   -12.412 -33.706 1.00 12.54  ? 213 ASN D CB  1 
ATOM   8105 C  CG  . ASN D 1 213 ? 3.044   -13.391 -32.552 1.00 13.45  ? 213 ASN D CG  1 
ATOM   8106 O  OD1 . ASN D 1 213 ? 4.062   -14.098 -32.399 1.00 22.67  ? 213 ASN D OD1 1 
ATOM   8107 N  ND2 . ASN D 1 213 ? 2.013   -13.398 -31.744 1.00 18.38  ? 213 ASN D ND2 1 
ATOM   8108 N  N   . PRO D 1 214 ? 4.934   -10.988 -36.027 1.00 10.08  ? 214 PRO D N   1 
ATOM   8109 C  CA  . PRO D 1 214 ? 4.891   -10.316 -37.305 1.00 8.81   ? 214 PRO D CA  1 
ATOM   8110 C  C   . PRO D 1 214 ? 3.702   -10.749 -38.153 1.00 8.43   ? 214 PRO D C   1 
ATOM   8111 O  O   . PRO D 1 214 ? 3.050   -11.794 -37.866 1.00 11.04  ? 214 PRO D O   1 
ATOM   8112 C  CB  . PRO D 1 214 ? 6.243   -10.701 -37.939 1.00 10.71  ? 214 PRO D CB  1 
ATOM   8113 C  CG  . PRO D 1 214 ? 6.360   -12.198 -37.511 1.00 13.03  ? 214 PRO D CG  1 
ATOM   8114 C  CD  . PRO D 1 214 ? 5.809   -12.206 -36.086 1.00 12.80  ? 214 PRO D CD  1 
ATOM   8115 N  N   . VAL D 1 215 ? 3.396   -9.937  -39.192 1.00 8.81   ? 215 VAL D N   1 
ATOM   8116 C  CA  . VAL D 1 215 ? 2.575   -10.347 -40.307 1.00 8.64   ? 215 VAL D CA  1 
ATOM   8117 C  C   . VAL D 1 215 ? 3.453   -10.622 -41.513 1.00 8.26   ? 215 VAL D C   1 
ATOM   8118 O  O   . VAL D 1 215 ? 4.650   -10.374 -41.476 1.00 8.87   ? 215 VAL D O   1 
ATOM   8119 C  CB  . VAL D 1 215 ? 1.554   -9.266  -40.674 1.00 9.32   ? 215 VAL D CB  1 
ATOM   8120 C  CG1 . VAL D 1 215 ? 0.569   -8.994  -39.532 1.00 10.93  ? 215 VAL D CG1 1 
ATOM   8121 C  CG2 . VAL D 1 215 ? 2.225   -7.977  -41.198 1.00 10.73  ? 215 VAL D CG2 1 
ATOM   8122 N  N   . GLN D 1 216 ? 2.875   -11.266 -42.565 1.00 9.17   ? 216 GLN D N   1 
ATOM   8123 C  CA  . GLN D 1 216 ? 3.635   -11.525 -43.756 1.00 8.80   ? 216 GLN D CA  1 
ATOM   8124 C  C   . GLN D 1 216 ? 3.003   -10.759 -44.920 1.00 8.75   ? 216 GLN D C   1 
ATOM   8125 O  O   . GLN D 1 216 ? 1.787   -10.646 -45.007 1.00 10.27  ? 216 GLN D O   1 
ATOM   8126 C  CB  . GLN D 1 216 ? 3.584   -13.047 -44.074 1.00 10.90  ? 216 GLN D CB  1 
ATOM   8127 C  CG  . GLN D 1 216 ? 4.257   -13.976 -43.066 1.00 14.25  ? 216 GLN D CG  1 
ATOM   8128 C  CD  . GLN D 1 216 ? 4.105   -15.447 -43.502 1.00 14.05  ? 216 GLN D CD  1 
ATOM   8129 O  OE1 . GLN D 1 216 ? 3.592   -15.821 -44.597 1.00 15.79  ? 216 GLN D OE1 1 
ATOM   8130 N  NE2 . GLN D 1 216 ? 4.530   -16.304 -42.587 1.00 29.12  ? 216 GLN D NE2 1 
ATOM   8131 N  N   . ILE D 1 217 ? 3.862   -10.284 -45.820 1.00 8.17   ? 217 ILE D N   1 
ATOM   8132 C  CA  . ILE D 1 217 ? 3.475   -9.854  -47.160 1.00 8.05   ? 217 ILE D CA  1 
ATOM   8133 C  C   . ILE D 1 217 ? 4.398   -10.559 -48.157 1.00 8.98   ? 217 ILE D C   1 
ATOM   8134 O  O   . ILE D 1 217 ? 5.488   -11.003 -47.747 1.00 9.22   ? 217 ILE D O   1 
ATOM   8135 C  CB  . ILE D 1 217 ? 3.512   -8.306  -47.286 1.00 8.61   ? 217 ILE D CB  1 
ATOM   8136 C  CG1 . ILE D 1 217 ? 4.958   -7.764  -47.326 1.00 8.63   ? 217 ILE D CG1 1 
ATOM   8137 C  CG2 . ILE D 1 217 ? 2.635   -7.599  -46.268 1.00 10.63  ? 217 ILE D CG2 1 
ATOM   8138 C  CD1 . ILE D 1 217 ? 5.009   -6.198  -47.439 1.00 11.25  ? 217 ILE D CD1 1 
ATOM   8139 N  N   . SER D 1 218 ? 4.040   -10.581 -49.466 1.00 8.12   ? 218 SER D N   1 
ATOM   8140 C  CA  . SER D 1 218 ? 4.836   -11.410 -50.373 1.00 8.99   ? 218 SER D CA  1 
ATOM   8141 C  C   . SER D 1 218 ? 6.081   -10.652 -50.860 1.00 7.64   ? 218 SER D C   1 
ATOM   8142 O  O   . SER D 1 218 ? 6.146   -9.399  -50.722 1.00 11.05  ? 218 SER D O   1 
ATOM   8143 C  CB  . SER D 1 218 ? 4.016   -11.873 -51.572 1.00 11.41  ? 218 SER D CB  1 
ATOM   8144 O  OG  . SER D 1 218 ? 3.649   -10.708 -52.339 1.00 12.36  ? 218 SER D OG  1 
ATOM   8145 N  N   . GLN D 1 219 ? 6.980   -11.358 -51.458 1.00 9.26   ? 219 GLN D N   1 
ATOM   8146 C  CA  . GLN D 1 219 ? 8.144   -10.792 -52.120 1.00 10.39  ? 219 GLN D CA  1 
ATOM   8147 C  C   . GLN D 1 219 ? 7.696   -9.762  -53.183 1.00 10.21  ? 219 GLN D C   1 
ATOM   8148 O  O   . GLN D 1 219 ? 8.285   -8.664  -53.266 1.00 10.47  ? 219 GLN D O   1 
ATOM   8149 C  CB  . GLN D 1 219 ? 8.920   -11.884 -52.830 1.00 12.93  ? 219 GLN D CB  1 
ATOM   8150 C  CG  . GLN D 1 219 ? 10.244  -11.413 -53.456 1.00 18.92  ? 219 GLN D CG  1 
ATOM   8151 C  CD  . GLN D 1 219 ? 10.160  -10.781 -54.833 1.00 18.63  ? 219 GLN D CD  1 
ATOM   8152 O  OE1 . GLN D 1 219 ? 9.239   -11.068 -55.599 1.00 31.40  ? 219 GLN D OE1 1 
ATOM   8153 N  NE2 . GLN D 1 219 ? 11.096  -9.862  -55.133 1.00 23.25  ? 219 GLN D NE2 1 
ATOM   8154 N  N   . GLU D 1 220 ? 6.637   -10.068 -53.936 1.00 10.13  ? 220 GLU D N   1 
ATOM   8155 C  CA  . GLU D 1 220 ? 6.116   -9.173  -54.964 1.00 10.03  ? 220 GLU D CA  1 
ATOM   8156 C  C   . GLU D 1 220 ? 5.576   -7.905  -54.324 1.00 10.16  ? 220 GLU D C   1 
ATOM   8157 O  O   . GLU D 1 220 ? 5.812   -6.829  -54.873 1.00 9.94   ? 220 GLU D O   1 
ATOM   8158 C  CB  . GLU D 1 220 ? 5.081   -9.854  -55.856 1.00 10.39  ? 220 GLU D CB  1 
ATOM   8159 C  CG  . GLU D 1 220 ? 5.702   -10.978 -56.674 1.00 12.50  ? 220 GLU D CG  1 
ATOM   8160 C  CD  . GLU D 1 220 ? 5.853   -12.327 -56.019 1.00 13.79  ? 220 GLU D CD  1 
ATOM   8161 O  OE1 . GLU D 1 220 ? 5.535   -12.466 -54.832 1.00 16.11  ? 220 GLU D OE1 1 
ATOM   8162 O  OE2 . GLU D 1 220 ? 6.288   -13.229 -56.738 1.00 21.10  ? 220 GLU D OE2 1 
ATOM   8163 N  N   . GLN D 1 221 ? 4.857   -8.011  -53.190 1.00 8.55   ? 221 GLN D N   1 
ATOM   8164 C  CA  . GLN D 1 221 ? 4.314   -6.833  -52.537 1.00 9.67   ? 221 GLN D CA  1 
ATOM   8165 C  C   . GLN D 1 221 ? 5.504   -5.998  -52.093 1.00 9.38   ? 221 GLN D C   1 
ATOM   8166 O  O   . GLN D 1 221 ? 5.440   -4.736  -52.187 1.00 10.38  ? 221 GLN D O   1 
ATOM   8167 C  CB  . GLN D 1 221 ? 3.447   -7.265  -51.355 1.00 9.17   ? 221 GLN D CB  1 
ATOM   8168 C  CG  . GLN D 1 221 ? 2.112   -7.773  -51.823 1.00 9.58   ? 221 GLN D CG  1 
ATOM   8169 C  CD  . GLN D 1 221 ? 1.210   -8.190  -50.708 1.00 10.62  ? 221 GLN D CD  1 
ATOM   8170 O  OE1 . GLN D 1 221 ? 1.524   -9.121  -49.938 1.00 11.24  ? 221 GLN D OE1 1 
ATOM   8171 N  NE2 . GLN D 1 221 ? 0.088   -7.516  -50.537 1.00 12.01  ? 221 GLN D NE2 1 
ATOM   8172 N  N   . LEU D 1 222 ? 6.518   -6.568  -51.398 1.00 9.88   ? 222 LEU D N   1 
ATOM   8173 C  CA  . LEU D 1 222 ? 7.696   -5.810  -50.961 1.00 10.35  ? 222 LEU D CA  1 
ATOM   8174 C  C   . LEU D 1 222 ? 8.419   -5.142  -52.127 1.00 9.40   ? 222 LEU D C   1 
ATOM   8175 O  O   . LEU D 1 222 ? 8.770   -3.953  -52.015 1.00 10.84  ? 222 LEU D O   1 
ATOM   8176 C  CB  . LEU D 1 222 ? 8.699   -6.699  -50.206 1.00 9.93   ? 222 LEU D CB  1 
ATOM   8177 C  CG  . LEU D 1 222 ? 8.297   -6.968  -48.765 1.00 11.83  ? 222 LEU D CG  1 
ATOM   8178 C  CD1 . LEU D 1 222 ? 8.926   -8.306  -48.293 1.00 12.75  ? 222 LEU D CD1 1 
ATOM   8179 C  CD2 . LEU D 1 222 ? 8.648   -5.746  -47.910 1.00 11.98  ? 222 LEU D CD2 1 
ATOM   8180 N  N   . LEU D 1 223 ? 8.642   -5.825  -53.221 1.00 10.59  ? 223 LEU D N   1 
ATOM   8181 C  CA  . LEU D 1 223 ? 9.309   -5.197  -54.342 1.00 9.28   ? 223 LEU D CA  1 
ATOM   8182 C  C   . LEU D 1 223 ? 8.454   -4.062  -54.905 1.00 10.44  ? 223 LEU D C   1 
ATOM   8183 O  O   . LEU D 1 223 ? 9.003   -2.977  -55.215 1.00 10.88  ? 223 LEU D O   1 
ATOM   8184 C  CB  . LEU D 1 223 ? 9.564   -6.221  -55.433 1.00 9.87   ? 223 LEU D CB  1 
ATOM   8185 C  CG  . LEU D 1 223 ? 10.302  -5.659  -56.661 1.00 11.09  ? 223 LEU D CG  1 
ATOM   8186 C  CD1 . LEU D 1 223 ? 11.715  -5.120  -56.351 1.00 16.61  ? 223 LEU D CD1 1 
ATOM   8187 C  CD2 . LEU D 1 223 ? 10.402  -6.756  -57.720 1.00 12.93  ? 223 LEU D CD2 1 
ATOM   8188 N  N   . ALA D 1 224 ? 7.118   -4.192  -55.011 1.00 10.76  ? 224 ALA D N   1 
ATOM   8189 C  CA  . ALA D 1 224 ? 6.279   -3.079  -55.460 1.00 11.39  ? 224 ALA D CA  1 
ATOM   8190 C  C   . ALA D 1 224 ? 6.392   -1.897  -54.497 1.00 9.72   ? 224 ALA D C   1 
ATOM   8191 O  O   . ALA D 1 224 ? 6.595   -0.736  -54.932 1.00 11.89  ? 224 ALA D O   1 
ATOM   8192 C  CB  . ALA D 1 224 ? 4.841   -3.514  -55.611 1.00 13.79  ? 224 ALA D CB  1 
ATOM   8193 N  N   . LEU D 1 225 ? 6.333   -2.161  -53.157 1.00 9.33   ? 225 LEU D N   1 
ATOM   8194 C  CA  . LEU D 1 225 ? 6.403   -1.090  -52.188 1.00 9.06   ? 225 LEU D CA  1 
ATOM   8195 C  C   . LEU D 1 225 ? 7.736   -0.356  -52.384 1.00 8.01   ? 225 LEU D C   1 
ATOM   8196 O  O   . LEU D 1 225 ? 7.843   0.884   -52.337 1.00 12.18  ? 225 LEU D O   1 
ATOM   8197 C  CB  . LEU D 1 225 ? 6.317   -1.665  -50.790 1.00 10.69  ? 225 LEU D CB  1 
ATOM   8198 C  CG  . LEU D 1 225 ? 6.491   -0.713  -49.628 1.00 11.05  ? 225 LEU D CG  1 
ATOM   8199 C  CD1 . LEU D 1 225 ? 5.462   0.435   -49.666 1.00 12.13  ? 225 LEU D CD1 1 
ATOM   8200 C  CD2 . LEU D 1 225 ? 6.430   -1.413  -48.292 1.00 11.98  ? 225 LEU D CD2 1 
ATOM   8201 N  N   . GLU D 1 226 ? 8.830   -1.116  -52.553 1.00 10.16  ? 226 GLU D N   1 
ATOM   8202 C  CA  . GLU D 1 226 ? 10.209  -0.629  -52.558 1.00 10.27  ? 226 GLU D CA  1 
ATOM   8203 C  C   . GLU D 1 226 ? 10.527  0.126   -53.854 1.00 10.42  ? 226 GLU D C   1 
ATOM   8204 O  O   . GLU D 1 226 ? 11.527  0.856   -53.885 1.00 13.87  ? 226 GLU D O   1 
ATOM   8205 C  CB  . GLU D 1 226 ? 11.195  -1.805  -52.454 1.00 10.28  ? 226 GLU D CB  1 
ATOM   8206 C  CG  . GLU D 1 226 ? 11.174  -2.451  -51.073 1.00 8.72   ? 226 GLU D CG  1 
ATOM   8207 C  CD  . GLU D 1 226 ? 11.616  -3.902  -51.077 1.00 8.74   ? 226 GLU D CD  1 
ATOM   8208 O  OE1 . GLU D 1 226 ? 12.043  -4.405  -52.184 1.00 13.34  ? 226 GLU D OE1 1 
ATOM   8209 O  OE2 . GLU D 1 226 ? 11.606  -4.530  -49.962 1.00 12.41  ? 226 GLU D OE2 1 
ATOM   8210 N  N   . THR D 1 227 ? 9.685   0.005   -54.885 1.00 9.80   ? 227 THR D N   1 
ATOM   8211 C  CA  . THR D 1 227 ? 9.972   0.623   -56.170 1.00 10.50  ? 227 THR D CA  1 
ATOM   8212 C  C   . THR D 1 227 ? 8.859   1.602   -56.599 1.00 10.07  ? 227 THR D C   1 
ATOM   8213 O  O   . THR D 1 227 ? 8.939   2.148   -57.689 1.00 13.97  ? 227 THR D O   1 
ATOM   8214 C  CB  . THR D 1 227 ? 10.186  -0.444  -57.259 1.00 11.95  ? 227 THR D CB  1 
ATOM   8215 O  OG1 . THR D 1 227 ? 8.979   -1.179  -57.430 1.00 11.70  ? 227 THR D OG1 1 
ATOM   8216 C  CG2 . THR D 1 227 ? 11.392  -1.331  -57.012 1.00 13.29  ? 227 THR D CG2 1 
ATOM   8217 N  N   . ALA D 1 228 ? 7.805   1.784   -55.778 1.00 10.29  ? 228 ALA D N   1 
ATOM   8218 C  CA  . ALA D 1 228 ? 6.635   2.562   -56.199 1.00 10.58  ? 228 ALA D CA  1 
ATOM   8219 C  C   . ALA D 1 228 ? 6.788   4.087   -55.991 1.00 12.64  ? 228 ALA D C   1 
ATOM   8220 O  O   . ALA D 1 228 ? 6.042   4.833   -56.647 1.00 14.63  ? 228 ALA D O   1 
ATOM   8221 C  CB  . ALA D 1 228 ? 5.433   2.066   -55.441 1.00 15.01  ? 228 ALA D CB  1 
ATOM   8222 N  N   . LEU D 1 229 ? 7.590   4.491   -54.991 1.00 10.00  ? 229 LEU D N   1 
ATOM   8223 C  CA  . LEU D 1 229 ? 7.492   5.858   -54.495 1.00 11.56  ? 229 LEU D CA  1 
ATOM   8224 C  C   . LEU D 1 229 ? 8.820   6.598   -54.636 1.00 9.83   ? 229 LEU D C   1 
ATOM   8225 O  O   . LEU D 1 229 ? 9.918   6.035   -54.534 1.00 12.19  ? 229 LEU D O   1 
ATOM   8226 C  CB  . LEU D 1 229 ? 7.073   5.760   -53.020 1.00 10.26  ? 229 LEU D CB  1 
ATOM   8227 C  CG  . LEU D 1 229 ? 5.755   5.028   -52.744 1.00 12.78  ? 229 LEU D CG  1 
ATOM   8228 C  CD1 . LEU D 1 229 ? 5.528   4.752   -51.269 1.00 16.16  ? 229 LEU D CD1 1 
ATOM   8229 C  CD2 . LEU D 1 229 ? 4.563   5.758   -53.304 1.00 17.60  ? 229 LEU D CD2 1 
ATOM   8230 N  N   . TYR D 1 230 ? 8.684   7.935   -54.730 1.00 12.21  ? 230 TYR D N   1 
ATOM   8231 C  CA  . TYR D 1 230 ? 9.750   8.914   -54.748 1.00 13.65  ? 230 TYR D CA  1 
ATOM   8232 C  C   . TYR D 1 230 ? 9.560   9.882   -53.584 1.00 11.40  ? 230 TYR D C   1 
ATOM   8233 O  O   . TYR D 1 230 ? 8.432   10.264  -53.227 1.00 13.24  ? 230 TYR D O   1 
ATOM   8234 C  CB  . TYR D 1 230 ? 9.825   9.637   -56.107 1.00 13.01  ? 230 TYR D CB  1 
ATOM   8235 C  CG  . TYR D 1 230 ? 10.328  8.693   -57.168 1.00 15.44  ? 230 TYR D CG  1 
ATOM   8236 C  CD1 . TYR D 1 230 ? 9.516   7.652   -57.600 1.00 17.73  ? 230 TYR D CD1 1 
ATOM   8237 C  CD2 . TYR D 1 230 ? 11.674  8.636   -57.503 1.00 16.60  ? 230 TYR D CD2 1 
ATOM   8238 C  CE1 . TYR D 1 230 ? 9.960   6.676   -58.462 1.00 19.65  ? 230 TYR D CE1 1 
ATOM   8239 C  CE2 . TYR D 1 230 ? 12.142  7.674   -58.387 1.00 20.09  ? 230 TYR D CE2 1 
ATOM   8240 C  CZ  . TYR D 1 230 ? 11.305  6.650   -58.819 1.00 21.54  ? 230 TYR D CZ  1 
ATOM   8241 O  OH  . TYR D 1 230 ? 11.790  5.711   -59.696 1.00 23.27  ? 230 TYR D OH  1 
ATOM   8242 N  N   . CYS D 1 231 ? 10.691  10.380  -53.090 1.00 13.63  ? 231 CYS D N   1 
ATOM   8243 C  CA  . CYS D 1 231 ? 10.704  11.434  -52.093 1.00 13.40  ? 231 CYS D CA  1 
ATOM   8244 C  C   . CYS D 1 231 ? 10.507  12.808  -52.706 1.00 13.31  ? 231 CYS D C   1 
ATOM   8245 O  O   . CYS D 1 231 ? 10.279  13.759  -51.965 1.00 15.99  ? 231 CYS D O   1 
ATOM   8246 C  CB  . CYS D 1 231 ? 12.044  11.492  -51.347 1.00 14.20  ? 231 CYS D CB  1 
ATOM   8247 S  SG  . CYS D 1 231 ? 12.533  9.957   -50.511 1.00 15.67  ? 231 CYS D SG  1 
ATOM   8248 N  N   . THR D 1 232 ? 10.640  12.916  -54.026 1.00 13.73  ? 232 THR D N   1 
ATOM   8249 C  CA  . THR D 1 232 ? 10.778  14.215  -54.676 1.00 13.85  ? 232 THR D CA  1 
ATOM   8250 C  C   . THR D 1 232 ? 9.506   14.505  -55.482 1.00 14.03  ? 232 THR D C   1 
ATOM   8251 O  O   . THR D 1 232 ? 8.751   13.619  -55.780 1.00 13.06  ? 232 THR D O   1 
ATOM   8252 C  CB  . THR D 1 232 ? 12.004  14.207  -55.581 1.00 13.62  ? 232 THR D CB  1 
ATOM   8253 O  OG1 . THR D 1 232 ? 12.059  12.934  -56.222 1.00 13.74  ? 232 THR D OG1 1 
ATOM   8254 C  CG2 . THR D 1 232 ? 13.271  14.431  -54.793 1.00 15.10  ? 232 THR D CG2 1 
ATOM   8255 N  N   A HIS D 1 233 ? 9.242   15.783  -55.743 0.50 15.77  ? 233 HIS D N   1 
ATOM   8256 N  N   B HIS D 1 233 ? 9.303   15.782  -55.811 0.50 16.28  ? 233 HIS D N   1 
ATOM   8257 C  CA  A HIS D 1 233 ? 8.125   16.202  -56.565 0.50 16.07  ? 233 HIS D CA  1 
ATOM   8258 C  CA  B HIS D 1 233 ? 8.208   16.231  -56.654 0.50 15.72  ? 233 HIS D CA  1 
ATOM   8259 C  C   A HIS D 1 233 ? 8.403   15.686  -57.971 0.50 16.55  ? 233 HIS D C   1 
ATOM   8260 C  C   B HIS D 1 233 ? 8.436   15.663  -58.046 0.50 16.49  ? 233 HIS D C   1 
ATOM   8261 O  O   A HIS D 1 233 ? 9.569   15.534  -58.363 0.50 15.14  ? 233 HIS D O   1 
ATOM   8262 O  O   B HIS D 1 233 ? 9.587   15.484  -58.466 0.50 15.63  ? 233 HIS D O   1 
ATOM   8263 C  CB  A HIS D 1 233 ? 7.988   17.739  -56.545 0.50 21.88  ? 233 HIS D CB  1 
ATOM   8264 C  CB  B HIS D 1 233 ? 8.174   17.773  -56.686 0.50 20.13  ? 233 HIS D CB  1 
ATOM   8265 C  CG  A HIS D 1 233 ? 7.644   18.364  -55.232 0.50 21.22  ? 233 HIS D CG  1 
ATOM   8266 C  CG  B HIS D 1 233 ? 7.012   18.373  -57.412 0.50 21.39  ? 233 HIS D CG  1 
ATOM   8267 N  ND1 A HIS D 1 233 ? 8.358   19.450  -54.729 0.50 27.01  ? 233 HIS D ND1 1 
ATOM   8268 N  ND1 B HIS D 1 233 ? 7.012   18.567  -58.795 0.50 21.05  ? 233 HIS D ND1 1 
ATOM   8269 C  CD2 A HIS D 1 233 ? 6.604   18.177  -54.388 0.50 20.96  ? 233 HIS D CD2 1 
ATOM   8270 C  CD2 B HIS D 1 233 ? 5.826   18.866  -56.965 0.50 23.68  ? 233 HIS D CD2 1 
ATOM   8271 C  CE1 A HIS D 1 233 ? 7.819   19.838  -53.598 0.50 28.02  ? 233 HIS D CE1 1 
ATOM   8272 C  CE1 B HIS D 1 233 ? 5.868   19.106  -59.168 0.50 25.24  ? 233 HIS D CE1 1 
ATOM   8273 N  NE2 A HIS D 1 233 ? 6.760   19.060  -53.357 0.50 27.31  ? 233 HIS D NE2 1 
ATOM   8274 N  NE2 B HIS D 1 233 ? 5.142   19.348  -58.066 0.50 25.87  ? 233 HIS D NE2 1 
ATOM   8275 N  N   A MET D 1 234 ? 7.319   15.472  -58.722 0.50 14.85  ? 234 MET D N   1 
ATOM   8276 N  N   B MET D 1 234 ? 7.320   15.469  -58.757 0.50 15.87  ? 234 MET D N   1 
ATOM   8277 C  CA  A MET D 1 234 ? 7.400   14.920  -60.066 0.50 16.80  ? 234 MET D CA  1 
ATOM   8278 C  CA  B MET D 1 234 ? 7.298   14.925  -60.105 0.50 17.44  ? 234 MET D CA  1 
ATOM   8279 C  C   A MET D 1 234 ? 8.408   15.691  -60.925 0.50 19.06  ? 234 MET D C   1 
ATOM   8280 C  C   B MET D 1 234 ? 8.225   15.709  -61.045 0.50 18.83  ? 234 MET D C   1 
ATOM   8281 O  O   A MET D 1 234 ? 9.222   15.096  -61.631 0.50 16.16  ? 234 MET D O   1 
ATOM   8282 O  O   B MET D 1 234 ? 8.805   15.104  -61.947 0.50 25.15  ? 234 MET D O   1 
ATOM   8283 C  CB  A MET D 1 234 ? 6.011   14.948  -60.712 0.50 19.01  ? 234 MET D CB  1 
ATOM   8284 C  CB  B MET D 1 234 ? 5.847   14.915  -60.612 0.50 17.64  ? 234 MET D CB  1 
ATOM   8285 C  CG  A MET D 1 234 ? 5.985   14.273  -62.080 0.50 20.13  ? 234 MET D CG  1 
ATOM   8286 C  CG  B MET D 1 234 ? 5.559   13.995  -61.821 0.50 25.34  ? 234 MET D CG  1 
ATOM   8287 S  SD  A MET D 1 234 ? 4.260   13.934  -62.511 0.50 33.60  ? 234 MET D SD  1 
ATOM   8288 S  SD  B MET D 1 234 ? 3.841   14.215  -62.428 0.50 34.31  ? 234 MET D SD  1 
ATOM   8289 C  CE  A MET D 1 234 ? 3.602   15.603  -62.455 0.50 28.66  ? 234 MET D CE  1 
ATOM   8290 C  CE  B MET D 1 234 ? 3.223   12.531  -62.553 0.50 29.90  ? 234 MET D CE  1 
ATOM   8291 N  N   . ASP D 1 235 ? 8.425   17.024  -60.806 1.00 19.91  ? 235 ASP D N   1 
ATOM   8292 C  CA  . ASP D 1 235 ? 9.270   17.850  -61.671 1.00 25.58  ? 235 ASP D CA  1 
ATOM   8293 C  C   . ASP D 1 235 ? 10.701  18.075  -61.131 1.00 22.44  ? 235 ASP D C   1 
ATOM   8294 O  O   . ASP D 1 235 ? 11.447  18.936  -61.634 1.00 22.85  ? 235 ASP D O   1 
ATOM   8295 C  CB  . ASP D 1 235 ? 8.550   19.179  -62.016 1.00 32.51  ? 235 ASP D CB  1 
ATOM   8296 C  CG  . ASP D 1 235 ? 8.342   20.099  -60.812 1.00 37.60  ? 235 ASP D CG  1 
ATOM   8297 O  OD1 . ASP D 1 235 ? 8.737   19.690  -59.687 1.00 43.23  ? 235 ASP D OD1 1 
ATOM   8298 O  OD2 . ASP D 1 235 ? 7.838   21.246  -60.987 1.00 47.22  ? 235 ASP D OD2 1 
ATOM   8299 N  N   . ASP D 1 236 ? 11.110  17.443  -60.024 1.00 22.19  ? 236 ASP D N   1 
ATOM   8300 C  CA  . ASP D 1 236 ? 12.437  17.713  -59.504 1.00 19.51  ? 236 ASP D CA  1 
ATOM   8301 C  C   . ASP D 1 236 ? 13.480  17.161  -60.483 1.00 23.03  ? 236 ASP D C   1 
ATOM   8302 O  O   . ASP D 1 236 ? 13.398  16.009  -60.916 1.00 21.65  ? 236 ASP D O   1 
ATOM   8303 C  CB  . ASP D 1 236 ? 12.602  17.088  -58.110 1.00 18.34  ? 236 ASP D CB  1 
ATOM   8304 C  CG  . ASP D 1 236 ? 13.791  17.588  -57.297 1.00 20.42  ? 236 ASP D CG  1 
ATOM   8305 O  OD1 . ASP D 1 236 ? 14.914  17.637  -57.866 1.00 25.43  ? 236 ASP D OD1 1 
ATOM   8306 O  OD2 . ASP D 1 236 ? 13.607  17.842  -56.080 1.00 25.29  ? 236 ASP D OD2 1 
ATOM   8307 N  N   . PRO D 1 237 ? 14.464  17.981  -60.935 1.00 19.37  ? 237 PRO D N   1 
ATOM   8308 C  CA  . PRO D 1 237 ? 15.530  17.441  -61.810 1.00 22.31  ? 237 PRO D CA  1 
ATOM   8309 C  C   . PRO D 1 237 ? 16.504  16.438  -61.162 1.00 22.67  ? 237 PRO D C   1 
ATOM   8310 O  O   . PRO D 1 237 ? 17.380  15.878  -61.838 1.00 26.17  ? 237 PRO D O   1 
ATOM   8311 C  CB  . PRO D 1 237 ? 16.241  18.718  -62.302 1.00 30.91  ? 237 PRO D CB  1 
ATOM   8312 C  CG  . PRO D 1 237 ? 16.005  19.729  -61.173 1.00 29.43  ? 237 PRO D CG  1 
ATOM   8313 C  CD  . PRO D 1 237 ? 14.688  19.368  -60.510 1.00 24.02  ? 237 PRO D CD  1 
ATOM   8314 N  N   . SER D 1 238 ? 16.341  16.202  -59.850 1.00 26.55  ? 238 SER D N   1 
ATOM   8315 C  CA  . SER D 1 238 ? 17.184  15.319  -59.040 1.00 24.30  ? 238 SER D CA  1 
ATOM   8316 C  C   . SER D 1 238 ? 16.324  14.286  -58.328 1.00 19.15  ? 238 SER D C   1 
ATOM   8317 O  O   . SER D 1 238 ? 16.158  14.359  -57.117 1.00 19.55  ? 238 SER D O   1 
ATOM   8318 C  CB  . SER D 1 238 ? 17.907  16.107  -57.993 1.00 30.42  ? 238 SER D CB  1 
ATOM   8319 O  OG  . SER D 1 238 ? 18.947  15.345  -57.425 1.00 46.23  ? 238 SER D OG  1 
ATOM   8320 N  N   . PRO D 1 239 ? 15.662  13.348  -59.030 1.00 19.54  ? 239 PRO D N   1 
ATOM   8321 C  CA  . PRO D 1 239 ? 14.701  12.479  -58.336 1.00 18.56  ? 239 PRO D CA  1 
ATOM   8322 C  C   . PRO D 1 239 ? 15.403  11.621  -57.291 1.00 15.39  ? 239 PRO D C   1 
ATOM   8323 O  O   . PRO D 1 239 ? 16.549  11.204  -57.484 1.00 16.79  ? 239 PRO D O   1 
ATOM   8324 C  CB  . PRO D 1 239 ? 14.093  11.594  -59.420 1.00 23.31  ? 239 PRO D CB  1 
ATOM   8325 C  CG  . PRO D 1 239 ? 14.970  11.834  -60.653 1.00 22.61  ? 239 PRO D CG  1 
ATOM   8326 C  CD  . PRO D 1 239 ? 15.689  13.159  -60.498 1.00 21.63  ? 239 PRO D CD  1 
ATOM   8327 N  N   . ARG D 1 240 ? 14.703  11.325  -56.183 1.00 14.33  ? 240 ARG D N   1 
ATOM   8328 C  CA  . ARG D 1 240 ? 15.262  10.406  -55.203 1.00 13.17  ? 240 ARG D CA  1 
ATOM   8329 C  C   . ARG D 1 240 ? 14.181  9.376   -54.893 1.00 13.58  ? 240 ARG D C   1 
ATOM   8330 O  O   . ARG D 1 240 ? 13.072  9.739   -54.533 1.00 13.63  ? 240 ARG D O   1 
ATOM   8331 C  CB  . ARG D 1 240 ? 15.650  11.145  -53.926 1.00 15.53  ? 240 ARG D CB  1 
ATOM   8332 C  CG  . ARG D 1 240 ? 16.880  12.031  -54.088 1.00 17.73  ? 240 ARG D CG  1 
ATOM   8333 C  CD  . ARG D 1 240 ? 17.121  12.876  -52.831 1.00 17.35  ? 240 ARG D CD  1 
ATOM   8334 N  NE  . ARG D 1 240 ? 16.106  13.878  -52.511 1.00 17.41  ? 240 ARG D NE  1 
ATOM   8335 C  CZ  . ARG D 1 240 ? 15.186  13.780  -51.534 1.00 21.96  ? 240 ARG D CZ  1 
ATOM   8336 N  NH1 . ARG D 1 240 ? 15.123  12.735  -50.723 1.00 18.09  ? 240 ARG D NH1 1 
ATOM   8337 N  NH2 . ARG D 1 240 ? 14.309  14.748  -51.364 1.00 19.15  ? 240 ARG D NH2 1 
ATOM   8338 N  N   . GLU D 1 241 ? 14.542  8.090   -55.018 1.00 12.13  ? 241 GLU D N   1 
ATOM   8339 C  CA  . GLU D 1 241 ? 13.645  6.985   -54.682 1.00 12.26  ? 241 GLU D CA  1 
ATOM   8340 C  C   . GLU D 1 241 ? 13.368  6.934   -53.177 1.00 12.34  ? 241 GLU D C   1 
ATOM   8341 O  O   . GLU D 1 241 ? 14.257  7.155   -52.355 1.00 12.43  ? 241 GLU D O   1 
ATOM   8342 C  CB  . GLU D 1 241 ? 14.203  5.622   -55.107 1.00 15.38  ? 241 GLU D CB  1 
ATOM   8343 C  CG  . GLU D 1 241 ? 14.444  5.433   -56.614 1.00 17.34  ? 241 GLU D CG  1 
ATOM   8344 C  CD  . GLU D 1 241 ? 15.375  4.306   -57.089 1.00 25.68  ? 241 GLU D CD  1 
ATOM   8345 O  OE1 . GLU D 1 241 ? 16.343  3.923   -56.397 1.00 35.59  ? 241 GLU D OE1 1 
ATOM   8346 O  OE2 . GLU D 1 241 ? 15.155  3.812   -58.174 1.00 29.37  ? 241 GLU D OE2 1 
ATOM   8347 N  N   . MET D 1 242 ? 12.134  6.621   -52.816 1.00 11.49  ? 242 MET D N   1 
ATOM   8348 C  CA  . MET D 1 242 ? 11.766  6.414   -51.435 1.00 11.19  ? 242 MET D CA  1 
ATOM   8349 C  C   . MET D 1 242 ? 12.094  4.978   -51.054 1.00 9.51   ? 242 MET D C   1 
ATOM   8350 O  O   . MET D 1 242 ? 11.279  4.050   -51.192 1.00 11.24  ? 242 MET D O   1 
ATOM   8351 C  CB  . MET D 1 242 ? 10.308  6.779   -51.190 1.00 11.95  ? 242 MET D CB  1 
ATOM   8352 C  CG  . MET D 1 242 ? 9.983   6.868   -49.716 1.00 11.46  ? 242 MET D CG  1 
ATOM   8353 S  SD  . MET D 1 242 ? 8.267   7.223   -49.354 1.00 11.65  ? 242 MET D SD  1 
ATOM   8354 C  CE  . MET D 1 242 ? 8.210   8.918   -49.940 1.00 15.53  ? 242 MET D CE  1 
ATOM   8355 N  N   . ILE D 1 243 ? 13.344  4.839   -50.586 1.00 9.71   ? 243 ILE D N   1 
ATOM   8356 C  CA  . ILE D 1 243 ? 13.865  3.518   -50.226 1.00 7.99   ? 243 ILE D CA  1 
ATOM   8357 C  C   . ILE D 1 243 ? 14.648  3.668   -48.898 1.00 7.57   ? 243 ILE D C   1 
ATOM   8358 O  O   . ILE D 1 243 ? 15.105  4.776   -48.537 1.00 9.13   ? 243 ILE D O   1 
ATOM   8359 C  CB  . ILE D 1 243 ? 14.826  2.901   -51.266 1.00 10.51  ? 243 ILE D CB  1 
ATOM   8360 C  CG1 . ILE D 1 243 ? 15.946  3.882   -51.631 1.00 12.18  ? 243 ILE D CG1 1 
ATOM   8361 C  CG2 . ILE D 1 243 ? 13.990  2.459   -52.443 1.00 11.86  ? 243 ILE D CG2 1 
ATOM   8362 C  CD1 . ILE D 1 243 ? 16.971  3.301   -52.597 1.00 15.14  ? 243 ILE D CD1 1 
ATOM   8363 N  N   . ASN D 1 244 ? 14.812  2.585   -48.181 1.00 9.17   ? 244 ASN D N   1 
ATOM   8364 C  CA  . ASN D 1 244 ? 15.597  2.577   -46.947 1.00 8.98   ? 244 ASN D CA  1 
ATOM   8365 C  C   . ASN D 1 244 ? 15.194  3.713   -45.994 1.00 8.05   ? 244 ASN D C   1 
ATOM   8366 O  O   . ASN D 1 244 ? 16.031  4.367   -45.366 1.00 9.29   ? 244 ASN D O   1 
ATOM   8367 C  CB  . ASN D 1 244 ? 17.119  2.661   -47.219 1.00 10.85  ? 244 ASN D CB  1 
ATOM   8368 C  CG  . ASN D 1 244 ? 17.560  1.647   -48.265 1.00 12.19  ? 244 ASN D CG  1 
ATOM   8369 O  OD1 . ASN D 1 244 ? 17.178  0.482   -48.121 1.00 12.65  ? 244 ASN D OD1 1 
ATOM   8370 N  ND2 . ASN D 1 244 ? 18.324  2.069   -49.278 1.00 13.76  ? 244 ASN D ND2 1 
ATOM   8371 N  N   . ASN D 1 245 ? 13.889  3.843   -45.806 1.00 7.25   ? 245 ASN D N   1 
ATOM   8372 C  CA  . ASN D 1 245 ? 13.351  4.945   -45.022 1.00 8.30   ? 245 ASN D CA  1 
ATOM   8373 C  C   . ASN D 1 245 ? 13.135  4.460   -43.585 1.00 7.10   ? 245 ASN D C   1 
ATOM   8374 O  O   . ASN D 1 245 ? 12.041  4.589   -43.046 1.00 8.18   ? 245 ASN D O   1 
ATOM   8375 C  CB  . ASN D 1 245 ? 12.094  5.551   -45.679 1.00 8.57   ? 245 ASN D CB  1 
ATOM   8376 C  CG  . ASN D 1 245 ? 10.962  4.574   -45.825 1.00 9.24   ? 245 ASN D CG  1 
ATOM   8377 O  OD1 . ASN D 1 245 ? 11.150  3.363   -45.896 1.00 9.21   ? 245 ASN D OD1 1 
ATOM   8378 N  ND2 . ASN D 1 245 ? 9.730   5.024   -45.917 1.00 10.46  ? 245 ASN D ND2 1 
ATOM   8379 N  N   . PHE D 1 246 ? 14.205  3.924   -42.988 1.00 7.38   ? 246 PHE D N   1 
ATOM   8380 C  CA  . PHE D 1 246 ? 14.147  3.506   -41.602 1.00 7.04   ? 246 PHE D CA  1 
ATOM   8381 C  C   . PHE D 1 246 ? 15.363  4.123   -40.915 1.00 7.60   ? 246 PHE D C   1 
ATOM   8382 O  O   . PHE D 1 246 ? 16.444  4.274   -41.514 1.00 7.80   ? 246 PHE D O   1 
ATOM   8383 C  CB  . PHE D 1 246 ? 14.214  1.944   -41.554 1.00 7.99   ? 246 PHE D CB  1 
ATOM   8384 C  CG  . PHE D 1 246 ? 15.455  1.275   -42.159 1.00 7.96   ? 246 PHE D CG  1 
ATOM   8385 C  CD1 . PHE D 1 246 ? 15.499  0.952   -43.514 1.00 8.80   ? 246 PHE D CD1 1 
ATOM   8386 C  CD2 . PHE D 1 246 ? 16.569  0.984   -41.367 1.00 8.65   ? 246 PHE D CD2 1 
ATOM   8387 C  CE1 . PHE D 1 246 ? 16.631  0.387   -44.062 1.00 8.27   ? 246 PHE D CE1 1 
ATOM   8388 C  CE2 . PHE D 1 246 ? 17.717  0.389   -41.901 1.00 9.19   ? 246 PHE D CE2 1 
ATOM   8389 C  CZ  . PHE D 1 246 ? 17.748  0.126   -43.255 1.00 8.58   ? 246 PHE D CZ  1 
ATOM   8390 N  N   . ARG D 1 247 ? 15.148  4.454   -39.650 1.00 7.65   ? 247 ARG D N   1 
ATOM   8391 C  CA  . ARG D 1 247 ? 16.227  4.967   -38.820 1.00 7.89   ? 247 ARG D CA  1 
ATOM   8392 C  C   . ARG D 1 247 ? 17.008  3.836   -38.173 1.00 8.68   ? 247 ARG D C   1 
ATOM   8393 O  O   . ARG D 1 247 ? 16.401  2.791   -37.846 1.00 7.71   ? 247 ARG D O   1 
ATOM   8394 C  CB  . ARG D 1 247 ? 15.670  5.897   -37.734 1.00 8.63   ? 247 ARG D CB  1 
ATOM   8395 C  CG  . ARG D 1 247 ? 16.674  6.764   -36.984 1.00 7.24   ? 247 ARG D CG  1 
ATOM   8396 C  CD  . ARG D 1 247 ? 16.057  7.405   -35.742 1.00 8.53   ? 247 ARG D CD  1 
ATOM   8397 N  NE  . ARG D 1 247 ? 16.910  8.513   -35.288 1.00 8.40   ? 247 ARG D NE  1 
ATOM   8398 C  CZ  . ARG D 1 247 ? 16.621  9.230   -34.169 1.00 8.10   ? 247 ARG D CZ  1 
ATOM   8399 N  NH1 . ARG D 1 247 ? 15.524  8.995   -33.459 1.00 8.38   ? 247 ARG D NH1 1 
ATOM   8400 N  NH2 . ARG D 1 247 ? 17.356  10.294  -33.854 1.00 8.53   ? 247 ARG D NH2 1 
ATOM   8401 N  N   . GLN D 1 248 ? 18.324  3.976   -38.015 1.00 8.59   ? 248 GLN D N   1 
ATOM   8402 C  CA  . GLN D 1 248 ? 19.044  2.944   -37.231 1.00 7.82   ? 248 GLN D CA  1 
ATOM   8403 C  C   . GLN D 1 248 ? 18.498  2.875   -35.808 1.00 7.37   ? 248 GLN D C   1 
ATOM   8404 O  O   . GLN D 1 248 ? 18.018  3.877   -35.243 1.00 8.14   ? 248 GLN D O   1 
ATOM   8405 C  CB  . GLN D 1 248 ? 20.528  3.290   -37.184 1.00 8.14   ? 248 GLN D CB  1 
ATOM   8406 C  CG  . GLN D 1 248 ? 21.232  3.253   -38.548 1.00 8.00   ? 248 GLN D CG  1 
ATOM   8407 C  CD  . GLN D 1 248 ? 21.192  1.832   -39.108 1.00 7.95   ? 248 GLN D CD  1 
ATOM   8408 O  OE1 . GLN D 1 248 ? 20.287  1.551   -39.887 1.00 9.15   ? 248 GLN D OE1 1 
ATOM   8409 N  NE2 . GLN D 1 248 ? 22.232  1.071   -38.824 1.00 10.91  ? 248 GLN D NE2 1 
ATOM   8410 N  N   . VAL D 1 249 ? 18.685  1.714   -35.160 1.00 8.37   ? 249 VAL D N   1 
ATOM   8411 C  CA  . VAL D 1 249 ? 18.398  1.628   -33.726 1.00 7.63   ? 249 VAL D CA  1 
ATOM   8412 C  C   . VAL D 1 249 ? 19.271  2.578   -32.864 1.00 8.86   ? 249 VAL D C   1 
ATOM   8413 O  O   . VAL D 1 249 ? 20.427  2.865   -33.197 1.00 9.06   ? 249 VAL D O   1 
ATOM   8414 C  CB  . VAL D 1 249 ? 18.446  0.160   -33.229 1.00 8.27   ? 249 VAL D CB  1 
ATOM   8415 C  CG1 . VAL D 1 249 ? 17.397  -0.684  -33.927 1.00 10.19  ? 249 VAL D CG1 1 
ATOM   8416 C  CG2 . VAL D 1 249 ? 19.854  -0.435  -33.391 1.00 10.22  ? 249 VAL D CG2 1 
ATOM   8417 N  N   . GLN D 1 250 ? 18.771  2.907   -31.677 1.00 8.78   ? 250 GLN D N   1 
ATOM   8418 C  CA  . GLN D 1 250 ? 19.309  3.940   -30.813 1.00 8.02   ? 250 GLN D CA  1 
ATOM   8419 C  C   . GLN D 1 250 ? 19.844  3.321   -29.529 1.00 8.35   ? 250 GLN D C   1 
ATOM   8420 O  O   . GLN D 1 250 ? 19.416  2.288   -29.071 1.00 10.22  ? 250 GLN D O   1 
ATOM   8421 C  CB  . GLN D 1 250 ? 18.199  4.944   -30.458 1.00 8.60   ? 250 GLN D CB  1 
ATOM   8422 C  CG  . GLN D 1 250 ? 17.551  5.561   -31.702 1.00 9.45   ? 250 GLN D CG  1 
ATOM   8423 C  CD  . GLN D 1 250 ? 18.477  6.476   -32.440 1.00 7.73   ? 250 GLN D CD  1 
ATOM   8424 O  OE1 . GLN D 1 250 ? 18.901  7.502   -31.886 1.00 11.11  ? 250 GLN D OE1 1 
ATOM   8425 N  NE2 . GLN D 1 250 ? 18.702  6.182   -33.734 1.00 8.70   ? 250 GLN D NE2 1 
ATOM   8426 N  N   . LYS D 1 251 ? 20.719  4.054   -28.843 1.00 9.73   ? 251 LYS D N   1 
ATOM   8427 C  CA  . LYS D 1 251 ? 21.120  3.675   -27.476 1.00 10.31  ? 251 LYS D CA  1 
ATOM   8428 C  C   . LYS D 1 251 ? 19.886  3.629   -26.570 1.00 9.16   ? 251 LYS D C   1 
ATOM   8429 O  O   . LYS D 1 251 ? 18.923  4.408   -26.646 1.00 10.30  ? 251 LYS D O   1 
ATOM   8430 C  CB  . LYS D 1 251 ? 22.032  4.769   -26.904 1.00 12.85  ? 251 LYS D CB  1 
ATOM   8431 C  CG  . LYS D 1 251 ? 23.404  4.770   -27.543 1.00 12.33  ? 251 LYS D CG  1 
ATOM   8432 C  CD  . LYS D 1 251 ? 24.235  3.599   -27.047 1.00 13.50  ? 251 LYS D CD  1 
ATOM   8433 C  CE  . LYS D 1 251 ? 25.697  3.683   -27.452 1.00 14.04  ? 251 LYS D CE  1 
ATOM   8434 N  NZ  . LYS D 1 251 ? 25.887  3.651   -28.936 1.00 10.81  ? 251 LYS D NZ  1 
ATOM   8435 N  N   . PHE D 1 252 ? 19.929  2.693   -25.613 1.00 11.76  ? 252 PHE D N   1 
ATOM   8436 C  CA  . PHE D 1 252 ? 18.844  2.534   -24.656 1.00 11.69  ? 252 PHE D CA  1 
ATOM   8437 C  C   . PHE D 1 252 ? 18.649  3.654   -23.622 1.00 15.36  ? 252 PHE D C   1 
ATOM   8438 O  O   . PHE D 1 252 ? 17.542  3.867   -23.122 1.00 17.54  ? 252 PHE D O   1 
ATOM   8439 C  CB  . PHE D 1 252 ? 18.938  1.176   -23.956 1.00 14.21  ? 252 PHE D CB  1 
ATOM   8440 C  CG  . PHE D 1 252 ? 18.246  0.137   -24.794 1.00 17.07  ? 252 PHE D CG  1 
ATOM   8441 C  CD1 . PHE D 1 252 ? 18.895  -0.434  -25.884 1.00 24.00  ? 252 PHE D CD1 1 
ATOM   8442 C  CD2 . PHE D 1 252 ? 16.929  -0.222  -24.498 1.00 22.27  ? 252 PHE D CD2 1 
ATOM   8443 C  CE1 . PHE D 1 252 ? 18.239  -1.394  -26.662 1.00 25.19  ? 252 PHE D CE1 1 
ATOM   8444 C  CE2 . PHE D 1 252 ? 16.270  -1.142  -25.295 1.00 23.50  ? 252 PHE D CE2 1 
ATOM   8445 C  CZ  . PHE D 1 252 ? 16.931  -1.714  -26.371 1.00 20.98  ? 252 PHE D CZ  1 
ATOM   8446 N  N   . ASP D 1 253 ? 19.704  4.397   -23.257 1.00 15.27  ? 253 ASP D N   1 
ATOM   8447 C  CA  . ASP D 1 253 ? 19.535  5.495   -22.293 1.00 15.60  ? 253 ASP D CA  1 
ATOM   8448 C  C   . ASP D 1 253 ? 18.903  4.936   -20.998 1.00 22.48  ? 253 ASP D C   1 
ATOM   8449 O  O   . ASP D 1 253 ? 18.010  5.563   -20.428 1.00 22.10  ? 253 ASP D O   1 
ATOM   8450 C  CB  . ASP D 1 253 ? 18.794  6.751   -22.795 1.00 19.60  ? 253 ASP D CB  1 
ATOM   8451 C  CG  . ASP D 1 253 ? 19.448  7.439   -24.004 1.00 19.76  ? 253 ASP D CG  1 
ATOM   8452 O  OD1 . ASP D 1 253 ? 20.700  7.335   -24.181 1.00 28.75  ? 253 ASP D OD1 1 
ATOM   8453 O  OD2 . ASP D 1 253 ? 18.680  8.031   -24.807 1.00 19.13  ? 253 ASP D OD2 1 
ATOM   8454 N  N   . GLU D 1 254 ? 19.277  3.695   -20.606 1.00 17.91  ? 254 GLU D N   1 
ATOM   8455 C  CA  . GLU D 1 254 ? 18.887  3.059   -19.341 1.00 20.36  ? 254 GLU D CA  1 
ATOM   8456 C  C   . GLU D 1 254 ? 17.444  2.538   -19.322 1.00 21.12  ? 254 GLU D C   1 
ATOM   8457 O  O   . GLU D 1 254 ? 17.013  1.979   -18.304 1.00 22.63  ? 254 GLU D O   1 
ATOM   8458 C  CB  . GLU D 1 254 ? 19.086  3.915   -18.082 1.00 27.65  ? 254 GLU D CB  1 
ATOM   8459 C  CG  . GLU D 1 254 ? 20.200  3.393   -17.198 1.00 35.54  ? 254 GLU D CG  1 
ATOM   8460 C  CD  . GLU D 1 254 ? 21.499  4.159   -17.258 1.00 54.39  ? 254 GLU D CD  1 
ATOM   8461 O  OE1 . GLU D 1 254 ? 21.525  5.319   -16.761 1.00 49.35  ? 254 GLU D OE1 1 
ATOM   8462 O  OE2 . GLU D 1 254 ? 22.487  3.583   -17.781 1.00 66.31  ? 254 GLU D OE2 1 
ATOM   8463 N  N   . ARG D 1 255 ? 16.709  2.677   -20.437 1.00 16.73  ? 255 ARG D N   1 
ATOM   8464 C  CA  . ARG D 1 255 ? 15.343  2.162   -20.522 1.00 13.29  ? 255 ARG D CA  1 
ATOM   8465 C  C   . ARG D 1 255 ? 15.334  0.608   -20.492 1.00 13.35  ? 255 ARG D C   1 
ATOM   8466 O  O   . ARG D 1 255 ? 16.267  -0.076  -20.997 1.00 18.46  ? 255 ARG D O   1 
ATOM   8467 C  CB  . ARG D 1 255 ? 14.677  2.605   -21.840 1.00 15.11  ? 255 ARG D CB  1 
ATOM   8468 C  CG  . ARG D 1 255 ? 14.429  4.118   -21.932 1.00 15.44  ? 255 ARG D CG  1 
ATOM   8469 C  CD  . ARG D 1 255 ? 13.919  4.410   -23.351 1.00 14.95  ? 255 ARG D CD  1 
ATOM   8470 N  NE  . ARG D 1 255 ? 15.014  4.416   -24.318 1.00 15.02  ? 255 ARG D NE  1 
ATOM   8471 C  CZ  . ARG D 1 255 ? 14.909  4.787   -25.612 1.00 13.40  ? 255 ARG D CZ  1 
ATOM   8472 N  NH1 . ARG D 1 255 ? 13.700  5.044   -26.123 1.00 12.56  ? 255 ARG D NH1 1 
ATOM   8473 N  NH2 . ARG D 1 255 ? 16.009  4.774   -26.383 1.00 13.88  ? 255 ARG D NH2 1 
ATOM   8474 N  N   . LEU D 1 256 ? 14.238  0.074   -19.933 1.00 13.31  ? 256 LEU D N   1 
ATOM   8475 C  CA  . LEU D 1 256 ? 13.807  -1.292  -20.178 1.00 12.50  ? 256 LEU D CA  1 
ATOM   8476 C  C   . LEU D 1 256 ? 12.646  -1.300  -21.161 1.00 13.25  ? 256 LEU D C   1 
ATOM   8477 O  O   . LEU D 1 256 ? 12.007  -0.283  -21.437 1.00 13.56  ? 256 LEU D O   1 
ATOM   8478 C  CB  . LEU D 1 256 ? 13.362  -1.931  -18.862 1.00 15.53  ? 256 LEU D CB  1 
ATOM   8479 C  CG  . LEU D 1 256 ? 14.470  -2.158  -17.838 1.00 18.41  ? 256 LEU D CG  1 
ATOM   8480 C  CD1 . LEU D 1 256 ? 13.898  -2.840  -16.595 1.00 24.17  ? 256 LEU D CD1 1 
ATOM   8481 C  CD2 . LEU D 1 256 ? 15.620  -2.994  -18.413 1.00 22.06  ? 256 LEU D CD2 1 
ATOM   8482 N  N   . VAL D 1 257 ? 12.418  -2.451  -21.767 1.00 13.54  ? 257 VAL D N   1 
ATOM   8483 C  CA  . VAL D 1 257 ? 11.243  -2.683  -22.604 1.00 11.88  ? 257 VAL D CA  1 
ATOM   8484 C  C   . VAL D 1 257 ? 10.399  -3.684  -21.841 1.00 11.49  ? 257 VAL D C   1 
ATOM   8485 O  O   . VAL D 1 257 ? 10.891  -4.729  -21.444 1.00 14.08  ? 257 VAL D O   1 
ATOM   8486 C  CB  . VAL D 1 257 ? 11.614  -3.274  -23.988 1.00 11.37  ? 257 VAL D CB  1 
ATOM   8487 C  CG1 . VAL D 1 257 ? 10.362  -3.703  -24.707 1.00 13.72  ? 257 VAL D CG1 1 
ATOM   8488 C  CG2 . VAL D 1 257 ? 12.448  -2.295  -24.816 1.00 14.18  ? 257 VAL D CG2 1 
ATOM   8489 N  N   . TYR D 1 258 ? 9.147   -3.328  -21.590 1.00 10.44  ? 258 TYR D N   1 
ATOM   8490 C  CA  . TYR D 1 258 ? 8.268   -4.142  -20.762 1.00 10.66  ? 258 TYR D CA  1 
ATOM   8491 C  C   . TYR D 1 258 ? 7.443   -5.028  -21.691 1.00 11.15  ? 258 TYR D C   1 
ATOM   8492 O  O   . TYR D 1 258 ? 7.042   -4.630  -22.807 1.00 12.35  ? 258 TYR D O   1 
ATOM   8493 C  CB  . TYR D 1 258 ? 7.418   -3.185  -19.912 1.00 12.11  ? 258 TYR D CB  1 
ATOM   8494 C  CG  . TYR D 1 258 ? 8.295   -2.312  -19.047 1.00 10.40  ? 258 TYR D CG  1 
ATOM   8495 C  CD1 . TYR D 1 258 ? 8.775   -2.801  -17.834 1.00 11.39  ? 258 TYR D CD1 1 
ATOM   8496 C  CD2 . TYR D 1 258 ? 8.657   -1.039  -19.462 1.00 13.57  ? 258 TYR D CD2 1 
ATOM   8497 C  CE1 . TYR D 1 258 ? 9.670   -2.082  -17.046 1.00 14.01  ? 258 TYR D CE1 1 
ATOM   8498 C  CE2 . TYR D 1 258 ? 9.546   -0.338  -18.674 1.00 13.92  ? 258 TYR D CE2 1 
ATOM   8499 C  CZ  . TYR D 1 258 ? 10.036  -0.826  -17.473 1.00 13.18  ? 258 TYR D CZ  1 
ATOM   8500 O  OH  . TYR D 1 258 ? 10.944  -0.051  -16.787 1.00 17.59  ? 258 TYR D OH  1 
ATOM   8501 N  N   . THR D 1 259 ? 7.225   -6.275  -21.225 1.00 9.40   ? 259 THR D N   1 
ATOM   8502 C  CA  . THR D 1 259 ? 6.511   -7.211  -22.075 1.00 10.24  ? 259 THR D CA  1 
ATOM   8503 C  C   . THR D 1 259 ? 5.221   -7.688  -21.402 1.00 9.69   ? 259 THR D C   1 
ATOM   8504 O  O   . THR D 1 259 ? 5.166   -7.804  -20.176 1.00 11.08  ? 259 THR D O   1 
ATOM   8505 C  CB  . THR D 1 259 ? 7.367   -8.425  -22.476 1.00 11.19  ? 259 THR D CB  1 
ATOM   8506 O  OG1 . THR D 1 259 ? 7.816   -9.057  -21.278 1.00 11.66  ? 259 THR D OG1 1 
ATOM   8507 C  CG2 . THR D 1 259 ? 8.575   -7.961  -23.257 1.00 13.20  ? 259 THR D CG2 1 
ATOM   8508 N  N   . SER D 1 260 ? 4.192   -8.001  -22.215 1.00 10.80  ? 260 SER D N   1 
ATOM   8509 C  CA  . SER D 1 260 ? 2.941   -8.549  -21.697 1.00 11.14  ? 260 SER D CA  1 
ATOM   8510 C  C   . SER D 1 260 ? 2.980   -10.080 -21.685 1.00 13.13  ? 260 SER D C   1 
ATOM   8511 O  O   . SER D 1 260 ? 1.982   -10.705 -21.341 1.00 17.39  ? 260 SER D O   1 
ATOM   8512 C  CB  . SER D 1 260 ? 1.787   -8.046  -22.551 1.00 12.74  ? 260 SER D CB  1 
ATOM   8513 O  OG  . SER D 1 260 ? 1.899   -8.644  -23.833 1.00 12.44  ? 260 SER D OG  1 
ATOM   8514 N  N   . PHE D 1 261 ? 4.144   -10.645 -22.043 1.00 16.54  ? 261 PHE D N   1 
ATOM   8515 C  CA  . PHE D 1 261 ? 4.322   -12.098 -22.086 1.00 14.91  ? 261 PHE D CA  1 
ATOM   8516 C  C   . PHE D 1 261 ? 5.681   -12.411 -21.452 1.00 18.88  ? 261 PHE D C   1 
ATOM   8517 O  O   . PHE D 1 261 ? 6.530   -11.534 -21.291 1.00 16.35  ? 261 PHE D O   1 
ATOM   8518 C  CB  . PHE D 1 261 ? 4.273   -12.519 -23.547 1.00 14.09  ? 261 PHE D CB  1 
ATOM   8519 C  CG  . PHE D 1 261 ? 5.344   -11.860 -24.378 1.00 14.15  ? 261 PHE D CG  1 
ATOM   8520 C  CD1 . PHE D 1 261 ? 5.094   -10.658 -25.006 1.00 11.88  ? 261 PHE D CD1 1 
ATOM   8521 C  CD2 . PHE D 1 261 ? 6.590   -12.438 -24.553 1.00 15.55  ? 261 PHE D CD2 1 
ATOM   8522 C  CE1 . PHE D 1 261 ? 6.094   -10.008 -25.737 1.00 12.98  ? 261 PHE D CE1 1 
ATOM   8523 C  CE2 . PHE D 1 261 ? 7.569   -11.832 -25.323 1.00 16.37  ? 261 PHE D CE2 1 
ATOM   8524 C  CZ  . PHE D 1 261 ? 7.331   -10.583 -25.901 1.00 13.41  ? 261 PHE D CZ  1 
ATOM   8525 N  N   . SER D 1 262 ? 5.867   -13.661 -21.027 1.00 25.08  ? 262 SER D N   1 
ATOM   8526 C  CA  . SER D 1 262 ? 7.144   -14.244 -20.606 1.00 29.59  ? 262 SER D CA  1 
ATOM   8527 C  C   . SER D 1 262 ? 7.553   -15.263 -21.671 1.00 33.94  ? 262 SER D C   1 
ATOM   8528 O  O   . SER D 1 262 ? 8.705   -15.314 -22.081 1.00 40.97  ? 262 SER D O   1 
ATOM   8529 C  CB  . SER D 1 262 ? 7.054   -14.880 -19.244 1.00 33.55  ? 262 SER D CB  1 
ATOM   8530 O  OG  . SER D 1 262 ? 6.668   -13.920 -18.262 1.00 45.91  ? 262 SER D OG  1 
ATOM   8531 N  N   . GLN D 1 263 ? 6.546   -16.053 -22.049 1.00 52.35  ? 263 GLN D N   1 
ATOM   8532 C  CA  . GLN D 1 263 ? 6.306   -16.902 -23.215 1.00 62.89  ? 263 GLN D CA  1 
ATOM   8533 C  C   . GLN D 1 263 ? 7.518   -17.090 -24.145 1.00 62.51  ? 263 GLN D C   1 
ATOM   8534 O  O   . GLN D 1 263 ? 7.847   -18.322 -24.376 1.00 76.19  ? 263 GLN D O   1 
ATOM   8535 C  CB  . GLN D 1 263 ? 5.071   -16.405 -23.988 1.00 53.53  ? 263 GLN D CB  1 
ATOM   8536 C  CG  . GLN D 1 263 ? 3.714   -16.787 -23.381 1.00 68.73  ? 263 GLN D CG  1 
ATOM   8537 C  CD  . GLN D 1 263 ? 3.031   -15.779 -22.473 1.00 62.60  ? 263 GLN D CD  1 
ATOM   8538 O  OE1 . GLN D 1 263 ? 3.496   -15.496 -21.350 1.00 43.16  ? 263 GLN D OE1 1 
ATOM   8539 N  NE2 . GLN D 1 263 ? 1.872   -15.283 -22.922 1.00 41.17  ? 263 GLN D NE2 1 
HETATM 8540 ZN ZN  . ZN  E 2 .   ? 22.995  0.931   12.213  1.00 8.77   ? 301 ZN  A ZN  1 
HETATM 8541 C  C1  . EDO F 3 .   ? 31.836  -8.493  -3.343  1.00 19.73  ? 302 EDO A C1  1 
HETATM 8542 O  O1  . EDO F 3 .   ? 30.639  -8.407  -2.572  1.00 15.37  ? 302 EDO A O1  1 
HETATM 8543 C  C2  . EDO F 3 .   ? 31.547  -8.594  -4.801  1.00 25.18  ? 302 EDO A C2  1 
HETATM 8544 O  O2  . EDO F 3 .   ? 30.848  -7.408  -5.158  1.00 31.79  ? 302 EDO A O2  1 
HETATM 8545 C  C1  . EDO G 3 .   ? 7.647   -8.320  16.528  1.00 36.93  ? 303 EDO A C1  1 
HETATM 8546 O  O1  . EDO G 3 .   ? 7.613   -9.298  15.520  1.00 18.19  ? 303 EDO A O1  1 
HETATM 8547 C  C2  . EDO G 3 .   ? 7.893   -6.930  16.049  1.00 28.90  ? 303 EDO A C2  1 
HETATM 8548 O  O2  . EDO G 3 .   ? 7.811   -5.844  17.010  1.00 40.72  ? 303 EDO A O2  1 
HETATM 8549 O  O18 . 84Z H 4 .   ? 27.569  7.383   12.728  1.00 14.91  ? 304 84Z A O18 1 
HETATM 8550 S  S16 . 84Z H 4 .   ? 27.668  7.285   11.256  1.00 15.64  ? 304 84Z A S16 1 
HETATM 8551 O  O17 . 84Z H 4 .   ? 28.942  6.812   10.708  1.00 18.58  ? 304 84Z A O17 1 
HETATM 8552 C  C19 . 84Z H 4 .   ? 27.398  8.900   10.726  1.00 18.91  ? 304 84Z A C19 1 
HETATM 8553 C  C24 . 84Z H 4 .   ? 27.032  9.962   11.550  1.00 21.31  ? 304 84Z A C24 1 
HETATM 8554 C  C23 . 84Z H 4 .   ? 26.763  11.267  11.055  1.00 23.33  ? 304 84Z A C23 1 
HETATM 8555 C  C22 . 84Z H 4 .   ? 26.887  11.444  9.684   1.00 19.35  ? 304 84Z A C22 1 
HETATM 8556 C  C21 . 84Z H 4 .   ? 27.305  10.409  8.898   1.00 21.55  ? 304 84Z A C21 1 
HETATM 8557 C  C20 . 84Z H 4 .   ? 27.506  9.085   9.373   1.00 19.22  ? 304 84Z A C20 1 
HETATM 8558 C  C3  . 84Z H 4 .   ? 26.404  6.108   10.782  1.00 12.08  ? 304 84Z A C3  1 
HETATM 8559 C  C2  . 84Z H 4 .   ? 26.661  5.407   9.612   1.00 12.03  ? 304 84Z A C2  1 
HETATM 8560 C  C4  . 84Z H 4 .   ? 25.265  5.928   11.588  1.00 11.11  ? 304 84Z A C4  1 
HETATM 8561 C  C12 . 84Z H 4 .   ? 24.767  6.738   12.747  1.00 12.55  ? 304 84Z A C12 1 
HETATM 8562 O  O14 . 84Z H 4 .   ? 24.754  8.045   12.418  1.00 15.97  ? 304 84Z A O14 1 
HETATM 8563 C  C15 . 84Z H 4 .   ? 24.269  9.045   13.235  1.00 21.39  ? 304 84Z A C15 1 
HETATM 8564 O  O13 . 84Z H 4 .   ? 24.241  6.409   13.726  1.00 16.90  ? 304 84Z A O13 1 
HETATM 8565 C  C5  . 84Z H 4 .   ? 24.471  4.814   11.250  1.00 10.63  ? 304 84Z A C5  1 
HETATM 8566 C  C6  . 84Z H 4 .   ? 24.575  4.065   10.044  1.00 8.42   ? 304 84Z A C6  1 
HETATM 8567 C  C1  . 84Z H 4 .   ? 25.718  4.396   9.288   1.00 10.52  ? 304 84Z A C1  1 
HETATM 8568 CL CL1 . 84Z H 4 .   ? 26.081  3.568   7.806   1.00 11.10  ? 304 84Z A CL1 1 
HETATM 8569 S  S7  . 84Z H 4 .   ? 23.689  2.578   9.825   1.00 9.79   ? 304 84Z A S7  1 
HETATM 8570 O  O8  . 84Z H 4 .   ? 24.602  1.355   9.639   1.00 9.10   ? 304 84Z A O8  1 
HETATM 8571 O  O9  . 84Z H 4 .   ? 22.846  2.563   8.539   1.00 9.03   ? 304 84Z A O9  1 
HETATM 8572 N  N10 . 84Z H 4 .   ? 22.568  2.115   11.108  1.00 17.19  ? 304 84Z A N10 1 
HETATM 8573 ZN ZN  . ZN  I 2 .   ? -8.189  3.751   4.809   1.00 8.04   ? 301 ZN  B ZN  1 
HETATM 8574 C  C1  . EDO J 3 .   ? 6.021   -4.430  14.929  1.00 26.61  ? 302 EDO B C1  1 
HETATM 8575 O  O1  . EDO J 3 .   ? 6.064   -5.862  14.630  1.00 23.10  ? 302 EDO B O1  1 
HETATM 8576 C  C2  . EDO J 3 .   ? 6.934   -3.603  14.150  1.00 31.21  ? 302 EDO B C2  1 
HETATM 8577 O  O2  . EDO J 3 .   ? 6.235   -2.826  13.172  1.00 18.39  ? 302 EDO B O2  1 
HETATM 8578 C  C1  . PEG K 5 .   ? -16.520 -3.628  20.440  1.00 12.83  ? 303 PEG B C1  1 
HETATM 8579 O  O1  . PEG K 5 .   ? -15.292 -4.148  20.907  1.00 31.08  ? 303 PEG B O1  1 
HETATM 8580 C  C2  . PEG K 5 .   ? -17.710 -3.770  21.350  1.00 20.26  ? 303 PEG B C2  1 
HETATM 8581 O  O2  . PEG K 5 .   ? -17.355 -3.587  22.733  1.00 37.47  ? 303 PEG B O2  1 
HETATM 8582 C  C3  . PEG K 5 .   ? -16.365 -2.572  22.941  1.00 31.29  ? 303 PEG B C3  1 
HETATM 8583 C  C4  . PEG K 5 .   ? -17.016 -1.254  23.284  1.00 42.21  ? 303 PEG B C4  1 
HETATM 8584 O  O4  . PEG K 5 .   ? -16.196 -0.150  22.951  1.00 39.99  ? 303 PEG B O4  1 
HETATM 8585 O  O18 . 84Z L 4 .   ? -11.549 11.017  4.331   1.00 12.75  ? 304 84Z B O18 1 
HETATM 8586 S  S16 . 84Z L 4 .   ? -11.507 10.933  5.810   1.00 12.21  ? 304 84Z B S16 1 
HETATM 8587 O  O17 . 84Z L 4 .   ? -12.787 10.672  6.484   1.00 15.04  ? 304 84Z B O17 1 
HETATM 8588 C  C19 . 84Z L 4 .   ? -10.945 12.463  6.309   1.00 13.92  ? 304 84Z B C19 1 
HETATM 8589 C  C24 . 84Z L 4 .   ? -10.423 13.358  5.504   1.00 15.47  ? 304 84Z B C24 1 
HETATM 8590 C  C23 . 84Z L 4 .   ? -9.853  14.559  5.975   1.00 17.80  ? 304 84Z B C23 1 
HETATM 8591 C  C22 . 84Z L 4 .   ? -9.829  14.836  7.328   1.00 13.60  ? 304 84Z B C22 1 
HETATM 8592 C  C21 . 84Z L 4 .   ? -10.339 13.966  8.262   1.00 18.63  ? 304 84Z B C21 1 
HETATM 8593 C  C20 . 84Z L 4 .   ? -10.854 12.727  7.722   1.00 14.11  ? 304 84Z B C20 1 
HETATM 8594 C  C3  . 84Z L 4 .   ? -10.480 9.550   6.245   1.00 9.42   ? 304 84Z B C3  1 
HETATM 8595 C  C2  . 84Z L 4 .   ? -10.870 8.912   7.415   1.00 10.89  ? 304 84Z B C2  1 
HETATM 8596 C  C4  . 84Z L 4 .   ? -9.434  9.090   5.418   1.00 10.65  ? 304 84Z B C4  1 
HETATM 8597 C  C12 . 84Z L 4 .   ? -8.905  9.842   4.279   1.00 10.38  ? 304 84Z B C12 1 
HETATM 8598 O  O14 . 84Z L 4 .   ? -8.616  11.164  4.700   1.00 12.05  ? 304 84Z B O14 1 
HETATM 8599 C  C15 . 84Z L 4 .   ? -7.992  12.070  3.874   1.00 13.79  ? 304 84Z B C15 1 
HETATM 8600 O  O13 . 84Z L 4 .   ? -8.561  9.534   3.218   1.00 12.68  ? 304 84Z B O13 1 
HETATM 8601 C  C5  . 84Z L 4 .   ? -8.872  7.856   5.745   1.00 10.02  ? 304 84Z B C5  1 
HETATM 8602 C  C6  . 84Z L 4 .   ? -9.083  7.201   6.921   1.00 10.22  ? 304 84Z B C6  1 
HETATM 8603 C  C1  . 84Z L 4 .   ? -10.162 7.699   7.705   1.00 9.04   ? 304 84Z B C1  1 
HETATM 8604 CL CL1 . 84Z L 4 .   ? -10.563 6.980   9.235   1.00 9.81   ? 304 84Z B CL1 1 
HETATM 8605 S  S7  . 84Z L 4 .   ? -8.452  5.591   7.151   1.00 9.27   ? 304 84Z B S7  1 
HETATM 8606 O  O8  . 84Z L 4 .   ? -9.599  4.692   7.250   1.00 8.74   ? 304 84Z B O8  1 
HETATM 8607 O  O9  . 84Z L 4 .   ? -7.660  5.704   8.369   1.00 8.42   ? 304 84Z B O9  1 
HETATM 8608 N  N10 . 84Z L 4 .   ? -7.751  5.362   5.336   1.00 12.81  ? 304 84Z B N10 1 
HETATM 8609 ZN ZN  . ZN  M 2 .   ? 37.953  2.283   -31.242 1.00 10.50  ? 301 ZN  C ZN  1 
HETATM 8610 C  C1  . EDO N 3 .   ? 46.895  -7.504  -46.636 1.00 26.66  ? 302 EDO C C1  1 
HETATM 8611 O  O1  . EDO N 3 .   ? 45.730  -7.328  -45.859 1.00 23.28  ? 302 EDO C O1  1 
HETATM 8612 C  C2  . EDO N 3 .   ? 46.525  -7.453  -48.099 1.00 36.84  ? 302 EDO C C2  1 
HETATM 8613 O  O2  . EDO N 3 .   ? 46.170  -6.178  -48.636 1.00 44.23  ? 302 EDO C O2  1 
HETATM 8614 C  C1  . EDO O 3 .   ? 21.060  3.476   -47.182 1.00 20.24  ? 303 EDO C C1  1 
HETATM 8615 O  O1  . EDO O 3 .   ? 22.537  3.192   -46.980 1.00 28.99  ? 303 EDO C O1  1 
HETATM 8616 C  C2  . EDO O 3 .   ? 20.384  4.724   -46.658 1.00 17.28  ? 303 EDO C C2  1 
HETATM 8617 O  O2  . EDO O 3 .   ? 19.020  4.722   -46.009 1.00 22.02  ? 303 EDO C O2  1 
HETATM 8618 C  C1  . EDO P 3 .   ? 48.233  -14.478 -39.729 1.00 27.59  ? 304 EDO C C1  1 
HETATM 8619 O  O1  . EDO P 3 .   ? 48.420  -13.099 -39.771 1.00 37.43  ? 304 EDO C O1  1 
HETATM 8620 C  C2  . EDO P 3 .   ? 49.380  -15.297 -40.157 1.00 36.89  ? 304 EDO C C2  1 
HETATM 8621 O  O2  . EDO P 3 .   ? 48.823  -16.471 -40.669 1.00 31.00  ? 304 EDO C O2  1 
HETATM 8622 O  O18 . 84Z Q 4 .   ? 42.631  8.636   -30.682 1.00 17.40  ? 305 84Z C O18 1 
HETATM 8623 S  S16 . 84Z Q 4 .   ? 42.676  8.503   -32.154 1.00 17.15  ? 305 84Z C S16 1 
HETATM 8624 O  O17 . 84Z Q 4 .   ? 43.961  7.832   -32.581 1.00 22.84  ? 305 84Z C O17 1 
HETATM 8625 C  C19 . 84Z Q 4 .   ? 42.384  10.151  -32.864 1.00 19.25  ? 305 84Z C C19 1 
HETATM 8626 C  C24 . 84Z Q 4 .   ? 41.936  11.127  -31.961 1.00 28.24  ? 305 84Z C C24 1 
HETATM 8627 C  C23 . 84Z Q 4 .   ? 41.695  12.473  -32.348 1.00 29.89  ? 305 84Z C C23 1 
HETATM 8628 C  C22 . 84Z Q 4 .   ? 41.808  12.740  -33.720 1.00 29.09  ? 305 84Z C C22 1 
HETATM 8629 C  C21 . 84Z Q 4 .   ? 42.270  11.769  -34.596 1.00 29.22  ? 305 84Z C C21 1 
HETATM 8630 C  C20 . 84Z Q 4 .   ? 42.458  10.404  -34.201 1.00 23.58  ? 305 84Z C C20 1 
HETATM 8631 C  C3  . 84Z Q 4 .   ? 41.480  7.358   -32.653 1.00 13.86  ? 305 84Z C C3  1 
HETATM 8632 C  C2  . 84Z Q 4 .   ? 41.711  6.641   -33.851 1.00 12.49  ? 305 84Z C C2  1 
HETATM 8633 C  C4  . 84Z Q 4 .   ? 40.308  7.073   -31.862 1.00 13.23  ? 305 84Z C C4  1 
HETATM 8634 C  C12 . 84Z Q 4 .   ? 39.796  7.882   -30.730 1.00 14.83  ? 305 84Z C C12 1 
HETATM 8635 O  O14 . 84Z Q 4 .   ? 39.808  9.267   -31.011 1.00 16.72  ? 305 84Z C O14 1 
HETATM 8636 C  C15 . 84Z Q 4 .   ? 39.185  10.228  -30.180 1.00 19.03  ? 305 84Z C C15 1 
HETATM 8637 O  O13 . 84Z Q 4 .   ? 39.202  7.478   -29.775 1.00 21.10  ? 305 84Z C O13 1 
HETATM 8638 C  C5  . 84Z Q 4 .   ? 39.448  6.015   -32.193 1.00 13.24  ? 305 84Z C C5  1 
HETATM 8639 C  C6  . 84Z Q 4 .   ? 39.683  5.322   -33.358 1.00 10.97  ? 305 84Z C C6  1 
HETATM 8640 C  C1  . 84Z Q 4 .   ? 40.838  5.589   -34.150 1.00 12.16  ? 305 84Z C C1  1 
HETATM 8641 CL CL1 . 84Z Q 4 .   ? 41.091  4.860   -35.682 1.00 12.67  ? 305 84Z C CL1 1 
HETATM 8642 S  S7  . 84Z Q 4 .   ? 38.707  3.909   -33.709 1.00 10.81  ? 305 84Z C S7  1 
HETATM 8643 O  O8  . 84Z Q 4 .   ? 37.976  4.175   -34.926 1.00 9.29   ? 305 84Z C O8  1 
HETATM 8644 O  O9  . 84Z Q 4 .   ? 39.476  2.763   -33.621 1.00 11.79  ? 305 84Z C O9  1 
HETATM 8645 N  N10 . 84Z Q 4 .   ? 37.562  3.804   -32.474 1.00 11.35  ? 305 84Z C N10 1 
HETATM 8646 ZN ZN  . ZN  R 2 .   ? 6.962   5.453   -38.538 1.00 8.29   ? 301 ZN  D ZN  1 
HETATM 8647 C  C1  . EDO S 3 .   ? -2.519  -1.394  -22.046 1.00 16.69  ? 302 EDO D C1  1 
HETATM 8648 O  O1  . EDO S 3 .   ? -1.451  -1.487  -22.893 1.00 20.27  ? 302 EDO D O1  1 
HETATM 8649 C  C2  . EDO S 3 .   ? -1.937  -1.219  -20.648 1.00 20.90  ? 302 EDO D C2  1 
HETATM 8650 O  O2  . EDO S 3 .   ? -0.908  -0.189  -20.552 1.00 23.61  ? 302 EDO D O2  1 
HETATM 8651 O  O18 . 84Z T 4 .   ? 3.639   12.563  -39.340 1.00 14.25  ? 303 84Z D O18 1 
HETATM 8652 S  S16 . 84Z T 4 .   ? 3.793   12.672  -37.856 1.00 13.51  ? 303 84Z D S16 1 
HETATM 8653 O  O17 . 84Z T 4 .   ? 2.518   12.547  -37.168 1.00 14.96  ? 303 84Z D O17 1 
HETATM 8654 C  C19 . 84Z T 4 .   ? 4.514   14.173  -37.399 1.00 13.19  ? 303 84Z D C19 1 
HETATM 8655 C  C24 . 84Z T 4 .   ? 4.935   14.980  -38.470 1.00 17.70  ? 303 84Z D C24 1 
HETATM 8656 C  C23 . 84Z T 4 .   ? 5.510   16.262  -38.219 1.00 18.50  ? 303 84Z D C23 1 
HETATM 8657 C  C22 . 84Z T 4 .   ? 5.629   16.673  -36.867 1.00 17.47  ? 303 84Z D C22 1 
HETATM 8658 C  C21 . 84Z T 4 .   ? 5.182   15.879  -35.780 1.00 16.58  ? 303 84Z D C21 1 
HETATM 8659 C  C20 . 84Z T 4 .   ? 4.663   14.617  -36.066 1.00 16.41  ? 303 84Z D C20 1 
HETATM 8660 C  C3  . 84Z T 4 .   ? 4.762   11.330  -37.362 1.00 10.31  ? 303 84Z D C3  1 
HETATM 8661 C  C2  . 84Z T 4 .   ? 4.414   10.757  -36.116 1.00 10.30  ? 303 84Z D C2  1 
HETATM 8662 C  C4  . 84Z T 4 .   ? 5.772   10.793  -38.219 1.00 12.17  ? 303 84Z D C4  1 
HETATM 8663 C  C12 . 84Z T 4 .   ? 6.345   11.409  -39.391 1.00 11.68  ? 303 84Z D C12 1 
HETATM 8664 O  O14 . 84Z T 4 .   ? 6.688   12.724  -39.157 1.00 14.87  ? 303 84Z D O14 1 
HETATM 8665 C  C15 . 84Z T 4 .   ? 7.311   13.494  -40.086 1.00 18.12  ? 303 84Z D C15 1 
HETATM 8666 O  O13 . 84Z T 4 .   ? 6.681   10.803  -40.369 1.00 17.64  ? 303 84Z D O13 1 
HETATM 8667 C  C5  . 84Z T 4 .   ? 6.362   9.534   -37.843 1.00 10.66  ? 303 84Z D C5  1 
HETATM 8668 C  C6  . 84Z T 4 .   ? 6.039   8.990   -36.578 1.00 8.94   ? 303 84Z D C6  1 
HETATM 8669 C  C1  . 84Z T 4 .   ? 5.039   9.581   -35.772 1.00 10.65  ? 303 84Z D C1  1 
HETATM 8670 CL CL1 . 84Z T 4 .   ? 4.732   8.951   -34.208 1.00 10.21  ? 303 84Z D CL1 1 
HETATM 8671 S  S7  . 84Z T 4 .   ? 6.750   7.354   -36.195 1.00 8.65   ? 303 84Z D S7  1 
HETATM 8672 O  O8  . 84Z T 4 .   ? 5.581   6.432   -36.113 1.00 9.47   ? 303 84Z D O8  1 
HETATM 8673 O  O9  . 84Z T 4 .   ? 7.577   7.545   -35.022 1.00 8.65   ? 303 84Z D O9  1 
HETATM 8674 N  N10 . 84Z T 4 .   ? 7.656   6.924   -37.470 1.00 10.67  ? 303 84Z D N10 1 
HETATM 8675 O  O   . HOH U 6 .   ? 43.416  -5.729  1.373   1.00 38.42  ? 401 HOH A O   1 
HETATM 8676 O  O   . HOH U 6 .   ? 24.869  0.191   19.861  1.00 24.35  ? 402 HOH A O   1 
HETATM 8677 O  O   . HOH U 6 .   ? 38.357  -14.925 23.048  1.00 48.03  ? 403 HOH A O   1 
HETATM 8678 O  O   . HOH U 6 .   ? 4.768   0.043   -8.426  1.00 24.55  ? 404 HOH A O   1 
HETATM 8679 O  O   . HOH U 6 .   ? 10.691  12.511  20.523  1.00 23.69  ? 405 HOH A O   1 
HETATM 8680 O  O   . HOH U 6 .   ? 28.269  -23.355 8.613   1.00 48.54  ? 406 HOH A O   1 
HETATM 8681 O  O   . HOH U 6 .   ? 42.864  -9.486  19.049  1.00 32.35  ? 407 HOH A O   1 
HETATM 8682 O  O   . HOH U 6 .   ? 9.648   -4.308  -1.504  1.00 43.06  ? 408 HOH A O   1 
HETATM 8683 O  O   . HOH U 6 .   ? 30.233  14.774  4.152   1.00 38.69  ? 409 HOH A O   1 
HETATM 8684 O  O   . HOH U 6 .   ? 20.657  -18.432 28.736  1.00 29.60  ? 410 HOH A O   1 
HETATM 8685 O  O   . HOH U 6 .   ? 7.772   -8.072  11.632  1.00 19.81  ? 411 HOH A O   1 
HETATM 8686 O  O   . HOH U 6 .   ? 31.563  5.802   32.587  1.00 29.94  ? 412 HOH A O   1 
HETATM 8687 O  O   . HOH U 6 .   ? 5.489   -3.537  20.445  1.00 26.08  ? 413 HOH A O   1 
HETATM 8688 O  O   . HOH U 6 .   ? 31.628  -5.177  33.453  1.00 43.00  ? 414 HOH A O   1 
HETATM 8689 O  O   . HOH U 6 .   ? 27.859  4.422   33.489  1.00 36.70  ? 415 HOH A O   1 
HETATM 8690 O  O   . HOH U 6 .   ? 39.479  -12.133 19.988  1.00 27.27  ? 416 HOH A O   1 
HETATM 8691 O  O   . HOH U 6 .   ? 20.209  -20.091 13.826  1.00 47.62  ? 417 HOH A O   1 
HETATM 8692 O  O   . HOH U 6 .   ? 5.179   11.022  18.299  1.00 31.21  ? 418 HOH A O   1 
HETATM 8693 O  O   . HOH U 6 .   ? 14.403  -9.709  25.964  1.00 18.22  ? 419 HOH A O   1 
HETATM 8694 O  O   . HOH U 6 .   ? 42.450  0.206   5.559   1.00 32.30  ? 420 HOH A O   1 
HETATM 8695 O  O   . HOH U 6 .   ? 12.854  -12.105 16.341  1.00 26.02  ? 421 HOH A O   1 
HETATM 8696 O  O   . HOH U 6 .   ? 18.319  -2.843  -5.806  1.00 27.87  ? 422 HOH A O   1 
HETATM 8697 O  O   . HOH U 6 .   ? 20.766  15.374  2.172   1.00 37.25  ? 423 HOH A O   1 
HETATM 8698 O  O   . HOH U 6 .   ? 19.559  -0.396  26.528  1.00 15.05  ? 424 HOH A O   1 
HETATM 8699 O  O   . HOH U 6 .   ? 28.147  -21.438 1.692   1.00 35.35  ? 425 HOH A O   1 
HETATM 8700 O  O   . HOH U 6 .   ? 17.924  3.380   12.824  1.00 12.43  ? 426 HOH A O   1 
HETATM 8701 O  O   . HOH U 6 .   ? 32.346  -16.555 10.295  1.00 34.57  ? 427 HOH A O   1 
HETATM 8702 O  O   . HOH U 6 .   ? 36.515  -2.896  -11.546 1.00 37.88  ? 428 HOH A O   1 
HETATM 8703 O  O   . HOH U 6 .   ? 6.318   15.960  15.750  1.00 29.57  ? 429 HOH A O   1 
HETATM 8704 O  O   . HOH U 6 .   ? 11.118  3.475   18.950  1.00 28.10  ? 430 HOH A O   1 
HETATM 8705 O  O   . HOH U 6 .   ? 38.445  7.091   18.747  1.00 36.79  ? 431 HOH A O   1 
HETATM 8706 O  O   . HOH U 6 .   ? 19.207  9.933   32.293  1.00 22.74  ? 432 HOH A O   1 
HETATM 8707 O  O   . HOH U 6 .   ? 42.017  2.684   1.004   1.00 18.43  ? 433 HOH A O   1 
HETATM 8708 O  O   . HOH U 6 .   ? 45.538  -0.533  14.217  1.00 28.98  ? 434 HOH A O   1 
HETATM 8709 O  O   . HOH U 6 .   ? 33.063  -15.599 13.159  1.00 37.07  ? 435 HOH A O   1 
HETATM 8710 O  O   . HOH U 6 .   ? 41.677  6.487   5.452   1.00 29.52  ? 436 HOH A O   1 
HETATM 8711 O  O   . HOH U 6 .   ? 27.748  -20.667 24.682  1.00 30.90  ? 437 HOH A O   1 
HETATM 8712 O  O   . HOH U 6 .   ? 33.974  1.965   -5.806  1.00 26.62  ? 438 HOH A O   1 
HETATM 8713 O  O   . HOH U 6 .   ? 41.198  -9.897  9.879   1.00 18.85  ? 439 HOH A O   1 
HETATM 8714 O  O   . HOH U 6 .   ? 29.439  -16.578 14.783  1.00 23.99  ? 440 HOH A O   1 
HETATM 8715 O  O   . HOH U 6 .   ? 20.855  -20.145 5.368   1.00 33.26  ? 441 HOH A O   1 
HETATM 8716 O  O   . HOH U 6 .   ? 18.238  -14.950 6.165   1.00 19.35  ? 442 HOH A O   1 
HETATM 8717 O  O   . HOH U 6 .   ? 21.525  -21.636 -0.459  1.00 45.46  ? 443 HOH A O   1 
HETATM 8718 O  O   . HOH U 6 .   ? 15.202  -6.677  21.022  1.00 12.69  ? 444 HOH A O   1 
HETATM 8719 O  O   . HOH U 6 .   ? 10.550  6.316   15.378  1.00 13.36  ? 445 HOH A O   1 
HETATM 8720 O  O   . HOH U 6 .   ? 32.945  7.290   15.736  1.00 29.35  ? 446 HOH A O   1 
HETATM 8721 O  O   . HOH U 6 .   ? 13.855  1.893   -0.216  1.00 19.07  ? 447 HOH A O   1 
HETATM 8722 O  O   . HOH U 6 .   ? 19.385  -6.283  -12.011 1.00 47.63  ? 448 HOH A O   1 
HETATM 8723 O  O   . HOH U 6 .   ? 10.272  4.856   8.702   1.00 10.65  ? 449 HOH A O   1 
HETATM 8724 O  O   . HOH U 6 .   ? 29.053  -7.686  -8.226  1.00 50.86  ? 450 HOH A O   1 
HETATM 8725 O  O   . HOH U 6 .   ? 39.442  -15.281 16.987  1.00 29.31  ? 451 HOH A O   1 
HETATM 8726 O  O   . HOH U 6 .   ? 7.620   -6.651  2.279   1.00 27.36  ? 452 HOH A O   1 
HETATM 8727 O  O   . HOH U 6 .   ? 7.956   -1.613  15.089  1.00 23.12  ? 453 HOH A O   1 
HETATM 8728 O  O   . HOH U 6 .   ? 25.979  -11.342 -12.322 1.00 51.57  ? 454 HOH A O   1 
HETATM 8729 O  O   . HOH U 6 .   ? 43.711  -3.697  12.891  1.00 18.39  ? 455 HOH A O   1 
HETATM 8730 O  O   . HOH U 6 .   ? 12.450  -2.506  10.946  1.00 10.14  ? 456 HOH A O   1 
HETATM 8731 O  O   . HOH U 6 .   ? 28.584  -3.852  2.528   1.00 11.60  ? 457 HOH A O   1 
HETATM 8732 O  O   . HOH U 6 .   ? 5.697   -11.890 13.117  1.00 23.11  ? 458 HOH A O   1 
HETATM 8733 O  O   . HOH U 6 .   ? 12.515  14.779  2.285   1.00 13.72  ? 459 HOH A O   1 
HETATM 8734 O  O   . HOH U 6 .   ? 9.165   11.606  1.119   1.00 16.88  ? 460 HOH A O   1 
HETATM 8735 O  O   . HOH U 6 .   ? 19.958  14.315  28.626  1.00 28.66  ? 461 HOH A O   1 
HETATM 8736 O  O   . HOH U 6 .   ? 38.138  -6.894  24.574  1.00 29.32  ? 462 HOH A O   1 
HETATM 8737 O  O   . HOH U 6 .   ? 25.681  -18.219 12.400  1.00 21.37  ? 463 HOH A O   1 
HETATM 8738 O  O   . HOH U 6 .   ? 11.356  5.470   2.119   1.00 11.11  ? 464 HOH A O   1 
HETATM 8739 O  O   . HOH U 6 .   ? 33.038  5.615   20.190  1.00 26.76  ? 465 HOH A O   1 
HETATM 8740 O  O   . HOH U 6 .   ? 37.261  -13.787 -1.427  1.00 48.74  ? 466 HOH A O   1 
HETATM 8741 O  O   . HOH U 6 .   ? 20.136  -15.468 -11.159 1.00 45.96  ? 467 HOH A O   1 
HETATM 8742 O  O   . HOH U 6 .   ? 13.580  16.601  11.764  1.00 15.31  ? 468 HOH A O   1 
HETATM 8743 O  O   . HOH U 6 .   ? 15.880  -11.852 26.916  1.00 20.48  ? 469 HOH A O   1 
HETATM 8744 O  O   . HOH U 6 .   ? 33.984  -14.796 8.698   1.00 36.73  ? 470 HOH A O   1 
HETATM 8745 O  O   . HOH U 6 .   ? 17.697  20.940  6.643   1.00 31.83  ? 471 HOH A O   1 
HETATM 8746 O  O   . HOH U 6 .   ? 16.951  -18.238 12.348  1.00 34.80  ? 472 HOH A O   1 
HETATM 8747 O  O   . HOH U 6 .   ? 12.067  -10.331 27.238  1.00 19.63  ? 473 HOH A O   1 
HETATM 8748 O  O   . HOH U 6 .   ? 10.961  -4.413  -5.086  1.00 34.30  ? 474 HOH A O   1 
HETATM 8749 O  O   . HOH U 6 .   ? 15.145  -15.755 14.933  1.00 20.21  ? 475 HOH A O   1 
HETATM 8750 O  O   . HOH U 6 .   ? 36.174  -6.554  26.396  1.00 31.01  ? 476 HOH A O   1 
HETATM 8751 O  O   . HOH U 6 .   ? 30.080  -15.156 -1.841  1.00 18.33  ? 477 HOH A O   1 
HETATM 8752 O  O   . HOH U 6 .   ? 11.095  -5.005  0.568   1.00 22.39  ? 478 HOH A O   1 
HETATM 8753 O  O   . HOH U 6 .   ? 12.273  5.405   28.957  1.00 34.76  ? 479 HOH A O   1 
HETATM 8754 O  O   . HOH U 6 .   ? 17.122  0.969   -0.475  1.00 17.67  ? 480 HOH A O   1 
HETATM 8755 O  O   . HOH U 6 .   ? 37.004  8.680   27.868  1.00 37.37  ? 481 HOH A O   1 
HETATM 8756 O  O   . HOH U 6 .   ? 36.776  -3.848  -0.734  1.00 19.76  ? 482 HOH A O   1 
HETATM 8757 O  O   . HOH U 6 .   ? 13.168  6.130   24.591  1.00 30.71  ? 483 HOH A O   1 
HETATM 8758 O  O   . HOH U 6 .   ? 39.932  -11.610 11.671  1.00 21.94  ? 484 HOH A O   1 
HETATM 8759 O  O   . HOH U 6 .   ? 35.188  -10.588 -3.052  1.00 29.79  ? 485 HOH A O   1 
HETATM 8760 O  O   . HOH U 6 .   ? 26.451  6.016   -3.725  1.00 33.93  ? 486 HOH A O   1 
HETATM 8761 O  O   . HOH U 6 .   ? 10.509  -3.310  2.634   1.00 13.43  ? 487 HOH A O   1 
HETATM 8762 O  O   . HOH U 6 .   ? 19.382  14.387  5.061   1.00 12.27  ? 488 HOH A O   1 
HETATM 8763 O  O   . HOH U 6 .   ? 26.086  12.581  6.066   1.00 27.27  ? 489 HOH A O   1 
HETATM 8764 O  O   . HOH U 6 .   ? 40.079  -12.950 8.040   1.00 39.71  ? 490 HOH A O   1 
HETATM 8765 O  O   . HOH U 6 .   ? 20.693  -9.655  31.830  1.00 18.46  ? 491 HOH A O   1 
HETATM 8766 O  O   . HOH U 6 .   ? 13.980  8.390   23.428  1.00 29.95  ? 492 HOH A O   1 
HETATM 8767 O  O   . HOH U 6 .   ? 33.962  -12.812 26.699  1.00 34.87  ? 493 HOH A O   1 
HETATM 8768 O  O   . HOH U 6 .   ? 31.922  -16.553 20.562  1.00 45.88  ? 494 HOH A O   1 
HETATM 8769 O  O   . HOH U 6 .   ? 9.223   -10.868 13.902  1.00 29.74  ? 495 HOH A O   1 
HETATM 8770 O  O   . HOH U 6 .   ? 19.423  -18.254 26.207  1.00 28.09  ? 496 HOH A O   1 
HETATM 8771 O  O   . HOH U 6 .   ? 46.493  -8.213  16.207  1.00 30.96  ? 497 HOH A O   1 
HETATM 8772 O  O   . HOH U 6 .   ? 28.443  2.789   -1.322  1.00 26.88  ? 498 HOH A O   1 
HETATM 8773 O  O   . HOH U 6 .   ? 38.558  4.586   11.358  1.00 23.66  ? 499 HOH A O   1 
HETATM 8774 O  O   . HOH U 6 .   ? 23.183  -12.065 9.637   1.00 12.09  ? 500 HOH A O   1 
HETATM 8775 O  O   . HOH U 6 .   ? 23.862  -15.869 29.649  1.00 24.71  ? 501 HOH A O   1 
HETATM 8776 O  O   . HOH U 6 .   ? 18.873  12.234  -0.723  1.00 17.31  ? 502 HOH A O   1 
HETATM 8777 O  O   . HOH U 6 .   ? 31.732  -12.759 2.516   1.00 21.56  ? 503 HOH A O   1 
HETATM 8778 O  O   . HOH U 6 .   ? 29.041  8.748   15.197  1.00 44.03  ? 504 HOH A O   1 
HETATM 8779 O  O   . HOH U 6 .   ? 17.244  0.561   28.513  1.00 20.44  ? 505 HOH A O   1 
HETATM 8780 O  O   . HOH U 6 .   ? 27.734  -4.168  31.163  1.00 34.82  ? 506 HOH A O   1 
HETATM 8781 O  O   . HOH U 6 .   ? 5.957   11.790  7.897   1.00 11.59  ? 507 HOH A O   1 
HETATM 8782 O  O   . HOH U 6 .   ? 29.318  -14.667 17.007  1.00 20.34  ? 508 HOH A O   1 
HETATM 8783 O  O   . HOH U 6 .   ? 7.354   5.093   11.147  1.00 9.32   ? 509 HOH A O   1 
HETATM 8784 O  O   . HOH U 6 .   ? 45.103  -4.294  7.679   1.00 25.80  ? 510 HOH A O   1 
HETATM 8785 O  O   . HOH U 6 .   ? 22.399  7.561   -4.266  1.00 31.89  ? 511 HOH A O   1 
HETATM 8786 O  O   . HOH U 6 .   ? 18.224  -15.500 33.776  1.00 35.77  ? 512 HOH A O   1 
HETATM 8787 O  O   . HOH U 6 .   ? 6.060   -3.615  -8.067  1.00 29.63  ? 513 HOH A O   1 
HETATM 8788 O  O   . HOH U 6 .   ? 39.658  -11.545 23.204  1.00 38.99  ? 514 HOH A O   1 
HETATM 8789 O  O   . HOH U 6 .   ? 8.645   3.071   7.324   1.00 8.14   ? 515 HOH A O   1 
HETATM 8790 O  O   . HOH U 6 .   ? 22.807  16.475  12.881  1.00 36.41  ? 516 HOH A O   1 
HETATM 8791 O  O   . HOH U 6 .   ? 10.972  11.319  8.079   1.00 10.85  ? 517 HOH A O   1 
HETATM 8792 O  O   . HOH U 6 .   ? 33.376  -14.449 3.500   1.00 24.11  ? 518 HOH A O   1 
HETATM 8793 O  O   . HOH U 6 .   ? 32.435  -16.354 17.342  1.00 34.87  ? 519 HOH A O   1 
HETATM 8794 O  O   . HOH U 6 .   ? 41.966  7.553   2.854   1.00 27.95  ? 520 HOH A O   1 
HETATM 8795 O  O   . HOH U 6 .   ? 8.863   -6.271  7.402   1.00 19.80  ? 521 HOH A O   1 
HETATM 8796 O  O   . HOH U 6 .   ? 20.721  18.214  7.771   1.00 31.42  ? 522 HOH A O   1 
HETATM 8797 O  O   . HOH U 6 .   ? 7.771   -2.000  -1.025  1.00 26.98  ? 523 HOH A O   1 
HETATM 8798 O  O   . HOH U 6 .   ? 10.103  -3.988  19.354  1.00 22.97  ? 524 HOH A O   1 
HETATM 8799 O  O   . HOH U 6 .   ? 26.048  -9.382  29.051  1.00 27.44  ? 525 HOH A O   1 
HETATM 8800 O  O   . HOH U 6 .   ? 7.254   0.681   -14.119 1.00 38.16  ? 526 HOH A O   1 
HETATM 8801 O  O   . HOH U 6 .   ? 11.925  7.677   8.606   1.00 10.34  ? 527 HOH A O   1 
HETATM 8802 O  O   . HOH U 6 .   ? 38.905  -5.173  -3.229  1.00 27.24  ? 528 HOH A O   1 
HETATM 8803 O  O   . HOH U 6 .   ? 20.746  4.169   16.558  1.00 24.62  ? 529 HOH A O   1 
HETATM 8804 O  O   . HOH U 6 .   ? 20.809  -2.337  -5.267  1.00 29.98  ? 530 HOH A O   1 
HETATM 8805 O  O   . HOH U 6 .   ? 34.068  -5.804  -6.456  1.00 35.38  ? 531 HOH A O   1 
HETATM 8806 O  O   . HOH U 6 .   ? 11.395  9.894   -2.034  1.00 21.67  ? 532 HOH A O   1 
HETATM 8807 O  O   . HOH U 6 .   ? 17.932  -15.993 -3.774  1.00 37.99  ? 533 HOH A O   1 
HETATM 8808 O  O   . HOH U 6 .   ? 4.752   -9.009  25.662  1.00 31.60  ? 534 HOH A O   1 
HETATM 8809 O  O   . HOH U 6 .   ? 17.670  9.855   0.157   1.00 12.70  ? 535 HOH A O   1 
HETATM 8810 O  O   . HOH U 6 .   ? 31.514  -20.576 8.452   1.00 28.89  ? 536 HOH A O   1 
HETATM 8811 O  O   . HOH U 6 .   ? 13.915  2.033   -2.942  1.00 17.88  ? 537 HOH A O   1 
HETATM 8812 O  O   . HOH U 6 .   ? 13.687  -12.373 20.611  1.00 19.00  ? 538 HOH A O   1 
HETATM 8813 O  O   . HOH U 6 .   ? 11.995  -15.391 8.157   1.00 22.11  ? 539 HOH A O   1 
HETATM 8814 O  O   . HOH U 6 .   ? 23.863  14.951  4.614   1.00 32.04  ? 540 HOH A O   1 
HETATM 8815 O  O   . HOH U 6 .   ? 7.558   9.342   14.087  1.00 17.76  ? 541 HOH A O   1 
HETATM 8816 O  O   . HOH U 6 .   ? 26.186  -18.136 20.529  1.00 23.02  ? 542 HOH A O   1 
HETATM 8817 O  O   . HOH U 6 .   ? 43.493  -9.080  11.397  1.00 23.64  ? 543 HOH A O   1 
HETATM 8818 O  O   . HOH U 6 .   ? 21.574  -3.590  -10.559 1.00 48.60  ? 544 HOH A O   1 
HETATM 8819 O  O   . HOH U 6 .   ? 16.754  -13.482 30.741  1.00 26.38  ? 545 HOH A O   1 
HETATM 8820 O  O   . HOH U 6 .   ? 14.184  4.644   -4.027  1.00 20.23  ? 546 HOH A O   1 
HETATM 8821 O  O   . HOH U 6 .   ? 8.205   -10.405 26.347  1.00 29.19  ? 547 HOH A O   1 
HETATM 8822 O  O   . HOH U 6 .   ? 26.117  -17.578 17.417  1.00 22.06  ? 548 HOH A O   1 
HETATM 8823 O  O   . HOH U 6 .   ? 44.277  -9.288  8.234   1.00 24.93  ? 549 HOH A O   1 
HETATM 8824 O  O   . HOH U 6 .   ? 24.300  -6.721  -8.257  1.00 56.35  ? 550 HOH A O   1 
HETATM 8825 O  O   . HOH U 6 .   ? 39.191  4.348   19.539  1.00 27.04  ? 551 HOH A O   1 
HETATM 8826 O  O   . HOH U 6 .   ? 16.615  11.274  -3.111  1.00 23.47  ? 552 HOH A O   1 
HETATM 8827 O  O   . HOH U 6 .   ? 32.282  -17.894 7.153   1.00 32.20  ? 553 HOH A O   1 
HETATM 8828 O  O   . HOH U 6 .   ? 36.858  5.771   14.270  1.00 31.41  ? 554 HOH A O   1 
HETATM 8829 O  O   . HOH U 6 .   ? 23.490  3.552   -2.040  1.00 19.40  ? 555 HOH A O   1 
HETATM 8830 O  O   . HOH U 6 .   ? 13.071  14.329  14.031  1.00 26.07  ? 556 HOH A O   1 
HETATM 8831 O  O   . HOH U 6 .   ? 15.188  -14.185 19.155  1.00 16.55  ? 557 HOH A O   1 
HETATM 8832 O  O   . HOH U 6 .   ? 17.156  -15.991 -7.705  1.00 45.08  ? 558 HOH A O   1 
HETATM 8833 O  O   . HOH U 6 .   ? 38.597  -12.892 5.534   1.00 24.34  ? 559 HOH A O   1 
HETATM 8834 O  O   . HOH U 6 .   ? 27.804  -15.874 -5.515  1.00 32.90  ? 560 HOH A O   1 
HETATM 8835 O  O   . HOH U 6 .   ? 36.337  7.824   9.654   1.00 36.08  ? 561 HOH A O   1 
HETATM 8836 O  O   . HOH U 6 .   ? 11.548  8.202   1.682   1.00 13.01  ? 562 HOH A O   1 
HETATM 8837 O  O   . HOH U 6 .   ? 16.038  4.741   21.655  1.00 20.00  ? 563 HOH A O   1 
HETATM 8838 O  O   . HOH U 6 .   ? 25.860  -15.726 6.592   1.00 14.04  ? 564 HOH A O   1 
HETATM 8839 O  O   . HOH U 6 .   ? 9.411   -2.421  10.332  1.00 25.65  ? 565 HOH A O   1 
HETATM 8840 O  O   . HOH U 6 .   ? 6.575   -9.545  4.470   1.00 23.31  ? 566 HOH A O   1 
HETATM 8841 O  O   . HOH U 6 .   ? 44.396  3.903   7.048   1.00 29.11  ? 567 HOH A O   1 
HETATM 8842 O  O   . HOH U 6 .   ? 41.612  5.103   12.689  1.00 34.43  ? 568 HOH A O   1 
HETATM 8843 O  O   . HOH U 6 .   ? 18.273  5.981   20.662  1.00 19.96  ? 569 HOH A O   1 
HETATM 8844 O  O   . HOH U 6 .   ? 23.033  12.208  12.688  1.00 28.15  ? 570 HOH A O   1 
HETATM 8845 O  O   . HOH U 6 .   ? 31.669  -18.531 4.197   1.00 26.42  ? 571 HOH A O   1 
HETATM 8846 O  O   . HOH U 6 .   ? 38.813  -14.982 12.428  1.00 28.24  ? 572 HOH A O   1 
HETATM 8847 O  O   . HOH U 6 .   ? 45.364  2.252   22.612  1.00 39.45  ? 573 HOH A O   1 
HETATM 8848 O  O   . HOH U 6 .   ? 17.594  -3.490  -8.309  1.00 29.88  ? 574 HOH A O   1 
HETATM 8849 O  O   . HOH U 6 .   ? 26.149  4.826   15.443  1.00 31.05  ? 575 HOH A O   1 
HETATM 8850 O  O   . HOH U 6 .   ? 27.519  -5.074  -5.221  1.00 20.71  ? 576 HOH A O   1 
HETATM 8851 O  O   . HOH U 6 .   ? 23.930  -21.280 -3.338  1.00 40.40  ? 577 HOH A O   1 
HETATM 8852 O  O   . HOH U 6 .   ? 15.874  17.386  18.713  1.00 33.68  ? 578 HOH A O   1 
HETATM 8853 O  O   . HOH U 6 .   ? 31.755  -2.123  -4.700  1.00 34.35  ? 579 HOH A O   1 
HETATM 8854 O  O   . HOH U 6 .   ? 8.910   4.139   2.682   1.00 17.12  ? 580 HOH A O   1 
HETATM 8855 O  O   . HOH U 6 .   ? 39.063  2.382   -6.058  1.00 32.69  ? 581 HOH A O   1 
HETATM 8856 O  O   . HOH U 6 .   ? 23.928  12.403  0.273   1.00 27.28  ? 582 HOH A O   1 
HETATM 8857 O  O   . HOH U 6 .   ? 12.455  4.666   22.266  1.00 26.17  ? 583 HOH A O   1 
HETATM 8858 O  O   . HOH U 6 .   ? 24.050  -20.788 26.598  1.00 30.77  ? 584 HOH A O   1 
HETATM 8859 O  O   . HOH U 6 .   ? 30.639  10.339  24.709  1.00 42.83  ? 585 HOH A O   1 
HETATM 8860 O  O   . HOH U 6 .   ? 8.449   -0.028  24.404  1.00 25.15  ? 586 HOH A O   1 
HETATM 8861 O  O   . HOH U 6 .   ? 8.749   4.178   19.525  1.00 30.68  ? 587 HOH A O   1 
HETATM 8862 O  O   . HOH U 6 .   ? 14.219  -1.679  28.854  1.00 22.40  ? 588 HOH A O   1 
HETATM 8863 O  O   . HOH U 6 .   ? 14.866  7.308   21.084  1.00 19.40  ? 589 HOH A O   1 
HETATM 8864 O  O   . HOH U 6 .   ? 17.919  10.450  22.013  1.00 28.75  ? 590 HOH A O   1 
HETATM 8865 O  O   . HOH U 6 .   ? 29.797  12.704  -4.301  1.00 34.02  ? 591 HOH A O   1 
HETATM 8866 O  O   . HOH U 6 .   ? 15.205  -16.882 19.109  1.00 38.42  ? 592 HOH A O   1 
HETATM 8867 O  O   . HOH U 6 .   ? 10.112  3.454   22.174  1.00 25.36  ? 593 HOH A O   1 
HETATM 8868 O  O   . HOH U 6 .   ? 13.199  5.336   -0.407  1.00 19.28  ? 594 HOH A O   1 
HETATM 8869 O  O   . HOH U 6 .   ? 32.322  7.947   31.122  1.00 26.07  ? 595 HOH A O   1 
HETATM 8870 O  O   . HOH U 6 .   ? 11.747  10.113  22.992  1.00 30.79  ? 596 HOH A O   1 
HETATM 8871 O  O   . HOH U 6 .   ? 42.491  3.633   5.103   1.00 33.34  ? 597 HOH A O   1 
HETATM 8872 O  O   . HOH U 6 .   ? 15.160  -13.396 16.521  1.00 15.68  ? 598 HOH A O   1 
HETATM 8873 O  O   . HOH U 6 .   ? 37.912  -5.750  29.177  1.00 32.45  ? 599 HOH A O   1 
HETATM 8874 O  O   . HOH U 6 .   ? 45.534  -5.635  13.434  1.00 27.89  ? 600 HOH A O   1 
HETATM 8875 O  O   . HOH U 6 .   ? 10.110  3.262   -2.441  1.00 32.34  ? 601 HOH A O   1 
HETATM 8876 O  O   . HOH U 6 .   ? 27.875  -20.778 15.328  1.00 36.41  ? 602 HOH A O   1 
HETATM 8877 O  O   . HOH U 6 .   ? 29.921  10.451  33.586  1.00 34.66  ? 603 HOH A O   1 
HETATM 8878 O  O   . HOH U 6 .   ? 24.678  16.596  2.059   1.00 32.36  ? 604 HOH A O   1 
HETATM 8879 O  O   . HOH U 6 .   ? 45.518  -6.233  6.007   1.00 22.77  ? 605 HOH A O   1 
HETATM 8880 O  O   . HOH U 6 .   ? 21.631  -4.012  31.832  1.00 34.43  ? 606 HOH A O   1 
HETATM 8881 O  O   . HOH U 6 .   ? 22.339  -18.837 15.096  1.00 29.41  ? 607 HOH A O   1 
HETATM 8882 O  O   . HOH U 6 .   ? 17.345  8.434   20.113  1.00 26.35  ? 608 HOH A O   1 
HETATM 8883 O  O   . HOH U 6 .   ? 30.570  7.328   13.894  1.00 26.66  ? 609 HOH A O   1 
HETATM 8884 O  O   . HOH U 6 .   ? 8.773   -1.304  19.318  1.00 29.93  ? 610 HOH A O   1 
HETATM 8885 O  O   . HOH U 6 .   ? 15.595  14.030  -0.622  1.00 34.03  ? 611 HOH A O   1 
HETATM 8886 O  O   . HOH U 6 .   ? 7.773   -15.898 7.474   1.00 48.15  ? 612 HOH A O   1 
HETATM 8887 O  O   . HOH U 6 .   ? 37.565  13.512  -0.710  1.00 34.04  ? 613 HOH A O   1 
HETATM 8888 O  O   . HOH U 6 .   ? 35.105  10.637  10.373  1.00 38.87  ? 614 HOH A O   1 
HETATM 8889 O  O   . HOH U 6 .   ? 4.234   13.377  19.440  1.00 29.64  ? 615 HOH A O   1 
HETATM 8890 O  O   . HOH U 6 .   ? 40.049  3.158   16.689  1.00 34.86  ? 616 HOH A O   1 
HETATM 8891 O  O   . HOH U 6 .   ? 34.614  -6.500  -10.933 1.00 38.95  ? 617 HOH A O   1 
HETATM 8892 O  O   . HOH U 6 .   ? 28.793  -18.433 20.599  1.00 25.07  ? 618 HOH A O   1 
HETATM 8893 O  O   . HOH U 6 .   ? 45.403  2.102   15.451  1.00 36.69  ? 619 HOH A O   1 
HETATM 8894 O  O   . HOH U 6 .   ? 5.019   -3.391  17.637  1.00 23.26  ? 620 HOH A O   1 
HETATM 8895 O  O   . HOH U 6 .   ? 17.922  -6.590  33.725  1.00 41.42  ? 621 HOH A O   1 
HETATM 8896 O  O   . HOH U 6 .   ? 27.000  10.617  15.145  1.00 33.01  ? 622 HOH A O   1 
HETATM 8897 O  O   . HOH U 6 .   ? 13.333  -14.548 12.552  1.00 32.64  ? 623 HOH A O   1 
HETATM 8898 O  O   . HOH U 6 .   ? 13.992  -15.940 26.854  1.00 30.36  ? 624 HOH A O   1 
HETATM 8899 O  O   . HOH U 6 .   ? 24.428  -11.205 30.265  1.00 24.57  ? 625 HOH A O   1 
HETATM 8900 O  O   . HOH U 6 .   ? 24.002  -15.629 -12.101 1.00 42.40  ? 626 HOH A O   1 
HETATM 8901 O  O   . HOH U 6 .   ? 36.694  -5.213  -10.233 1.00 40.99  ? 627 HOH A O   1 
HETATM 8902 O  O   . HOH U 6 .   ? 5.901   -0.602  -2.859  1.00 32.41  ? 628 HOH A O   1 
HETATM 8903 O  O   . HOH U 6 .   ? 7.924   2.141   -3.491  1.00 31.23  ? 629 HOH A O   1 
HETATM 8904 O  O   . HOH U 6 .   ? 13.807  21.448  11.629  1.00 28.10  ? 630 HOH A O   1 
HETATM 8905 O  O   . HOH U 6 .   ? 24.135  -19.541 16.574  1.00 32.01  ? 631 HOH A O   1 
HETATM 8906 O  O   . HOH U 6 .   ? 44.415  -2.581  15.529  1.00 27.75  ? 632 HOH A O   1 
HETATM 8907 O  O   . HOH U 6 .   ? 40.340  -3.452  -2.044  1.00 42.89  ? 633 HOH A O   1 
HETATM 8908 O  O   . HOH U 6 .   ? 7.110   -5.526  4.976   1.00 35.67  ? 634 HOH A O   1 
HETATM 8909 O  O   . HOH U 6 .   ? 29.824  -3.836  -5.822  1.00 65.07  ? 635 HOH A O   1 
HETATM 8910 O  O   . HOH U 6 .   ? 30.193  -17.594 18.432  1.00 30.85  ? 636 HOH A O   1 
HETATM 8911 O  O   . HOH U 6 .   ? 23.503  -3.755  -5.403  1.00 35.64  ? 637 HOH A O   1 
HETATM 8912 O  O   . HOH U 6 .   ? 26.516  -6.402  -7.454  1.00 33.75  ? 638 HOH A O   1 
HETATM 8913 O  O   . HOH U 6 .   ? 36.150  -16.019 13.951  1.00 39.18  ? 639 HOH A O   1 
HETATM 8914 O  O   . HOH U 6 .   ? 27.207  -18.116 14.796  1.00 40.90  ? 640 HOH A O   1 
HETATM 8915 O  O   . HOH U 6 .   ? 36.206  -8.598  27.887  1.00 42.04  ? 641 HOH A O   1 
HETATM 8916 O  O   . HOH U 6 .   ? 7.882   6.710   15.544  1.00 17.32  ? 642 HOH A O   1 
HETATM 8917 O  O   . HOH U 6 .   ? 20.812  -0.076  -7.265  1.00 39.55  ? 643 HOH A O   1 
HETATM 8918 O  O   . HOH U 6 .   ? 13.406  13.849  -2.034  1.00 32.61  ? 644 HOH A O   1 
HETATM 8919 O  O   . HOH U 6 .   ? 33.923  -17.130 2.711   1.00 28.98  ? 645 HOH A O   1 
HETATM 8920 O  O   . HOH U 6 .   ? 14.658  -12.197 29.432  1.00 22.76  ? 646 HOH A O   1 
HETATM 8921 O  O   . HOH U 6 .   ? 24.085  -2.813  33.099  1.00 33.20  ? 647 HOH A O   1 
HETATM 8922 O  O   . HOH U 6 .   ? 23.453  -9.673  32.539  1.00 26.27  ? 648 HOH A O   1 
HETATM 8923 O  O   . HOH U 6 .   ? 27.381  -9.280  -13.386 1.00 36.40  ? 649 HOH A O   1 
HETATM 8924 O  O   . HOH U 6 .   ? 27.305  -6.461  -11.498 1.00 49.12  ? 650 HOH A O   1 
HETATM 8925 O  O   . HOH U 6 .   ? 25.171  -4.961  31.508  1.00 35.63  ? 651 HOH A O   1 
HETATM 8926 O  O   . HOH U 6 .   ? 24.490  -20.620 11.747  1.00 36.81  ? 652 HOH A O   1 
HETATM 8927 O  O   . HOH U 6 .   ? 30.646  -17.590 -2.758  1.00 33.78  ? 653 HOH A O   1 
HETATM 8928 O  O   . HOH U 6 .   ? 12.743  19.009  13.074  1.00 36.10  ? 654 HOH A O   1 
HETATM 8929 O  O   . HOH U 6 .   ? 31.716  -17.041 -5.292  1.00 40.71  ? 655 HOH A O   1 
HETATM 8930 O  O   . HOH U 6 .   ? 17.190  -17.517 -5.522  1.00 42.45  ? 656 HOH A O   1 
HETATM 8931 O  O   . HOH U 6 .   ? 15.638  -5.280  33.967  1.00 34.91  ? 657 HOH A O   1 
HETATM 8932 O  O   . HOH U 6 .   ? 5.501   -13.032 15.619  1.00 24.27  ? 658 HOH A O   1 
HETATM 8933 O  O   . HOH U 6 .   ? 5.154   -7.204  1.013   1.00 22.77  ? 659 HOH A O   1 
HETATM 8934 O  O   . HOH U 6 .   ? 32.412  -14.871 28.199  1.00 34.01  ? 660 HOH A O   1 
HETATM 8935 O  O   . HOH U 6 .   ? 16.400  -16.028 7.832   1.00 23.10  ? 661 HOH A O   1 
HETATM 8936 O  O   . HOH U 6 .   ? 14.953  -13.674 25.475  1.00 30.31  ? 662 HOH A O   1 
HETATM 8937 O  O   . HOH U 6 .   ? 46.827  -8.483  8.991   1.00 43.46  ? 663 HOH A O   1 
HETATM 8938 O  O   . HOH U 6 .   ? 21.082  12.388  -2.374  1.00 33.12  ? 664 HOH A O   1 
HETATM 8939 O  O   . HOH U 6 .   ? 21.242  16.392  5.237   1.00 30.40  ? 665 HOH A O   1 
HETATM 8940 O  O   . HOH U 6 .   ? 15.197  4.886   -6.572  1.00 41.39  ? 666 HOH A O   1 
HETATM 8941 O  O   . HOH U 6 .   ? 4.112   13.682  22.441  1.00 36.15  ? 667 HOH A O   1 
HETATM 8942 O  O   . HOH U 6 .   ? 12.489  -10.538 30.062  1.00 23.99  ? 668 HOH A O   1 
HETATM 8943 O  O   . HOH U 6 .   ? 11.545  -12.883 26.004  1.00 33.11  ? 669 HOH A O   1 
HETATM 8944 O  O   . HOH U 6 .   ? 13.747  -17.086 6.463   1.00 39.99  ? 670 HOH A O   1 
HETATM 8945 O  O   . HOH U 6 .   ? 18.946  10.416  -4.456  1.00 28.55  ? 671 HOH A O   1 
HETATM 8946 O  O   . HOH U 6 .   ? 16.851  16.261  -1.140  1.00 40.10  ? 672 HOH A O   1 
HETATM 8947 O  O   . HOH U 6 .   ? 19.441  -11.135 33.698  1.00 26.83  ? 673 HOH A O   1 
HETATM 8948 O  O   . HOH U 6 .   ? 11.867  5.508   -4.541  1.00 35.95  ? 674 HOH A O   1 
HETATM 8949 O  O   . HOH U 6 .   ? 27.866  -20.808 27.807  1.00 48.87  ? 675 HOH A O   1 
HETATM 8950 O  O   . HOH U 6 .   ? 13.504  -13.509 23.150  1.00 27.50  ? 676 HOH A O   1 
HETATM 8951 O  O   . HOH U 6 .   ? 22.817  16.717  8.625   1.00 34.68  ? 677 HOH A O   1 
HETATM 8952 O  O   . HOH U 6 .   ? 18.421  6.777   -6.922  1.00 37.34  ? 678 HOH A O   1 
HETATM 8953 O  O   . HOH U 6 .   ? 24.424  -7.259  32.759  1.00 37.99  ? 679 HOH A O   1 
HETATM 8954 O  O   . HOH U 6 .   ? 12.976  6.208   -8.304  1.00 31.96  ? 680 HOH A O   1 
HETATM 8955 O  O   . HOH V 6 .   ? -5.655  17.629  12.539  1.00 44.37  ? 401 HOH B O   1 
HETATM 8956 O  O   . HOH V 6 .   ? -14.700 1.458   23.281  1.00 30.20  ? 402 HOH B O   1 
HETATM 8957 O  O   . HOH V 6 .   ? -12.944 19.177  10.216  1.00 34.84  ? 403 HOH B O   1 
HETATM 8958 O  O   . HOH V 6 .   ? -13.934 8.154   -15.883 1.00 26.83  ? 404 HOH B O   1 
HETATM 8959 O  O   . HOH V 6 .   ? 4.063   8.096   18.465  1.00 29.07  ? 405 HOH B O   1 
HETATM 8960 O  O   . HOH V 6 .   ? -13.780 19.337  14.055  1.00 42.71  ? 406 HOH B O   1 
HETATM 8961 O  O   . HOH V 6 .   ? -0.198  16.949  -11.345 1.00 21.07  ? 407 HOH B O   1 
HETATM 8962 O  O   . HOH V 6 .   ? 6.409   1.022   22.100  1.00 41.02  ? 408 HOH B O   1 
HETATM 8963 O  O   . HOH V 6 .   ? -0.672  4.463   -16.649 1.00 20.69  ? 409 HOH B O   1 
HETATM 8964 O  O   . HOH V 6 .   ? -26.698 9.294   -2.973  1.00 30.32  ? 410 HOH B O   1 
HETATM 8965 O  O   . HOH V 6 .   ? -18.078 19.819  9.805   1.00 32.49  ? 411 HOH B O   1 
HETATM 8966 O  O   . HOH V 6 .   ? -27.207 -3.370  -5.918  1.00 26.06  ? 412 HOH B O   1 
HETATM 8967 O  O   . HOH V 6 .   ? 1.798   16.986  0.310   1.00 42.81  ? 413 HOH B O   1 
HETATM 8968 O  O   . HOH V 6 .   ? -0.353  -14.530 13.435  1.00 41.30  ? 414 HOH B O   1 
HETATM 8969 O  O   . HOH V 6 .   ? -26.266 8.847   16.521  1.00 21.14  ? 415 HOH B O   1 
HETATM 8970 O  O   . HOH V 6 .   ? 6.494   7.346   17.880  1.00 43.25  ? 416 HOH B O   1 
HETATM 8971 O  O   . HOH V 6 .   ? -16.695 -16.721 16.789  1.00 34.32  ? 417 HOH B O   1 
HETATM 8972 O  O   . HOH V 6 .   ? -1.907  -7.995  -9.194  1.00 22.32  ? 418 HOH B O   1 
HETATM 8973 O  O   . HOH V 6 .   ? -19.612 -7.175  -11.726 1.00 30.00  ? 419 HOH B O   1 
HETATM 8974 O  O   . HOH V 6 .   ? -2.785  5.295   3.790   1.00 9.83   ? 420 HOH B O   1 
HETATM 8975 O  O   . HOH V 6 .   ? -12.750 -2.127  -11.934 1.00 31.19  ? 421 HOH B O   1 
HETATM 8976 O  O   . HOH V 6 .   ? -21.536 -9.932  9.727   1.00 34.14  ? 422 HOH B O   1 
HETATM 8977 O  O   . HOH V 6 .   ? -27.830 6.904   19.616  1.00 33.70  ? 423 HOH B O   1 
HETATM 8978 O  O   . HOH V 6 .   ? -7.829  4.816   -0.355  1.00 13.99  ? 424 HOH B O   1 
HETATM 8979 O  O   . HOH V 6 .   ? -20.708 -11.080 5.298   1.00 32.98  ? 425 HOH B O   1 
HETATM 8980 O  O   . HOH V 6 .   ? -8.662  19.080  -15.233 1.00 38.70  ? 426 HOH B O   1 
HETATM 8981 O  O   . HOH V 6 .   ? -5.793  -12.554 11.784  1.00 17.39  ? 427 HOH B O   1 
HETATM 8982 O  O   . HOH V 6 .   ? 3.854   11.539  -14.389 1.00 38.31  ? 428 HOH B O   1 
HETATM 8983 O  O   . HOH V 6 .   ? -4.416  11.479  -15.109 1.00 15.64  ? 429 HOH B O   1 
HETATM 8984 O  O   . HOH V 6 .   ? -4.163  16.248  -11.395 1.00 13.89  ? 430 HOH B O   1 
HETATM 8985 O  O   . HOH V 6 .   ? -12.996 -3.517  26.259  1.00 36.87  ? 431 HOH B O   1 
HETATM 8986 O  O   . HOH V 6 .   ? 1.282   0.677   -15.909 1.00 38.09  ? 432 HOH B O   1 
HETATM 8987 O  O   . HOH V 6 .   ? -29.915 -4.209  -0.813  1.00 18.76  ? 433 HOH B O   1 
HETATM 8988 O  O   . HOH V 6 .   ? -16.957 11.482  1.692   1.00 29.64  ? 434 HOH B O   1 
HETATM 8989 O  O   . HOH V 6 .   ? 0.915   18.298  -14.135 1.00 21.41  ? 435 HOH B O   1 
HETATM 8990 O  O   . HOH V 6 .   ? -29.812 4.986   16.990  1.00 44.68  ? 436 HOH B O   1 
HETATM 8991 O  O   . HOH V 6 .   ? -5.497  -11.541 -15.091 1.00 33.40  ? 437 HOH B O   1 
HETATM 8992 O  O   . HOH V 6 .   ? -17.149 11.434  4.701   1.00 32.75  ? 438 HOH B O   1 
HETATM 8993 O  O   . HOH V 6 .   ? -7.409  -7.450  28.072  1.00 26.04  ? 439 HOH B O   1 
HETATM 8994 O  O   . HOH V 6 .   ? -3.615  19.426  -20.225 1.00 31.05  ? 440 HOH B O   1 
HETATM 8995 O  O   . HOH V 6 .   ? -10.514 14.552  -14.117 1.00 15.12  ? 441 HOH B O   1 
HETATM 8996 O  O   . HOH V 6 .   ? -17.584 10.296  -14.399 1.00 43.76  ? 442 HOH B O   1 
HETATM 8997 O  O   . HOH V 6 .   ? -3.015  -12.799 15.301  1.00 26.78  ? 443 HOH B O   1 
HETATM 8998 O  O   . HOH V 6 .   ? -27.195 -9.884  1.395   1.00 23.36  ? 444 HOH B O   1 
HETATM 8999 O  O   . HOH V 6 .   ? -16.541 -12.449 25.746  1.00 24.91  ? 445 HOH B O   1 
HETATM 9000 O  O   . HOH V 6 .   ? 5.937   -9.271  13.399  1.00 15.46  ? 446 HOH B O   1 
HETATM 9001 O  O   . HOH V 6 .   ? 4.317   -2.492  -10.979 1.00 46.65  ? 447 HOH B O   1 
HETATM 9002 O  O   . HOH V 6 .   ? -9.577  8.481   -20.682 1.00 21.43  ? 448 HOH B O   1 
HETATM 9003 O  O   . HOH V 6 .   ? -21.226 -5.215  21.758  1.00 25.58  ? 449 HOH B O   1 
HETATM 9004 O  O   . HOH V 6 .   ? -14.691 -13.442 24.060  1.00 27.17  ? 450 HOH B O   1 
HETATM 9005 O  O   . HOH V 6 .   ? -8.302  -16.339 9.623   1.00 37.23  ? 451 HOH B O   1 
HETATM 9006 O  O   . HOH V 6 .   ? 5.117   16.008  13.532  1.00 25.10  ? 452 HOH B O   1 
HETATM 9007 O  O   . HOH V 6 .   ? -10.751 3.066   -2.655  1.00 13.20  ? 453 HOH B O   1 
HETATM 9008 O  O   . HOH V 6 .   ? -24.597 -2.149  -6.476  1.00 19.37  ? 454 HOH B O   1 
HETATM 9009 O  O   . HOH V 6 .   ? 6.874   -11.437 17.246  1.00 19.64  ? 455 HOH B O   1 
HETATM 9010 O  O   . HOH V 6 .   ? -24.030 -7.808  20.039  1.00 33.11  ? 456 HOH B O   1 
HETATM 9011 O  O   . HOH V 6 .   ? 1.651   6.765   -8.202  1.00 16.02  ? 457 HOH B O   1 
HETATM 9012 O  O   . HOH V 6 .   ? 7.858   11.889  14.785  1.00 21.29  ? 458 HOH B O   1 
HETATM 9013 O  O   . HOH V 6 .   ? -3.418  2.598   21.239  1.00 21.05  ? 459 HOH B O   1 
HETATM 9014 O  O   . HOH V 6 .   ? 5.207   6.462   0.920   1.00 10.36  ? 460 HOH B O   1 
HETATM 9015 O  O   . HOH V 6 .   ? -13.181 -17.347 6.395   1.00 34.25  ? 461 HOH B O   1 
HETATM 9016 O  O   . HOH V 6 .   ? -12.908 10.812  -2.739  1.00 15.00  ? 462 HOH B O   1 
HETATM 9017 O  O   . HOH V 6 .   ? -13.992 0.405   14.958  1.00 10.45  ? 463 HOH B O   1 
HETATM 9018 O  O   . HOH V 6 .   ? -14.058 -14.659 5.721   1.00 14.81  ? 464 HOH B O   1 
HETATM 9019 O  O   . HOH V 6 .   ? -12.073 -13.591 -11.391 1.00 15.20  ? 465 HOH B O   1 
HETATM 9020 O  O   . HOH V 6 .   ? 9.204   7.078   -2.219  1.00 35.03  ? 466 HOH B O   1 
HETATM 9021 O  O   . HOH V 6 .   ? -23.703 -8.878  14.421  1.00 35.59  ? 467 HOH B O   1 
HETATM 9022 O  O   . HOH V 6 .   ? 3.701   -2.096  13.864  1.00 12.26  ? 468 HOH B O   1 
HETATM 9023 O  O   . HOH V 6 .   ? -2.823  -5.175  -4.218  1.00 10.21  ? 469 HOH B O   1 
HETATM 9024 O  O   . HOH V 6 .   ? 7.249   -10.938 24.212  1.00 34.29  ? 470 HOH B O   1 
HETATM 9025 O  O   . HOH V 6 .   ? -27.716 -4.150  8.407   1.00 16.44  ? 471 HOH B O   1 
HETATM 9026 O  O   . HOH V 6 .   ? 9.049   7.328   8.448   1.00 13.07  ? 472 HOH B O   1 
HETATM 9027 O  O   . HOH V 6 .   ? -3.795  12.643  -18.285 1.00 17.90  ? 473 HOH B O   1 
HETATM 9028 O  O   . HOH V 6 .   ? -8.617  -8.086  -14.531 1.00 14.75  ? 474 HOH B O   1 
HETATM 9029 O  O   . HOH V 6 .   ? 4.324   13.042  -18.328 1.00 28.72  ? 475 HOH B O   1 
HETATM 9030 O  O   . HOH V 6 .   ? -20.050 -12.200 -2.598  1.00 27.76  ? 476 HOH B O   1 
HETATM 9031 O  O   . HOH V 6 .   ? -6.345  -3.497  -16.706 1.00 31.59  ? 477 HOH B O   1 
HETATM 9032 O  O   . HOH V 6 .   ? 5.820   12.440  -4.302  1.00 15.92  ? 478 HOH B O   1 
HETATM 9033 O  O   . HOH V 6 .   ? -23.155 9.644   6.393   1.00 16.46  ? 479 HOH B O   1 
HETATM 9034 O  O   . HOH V 6 .   ? 3.651   3.558   -2.601  1.00 22.34  ? 480 HOH B O   1 
HETATM 9035 O  O   . HOH V 6 .   ? -16.698 2.818   21.932  1.00 24.94  ? 481 HOH B O   1 
HETATM 9036 O  O   . HOH V 6 .   ? -22.064 1.530   18.622  1.00 19.01  ? 482 HOH B O   1 
HETATM 9037 O  O   . HOH V 6 .   ? 4.607   17.198  3.425   1.00 30.70  ? 483 HOH B O   1 
HETATM 9038 O  O   . HOH V 6 .   ? -10.257 -8.887  8.217   1.00 10.29  ? 484 HOH B O   1 
HETATM 9039 O  O   . HOH V 6 .   ? -7.629  -15.632 -7.878  1.00 12.17  ? 485 HOH B O   1 
HETATM 9040 O  O   . HOH V 6 .   ? -17.401 -12.613 3.246   1.00 22.62  ? 486 HOH B O   1 
HETATM 9041 O  O   . HOH V 6 .   ? -20.625 -11.877 0.854   1.00 33.26  ? 487 HOH B O   1 
HETATM 9042 O  O   . HOH V 6 .   ? 4.309   6.568   14.208  1.00 11.61  ? 488 HOH B O   1 
HETATM 9043 O  O   . HOH V 6 .   ? -1.728  16.700  10.893  1.00 12.45  ? 489 HOH B O   1 
HETATM 9044 O  O   . HOH V 6 .   ? -21.587 -8.643  -8.633  1.00 17.91  ? 490 HOH B O   1 
HETATM 9045 O  O   . HOH V 6 .   ? 1.026   6.755   20.877  1.00 30.25  ? 491 HOH B O   1 
HETATM 9046 O  O   . HOH V 6 .   ? -29.301 2.416   5.491   1.00 33.92  ? 492 HOH B O   1 
HETATM 9047 O  O   . HOH V 6 .   ? -0.410  0.591   26.762  1.00 44.56  ? 493 HOH B O   1 
HETATM 9048 O  O   . HOH V 6 .   ? -16.442 9.820   20.466  1.00 28.53  ? 494 HOH B O   1 
HETATM 9049 O  O   . HOH V 6 .   ? -1.248  -0.162  -12.490 1.00 21.52  ? 495 HOH B O   1 
HETATM 9050 O  O   . HOH V 6 .   ? -17.059 -10.386 20.163  1.00 15.28  ? 496 HOH B O   1 
HETATM 9051 O  O   . HOH V 6 .   ? 1.336   14.557  -11.282 1.00 13.71  ? 497 HOH B O   1 
HETATM 9052 O  O   . HOH V 6 .   ? -26.741 -6.779  -1.812  1.00 19.09  ? 498 HOH B O   1 
HETATM 9053 O  O   . HOH V 6 .   ? 8.074   4.739   5.147   1.00 9.22   ? 499 HOH B O   1 
HETATM 9054 O  O   . HOH V 6 .   ? -20.471 -9.419  14.917  1.00 20.76  ? 500 HOH B O   1 
HETATM 9055 O  O   . HOH V 6 .   ? -20.243 -11.699 8.055   1.00 25.84  ? 501 HOH B O   1 
HETATM 9056 O  O   . HOH V 6 .   ? -27.041 -6.207  6.552   1.00 17.32  ? 502 HOH B O   1 
HETATM 9057 O  O   . HOH V 6 .   ? 1.754   -1.465  5.683   1.00 9.53   ? 503 HOH B O   1 
HETATM 9058 O  O   . HOH V 6 .   ? 4.949   -9.567  -12.188 1.00 27.34  ? 504 HOH B O   1 
HETATM 9059 O  O   . HOH V 6 .   ? -18.383 -8.060  15.983  1.00 17.88  ? 505 HOH B O   1 
HETATM 9060 O  O   . HOH V 6 .   ? 0.250   -13.681 8.630   1.00 34.89  ? 506 HOH B O   1 
HETATM 9061 O  O   . HOH V 6 .   ? 5.299   5.686   7.671   1.00 10.75  ? 507 HOH B O   1 
HETATM 9062 O  O   . HOH V 6 .   ? -13.292 -6.650  -11.214 1.00 15.94  ? 508 HOH B O   1 
HETATM 9063 O  O   . HOH V 6 .   ? -1.968  20.607  8.026   1.00 33.09  ? 509 HOH B O   1 
HETATM 9064 O  O   . HOH V 6 .   ? 5.581   -7.944  -1.428  1.00 31.37  ? 510 HOH B O   1 
HETATM 9065 O  O   . HOH V 6 .   ? -14.017 -15.319 28.445  1.00 25.65  ? 511 HOH B O   1 
HETATM 9066 O  O   . HOH V 6 .   ? 5.218   19.922  10.815  1.00 18.78  ? 512 HOH B O   1 
HETATM 9067 O  O   . HOH V 6 .   ? 3.789   -2.211  22.518  1.00 24.25  ? 513 HOH B O   1 
HETATM 9068 O  O   . HOH V 6 .   ? -22.913 -2.000  -8.625  1.00 16.54  ? 514 HOH B O   1 
HETATM 9069 O  O   . HOH V 6 .   ? -32.012 5.349   -8.071  1.00 32.62  ? 515 HOH B O   1 
HETATM 9070 O  O   . HOH V 6 .   ? -0.858  12.146  15.997  1.00 15.46  ? 516 HOH B O   1 
HETATM 9071 O  O   . HOH V 6 .   ? -10.506 13.683  1.928   1.00 22.76  ? 517 HOH B O   1 
HETATM 9072 O  O   . HOH V 6 .   ? -23.915 0.813   21.279  1.00 27.36  ? 518 HOH B O   1 
HETATM 9073 O  O   . HOH V 6 .   ? -5.636  1.709   -9.744  1.00 10.07  ? 519 HOH B O   1 
HETATM 9074 O  O   . HOH V 6 .   ? 4.017   15.011  1.713   1.00 28.38  ? 520 HOH B O   1 
HETATM 9075 O  O   . HOH V 6 .   ? -21.216 10.459  3.300   1.00 33.12  ? 521 HOH B O   1 
HETATM 9076 O  O   . HOH V 6 .   ? -9.649  20.524  13.829  1.00 40.23  ? 522 HOH B O   1 
HETATM 9077 O  O   . HOH V 6 .   ? -8.582  8.791   19.844  1.00 25.28  ? 523 HOH B O   1 
HETATM 9078 O  O   . HOH V 6 .   ? -1.069  14.269  -4.641  1.00 32.16  ? 524 HOH B O   1 
HETATM 9079 O  O   . HOH V 6 .   ? -10.615 18.036  -8.758  1.00 29.12  ? 525 HOH B O   1 
HETATM 9080 O  O   . HOH V 6 .   ? -10.688 7.813   2.424   1.00 14.39  ? 526 HOH B O   1 
HETATM 9081 O  O   . HOH V 6 .   ? -6.150  -16.607 5.416   1.00 29.40  ? 527 HOH B O   1 
HETATM 9082 O  O   . HOH V 6 .   ? 6.582   3.422   9.067   1.00 8.44   ? 528 HOH B O   1 
HETATM 9083 O  O   . HOH V 6 .   ? 4.178   -4.925  -0.040  1.00 36.99  ? 529 HOH B O   1 
HETATM 9084 O  O   . HOH V 6 .   ? -16.969 -10.799 1.127   1.00 12.83  ? 530 HOH B O   1 
HETATM 9085 O  O   . HOH V 6 .   ? -17.851 -3.973  27.033  1.00 28.37  ? 531 HOH B O   1 
HETATM 9086 O  O   . HOH V 6 .   ? -9.869  17.079  10.504  1.00 39.14  ? 532 HOH B O   1 
HETATM 9087 O  O   . HOH V 6 .   ? 2.213   7.405   -14.601 1.00 33.24  ? 533 HOH B O   1 
HETATM 9088 O  O   . HOH V 6 .   ? -11.988 -17.122 21.633  1.00 39.90  ? 534 HOH B O   1 
HETATM 9089 O  O   . HOH V 6 .   ? -3.719  2.456   -11.939 1.00 12.34  ? 535 HOH B O   1 
HETATM 9090 O  O   . HOH V 6 .   ? -1.528  14.658  16.860  1.00 23.60  ? 536 HOH B O   1 
HETATM 9091 O  O   . HOH V 6 .   ? -3.213  -12.436 -1.124  1.00 19.57  ? 537 HOH B O   1 
HETATM 9092 O  O   . HOH V 6 .   ? 6.470   4.929   13.715  1.00 11.53  ? 538 HOH B O   1 
HETATM 9093 O  O   . HOH V 6 .   ? -30.826 7.486   -4.376  1.00 29.67  ? 539 HOH B O   1 
HETATM 9094 O  O   . HOH V 6 .   ? -16.397 -5.256  -12.740 1.00 22.11  ? 540 HOH B O   1 
HETATM 9095 O  O   . HOH V 6 .   ? 2.820   -13.252 15.846  1.00 16.60  ? 541 HOH B O   1 
HETATM 9096 O  O   . HOH V 6 .   ? -11.149 2.294   -14.747 1.00 28.13  ? 542 HOH B O   1 
HETATM 9097 O  O   . HOH V 6 .   ? 4.172   10.139  -6.788  1.00 17.93  ? 543 HOH B O   1 
HETATM 9098 O  O   . HOH V 6 .   ? -0.457  -13.237 22.205  1.00 31.77  ? 544 HOH B O   1 
HETATM 9099 O  O   . HOH V 6 .   ? -3.544  14.137  -6.562  1.00 32.66  ? 545 HOH B O   1 
HETATM 9100 O  O   . HOH V 6 .   ? -2.694  -0.294  25.250  1.00 22.62  ? 546 HOH B O   1 
HETATM 9101 O  O   . HOH V 6 .   ? 2.142   5.303   -5.722  1.00 14.89  ? 547 HOH B O   1 
HETATM 9102 O  O   . HOH V 6 .   ? -14.464 -14.014 0.710   1.00 18.93  ? 548 HOH B O   1 
HETATM 9103 O  O   . HOH V 6 .   ? -8.484  4.763   -3.102  1.00 13.86  ? 549 HOH B O   1 
HETATM 9104 O  O   . HOH V 6 .   ? -19.693 -16.079 10.047  1.00 26.29  ? 550 HOH B O   1 
HETATM 9105 O  O   . HOH V 6 .   ? 0.577   8.254   -4.517  1.00 17.70  ? 551 HOH B O   1 
HETATM 9106 O  O   . HOH V 6 .   ? -10.589 -10.637 29.645  1.00 23.07  ? 552 HOH B O   1 
HETATM 9107 O  O   . HOH V 6 .   ? 1.600   9.198   -6.926  1.00 14.47  ? 553 HOH B O   1 
HETATM 9108 O  O   . HOH V 6 .   ? -5.615  2.320   -16.841 1.00 36.05  ? 554 HOH B O   1 
HETATM 9109 O  O   . HOH V 6 .   ? 4.787   9.349   14.383  1.00 14.83  ? 555 HOH B O   1 
HETATM 9110 O  O   . HOH V 6 .   ? 2.129   6.234   -12.372 1.00 20.25  ? 556 HOH B O   1 
HETATM 9111 O  O   . HOH V 6 .   ? -12.744 -0.527  22.675  1.00 19.31  ? 557 HOH B O   1 
HETATM 9112 O  O   . HOH V 6 .   ? -21.919 4.606   -12.294 1.00 37.61  ? 558 HOH B O   1 
HETATM 9113 O  O   . HOH V 6 .   ? -27.497 7.412   -12.127 1.00 32.95  ? 559 HOH B O   1 
HETATM 9114 O  O   . HOH V 6 .   ? 1.255   -10.362 -10.153 1.00 38.16  ? 560 HOH B O   1 
HETATM 9115 O  O   . HOH V 6 .   ? -23.283 11.420  -0.983  1.00 30.01  ? 561 HOH B O   1 
HETATM 9116 O  O   . HOH V 6 .   ? 4.849   -5.173  8.697   1.00 33.90  ? 562 HOH B O   1 
HETATM 9117 O  O   . HOH V 6 .   ? -17.580 12.988  -12.852 1.00 39.32  ? 563 HOH B O   1 
HETATM 9118 O  O   . HOH V 6 .   ? -30.528 -3.316  9.864   1.00 21.98  ? 564 HOH B O   1 
HETATM 9119 O  O   . HOH V 6 .   ? -29.370 8.430   6.443   1.00 34.04  ? 565 HOH B O   1 
HETATM 9120 O  O   . HOH V 6 .   ? 4.185   8.313   7.677   1.00 10.40  ? 566 HOH B O   1 
HETATM 9121 O  O   . HOH V 6 .   ? -24.251 15.195  17.238  1.00 58.60  ? 567 HOH B O   1 
HETATM 9122 O  O   . HOH V 6 .   ? -14.621 11.190  3.689   1.00 19.43  ? 568 HOH B O   1 
HETATM 9123 O  O   . HOH V 6 .   ? -9.307  -1.709  -14.451 1.00 18.58  ? 569 HOH B O   1 
HETATM 9124 O  O   . HOH V 6 .   ? -14.791 13.688  -7.219  1.00 31.76  ? 570 HOH B O   1 
HETATM 9125 O  O   . HOH V 6 .   ? -1.882  -11.368 -3.259  1.00 16.05  ? 571 HOH B O   1 
HETATM 9126 O  O   . HOH V 6 .   ? -1.353  6.061   -4.907  1.00 12.61  ? 572 HOH B O   1 
HETATM 9127 O  O   . HOH V 6 .   ? -5.883  -15.387 13.169  1.00 32.42  ? 573 HOH B O   1 
HETATM 9128 O  O   . HOH V 6 .   ? -14.357 -10.960 23.854  1.00 23.29  ? 574 HOH B O   1 
HETATM 9129 O  O   . HOH V 6 .   ? -5.462  6.133   -0.260  1.00 16.75  ? 575 HOH B O   1 
HETATM 9130 O  O   . HOH V 6 .   ? -4.042  -12.771 25.699  1.00 30.66  ? 576 HOH B O   1 
HETATM 9131 O  O   . HOH V 6 .   ? -20.213 12.829  7.730   1.00 44.61  ? 577 HOH B O   1 
HETATM 9132 O  O   . HOH V 6 .   ? -15.802 -8.573  -13.234 1.00 29.15  ? 578 HOH B O   1 
HETATM 9133 O  O   . HOH V 6 .   ? -25.387 -7.429  12.679  1.00 23.91  ? 579 HOH B O   1 
HETATM 9134 O  O   . HOH V 6 .   ? -29.877 -3.013  6.965   1.00 24.28  ? 580 HOH B O   1 
HETATM 9135 O  O   . HOH V 6 .   ? -4.728  0.364   21.799  1.00 19.49  ? 581 HOH B O   1 
HETATM 9136 O  O   . HOH V 6 .   ? -13.383 -11.975 11.580  1.00 12.15  ? 582 HOH B O   1 
HETATM 9137 O  O   . HOH V 6 .   ? 11.490  14.525  0.035   1.00 25.80  ? 583 HOH B O   1 
HETATM 9138 O  O   . HOH V 6 .   ? -24.250 9.222   -1.580  1.00 18.72  ? 584 HOH B O   1 
HETATM 9139 O  O   . HOH V 6 .   ? 3.027   -3.430  16.237  1.00 22.09  ? 585 HOH B O   1 
HETATM 9140 O  O   . HOH V 6 .   ? -5.790  14.650  3.212   1.00 22.34  ? 586 HOH B O   1 
HETATM 9141 O  O   . HOH V 6 .   ? -4.845  -12.739 22.298  1.00 39.31  ? 587 HOH B O   1 
HETATM 9142 O  O   . HOH V 6 .   ? 4.383   -1.963  6.451   1.00 16.22  ? 588 HOH B O   1 
HETATM 9143 O  O   . HOH V 6 .   ? 8.751   8.955   1.896   1.00 16.18  ? 589 HOH B O   1 
HETATM 9144 O  O   . HOH V 6 .   ? 4.235   -2.158  -3.261  1.00 28.77  ? 590 HOH B O   1 
HETATM 9145 O  O   . HOH V 6 .   ? -32.881 -3.580  -2.007  1.00 27.54  ? 591 HOH B O   1 
HETATM 9146 O  O   . HOH V 6 .   ? -3.393  7.658   -3.730  1.00 15.18  ? 592 HOH B O   1 
HETATM 9147 O  O   . HOH V 6 .   ? -26.274 -9.598  5.895   1.00 23.01  ? 593 HOH B O   1 
HETATM 9148 O  O   . HOH V 6 .   ? -1.888  11.975  -5.120  1.00 19.54  ? 594 HOH B O   1 
HETATM 9149 O  O   . HOH V 6 .   ? -0.822  16.378  -8.802  1.00 25.51  ? 595 HOH B O   1 
HETATM 9150 O  O   . HOH V 6 .   ? -19.574 -13.594 14.360  1.00 20.81  ? 596 HOH B O   1 
HETATM 9151 O  O   . HOH V 6 .   ? -26.707 10.540  5.036   1.00 30.45  ? 597 HOH B O   1 
HETATM 9152 O  O   . HOH V 6 .   ? -29.439 7.550   -1.502  1.00 31.83  ? 598 HOH B O   1 
HETATM 9153 O  O   . HOH V 6 .   ? 6.766   -13.575 20.038  1.00 35.74  ? 599 HOH B O   1 
HETATM 9154 O  O   . HOH V 6 .   ? 4.296   -9.101  2.950   1.00 20.50  ? 600 HOH B O   1 
HETATM 9155 O  O   . HOH V 6 .   ? 4.297   3.648   -5.907  1.00 17.03  ? 601 HOH B O   1 
HETATM 9156 O  O   . HOH V 6 .   ? -14.748 -14.561 -2.620  1.00 16.45  ? 602 HOH B O   1 
HETATM 9157 O  O   . HOH V 6 .   ? -9.370  16.912  -16.179 1.00 29.06  ? 603 HOH B O   1 
HETATM 9158 O  O   . HOH V 6 .   ? -22.843 7.103   -12.534 1.00 32.96  ? 604 HOH B O   1 
HETATM 9159 O  O   . HOH V 6 .   ? -8.342  11.051  0.669   1.00 20.12  ? 605 HOH B O   1 
HETATM 9160 O  O   . HOH V 6 .   ? -14.241 14.437  -16.292 1.00 40.33  ? 606 HOH B O   1 
HETATM 9161 O  O   . HOH V 6 .   ? 6.898   -1.108  17.465  1.00 22.27  ? 607 HOH B O   1 
HETATM 9162 O  O   . HOH V 6 .   ? -5.219  16.328  1.174   1.00 52.16  ? 608 HOH B O   1 
HETATM 9163 O  O   . HOH V 6 .   ? 0.548   13.460  19.308  1.00 30.00  ? 609 HOH B O   1 
HETATM 9164 O  O   . HOH V 6 .   ? -30.808 6.661   11.336  1.00 40.05  ? 610 HOH B O   1 
HETATM 9165 O  O   . HOH V 6 .   ? -13.327 13.049  -0.937  1.00 28.54  ? 611 HOH B O   1 
HETATM 9166 O  O   . HOH V 6 .   ? 2.706   6.800   16.743  1.00 22.63  ? 612 HOH B O   1 
HETATM 9167 O  O   . HOH V 6 .   ? -5.416  15.139  -4.935  1.00 27.06  ? 613 HOH B O   1 
HETATM 9168 O  O   . HOH V 6 .   ? -20.190 -13.230 11.477  1.00 28.06  ? 614 HOH B O   1 
HETATM 9169 O  O   . HOH V 6 .   ? -8.838  -20.482 -0.871  1.00 18.50  ? 615 HOH B O   1 
HETATM 9170 O  O   . HOH V 6 .   ? -26.991 9.413   12.535  1.00 29.50  ? 616 HOH B O   1 
HETATM 9171 O  O   . HOH V 6 .   ? -6.731  15.532  16.082  1.00 34.63  ? 617 HOH B O   1 
HETATM 9172 O  O   . HOH V 6 .   ? 3.681   -16.205 18.225  1.00 32.87  ? 618 HOH B O   1 
HETATM 9173 O  O   . HOH V 6 .   ? -15.135 -0.219  -14.030 1.00 36.66  ? 619 HOH B O   1 
HETATM 9174 O  O   . HOH V 6 .   ? 7.868   -3.072  3.450   1.00 23.05  ? 620 HOH B O   1 
HETATM 9175 O  O   . HOH V 6 .   ? 3.154   21.376  9.347   1.00 22.85  ? 621 HOH B O   1 
HETATM 9176 O  O   . HOH V 6 .   ? -30.780 2.461   2.107   1.00 24.82  ? 622 HOH B O   1 
HETATM 9177 O  O   . HOH V 6 .   ? -12.025 21.480  12.174  1.00 39.37  ? 623 HOH B O   1 
HETATM 9178 O  O   . HOH V 6 .   ? -15.497 -3.268  25.620  1.00 43.34  ? 624 HOH B O   1 
HETATM 9179 O  O   . HOH V 6 .   ? -27.232 -6.079  -4.886  1.00 26.38  ? 625 HOH B O   1 
HETATM 9180 O  O   . HOH V 6 .   ? -18.486 14.876  7.180   1.00 32.02  ? 626 HOH B O   1 
HETATM 9181 O  O   . HOH V 6 .   ? -25.546 2.744   19.714  1.00 40.48  ? 627 HOH B O   1 
HETATM 9182 O  O   . HOH V 6 .   ? -2.975  -11.909 1.068   1.00 25.17  ? 628 HOH B O   1 
HETATM 9183 O  O   . HOH V 6 .   ? -3.152  1.946   -14.605 1.00 31.51  ? 629 HOH B O   1 
HETATM 9184 O  O   . HOH V 6 .   ? -1.833  9.919   -3.268  1.00 24.77  ? 630 HOH B O   1 
HETATM 9185 O  O   . HOH V 6 .   ? -24.790 -1.021  -11.484 1.00 27.24  ? 631 HOH B O   1 
HETATM 9186 O  O   . HOH V 6 .   ? 12.400  17.565  0.286   1.00 43.77  ? 632 HOH B O   1 
HETATM 9187 O  O   . HOH V 6 .   ? -30.325 5.206   2.226   1.00 41.90  ? 633 HOH B O   1 
HETATM 9188 O  O   . HOH V 6 .   ? 7.756   1.592   19.759  1.00 30.95  ? 634 HOH B O   1 
HETATM 9189 O  O   . HOH V 6 .   ? -14.609 17.249  19.759  1.00 37.13  ? 635 HOH B O   1 
HETATM 9190 O  O   . HOH V 6 .   ? -33.508 3.175   2.635   1.00 27.24  ? 636 HOH B O   1 
HETATM 9191 O  O   . HOH V 6 .   ? -0.566  -12.473 15.348  1.00 31.32  ? 637 HOH B O   1 
HETATM 9192 O  O   . HOH V 6 .   ? -0.894  -12.908 4.037   1.00 38.21  ? 638 HOH B O   1 
HETATM 9193 O  O   . HOH V 6 .   ? -24.731 8.584   1.154   1.00 27.78  ? 639 HOH B O   1 
HETATM 9194 O  O   . HOH V 6 .   ? -21.428 -6.198  -9.951  1.00 24.21  ? 640 HOH B O   1 
HETATM 9195 O  O   . HOH V 6 .   ? -28.316 8.964   14.978  1.00 50.62  ? 641 HOH B O   1 
HETATM 9196 O  O   . HOH V 6 .   ? -3.511  16.087  -8.695  1.00 43.52  ? 642 HOH B O   1 
HETATM 9197 O  O   . HOH V 6 .   ? -8.811  19.432  16.736  1.00 45.99  ? 643 HOH B O   1 
HETATM 9198 O  O   . HOH V 6 .   ? -13.146 -16.885 23.824  1.00 50.62  ? 644 HOH B O   1 
HETATM 9199 O  O   . HOH V 6 .   ? -6.936  21.559  -15.139 1.00 43.29  ? 645 HOH B O   1 
HETATM 9200 O  O   . HOH V 6 .   ? -0.210  -13.020 -4.484  1.00 26.23  ? 646 HOH B O   1 
HETATM 9201 O  O   . HOH V 6 .   ? -4.511  -18.220 3.940   1.00 43.25  ? 647 HOH B O   1 
HETATM 9202 O  O   . HOH V 6 .   ? -22.528 11.953  6.768   1.00 33.79  ? 648 HOH B O   1 
HETATM 9203 O  O   . HOH V 6 .   ? -18.814 15.902  22.471  1.00 37.25  ? 649 HOH B O   1 
HETATM 9204 O  O   . HOH V 6 .   ? -17.490 -14.172 -2.319  1.00 26.03  ? 650 HOH B O   1 
HETATM 9205 O  O   . HOH V 6 .   ? 12.609  11.594  -3.741  1.00 25.89  ? 651 HOH B O   1 
HETATM 9206 O  O   . HOH V 6 .   ? -0.677  20.282  -0.310  1.00 42.59  ? 652 HOH B O   1 
HETATM 9207 O  O   . HOH V 6 .   ? -7.542  13.775  1.071   1.00 25.34  ? 653 HOH B O   1 
HETATM 9208 O  O   . HOH V 6 .   ? 1.384   -0.092  -12.118 1.00 35.24  ? 654 HOH B O   1 
HETATM 9209 O  O   . HOH V 6 .   ? 6.042   -2.623  1.189   1.00 35.48  ? 655 HOH B O   1 
HETATM 9210 O  O   . HOH V 6 .   ? -11.803 19.848  17.574  1.00 40.80  ? 656 HOH B O   1 
HETATM 9211 O  O   . HOH V 6 .   ? 7.648   7.661   -0.135  1.00 19.25  ? 657 HOH B O   1 
HETATM 9212 O  O   . HOH V 6 .   ? 5.667   3.008   -3.546  1.00 33.06  ? 658 HOH B O   1 
HETATM 9213 O  O   . HOH V 6 .   ? -10.603 16.442  -6.470  1.00 34.29  ? 659 HOH B O   1 
HETATM 9214 O  O   . HOH V 6 .   ? -7.533  15.575  -1.134  1.00 46.20  ? 660 HOH B O   1 
HETATM 9215 O  O   . HOH V 6 .   ? -23.217 -4.381  -10.033 1.00 30.67  ? 661 HOH B O   1 
HETATM 9216 O  O   . HOH V 6 .   ? 1.032   22.794  9.820   1.00 35.09  ? 662 HOH B O   1 
HETATM 9217 O  O   . HOH V 6 .   ? 3.903   14.913  -10.427 1.00 33.83  ? 663 HOH B O   1 
HETATM 9218 O  O   . HOH V 6 .   ? -15.470 5.328   26.754  1.00 32.40  ? 664 HOH B O   1 
HETATM 9219 O  O   . HOH V 6 .   ? -29.345 -7.477  6.248   1.00 29.45  ? 665 HOH B O   1 
HETATM 9220 O  O   . HOH V 6 .   ? -11.290 -8.175  -14.905 1.00 18.19  ? 666 HOH B O   1 
HETATM 9221 O  O   . HOH V 6 .   ? -12.720 -8.863  -12.625 1.00 23.30  ? 667 HOH B O   1 
HETATM 9222 O  O   . HOH V 6 .   ? -21.433 -11.977 15.737  1.00 27.51  ? 668 HOH B O   1 
HETATM 9223 O  O   . HOH V 6 .   ? -7.942  -5.689  -15.821 1.00 22.66  ? 669 HOH B O   1 
HETATM 9224 O  O   . HOH V 6 .   ? -29.520 7.442   1.097   1.00 33.06  ? 670 HOH B O   1 
HETATM 9225 O  O   . HOH V 6 .   ? -18.420 -11.650 24.014  1.00 40.44  ? 671 HOH B O   1 
HETATM 9226 O  O   . HOH V 6 .   ? 4.849   -12.285 24.359  1.00 39.81  ? 672 HOH B O   1 
HETATM 9227 O  O   . HOH V 6 .   ? -13.620 -4.728  -13.004 1.00 21.84  ? 673 HOH B O   1 
HETATM 9228 O  O   . HOH V 6 .   ? -19.926 -9.903  -12.457 1.00 26.95  ? 674 HOH B O   1 
HETATM 9229 O  O   . HOH V 6 .   ? -0.700  -11.782 -9.243  1.00 33.75  ? 675 HOH B O   1 
HETATM 9230 O  O   . HOH V 6 .   ? -10.053 20.553  -7.896  1.00 45.08  ? 676 HOH B O   1 
HETATM 9231 O  O   . HOH V 6 .   ? 0.438   6.647   -16.646 1.00 29.98  ? 677 HOH B O   1 
HETATM 9232 O  O   . HOH V 6 .   ? 2.075   -15.906 16.547  1.00 27.62  ? 678 HOH B O   1 
HETATM 9233 O  O   . HOH V 6 .   ? -11.639 -1.651  24.733  1.00 31.33  ? 679 HOH B O   1 
HETATM 9234 O  O   . HOH V 6 .   ? -11.920 -0.443  -14.000 1.00 25.61  ? 680 HOH B O   1 
HETATM 9235 O  O   . HOH V 6 .   ? -10.728 16.722  -19.066 1.00 27.97  ? 681 HOH B O   1 
HETATM 9236 O  O   . HOH V 6 .   ? -3.875  15.563  18.177  1.00 37.13  ? 682 HOH B O   1 
HETATM 9237 O  O   . HOH V 6 .   ? -15.568 -14.577 3.499   1.00 28.47  ? 683 HOH B O   1 
HETATM 9238 O  O   . HOH V 6 .   ? -17.891 -12.650 21.230  1.00 29.87  ? 684 HOH B O   1 
HETATM 9239 O  O   . HOH V 6 .   ? -19.319 -16.442 -4.120  1.00 31.29  ? 685 HOH B O   1 
HETATM 9240 O  O   . HOH V 6 .   ? -29.134 -6.009  -2.694  1.00 28.66  ? 686 HOH B O   1 
HETATM 9241 O  O   . HOH V 6 .   ? -20.782 -10.697 -10.019 1.00 22.71  ? 687 HOH B O   1 
HETATM 9242 O  O   . HOH V 6 .   ? -22.986 -12.758 0.838   1.00 39.76  ? 688 HOH B O   1 
HETATM 9243 O  O   . HOH V 6 .   ? -4.230  -13.831 9.700   1.00 31.44  ? 689 HOH B O   1 
HETATM 9244 O  O   . HOH V 6 .   ? -24.197 -9.462  -8.229  1.00 38.01  ? 690 HOH B O   1 
HETATM 9245 O  O   . HOH V 6 .   ? 2.505   -11.334 -12.075 1.00 32.92  ? 691 HOH B O   1 
HETATM 9246 O  O   . HOH V 6 .   ? 3.596   6.307   -9.976  1.00 30.73  ? 692 HOH B O   1 
HETATM 9247 O  O   . HOH V 6 .   ? -13.234 -11.758 -13.130 1.00 20.76  ? 693 HOH B O   1 
HETATM 9248 O  O   . HOH V 6 .   ? -2.974  19.022  10.220  1.00 30.54  ? 694 HOH B O   1 
HETATM 9249 O  O   . HOH V 6 .   ? -27.301 9.327   1.495   1.00 33.69  ? 695 HOH B O   1 
HETATM 9250 O  O   . HOH V 6 .   ? 10.555  9.811   -7.088  1.00 35.66  ? 696 HOH B O   1 
HETATM 9251 O  O   . HOH V 6 .   ? -10.002 -3.960  -15.930 1.00 25.04  ? 697 HOH B O   1 
HETATM 9252 O  O   . HOH V 6 .   ? -19.109 -15.956 15.718  1.00 32.53  ? 698 HOH B O   1 
HETATM 9253 O  O   . HOH V 6 .   ? -3.032  11.030  21.152  1.00 32.52  ? 699 HOH B O   1 
HETATM 9254 O  O   . HOH V 6 .   ? -7.488  -10.117 -16.077 1.00 17.27  ? 700 HOH B O   1 
HETATM 9255 O  O   . HOH V 6 .   ? 12.887  11.829  -6.324  1.00 34.59  ? 701 HOH B O   1 
HETATM 9256 O  O   . HOH V 6 .   ? -2.278  -14.361 8.735   1.00 35.85  ? 702 HOH B O   1 
HETATM 9257 O  O   . HOH V 6 .   ? -9.467  -11.627 -17.095 1.00 33.12  ? 703 HOH B O   1 
HETATM 9258 O  O   . HOH V 6 .   ? -0.108  7.825   23.398  1.00 32.84  ? 704 HOH B O   1 
HETATM 9259 O  O   . HOH V 6 .   ? -3.513  3.956   23.711  1.00 31.35  ? 705 HOH B O   1 
HETATM 9260 O  O   . HOH V 6 .   ? -5.061  19.220  9.094   1.00 46.45  ? 706 HOH B O   1 
HETATM 9261 O  O   . HOH V 6 .   ? -7.645  20.542  9.681   1.00 33.54  ? 707 HOH B O   1 
HETATM 9262 O  O   . HOH V 6 .   ? -25.707 -5.846  -8.971  1.00 41.65  ? 708 HOH B O   1 
HETATM 9263 O  O   . HOH V 6 .   ? -12.156 -11.389 -15.370 1.00 53.40  ? 709 HOH B O   1 
HETATM 9264 O  O   . HOH V 6 .   ? -21.978 -12.925 -9.996  1.00 33.06  ? 710 HOH B O   1 
HETATM 9265 O  O   . HOH V 6 .   ? -12.369 -5.558  -15.370 1.00 27.79  ? 711 HOH B O   1 
HETATM 9266 O  O   . HOH V 6 .   ? -5.760  21.875  13.560  1.00 32.64  ? 712 HOH B O   1 
HETATM 9267 O  O   . HOH V 6 .   ? -2.093  9.740   23.505  1.00 34.32  ? 713 HOH B O   1 
HETATM 9268 O  O   . HOH W 6 .   ? 19.819  1.097   -51.740 1.00 24.40  ? 401 HOH C O   1 
HETATM 9269 O  O   . HOH W 6 .   ? 43.140  -22.202 -34.895 1.00 63.32  ? 402 HOH C O   1 
HETATM 9270 O  O   . HOH W 6 .   ? 47.732  6.901   -23.030 1.00 34.14  ? 403 HOH C O   1 
HETATM 9271 O  O   . HOH W 6 .   ? 46.656  -11.893 -40.827 1.00 25.91  ? 404 HOH C O   1 
HETATM 9272 O  O   . HOH W 6 .   ? 33.476  22.084  -35.636 1.00 40.55  ? 405 HOH C O   1 
HETATM 9273 O  O   . HOH W 6 .   ? 54.458  -14.178 -26.260 1.00 61.56  ? 406 HOH C O   1 
HETATM 9274 O  O   . HOH W 6 .   ? 48.065  -14.370 -30.153 1.00 38.00  ? 407 HOH C O   1 
HETATM 9275 O  O   . HOH W 6 .   ? 58.778  -2.734  -30.504 1.00 32.38  ? 408 HOH C O   1 
HETATM 9276 O  O   . HOH W 6 .   ? 41.137  13.831  -37.517 1.00 23.29  ? 409 HOH C O   1 
HETATM 9277 O  O   . HOH W 6 .   ? 50.160  -9.954  -46.306 1.00 35.91  ? 410 HOH C O   1 
HETATM 9278 O  O   . HOH W 6 .   ? 21.800  17.527  -28.202 1.00 38.55  ? 411 HOH C O   1 
HETATM 9279 O  O   . HOH W 6 .   ? 44.199  -5.564  -50.584 1.00 25.23  ? 412 HOH C O   1 
HETATM 9280 O  O   . HOH W 6 .   ? 56.223  5.758   -30.669 1.00 36.63  ? 413 HOH C O   1 
HETATM 9281 O  O   . HOH W 6 .   ? 35.707  -17.612 -14.829 1.00 32.76  ? 414 HOH C O   1 
HETATM 9282 O  O   . HOH W 6 .   ? 56.463  7.644   -37.903 1.00 31.01  ? 415 HOH C O   1 
HETATM 9283 O  O   . HOH W 6 .   ? 26.180  4.999   -24.447 1.00 29.17  ? 416 HOH C O   1 
HETATM 9284 O  O   . HOH W 6 .   ? 42.461  -3.827  -12.127 1.00 33.76  ? 417 HOH C O   1 
HETATM 9285 O  O   . HOH W 6 .   ? 52.925  -6.157  -18.838 1.00 28.38  ? 418 HOH C O   1 
HETATM 9286 O  O   . HOH W 6 .   ? 33.946  11.120  -11.158 1.00 43.00  ? 419 HOH C O   1 
HETATM 9287 O  O   . HOH W 6 .   ? 33.371  -1.771  -49.332 1.00 22.75  ? 420 HOH C O   1 
HETATM 9288 O  O   . HOH W 6 .   ? 32.953  4.867   -30.742 1.00 13.85  ? 421 HOH C O   1 
HETATM 9289 O  O   . HOH W 6 .   ? 37.128  -20.863 -43.357 1.00 47.70  ? 422 HOH C O   1 
HETATM 9290 O  O   . HOH W 6 .   ? 25.415  6.303   -34.830 1.00 9.97   ? 423 HOH C O   1 
HETATM 9291 O  O   . HOH W 6 .   ? 31.538  -16.656 -30.898 1.00 35.50  ? 424 HOH C O   1 
HETATM 9292 O  O   . HOH W 6 .   ? 22.710  -6.585  -31.669 1.00 20.38  ? 425 HOH C O   1 
HETATM 9293 O  O   . HOH W 6 .   ? 29.199  -8.430  -17.552 1.00 24.78  ? 426 HOH C O   1 
HETATM 9294 O  O   . HOH W 6 .   ? 54.422  -11.204 -23.344 1.00 36.31  ? 427 HOH C O   1 
HETATM 9295 O  O   . HOH W 6 .   ? 57.029  3.878   -42.272 1.00 20.88  ? 428 HOH C O   1 
HETATM 9296 O  O   . HOH W 6 .   ? 35.480  -8.928  -11.642 1.00 27.12  ? 429 HOH C O   1 
HETATM 9297 O  O   . HOH W 6 .   ? 33.177  -13.763 -37.290 1.00 20.33  ? 430 HOH C O   1 
HETATM 9298 O  O   . HOH W 6 .   ? 36.194  -13.663 -55.058 1.00 37.95  ? 431 HOH C O   1 
HETATM 9299 O  O   . HOH W 6 .   ? 54.832  -10.670 -31.615 1.00 27.43  ? 432 HOH C O   1 
HETATM 9300 O  O   . HOH W 6 .   ? 20.942  -2.787  -51.429 1.00 33.86  ? 433 HOH C O   1 
HETATM 9301 O  O   . HOH W 6 .   ? 26.884  -8.781  -16.175 1.00 24.55  ? 434 HOH C O   1 
HETATM 9302 O  O   . HOH W 6 .   ? 27.728  -10.501 -26.929 1.00 22.67  ? 435 HOH C O   1 
HETATM 9303 O  O   . HOH W 6 .   ? 24.326  12.945  -42.567 1.00 14.83  ? 436 HOH C O   1 
HETATM 9304 O  O   . HOH W 6 .   ? 25.693  8.050   -28.228 1.00 16.25  ? 437 HOH C O   1 
HETATM 9305 O  O   . HOH W 6 .   ? 52.697  5.119   -49.287 1.00 40.01  ? 438 HOH C O   1 
HETATM 9306 O  O   . HOH W 6 .   ? 30.110  -5.129  -22.330 1.00 16.38  ? 439 HOH C O   1 
HETATM 9307 O  O   . HOH W 6 .   ? 56.091  -8.984  -33.428 1.00 28.73  ? 440 HOH C O   1 
HETATM 9308 O  O   . HOH W 6 .   ? 28.848  3.163   -43.680 1.00 16.75  ? 441 HOH C O   1 
HETATM 9309 O  O   . HOH W 6 .   ? 27.712  16.011  -41.390 1.00 13.48  ? 442 HOH C O   1 
HETATM 9310 O  O   . HOH W 6 .   ? 24.700  -3.771  -44.954 1.00 34.73  ? 443 HOH C O   1 
HETATM 9311 O  O   . HOH W 6 .   ? 22.031  -8.635  -39.373 1.00 50.98  ? 444 HOH C O   1 
HETATM 9312 O  O   . HOH W 6 .   ? 27.488  -1.020  -32.496 1.00 10.35  ? 445 HOH C O   1 
HETATM 9313 O  O   . HOH W 6 .   ? 32.279  1.894   -14.885 1.00 24.54  ? 446 HOH C O   1 
HETATM 9314 O  O   . HOH W 6 .   ? 42.968  -19.747 -28.035 1.00 40.20  ? 447 HOH C O   1 
HETATM 9315 O  O   . HOH W 6 .   ? 28.861  -14.837 -16.397 1.00 42.11  ? 448 HOH C O   1 
HETATM 9316 O  O   . HOH W 6 .   ? 35.704  -19.131 -37.651 1.00 38.04  ? 449 HOH C O   1 
HETATM 9317 O  O   . HOH W 6 .   ? 35.579  16.859  -41.927 1.00 31.92  ? 450 HOH C O   1 
HETATM 9318 O  O   . HOH W 6 .   ? 41.924  -8.196  -55.222 1.00 25.37  ? 451 HOH C O   1 
HETATM 9319 O  O   . HOH W 6 .   ? 48.872  -13.829 -34.930 1.00 36.06  ? 452 HOH C O   1 
HETATM 9320 O  O   . HOH W 6 .   ? 43.576  -2.598  -40.815 1.00 12.76  ? 453 HOH C O   1 
HETATM 9321 O  O   . HOH W 6 .   ? 22.698  -5.451  -41.281 1.00 22.54  ? 454 HOH C O   1 
HETATM 9322 O  O   . HOH W 6 .   ? 43.781  3.985   -44.678 1.00 23.63  ? 455 HOH C O   1 
HETATM 9323 O  O   . HOH W 6 .   ? 47.334  -15.426 -32.834 1.00 38.53  ? 456 HOH C O   1 
HETATM 9324 O  O   . HOH W 6 .   ? 51.738  -2.811  -44.092 1.00 24.70  ? 457 HOH C O   1 
HETATM 9325 O  O   . HOH W 6 .   ? 25.990  -3.406  -48.515 1.00 25.50  ? 458 HOH C O   1 
HETATM 9326 O  O   . HOH W 6 .   ? 28.859  18.127  -31.981 1.00 17.50  ? 459 HOH C O   1 
HETATM 9327 O  O   . HOH W 6 .   ? 42.607  -19.685 -18.903 1.00 38.93  ? 460 HOH C O   1 
HETATM 9328 O  O   . HOH W 6 .   ? 48.928  2.653   -49.204 1.00 37.12  ? 461 HOH C O   1 
HETATM 9329 O  O   . HOH W 6 .   ? 26.353  6.779   -41.489 1.00 11.40  ? 462 HOH C O   1 
HETATM 9330 O  O   . HOH W 6 .   ? 38.860  -14.536 -13.792 1.00 33.46  ? 463 HOH C O   1 
HETATM 9331 O  O   . HOH W 6 .   ? 29.919  -14.249 -28.252 1.00 26.25  ? 464 HOH C O   1 
HETATM 9332 O  O   . HOH W 6 .   ? 51.037  -5.662  -16.724 1.00 36.68  ? 465 HOH C O   1 
HETATM 9333 O  O   . HOH W 6 .   ? 22.520  6.709   -32.386 1.00 10.89  ? 466 HOH C O   1 
HETATM 9334 O  O   . HOH W 6 .   ? 60.356  -2.671  -35.749 1.00 32.83  ? 467 HOH C O   1 
HETATM 9335 O  O   . HOH W 6 .   ? 25.545  -2.032  -40.937 1.00 14.37  ? 468 HOH C O   1 
HETATM 9336 O  O   . HOH W 6 .   ? 24.520  -3.212  -27.333 1.00 32.64  ? 469 HOH C O   1 
HETATM 9337 O  O   . HOH W 6 .   ? 53.819  -4.229  -46.661 1.00 30.03  ? 470 HOH C O   1 
HETATM 9338 O  O   . HOH W 6 .   ? 35.846  19.402  -36.078 1.00 33.37  ? 471 HOH C O   1 
HETATM 9339 O  O   . HOH W 6 .   ? 37.424  8.462   -47.795 1.00 30.81  ? 472 HOH C O   1 
HETATM 9340 O  O   . HOH W 6 .   ? 34.396  1.162   -16.808 1.00 21.18  ? 473 HOH C O   1 
HETATM 9341 O  O   . HOH W 6 .   ? 34.314  -17.038 -17.280 1.00 32.13  ? 474 HOH C O   1 
HETATM 9342 O  O   . HOH W 6 .   ? 20.537  -10.351 -30.124 1.00 18.02  ? 475 HOH C O   1 
HETATM 9343 O  O   . HOH W 6 .   ? 45.148  -14.213 -45.058 1.00 22.64  ? 476 HOH C O   1 
HETATM 9344 O  O   . HOH W 6 .   ? 38.097  -10.759 -33.664 1.00 14.57  ? 477 HOH C O   1 
HETATM 9345 O  O   . HOH W 6 .   ? 26.248  -3.713  -42.911 1.00 18.91  ? 478 HOH C O   1 
HETATM 9346 O  O   . HOH W 6 .   ? 47.725  8.354   -27.605 1.00 42.04  ? 479 HOH C O   1 
HETATM 9347 O  O   . HOH W 6 .   ? 38.149  13.450  -31.043 1.00 36.30  ? 480 HOH C O   1 
HETATM 9348 O  O   . HOH W 6 .   ? 44.381  -15.501 -28.547 1.00 36.18  ? 481 HOH C O   1 
HETATM 9349 O  O   . HOH W 6 .   ? 32.186  2.246   -43.970 1.00 18.57  ? 482 HOH C O   1 
HETATM 9350 O  O   . HOH W 6 .   ? 29.305  5.880   -47.558 1.00 22.17  ? 483 HOH C O   1 
HETATM 9351 O  O   . HOH W 6 .   ? 48.648  -12.037 -16.646 1.00 35.90  ? 484 HOH C O   1 
HETATM 9352 O  O   . HOH W 6 .   ? 35.789  5.893   -27.048 1.00 24.65  ? 485 HOH C O   1 
HETATM 9353 O  O   . HOH W 6 .   ? 28.053  7.218   -19.069 1.00 35.68  ? 486 HOH C O   1 
HETATM 9354 O  O   . HOH W 6 .   ? 56.803  9.022   -40.616 1.00 32.02  ? 487 HOH C O   1 
HETATM 9355 O  O   . HOH W 6 .   ? 20.702  17.627  -30.158 1.00 23.94  ? 488 HOH C O   1 
HETATM 9356 O  O   . HOH W 6 .   ? 23.724  4.494   -36.205 1.00 8.50   ? 489 HOH C O   1 
HETATM 9357 O  O   . HOH W 6 .   ? 33.190  7.042   -22.727 1.00 31.81  ? 490 HOH C O   1 
HETATM 9358 O  O   . HOH W 6 .   ? 21.208  13.378  -35.787 1.00 12.81  ? 491 HOH C O   1 
HETATM 9359 O  O   . HOH W 6 .   ? 28.493  -10.847 -22.639 1.00 23.21  ? 492 HOH C O   1 
HETATM 9360 O  O   . HOH W 6 .   ? 33.994  13.319  -44.440 1.00 17.79  ? 493 HOH C O   1 
HETATM 9361 O  O   . HOH W 6 .   ? 23.836  -4.765  -36.209 1.00 18.36  ? 494 HOH C O   1 
HETATM 9362 O  O   . HOH W 6 .   ? 49.246  -5.229  -49.919 1.00 40.97  ? 495 HOH C O   1 
HETATM 9363 O  O   . HOH W 6 .   ? 34.537  15.758  -38.615 1.00 13.57  ? 496 HOH C O   1 
HETATM 9364 O  O   . HOH W 6 .   ? 22.726  -14.041 -36.376 1.00 35.45  ? 497 HOH C O   1 
HETATM 9365 O  O   . HOH W 6 .   ? 42.418  -4.286  -48.691 1.00 23.02  ? 498 HOH C O   1 
HETATM 9366 O  O   . HOH W 6 .   ? 27.090  6.380   -14.414 1.00 39.78  ? 499 HOH C O   1 
HETATM 9367 O  O   . HOH W 6 .   ? 51.096  8.268   -33.847 1.00 33.95  ? 500 HOH C O   1 
HETATM 9368 O  O   . HOH W 6 .   ? 39.912  17.967  -41.330 1.00 32.21  ? 501 HOH C O   1 
HETATM 9369 O  O   . HOH W 6 .   ? 32.752  11.013  -43.483 1.00 11.61  ? 502 HOH C O   1 
HETATM 9370 O  O   . HOH W 6 .   ? 40.391  -11.854 -55.607 1.00 28.70  ? 503 HOH C O   1 
HETATM 9371 O  O   . HOH W 6 .   ? 44.172  -13.578 -26.407 1.00 25.85  ? 504 HOH C O   1 
HETATM 9372 O  O   . HOH W 6 .   ? 40.648  -16.911 -30.862 1.00 25.76  ? 505 HOH C O   1 
HETATM 9373 O  O   . HOH W 6 .   ? 27.074  9.148   -35.029 1.00 11.89  ? 506 HOH C O   1 
HETATM 9374 O  O   . HOH W 6 .   ? 25.196  -2.132  -23.754 1.00 27.39  ? 507 HOH C O   1 
HETATM 9375 O  O   . HOH W 6 .   ? 22.809  0.020   -28.208 1.00 29.37  ? 508 HOH C O   1 
HETATM 9376 O  O   . HOH W 6 .   ? 38.444  4.637   -45.562 1.00 17.96  ? 509 HOH C O   1 
HETATM 9377 O  O   . HOH W 6 .   ? 60.111  2.741   -20.850 1.00 40.25  ? 510 HOH C O   1 
HETATM 9378 O  O   . HOH W 6 .   ? 30.676  -10.673 -16.738 1.00 33.85  ? 511 HOH C O   1 
HETATM 9379 O  O   . HOH W 6 .   ? 53.486  5.828   -31.939 1.00 26.07  ? 512 HOH C O   1 
HETATM 9380 O  O   . HOH W 6 .   ? 26.447  10.984  -45.498 1.00 20.30  ? 513 HOH C O   1 
HETATM 9381 O  O   . HOH W 6 .   ? 35.987  -1.286  -48.699 1.00 21.06  ? 514 HOH C O   1 
HETATM 9382 O  O   . HOH W 6 .   ? 24.503  -0.881  -33.141 1.00 18.95  ? 515 HOH C O   1 
HETATM 9383 O  O   . HOH W 6 .   ? 26.948  -13.841 -34.952 1.00 20.55  ? 516 HOH C O   1 
HETATM 9384 O  O   . HOH W 6 .   ? 53.630  -11.746 -37.718 1.00 31.36  ? 517 HOH C O   1 
HETATM 9385 O  O   . HOH W 6 .   ? 54.038  5.205   -23.700 1.00 30.13  ? 518 HOH C O   1 
HETATM 9386 O  O   . HOH W 6 .   ? 51.682  6.939   -28.964 1.00 35.62  ? 519 HOH C O   1 
HETATM 9387 O  O   . HOH W 6 .   ? 26.701  9.522   -41.950 1.00 11.93  ? 520 HOH C O   1 
HETATM 9388 O  O   . HOH W 6 .   ? 45.280  8.127   -29.355 1.00 49.50  ? 521 HOH C O   1 
HETATM 9389 O  O   . HOH W 6 .   ? 22.678  -0.763  -44.482 1.00 26.91  ? 522 HOH C O   1 
HETATM 9390 O  O   . HOH W 6 .   ? 58.398  -8.292  -31.986 1.00 33.95  ? 523 HOH C O   1 
HETATM 9391 O  O   . HOH W 6 .   ? 46.626  -17.445 -39.069 1.00 29.69  ? 524 HOH C O   1 
HETATM 9392 O  O   . HOH W 6 .   ? 21.018  0.937   -46.001 1.00 33.65  ? 525 HOH C O   1 
HETATM 9393 O  O   . HOH W 6 .   ? 30.090  -12.683 -24.164 1.00 18.67  ? 526 HOH C O   1 
HETATM 9394 O  O   . HOH W 6 .   ? 26.004  14.282  -23.398 1.00 32.60  ? 527 HOH C O   1 
HETATM 9395 O  O   . HOH W 6 .   ? 24.718  18.827  -29.001 1.00 34.53  ? 528 HOH C O   1 
HETATM 9396 O  O   . HOH W 6 .   ? 22.984  -8.788  -17.453 1.00 36.74  ? 529 HOH C O   1 
HETATM 9397 O  O   . HOH W 6 .   ? 28.329  15.997  -29.634 1.00 27.37  ? 530 HOH C O   1 
HETATM 9398 O  O   . HOH W 6 .   ? 22.898  10.856  -29.451 1.00 17.03  ? 531 HOH C O   1 
HETATM 9399 O  O   . HOH W 6 .   ? 38.735  -19.385 -16.750 1.00 42.30  ? 532 HOH C O   1 
HETATM 9400 O  O   . HOH W 6 .   ? 28.978  3.301   -46.435 1.00 20.09  ? 533 HOH C O   1 
HETATM 9401 O  O   . HOH W 6 .   ? 46.821  -1.145  -47.964 1.00 27.40  ? 534 HOH C O   1 
HETATM 9402 O  O   . HOH W 6 .   ? 23.963  5.355   -40.839 1.00 14.08  ? 535 HOH C O   1 
HETATM 9403 O  O   . HOH W 6 .   ? 30.768  6.320   -21.745 1.00 31.20  ? 536 HOH C O   1 
HETATM 9404 O  O   . HOH W 6 .   ? 31.776  12.507  -46.669 1.00 21.25  ? 537 HOH C O   1 
HETATM 9405 O  O   . HOH W 6 .   ? 27.288  6.090   -21.267 1.00 34.09  ? 538 HOH C O   1 
HETATM 9406 O  O   . HOH W 6 .   ? 40.915  -16.846 -22.988 1.00 25.71  ? 539 HOH C O   1 
HETATM 9407 O  O   . HOH W 6 .   ? 39.205  -19.980 -46.872 1.00 34.54  ? 540 HOH C O   1 
HETATM 9408 O  O   . HOH W 6 .   ? 29.139  -0.553  -14.582 1.00 28.38  ? 541 HOH C O   1 
HETATM 9409 O  O   . HOH W 6 .   ? 40.761  -14.418 -36.722 1.00 16.08  ? 542 HOH C O   1 
HETATM 9410 O  O   . HOH W 6 .   ? 59.135  -8.429  -35.284 1.00 32.52  ? 543 HOH C O   1 
HETATM 9411 O  O   . HOH W 6 .   ? 25.032  4.889   -21.349 1.00 30.61  ? 544 HOH C O   1 
HETATM 9412 O  O   . HOH W 6 .   ? 29.780  8.823   -22.507 1.00 26.35  ? 545 HOH C O   1 
HETATM 9413 O  O   . HOH W 6 .   ? 38.958  16.445  -39.237 1.00 26.27  ? 546 HOH C O   1 
HETATM 9414 O  O   . HOH W 6 .   ? 24.235  -9.428  -29.301 1.00 31.74  ? 547 HOH C O   1 
HETATM 9415 O  O   . HOH W 6 .   ? 33.068  -14.803 -9.772  1.00 48.29  ? 548 HOH C O   1 
HETATM 9416 O  O   . HOH W 6 .   ? 39.048  13.436  -43.437 1.00 26.94  ? 549 HOH C O   1 
HETATM 9417 O  O   . HOH W 6 .   ? 47.198  -16.820 -36.109 1.00 36.20  ? 550 HOH C O   1 
HETATM 9418 O  O   . HOH W 6 .   ? 32.549  -2.417  -51.849 1.00 34.73  ? 551 HOH C O   1 
HETATM 9419 O  O   . HOH W 6 .   ? 25.156  4.205   -45.942 1.00 25.17  ? 552 HOH C O   1 
HETATM 9420 O  O   . HOH W 6 .   ? 45.416  16.574  -38.932 1.00 35.05  ? 553 HOH C O   1 
HETATM 9421 O  O   . HOH W 6 .   ? 39.878  -5.345  -49.729 1.00 33.31  ? 554 HOH C O   1 
HETATM 9422 O  O   . HOH W 6 .   ? 41.247  6.939   -47.152 1.00 31.56  ? 555 HOH C O   1 
HETATM 9423 O  O   . HOH W 6 .   ? 40.973  -16.542 -26.000 1.00 28.65  ? 556 HOH C O   1 
HETATM 9424 O  O   . HOH W 6 .   ? 44.494  13.797  -47.852 1.00 31.91  ? 557 HOH C O   1 
HETATM 9425 O  O   . HOH W 6 .   ? 19.636  15.272  -24.062 1.00 40.61  ? 558 HOH C O   1 
HETATM 9426 O  O   . HOH W 6 .   ? 47.457  -12.786 -53.509 1.00 23.98  ? 559 HOH C O   1 
HETATM 9427 O  O   . HOH W 6 .   ? 28.260  6.577   -43.977 1.00 18.16  ? 560 HOH C O   1 
HETATM 9428 O  O   . HOH W 6 .   ? 46.903  7.904   -11.906 1.00 31.56  ? 561 HOH C O   1 
HETATM 9429 O  O   . HOH W 6 .   ? 52.486  -4.981  -13.921 1.00 44.17  ? 562 HOH C O   1 
HETATM 9430 O  O   . HOH W 6 .   ? 41.089  6.418   -27.365 1.00 27.30  ? 563 HOH C O   1 
HETATM 9431 O  O   . HOH W 6 .   ? 33.053  -15.180 -47.340 1.00 35.52  ? 564 HOH C O   1 
HETATM 9432 O  O   . HOH W 6 .   ? 30.023  -11.915 -26.837 1.00 19.04  ? 565 HOH C O   1 
HETATM 9433 O  O   . HOH W 6 .   ? 48.316  18.681  -40.978 1.00 50.52  ? 566 HOH C O   1 
HETATM 9434 O  O   . HOH W 6 .   ? 40.708  -8.044  -14.177 1.00 40.42  ? 567 HOH C O   1 
HETATM 9435 O  O   . HOH W 6 .   ? 28.016  -12.728 -30.297 1.00 29.23  ? 568 HOH C O   1 
HETATM 9436 O  O   . HOH W 6 .   ? 43.859  -19.996 -41.184 1.00 31.09  ? 569 HOH C O   1 
HETATM 9437 O  O   . HOH W 6 .   ? 54.455  -10.139 -19.908 1.00 56.58  ? 570 HOH C O   1 
HETATM 9438 O  O   . HOH W 6 .   ? 22.889  -0.934  -23.879 1.00 55.96  ? 571 HOH C O   1 
HETATM 9439 O  O   . HOH W 6 .   ? 57.338  5.236   -38.060 1.00 33.41  ? 572 HOH C O   1 
HETATM 9440 O  O   . HOH W 6 .   ? 21.257  -1.556  -30.102 1.00 25.69  ? 573 HOH C O   1 
HETATM 9441 O  O   . HOH W 6 .   ? 32.266  9.744   -23.164 1.00 29.17  ? 574 HOH C O   1 
HETATM 9442 O  O   . HOH W 6 .   ? 32.232  22.005  -37.741 1.00 30.79  ? 575 HOH C O   1 
HETATM 9443 O  O   . HOH W 6 .   ? 56.544  11.612  -42.601 1.00 45.90  ? 576 HOH C O   1 
HETATM 9444 O  O   . HOH W 6 .   ? 51.855  9.213   -15.260 1.00 48.78  ? 577 HOH C O   1 
HETATM 9445 O  O   . HOH W 6 .   ? 54.112  6.805   -27.955 1.00 33.56  ? 578 HOH C O   1 
HETATM 9446 O  O   . HOH W 6 .   ? 30.924  15.171  -44.509 1.00 36.96  ? 579 HOH C O   1 
HETATM 9447 O  O   . HOH W 6 .   ? 39.309  -10.570 -13.261 1.00 31.12  ? 580 HOH C O   1 
HETATM 9448 O  O   . HOH W 6 .   ? 43.714  -17.013 -22.828 1.00 37.31  ? 581 HOH C O   1 
HETATM 9449 O  O   . HOH W 6 .   ? 42.863  -5.806  -54.764 1.00 27.32  ? 582 HOH C O   1 
HETATM 9450 O  O   . HOH W 6 .   ? 28.334  15.128  -45.578 1.00 25.83  ? 583 HOH C O   1 
HETATM 9451 O  O   . HOH W 6 .   ? 45.103  -16.270 -24.874 1.00 32.51  ? 584 HOH C O   1 
HETATM 9452 O  O   . HOH W 6 .   ? 21.595  -4.102  -32.454 1.00 37.47  ? 585 HOH C O   1 
HETATM 9453 O  O   . HOH W 6 .   ? 31.503  -12.423 -12.671 1.00 38.06  ? 586 HOH C O   1 
HETATM 9454 O  O   . HOH W 6 .   ? 34.477  21.847  -38.488 1.00 32.39  ? 587 HOH C O   1 
HETATM 9455 O  O   . HOH W 6 .   ? 23.090  8.344   -28.015 1.00 19.22  ? 588 HOH C O   1 
HETATM 9456 O  O   . HOH W 6 .   ? 35.907  0.543   -50.713 1.00 46.45  ? 589 HOH C O   1 
HETATM 9457 O  O   . HOH W 6 .   ? 22.240  -4.025  -38.435 1.00 29.19  ? 590 HOH C O   1 
HETATM 9458 O  O   . HOH W 6 .   ? 38.221  -9.084  -10.923 1.00 34.87  ? 591 HOH C O   1 
HETATM 9459 O  O   . HOH W 6 .   ? 59.606  -2.064  -28.206 1.00 45.45  ? 592 HOH C O   1 
HETATM 9460 O  O   . HOH W 6 .   ? 45.427  -18.756 -21.357 1.00 35.63  ? 593 HOH C O   1 
HETATM 9461 O  O   . HOH W 6 .   ? 42.171  -16.723 -28.443 1.00 33.02  ? 594 HOH C O   1 
HETATM 9462 O  O   . HOH W 6 .   ? 38.562  -2.889  -48.983 1.00 31.11  ? 595 HOH C O   1 
HETATM 9463 O  O   . HOH W 6 .   ? 31.393  -16.185 -42.336 1.00 37.43  ? 596 HOH C O   1 
HETATM 9464 O  O   . HOH W 6 .   ? 29.586  -11.020 -14.028 1.00 30.42  ? 597 HOH C O   1 
HETATM 9465 O  O   . HOH W 6 .   ? 32.126  -16.773 -48.964 1.00 41.18  ? 598 HOH C O   1 
HETATM 9466 O  O   . HOH W 6 .   ? 45.600  -16.489 -46.118 1.00 39.90  ? 599 HOH C O   1 
HETATM 9467 O  O   . HOH W 6 .   ? 27.809  19.917  -30.394 1.00 47.16  ? 600 HOH C O   1 
HETATM 9468 O  O   . HOH W 6 .   ? 26.434  6.542   -45.791 1.00 26.18  ? 601 HOH C O   1 
HETATM 9469 O  O   . HOH W 6 .   ? 24.927  -15.294 -35.074 1.00 47.51  ? 602 HOH C O   1 
HETATM 9470 O  O   . HOH W 6 .   ? 36.235  13.382  -46.037 1.00 32.14  ? 603 HOH C O   1 
HETATM 9471 O  O   . HOH W 6 .   ? 31.283  -14.988 -35.683 1.00 31.54  ? 604 HOH C O   1 
HETATM 9472 O  O   . HOH W 6 .   ? 32.222  17.079  -44.687 1.00 39.98  ? 605 HOH C O   1 
HETATM 9473 O  O   . HOH W 6 .   ? 29.865  -12.776 -17.979 1.00 35.22  ? 606 HOH C O   1 
HETATM 9474 O  O   . HOH W 6 .   ? 50.607  -13.507 -16.705 1.00 39.49  ? 607 HOH C O   1 
HETATM 9475 O  O   . HOH W 6 .   ? 36.429  17.674  -38.684 1.00 31.80  ? 608 HOH C O   1 
HETATM 9476 O  O   . HOH W 6 .   ? 47.326  -14.209 -15.250 1.00 45.94  ? 609 HOH C O   1 
HETATM 9477 O  O   . HOH W 6 .   ? 19.451  15.789  -21.267 1.00 28.97  ? 610 HOH C O   1 
HETATM 9478 O  O   . HOH W 6 .   ? 34.743  9.079   -48.232 1.00 34.64  ? 611 HOH C O   1 
HETATM 9479 O  O   . HOH W 6 .   ? 30.210  5.897   -50.121 1.00 41.83  ? 612 HOH C O   1 
HETATM 9480 O  O   . HOH W 6 .   ? 33.960  18.608  -43.458 1.00 33.16  ? 613 HOH C O   1 
HETATM 9481 O  O   . HOH W 6 .   ? 34.164  11.478  -48.016 1.00 29.36  ? 614 HOH C O   1 
HETATM 9482 O  O   . HOH W 6 .   ? 28.651  -15.466 -36.246 1.00 34.12  ? 615 HOH C O   1 
HETATM 9483 O  O   . HOH W 6 .   ? 39.861  15.744  -32.307 1.00 33.70  ? 616 HOH C O   1 
HETATM 9484 O  O   . HOH W 6 .   ? 26.941  6.572   -48.146 1.00 39.87  ? 617 HOH C O   1 
HETATM 9485 O  O   . HOH W 6 .   ? 37.902  18.006  -35.372 1.00 37.72  ? 618 HOH C O   1 
HETATM 9486 O  O   . HOH W 6 .   ? 39.054  -6.790  -10.609 1.00 35.33  ? 619 HOH C O   1 
HETATM 9487 O  O   . HOH W 6 .   ? 33.363  7.635   -50.492 1.00 35.53  ? 620 HOH C O   1 
HETATM 9488 O  O   . HOH W 6 .   ? 33.237  20.989  -43.173 1.00 32.51  ? 621 HOH C O   1 
HETATM 9489 O  O   . HOH X 6 .   ? -11.741 -4.425  -32.288 1.00 35.54  ? 401 HOH D O   1 
HETATM 9490 O  O   . HOH X 6 .   ? 4.325   4.539   -45.949 1.00 19.63  ? 402 HOH D O   1 
HETATM 9491 O  O   . HOH X 6 .   ? -12.014 -3.761  -36.134 1.00 29.70  ? 403 HOH D O   1 
HETATM 9492 O  O   . HOH X 6 .   ? -14.198 4.652   -37.195 1.00 18.90  ? 404 HOH D O   1 
HETATM 9493 O  O   . HOH X 6 .   ? -7.887  -6.507  -28.015 1.00 38.74  ? 405 HOH D O   1 
HETATM 9494 O  O   . HOH X 6 .   ? 15.447  18.029  -54.524 1.00 32.98  ? 406 HOH D O   1 
HETATM 9495 O  O   . HOH X 6 .   ? -6.193  -9.041  -37.570 1.00 40.71  ? 407 HOH D O   1 
HETATM 9496 O  O   . HOH X 6 .   ? 21.326  18.484  -42.916 1.00 31.79  ? 408 HOH D O   1 
HETATM 9497 O  O   . HOH X 6 .   ? 23.119  13.674  -28.854 1.00 23.77  ? 409 HOH D O   1 
HETATM 9498 O  O   . HOH X 6 .   ? -6.348  15.640  -52.657 1.00 35.20  ? 410 HOH D O   1 
HETATM 9499 O  O   . HOH X 6 .   ? 0.238   -10.629 -18.452 1.00 40.44  ? 411 HOH D O   1 
HETATM 9500 O  O   . HOH X 6 .   ? 6.796   12.457  -42.756 1.00 49.62  ? 412 HOH D O   1 
HETATM 9501 O  O   . HOH X 6 .   ? -10.195 11.669  -26.301 1.00 15.23  ? 413 HOH D O   1 
HETATM 9502 O  O   . HOH X 6 .   ? -12.260 -1.976  -48.506 1.00 29.98  ? 414 HOH D O   1 
HETATM 9503 O  O   . HOH X 6 .   ? -2.653  -10.559 -39.397 1.00 21.39  ? 415 HOH D O   1 
HETATM 9504 O  O   . HOH X 6 .   ? -14.892 -2.271  -43.782 1.00 19.86  ? 416 HOH D O   1 
HETATM 9505 O  O   . HOH X 6 .   ? 14.250  19.609  -43.236 1.00 35.95  ? 417 HOH D O   1 
HETATM 9506 O  O   . HOH X 6 .   ? 1.728   7.858   -22.947 1.00 24.78  ? 418 HOH D O   1 
HETATM 9507 O  O   . HOH X 6 .   ? -5.987  -2.786  -21.354 1.00 26.30  ? 419 HOH D O   1 
HETATM 9508 O  O   . HOH X 6 .   ? 12.816  -6.818  -52.425 1.00 22.51  ? 420 HOH D O   1 
HETATM 9509 O  O   . HOH X 6 .   ? -2.696  11.028  -57.826 1.00 38.79  ? 421 HOH D O   1 
HETATM 9510 O  O   . HOH X 6 .   ? 1.037   -11.979 -14.163 1.00 32.80  ? 422 HOH D O   1 
HETATM 9511 O  O   . HOH X 6 .   ? -5.144  -5.924  -54.231 1.00 34.23  ? 423 HOH D O   1 
HETATM 9512 O  O   . HOH X 6 .   ? -3.205  22.315  -34.994 1.00 32.97  ? 424 HOH D O   1 
HETATM 9513 O  O   . HOH X 6 .   ? 17.013  18.580  -43.601 1.00 28.39  ? 425 HOH D O   1 
HETATM 9514 O  O   . HOH X 6 .   ? -12.456 -1.769  -34.040 1.00 16.41  ? 426 HOH D O   1 
HETATM 9515 O  O   . HOH X 6 .   ? 12.413  6.841   -39.587 1.00 10.15  ? 427 HOH D O   1 
HETATM 9516 O  O   . HOH X 6 .   ? 18.661  -2.622  -54.354 1.00 30.46  ? 428 HOH D O   1 
HETATM 9517 O  O   . HOH X 6 .   ? -15.478 5.620   -32.083 1.00 43.34  ? 429 HOH D O   1 
HETATM 9518 O  O   . HOH X 6 .   ? 15.078  -13.624 -30.909 1.00 38.70  ? 430 HOH D O   1 
HETATM 9519 O  O   . HOH X 6 .   ? -9.612  15.167  -30.999 1.00 29.90  ? 431 HOH D O   1 
HETATM 9520 O  O   . HOH X 6 .   ? -15.474 3.683   -51.386 1.00 42.53  ? 432 HOH D O   1 
HETATM 9521 O  O   . HOH X 6 .   ? -9.203  5.712   -22.052 1.00 47.39  ? 433 HOH D O   1 
HETATM 9522 O  O   . HOH X 6 .   ? -11.386 11.049  -45.801 1.00 36.97  ? 434 HOH D O   1 
HETATM 9523 O  O   . HOH X 6 .   ? 16.385  19.663  -57.076 1.00 35.50  ? 435 HOH D O   1 
HETATM 9524 O  O   . HOH X 6 .   ? 2.121   12.335  -46.375 1.00 25.98  ? 436 HOH D O   1 
HETATM 9525 O  O   . HOH X 6 .   ? 11.027  13.161  -58.627 1.00 16.43  ? 437 HOH D O   1 
HETATM 9526 O  O   . HOH X 6 .   ? -1.629  -4.657  -55.956 1.00 30.48  ? 438 HOH D O   1 
HETATM 9527 O  O   . HOH X 6 .   ? -12.040 -4.901  -44.397 1.00 21.20  ? 439 HOH D O   1 
HETATM 9528 O  O   . HOH X 6 .   ? 2.539   -11.972 -54.377 1.00 19.51  ? 440 HOH D O   1 
HETATM 9529 O  O   . HOH X 6 .   ? 9.015   -10.829 -31.278 1.00 17.66  ? 441 HOH D O   1 
HETATM 9530 O  O   . HOH X 6 .   ? 22.137  -9.806  -19.278 1.00 35.69  ? 442 HOH D O   1 
HETATM 9531 O  O   . HOH X 6 .   ? 2.521   -15.567 -29.774 1.00 24.17  ? 443 HOH D O   1 
HETATM 9532 O  O   . HOH X 6 .   ? 1.479   -15.359 -36.616 1.00 30.85  ? 444 HOH D O   1 
HETATM 9533 O  O   . HOH X 6 .   ? -7.772  3.719   -21.445 1.00 28.66  ? 445 HOH D O   1 
HETATM 9534 O  O   . HOH X 6 .   ? 20.106  15.870  -49.344 1.00 33.80  ? 446 HOH D O   1 
HETATM 9535 O  O   . HOH X 6 .   ? -7.863  13.372  -44.326 1.00 32.36  ? 447 HOH D O   1 
HETATM 9536 O  O   . HOH X 6 .   ? -5.908  4.244   -24.423 1.00 15.03  ? 448 HOH D O   1 
HETATM 9537 O  O   . HOH X 6 .   ? 23.414  1.493   -19.144 1.00 43.28  ? 449 HOH D O   1 
HETATM 9538 O  O   . HOH X 6 .   ? 20.561  -1.452  -40.013 1.00 26.23  ? 450 HOH D O   1 
HETATM 9539 O  O   . HOH X 6 .   ? -9.799  -0.436  -49.391 1.00 29.40  ? 451 HOH D O   1 
HETATM 9540 O  O   . HOH X 6 .   ? -5.265  19.696  -22.187 1.00 24.31  ? 452 HOH D O   1 
HETATM 9541 O  O   . HOH X 6 .   ? 3.613   -13.965 -39.325 1.00 36.08  ? 453 HOH D O   1 
HETATM 9542 O  O   . HOH X 6 .   ? 5.077   -0.623  -18.517 1.00 37.54  ? 454 HOH D O   1 
HETATM 9543 O  O   . HOH X 6 .   ? -5.290  -9.917  -34.925 1.00 30.56  ? 455 HOH D O   1 
HETATM 9544 O  O   . HOH X 6 .   ? 21.859  -9.928  -26.151 1.00 20.69  ? 456 HOH D O   1 
HETATM 9545 O  O   . HOH X 6 .   ? -1.525  -9.039  -16.956 1.00 19.71  ? 457 HOH D O   1 
HETATM 9546 O  O   . HOH X 6 .   ? -6.505  5.460   -55.885 1.00 37.37  ? 458 HOH D O   1 
HETATM 9547 O  O   . HOH X 6 .   ? 19.600  8.239   -29.403 1.00 11.62  ? 459 HOH D O   1 
HETATM 9548 O  O   . HOH X 6 .   ? 13.206  11.162  -46.734 1.00 24.12  ? 460 HOH D O   1 
HETATM 9549 O  O   . HOH X 6 .   ? 11.288  17.724  -54.734 1.00 22.05  ? 461 HOH D O   1 
HETATM 9550 O  O   . HOH X 6 .   ? 20.279  7.867   -42.638 1.00 11.72  ? 462 HOH D O   1 
HETATM 9551 O  O   . HOH X 6 .   ? 8.666   -15.084 -37.746 1.00 30.97  ? 463 HOH D O   1 
HETATM 9552 O  O   . HOH X 6 .   ? 19.612  -1.207  -46.714 1.00 42.55  ? 464 HOH D O   1 
HETATM 9553 O  O   . HOH X 6 .   ? 4.500   9.439   -41.155 1.00 22.29  ? 465 HOH D O   1 
HETATM 9554 O  O   . HOH X 6 .   ? 20.893  -7.733  -29.968 1.00 15.21  ? 466 HOH D O   1 
HETATM 9555 O  O   . HOH X 6 .   ? 24.248  8.840   -35.248 1.00 13.05  ? 467 HOH D O   1 
HETATM 9556 O  O   . HOH X 6 .   ? -5.455  -7.245  -27.932 1.00 21.66  ? 468 HOH D O   1 
HETATM 9557 O  O   . HOH X 6 .   ? 4.449   17.389  -18.054 1.00 37.76  ? 469 HOH D O   1 
HETATM 9558 O  O   . HOH X 6 .   ? -7.032  -7.107  -51.437 1.00 20.27  ? 470 HOH D O   1 
HETATM 9559 O  O   . HOH X 6 .   ? 9.635   7.925   -43.292 1.00 17.89  ? 471 HOH D O   1 
HETATM 9560 O  O   . HOH X 6 .   ? 5.814   8.466   -63.705 1.00 38.05  ? 472 HOH D O   1 
HETATM 9561 O  O   . HOH X 6 .   ? -6.729  10.972  -19.766 1.00 15.52  ? 473 HOH D O   1 
HETATM 9562 O  O   . HOH X 6 .   ? 0.680   -12.844 -37.068 1.00 14.80  ? 474 HOH D O   1 
HETATM 9563 O  O   . HOH X 6 .   ? 20.903  13.787  -47.866 1.00 17.25  ? 475 HOH D O   1 
HETATM 9564 O  O   . HOH X 6 .   ? 16.777  7.871   -51.622 1.00 18.37  ? 476 HOH D O   1 
HETATM 9565 O  O   . HOH X 6 .   ? 0.537   19.385  -21.908 1.00 32.11  ? 477 HOH D O   1 
HETATM 9566 O  O   . HOH X 6 .   ? -2.019  -14.485 -25.969 1.00 29.93  ? 478 HOH D O   1 
HETATM 9567 O  O   . HOH X 6 .   ? 16.772  0.103   -37.619 1.00 9.88   ? 479 HOH D O   1 
HETATM 9568 O  O   . HOH X 6 .   ? 11.623  15.199  -50.084 1.00 41.40  ? 480 HOH D O   1 
HETATM 9569 O  O   . HOH X 6 .   ? -5.410  -10.382 -45.372 1.00 26.56  ? 481 HOH D O   1 
HETATM 9570 O  O   . HOH X 6 .   ? 1.370   2.423   -28.222 1.00 10.51  ? 482 HOH D O   1 
HETATM 9571 O  O   . HOH X 6 .   ? 18.251  7.151   -27.354 1.00 15.57  ? 483 HOH D O   1 
HETATM 9572 O  O   . HOH X 6 .   ? 4.529   3.862   -58.701 1.00 26.79  ? 484 HOH D O   1 
HETATM 9573 O  O   . HOH X 6 .   ? 9.346   -10.329 -58.225 1.00 23.92  ? 485 HOH D O   1 
HETATM 9574 O  O   . HOH X 6 .   ? -2.625  11.085  -46.004 1.00 27.03  ? 486 HOH D O   1 
HETATM 9575 O  O   . HOH X 6 .   ? 9.247   3.127   -53.015 1.00 11.27  ? 487 HOH D O   1 
HETATM 9576 O  O   . HOH X 6 .   ? 1.160   9.197   -59.470 1.00 21.51  ? 488 HOH D O   1 
HETATM 9577 O  O   . HOH X 6 .   ? 12.852  19.843  -29.456 1.00 23.99  ? 489 HOH D O   1 
HETATM 9578 O  O   . HOH X 6 .   ? -5.589  -10.051 -41.865 1.00 36.97  ? 490 HOH D O   1 
HETATM 9579 O  O   . HOH X 6 .   ? 19.883  18.803  -40.217 1.00 50.65  ? 491 HOH D O   1 
HETATM 9580 O  O   . HOH X 6 .   ? 12.076  -3.777  -47.354 1.00 11.67  ? 492 HOH D O   1 
HETATM 9581 O  O   . HOH X 6 .   ? -5.152  -10.876 -31.210 1.00 32.38  ? 493 HOH D O   1 
HETATM 9582 O  O   . HOH X 6 .   ? -9.914  15.181  -21.079 1.00 19.71  ? 494 HOH D O   1 
HETATM 9583 O  O   . HOH X 6 .   ? 8.449   -9.094  -13.951 1.00 28.59  ? 495 HOH D O   1 
HETATM 9584 O  O   . HOH X 6 .   ? -11.893 10.002  -23.532 1.00 24.65  ? 496 HOH D O   1 
HETATM 9585 O  O   . HOH X 6 .   ? -2.700  8.161   -61.222 1.00 58.34  ? 497 HOH D O   1 
HETATM 9586 O  O   . HOH X 6 .   ? 19.773  -4.247  -34.502 1.00 21.77  ? 498 HOH D O   1 
HETATM 9587 O  O   . HOH X 6 .   ? 4.698   15.815  -57.391 1.00 20.87  ? 499 HOH D O   1 
HETATM 9588 O  O   . HOH X 6 .   ? 20.228  11.053  -29.339 1.00 16.51  ? 500 HOH D O   1 
HETATM 9589 O  O   . HOH X 6 .   ? 10.984  12.997  -61.419 1.00 21.68  ? 501 HOH D O   1 
HETATM 9590 O  O   . HOH X 6 .   ? 20.270  21.555  -33.073 1.00 25.95  ? 502 HOH D O   1 
HETATM 9591 O  O   . HOH X 6 .   ? 0.485   -0.119  -18.174 1.00 33.36  ? 503 HOH D O   1 
HETATM 9592 O  O   . HOH X 6 .   ? 21.494  2.222   -21.333 1.00 29.04  ? 504 HOH D O   1 
HETATM 9593 O  O   . HOH X 6 .   ? -14.130 9.300   -44.840 1.00 26.15  ? 505 HOH D O   1 
HETATM 9594 O  O   . HOH X 6 .   ? 22.967  23.067  -35.928 1.00 16.40  ? 506 HOH D O   1 
HETATM 9595 O  O   . HOH X 6 .   ? 6.244   -6.637  -57.594 1.00 14.72  ? 507 HOH D O   1 
HETATM 9596 O  O   . HOH X 6 .   ? 20.494  7.230   -35.908 1.00 10.49  ? 508 HOH D O   1 
HETATM 9597 O  O   . HOH X 6 .   ? 23.206  6.183   -38.411 1.00 10.40  ? 509 HOH D O   1 
HETATM 9598 O  O   . HOH X 6 .   ? 18.996  -0.401  -20.700 1.00 26.73  ? 510 HOH D O   1 
HETATM 9599 O  O   . HOH X 6 .   ? 10.834  10.093  -61.733 1.00 39.48  ? 511 HOH D O   1 
HETATM 9600 O  O   . HOH X 6 .   ? 26.458  15.958  -43.745 1.00 24.52  ? 512 HOH D O   1 
HETATM 9601 O  O   . HOH X 6 .   ? 5.725   12.178  -22.943 1.00 32.66  ? 513 HOH D O   1 
HETATM 9602 O  O   . HOH X 6 .   ? -1.970  -8.029  -22.679 1.00 15.87  ? 514 HOH D O   1 
HETATM 9603 O  O   . HOH X 6 .   ? 20.494  -7.317  -44.812 1.00 29.99  ? 515 HOH D O   1 
HETATM 9604 O  O   . HOH X 6 .   ? 4.621   -7.070  -34.868 1.00 10.51  ? 516 HOH D O   1 
HETATM 9605 O  O   . HOH X 6 .   ? 4.234   -0.658  -14.822 1.00 35.30  ? 517 HOH D O   1 
HETATM 9606 O  O   . HOH X 6 .   ? -7.656  11.849  -36.978 1.00 16.73  ? 518 HOH D O   1 
HETATM 9607 O  O   . HOH X 6 .   ? 6.769   17.855  -33.098 1.00 18.60  ? 519 HOH D O   1 
HETATM 9608 O  O   . HOH X 6 .   ? 11.745  21.622  -62.258 1.00 35.33  ? 520 HOH D O   1 
HETATM 9609 O  O   . HOH X 6 .   ? 11.925  -11.307 -27.800 1.00 32.16  ? 521 HOH D O   1 
HETATM 9610 O  O   . HOH X 6 .   ? 18.841  16.542  -42.070 1.00 33.03  ? 522 HOH D O   1 
HETATM 9611 O  O   . HOH X 6 .   ? 12.561  1.747   -18.154 1.00 16.44  ? 523 HOH D O   1 
HETATM 9612 O  O   . HOH X 6 .   ? 18.816  -0.360  -29.676 1.00 12.81  ? 524 HOH D O   1 
HETATM 9613 O  O   . HOH X 6 .   ? 13.708  18.386  -32.627 1.00 12.25  ? 525 HOH D O   1 
HETATM 9614 O  O   . HOH X 6 .   ? 19.068  -4.855  -18.416 1.00 28.72  ? 526 HOH D O   1 
HETATM 9615 O  O   . HOH X 6 .   ? 11.315  3.726   -55.214 1.00 16.63  ? 527 HOH D O   1 
HETATM 9616 O  O   . HOH X 6 .   ? -8.212  -0.340  -51.615 1.00 21.61  ? 528 HOH D O   1 
HETATM 9617 O  O   . HOH X 6 .   ? 7.898   -4.944  -14.641 1.00 25.04  ? 529 HOH D O   1 
HETATM 9618 O  O   . HOH X 6 .   ? -12.593 7.288   -23.728 1.00 29.67  ? 530 HOH D O   1 
HETATM 9619 O  O   . HOH X 6 .   ? -12.207 -7.949  -41.088 1.00 25.60  ? 531 HOH D O   1 
HETATM 9620 O  O   . HOH X 6 .   ? 9.679   -13.831 -55.776 1.00 44.58  ? 532 HOH D O   1 
HETATM 9621 O  O   . HOH X 6 .   ? -3.284  -5.805  -26.925 1.00 18.97  ? 533 HOH D O   1 
HETATM 9622 O  O   . HOH X 6 .   ? -1.818  13.236  -41.818 1.00 24.52  ? 534 HOH D O   1 
HETATM 9623 O  O   . HOH X 6 .   ? -13.024 12.443  -32.522 1.00 38.60  ? 535 HOH D O   1 
HETATM 9624 O  O   . HOH X 6 .   ? 11.725  -12.725 -40.162 1.00 36.25  ? 536 HOH D O   1 
HETATM 9625 O  O   . HOH X 6 .   ? 7.882   17.391  -25.133 1.00 28.33  ? 537 HOH D O   1 
HETATM 9626 O  O   . HOH X 6 .   ? -0.298  0.872   -57.156 1.00 57.14  ? 538 HOH D O   1 
HETATM 9627 O  O   . HOH X 6 .   ? -2.088  11.664  -20.334 1.00 18.69  ? 539 HOH D O   1 
HETATM 9628 O  O   . HOH X 6 .   ? 1.404   -17.528 -26.817 1.00 29.44  ? 540 HOH D O   1 
HETATM 9629 O  O   . HOH X 6 .   ? 1.579   7.516   -18.832 1.00 31.41  ? 541 HOH D O   1 
HETATM 9630 O  O   . HOH X 6 .   ? 12.792  -9.918  -46.361 1.00 16.58  ? 542 HOH D O   1 
HETATM 9631 O  O   . HOH X 6 .   ? 21.710  5.016   -34.502 1.00 8.60   ? 543 HOH D O   1 
HETATM 9632 O  O   . HOH X 6 .   ? 17.659  -11.685 -27.523 1.00 18.61  ? 544 HOH D O   1 
HETATM 9633 O  O   . HOH X 6 .   ? 24.192  18.316  -42.869 1.00 20.84  ? 545 HOH D O   1 
HETATM 9634 O  O   . HOH X 6 .   ? 14.188  16.276  -26.607 1.00 20.16  ? 546 HOH D O   1 
HETATM 9635 O  O   . HOH X 6 .   ? 1.354   -5.257  -54.408 1.00 19.28  ? 547 HOH D O   1 
HETATM 9636 O  O   . HOH X 6 .   ? 9.044   21.737  -29.786 1.00 16.12  ? 548 HOH D O   1 
HETATM 9637 O  O   . HOH X 6 .   ? 3.068   21.257  -31.720 1.00 28.99  ? 549 HOH D O   1 
HETATM 9638 O  O   . HOH X 6 .   ? -4.984  -13.911 -32.569 1.00 24.15  ? 550 HOH D O   1 
HETATM 9639 O  O   . HOH X 6 .   ? 14.726  2.150   -16.633 1.00 33.17  ? 551 HOH D O   1 
HETATM 9640 O  O   . HOH X 6 .   ? 22.211  1.003   -25.563 1.00 29.30  ? 552 HOH D O   1 
HETATM 9641 O  O   . HOH X 6 .   ? -14.000 12.061  -49.781 1.00 40.09  ? 553 HOH D O   1 
HETATM 9642 O  O   . HOH X 6 .   ? -2.195  -8.932  -41.846 1.00 13.95  ? 554 HOH D O   1 
HETATM 9643 O  O   . HOH X 6 .   ? 14.614  17.486  -52.075 1.00 30.24  ? 555 HOH D O   1 
HETATM 9644 O  O   . HOH X 6 .   ? -18.608 5.216   -40.929 1.00 30.73  ? 556 HOH D O   1 
HETATM 9645 O  O   . HOH X 6 .   ? 15.733  9.591   -48.053 1.00 21.34  ? 557 HOH D O   1 
HETATM 9646 O  O   . HOH X 6 .   ? 19.207  11.413  -50.319 1.00 19.08  ? 558 HOH D O   1 
HETATM 9647 O  O   . HOH X 6 .   ? -5.947  12.439  -40.159 1.00 29.53  ? 559 HOH D O   1 
HETATM 9648 O  O   . HOH X 6 .   ? 6.162   21.522  -25.701 1.00 20.84  ? 560 HOH D O   1 
HETATM 9649 O  O   . HOH X 6 .   ? 8.220   8.973   -24.412 1.00 16.87  ? 561 HOH D O   1 
HETATM 9650 O  O   . HOH X 6 .   ? 8.960   -13.579 -29.517 1.00 34.15  ? 562 HOH D O   1 
HETATM 9651 O  O   . HOH X 6 .   ? 26.223  12.798  -35.665 1.00 12.66  ? 563 HOH D O   1 
HETATM 9652 O  O   . HOH X 6 .   ? -12.345 -4.432  -47.588 1.00 22.94  ? 564 HOH D O   1 
HETATM 9653 O  O   . HOH X 6 .   ? 1.144   24.102  -29.821 1.00 30.21  ? 565 HOH D O   1 
HETATM 9654 O  O   . HOH X 6 .   ? 19.071  -13.346 -33.534 1.00 31.97  ? 566 HOH D O   1 
HETATM 9655 O  O   . HOH X 6 .   ? 21.205  9.346   -26.163 1.00 27.88  ? 567 HOH D O   1 
HETATM 9656 O  O   . HOH X 6 .   ? 21.007  -4.336  -28.761 1.00 19.50  ? 568 HOH D O   1 
HETATM 9657 O  O   . HOH X 6 .   ? -14.719 -0.684  -35.629 1.00 20.67  ? 569 HOH D O   1 
HETATM 9658 O  O   . HOH X 6 .   ? 9.210   16.187  -40.135 1.00 28.68  ? 570 HOH D O   1 
HETATM 9659 O  O   . HOH X 6 .   ? 19.120  -3.805  -43.487 1.00 18.31  ? 571 HOH D O   1 
HETATM 9660 O  O   . HOH X 6 .   ? 23.855  10.334  -41.718 1.00 14.53  ? 572 HOH D O   1 
HETATM 9661 O  O   . HOH X 6 .   ? 17.199  7.305   -55.800 1.00 23.01  ? 573 HOH D O   1 
HETATM 9662 O  O   . HOH X 6 .   ? 24.176  8.180   -45.739 1.00 28.30  ? 574 HOH D O   1 
HETATM 9663 O  O   . HOH X 6 .   ? -10.401 -4.727  -29.545 1.00 20.15  ? 575 HOH D O   1 
HETATM 9664 O  O   . HOH X 6 .   ? 21.703  6.570   -29.845 1.00 12.24  ? 576 HOH D O   1 
HETATM 9665 O  O   . HOH X 6 .   ? -2.937  -1.082  -17.064 1.00 42.13  ? 577 HOH D O   1 
HETATM 9666 O  O   . HOH X 6 .   ? 11.885  8.928   -47.225 1.00 17.54  ? 578 HOH D O   1 
HETATM 9667 O  O   . HOH X 6 .   ? 14.846  13.737  -27.416 1.00 13.69  ? 579 HOH D O   1 
HETATM 9668 O  O   . HOH X 6 .   ? 16.733  10.355  -50.459 1.00 18.77  ? 580 HOH D O   1 
HETATM 9669 O  O   . HOH X 6 .   ? 4.513   19.169  -22.544 1.00 32.05  ? 581 HOH D O   1 
HETATM 9670 O  O   . HOH X 6 .   ? 16.659  15.816  -54.672 1.00 27.85  ? 582 HOH D O   1 
HETATM 9671 O  O   . HOH X 6 .   ? 11.145  -0.719  -13.981 1.00 32.64  ? 583 HOH D O   1 
HETATM 9672 O  O   . HOH X 6 .   ? 16.548  15.011  -24.249 1.00 28.80  ? 584 HOH D O   1 
HETATM 9673 O  O   . HOH X 6 .   ? 13.791  0.879   -55.686 1.00 21.87  ? 585 HOH D O   1 
HETATM 9674 O  O   . HOH X 6 .   ? -12.532 8.519   -55.422 1.00 34.68  ? 586 HOH D O   1 
HETATM 9675 O  O   . HOH X 6 .   ? 10.725  2.303   -21.672 1.00 17.20  ? 587 HOH D O   1 
HETATM 9676 O  O   . HOH X 6 .   ? -8.330  9.547   -55.604 1.00 34.21  ? 588 HOH D O   1 
HETATM 9677 O  O   . HOH X 6 .   ? -2.564  17.104  -36.707 1.00 26.77  ? 589 HOH D O   1 
HETATM 9678 O  O   . HOH X 6 .   ? 0.872   -8.368  -18.938 1.00 23.54  ? 590 HOH D O   1 
HETATM 9679 O  O   . HOH X 6 .   ? -9.295  16.073  -28.733 1.00 29.64  ? 591 HOH D O   1 
HETATM 9680 O  O   . HOH X 6 .   ? 4.195   19.261  -52.015 1.00 34.85  ? 592 HOH D O   1 
HETATM 9681 O  O   . HOH X 6 .   ? 10.810  -10.638 -17.016 1.00 33.49  ? 593 HOH D O   1 
HETATM 9682 O  O   . HOH X 6 .   ? 19.406  9.876   -35.887 1.00 9.78   ? 594 HOH D O   1 
HETATM 9683 O  O   . HOH X 6 .   ? 0.155   -12.292 -42.325 1.00 19.63  ? 595 HOH D O   1 
HETATM 9684 O  O   . HOH X 6 .   ? 19.397  -0.433  -37.014 1.00 15.24  ? 596 HOH D O   1 
HETATM 9685 O  O   . HOH X 6 .   ? 22.739  -5.301  -26.594 1.00 24.85  ? 597 HOH D O   1 
HETATM 9686 O  O   . HOH X 6 .   ? -14.009 8.083   -25.583 1.00 36.58  ? 598 HOH D O   1 
HETATM 9687 O  O   . HOH X 6 .   ? 17.193  6.741   -49.135 1.00 17.99  ? 599 HOH D O   1 
HETATM 9688 O  O   . HOH X 6 .   ? 2.770   1.221   -20.378 1.00 26.15  ? 600 HOH D O   1 
HETATM 9689 O  O   . HOH X 6 .   ? 11.589  -11.273 -44.300 1.00 20.64  ? 601 HOH D O   1 
HETATM 9690 O  O   . HOH X 6 .   ? -11.076 -7.654  -36.476 1.00 45.68  ? 602 HOH D O   1 
HETATM 9691 O  O   . HOH X 6 .   ? 13.389  13.449  -48.458 1.00 23.93  ? 603 HOH D O   1 
HETATM 9692 O  O   . HOH X 6 .   ? -4.435  14.635  -35.926 1.00 22.79  ? 604 HOH D O   1 
HETATM 9693 O  O   . HOH X 6 .   ? 19.019  -7.682  -40.318 1.00 18.39  ? 605 HOH D O   1 
HETATM 9694 O  O   . HOH X 6 .   ? -4.307  21.211  -25.856 1.00 32.69  ? 606 HOH D O   1 
HETATM 9695 O  O   . HOH X 6 .   ? -17.761 -1.690  -45.295 1.00 35.78  ? 607 HOH D O   1 
HETATM 9696 O  O   . HOH X 6 .   ? 18.558  22.917  -34.419 1.00 23.87  ? 608 HOH D O   1 
HETATM 9697 O  O   . HOH X 6 .   ? -4.621  -11.516 -28.306 1.00 25.50  ? 609 HOH D O   1 
HETATM 9698 O  O   . HOH X 6 .   ? 19.335  4.846   -49.328 1.00 18.02  ? 610 HOH D O   1 
HETATM 9699 O  O   . HOH X 6 .   ? 4.550   23.082  -27.623 1.00 34.35  ? 611 HOH D O   1 
HETATM 9700 O  O   . HOH X 6 .   ? -2.568  14.162  -56.381 1.00 31.81  ? 612 HOH D O   1 
HETATM 9701 O  O   . HOH X 6 .   ? 1.492   -10.067 -31.356 1.00 12.00  ? 613 HOH D O   1 
HETATM 9702 O  O   . HOH X 6 .   ? -11.183 12.754  -38.204 1.00 28.86  ? 614 HOH D O   1 
HETATM 9703 O  O   . HOH X 6 .   ? 5.554   9.219   -23.822 1.00 25.53  ? 615 HOH D O   1 
HETATM 9704 O  O   . HOH X 6 .   ? 3.051   9.262   -24.810 1.00 16.51  ? 616 HOH D O   1 
HETATM 9705 O  O   . HOH X 6 .   ? -4.017  10.054  -17.499 1.00 17.52  ? 617 HOH D O   1 
HETATM 9706 O  O   . HOH X 6 .   ? 13.770  7.447   -48.377 1.00 13.46  ? 618 HOH D O   1 
HETATM 9707 O  O   . HOH X 6 .   ? 9.293   17.437  -27.406 1.00 20.42  ? 619 HOH D O   1 
HETATM 9708 O  O   . HOH X 6 .   ? 0.864   15.481  -59.821 1.00 38.73  ? 620 HOH D O   1 
HETATM 9709 O  O   . HOH X 6 .   ? -8.922  10.976  -44.835 1.00 19.16  ? 621 HOH D O   1 
HETATM 9710 O  O   . HOH X 6 .   ? 5.258   8.523   -43.511 1.00 26.26  ? 622 HOH D O   1 
HETATM 9711 O  O   . HOH X 6 .   ? 22.720  18.808  -48.901 1.00 42.51  ? 623 HOH D O   1 
HETATM 9712 O  O   . HOH X 6 .   ? -8.112  15.838  -34.904 1.00 30.81  ? 624 HOH D O   1 
HETATM 9713 O  O   . HOH X 6 .   ? 9.629   20.005  -31.969 1.00 16.77  ? 625 HOH D O   1 
HETATM 9714 O  O   . HOH X 6 .   ? -15.684 9.570   -47.522 1.00 26.30  ? 626 HOH D O   1 
HETATM 9715 O  O   . HOH X 6 .   ? -0.067  -12.962 -45.555 1.00 15.14  ? 627 HOH D O   1 
HETATM 9716 O  O   . HOH X 6 .   ? -11.091 12.154  -30.662 1.00 25.11  ? 628 HOH D O   1 
HETATM 9717 O  O   . HOH X 6 .   ? 6.081   -0.406  -57.921 1.00 21.10  ? 629 HOH D O   1 
HETATM 9718 O  O   . HOH X 6 .   ? -15.974 4.390   -41.280 1.00 21.87  ? 630 HOH D O   1 
HETATM 9719 O  O   . HOH X 6 .   ? 22.618  3.589   -23.623 1.00 24.48  ? 631 HOH D O   1 
HETATM 9720 O  O   . HOH X 6 .   ? -14.804 10.335  -31.489 1.00 37.24  ? 632 HOH D O   1 
HETATM 9721 O  O   . HOH X 6 .   ? 12.325  -2.543  -12.763 1.00 51.09  ? 633 HOH D O   1 
HETATM 9722 O  O   . HOH X 6 .   ? 17.811  -10.775 -48.863 1.00 36.69  ? 634 HOH D O   1 
HETATM 9723 O  O   . HOH X 6 .   ? 12.012  -10.298 -58.066 1.00 22.09  ? 635 HOH D O   1 
HETATM 9724 O  O   . HOH X 6 .   ? 0.623   12.964  -40.007 1.00 22.74  ? 636 HOH D O   1 
HETATM 9725 O  O   . HOH X 6 .   ? 14.180  -11.768 -21.205 1.00 40.95  ? 637 HOH D O   1 
HETATM 9726 O  O   . HOH X 6 .   ? 9.645   16.744  -48.526 1.00 37.69  ? 638 HOH D O   1 
HETATM 9727 O  O   . HOH X 6 .   ? 22.769  -1.760  -40.055 1.00 27.02  ? 639 HOH D O   1 
HETATM 9728 O  O   . HOH X 6 .   ? 5.292   3.203   -19.900 1.00 45.50  ? 640 HOH D O   1 
HETATM 9729 O  O   . HOH X 6 .   ? 13.806  -8.753  -56.294 1.00 28.41  ? 641 HOH D O   1 
HETATM 9730 O  O   . HOH X 6 .   ? -9.003  -5.642  -22.893 1.00 37.61  ? 642 HOH D O   1 
HETATM 9731 O  O   . HOH X 6 .   ? -7.930  19.125  -26.791 1.00 34.71  ? 643 HOH D O   1 
HETATM 9732 O  O   . HOH X 6 .   ? 11.723  -10.383 -41.972 1.00 18.98  ? 644 HOH D O   1 
HETATM 9733 O  O   . HOH X 6 .   ? 16.481  0.840   -55.631 1.00 38.02  ? 645 HOH D O   1 
HETATM 9734 O  O   . HOH X 6 .   ? -17.398 5.323   -52.019 1.00 44.20  ? 646 HOH D O   1 
HETATM 9735 O  O   . HOH X 6 .   ? -8.400  12.612  -40.832 1.00 30.43  ? 647 HOH D O   1 
HETATM 9736 O  O   . HOH X 6 .   ? -4.689  -13.587 -29.758 1.00 40.25  ? 648 HOH D O   1 
HETATM 9737 O  O   . HOH X 6 .   ? 1.864   14.521  -44.415 1.00 42.54  ? 649 HOH D O   1 
HETATM 9738 O  O   . HOH X 6 .   ? -0.998  3.289   -19.173 1.00 32.64  ? 650 HOH D O   1 
HETATM 9739 O  O   . HOH X 6 .   ? 19.433  -8.990  -48.521 1.00 37.47  ? 651 HOH D O   1 
HETATM 9740 O  O   . HOH X 6 .   ? 13.652  -11.426 -38.840 1.00 33.86  ? 652 HOH D O   1 
HETATM 9741 O  O   . HOH X 6 .   ? 14.438  -11.216 -27.614 1.00 40.60  ? 653 HOH D O   1 
HETATM 9742 O  O   . HOH X 6 .   ? 17.289  17.596  -26.962 1.00 39.28  ? 654 HOH D O   1 
HETATM 9743 O  O   . HOH X 6 .   ? 16.285  24.152  -34.253 1.00 24.27  ? 655 HOH D O   1 
HETATM 9744 O  O   . HOH X 6 .   ? 27.247  18.450  -43.965 1.00 45.57  ? 656 HOH D O   1 
HETATM 9745 O  O   . HOH X 6 .   ? -14.451 -6.731  -40.706 1.00 35.40  ? 657 HOH D O   1 
HETATM 9746 O  O   . HOH X 6 .   ? 10.404  19.913  -28.290 1.00 27.50  ? 658 HOH D O   1 
HETATM 9747 O  O   . HOH X 6 .   ? 19.443  15.471  -54.005 1.00 44.75  ? 659 HOH D O   1 
HETATM 9748 O  O   . HOH X 6 .   ? 18.577  -0.005  -54.164 1.00 33.23  ? 660 HOH D O   1 
HETATM 9749 O  O   . HOH X 6 .   ? 1.733   -14.284 -17.634 1.00 36.28  ? 661 HOH D O   1 
HETATM 9750 O  O   . HOH X 6 .   ? -5.302  14.404  -56.733 1.00 36.44  ? 662 HOH D O   1 
HETATM 9751 O  O   . HOH X 6 .   ? 27.601  12.860  -47.244 1.00 26.68  ? 663 HOH D O   1 
HETATM 9752 O  O   . HOH X 6 .   ? -2.720  -12.510 -45.428 1.00 21.38  ? 664 HOH D O   1 
HETATM 9753 O  O   . HOH X 6 .   ? -9.571  10.370  -42.265 1.00 26.29  ? 665 HOH D O   1 
HETATM 9754 O  O   . HOH X 6 .   ? -15.009 6.869   -41.095 1.00 35.01  ? 666 HOH D O   1 
HETATM 9755 O  O   . HOH X 6 .   ? 20.484  -2.778  -36.590 1.00 34.37  ? 667 HOH D O   1 
HETATM 9756 O  O   . HOH X 6 .   ? 14.586  -11.807 -47.665 1.00 28.07  ? 668 HOH D O   1 
HETATM 9757 O  O   . HOH X 6 .   ? 22.727  8.950   -43.664 1.00 20.38  ? 669 HOH D O   1 
HETATM 9758 O  O   . HOH X 6 .   ? 7.430   -4.390  -58.658 1.00 21.56  ? 670 HOH D O   1 
HETATM 9759 O  O   . HOH X 6 .   ? 12.441  -12.734 -56.973 1.00 25.09  ? 671 HOH D O   1 
HETATM 9760 O  O   . HOH X 6 .   ? 11.835  17.717  -52.204 1.00 35.75  ? 672 HOH D O   1 
HETATM 9761 O  O   . HOH X 6 .   ? 2.224   -7.434  -55.738 1.00 24.83  ? 673 HOH D O   1 
HETATM 9762 O  O   . HOH X 6 .   ? -8.848  1.680   -19.819 1.00 35.99  ? 674 HOH D O   1 
HETATM 9763 O  O   . HOH X 6 .   ? 18.801  15.513  -65.308 1.00 45.36  ? 675 HOH D O   1 
HETATM 9764 O  O   . HOH X 6 .   ? 4.733   15.414  -41.895 1.00 26.19  ? 676 HOH D O   1 
HETATM 9765 O  O   . HOH X 6 .   ? -1.063  -12.687 -39.136 1.00 28.15  ? 677 HOH D O   1 
HETATM 9766 O  O   . HOH X 6 .   ? 3.591   -6.812  -58.096 1.00 20.52  ? 678 HOH D O   1 
HETATM 9767 O  O   . HOH X 6 .   ? 22.566  -7.770  -27.724 1.00 18.56  ? 679 HOH D O   1 
HETATM 9768 O  O   . HOH X 6 .   ? 1.919   -15.944 -39.627 1.00 33.33  ? 680 HOH D O   1 
HETATM 9769 O  O   . HOH X 6 .   ? -6.438  -9.524  -26.626 1.00 37.93  ? 681 HOH D O   1 
HETATM 9770 O  O   . HOH X 6 .   ? 23.520  12.077  -51.156 1.00 33.50  ? 682 HOH D O   1 
HETATM 9771 O  O   . HOH X 6 .   ? -0.352  15.249  -38.144 1.00 32.10  ? 683 HOH D O   1 
HETATM 9772 O  O   . HOH X 6 .   ? 15.677  -10.236 -55.105 1.00 33.21  ? 684 HOH D O   1 
HETATM 9773 O  O   . HOH X 6 .   ? -8.230  -10.760 -42.284 1.00 40.15  ? 685 HOH D O   1 
HETATM 9774 O  O   . HOH X 6 .   ? 21.007  -1.826  -42.488 1.00 22.00  ? 686 HOH D O   1 
HETATM 9775 O  O   . HOH X 6 .   ? 16.806  -14.291 -26.976 1.00 38.18  ? 687 HOH D O   1 
HETATM 9776 O  O   . HOH X 6 .   ? 1.145   -3.642  -56.332 1.00 42.32  ? 688 HOH D O   1 
HETATM 9777 O  O   . HOH X 6 .   ? 7.384   15.569  -42.630 1.00 31.23  ? 689 HOH D O   1 
HETATM 9778 O  O   . HOH X 6 .   ? -2.948  -10.085 -21.176 1.00 26.02  ? 690 HOH D O   1 
HETATM 9779 O  O   . HOH X 6 .   ? 5.471   -2.520  -59.254 1.00 26.65  ? 691 HOH D O   1 
HETATM 9780 O  O   . HOH X 6 .   ? -2.306  -14.881 -39.732 1.00 34.57  ? 692 HOH D O   1 
HETATM 9781 O  O   . HOH X 6 .   ? 3.816   1.287   -58.537 1.00 28.22  ? 693 HOH D O   1 
HETATM 9782 O  O   . HOH X 6 .   ? 20.312  -11.591 -27.692 1.00 20.24  ? 694 HOH D O   1 
HETATM 9783 O  O   . HOH X 6 .   ? -6.273  -9.051  -52.791 1.00 31.17  ? 695 HOH D O   1 
HETATM 9784 O  O   . HOH X 6 .   ? -3.605  -9.088  -18.746 1.00 24.90  ? 696 HOH D O   1 
HETATM 9785 O  O   . HOH X 6 .   ? 10.386  -12.195 -33.241 1.00 29.32  ? 697 HOH D O   1 
HETATM 9786 O  O   . HOH X 6 .   ? -1.003  -15.622 -44.632 1.00 37.20  ? 698 HOH D O   1 
HETATM 9787 O  O   . HOH X 6 .   ? -14.332 9.377   -42.198 1.00 31.08  ? 699 HOH D O   1 
HETATM 9788 O  O   . HOH X 6 .   ? 8.701   3.980   -17.989 1.00 36.67  ? 700 HOH D O   1 
HETATM 9789 O  O   . HOH X 6 .   ? 2.810   -0.488  -57.163 1.00 32.25  ? 701 HOH D O   1 
HETATM 9790 O  O   . HOH X 6 .   ? 9.354   -4.267  -60.575 1.00 31.62  ? 702 HOH D O   1 
HETATM 9791 O  O   . HOH X 6 .   ? -7.780  -6.889  -18.599 1.00 29.59  ? 703 HOH D O   1 
HETATM 9792 O  O   . HOH X 6 .   ? 1.438   -10.222 -56.224 1.00 31.53  ? 704 HOH D O   1 
HETATM 9793 O  O   . HOH X 6 .   ? 20.154  -6.044  -42.207 1.00 19.05  ? 705 HOH D O   1 
HETATM 9794 O  O   . HOH X 6 .   ? 12.230  20.720  -32.596 1.00 20.36  ? 706 HOH D O   1 
HETATM 9795 O  O   . HOH X 6 .   ? -12.186 10.932  -42.096 1.00 31.82  ? 707 HOH D O   1 
HETATM 9796 O  O   . HOH X 6 .   ? 7.631   20.397  -33.781 1.00 25.90  ? 708 HOH D O   1 
HETATM 9797 O  O   . HOH X 6 .   ? 14.403  15.146  -23.192 1.00 36.85  ? 709 HOH D O   1 
HETATM 9798 O  O   . HOH X 6 .   ? -10.542 18.606  -28.714 1.00 33.19  ? 710 HOH D O   1 
HETATM 9799 O  O   . HOH X 6 .   ? 7.333   -8.643  -59.061 1.00 26.34  ? 711 HOH D O   1 
HETATM 9800 O  O   . HOH X 6 .   ? 11.001  3.804   -19.367 1.00 20.55  ? 712 HOH D O   1 
HETATM 9801 O  O   . HOH X 6 .   ? 5.658   -10.390 -60.393 1.00 35.89  ? 713 HOH D O   1 
HETATM 9802 O  O   . HOH X 6 .   ? -2.089  21.988  -26.010 1.00 28.57  ? 714 HOH D O   1 
HETATM 9803 O  O   . HOH X 6 .   ? 2.419   -11.213 -58.479 1.00 36.76  ? 715 HOH D O   1 
HETATM 9804 O  O   . HOH X 6 .   ? 11.885  -13.896 -36.684 1.00 33.07  ? 716 HOH D O   1 
HETATM 9805 O  O   . HOH X 6 .   ? 12.641  16.974  -24.441 1.00 31.77  ? 717 HOH D O   1 
HETATM 9806 O  O   . HOH X 6 .   ? 28.017  13.037  -49.855 1.00 31.33  ? 718 HOH D O   1 
HETATM 9807 O  O   . HOH X 6 .   ? 10.267  8.302   -19.713 1.00 27.50  ? 719 HOH D O   1 
HETATM 9808 O  O   . HOH X 6 .   ? 12.168  6.007   -19.776 1.00 25.78  ? 720 HOH D O   1 
HETATM 9809 O  O   . HOH X 6 .   ? 10.538  23.986  -30.669 1.00 21.39  ? 721 HOH D O   1 
HETATM 9810 O  O   . HOH X 6 .   ? 13.166  22.786  -30.884 1.00 20.71  ? 722 HOH D O   1 
HETATM 9811 O  O   . HOH X 6 .   ? -6.332  -9.108  -18.410 1.00 23.68  ? 723 HOH D O   1 
HETATM 9812 O  O   . HOH X 6 .   ? -5.055  -11.518 -22.186 1.00 33.40  ? 724 HOH D O   1 
HETATM 9813 O  O   . HOH X 6 .   ? 15.151  24.517  -31.877 1.00 22.02  ? 725 HOH D O   1 
HETATM 9814 O  O   . HOH X 6 .   ? -7.108  -11.590 -52.834 1.00 31.66  ? 726 HOH D O   1 
HETATM 9815 O  O   . HOH X 6 .   ? 2.794   -4.302  -58.865 1.00 28.51  ? 727 HOH D O   1 
HETATM 9816 O  O   . HOH X 6 .   ? 16.570  22.962  -27.894 1.00 24.46  ? 728 HOH D O   1 
HETATM 9817 O  O   . HOH X 6 .   ? -4.146  -14.167 -41.769 1.00 36.66  ? 729 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   ? 0.8285 0.6415 0.5420 -0.4270 -0.0495 -0.1392 3   LYS A N   
2    C  CA  . LYS A 3   ? 0.6057 0.4875 0.6985 -0.2004 -0.0011 -0.0715 3   LYS A CA  
3    C  C   . LYS A 3   ? 0.4623 0.2837 0.4701 0.0370  -0.1498 0.0473  3   LYS A C   
4    O  O   . LYS A 3   ? 0.6664 0.5500 0.4971 0.0582  -0.2673 0.0881  3   LYS A O   
5    C  CB  . LYS A 3   ? 0.8901 1.1095 0.8625 -0.2746 0.2318  0.0044  3   LYS A CB  
6    C  CG  . LYS A 3   ? 0.7979 1.3628 0.6028 -0.3130 0.3472  -0.0624 3   LYS A CG  
7    C  CD  . LYS A 3   ? 0.2383 1.3034 0.9133 -0.1934 -0.0006 -0.3648 3   LYS A CD  
8    C  CE  . LYS A 3   ? 0.4752 1.4306 1.3839 -0.1562 0.1009  -0.5774 3   LYS A CE  
9    N  NZ  . LYS A 3   ? 0.8590 1.0087 1.0836 0.1392  0.1085  -0.8966 3   LYS A NZ  
10   N  N   . TRP A 4   ? 0.2581 0.1703 0.3269 -0.0886 -0.0063 -0.0882 4   TRP A N   
11   C  CA  . TRP A 4   ? 0.2155 0.0870 0.2543 -0.0227 -0.0480 -0.0148 4   TRP A CA  
12   C  C   . TRP A 4   ? 0.1807 0.1058 0.2171 0.0026  -0.0477 -0.0179 4   TRP A C   
13   O  O   . TRP A 4   ? 0.2507 0.1578 0.2716 -0.0208 -0.1268 -0.0091 4   TRP A O   
14   C  CB  . TRP A 4   ? 0.2044 0.0551 0.2444 -0.0231 -0.0502 0.0065  4   TRP A CB  
15   C  CG  . TRP A 4   ? 0.2195 0.0651 0.1787 -0.0084 -0.0524 0.0120  4   TRP A CG  
16   C  CD1 . TRP A 4   ? 0.2198 0.1505 0.1584 -0.0332 -0.0332 0.0119  4   TRP A CD1 
17   C  CD2 . TRP A 4   ? 0.2094 0.0589 0.1531 -0.0185 -0.0432 0.0199  4   TRP A CD2 
18   N  NE1 . TRP A 4   ? 0.2196 0.1349 0.1884 -0.0345 -0.0467 -0.0192 4   TRP A NE1 
19   C  CE2 . TRP A 4   ? 0.2387 0.1115 0.1796 -0.0006 -0.0731 0.0040  4   TRP A CE2 
20   C  CE3 . TRP A 4   ? 0.2144 0.0513 0.1930 -0.0148 -0.0710 -0.0073 4   TRP A CE3 
21   C  CZ2 . TRP A 4   ? 0.2218 0.1380 0.1714 0.0214  -0.0433 0.0068  4   TRP A CZ2 
22   C  CZ3 . TRP A 4   ? 0.2383 0.0792 0.1782 0.0262  -0.0619 0.0069  4   TRP A CZ3 
23   C  CH2 . TRP A 4   ? 0.2370 0.1185 0.1907 0.0273  -0.0403 -0.0330 4   TRP A CH2 
24   N  N   . THR A 5   ? 0.1893 0.0642 0.2457 0.0138  -0.0278 -0.0111 5   THR A N   
25   C  CA  . THR A 5   ? 0.2182 0.0933 0.2017 0.0302  -0.0289 -0.0074 5   THR A CA  
26   C  C   . THR A 5   ? 0.1560 0.0803 0.1505 0.0324  -0.0109 0.0295  5   THR A C   
27   O  O   . THR A 5   ? 0.2053 0.0807 0.1665 0.0485  -0.0322 0.0233  5   THR A O   
28   C  CB  . THR A 5   ? 0.2441 0.0835 0.2489 -0.0070 -0.0201 -0.1024 5   THR A CB  
29   O  OG1 . THR A 5   ? 0.2192 0.1798 0.2809 -0.0176 -0.0044 -0.0611 5   THR A OG1 
30   C  CG2 . THR A 5   ? 0.2681 0.0626 0.3581 -0.0094 -0.0893 -0.1001 5   THR A CG2 
31   N  N   . TYR A 6   ? 0.2213 0.0476 0.1902 0.0103  -0.0167 0.0158  6   TYR A N   
32   C  CA  . TYR A 6   ? 0.2522 0.0102 0.1886 0.0297  -0.0090 0.0062  6   TYR A CA  
33   C  C   . TYR A 6   ? 0.2371 0.0539 0.2095 0.0011  0.0018  0.0049  6   TYR A C   
34   O  O   . TYR A 6   ? 0.2512 0.0783 0.2178 0.0062  -0.0032 -0.0234 6   TYR A O   
35   C  CB  . TYR A 6   ? 0.2125 0.0606 0.2331 0.0628  0.0085  0.0506  6   TYR A CB  
36   C  CG  . TYR A 6   ? 0.2056 0.0380 0.2013 0.0201  0.0006  0.0119  6   TYR A CG  
37   C  CD1 . TYR A 6   ? 0.2500 0.0108 0.1764 0.0045  0.0056  0.0274  6   TYR A CD1 
38   C  CD2 . TYR A 6   ? 0.2309 0.0135 0.1863 -0.0013 -0.0176 0.0359  6   TYR A CD2 
39   C  CE1 . TYR A 6   ? 0.2009 0.0134 0.2444 -0.0231 0.0018  0.0319  6   TYR A CE1 
40   C  CE2 . TYR A 6   ? 0.2040 0.0559 0.1814 -0.0158 -0.0130 0.0307  6   TYR A CE2 
41   C  CZ  . TYR A 6   ? 0.1857 0.0118 0.1852 0.0068  0.0086  0.0308  6   TYR A CZ  
42   O  OH  . TYR A 6   ? 0.1868 0.1046 0.1764 -0.0229 0.0098  0.0020  6   TYR A OH  
43   N  N   . PHE A 7   ? 0.2568 0.0663 0.4566 0.0506  0.0597  -0.0583 7   PHE A N   
44   C  CA  . PHE A 7   ? 0.3305 0.1471 0.4443 0.0078  0.0999  -0.0607 7   PHE A CA  
45   C  C   . PHE A 7   ? 0.3041 0.1934 0.6635 0.0121  0.2045  -0.1605 7   PHE A C   
46   O  O   . PHE A 7   ? 0.4002 0.2103 1.0912 -0.1127 0.3168  -0.1141 7   PHE A O   
47   C  CB  . PHE A 7   ? 0.3725 0.2462 0.3983 -0.1678 0.0140  -0.0672 7   PHE A CB  
48   N  N   . GLY A 8   ? 0.2922 0.1442 0.4512 -0.0542 0.0442  0.0020  8   GLY A N   
49   C  CA  . GLY A 8   ? 0.3674 0.1513 0.2469 -0.0155 -0.0439 -0.0370 8   GLY A CA  
50   C  C   . GLY A 8   ? 0.3823 0.1220 0.3016 0.0664  -0.0154 -0.0348 8   GLY A C   
51   O  O   . GLY A 8   ? 0.5401 0.1240 0.3040 0.0820  0.0058  -0.0376 8   GLY A O   
52   N  N   . PRO A 9   ? 0.3351 0.1442 0.3204 0.1007  0.0423  -0.0948 9   PRO A N   
53   C  CA  . PRO A 9   ? 0.3060 0.1550 0.4101 0.1272  0.0214  -0.0425 9   PRO A CA  
54   C  C   . PRO A 9   ? 0.3115 0.0397 0.3863 0.0534  0.0134  -0.0581 9   PRO A C   
55   O  O   . PRO A 9   ? 0.2703 0.1489 0.3287 0.0000  -0.0523 -0.0684 9   PRO A O   
56   C  CB  . PRO A 9   ? 0.5181 0.1395 0.4953 0.1156  0.1005  -0.0546 9   PRO A CB  
57   C  CG  . PRO A 9   ? 0.4674 0.2439 0.4875 0.1121  -0.0447 -0.0704 9   PRO A CG  
58   C  CD  . PRO A 9   ? 0.3306 0.2222 0.3486 0.0446  0.0443  -0.1324 9   PRO A CD  
59   N  N   . ASP A 10  ? 0.3362 0.0267 0.3514 0.0332  -0.0177 -0.0193 10  ASP A N   
60   C  CA  . ASP A 10  ? 0.2134 0.0881 0.3613 0.0218  -0.0831 -0.0502 10  ASP A CA  
61   C  C   . ASP A 10  ? 0.2365 0.0826 0.2472 -0.0151 -0.0329 -0.0329 10  ASP A C   
62   O  O   . ASP A 10  ? 0.2388 0.0536 0.2708 -0.0033 -0.0425 -0.0200 10  ASP A O   
63   C  CB  . ASP A 10  ? 0.3277 0.1844 0.3632 -0.0471 -0.0734 -0.1471 10  ASP A CB  
64   C  CG  . ASP A 10  ? 0.4374 0.1714 0.3531 -0.0052 -0.0708 -0.0963 10  ASP A CG  
65   O  OD1 . ASP A 10  ? 0.5727 0.1661 0.4257 0.0130  -0.0220 -0.0348 10  ASP A OD1 
66   O  OD2 . ASP A 10  ? 0.6029 0.2383 0.3422 -0.0541 -0.0435 -0.1008 10  ASP A OD2 
67   N  N   . GLY A 11  ? 0.2527 0.0445 0.2615 0.0168  -0.0584 -0.0240 11  GLY A N   
68   C  CA  . GLY A 11  ? 0.2119 0.0287 0.1952 0.0009  -0.0157 0.0081  11  GLY A CA  
69   C  C   . GLY A 11  ? 0.1775 0.0145 0.1755 -0.0207 -0.0641 0.0000  11  GLY A C   
70   O  O   . GLY A 11  ? 0.1819 0.0480 0.1992 -0.0135 -0.0280 0.0364  11  GLY A O   
71   N  N   . GLU A 12  ? 0.1503 0.0268 0.1882 -0.0153 -0.0524 -0.0171 12  GLU A N   
72   C  CA  . GLU A 12  ? 0.1983 0.0097 0.1797 0.0080  -0.0397 0.0207  12  GLU A CA  
73   C  C   . GLU A 12  ? 0.1657 0.0113 0.2094 -0.0233 -0.0485 0.0247  12  GLU A C   
74   O  O   . GLU A 12  ? 0.1292 0.0192 0.2039 0.0012  -0.0426 0.0480  12  GLU A O   
75   C  CB  . GLU A 12  ? 0.1627 0.0103 0.2230 -0.0249 -0.0474 0.0077  12  GLU A CB  
76   C  CG  . GLU A 12  ? 0.1551 0.0103 0.1807 -0.0236 -0.0293 -0.0010 12  GLU A CG  
77   C  CD  . GLU A 12  ? 0.1388 0.0113 0.1762 0.0024  -0.0657 -0.0138 12  GLU A CD  
78   O  OE1 . GLU A 12  ? 0.1607 0.0127 0.1496 -0.0077 -0.0249 0.0170  12  GLU A OE1 
79   O  OE2 . GLU A 12  ? 0.1704 0.0256 0.1884 0.0059  -0.0440 -0.0011 12  GLU A OE2 
80   N  N   . ASN A 13  ? 0.1735 0.0102 0.2317 -0.0040 -0.0476 0.0295  13  ASN A N   
81   C  CA  . ASN A 13  ? 0.1416 0.0077 0.2290 -0.0040 -0.0428 0.0178  13  ASN A CA  
82   C  C   . ASN A 13  ? 0.1288 0.0206 0.1995 -0.0273 -0.0408 0.0204  13  ASN A C   
83   O  O   . ASN A 13  ? 0.1416 0.0311 0.1972 0.0055  -0.0223 0.0066  13  ASN A O   
84   C  CB  . ASN A 13  ? 0.1483 0.0110 0.1922 0.0063  -0.0268 0.0271  13  ASN A CB  
85   C  CG  . ASN A 13  ? 0.2312 0.0088 0.2088 0.0103  -0.0356 0.0182  13  ASN A CG  
86   O  OD1 . ASN A 13  ? 0.1527 0.0282 0.2155 -0.0164 -0.0013 0.0232  13  ASN A OD1 
87   N  ND2 . ASN A 13  ? 0.2060 0.0669 0.1733 0.0467  -0.0405 0.0103  13  ASN A ND2 
88   N  N   . SER A 14  ? 0.1627 0.0080 0.2320 -0.0148 -0.0278 -0.0055 14  SER A N   
89   C  CA  . SER A 14  ? 0.1455 0.0067 0.1938 0.0031  0.0101  0.0077  14  SER A CA  
90   C  C   . SER A 14  ? 0.1637 0.0099 0.1969 -0.0108 -0.0099 0.0238  14  SER A C   
91   O  O   . SER A 14  ? 0.1571 0.0207 0.1909 -0.0407 -0.0331 0.0244  14  SER A O   
92   C  CB  . SER A 14  ? 0.2147 0.0131 0.2673 -0.0324 0.0769  -0.0318 14  SER A CB  
93   O  OG  . SER A 14  ? 0.2187 0.0839 0.3703 -0.0154 0.0493  -0.0407 14  SER A OG  
94   N  N   . TRP A 15  ? 0.1347 0.0300 0.1915 0.0055  -0.0348 -0.0070 15  TRP A N   
95   C  CA  . TRP A 15  ? 0.1509 0.0304 0.2060 0.0241  -0.0331 0.0216  15  TRP A CA  
96   C  C   . TRP A 15  ? 0.1492 0.0101 0.1884 -0.0133 -0.0255 -0.0183 15  TRP A C   
97   O  O   . TRP A 15  ? 0.1600 0.0092 0.2398 -0.0210 -0.0688 0.0138  15  TRP A O   
98   C  CB  . TRP A 15  ? 0.1485 0.0357 0.2191 0.0281  -0.0064 0.0216  15  TRP A CB  
99   C  CG  . TRP A 15  ? 0.1643 0.0147 0.1782 0.0223  -0.0447 -0.0080 15  TRP A CG  
100  C  CD1 . TRP A 15  ? 0.2103 0.0415 0.1775 -0.0283 -0.0005 0.0318  15  TRP A CD1 
101  C  CD2 . TRP A 15  ? 0.1435 0.0262 0.1873 0.0389  -0.0310 0.0039  15  TRP A CD2 
102  N  NE1 . TRP A 15  ? 0.1873 0.0476 0.1649 -0.0111 -0.0434 0.0076  15  TRP A NE1 
103  C  CE2 . TRP A 15  ? 0.1862 0.0090 0.1841 -0.0191 -0.0344 0.0139  15  TRP A CE2 
104  C  CE3 . TRP A 15  ? 0.1395 0.0101 0.1879 0.0022  0.0027  0.0064  15  TRP A CE3 
105  C  CZ2 . TRP A 15  ? 0.1223 0.0128 0.2345 -0.0114 -0.0223 0.0255  15  TRP A CZ2 
106  C  CZ3 . TRP A 15  ? 0.1286 0.0189 0.2382 -0.0241 -0.0314 0.0439  15  TRP A CZ3 
107  C  CH2 . TRP A 15  ? 0.1286 0.0316 0.2199 0.0001  -0.0079 0.0247  15  TRP A CH2 
108  N  N   . SER A 16  ? 0.1528 0.0101 0.1692 0.0132  -0.0354 0.0044  16  SER A N   
109  C  CA  . SER A 16  ? 0.1751 0.0088 0.1866 0.0084  -0.0478 0.0161  16  SER A CA  
110  C  C   . SER A 16  ? 0.1629 0.0081 0.1823 -0.0164 -0.0183 -0.0007 16  SER A C   
111  O  O   . SER A 16  ? 0.1685 0.0462 0.1743 -0.0052 -0.0324 0.0245  16  SER A O   
112  C  CB  . SER A 16  ? 0.1770 0.0094 0.1770 0.0211  -0.0419 -0.0137 16  SER A CB  
113  O  OG  . SER A 16  ? 0.1847 0.0093 0.2405 0.0023  -0.0322 0.0259  16  SER A OG  
114  N  N   A LYS A 17  ? 0.1655 0.0090 0.1848 0.0095  -0.0229 0.0179  17  LYS A N   
115  N  N   B LYS A 17  ? 0.1740 0.0120 0.1812 0.0251  -0.0319 0.0131  17  LYS A N   
116  C  CA  A LYS A 17  ? 0.1909 0.0073 0.2390 -0.0129 -0.0224 0.0063  17  LYS A CA  
117  C  CA  B LYS A 17  ? 0.1914 0.0073 0.2072 0.0073  -0.0319 0.0104  17  LYS A CA  
118  C  C   A LYS A 17  ? 0.1963 0.0172 0.1897 -0.0212 -0.0093 0.0137  17  LYS A C   
119  C  C   B LYS A 17  ? 0.2046 0.0199 0.1825 -0.0111 -0.0072 0.0146  17  LYS A C   
120  O  O   A LYS A 17  ? 0.2199 0.0115 0.2383 -0.0233 -0.0410 0.0288  17  LYS A O   
121  O  O   B LYS A 17  ? 0.2227 0.0101 0.2360 -0.0146 -0.0342 0.0277  17  LYS A O   
122  C  CB  A LYS A 17  ? 0.2128 0.0155 0.3009 -0.0405 0.0440  0.0101  17  LYS A CB  
123  C  CB  B LYS A 17  ? 0.2358 0.0126 0.2331 -0.0225 0.0005  -0.0198 17  LYS A CB  
124  C  CG  A LYS A 17  ? 0.2374 0.0679 0.2992 -0.1139 0.0187  -0.0486 17  LYS A CG  
125  C  CG  B LYS A 17  ? 0.2053 0.0168 0.2080 -0.0400 -0.0298 -0.0158 17  LYS A CG  
126  C  CD  A LYS A 17  ? 0.2392 0.1954 0.3601 -0.2090 0.0985  -0.0682 17  LYS A CD  
127  C  CD  B LYS A 17  ? 0.2759 0.0784 0.2357 -0.0259 -0.0022 -0.0763 17  LYS A CD  
128  C  CE  A LYS A 17  ? 0.3207 0.1564 0.3283 -0.1672 0.0880  -0.0671 17  LYS A CE  
129  C  CE  B LYS A 17  ? 0.2915 0.0870 0.2594 -0.1309 0.0234  0.0032  17  LYS A CE  
130  N  NZ  A LYS A 17  ? 0.2369 0.3259 0.3322 -0.0259 0.0192  -0.0378 17  LYS A NZ  
131  N  NZ  B LYS A 17  ? 0.3982 0.1765 0.4209 -0.0234 0.0538  -0.1268 17  LYS A NZ  
132  N  N   A LYS A 18  ? 0.1902 0.0101 0.2365 -0.0158 -0.0208 0.0252  18  LYS A N   
133  N  N   B LYS A 18  ? 0.1875 0.0092 0.2407 -0.0078 -0.0182 0.0251  18  LYS A N   
134  C  CA  A LYS A 18  ? 0.1793 0.0672 0.2204 -0.0322 -0.0055 -0.0110 18  LYS A CA  
135  C  CA  B LYS A 18  ? 0.1829 0.0203 0.2412 -0.0179 -0.0079 0.0096  18  LYS A CA  
136  C  C   A LYS A 18  ? 0.1620 0.0371 0.2184 -0.0236 -0.0315 0.0018  18  LYS A C   
137  C  C   B LYS A 18  ? 0.1668 0.0354 0.2417 -0.0162 -0.0339 -0.0212 18  LYS A C   
138  O  O   A LYS A 18  ? 0.1646 0.0124 0.1737 -0.0152 -0.0496 0.0312  18  LYS A O   
139  O  O   B LYS A 18  ? 0.1521 0.1456 0.1349 0.0462  -0.0419 0.0819  18  LYS A O   
140  C  CB  A LYS A 18  ? 0.2293 0.0924 0.2415 -0.0041 -0.0533 -0.0118 18  LYS A CB  
141  C  CB  B LYS A 18  ? 0.2032 0.0177 0.2630 -0.0469 -0.0299 0.0132  18  LYS A CB  
142  C  CG  A LYS A 18  ? 0.2610 0.1604 0.3185 0.0113  -0.0587 -0.0829 18  LYS A CG  
143  C  CG  B LYS A 18  ? 0.2186 0.0359 0.2635 -0.0716 -0.0370 0.0491  18  LYS A CG  
144  C  CD  A LYS A 18  ? 0.3607 0.1579 0.3211 0.0173  -0.0172 -0.0387 18  LYS A CD  
145  C  CD  B LYS A 18  ? 0.2624 0.1947 0.3025 -0.0376 -0.1074 0.0073  18  LYS A CD  
146  C  CE  A LYS A 18  ? 0.3084 0.0467 0.4360 0.0876  -0.1131 -0.0533 18  LYS A CE  
147  C  CE  B LYS A 18  ? 0.2422 0.2991 0.4073 -0.0061 -0.2016 -0.0275 18  LYS A CE  
148  N  NZ  A LYS A 18  ? 0.4092 0.1216 0.5352 0.0237  -0.0198 -0.0453 18  LYS A NZ  
149  N  NZ  B LYS A 18  ? 0.4485 0.3970 0.2879 -0.0358 -0.1008 -0.0465 18  LYS A NZ  
150  N  N   . TYR A 19  ? 0.1836 0.0186 0.1988 0.0021  -0.0347 0.0092  19  TYR A N   
151  C  CA  . TYR A 19  ? 0.2023 0.0088 0.2098 -0.0220 -0.0116 -0.0017 19  TYR A CA  
152  C  C   . TYR A 19  ? 0.1360 0.0083 0.2164 -0.0149 -0.0241 0.0107  19  TYR A C   
153  O  O   . TYR A 19  ? 0.1495 0.0084 0.2041 -0.0168 -0.0154 -0.0023 19  TYR A O   
154  C  CB  . TYR A 19  ? 0.1890 0.0374 0.1987 -0.0607 -0.0502 0.0366  19  TYR A CB  
155  C  CG  . TYR A 19  ? 0.1730 0.0096 0.2056 0.0019  -0.0678 0.0229  19  TYR A CG  
156  C  CD1 . TYR A 19  ? 0.1913 0.0744 0.2203 -0.0333 -0.0723 0.0230  19  TYR A CD1 
157  C  CD2 . TYR A 19  ? 0.2295 0.0117 0.2286 -0.0005 -0.0573 0.0335  19  TYR A CD2 
158  C  CE1 . TYR A 19  ? 0.2273 0.0247 0.2186 -0.0163 -0.0787 0.0206  19  TYR A CE1 
159  C  CE2 . TYR A 19  ? 0.2542 0.0162 0.2211 0.0044  -0.0544 0.0334  19  TYR A CE2 
160  C  CZ  . TYR A 19  ? 0.2663 0.0650 0.2119 -0.0347 -0.0696 0.0092  19  TYR A CZ  
161  O  OH  . TYR A 19  ? 0.3278 0.1033 0.2274 -0.0273 -0.1075 0.0369  19  TYR A OH  
162  N  N   . PRO A 20  ? 0.1442 0.0090 0.2328 -0.0179 -0.0419 -0.0033 20  PRO A N   
163  C  CA  . PRO A 20  ? 0.1643 0.0082 0.2116 -0.0145 -0.0515 0.0146  20  PRO A CA  
164  C  C   . PRO A 20  ? 0.1162 0.0449 0.2449 0.0271  -0.0011 -0.0172 20  PRO A C   
165  O  O   . PRO A 20  ? 0.1480 0.0440 0.2121 0.0127  -0.0321 0.0219  20  PRO A O   
166  C  CB  . PRO A 20  ? 0.1456 0.0396 0.2159 -0.0151 -0.0386 0.0425  20  PRO A CB  
167  C  CG  . PRO A 20  ? 0.2085 0.1503 0.2906 -0.0806 -0.0819 0.0178  20  PRO A CG  
168  C  CD  . PRO A 20  ? 0.1556 0.0189 0.2543 -0.0298 -0.0633 -0.0258 20  PRO A CD  
169  N  N   . SER A 21  ? 0.1252 0.0434 0.2275 0.0331  -0.0148 0.0201  21  SER A N   
170  C  CA  . SER A 21  ? 0.1269 0.0699 0.1517 0.0441  0.0000  0.0162  21  SER A CA  
171  C  C   . SER A 21  ? 0.0925 0.0771 0.1963 0.0211  -0.0223 -0.0145 21  SER A C   
172  O  O   . SER A 21  ? 0.1597 0.0505 0.1430 0.0400  -0.0326 0.0124  21  SER A O   
173  C  CB  . SER A 21  ? 0.1148 0.0961 0.2053 0.0179  0.0134  0.0164  21  SER A CB  
174  O  OG  . SER A 21  ? 0.1309 0.0969 0.2483 0.0154  0.0042  0.0569  21  SER A OG  
175  N  N   . CYS A 22  ? 0.1225 0.0216 0.1665 -0.0068 -0.0264 0.0171  22  CYS A N   
176  C  CA  . CYS A 22  ? 0.1223 0.0458 0.1492 0.0097  -0.0198 0.0422  22  CYS A CA  
177  C  C   . CYS A 22  ? 0.1169 0.0091 0.1438 -0.0151 -0.0161 -0.0074 22  CYS A C   
178  O  O   . CYS A 22  ? 0.1320 0.0128 0.1917 -0.0234 -0.0302 0.0251  22  CYS A O   
179  C  CB  . CYS A 22  ? 0.1866 0.0230 0.1449 -0.0069 -0.0141 0.0163  22  CYS A CB  
180  S  SG  . CYS A 22  ? 0.1866 0.0125 0.2125 -0.0245 -0.0318 0.0281  22  CYS A SG  
181  N  N   . GLY A 23  ? 0.1254 0.0369 0.1912 0.0074  -0.0361 0.0190  23  GLY A N   
182  C  CA  . GLY A 23  ? 0.1424 0.0171 0.2048 -0.0125 -0.0442 0.0461  23  GLY A CA  
183  C  C   . GLY A 23  ? 0.1676 0.0112 0.2351 -0.0125 -0.0321 0.0323  23  GLY A C   
184  O  O   . GLY A 23  ? 0.1699 0.0106 0.2266 -0.0146 -0.0315 0.0279  23  GLY A O   
185  N  N   . GLY A 24  ? 0.1708 0.0551 0.1902 0.0079  -0.0366 0.0294  24  GLY A N   
186  C  CA  . GLY A 24  ? 0.2016 0.1011 0.1753 0.0258  -0.0548 0.0001  24  GLY A CA  
187  C  C   . GLY A 24  ? 0.1782 0.0763 0.1283 0.0063  -0.0300 0.0476  24  GLY A C   
188  O  O   . GLY A 24  ? 0.1995 0.0877 0.1769 -0.0089 -0.0127 0.0312  24  GLY A O   
189  N  N   . LEU A 25  ? 0.2137 0.0941 0.1693 0.0480  -0.0208 0.0152  25  LEU A N   
190  C  CA  . LEU A 25  ? 0.2581 0.0922 0.1555 0.0854  -0.0185 0.0280  25  LEU A CA  
191  C  C   . LEU A 25  ? 0.2303 0.0542 0.1243 0.0333  -0.0452 0.0221  25  LEU A C   
192  O  O   . LEU A 25  ? 0.2092 0.0740 0.1597 0.0043  -0.0152 0.0218  25  LEU A O   
193  C  CB  . LEU A 25  ? 0.4318 0.1123 0.1112 0.0347  -0.0495 0.0351  25  LEU A CB  
194  C  CG  . LEU A 25  ? 0.4291 0.2552 0.2495 0.0763  -0.0512 0.1302  25  LEU A CG  
195  C  CD1 . LEU A 25  ? 0.5418 0.1726 0.1891 0.0380  -0.0647 0.0662  25  LEU A CD1 
196  C  CD2 . LEU A 25  ? 0.4375 0.1901 0.2509 0.0838  -0.0358 0.1001  25  LEU A CD2 
197  N  N   . LEU A 26  ? 0.2744 0.0629 0.1492 0.0034  -0.0222 0.0158  26  LEU A N   
198  C  CA  . LEU A 26  ? 0.2010 0.1262 0.1327 0.0109  -0.0335 0.0211  26  LEU A CA  
199  C  C   . LEU A 26  ? 0.1931 0.0559 0.1391 0.0012  0.0044  0.0212  26  LEU A C   
200  O  O   . LEU A 26  ? 0.2189 0.1567 0.1428 0.0522  -0.0113 0.0141  26  LEU A O   
201  C  CB  . LEU A 26  ? 0.2551 0.1279 0.1775 0.0267  0.0458  0.0257  26  LEU A CB  
202  C  CG  . LEU A 26  ? 0.4031 0.2954 0.2055 -0.0178 0.0991  -0.0785 26  LEU A CG  
203  C  CD1 . LEU A 26  ? 0.4183 0.4382 0.2115 0.0151  0.1296  0.0165  26  LEU A CD1 
204  C  CD2 . LEU A 26  ? 0.4132 0.2663 0.1949 -0.0480 0.0456  -0.0098 26  LEU A CD2 
205  N  N   . GLN A 27  ? 0.2067 0.0422 0.1062 0.0006  0.0046  -0.0027 27  GLN A N   
206  C  CA  . GLN A 27  ? 0.1298 0.0640 0.1114 0.0160  -0.0065 0.0377  27  GLN A CA  
207  C  C   . GLN A 27  ? 0.1270 0.0554 0.1410 -0.0041 -0.0355 0.0324  27  GLN A C   
208  O  O   . GLN A 27  ? 0.1435 0.0766 0.1542 0.0035  -0.0506 0.0259  27  GLN A O   
209  C  CB  . GLN A 27  ? 0.1773 0.0170 0.1538 0.0332  -0.0057 0.0237  27  GLN A CB  
210  C  CG  . GLN A 27  ? 0.1243 0.0129 0.1284 0.0003  -0.0087 0.0245  27  GLN A CG  
211  C  CD  . GLN A 27  ? 0.1159 0.0580 0.1478 0.0229  -0.0193 0.0168  27  GLN A CD  
212  O  OE1 . GLN A 27  ? 0.1581 0.0478 0.1421 0.0030  -0.0034 0.0381  27  GLN A OE1 
213  N  NE2 . GLN A 27  ? 0.1275 0.0449 0.1654 0.0126  -0.0072 0.0326  27  GLN A NE2 
214  N  N   . SER A 28  ? 0.1106 0.0322 0.1284 0.0157  -0.0192 0.0456  28  SER A N   
215  C  CA  . SER A 28  ? 0.1216 0.0564 0.1301 0.0165  -0.0120 0.0678  28  SER A CA  
216  C  C   . SER A 28  ? 0.0954 0.0879 0.1410 -0.0145 0.0011  0.0304  28  SER A C   
217  O  O   . SER A 28  ? 0.1027 0.1053 0.1279 0.0356  -0.0196 0.0098  28  SER A O   
218  C  CB  . SER A 28  ? 0.1173 0.0323 0.1410 0.0219  -0.0201 0.0217  28  SER A CB  
219  O  OG  . SER A 28  ? 0.1223 0.0581 0.1538 0.0126  -0.0006 -0.0015 28  SER A OG  
220  N  N   . PRO A 29  ? 0.1060 0.0340 0.1284 -0.0159 -0.0035 0.0012  29  PRO A N   
221  C  CA  . PRO A 29  ? 0.1494 0.0365 0.1383 0.0019  -0.0116 0.0034  29  PRO A CA  
222  C  C   . PRO A 29  ? 0.1205 0.0431 0.1166 0.0178  -0.0085 -0.0050 29  PRO A C   
223  O  O   . PRO A 29  ? 0.1392 0.0491 0.1699 0.0174  -0.0116 0.0117  29  PRO A O   
224  C  CB  . PRO A 29  ? 0.1417 0.0742 0.1347 -0.0013 -0.0089 0.0131  29  PRO A CB  
225  C  CG  . PRO A 29  ? 0.1834 0.0117 0.1537 -0.0095 0.0142  0.0215  29  PRO A CG  
226  C  CD  . PRO A 29  ? 0.1288 0.0099 0.1215 -0.0118 -0.0079 0.0125  29  PRO A CD  
227  N  N   . ILE A 30  ? 0.1621 0.0379 0.1550 0.0157  -0.0076 0.0016  30  ILE A N   
228  C  CA  . ILE A 30  ? 0.1391 0.0559 0.1532 0.0330  -0.0149 0.0078  30  ILE A CA  
229  C  C   . ILE A 30  ? 0.1232 0.0737 0.1710 -0.0013 -0.0363 0.0184  30  ILE A C   
230  O  O   . ILE A 30  ? 0.1410 0.0268 0.1855 0.0181  -0.0387 0.0049  30  ILE A O   
231  C  CB  . ILE A 30  ? 0.1586 0.0498 0.1762 -0.0120 0.0223  0.0149  30  ILE A CB  
232  C  CG1 . ILE A 30  ? 0.1179 0.1334 0.1428 -0.0171 0.0127  0.0096  30  ILE A CG1 
233  C  CG2 . ILE A 30  ? 0.1650 0.0469 0.1744 -0.0482 0.0262  -0.0017 30  ILE A CG2 
234  C  CD1 . ILE A 30  ? 0.1883 0.2412 0.1359 0.0067  -0.0093 0.0009  30  ILE A CD1 
235  N  N   . ASP A 31  ? 0.1039 0.0349 0.1600 0.0183  -0.0368 0.0233  31  ASP A N   
236  C  CA  . ASP A 31  ? 0.1413 0.0518 0.2060 -0.0113 0.0084  0.0287  31  ASP A CA  
237  C  C   . ASP A 31  ? 0.1557 0.0722 0.1574 0.0128  -0.0046 0.0505  31  ASP A C   
238  O  O   . ASP A 31  ? 0.1983 0.0961 0.1613 -0.0189 -0.0502 0.0303  31  ASP A O   
239  C  CB  . ASP A 31  ? 0.1341 0.0627 0.2227 0.0124  -0.0269 0.0491  31  ASP A CB  
240  C  CG  . ASP A 31  ? 0.1715 0.0649 0.2506 0.0150  -0.0197 0.0624  31  ASP A CG  
241  O  OD1 . ASP A 31  ? 0.1467 0.0723 0.2040 0.0009  -0.0311 0.0329  31  ASP A OD1 
242  O  OD2 . ASP A 31  ? 0.2048 0.1694 0.2741 -0.0187 -0.0473 0.0628  31  ASP A OD2 
243  N  N   . LEU A 32  ? 0.1250 0.0658 0.1726 -0.0013 -0.0192 0.0396  32  LEU A N   
244  C  CA  . LEU A 32  ? 0.1448 0.1362 0.1482 0.0110  -0.0172 0.0111  32  LEU A CA  
245  C  C   . LEU A 32  ? 0.1349 0.2006 0.2455 -0.0305 -0.0154 0.0883  32  LEU A C   
246  O  O   . LEU A 32  ? 0.1893 0.0626 0.2483 0.0006  -0.0085 0.0140  32  LEU A O   
247  C  CB  . LEU A 32  ? 0.1363 0.0981 0.1791 0.0088  -0.0283 -0.0189 32  LEU A CB  
248  C  CG  . LEU A 32  ? 0.1415 0.1172 0.1409 -0.0152 -0.0188 -0.0130 32  LEU A CG  
249  C  CD1 . LEU A 32  ? 0.1507 0.1341 0.2071 -0.0116 -0.0269 0.0417  32  LEU A CD1 
250  C  CD2 . LEU A 32  ? 0.1879 0.1839 0.1689 0.0134  0.0250  0.0141  32  LEU A CD2 
251  N  N   A HIS A 33  ? 0.2547 0.2827 0.1884 -0.0732 -0.0688 0.0441  33  HIS A N   
252  N  N   B HIS A 33  ? 0.1976 0.1927 0.2013 -0.0732 -0.0242 0.0760  33  HIS A N   
253  C  CA  A HIS A 33  ? 0.2595 0.3565 0.2198 -0.1109 -0.0952 0.0603  33  HIS A CA  
254  C  CA  B HIS A 33  ? 0.1431 0.2533 0.2369 -0.0121 -0.1047 0.0532  33  HIS A CA  
255  C  C   A HIS A 33  ? 0.2496 0.3197 0.2787 -0.0636 -0.0702 0.0365  33  HIS A C   
256  C  C   B HIS A 33  ? 0.2128 0.2714 0.2495 -0.0157 -0.0384 0.0530  33  HIS A C   
257  O  O   A HIS A 33  ? 0.1184 0.5213 0.1979 -0.0573 -0.0479 -0.0637 33  HIS A O   
258  O  O   B HIS A 33  ? 0.2531 0.1042 0.2672 -0.0465 -0.0296 0.0540  33  HIS A O   
259  C  CB  A HIS A 33  ? 0.2947 0.4480 0.1679 -0.0785 0.0134  0.0774  33  HIS A CB  
260  C  CB  B HIS A 33  ? 0.1239 0.2067 0.2466 -0.0128 0.0010  0.0741  33  HIS A CB  
261  C  CG  A HIS A 33  ? 0.3244 0.4393 0.1591 -0.1273 0.0958  0.1295  33  HIS A CG  
262  C  CG  B HIS A 33  ? 0.1049 0.0990 0.2918 0.0325  0.0065  0.0237  33  HIS A CG  
263  N  ND1 A HIS A 33  ? 0.2713 0.4285 0.2196 -0.0719 0.0524  -0.0111 33  HIS A ND1 
264  N  ND1 B HIS A 33  ? 0.1377 0.2250 0.3243 -0.0256 0.0089  -0.0293 33  HIS A ND1 
265  C  CD2 A HIS A 33  ? 0.4056 0.5547 0.1337 -0.1485 0.0924  0.1187  33  HIS A CD2 
266  C  CD2 B HIS A 33  ? 0.1076 0.1599 0.2949 0.0065  0.0132  0.0046  33  HIS A CD2 
267  C  CE1 A HIS A 33  ? 0.3240 0.5412 0.2281 -0.1047 0.0162  0.0314  33  HIS A CE1 
268  C  CE1 B HIS A 33  ? 0.1482 0.1909 0.3301 -0.0522 -0.0198 -0.0611 33  HIS A CE1 
269  N  NE2 A HIS A 33  ? 0.3913 0.4161 0.2891 -0.1655 0.1268  0.0243  33  HIS A NE2 
270  N  NE2 B HIS A 33  ? 0.1557 0.2532 0.3283 -0.0401 0.0231  -0.0464 33  HIS A NE2 
271  N  N   . SER A 34  ? 0.2841 0.2869 0.3364 -0.0281 -0.1125 0.0439  34  SER A N   
272  C  CA  . SER A 34  ? 0.3342 0.2448 0.4823 -0.1274 -0.0590 -0.0103 34  SER A CA  
273  C  C   . SER A 34  ? 0.3346 0.3062 0.4335 -0.0812 -0.0965 -0.0584 34  SER A C   
274  O  O   . SER A 34  ? 0.3905 0.4815 0.4181 0.0089  -0.1415 -0.1664 34  SER A O   
275  C  CB  . SER A 34  ? 0.4453 0.3238 0.8996 -0.2404 -0.0177 0.0311  34  SER A CB  
276  O  OG  . SER A 34  ? 0.7245 0.3085 1.0252 -0.0807 0.1930  -0.0068 34  SER A OG  
277  N  N   . ASP A 35  ? 0.2830 0.5423 0.3712 -0.0494 -0.1079 -0.0434 35  ASP A N   
278  C  CA  . ASP A 35  ? 0.3310 0.4798 0.4044 -0.0111 -0.1406 -0.0355 35  ASP A CA  
279  C  C   . ASP A 35  ? 0.3046 0.4695 0.3911 0.0063  -0.1566 -0.0533 35  ASP A C   
280  O  O   . ASP A 35  ? 0.3927 0.6024 0.4140 -0.0212 -0.2210 -0.0267 35  ASP A O   
281  C  CB  . ASP A 35  ? 0.2515 0.7043 0.3248 -0.0752 -0.0506 0.0282  35  ASP A CB  
282  C  CG  . ASP A 35  ? 0.3697 0.6776 0.5360 -0.1241 0.0950  -0.1192 35  ASP A CG  
283  O  OD1 . ASP A 35  ? 0.3893 0.6593 0.8423 -0.2624 -0.0396 -0.2470 35  ASP A OD1 
284  O  OD2 . ASP A 35  ? 0.2927 0.9605 0.4903 -0.1134 0.0487  -0.1639 35  ASP A OD2 
285  N  N   . ILE A 36  ? 0.2037 0.4362 0.2376 0.0352  -0.0666 -0.0326 36  ILE A N   
286  C  CA  . ILE A 36  ? 0.1833 0.4823 0.2746 0.0334  -0.0633 0.0051  36  ILE A CA  
287  C  C   . ILE A 36  ? 0.2038 0.3855 0.1828 0.0675  -0.0478 0.0135  36  ILE A C   
288  O  O   . ILE A 36  ? 0.2324 0.4982 0.2195 0.0108  -0.0024 0.0672  36  ILE A O   
289  C  CB  . ILE A 36  ? 0.1995 0.4602 0.1949 0.0197  0.0002  0.0478  36  ILE A CB  
290  C  CG1 . ILE A 36  ? 0.2969 0.3121 0.1861 -0.0917 -0.0025 0.0612  36  ILE A CG1 
291  C  CG2 . ILE A 36  ? 0.2272 0.5527 0.3145 0.0424  -0.0620 0.0524  36  ILE A CG2 
292  C  CD1 . ILE A 36  ? 0.3388 0.2399 0.2882 -0.0075 0.0819  0.0365  36  ILE A CD1 
293  N  N   . LEU A 37  ? 0.2268 0.3629 0.2240 0.0057  -0.0461 0.0211  37  LEU A N   
294  C  CA  . LEU A 37  ? 0.2202 0.3086 0.2670 0.0188  0.0254  0.0280  37  LEU A CA  
295  C  C   . LEU A 37  ? 0.2433 0.4034 0.2531 0.0155  -0.0271 -0.0107 37  LEU A C   
296  O  O   . LEU A 37  ? 0.3416 0.3897 0.2942 -0.0032 -0.0532 -0.0460 37  LEU A O   
297  C  CB  . LEU A 37  ? 0.2588 0.3808 0.1823 -0.0558 -0.0285 0.0237  37  LEU A CB  
298  C  CG  . LEU A 37  ? 0.2531 0.3249 0.2026 -0.0663 -0.0106 0.0013  37  LEU A CG  
299  C  CD1 . LEU A 37  ? 0.2949 0.3143 0.2961 -0.0996 -0.0139 0.0480  37  LEU A CD1 
300  C  CD2 . LEU A 37  ? 0.2223 0.2784 0.2175 -0.0167 -0.0153 -0.0108 37  LEU A CD2 
301  N  N   . GLN A 38  ? 0.2326 0.4101 0.1800 0.0131  -0.0690 -0.0358 38  GLN A N   
302  C  CA  . GLN A 38  ? 0.2521 0.4020 0.2010 0.0346  -0.0675 -0.0420 38  GLN A CA  
303  C  C   . GLN A 38  ? 0.2662 0.3033 0.1593 0.0526  -0.0370 0.0189  38  GLN A C   
304  O  O   . GLN A 38  ? 0.2579 0.3398 0.1967 0.0526  -0.0677 -0.0231 38  GLN A O   
305  C  CB  . GLN A 38  ? 0.3118 0.4494 0.2034 0.0710  -0.0766 -0.0348 38  GLN A CB  
306  C  CG  . GLN A 38  ? 0.3810 0.5019 0.2618 0.1231  -0.0186 -0.0329 38  GLN A CG  
307  C  CD  . GLN A 38  ? 0.3939 0.5268 0.2622 0.0274  -0.0337 -0.0561 38  GLN A CD  
308  O  OE1 . GLN A 38  ? 0.4205 0.7059 0.4024 0.1455  -0.1246 -0.2569 38  GLN A OE1 
309  N  NE2 . GLN A 38  ? 0.3944 0.6793 0.4042 0.0193  0.1031  -0.0100 38  GLN A NE2 
310  N  N   . TYR A 39  ? 0.3219 0.3209 0.2358 0.0427  -0.0447 -0.0091 39  TYR A N   
311  C  CA  . TYR A 39  ? 0.3153 0.1336 0.2508 0.0273  -0.0163 -0.0273 39  TYR A CA  
312  C  C   . TYR A 39  ? 0.3051 0.2358 0.2067 0.0417  -0.0343 -0.0149 39  TYR A C   
313  O  O   . TYR A 39  ? 0.3052 0.2361 0.2213 0.0473  -0.0416 0.0010  39  TYR A O   
314  C  CB  . TYR A 39  ? 0.3827 0.1423 0.2317 -0.0152 0.0254  -0.0414 39  TYR A CB  
315  C  CG  . TYR A 39  ? 0.3850 0.0769 0.2786 0.0019  -0.0177 -0.0651 39  TYR A CG  
316  C  CD1 . TYR A 39  ? 0.3315 0.2511 0.2822 0.0186  0.0024  -0.0155 39  TYR A CD1 
317  C  CD2 . TYR A 39  ? 0.4635 0.1654 0.3427 0.0499  0.0234  -0.1252 39  TYR A CD2 
318  C  CE1 . TYR A 39  ? 0.3310 0.1257 0.3181 0.0127  0.0290  -0.0566 39  TYR A CE1 
319  C  CE2 . TYR A 39  ? 0.4903 0.2907 0.4774 0.0982  0.0125  -0.1345 39  TYR A CE2 
320  C  CZ  . TYR A 39  ? 0.3802 0.3046 0.4019 0.1211  0.0722  -0.1080 39  TYR A CZ  
321  O  OH  . TYR A 39  ? 0.4324 0.3288 0.6423 0.2108  -0.0653 -0.2104 39  TYR A OH  
322  N  N   . ASP A 40  ? 0.3255 0.1445 0.2278 -0.0149 -0.0126 -0.0072 40  ASP A N   
323  C  CA  . ASP A 40  ? 0.2981 0.1315 0.2846 0.0466  -0.0053 0.0427  40  ASP A CA  
324  C  C   . ASP A 40  ? 0.2931 0.1108 0.2049 0.0512  -0.0054 -0.0309 40  ASP A C   
325  O  O   . ASP A 40  ? 0.2937 0.1380 0.1941 -0.0150 0.0092  -0.0038 40  ASP A O   
326  C  CB  . ASP A 40  ? 0.3378 0.1340 0.2113 0.0828  0.0337  0.0238  40  ASP A CB  
327  C  CG  . ASP A 40  ? 0.3779 0.1963 0.3761 0.1018  0.0612  0.1060  40  ASP A CG  
328  O  OD1 . ASP A 40  ? 0.3471 0.4142 0.3037 0.1138  0.0810  0.1298  40  ASP A OD1 
329  O  OD2 . ASP A 40  ? 0.6319 0.2009 0.4382 0.1116  0.0766  0.0864  40  ASP A OD2 
330  N  N   . ALA A 41  ? 0.4324 0.2534 0.2389 0.1204  0.0248  -0.0738 41  ALA A N   
331  C  CA  . ALA A 41  ? 0.4586 0.3861 0.2698 0.1611  0.0226  -0.0944 41  ALA A CA  
332  C  C   . ALA A 41  ? 0.4846 0.4389 0.2274 0.1263  0.0244  0.0728  41  ALA A C   
333  O  O   . ALA A 41  ? 0.5686 0.4814 0.2823 0.2884  0.0545  -0.0552 41  ALA A O   
334  C  CB  . ALA A 41  ? 0.5105 0.5252 0.3177 0.0315  0.0273  -0.2039 41  ALA A CB  
335  N  N   . SER A 42  ? 0.4990 0.3974 0.2230 0.1165  0.1188  0.0653  42  SER A N   
336  C  CA  . SER A 42  ? 0.5008 0.2552 0.3012 0.1336  0.2081  0.1230  42  SER A CA  
337  C  C   . SER A 42  ? 0.4037 0.3998 0.3611 0.0377  0.1158  0.1973  42  SER A C   
338  O  O   . SER A 42  ? 0.3271 0.5514 0.4536 0.0212  0.1205  0.2285  42  SER A O   
339  C  CB  . SER A 42  ? 0.3771 0.3134 0.6062 0.1131  0.1713  0.2628  42  SER A CB  
340  O  OG  . SER A 42  ? 0.5970 0.4386 0.5313 0.1637  0.2080  0.2472  42  SER A OG  
341  N  N   . LEU A 43  ? 0.3028 0.1521 0.3139 -0.0040 0.0727  0.0403  43  LEU A N   
342  C  CA  . LEU A 43  ? 0.2444 0.1880 0.3369 0.0127  0.0638  -0.0203 43  LEU A CA  
343  C  C   . LEU A 43  ? 0.1672 0.2332 0.3511 -0.0322 0.0331  -0.0033 43  LEU A C   
344  O  O   . LEU A 43  ? 0.2185 0.2309 0.4514 -0.0364 0.0530  0.0097  43  LEU A O   
345  C  CB  . LEU A 43  ? 0.2037 0.1293 0.3052 0.0194  0.0249  -0.0075 43  LEU A CB  
346  C  CG  . LEU A 43  ? 0.2256 0.1462 0.3186 0.0248  0.0433  0.0345  43  LEU A CG  
347  C  CD1 . LEU A 43  ? 0.2048 0.1514 0.2622 0.0308  0.0133  0.0595  43  LEU A CD1 
348  C  CD2 . LEU A 43  ? 0.2344 0.1556 0.2625 0.0067  0.0328  0.0964  43  LEU A CD2 
349  N  N   . THR A 44  ? 0.1836 0.2706 0.2435 -0.0501 0.0532  -0.0409 44  THR A N   
350  C  CA  . THR A 44  ? 0.2230 0.2698 0.2302 0.0167  0.0650  -0.0351 44  THR A CA  
351  C  C   . THR A 44  ? 0.2026 0.2528 0.2149 -0.0027 0.0704  0.0055  44  THR A C   
352  O  O   . THR A 44  ? 0.1870 0.2685 0.2207 0.0064  0.0190  -0.0170 44  THR A O   
353  C  CB  . THR A 44  ? 0.2630 0.3494 0.2881 -0.0188 0.1035  -0.0663 44  THR A CB  
354  O  OG1 . THR A 44  ? 0.2286 0.2982 0.4034 0.0020  0.0718  0.0081  44  THR A OG1 
355  C  CG2 . THR A 44  ? 0.3100 0.5254 0.2674 0.1228  0.0734  -0.0296 44  THR A CG2 
356  N  N   . PRO A 45  ? 0.2282 0.1650 0.2469 0.0280  0.0403  -0.0726 45  PRO A N   
357  C  CA  . PRO A 45  ? 0.1642 0.1908 0.2495 0.0196  0.0387  -0.0565 45  PRO A CA  
358  C  C   . PRO A 45  ? 0.2049 0.2074 0.2374 0.0032  0.0203  -0.0454 45  PRO A C   
359  O  O   . PRO A 45  ? 0.2285 0.2649 0.3080 -0.0153 0.0499  -0.0814 45  PRO A O   
360  C  CB  . PRO A 45  ? 0.2322 0.2131 0.3252 0.0693  0.0436  -0.0548 45  PRO A CB  
361  C  CG  . PRO A 45  ? 0.2996 0.1925 0.3373 0.0496  0.0385  -0.0494 45  PRO A CG  
362  C  CD  . PRO A 45  ? 0.2518 0.2418 0.2902 0.1204  0.0343  -0.0788 45  PRO A CD  
363  N  N   . LEU A 46  ? 0.1836 0.1352 0.2141 0.0335  0.0118  0.0185  46  LEU A N   
364  C  CA  . LEU A 46  ? 0.1509 0.2069 0.2447 0.0221  0.0050  -0.0070 46  LEU A CA  
365  C  C   . LEU A 46  ? 0.1710 0.1866 0.2411 0.0323  0.0096  0.0145  46  LEU A C   
366  O  O   . LEU A 46  ? 0.2543 0.2321 0.2439 -0.0048 0.0119  0.0270  46  LEU A O   
367  C  CB  . LEU A 46  ? 0.2054 0.0837 0.2283 0.0488  -0.0197 0.0341  46  LEU A CB  
368  C  CG  . LEU A 46  ? 0.1647 0.1549 0.2720 0.0461  -0.0012 0.0748  46  LEU A CG  
369  C  CD1 . LEU A 46  ? 0.1571 0.2297 0.3010 0.0362  -0.0366 -0.0238 46  LEU A CD1 
370  C  CD2 . LEU A 46  ? 0.2247 0.2462 0.2972 -0.0272 -0.0390 0.1240  46  LEU A CD2 
371  N  N   . GLU A 47  ? 0.1640 0.1826 0.2189 0.0293  -0.0018 -0.0396 47  GLU A N   
372  C  CA  . GLU A 47  ? 0.1870 0.1726 0.2289 0.0391  -0.0032 0.0175  47  GLU A CA  
373  C  C   . GLU A 47  ? 0.1618 0.2207 0.2037 0.0592  -0.0408 0.0092  47  GLU A C   
374  O  O   . GLU A 47  ? 0.2101 0.2084 0.1818 0.0735  -0.0086 0.0282  47  GLU A O   
375  C  CB  . GLU A 47  ? 0.1986 0.2297 0.2827 0.0068  0.0151  -0.0369 47  GLU A CB  
376  C  CG  . GLU A 47  ? 0.3321 0.4049 0.3488 0.0510  0.0255  -0.1489 47  GLU A CG  
377  N  N   . PHE A 48  ? 0.1133 0.1525 0.2220 0.0320  -0.0225 0.0499  48  PHE A N   
378  C  CA  . PHE A 48  ? 0.1345 0.1604 0.2448 -0.0370 -0.0061 0.0367  48  PHE A CA  
379  C  C   . PHE A 48  ? 0.1212 0.1193 0.2450 -0.0069 -0.0004 0.0440  48  PHE A C   
380  O  O   . PHE A 48  ? 0.1902 0.1518 0.3325 0.0044  -0.0441 0.0825  48  PHE A O   
381  C  CB  . PHE A 48  ? 0.1300 0.2133 0.2664 -0.0135 0.0094  0.0520  48  PHE A CB  
382  C  CG  . PHE A 48  ? 0.1449 0.1506 0.2038 -0.0024 0.0195  0.0130  48  PHE A CG  
383  C  CD1 . PHE A 48  ? 0.1638 0.2196 0.2186 0.0428  0.0151  0.0108  48  PHE A CD1 
384  C  CD2 . PHE A 48  ? 0.1940 0.1657 0.2401 -0.0137 0.0476  0.0183  48  PHE A CD2 
385  C  CE1 . PHE A 48  ? 0.2001 0.1872 0.1927 0.0061  0.0128  0.0022  48  PHE A CE1 
386  C  CE2 . PHE A 48  ? 0.1776 0.1751 0.2611 -0.0098 0.0595  0.0318  48  PHE A CE2 
387  C  CZ  . PHE A 48  ? 0.1934 0.1832 0.2370 0.0355  0.0472  -0.0248 48  PHE A CZ  
388  N  N   . GLN A 49  ? 0.1191 0.1200 0.2257 -0.0077 0.0221  0.0354  49  GLN A N   
389  C  CA  . GLN A 49  ? 0.1305 0.1584 0.2254 -0.0228 0.0077  0.0403  49  GLN A CA  
390  C  C   . GLN A 49  ? 0.0954 0.1467 0.2006 0.0353  -0.0041 0.0488  49  GLN A C   
391  O  O   . GLN A 49  ? 0.1225 0.1410 0.2067 0.0512  -0.0108 0.0467  49  GLN A O   
392  C  CB  . GLN A 49  ? 0.1654 0.1611 0.2116 -0.0069 0.0367  0.0170  49  GLN A CB  
393  C  CG  . GLN A 49  ? 0.2403 0.2376 0.2034 -0.0212 0.0482  0.0000  49  GLN A CG  
394  C  CD  . GLN A 49  ? 0.3407 0.4131 0.4271 0.1146  -0.0291 -0.1145 49  GLN A CD  
395  O  OE1 . GLN A 49  ? 0.5437 0.4204 0.4903 0.2096  0.0080  -0.1543 49  GLN A OE1 
396  N  NE2 . GLN A 49  ? 0.4194 0.4393 0.3723 0.2066  -0.0329 -0.0798 49  GLN A NE2 
397  N  N   . GLY A 50  ? 0.1042 0.1507 0.1958 0.0086  -0.0201 0.0551  50  GLY A N   
398  C  CA  . GLY A 50  ? 0.1011 0.2837 0.1866 -0.0174 -0.0262 0.0344  50  GLY A CA  
399  C  C   . GLY A 50  ? 0.0963 0.2790 0.1771 0.0020  -0.0313 0.0071  50  GLY A C   
400  O  O   . GLY A 50  ? 0.1284 0.2097 0.2186 -0.0100 -0.0461 0.0305  50  GLY A O   
401  N  N   . TYR A 51  ? 0.1042 0.2146 0.2125 0.0285  -0.0033 0.0828  51  TYR A N   
402  C  CA  . TYR A 51  ? 0.1311 0.2249 0.1902 -0.0010 -0.0019 0.0567  51  TYR A CA  
403  C  C   . TYR A 51  ? 0.1485 0.1509 0.2044 0.0380  0.0026  0.0441  51  TYR A C   
404  O  O   . TYR A 51  ? 0.1388 0.2110 0.1785 0.0347  -0.0119 0.0670  51  TYR A O   
405  C  CB  . TYR A 51  ? 0.0916 0.2144 0.2060 0.0380  -0.0345 0.0618  51  TYR A CB  
406  C  CG  . TYR A 51  ? 0.0952 0.1893 0.1670 0.0403  -0.0223 0.0495  51  TYR A CG  
407  C  CD1 . TYR A 51  ? 0.1295 0.2020 0.1573 0.0238  -0.0264 0.0465  51  TYR A CD1 
408  C  CD2 . TYR A 51  ? 0.1056 0.0861 0.2293 0.0447  -0.0085 0.0793  51  TYR A CD2 
409  C  CE1 . TYR A 51  ? 0.0993 0.1949 0.1762 0.0147  -0.0270 0.0350  51  TYR A CE1 
410  C  CE2 . TYR A 51  ? 0.1126 0.0708 0.1848 0.0444  -0.0063 0.0529  51  TYR A CE2 
411  C  CZ  . TYR A 51  ? 0.1065 0.1441 0.2001 -0.0012 -0.0322 0.0898  51  TYR A CZ  
412  O  OH  . TYR A 51  ? 0.1380 0.1625 0.1866 0.0111  -0.0397 0.0904  51  TYR A OH  
413  N  N   . ASN A 52  ? 0.1611 0.1909 0.2263 0.0664  0.0084  0.0958  52  ASN A N   
414  C  CA  . ASN A 52  ? 0.1678 0.2700 0.2421 0.1016  -0.0285 0.0610  52  ASN A CA  
415  C  C   . ASN A 52  ? 0.1710 0.2026 0.3115 0.0947  -0.0146 0.0700  52  ASN A C   
416  O  O   . ASN A 52  ? 0.1713 0.3470 0.3383 0.0895  -0.0190 -0.0310 52  ASN A O   
417  C  CB  . ASN A 52  ? 0.1746 0.2168 0.2859 0.0724  -0.0275 0.1041  52  ASN A CB  
418  C  CG  . ASN A 52  ? 0.2597 0.3646 0.2861 0.1518  -0.0173 0.1394  52  ASN A CG  
419  O  OD1 . ASN A 52  ? 0.1920 0.4766 0.3137 0.0807  -0.0265 0.1761  52  ASN A OD1 
420  N  ND2 . ASN A 52  ? 0.4357 0.4298 0.5073 0.2927  -0.0124 0.1843  52  ASN A ND2 
421  N  N   . LEU A 53  ? 0.1555 0.2053 0.2649 0.0617  -0.0479 0.0245  53  LEU A N   
422  C  CA  . LEU A 53  ? 0.1582 0.2382 0.2869 0.0697  -0.0525 -0.0054 53  LEU A CA  
423  C  C   . LEU A 53  ? 0.1724 0.2798 0.4329 0.0805  -0.1491 -0.0283 53  LEU A C   
424  O  O   . LEU A 53  ? 0.3848 0.3912 0.4106 0.1030  -0.2660 0.0502  53  LEU A O   
425  C  CB  . LEU A 53  ? 0.1631 0.2234 0.2210 0.0721  -0.0443 0.0311  53  LEU A CB  
426  C  CG  . LEU A 53  ? 0.1564 0.2157 0.1722 0.0408  -0.0287 0.0513  53  LEU A CG  
427  C  CD1 . LEU A 53  ? 0.1370 0.3457 0.2450 0.1059  -0.0236 0.0271  53  LEU A CD1 
428  C  CD2 . LEU A 53  ? 0.3148 0.2380 0.2776 0.0300  0.0306  0.1465  53  LEU A CD2 
429  N  N   . SER A 54  ? 0.1765 0.3687 0.5220 0.0771  -0.1018 -0.0926 54  SER A N   
430  C  CA  . SER A 54  ? 0.3046 0.3811 0.5003 -0.0130 -0.1486 -0.0175 54  SER A CA  
431  C  C   . SER A 54  ? 0.2642 0.3138 0.5315 -0.0793 -0.1275 0.0016  54  SER A C   
432  O  O   . SER A 54  ? 0.1981 0.4816 0.4968 0.0364  -0.1263 0.0353  54  SER A O   
433  C  CB  . SER A 54  ? 0.1187 0.4311 0.4875 0.0367  -0.0223 -0.0989 54  SER A CB  
434  O  OG  . SER A 54  ? 0.2295 0.5319 0.5213 0.1557  -0.0785 -0.1210 54  SER A OG  
435  N  N   . ALA A 55  ? 0.3443 0.2852 0.6881 -0.0291 -0.1999 0.0195  55  ALA A N   
436  C  CA  . ALA A 55  ? 0.3761 0.3287 0.7069 0.1394  -0.0347 0.0187  55  ALA A CA  
437  C  C   . ALA A 55  ? 0.4684 0.4282 0.7404 0.0063  -0.0902 0.0335  55  ALA A C   
438  O  O   . ALA A 55  ? 0.4799 0.7274 0.3820 -0.0591 -0.3658 0.1483  55  ALA A O   
439  C  CB  . ALA A 55  ? 0.5624 0.4516 0.8036 0.0932  -0.3952 0.1182  55  ALA A CB  
440  N  N   . ASN A 56  ? 0.4920 0.4588 0.7974 -0.0064 -0.0615 0.1032  56  ASN A N   
441  C  CA  . ASN A 56  ? 0.5046 0.4392 0.8747 -0.1703 -0.1145 -0.0391 56  ASN A CA  
442  C  C   . ASN A 56  ? 0.4450 0.6649 0.4680 -0.0440 -0.1819 0.0149  56  ASN A C   
443  O  O   . ASN A 56  ? 0.3398 0.7677 0.5250 -0.0616 -0.1474 -0.0294 56  ASN A O   
444  C  CB  . ASN A 56  ? 0.6748 0.4729 0.9604 -0.1005 -0.1061 0.1565  56  ASN A CB  
445  C  CG  . ASN A 56  ? 0.3407 0.5545 0.8305 -0.1283 0.0972  0.1530  56  ASN A CG  
446  O  OD1 . ASN A 56  ? 0.6386 0.9851 0.7524 -0.0196 -0.1026 0.1268  56  ASN A OD1 
447  N  ND2 . ASN A 56  ? 0.3830 0.7281 0.8810 -0.1424 0.0798  0.0642  56  ASN A ND2 
448  N  N   . LYS A 57  ? 0.2583 0.3610 0.3899 0.0227  -0.0666 0.0416  57  LYS A N   
449  C  CA  . LYS A 57  ? 0.2458 0.3630 0.2493 -0.0008 -0.0644 0.0142  57  LYS A CA  
450  C  C   . LYS A 57  ? 0.2006 0.3775 0.2295 -0.0159 -0.0924 -0.0154 57  LYS A C   
451  O  O   . LYS A 57  ? 0.1584 0.4055 0.3083 0.0376  -0.0644 0.0651  57  LYS A O   
452  C  CB  . LYS A 57  ? 0.1782 0.3449 0.2310 -0.0142 -0.0086 -0.0108 57  LYS A CB  
453  C  CG  . LYS A 57  ? 0.1927 0.3514 0.2676 -0.0622 0.0086  -0.0487 57  LYS A CG  
454  C  CD  . LYS A 57  ? 0.2329 0.4456 0.2538 -0.0086 0.0132  -0.0977 57  LYS A CD  
455  C  CE  . LYS A 57  ? 0.2712 0.3310 0.3409 -0.1098 0.0411  -0.0884 57  LYS A CE  
456  N  NZ  . LYS A 57  ? 0.3389 0.3040 0.5334 -0.0873 0.0601  -0.0541 57  LYS A NZ  
457  N  N   . GLN A 58  ? 0.1825 0.4187 0.2541 0.0228  -0.0423 0.0039  58  GLN A N   
458  C  CA  . GLN A 58  ? 0.1649 0.3833 0.1848 -0.0036 -0.0727 -0.0041 58  GLN A CA  
459  C  C   . GLN A 58  ? 0.1632 0.4099 0.2031 -0.0044 -0.0776 0.0267  58  GLN A C   
460  O  O   . GLN A 58  ? 0.2035 0.4102 0.3095 -0.0416 -0.0570 0.0385  58  GLN A O   
461  C  CB  . GLN A 58  ? 0.2161 0.3782 0.1800 -0.0036 -0.0744 -0.0122 58  GLN A CB  
462  C  CG  . GLN A 58  ? 0.2146 0.2897 0.1933 0.0335  -0.0514 -0.0435 58  GLN A CG  
463  C  CD  . GLN A 58  ? 0.2448 0.3328 0.1826 0.0635  -0.0666 -0.0380 58  GLN A CD  
464  O  OE1 . GLN A 58  ? 0.2282 0.2962 0.2944 0.0015  -0.0939 -0.0208 58  GLN A OE1 
465  N  NE2 . GLN A 58  ? 0.2840 0.3171 0.2552 0.0674  -0.1289 -0.0386 58  GLN A NE2 
466  N  N   . PHE A 59  ? 0.1599 0.4329 0.1851 0.0233  -0.0803 0.0303  59  PHE A N   
467  C  CA  . PHE A 59  ? 0.1708 0.3240 0.2056 0.0260  -0.0804 0.0301  59  PHE A CA  
468  C  C   . PHE A 59  ? 0.1904 0.3513 0.2010 0.0167  -0.0810 -0.0013 59  PHE A C   
469  O  O   . PHE A 59  ? 0.1970 0.4069 0.2081 -0.0001 -0.0523 -0.0024 59  PHE A O   
470  C  CB  . PHE A 59  ? 0.2027 0.3915 0.1581 0.0346  -0.0321 0.0044  59  PHE A CB  
471  C  CG  . PHE A 59  ? 0.1395 0.3327 0.1697 0.0016  -0.0364 0.0308  59  PHE A CG  
472  C  CD1 . PHE A 59  ? 0.2368 0.4329 0.1785 0.0460  0.0181  0.0378  59  PHE A CD1 
473  C  CD2 . PHE A 59  ? 0.1805 0.3893 0.2340 0.0793  -0.0596 -0.0164 59  PHE A CD2 
474  C  CE1 . PHE A 59  ? 0.2336 0.4313 0.1884 0.0276  0.0453  0.0381  59  PHE A CE1 
475  C  CE2 . PHE A 59  ? 0.1509 0.3213 0.2236 0.0064  -0.0283 0.0072  59  PHE A CE2 
476  C  CZ  . PHE A 59  ? 0.1887 0.4398 0.2135 -0.0151 -0.0350 0.0214  59  PHE A CZ  
477  N  N   . LEU A 60  ? 0.1875 0.3431 0.2012 0.0237  -0.0907 -0.0031 60  LEU A N   
478  C  CA  . LEU A 60  ? 0.1981 0.3560 0.1629 0.0138  -0.0835 -0.0201 60  LEU A CA  
479  C  C   . LEU A 60  ? 0.1796 0.4312 0.1972 0.0432  -0.1115 0.0073  60  LEU A C   
480  O  O   . LEU A 60  ? 0.1787 0.4020 0.1859 0.0329  -0.0996 -0.0274 60  LEU A O   
481  C  CB  . LEU A 60  ? 0.2295 0.3830 0.3171 -0.0767 -0.0324 -0.0158 60  LEU A CB  
482  C  CG  . LEU A 60  ? 0.2663 0.4120 0.2751 -0.0876 -0.0124 -0.0019 60  LEU A CG  
483  C  CD1 . LEU A 60  ? 0.2979 0.5475 0.2868 -0.0605 -0.0333 -0.1008 60  LEU A CD1 
484  C  CD2 . LEU A 60  ? 0.4521 0.4829 0.2779 -0.0493 -0.0326 0.1089  60  LEU A CD2 
485  N  N   . LEU A 61  ? 0.2257 0.4391 0.1773 0.0623  -0.0759 -0.0607 61  LEU A N   
486  C  CA  . LEU A 61  ? 0.2170 0.3114 0.1926 0.0809  -0.0680 -0.0234 61  LEU A CA  
487  C  C   . LEU A 61  ? 0.1889 0.3553 0.2037 0.0768  -0.0544 -0.0410 61  LEU A C   
488  O  O   . LEU A 61  ? 0.2773 0.4478 0.1893 0.0877  -0.0672 -0.0476 61  LEU A O   
489  C  CB  . LEU A 61  ? 0.1925 0.4042 0.1797 0.0460  -0.0949 0.0171  61  LEU A CB  
490  C  CG  . LEU A 61  ? 0.2090 0.3597 0.2099 0.0407  -0.0693 -0.0089 61  LEU A CG  
491  C  CD1 . LEU A 61  ? 0.1830 0.3639 0.2539 0.0222  -0.0515 -0.0521 61  LEU A CD1 
492  C  CD2 . LEU A 61  ? 0.3310 0.3379 0.2245 0.1072  -0.0149 0.0139  61  LEU A CD2 
493  N  N   . THR A 62  ? 0.1895 0.4159 0.2110 0.1050  -0.0712 -0.0792 62  THR A N   
494  C  CA  . THR A 62  ? 0.2063 0.4700 0.2806 0.1456  -0.0609 -0.0991 62  THR A CA  
495  C  C   . THR A 62  ? 0.2056 0.5905 0.2906 0.1773  -0.0334 -0.0954 62  THR A C   
496  O  O   . THR A 62  ? 0.2682 0.6078 0.1941 0.1450  -0.0527 -0.0601 62  THR A O   
497  C  CB  . THR A 62  ? 0.3683 0.4575 0.3538 0.1329  -0.1201 -0.0094 62  THR A CB  
498  O  OG1 . THR A 62  ? 0.3699 0.5278 0.3894 0.0431  -0.0801 0.0118  62  THR A OG1 
499  C  CG2 . THR A 62  ? 0.3450 0.5898 0.2211 0.2188  -0.0653 0.0137  62  THR A CG2 
500  N  N   . ASN A 63  ? 0.2581 0.7158 0.2092 0.1831  -0.0527 -0.1229 63  ASN A N   
501  C  CA  . ASN A 63  ? 0.2782 0.7620 0.2096 0.2190  -0.0496 -0.0824 63  ASN A CA  
502  C  C   . ASN A 63  ? 0.2570 0.8192 0.2037 0.1764  0.0708  0.0372  63  ASN A C   
503  O  O   . ASN A 63  ? 0.3010 0.7668 0.3258 0.1790  0.0422  0.0995  63  ASN A O   
504  C  CB  . ASN A 63  ? 0.2380 0.5948 0.2663 0.1665  -0.0296 -0.0952 63  ASN A CB  
505  C  CG  . ASN A 63  ? 0.2365 0.6164 0.2830 0.1417  -0.0679 -0.0602 63  ASN A CG  
506  O  OD1 . ASN A 63  ? 0.2536 0.4832 0.2340 0.1274  -0.0715 -0.0979 63  ASN A OD1 
507  N  ND2 . ASN A 63  ? 0.2796 0.2613 0.3315 0.0803  -0.1128 -0.1650 63  ASN A ND2 
508  N  N   . ASN A 64  ? 0.4448 1.0197 0.1663 0.2103  0.0664  -0.0196 64  ASN A N   
509  C  CA  . ASN A 64  ? 0.2588 1.0721 0.4048 0.0906  0.1002  0.1833  64  ASN A CA  
510  C  C   . ASN A 64  ? 0.3209 0.9168 0.5728 0.1735  0.0693  0.1750  64  ASN A C   
511  O  O   . ASN A 64  ? 0.3106 1.0607 0.5382 0.1573  0.0311  0.3815  64  ASN A O   
512  C  CB  . ASN A 64  ? 0.3299 1.3178 0.4533 0.1966  0.0917  0.2438  64  ASN A CB  
513  C  CG  . ASN A 64  ? 0.5992 1.4152 0.6707 0.2612  -0.0420 0.0263  64  ASN A CG  
514  O  OD1 . ASN A 64  ? 0.7173 1.5129 0.2802 0.3917  -0.1018 0.1782  64  ASN A OD1 
515  N  ND2 . ASN A 64  ? 0.8187 1.0473 0.7839 0.4228  0.2673  0.0822  64  ASN A ND2 
516  N  N   . GLY A 65  ? 0.3415 0.9033 0.2416 0.0891  -0.0864 0.1280  65  GLY A N   
517  C  CA  . GLY A 65  ? 0.3814 0.8087 0.2551 0.1268  0.0575  0.0625  65  GLY A CA  
518  C  C   . GLY A 65  ? 0.2440 0.7681 0.4412 0.2546  -0.0171 -0.0062 65  GLY A C   
519  O  O   . GLY A 65  ? 0.2435 0.5801 0.1962 0.1150  -0.0081 -0.0004 65  GLY A O   
520  N  N   . HIS A 66  ? 0.3465 0.7975 0.3781 0.1724  0.0178  -0.0179 66  HIS A N   
521  C  CA  . HIS A 66  ? 0.4504 0.4507 0.3570 0.1728  -0.0597 0.1098  66  HIS A CA  
522  C  C   . HIS A 66  ? 0.2375 0.4529 0.2260 0.0004  -0.0545 -0.1390 66  HIS A C   
523  O  O   . HIS A 66  ? 0.3140 0.2653 0.3471 0.0603  -0.1238 -0.0040 66  HIS A O   
524  C  CB  . HIS A 66  ? 0.4975 0.1879 0.4767 0.1093  -0.0717 0.1579  66  HIS A CB  
525  C  CG  . HIS A 66  ? 0.6301 0.1807 0.3771 0.1020  0.0351  0.1985  66  HIS A CG  
526  N  ND1 . HIS A 66  ? 0.7627 0.4899 0.4483 0.3240  -0.0933 0.1553  66  HIS A ND1 
527  C  CD2 . HIS A 66  ? 0.3704 0.7228 0.2978 -0.0597 -0.1497 0.0237  66  HIS A CD2 
528  C  CE1 . HIS A 66  ? 0.2265 0.6176 0.1423 0.0578  -0.0734 -0.0109 66  HIS A CE1 
529  N  NE2 . HIS A 66  ? 0.2504 0.7835 0.2939 0.0087  -0.0132 0.0523  66  HIS A NE2 
530  N  N   . SER A 67  ? 0.3355 0.4153 0.2317 0.1035  -0.0760 -0.0257 67  SER A N   
531  C  CA  . SER A 67  ? 0.2083 0.4737 0.2109 0.0402  -0.0594 -0.0293 67  SER A CA  
532  C  C   . SER A 67  ? 0.3102 0.4413 0.1693 0.1128  -0.1037 -0.0702 67  SER A C   
533  O  O   . SER A 67  ? 0.3531 0.3366 0.3495 -0.0873 -0.1298 0.0160  67  SER A O   
534  C  CB  . SER A 67  ? 0.3474 0.1772 0.2259 -0.0132 -0.0476 -0.0178 67  SER A CB  
535  O  OG  . SER A 67  ? 0.3436 0.2188 0.3613 -0.0119 0.0403  -0.0673 67  SER A OG  
536  N  N   . VAL A 68  ? 0.1629 0.4808 0.3154 0.0469  -0.0561 0.0144  68  VAL A N   
537  C  CA  . VAL A 68  ? 0.1180 0.6827 0.2567 0.1323  -0.0339 -0.0541 68  VAL A CA  
538  C  C   . VAL A 68  ? 0.1934 0.5723 0.2297 0.1008  -0.0012 -0.0537 68  VAL A C   
539  O  O   . VAL A 68  ? 0.2013 0.5968 0.1625 0.0454  -0.0291 0.0178  68  VAL A O   
540  C  CB  . VAL A 68  ? 0.2982 0.7073 0.2149 -0.0181 -0.0480 -0.0625 68  VAL A CB  
541  C  CG1 . VAL A 68  ? 0.1905 0.7149 0.3030 -0.0346 -0.0494 0.0890  68  VAL A CG1 
542  C  CG2 . VAL A 68  ? 0.2577 0.5382 0.2628 -0.0106 -0.0356 -0.0394 68  VAL A CG2 
543  N  N   . LYS A 69  ? 0.1797 0.4827 0.1790 0.1070  -0.0499 -0.0336 69  LYS A N   
544  C  CA  . LYS A 69  ? 0.1469 0.3538 0.1743 0.0474  -0.0498 -0.0190 69  LYS A CA  
545  C  C   . LYS A 69  ? 0.1442 0.3449 0.1500 0.0595  -0.0423 -0.0592 69  LYS A C   
546  O  O   . LYS A 69  ? 0.2284 0.3949 0.1761 0.0552  -0.0776 -0.0751 69  LYS A O   
547  C  CB  . LYS A 69  ? 0.1772 0.5595 0.2137 0.0420  -0.0797 0.1461  69  LYS A CB  
548  C  CG  . LYS A 69  ? 0.2963 0.3046 0.5656 0.0219  0.0198  0.1656  69  LYS A CG  
549  C  CD  . LYS A 69  ? 0.3639 0.2949 0.5939 -0.1714 0.1044  -0.0122 69  LYS A CD  
550  C  CE  . LYS A 69  ? 0.3251 0.3876 0.5636 -0.0762 0.0227  0.0743  69  LYS A CE  
551  N  NZ  . LYS A 69  ? 0.3917 0.3625 0.3771 -0.1260 -0.1094 0.0506  69  LYS A NZ  
552  N  N   . LEU A 70  ? 0.1132 0.2085 0.1779 0.0041  -0.0351 -0.0036 70  LEU A N   
553  C  CA  . LEU A 70  ? 0.1269 0.2387 0.1463 0.0273  -0.0428 0.0130  70  LEU A CA  
554  C  C   . LEU A 70  ? 0.1255 0.2281 0.1610 0.0314  -0.0497 0.0105  70  LEU A C   
555  O  O   . LEU A 70  ? 0.1388 0.2477 0.1527 0.0012  -0.0479 0.0033  70  LEU A O   
556  C  CB  . LEU A 70  ? 0.1721 0.2531 0.2354 0.0782  -0.0662 0.0388  70  LEU A CB  
557  C  CG  . LEU A 70  ? 0.1546 0.2647 0.2002 0.0522  -0.0568 0.0579  70  LEU A CG  
558  C  CD1 . LEU A 70  ? 0.1491 0.3336 0.2472 0.0632  -0.0942 0.0126  70  LEU A CD1 
559  C  CD2 . LEU A 70  ? 0.1866 0.2661 0.2443 0.0943  -0.0484 0.0413  70  LEU A CD2 
560  N  N   . ASN A 71  ? 0.1406 0.2506 0.1866 0.0145  -0.0523 -0.0168 71  ASN A N   
561  C  CA  . ASN A 71  ? 0.1316 0.2460 0.2310 -0.0212 -0.0625 -0.0047 71  ASN A CA  
562  C  C   . ASN A 71  ? 0.1794 0.2421 0.2182 -0.0060 -0.0094 0.0542  71  ASN A C   
563  O  O   . ASN A 71  ? 0.1985 0.3040 0.1909 0.0297  -0.0497 0.0192  71  ASN A O   
564  C  CB  . ASN A 71  ? 0.2157 0.2148 0.2321 -0.0352 -0.0374 -0.0126 71  ASN A CB  
565  C  CG  . ASN A 71  ? 0.3409 0.2633 0.3340 -0.0051 -0.0167 -0.0746 71  ASN A CG  
566  O  OD1 . ASN A 71  ? 0.3606 0.2199 0.3624 -0.0157 -0.0469 -0.0496 71  ASN A OD1 
567  N  ND2 . ASN A 71  ? 0.3561 0.2785 0.3929 -0.1075 -0.0561 -0.0050 71  ASN A ND2 
568  N  N   . LEU A 72  ? 0.1283 0.3019 0.1869 0.0095  -0.0433 -0.0122 72  LEU A N   
569  C  CA  . LEU A 72  ? 0.1014 0.2275 0.1775 -0.0148 -0.0485 0.0438  72  LEU A CA  
570  C  C   . LEU A 72  ? 0.1056 0.2221 0.2119 -0.0439 -0.0749 0.0510  72  LEU A C   
571  O  O   . LEU A 72  ? 0.1991 0.2069 0.2750 0.0018  0.0011  0.0502  72  LEU A O   
572  C  CB  . LEU A 72  ? 0.1082 0.2353 0.1848 0.0118  -0.0577 0.0124  72  LEU A CB  
573  C  CG  . LEU A 72  ? 0.1481 0.1834 0.1546 0.0321  -0.0390 0.0210  72  LEU A CG  
574  C  CD1 . LEU A 72  ? 0.1342 0.1324 0.1826 0.0032  -0.0526 0.0558  72  LEU A CD1 
575  C  CD2 . LEU A 72  ? 0.1438 0.2295 0.2149 0.0198  -0.0551 0.0703  72  LEU A CD2 
576  N  N   . PRO A 73  ? 0.1397 0.2375 0.2649 -0.0023 -0.0359 0.0648  73  PRO A N   
577  C  CA  . PRO A 73  ? 0.1401 0.2056 0.2565 0.0019  -0.0098 0.0011  73  PRO A CA  
578  C  C   . PRO A 73  ? 0.1531 0.1298 0.2502 -0.0373 -0.0223 0.0344  73  PRO A C   
579  O  O   . PRO A 73  ? 0.1412 0.1496 0.2575 -0.0268 -0.0193 0.0306  73  PRO A O   
580  C  CB  . PRO A 73  ? 0.1668 0.2060 0.2636 0.0147  -0.0145 0.0319  73  PRO A CB  
581  C  CG  . PRO A 73  ? 0.1597 0.2292 0.2887 0.0107  -0.0416 0.0702  73  PRO A CG  
582  C  CD  . PRO A 73  ? 0.1654 0.2263 0.2710 0.0501  -0.0226 0.0444  73  PRO A CD  
583  N  N   . SER A 74  ? 0.2252 0.1956 0.2763 -0.0408 -0.0165 0.0908  74  SER A N   
584  C  CA  . SER A 74  ? 0.2173 0.1362 0.2735 -0.0406 -0.0250 0.0728  74  SER A CA  
585  C  C   . SER A 74  ? 0.1707 0.1117 0.2885 -0.0388 -0.0282 0.0903  74  SER A C   
586  O  O   . SER A 74  ? 0.2044 0.2559 0.2894 0.0271  -0.0257 0.0840  74  SER A O   
587  C  CB  . SER A 74  ? 0.2644 0.1721 0.3719 -0.0683 -0.0265 0.1353  74  SER A CB  
588  O  OG  . SER A 74  ? 0.3016 0.2448 0.3527 -0.1128 -0.0234 0.0463  74  SER A OG  
589  N  N   . ASP A 75  ? 0.1469 0.2830 0.2347 0.0179  -0.0447 0.0355  75  ASP A N   
590  C  CA  . ASP A 75  ? 0.1250 0.2447 0.2449 0.0114  -0.0177 0.0707  75  ASP A CA  
591  C  C   . ASP A 75  ? 0.0834 0.2015 0.2027 0.0480  -0.0153 0.0070  75  ASP A C   
592  O  O   . ASP A 75  ? 0.1225 0.2170 0.2628 0.0444  0.0165  -0.0108 75  ASP A O   
593  C  CB  . ASP A 75  ? 0.1561 0.3708 0.2803 0.0952  -0.0336 0.0450  75  ASP A CB  
594  C  CG  . ASP A 75  ? 0.1541 0.3894 0.2529 0.0927  -0.0445 0.0210  75  ASP A CG  
595  O  OD1 . ASP A 75  ? 0.2428 0.4070 0.2870 0.1037  -0.0003 0.0557  75  ASP A OD1 
596  O  OD2 . ASP A 75  ? 0.2491 0.3638 0.2626 0.0092  0.0071  0.0089  75  ASP A OD2 
597  N  N   . MET A 76  ? 0.1090 0.1713 0.1717 -0.0003 -0.0201 0.0452  76  MET A N   
598  C  CA  . MET A 76  ? 0.0999 0.1997 0.1798 -0.0021 -0.0104 0.0603  76  MET A CA  
599  C  C   . MET A 76  ? 0.0916 0.1600 0.2085 0.0116  -0.0475 0.0190  76  MET A C   
600  O  O   . MET A 76  ? 0.1252 0.1444 0.1739 0.0113  -0.0070 0.0469  76  MET A O   
601  C  CB  . MET A 76  ? 0.1214 0.1895 0.1851 0.0066  0.0035  0.0578  76  MET A CB  
602  C  CG  . MET A 76  ? 0.1100 0.2268 0.2049 -0.0049 -0.0212 0.0402  76  MET A CG  
603  S  SD  . MET A 76  ? 0.1632 0.1742 0.2120 0.0089  0.0145  0.0524  76  MET A SD  
604  C  CE  . MET A 76  ? 0.1561 0.2089 0.2211 0.0054  0.0242  0.0521  76  MET A CE  
605  N  N   . HIS A 77  ? 0.1268 0.1275 0.1546 -0.0178 -0.0203 0.0578  77  HIS A N   
606  C  CA  . HIS A 77  ? 0.1115 0.1707 0.1164 -0.0040 0.0055  0.0247  77  HIS A CA  
607  C  C   . HIS A 77  ? 0.1222 0.1494 0.1442 0.0104  -0.0226 0.0396  77  HIS A C   
608  O  O   . HIS A 77  ? 0.1132 0.1433 0.1902 0.0004  -0.0290 0.0476  77  HIS A O   
609  C  CB  . HIS A 77  ? 0.1097 0.1458 0.1750 -0.0160 0.0084  0.0419  77  HIS A CB  
610  C  CG  . HIS A 77  ? 0.1191 0.2056 0.1593 0.0058  0.0133  0.0290  77  HIS A CG  
611  N  ND1 . HIS A 77  ? 0.1388 0.2984 0.1991 0.0148  -0.0003 0.0315  77  HIS A ND1 
612  C  CD2 . HIS A 77  ? 0.1301 0.2418 0.1832 -0.0038 0.0111  0.0052  77  HIS A CD2 
613  C  CE1 . HIS A 77  ? 0.1834 0.2670 0.1922 0.0255  0.0097  0.0509  77  HIS A CE1 
614  N  NE2 . HIS A 77  ? 0.1532 0.1810 0.2426 0.0064  0.0181  0.0630  77  HIS A NE2 
615  N  N   . ILE A 78  ? 0.1133 0.1997 0.1478 -0.0044 -0.0348 0.0110  78  ILE A N   
616  C  CA  . ILE A 78  ? 0.1027 0.1941 0.1503 0.0006  -0.0141 -0.0060 78  ILE A CA  
617  C  C   . ILE A 78  ? 0.0848 0.1875 0.1959 0.0040  0.0168  0.0074  78  ILE A C   
618  O  O   . ILE A 78  ? 0.1523 0.2134 0.1905 -0.0447 0.0159  0.0211  78  ILE A O   
619  C  CB  . ILE A 78  ? 0.0735 0.2130 0.2177 -0.0342 0.0113  -0.0072 78  ILE A CB  
620  C  CG1 . ILE A 78  ? 0.1298 0.2063 0.2495 -0.0172 0.0341  0.0445  78  ILE A CG1 
621  C  CG2 . ILE A 78  ? 0.1539 0.2092 0.2476 -0.0284 -0.0488 -0.0029 78  ILE A CG2 
622  C  CD1 . ILE A 78  ? 0.1047 0.3209 0.3267 0.0233  0.0372  -0.0097 78  ILE A CD1 
623  N  N   . GLN A 79  ? 0.1236 0.2031 0.2142 0.0273  -0.0061 -0.0111 79  GLN A N   
624  C  CA  . GLN A 79  ? 0.1523 0.2414 0.2246 0.0085  0.0115  -0.0260 79  GLN A CA  
625  C  C   . GLN A 79  ? 0.1621 0.2162 0.1992 0.0108  -0.0074 0.0162  79  GLN A C   
626  O  O   . GLN A 79  ? 0.2189 0.2274 0.2249 -0.0127 0.0044  0.0171  79  GLN A O   
627  C  CB  . GLN A 79  ? 0.1930 0.1758 0.2997 0.0070  -0.0157 -0.0194 79  GLN A CB  
628  C  CG  . GLN A 79  ? 0.2406 0.3082 0.4025 0.0619  0.1074  -0.0194 79  GLN A CG  
629  C  CD  . GLN A 79  ? 0.3215 0.3257 0.6130 -0.0175 0.0233  -0.0523 79  GLN A CD  
630  O  OE1 . GLN A 79  ? 0.4573 0.1470 0.8910 0.0677  -0.2295 -0.1351 79  GLN A OE1 
631  N  NE2 . GLN A 79  ? 0.4947 0.5906 0.7291 0.2863  0.0126  -0.0648 79  GLN A NE2 
632  N  N   . GLY A 80  ? 0.2017 0.2978 0.1744 -0.0272 -0.0010 -0.0050 80  GLY A N   
633  C  CA  . GLY A 80  ? 0.2536 0.3565 0.1611 -0.0222 -0.0420 -0.0023 80  GLY A CA  
634  C  C   . GLY A 80  ? 0.2254 0.3070 0.1679 -0.0003 0.0096  -0.0319 80  GLY A C   
635  O  O   . GLY A 80  ? 0.2387 0.3412 0.2285 -0.0241 -0.0109 -0.0732 80  GLY A O   
636  N  N   . LEU A 81  ? 0.2157 0.2354 0.1816 -0.0273 0.0008  0.0171  81  LEU A N   
637  C  CA  . LEU A 81  ? 0.2286 0.2711 0.1751 -0.0193 -0.0010 0.0281  81  LEU A CA  
638  C  C   . LEU A 81  ? 0.2706 0.2349 0.1963 -0.0233 0.0061  0.0309  81  LEU A C   
639  O  O   . LEU A 81  ? 0.2661 0.4591 0.2094 -0.0579 0.0344  0.0397  81  LEU A O   
640  C  CB  . LEU A 81  ? 0.2297 0.2290 0.1772 -0.0446 0.0030  0.0469  81  LEU A CB  
641  C  CG  . LEU A 81  ? 0.1902 0.2026 0.2146 -0.0488 0.0145  0.0310  81  LEU A CG  
642  C  CD1 . LEU A 81  ? 0.2073 0.2266 0.2315 -0.0205 0.0275  0.0204  81  LEU A CD1 
643  C  CD2 . LEU A 81  ? 0.2094 0.2614 0.2503 -0.0690 -0.0113 0.0272  81  LEU A CD2 
644  N  N   . GLN A 82  ? 0.3089 0.2528 0.2030 -0.0653 -0.0138 0.0917  82  GLN A N   
645  C  CA  . GLN A 82  ? 0.3147 0.3049 0.2046 -0.1152 -0.0077 0.0793  82  GLN A CA  
646  C  C   . GLN A 82  ? 0.2985 0.3872 0.2371 -0.1198 0.0392  -0.0147 82  GLN A C   
647  O  O   . GLN A 82  ? 0.2926 0.5070 0.2700 -0.0735 0.0407  0.0719  82  GLN A O   
648  C  CB  . GLN A 82  ? 0.4496 0.3380 0.1692 -0.1354 -0.0996 0.0935  82  GLN A CB  
649  C  CG  . GLN A 82  ? 0.4099 0.4321 0.2015 -0.0967 -0.0800 -0.0117 82  GLN A CG  
650  C  CD  . GLN A 82  ? 0.4509 0.6540 0.2153 -0.1631 0.0116  0.0029  82  GLN A CD  
651  O  OE1 . GLN A 82  ? 0.4142 0.5580 0.3707 -0.1495 -0.0076 0.0804  82  GLN A OE1 
652  N  NE2 . GLN A 82  ? 0.5552 0.3148 0.3651 0.0773  -0.0960 0.0971  82  GLN A NE2 
653  N  N   . SER A 83  ? 0.2340 0.3016 0.1969 -0.0770 -0.0138 0.0643  83  SER A N   
654  C  CA  . SER A 83  ? 0.1944 0.2995 0.1699 -0.0521 -0.0580 0.0968  83  SER A CA  
655  C  C   . SER A 83  ? 0.1347 0.2549 0.1647 -0.0351 -0.0482 0.0787  83  SER A C   
656  O  O   . SER A 83  ? 0.1166 0.2936 0.2152 -0.0288 -0.0228 0.0932  83  SER A O   
657  C  CB  . SER A 83  ? 0.1694 0.3286 0.2196 -0.0168 -0.0406 0.1236  83  SER A CB  
658  O  OG  . SER A 83  ? 0.2815 0.2775 0.2297 -0.0756 -0.0293 0.1344  83  SER A OG  
659  N  N   . ARG A 84  ? 0.1333 0.2833 0.1597 -0.0220 -0.0559 0.0798  84  ARG A N   
660  C  CA  . ARG A 84  ? 0.1126 0.2166 0.1556 -0.0212 -0.0614 0.0687  84  ARG A CA  
661  C  C   . ARG A 84  ? 0.1647 0.2386 0.1711 -0.0390 -0.0177 0.0768  84  ARG A C   
662  O  O   . ARG A 84  ? 0.1445 0.2207 0.1768 -0.0288 -0.0196 0.0815  84  ARG A O   
663  C  CB  . ARG A 84  ? 0.1191 0.3200 0.1568 -0.0321 -0.0722 0.0867  84  ARG A CB  
664  C  CG  . ARG A 84  ? 0.1114 0.2868 0.1532 0.0410  -0.0480 0.0754  84  ARG A CG  
665  C  CD  . ARG A 84  ? 0.0967 0.3046 0.1992 0.0740  -0.0353 0.0749  84  ARG A CD  
666  N  NE  . ARG A 84  ? 0.1132 0.2328 0.2412 0.0391  -0.0077 0.0479  84  ARG A NE  
667  C  CZ  . ARG A 84  ? 0.1230 0.2491 0.2028 0.0247  -0.0193 0.0640  84  ARG A CZ  
668  N  NH1 . ARG A 84  ? 0.1306 0.2825 0.2551 -0.0163 -0.0666 0.0340  84  ARG A NH1 
669  N  NH2 . ARG A 84  ? 0.1191 0.1737 0.3330 0.0138  0.0097  0.0644  84  ARG A NH2 
670  N  N   . TYR A 85  ? 0.1243 0.1965 0.1674 -0.0038 0.0012  0.0592  85  TYR A N   
671  C  CA  . TYR A 85  ? 0.1022 0.2112 0.1439 -0.0182 -0.0071 0.0402  85  TYR A CA  
672  C  C   . TYR A 85  ? 0.0972 0.1596 0.1664 -0.0207 -0.0368 0.0519  85  TYR A C   
673  O  O   . TYR A 85  ? 0.1636 0.1663 0.2031 -0.0207 -0.0229 0.0629  85  TYR A O   
674  C  CB  . TYR A 85  ? 0.0671 0.2225 0.1999 0.0200  -0.0187 0.0505  85  TYR A CB  
675  C  CG  . TYR A 85  ? 0.0866 0.1945 0.1690 -0.0392 -0.0074 0.0791  85  TYR A CG  
676  C  CD1 . TYR A 85  ? 0.1629 0.2407 0.1625 -0.0124 -0.0190 0.0817  85  TYR A CD1 
677  C  CD2 . TYR A 85  ? 0.1182 0.2654 0.1556 -0.0038 -0.0058 0.0725  85  TYR A CD2 
678  C  CE1 . TYR A 85  ? 0.1625 0.2035 0.1474 -0.0027 -0.0084 0.0597  85  TYR A CE1 
679  C  CE2 . TYR A 85  ? 0.1115 0.2533 0.1613 -0.0502 -0.0277 0.0719  85  TYR A CE2 
680  C  CZ  . TYR A 85  ? 0.1323 0.2376 0.1798 -0.0013 -0.0456 0.0523  85  TYR A CZ  
681  O  OH  . TYR A 85  ? 0.1995 0.3488 0.1886 0.0097  -0.0688 0.0859  85  TYR A OH  
682  N  N   . SER A 86  ? 0.0956 0.1909 0.1615 -0.0077 -0.0258 0.0105  86  SER A N   
683  C  CA  . SER A 86  ? 0.1295 0.1320 0.1469 -0.0370 -0.0212 0.0381  86  SER A CA  
684  C  C   . SER A 86  ? 0.0880 0.1351 0.1733 -0.0131 -0.0383 0.0719  86  SER A C   
685  O  O   . SER A 86  ? 0.1221 0.1794 0.1970 0.0263  -0.0320 0.0946  86  SER A O   
686  C  CB  . SER A 86  ? 0.1318 0.1503 0.1557 -0.0423 -0.0088 0.0194  86  SER A CB  
687  O  OG  . SER A 86  ? 0.1410 0.1999 0.1728 -0.0147 0.0104  0.0487  86  SER A OG  
688  N  N   . ALA A 87  ? 0.1395 0.1787 0.1402 -0.0104 -0.0212 0.0717  87  ALA A N   
689  C  CA  . ALA A 87  ? 0.1769 0.1604 0.1793 0.0140  0.0024  0.0634  87  ALA A CA  
690  C  C   . ALA A 87  ? 0.1169 0.1514 0.2078 0.0054  -0.0089 0.0364  87  ALA A C   
691  O  O   . ALA A 87  ? 0.1352 0.2109 0.2124 -0.0128 -0.0240 0.0359  87  ALA A O   
692  C  CB  . ALA A 87  ? 0.1909 0.1610 0.1643 0.0388  0.0172  0.0612  87  ALA A CB  
693  N  N   . THR A 88  ? 0.1406 0.1284 0.1893 -0.0052 0.0038  0.0385  88  THR A N   
694  C  CA  . THR A 88  ? 0.1356 0.0850 0.2242 0.0176  -0.0510 0.0330  88  THR A CA  
695  C  C   . THR A 88  ? 0.1582 0.0583 0.1767 -0.0135 -0.0659 0.0249  88  THR A C   
696  O  O   . THR A 88  ? 0.1380 0.1509 0.1933 0.0044  -0.0589 -0.0106 88  THR A O   
697  C  CB  . THR A 88  ? 0.1843 0.0674 0.2558 0.0369  0.0005  0.0509  88  THR A CB  
698  O  OG1 . THR A 88  ? 0.3689 0.1744 0.2617 0.0446  -0.0295 0.0153  88  THR A OG1 
699  C  CG2 . THR A 88  ? 0.1713 0.2328 0.2558 0.0750  -0.0386 0.0494  88  THR A CG2 
700  N  N   . GLN A 89  ? 0.1399 0.0970 0.1764 -0.0106 -0.0334 0.0121  89  GLN A N   
701  C  CA  . GLN A 89  ? 0.1287 0.1367 0.1668 0.0127  -0.0414 0.0062  89  GLN A CA  
702  C  C   . GLN A 89  ? 0.1087 0.1467 0.1674 0.0256  -0.0540 0.0587  89  GLN A C   
703  O  O   . GLN A 89  ? 0.1295 0.1646 0.1470 0.0436  -0.0400 0.0276  89  GLN A O   
704  C  CB  . GLN A 89  ? 0.1394 0.1198 0.2097 0.0215  -0.0491 0.0130  89  GLN A CB  
705  C  CG  . GLN A 89  ? 0.1582 0.1329 0.2394 0.0548  -0.0526 0.0048  89  GLN A CG  
706  C  CD  . GLN A 89  ? 0.1694 0.0837 0.1870 -0.0173 -0.0895 0.0148  89  GLN A CD  
707  O  OE1 . GLN A 89  ? 0.1744 0.1257 0.2085 -0.0117 -0.0223 0.0598  89  GLN A OE1 
708  N  NE2 . GLN A 89  ? 0.2254 0.2253 0.3078 0.0804  -0.0081 -0.0731 89  GLN A NE2 
709  N  N   . LEU A 90  ? 0.1166 0.1326 0.1408 -0.0006 -0.0155 0.0143  90  LEU A N   
710  C  CA  . LEU A 90  ? 0.1115 0.1136 0.1671 0.0076  0.0048  0.0399  90  LEU A CA  
711  C  C   . LEU A 90  ? 0.1306 0.0972 0.1403 0.0000  -0.0062 0.0438  90  LEU A C   
712  O  O   . LEU A 90  ? 0.1345 0.1772 0.1625 0.0185  -0.0500 0.0027  90  LEU A O   
713  C  CB  . LEU A 90  ? 0.1394 0.1241 0.1634 0.0207  -0.0292 0.0640  90  LEU A CB  
714  C  CG  . LEU A 90  ? 0.1846 0.1498 0.1399 0.0776  -0.0259 0.0346  90  LEU A CG  
715  C  CD1 . LEU A 90  ? 0.1848 0.1761 0.1575 0.0388  -0.0250 0.0557  90  LEU A CD1 
716  C  CD2 . LEU A 90  ? 0.1758 0.1395 0.2211 0.0792  -0.0106 0.0591  90  LEU A CD2 
717  N  N   . HIS A 91  ? 0.1151 0.1185 0.1706 0.0032  0.0153  0.0347  91  HIS A N   
718  C  CA  . HIS A 91  ? 0.1164 0.0347 0.1852 0.0106  0.0155  0.0337  91  HIS A CA  
719  C  C   . HIS A 91  ? 0.0746 0.1266 0.1834 0.0139  -0.0240 -0.0154 91  HIS A C   
720  O  O   . HIS A 91  ? 0.1385 0.0965 0.1534 0.0098  -0.0160 0.0148  91  HIS A O   
721  C  CB  . HIS A 91  ? 0.1963 0.0277 0.1191 0.0120  -0.0267 0.0128  91  HIS A CB  
722  C  CG  . HIS A 91  ? 0.1692 0.0591 0.1141 -0.0131 -0.0313 -0.0168 91  HIS A CG  
723  N  ND1 . HIS A 91  ? 0.1542 0.1194 0.1319 -0.0171 -0.0285 0.0241  91  HIS A ND1 
724  C  CD2 . HIS A 91  ? 0.1693 0.0311 0.1349 -0.0083 -0.0549 0.0482  91  HIS A CD2 
725  C  CE1 . HIS A 91  ? 0.1428 0.0952 0.1293 -0.0033 -0.0234 0.0147  91  HIS A CE1 
726  N  NE2 . HIS A 91  ? 0.1374 0.0531 0.1327 0.0296  -0.0488 0.0432  91  HIS A NE2 
727  N  N   . LEU A 92  ? 0.0963 0.1148 0.1509 0.0036  -0.0266 0.0232  92  LEU A N   
728  C  CA  . LEU A 92  ? 0.0985 0.1133 0.1409 -0.0052 -0.0262 0.0367  92  LEU A CA  
729  C  C   . LEU A 92  ? 0.1258 0.1369 0.1033 0.0116  -0.0033 0.0051  92  LEU A C   
730  O  O   . LEU A 92  ? 0.1376 0.1280 0.1323 0.0170  -0.0198 -0.0062 92  LEU A O   
731  C  CB  . LEU A 92  ? 0.1678 0.0974 0.1958 0.0222  -0.0231 0.0577  92  LEU A CB  
732  C  CG  . LEU A 92  ? 0.1435 0.0970 0.1372 0.0131  -0.0392 0.0600  92  LEU A CG  
733  C  CD1 . LEU A 92  ? 0.1988 0.1463 0.2177 0.0416  -0.0990 0.0173  92  LEU A CD1 
734  C  CD2 . LEU A 92  ? 0.2198 0.1053 0.2418 -0.0336 0.0006  0.0418  92  LEU A CD2 
735  N  N   . HIS A 93  ? 0.1130 0.0873 0.1434 0.0295  -0.0099 0.0212  93  HIS A N   
736  C  CA  . HIS A 93  ? 0.0970 0.1326 0.1179 0.0015  -0.0265 0.0345  93  HIS A CA  
737  C  C   . HIS A 93  ? 0.0961 0.0586 0.1172 0.0423  -0.0118 0.0265  93  HIS A C   
738  O  O   . HIS A 93  ? 0.1597 0.0541 0.1408 0.0249  0.0089  0.0141  93  HIS A O   
739  C  CB  . HIS A 93  ? 0.1245 0.0986 0.0936 -0.0006 -0.0033 0.0301  93  HIS A CB  
740  C  CG  . HIS A 93  ? 0.1128 0.0624 0.1391 0.0004  -0.0269 0.0469  93  HIS A CG  
741  N  ND1 . HIS A 93  ? 0.1388 0.0674 0.1358 0.0183  -0.0218 -0.0084 93  HIS A ND1 
742  C  CD2 . HIS A 93  ? 0.1374 0.0663 0.1567 0.0194  -0.0140 0.0198  93  HIS A CD2 
743  C  CE1 . HIS A 93  ? 0.1384 0.1586 0.1749 -0.0058 -0.0310 0.0152  93  HIS A CE1 
744  N  NE2 . HIS A 93  ? 0.1349 0.0748 0.1597 -0.0100 -0.0673 0.0275  93  HIS A NE2 
745  N  N   . TRP A 94  ? 0.1154 0.0670 0.1327 0.0221  0.0034  0.0253  94  TRP A N   
746  C  CA  . TRP A 94  ? 0.1101 0.1137 0.1118 0.0121  0.0013  0.0365  94  TRP A CA  
747  C  C   . TRP A 94  ? 0.1108 0.1130 0.1733 0.0229  -0.0157 0.0354  94  TRP A C   
748  O  O   . TRP A 94  ? 0.1615 0.1065 0.1428 0.0498  0.0033  0.0077  94  TRP A O   
749  C  CB  . TRP A 94  ? 0.1934 0.0706 0.1198 0.0153  -0.0333 0.0272  94  TRP A CB  
750  C  CG  . TRP A 94  ? 0.1471 0.0651 0.1545 0.0194  -0.0144 0.0059  94  TRP A CG  
751  C  CD1 . TRP A 94  ? 0.1510 0.0952 0.1367 0.0064  -0.0387 0.0118  94  TRP A CD1 
752  C  CD2 . TRP A 94  ? 0.1779 0.1099 0.1119 -0.0111 -0.0309 0.0140  94  TRP A CD2 
753  N  NE1 . TRP A 94  ? 0.1568 0.0884 0.1733 -0.0208 0.0087  0.0120  94  TRP A NE1 
754  C  CE2 . TRP A 94  ? 0.1473 0.0798 0.1563 0.0211  0.0142  0.0109  94  TRP A CE2 
755  C  CE3 . TRP A 94  ? 0.1534 0.1029 0.1416 -0.0201 -0.0367 0.0247  94  TRP A CE3 
756  C  CZ2 . TRP A 94  ? 0.1688 0.1313 0.1568 -0.0201 0.0033  0.0241  94  TRP A CZ2 
757  C  CZ3 . TRP A 94  ? 0.1523 0.1212 0.1534 -0.0262 -0.0247 0.0087  94  TRP A CZ3 
758  C  CH2 . TRP A 94  ? 0.1306 0.1027 0.1954 0.0222  -0.0233 -0.0046 94  TRP A CH2 
759  N  N   . GLY A 95  ? 0.1326 0.1028 0.1652 -0.0104 -0.0015 -0.0095 95  GLY A N   
760  C  CA  . GLY A 95  ? 0.1331 0.1534 0.1480 -0.0239 0.0168  0.0153  95  GLY A CA  
761  C  C   . GLY A 95  ? 0.1243 0.1506 0.1207 -0.0161 -0.0329 0.0648  95  GLY A C   
762  O  O   . GLY A 95  ? 0.1645 0.1316 0.1521 0.0036  -0.0027 -0.0098 95  GLY A O   
763  N  N   . ASN A 96  ? 0.1453 0.1747 0.1355 0.0133  0.0529  0.0462  96  ASN A N   
764  C  CA  . ASN A 96  ? 0.1837 0.1485 0.1254 0.0283  0.0468  0.0618  96  ASN A CA  
765  C  C   . ASN A 96  ? 0.1861 0.1498 0.1344 -0.0029 0.0375  0.0178  96  ASN A C   
766  O  O   . ASN A 96  ? 0.1895 0.1263 0.1614 0.0265  0.0043  -0.0037 96  ASN A O   
767  C  CB  . ASN A 96  ? 0.1507 0.1952 0.1685 0.0245  0.0513  0.0078  96  ASN A CB  
768  C  CG  . ASN A 96  ? 0.1424 0.1161 0.2512 0.0149  0.0619  0.0412  96  ASN A CG  
769  O  OD1 . ASN A 96  ? 0.2124 0.1313 0.2902 0.0031  0.0677  0.0873  96  ASN A OD1 
770  N  ND2 . ASN A 96  ? 0.2500 0.0995 0.2615 -0.0379 0.0234  0.0037  96  ASN A ND2 
771  N  N   . PRO A 97  ? 0.2055 0.1657 0.1327 -0.0126 0.0121  0.0340  97  PRO A N   
772  C  CA  . PRO A 97  ? 0.1967 0.2049 0.1582 -0.0282 0.0208  0.0693  97  PRO A CA  
773  C  C   . PRO A 97  ? 0.1765 0.1509 0.1453 -0.0207 0.0058  0.0763  97  PRO A C   
774  O  O   . PRO A 97  ? 0.2196 0.1671 0.2634 -0.0407 0.0128  0.0833  97  PRO A O   
775  C  CB  . PRO A 97  ? 0.2240 0.2013 0.1790 -0.0168 -0.0075 0.0488  97  PRO A CB  
776  C  CG  . PRO A 97  ? 0.3010 0.1470 0.1751 -0.0328 0.0245  0.0194  97  PRO A CG  
777  C  CD  . PRO A 97  ? 0.2225 0.1985 0.1610 0.0015  0.0348  -0.0013 97  PRO A CD  
778  N  N   . ASN A 98  ? 0.1658 0.1746 0.1602 -0.0087 0.0160  0.0520  98  ASN A N   
779  C  CA  . ASN A 98  ? 0.1801 0.1372 0.1976 0.0092  0.0084  0.0182  98  ASN A CA  
780  C  C   . ASN A 98  ? 0.1737 0.2260 0.1958 -0.0156 0.0072  0.0242  98  ASN A C   
781  O  O   . ASN A 98  ? 0.1620 0.3216 0.2473 -0.0243 -0.0033 0.0125  98  ASN A O   
782  C  CB  . ASN A 98  ? 0.2328 0.1689 0.2397 0.0355  0.0043  -0.0227 98  ASN A CB  
783  C  CG  . ASN A 98  ? 0.3879 0.2128 0.2813 0.0194  0.0595  -0.0828 98  ASN A CG  
784  O  OD1 . ASN A 98  ? 0.4731 0.4214 0.3637 0.0042  0.0452  0.0803  98  ASN A OD1 
785  N  ND2 . ASN A 98  ? 0.5546 0.2838 0.4125 0.1045  0.0788  -0.1485 98  ASN A ND2 
786  N  N   . ASP A 99  ? 0.1671 0.1622 0.1570 0.0321  0.0032  0.0204  99  ASP A N   
787  C  CA  . ASP A 99  ? 0.1579 0.1178 0.1671 0.0039  -0.0149 0.0062  99  ASP A CA  
788  C  C   . ASP A 99  ? 0.1798 0.1456 0.1956 0.0039  0.0166  0.0226  99  ASP A C   
789  O  O   . ASP A 99  ? 0.1787 0.1243 0.2095 -0.0149 0.0119  -0.0055 99  ASP A O   
790  C  CB  . ASP A 99  ? 0.2092 0.1550 0.1665 0.0406  -0.0219 0.0092  99  ASP A CB  
791  C  CG  . ASP A 99  ? 0.2092 0.0917 0.1647 0.0263  -0.0127 0.0223  99  ASP A CG  
792  O  OD1 . ASP A 99  ? 0.3098 0.0977 0.2477 0.0441  -0.0336 -0.0172 99  ASP A OD1 
793  O  OD2 . ASP A 99  ? 0.2660 0.2520 0.2805 0.0820  -0.1094 0.0093  99  ASP A OD2 
794  N  N   . PRO A 100 ? 0.1622 0.1130 0.1859 -0.0159 0.0269  0.0348  100 PRO A N   
795  C  CA  . PRO A 100 ? 0.1660 0.1225 0.1735 0.0271  0.0217  0.0479  100 PRO A CA  
796  C  C   . PRO A 100 ? 0.1320 0.1584 0.1754 0.0573  0.0141  0.0094  100 PRO A C   
797  O  O   . PRO A 100 ? 0.1897 0.0968 0.2543 0.0287  0.0702  0.0562  100 PRO A O   
798  C  CB  . PRO A 100 ? 0.2022 0.1155 0.2049 0.0042  -0.0031 0.0635  100 PRO A CB  
799  C  CG  . PRO A 100 ? 0.1701 0.1262 0.2105 0.0212  0.0179  0.0741  100 PRO A CG  
800  C  CD  . PRO A 100 ? 0.1857 0.1083 0.1900 0.0205  0.0284  0.0618  100 PRO A CD  
801  N  N   . HIS A 101 ? 0.2130 0.1243 0.1895 -0.0124 0.0289  0.0536  101 HIS A N   
802  C  CA  . HIS A 101 ? 0.1678 0.1178 0.2108 -0.0625 0.0127  0.0416  101 HIS A CA  
803  C  C   . HIS A 101 ? 0.1492 0.0744 0.2540 -0.0008 -0.0247 0.0565  101 HIS A C   
804  O  O   . HIS A 101 ? 0.1998 0.1729 0.3726 0.0035  -0.0971 0.1012  101 HIS A O   
805  C  CB  . HIS A 101 ? 0.1981 0.1333 0.2608 -0.0690 -0.0296 0.0306  101 HIS A CB  
806  C  CG  . HIS A 101 ? 0.1826 0.0529 0.2419 -0.0271 0.0135  -0.0261 101 HIS A CG  
807  N  ND1 . HIS A 101 ? 0.2259 0.0744 0.3811 -0.0208 0.0335  -0.0692 101 HIS A ND1 
808  C  CD2 . HIS A 101 ? 0.1812 0.0829 0.2374 -0.0554 0.0220  0.0009  101 HIS A CD2 
809  C  CE1 . HIS A 101 ? 0.2200 0.0467 0.4480 0.0024  0.0411  -0.0279 101 HIS A CE1 
810  N  NE2 . HIS A 101 ? 0.2646 0.0771 0.2864 -0.0154 0.0339  -0.0030 101 HIS A NE2 
811  N  N   . GLY A 102 ? 0.1509 0.0595 0.1703 -0.0127 0.0271  -0.0064 102 GLY A N   
812  C  CA  . GLY A 102 ? 0.1067 0.0670 0.1821 -0.0012 0.0030  0.0378  102 GLY A CA  
813  C  C   . GLY A 102 ? 0.1089 0.0523 0.1692 0.0343  0.0006  0.0044  102 GLY A C   
814  O  O   . GLY A 102 ? 0.1527 0.0631 0.1703 0.0057  0.0104  0.0340  102 GLY A O   
815  N  N   . SER A 103 ? 0.1492 0.0349 0.1434 0.0055  0.0059  0.0186  103 SER A N   
816  C  CA  . SER A 103 ? 0.1159 0.0460 0.1291 0.0190  -0.0140 0.0039  103 SER A CA  
817  C  C   . SER A 103 ? 0.1221 0.0692 0.1433 0.0234  -0.0004 0.0287  103 SER A C   
818  O  O   . SER A 103 ? 0.1309 0.0942 0.1676 0.0145  0.0012  0.0564  103 SER A O   
819  C  CB  . SER A 103 ? 0.1275 0.0556 0.1811 0.0183  -0.0032 -0.0161 103 SER A CB  
820  O  OG  . SER A 103 ? 0.1270 0.0450 0.1586 0.0048  -0.0161 0.0179  103 SER A OG  
821  N  N   . GLU A 104 ? 0.1250 0.0775 0.1315 -0.0003 -0.0211 0.0345  104 GLU A N   
822  C  CA  . GLU A 104 ? 0.1233 0.0726 0.1126 0.0002  -0.0053 0.0298  104 GLU A CA  
823  C  C   . GLU A 104 ? 0.1248 0.0128 0.1463 0.0125  -0.0191 0.0244  104 GLU A C   
824  O  O   . GLU A 104 ? 0.1249 0.0079 0.1785 0.0127  -0.0238 -0.0083 104 GLU A O   
825  C  CB  . GLU A 104 ? 0.1417 0.0947 0.1397 -0.0269 -0.0240 0.0234  104 GLU A CB  
826  C  CG  . GLU A 104 ? 0.1764 0.0299 0.1828 -0.0417 -0.0249 0.0160  104 GLU A CG  
827  C  CD  . GLU A 104 ? 0.1241 0.0217 0.1190 -0.0013 0.0091  0.0304  104 GLU A CD  
828  O  OE1 . GLU A 104 ? 0.1333 0.0532 0.1676 0.0094  0.0107  0.0294  104 GLU A OE1 
829  O  OE2 . GLU A 104 ? 0.1248 0.0944 0.1561 0.0307  -0.0128 0.0149  104 GLU A OE2 
830  N  N   . HIS A 105 ? 0.1263 0.0620 0.1431 0.0032  0.0043  0.0093  105 HIS A N   
831  C  CA  . HIS A 105 ? 0.1259 0.0441 0.1446 0.0122  -0.0275 0.0269  105 HIS A CA  
832  C  C   . HIS A 105 ? 0.1100 0.0462 0.1647 0.0295  -0.0078 0.0366  105 HIS A C   
833  O  O   . HIS A 105 ? 0.1581 0.0308 0.1593 -0.0043 -0.0263 0.0194  105 HIS A O   
834  C  CB  . HIS A 105 ? 0.1280 0.0550 0.1584 0.0312  -0.0111 0.0284  105 HIS A CB  
835  C  CG  . HIS A 105 ? 0.1196 0.0432 0.1649 0.0173  -0.0374 0.0268  105 HIS A CG  
836  N  ND1 . HIS A 105 ? 0.1125 0.0780 0.1403 0.0024  -0.0005 0.0058  105 HIS A ND1 
837  C  CD2 . HIS A 105 ? 0.1288 0.0405 0.1618 0.0153  -0.0095 0.0257  105 HIS A CD2 
838  C  CE1 . HIS A 105 ? 0.1126 0.0562 0.1769 0.0283  -0.0351 0.0387  105 HIS A CE1 
839  N  NE2 . HIS A 105 ? 0.1541 0.0311 0.1607 0.0022  -0.0300 0.0228  105 HIS A NE2 
840  N  N   . THR A 106 ? 0.1171 0.0251 0.1775 0.0086  -0.0063 0.0305  106 THR A N   
841  C  CA  . THR A 106 ? 0.1159 0.0320 0.1840 0.0021  -0.0111 0.0279  106 THR A CA  
842  C  C   . THR A 106 ? 0.1205 0.0408 0.1510 0.0172  -0.0176 0.0421  106 THR A C   
843  O  O   . THR A 106 ? 0.1750 0.0510 0.1564 -0.0207 -0.0179 0.0352  106 THR A O   
844  C  CB  . THR A 106 ? 0.1240 0.0390 0.1646 0.0044  0.0035  0.0209  106 THR A CB  
845  O  OG1 . THR A 106 ? 0.1311 0.0189 0.2040 0.0068  -0.0113 0.0438  106 THR A OG1 
846  C  CG2 . THR A 106 ? 0.1482 0.0320 0.2401 -0.0183 0.0329  -0.0240 106 THR A CG2 
847  N  N   . VAL A 107 ? 0.1311 0.0422 0.2098 -0.0040 0.0060  0.0207  107 VAL A N   
848  C  CA  . VAL A 107 ? 0.1525 0.0701 0.1905 0.0228  -0.0059 0.0148  107 VAL A CA  
849  C  C   . VAL A 107 ? 0.1629 0.0214 0.2105 0.0154  -0.0147 0.0234  107 VAL A C   
850  O  O   . VAL A 107 ? 0.1728 0.0649 0.2243 -0.0277 -0.0077 0.0133  107 VAL A O   
851  C  CB  . VAL A 107 ? 0.1496 0.0277 0.2667 0.0116  -0.0097 -0.0061 107 VAL A CB  
852  C  CG1 . VAL A 107 ? 0.1909 0.0729 0.1990 -0.0019 -0.0085 0.0034  107 VAL A CG1 
853  C  CG2 . VAL A 107 ? 0.1805 0.0261 0.2931 -0.0046 -0.0113 0.0122  107 VAL A CG2 
854  N  N   . SER A 108 ? 0.1352 0.0837 0.2198 -0.0043 -0.0116 -0.0212 108 SER A N   
855  C  CA  . SER A 108 ? 0.1359 0.0186 0.2467 -0.0055 -0.0324 0.0167  108 SER A CA  
856  C  C   . SER A 108 ? 0.1541 0.0958 0.2786 -0.0320 -0.0286 -0.0190 108 SER A C   
857  O  O   . SER A 108 ? 0.1492 0.1039 0.2523 -0.0152 -0.0070 -0.0118 108 SER A O   
858  C  CB  . SER A 108 ? 0.2706 0.0175 0.3246 -0.0067 -0.0137 -0.0588 108 SER A CB  
859  O  OG  . SER A 108 ? 0.2619 0.1654 0.3891 -0.0861 0.0131  -0.1007 108 SER A OG  
860  N  N   . GLY A 109 ? 0.1888 0.0645 0.1701 0.0414  -0.0473 0.0122  109 GLY A N   
861  C  CA  . GLY A 109 ? 0.1692 0.1599 0.1869 0.0302  -0.0242 -0.0142 109 GLY A CA  
862  C  C   . GLY A 109 ? 0.1708 0.1974 0.1837 -0.0304 0.0020  0.0126  109 GLY A C   
863  O  O   . GLY A 109 ? 0.1707 0.3337 0.2388 -0.0096 -0.0125 -0.0807 109 GLY A O   
864  N  N   . GLN A 110 ? 0.1848 0.1309 0.1866 -0.0523 -0.0348 0.0399  110 GLN A N   
865  C  CA  . GLN A 110 ? 0.2161 0.0862 0.1909 -0.0651 0.0015  0.0471  110 GLN A CA  
866  C  C   . GLN A 110 ? 0.1825 0.0484 0.1750 -0.0125 -0.0035 0.0302  110 GLN A C   
867  O  O   . GLN A 110 ? 0.2060 0.0128 0.1789 -0.0044 -0.0054 0.0146  110 GLN A O   
868  C  CB  . GLN A 110 ? 0.3176 0.0794 0.2344 -0.0586 -0.0473 0.0424  110 GLN A CB  
869  C  CG  . GLN A 110 ? 0.2487 0.1714 0.2988 -0.0570 -0.0140 0.0190  110 GLN A CG  
870  C  CD  . GLN A 110 ? 0.2392 0.2254 0.3286 -0.0073 -0.0330 0.1087  110 GLN A CD  
871  O  OE1 . GLN A 110 ? 0.2625 0.1318 0.3434 -0.0277 -0.0535 0.0739  110 GLN A OE1 
872  N  NE2 . GLN A 110 ? 0.2174 0.1880 0.3433 -0.0529 -0.0408 0.0606  110 GLN A NE2 
873  N  N   . HIS A 111 ? 0.1516 0.1762 0.1706 0.0469  -0.0253 0.0072  111 HIS A N   
874  C  CA  . HIS A 111 ? 0.2035 0.1010 0.1776 0.0122  -0.0197 -0.0019 111 HIS A CA  
875  C  C   . HIS A 111 ? 0.1751 0.1189 0.1889 -0.0636 -0.0537 0.0776  111 HIS A C   
876  O  O   . HIS A 111 ? 0.2268 0.2059 0.3886 -0.1403 -0.0895 0.1683  111 HIS A O   
877  C  CB  . HIS A 111 ? 0.3680 0.0331 0.2773 0.0372  0.0347  0.0013  111 HIS A CB  
878  C  CG  . HIS A 111 ? 0.1261 0.0153 0.3189 0.0233  0.0796  -0.0097 111 HIS A CG  
879  N  ND1 . HIS A 111 ? 0.1866 0.1010 0.4850 0.0443  0.0201  0.0292  111 HIS A ND1 
880  C  CD2 . HIS A 111 ? 0.0893 0.0932 0.2555 -0.0178 0.0341  0.0211  111 HIS A CD2 
881  C  CE1 . HIS A 111 ? 0.1995 0.1439 0.3220 0.0337  0.0215  0.0936  111 HIS A CE1 
882  N  NE2 . HIS A 111 ? 0.2209 0.1657 0.3478 0.0663  0.0039  0.0241  111 HIS A NE2 
883  N  N   . PHE A 112 ? 0.1728 0.0710 0.1503 -0.0302 -0.0425 0.0022  112 PHE A N   
884  C  CA  . PHE A 112 ? 0.1553 0.0787 0.1452 -0.0441 -0.0247 0.0380  112 PHE A CA  
885  C  C   . PHE A 112 ? 0.1535 0.0641 0.1988 0.0221  -0.0178 0.0070  112 PHE A C   
886  O  O   . PHE A 112 ? 0.1816 0.0568 0.1460 0.0328  -0.0125 0.0320  112 PHE A O   
887  C  CB  . PHE A 112 ? 0.1628 0.0812 0.1618 -0.0494 -0.0022 0.0099  112 PHE A CB  
888  C  CG  . PHE A 112 ? 0.2012 0.0706 0.1726 -0.0449 0.0115  0.0203  112 PHE A CG  
889  C  CD1 . PHE A 112 ? 0.2076 0.1704 0.1750 -0.0580 -0.0070 -0.0201 112 PHE A CD1 
890  C  CD2 . PHE A 112 ? 0.2584 0.0277 0.2928 -0.0548 0.0089  -0.0059 112 PHE A CD2 
891  C  CE1 . PHE A 112 ? 0.2771 0.1679 0.2254 -0.0646 0.0113  -0.0313 112 PHE A CE1 
892  C  CE2 . PHE A 112 ? 0.2415 0.0765 0.3179 -0.0540 0.0339  -0.0418 112 PHE A CE2 
893  C  CZ  . PHE A 112 ? 0.3104 0.1426 0.3063 -0.1004 0.0188  -0.0906 112 PHE A CZ  
894  N  N   . ALA A 113 ? 0.1640 0.0329 0.1670 0.0179  0.0148  0.0266  113 ALA A N   
895  C  CA  . ALA A 113 ? 0.1674 0.0656 0.1542 -0.0043 0.0065  0.0456  113 ALA A CA  
896  C  C   . ALA A 113 ? 0.1635 0.0708 0.1613 -0.0018 0.0373  0.0452  113 ALA A C   
897  O  O   . ALA A 113 ? 0.1532 0.1093 0.1444 0.0337  0.0027  0.0226  113 ALA A O   
898  C  CB  . ALA A 113 ? 0.1690 0.0841 0.1852 0.0058  0.0027  0.0615  113 ALA A CB  
899  N  N   . ALA A 114 ? 0.1409 0.0521 0.1584 -0.0107 0.0206  0.0368  114 ALA A N   
900  C  CA  . ALA A 114 ? 0.1377 0.0566 0.1112 -0.0158 -0.0041 0.0469  114 ALA A CA  
901  C  C   . ALA A 114 ? 0.1089 0.0662 0.1259 0.0325  -0.0071 0.0111  114 ALA A C   
902  O  O   . ALA A 114 ? 0.1512 0.0555 0.1510 0.0110  0.0054  0.0118  114 ALA A O   
903  C  CB  . ALA A 114 ? 0.1512 0.1085 0.1561 0.0178  -0.0359 0.0436  114 ALA A CB  
904  N  N   . GLU A 115 ? 0.1392 0.1054 0.1137 0.0053  -0.0004 0.0523  115 GLU A N   
905  C  CA  . GLU A 115 ? 0.1377 0.0753 0.0929 0.0179  -0.0148 0.0172  115 GLU A CA  
906  C  C   . GLU A 115 ? 0.1423 0.1434 0.0996 -0.0058 0.0154  0.0107  115 GLU A C   
907  O  O   . GLU A 115 ? 0.1200 0.1071 0.1505 0.0403  -0.0302 -0.0021 115 GLU A O   
908  C  CB  . GLU A 115 ? 0.1530 0.1180 0.0771 0.0085  -0.0132 0.0350  115 GLU A CB  
909  C  CG  . GLU A 115 ? 0.1631 0.0825 0.0891 0.0242  -0.0066 0.0241  115 GLU A CG  
910  C  CD  . GLU A 115 ? 0.1161 0.0747 0.0986 0.0184  -0.0071 -0.0116 115 GLU A CD  
911  O  OE1 . GLU A 115 ? 0.1232 0.0487 0.1410 0.0100  -0.0109 0.0232  115 GLU A OE1 
912  O  OE2 . GLU A 115 ? 0.1197 0.0798 0.1273 0.0097  -0.0175 0.0238  115 GLU A OE2 
913  N  N   . LEU A 116 ? 0.1334 0.0760 0.1245 -0.0013 0.0111  0.0250  116 LEU A N   
914  C  CA  . LEU A 116 ? 0.1020 0.0904 0.1764 0.0271  0.0184  0.0279  116 LEU A CA  
915  C  C   . LEU A 116 ? 0.0990 0.1076 0.1500 0.0176  0.0184  -0.0058 116 LEU A C   
916  O  O   . LEU A 116 ? 0.1232 0.0675 0.1358 0.0204  -0.0126 0.0107  116 LEU A O   
917  C  CB  . LEU A 116 ? 0.1319 0.1218 0.2125 0.0458  -0.0179 0.0326  116 LEU A CB  
918  C  CG  . LEU A 116 ? 0.1553 0.0930 0.2412 0.0036  -0.0392 0.0601  116 LEU A CG  
919  C  CD1 . LEU A 116 ? 0.2242 0.1273 0.2651 0.0139  -0.0012 0.0253  116 LEU A CD1 
920  C  CD2 . LEU A 116 ? 0.1976 0.1319 0.2301 0.0451  0.0270  0.0548  116 LEU A CD2 
921  N  N   . HIS A 117 ? 0.1166 0.0787 0.1449 0.0245  -0.0087 0.0497  117 HIS A N   
922  C  CA  . HIS A 117 ? 0.1097 0.0996 0.1658 0.0285  0.0037  0.0442  117 HIS A CA  
923  C  C   . HIS A 117 ? 0.1250 0.0595 0.1166 0.0010  0.0088  0.0398  117 HIS A C   
924  O  O   . HIS A 117 ? 0.1209 0.1273 0.1349 0.0003  -0.0161 0.0104  117 HIS A O   
925  C  CB  . HIS A 117 ? 0.1166 0.0841 0.1399 0.0177  -0.0093 0.0374  117 HIS A CB  
926  C  CG  . HIS A 117 ? 0.1233 0.0134 0.1405 0.0035  0.0003  0.0238  117 HIS A CG  
927  N  ND1 . HIS A 117 ? 0.1724 0.0230 0.1297 0.0316  -0.0099 0.0142  117 HIS A ND1 
928  C  CD2 . HIS A 117 ? 0.1056 0.0464 0.1446 -0.0142 -0.0122 0.0212  117 HIS A CD2 
929  C  CE1 . HIS A 117 ? 0.1507 0.0821 0.1108 0.0161  -0.0110 0.0508  117 HIS A CE1 
930  N  NE2 . HIS A 117 ? 0.1082 0.0902 0.1579 -0.0019 -0.0185 0.0279  117 HIS A NE2 
931  N  N   . ILE A 118 ? 0.1111 0.0942 0.1171 0.0087  0.0089  0.0366  118 ILE A N   
932  C  CA  . ILE A 118 ? 0.1176 0.1162 0.1336 0.0139  0.0125  0.0278  118 ILE A CA  
933  C  C   . ILE A 118 ? 0.1768 0.0884 0.1753 -0.0072 -0.0069 0.0430  118 ILE A C   
934  O  O   . ILE A 118 ? 0.1530 0.1252 0.1329 0.0332  -0.0068 0.0504  118 ILE A O   
935  C  CB  . ILE A 118 ? 0.0986 0.1266 0.1814 0.0182  -0.0109 0.0686  118 ILE A CB  
936  C  CG1 . ILE A 118 ? 0.1417 0.0444 0.1796 0.0113  -0.0110 0.0306  118 ILE A CG1 
937  C  CG2 . ILE A 118 ? 0.0992 0.1518 0.1773 0.0142  -0.0138 0.0446  118 ILE A CG2 
938  C  CD1 . ILE A 118 ? 0.1484 0.0899 0.2017 0.0472  -0.0440 0.0193  118 ILE A CD1 
939  N  N   . VAL A 119 ? 0.1146 0.0742 0.1615 -0.0087 0.0193  0.0330  119 VAL A N   
940  C  CA  . VAL A 119 ? 0.1247 0.0807 0.1901 0.0226  0.0326  0.0447  119 VAL A CA  
941  C  C   . VAL A 119 ? 0.0968 0.0713 0.1642 -0.0140 -0.0156 0.0456  119 VAL A C   
942  O  O   . VAL A 119 ? 0.1132 0.1118 0.1844 -0.0021 -0.0390 0.0271  119 VAL A O   
943  C  CB  . VAL A 119 ? 0.1097 0.1126 0.1528 0.0279  0.0097  0.0297  119 VAL A CB  
944  C  CG1 . VAL A 119 ? 0.1582 0.0891 0.2130 0.0060  0.0026  0.0528  119 VAL A CG1 
945  C  CG2 . VAL A 119 ? 0.1022 0.1582 0.1877 0.0036  0.0064  0.0305  119 VAL A CG2 
946  N  N   . HIS A 120 ? 0.1229 0.0848 0.1676 0.0217  -0.0068 0.0566  120 HIS A N   
947  C  CA  . HIS A 120 ? 0.1097 0.1177 0.1948 0.0266  -0.0075 0.0609  120 HIS A CA  
948  C  C   . HIS A 120 ? 0.1241 0.1121 0.1754 0.0179  -0.0085 0.0484  120 HIS A C   
949  O  O   . HIS A 120 ? 0.1351 0.0915 0.1905 0.0021  -0.0307 0.0619  120 HIS A O   
950  C  CB  . HIS A 120 ? 0.0934 0.1765 0.1764 0.0392  0.0055  0.0520  120 HIS A CB  
951  C  CG  . HIS A 120 ? 0.1257 0.1898 0.1428 0.0252  0.0044  0.0644  120 HIS A CG  
952  N  ND1 . HIS A 120 ? 0.1315 0.1054 0.1667 0.0340  0.0344  0.0253  120 HIS A ND1 
953  C  CD2 . HIS A 120 ? 0.0819 0.1356 0.1909 -0.0232 -0.0222 0.0551  120 HIS A CD2 
954  C  CE1 . HIS A 120 ? 0.1521 0.1273 0.1523 0.0403  0.0003  0.0173  120 HIS A CE1 
955  N  NE2 . HIS A 120 ? 0.1631 0.1115 0.1812 0.0236  0.0308  0.0431  120 HIS A NE2 
956  N  N   . TYR A 121 ? 0.1309 0.0930 0.2196 -0.0055 -0.0407 0.0791  121 TYR A N   
957  C  CA  . TYR A 121 ? 0.1434 0.1017 0.2586 0.0278  0.0105  0.1008  121 TYR A CA  
958  C  C   . TYR A 121 ? 0.1097 0.1268 0.2107 0.0042  -0.0125 0.0889  121 TYR A C   
959  O  O   . TYR A 121 ? 0.1207 0.1441 0.2182 0.0136  -0.0199 0.0978  121 TYR A O   
960  C  CB  . TYR A 121 ? 0.1703 0.0902 0.3145 0.0138  -0.0132 0.0990  121 TYR A CB  
961  C  CG  . TYR A 121 ? 0.1421 0.1345 0.3416 0.0409  0.0225  0.0447  121 TYR A CG  
962  C  CD1 . TYR A 121 ? 0.2216 0.1220 0.3202 0.0119  -0.0240 0.0152  121 TYR A CD1 
963  C  CD2 . TYR A 121 ? 0.1682 0.1376 0.3565 0.0272  0.0238  0.0547  121 TYR A CD2 
964  C  CE1 . TYR A 121 ? 0.2148 0.1123 0.2974 -0.0447 0.0249  0.0065  121 TYR A CE1 
965  C  CE2 . TYR A 121 ? 0.1883 0.1954 0.3222 0.0106  0.0134  0.0584  121 TYR A CE2 
966  C  CZ  . TYR A 121 ? 0.1810 0.2089 0.3260 -0.0795 -0.0260 0.0469  121 TYR A CZ  
967  O  OH  . TYR A 121 ? 0.2074 0.1595 0.4115 -0.0341 -0.0671 -0.0336 121 TYR A OH  
968  N  N   . ASN A 122 ? 0.1496 0.1823 0.2006 0.0135  -0.0108 0.0904  122 ASN A N   
969  C  CA  . ASN A 122 ? 0.0866 0.2840 0.1926 -0.0039 -0.0326 0.1110  122 ASN A CA  
970  C  C   . ASN A 122 ? 0.1081 0.2477 0.2432 -0.0039 -0.0458 0.1313  122 ASN A C   
971  O  O   . ASN A 122 ? 0.1399 0.2443 0.2513 0.0153  -0.0207 0.1350  122 ASN A O   
972  C  CB  . ASN A 122 ? 0.1467 0.2961 0.2064 -0.0013 -0.0712 0.0901  122 ASN A CB  
973  C  CG  . ASN A 122 ? 0.1952 0.3188 0.2135 0.0732  -0.0541 0.1204  122 ASN A CG  
974  O  OD1 . ASN A 122 ? 0.1848 0.3312 0.2109 0.0089  -0.0295 0.1604  122 ASN A OD1 
975  N  ND2 . ASN A 122 ? 0.2723 0.3837 0.2906 -0.0130 -0.0851 0.0660  122 ASN A ND2 
976  N  N   . SER A 123 ? 0.0925 0.2290 0.2174 0.0009  -0.0395 0.1043  123 SER A N   
977  C  CA  . SER A 123 ? 0.1051 0.1858 0.2191 0.0074  -0.0383 0.1010  123 SER A CA  
978  C  C   . SER A 123 ? 0.1172 0.2212 0.2380 0.0076  -0.0104 0.0836  123 SER A C   
979  O  O   . SER A 123 ? 0.1205 0.3032 0.2955 -0.0380 0.0008  0.1122  123 SER A O   
980  C  CB  . SER A 123 ? 0.0950 0.1808 0.1645 0.0152  -0.0354 0.0626  123 SER A CB  
981  O  OG  . SER A 123 ? 0.1438 0.1987 0.2329 0.0376  -0.0088 0.0728  123 SER A OG  
982  N  N   . ASP A 124 ? 0.1402 0.2426 0.2081 0.0152  -0.0148 0.1273  124 ASP A N   
983  C  CA  . ASP A 124 ? 0.1995 0.3337 0.2293 0.0317  -0.0037 0.1719  124 ASP A CA  
984  C  C   . ASP A 124 ? 0.1945 0.3419 0.2735 -0.0044 -0.0085 0.2249  124 ASP A C   
985  O  O   . ASP A 124 ? 0.2451 0.4135 0.4140 -0.0177 0.0405  0.2913  124 ASP A O   
986  C  CB  . ASP A 124 ? 0.1769 0.3904 0.1632 -0.0050 -0.0229 0.1680  124 ASP A CB  
987  C  CG  . ASP A 124 ? 0.0669 0.2689 0.2131 -0.0627 0.0032  0.0651  124 ASP A CG  
988  O  OD1 . ASP A 124 ? 0.1164 0.3127 0.2327 -0.0308 -0.0266 0.0985  124 ASP A OD1 
989  O  OD2 . ASP A 124 ? 0.1821 0.3418 0.2193 -0.1248 0.0064  0.0782  124 ASP A OD2 
990  N  N   . LEU A 125 ? 0.2307 0.3389 0.3507 0.0558  -0.0167 0.2406  125 LEU A N   
991  C  CA  . LEU A 125 ? 0.2415 0.3073 0.4408 0.0754  0.0461  0.2183  125 LEU A CA  
992  C  C   . LEU A 125 ? 0.2805 0.2898 0.4536 -0.0176 -0.0177 0.2622  125 LEU A C   
993  O  O   . LEU A 125 ? 0.2964 0.2879 0.6795 0.0824  0.1307  0.3133  125 LEU A O   
994  C  CB  . LEU A 125 ? 0.2631 0.3396 0.4049 0.1074  0.0064  0.2167  125 LEU A CB  
995  C  CG  . LEU A 125 ? 0.3912 0.4519 0.5127 0.0858  -0.1719 -0.0612 125 LEU A CG  
996  C  CD1 . LEU A 125 ? 0.4483 0.3229 0.7029 0.0542  -0.2174 0.1606  125 LEU A CD1 
997  C  CD2 . LEU A 125 ? 0.4365 0.6379 0.5417 0.2373  -0.1644 0.0262  125 LEU A CD2 
998  N  N   . TYR A 126 ? 0.1625 0.2070 0.4278 -0.0173 -0.0088 0.2031  126 TYR A N   
999  C  CA  . TYR A 126 ? 0.2207 0.2772 0.4350 0.0129  0.0012  0.1715  126 TYR A CA  
1000 C  C   . TYR A 126 ? 0.1855 0.1786 0.4903 0.0207  -0.0133 0.2111  126 TYR A C   
1001 O  O   . TYR A 126 ? 0.2502 0.1399 0.4353 -0.0037 -0.0702 0.1588  126 TYR A O   
1002 C  CB  . TYR A 126 ? 0.2031 0.1986 0.3546 0.0230  -0.0370 0.1546  126 TYR A CB  
1003 C  CG  . TYR A 126 ? 0.2430 0.1805 0.3183 0.0115  -0.0316 0.1565  126 TYR A CG  
1004 C  CD1 . TYR A 126 ? 0.3273 0.1949 0.2898 0.0111  -0.0357 0.1586  126 TYR A CD1 
1005 C  CD2 . TYR A 126 ? 0.3454 0.2497 0.3963 -0.0171 -0.0996 0.1762  126 TYR A CD2 
1006 C  CE1 . TYR A 126 ? 0.3200 0.3565 0.2500 0.0438  -0.0012 0.1934  126 TYR A CE1 
1007 C  CE2 . TYR A 126 ? 0.2579 0.3224 0.3383 0.0642  -0.0189 0.1669  126 TYR A CE2 
1008 C  CZ  . TYR A 126 ? 0.4901 0.2741 0.2873 0.0793  -0.0748 0.1262  126 TYR A CZ  
1009 O  OH  . TYR A 126 ? 0.5958 0.4371 0.2468 0.2192  -0.0754 0.0854  126 TYR A OH  
1010 N  N   . PRO A 127 ? 0.2284 0.2430 0.5797 -0.0138 -0.0514 0.1602  127 PRO A N   
1011 C  CA  . PRO A 127 ? 0.3416 0.1962 0.6377 0.0252  -0.1197 0.2157  127 PRO A CA  
1012 C  C   . PRO A 127 ? 0.3283 0.1811 0.5094 -0.0535 -0.1936 0.0845  127 PRO A C   
1013 O  O   . PRO A 127 ? 0.4501 0.2825 0.5756 0.0736  -0.2788 0.0152  127 PRO A O   
1014 C  CB  . PRO A 127 ? 0.2809 0.2541 0.8679 -0.0176 -0.1620 0.1328  127 PRO A CB  
1015 C  CG  . PRO A 127 ? 0.2473 0.3282 0.8052 0.0433  -0.0913 0.1064  127 PRO A CG  
1016 C  CD  . PRO A 127 ? 0.2737 0.2537 0.6451 0.0554  -0.0463 0.1654  127 PRO A CD  
1017 N  N   . ASP A 128 ? 0.3420 0.2934 0.4925 -0.0692 -0.1842 0.0312  128 ASP A N   
1018 C  CA  . ASP A 128 ? 0.4899 0.1974 0.4867 -0.0514 -0.1879 0.0305  128 ASP A CA  
1019 C  C   . ASP A 128 ? 0.4227 0.1905 0.3644 0.0177  -0.0853 0.1158  128 ASP A C   
1020 O  O   . ASP A 128 ? 0.4266 0.1234 0.3475 0.0466  -0.1287 0.0326  128 ASP A O   
1021 C  CB  . ASP A 128 ? 0.5315 0.1654 0.4734 -0.0047 -0.1764 0.0602  128 ASP A CB  
1022 C  CG  . ASP A 128 ? 0.4393 0.2058 0.6565 0.0096  -0.1954 0.1385  128 ASP A CG  
1023 O  OD1 . ASP A 128 ? 0.4978 0.2620 0.5368 0.0469  -0.2153 0.0245  128 ASP A OD1 
1024 O  OD2 . ASP A 128 ? 0.4960 0.3875 0.7203 -0.0189 -0.1755 -0.1304 128 ASP A OD2 
1025 N  N   . ALA A 129 ? 0.4785 0.1180 0.3723 0.0428  0.0179  0.0359  129 ALA A N   
1026 C  CA  . ALA A 129 ? 0.4728 0.2289 0.3186 0.1246  -0.0134 0.0970  129 ALA A CA  
1027 C  C   . ALA A 129 ? 0.4627 0.1754 0.3419 0.0908  0.0479  0.0895  129 ALA A C   
1028 O  O   . ALA A 129 ? 0.5237 0.2182 0.3759 0.0732  -0.0008 0.0157  129 ALA A O   
1029 C  CB  . ALA A 129 ? 0.5774 0.1527 0.2638 0.0713  0.0135  0.0098  129 ALA A CB  
1030 N  N   . SER A 130 ? 0.5792 0.2175 0.4286 0.0699  -0.0566 0.0754  130 SER A N   
1031 C  CA  . SER A 130 ? 0.6068 0.1464 0.3657 -0.0006 -0.0212 0.0769  130 SER A CA  
1032 C  C   . SER A 130 ? 0.4472 0.3084 0.3858 0.0705  -0.0204 0.1183  130 SER A C   
1033 O  O   . SER A 130 ? 0.4463 0.2555 0.5465 0.0201  -0.0677 0.1593  130 SER A O   
1034 C  CB  . SER A 130 ? 0.7750 0.0410 0.5588 -0.0508 0.0573  -0.0244 130 SER A CB  
1035 O  OG  . SER A 130 ? 0.6624 0.2460 0.6154 0.0536  0.0420  0.0846  130 SER A OG  
1036 N  N   . THR A 131 ? 0.4694 0.1611 0.3471 -0.0280 -0.0256 0.0275  131 THR A N   
1037 C  CA  . THR A 131 ? 0.3014 0.1877 0.3793 -0.0301 -0.0675 0.0784  131 THR A CA  
1038 C  C   . THR A 131 ? 0.2240 0.0681 0.4176 -0.0184 -0.0600 0.0894  131 THR A C   
1039 O  O   . THR A 131 ? 0.2469 0.1999 0.4433 0.0286  -0.0100 0.1694  131 THR A O   
1040 C  CB  . THR A 131 ? 0.2969 0.1207 0.3489 -0.0013 -0.0586 -0.0204 131 THR A CB  
1041 O  OG1 . THR A 131 ? 0.5029 0.2289 0.5326 -0.0914 -0.1942 -0.0571 131 THR A OG1 
1042 C  CG2 . THR A 131 ? 0.3216 0.2261 0.3769 0.0560  -0.1253 0.0781  131 THR A CG2 
1043 N  N   . ALA A 132 ? 0.2879 0.0672 0.4236 -0.0060 0.0307  0.0917  132 ALA A N   
1044 C  CA  . ALA A 132 ? 0.2243 0.1146 0.4123 0.0061  -0.0582 0.0717  132 ALA A CA  
1045 C  C   . ALA A 132 ? 0.2320 0.1613 0.4211 0.0136  0.0400  0.0817  132 ALA A C   
1046 O  O   . ALA A 132 ? 0.2627 0.0842 0.4801 -0.0234 0.0334  0.0952  132 ALA A O   
1047 C  CB  . ALA A 132 ? 0.2614 0.1098 0.3811 0.0185  0.0072  0.0798  132 ALA A CB  
1048 N  N   . SER A 133 ? 0.2969 0.1139 0.3992 -0.0592 0.0348  0.0922  133 SER A N   
1049 C  CA  . SER A 133 ? 0.2807 0.1678 0.4349 -0.0420 0.0558  0.0273  133 SER A CA  
1050 C  C   . SER A 133 ? 0.2770 0.2270 0.4565 -0.0739 0.0189  -0.0229 133 SER A C   
1051 O  O   . SER A 133 ? 0.2621 0.0935 0.5793 -0.0606 0.0781  -0.0629 133 SER A O   
1052 C  CB  . SER A 133 ? 0.3883 0.1599 0.4745 -0.0047 0.0714  -0.0479 133 SER A CB  
1053 O  OG  . SER A 133 ? 0.2824 0.1384 0.4180 0.0207  0.0582  0.0024  133 SER A OG  
1054 N  N   . ASN A 134 ? 0.2651 0.1654 0.5148 -0.0126 -0.0220 0.0070  134 ASN A N   
1055 C  CA  . ASN A 134 ? 0.2327 0.1855 0.5445 0.0087  -0.0290 -0.0208 134 ASN A CA  
1056 C  C   . ASN A 134 ? 0.2085 0.2858 0.5150 0.0145  -0.0373 0.0762  134 ASN A C   
1057 O  O   . ASN A 134 ? 0.3431 0.4203 0.6059 0.0478  -0.0217 0.2054  134 ASN A O   
1058 C  CB  . ASN A 134 ? 0.2024 0.1141 0.5736 0.0250  -0.0041 0.0828  134 ASN A CB  
1059 C  CG  . ASN A 134 ? 0.2858 0.1726 0.5789 -0.0454 0.1050  0.0792  134 ASN A CG  
1060 O  OD1 . ASN A 134 ? 0.2852 0.2542 0.7446 -0.0321 0.0354  -0.0447 134 ASN A OD1 
1061 N  ND2 . ASN A 134 ? 0.3115 0.1729 0.6966 0.0048  -0.0992 0.0938  134 ASN A ND2 
1062 N  N   . LYS A 135 ? 0.1846 0.2296 0.4911 -0.0277 -0.0065 0.0964  135 LYS A N   
1063 C  CA  . LYS A 135 ? 0.2023 0.3804 0.4508 0.0286  0.0084  0.1360  135 LYS A CA  
1064 C  C   . LYS A 135 ? 0.2565 0.2984 0.2910 0.0718  -0.0405 0.1908  135 LYS A C   
1065 O  O   . LYS A 135 ? 0.2601 0.2629 0.2818 0.0769  0.0363  0.1187  135 LYS A O   
1066 C  CB  . LYS A 135 ? 0.2078 0.3301 0.3774 0.0392  0.0374  0.1699  135 LYS A CB  
1067 C  CG  . LYS A 135 ? 0.3132 0.3397 0.5765 -0.0109 -0.1509 0.2316  135 LYS A CG  
1068 C  CD  . LYS A 135 ? 0.2532 0.3448 0.7005 0.0403  -0.0149 0.1978  135 LYS A CD  
1069 C  CE  . LYS A 135 ? 0.3443 0.4134 0.6048 0.0862  0.0178  0.1083  135 LYS A CE  
1070 N  NZ  . LYS A 135 ? 0.3393 0.4362 0.5201 0.0713  -0.0526 0.1715  135 LYS A NZ  
1071 N  N   . SER A 136 ? 0.3239 0.3786 0.2969 0.1571  -0.0013 0.0708  136 SER A N   
1072 C  CA  . SER A 136 ? 0.3757 0.3917 0.2153 0.1889  0.0665  0.0602  136 SER A CA  
1073 C  C   . SER A 136 ? 0.2681 0.3488 0.2089 0.0768  0.0261  0.1160  136 SER A C   
1074 O  O   . SER A 136 ? 0.2930 0.4864 0.3528 0.0649  0.0401  0.2534  136 SER A O   
1075 C  CB  . SER A 136 ? 0.5640 0.6217 0.2009 0.1406  0.0118  0.0639  136 SER A CB  
1076 O  OG  . SER A 136 ? 0.7397 0.6010 0.2153 0.2338  -0.0340 0.1010  136 SER A OG  
1077 N  N   . GLU A 137 ? 0.3510 0.3400 0.2530 0.0924  -0.0120 0.1638  137 GLU A N   
1078 C  CA  . GLU A 137 ? 0.3387 0.2527 0.2390 0.0339  0.0269  0.1355  137 GLU A CA  
1079 C  C   . GLU A 137 ? 0.2383 0.2791 0.2278 0.0612  0.0614  0.1140  137 GLU A C   
1080 O  O   . GLU A 137 ? 0.3156 0.2388 0.2561 0.1286  0.0456  0.0767  137 GLU A O   
1081 C  CB  . GLU A 137 ? 0.4223 0.3467 0.2779 0.1261  -0.0111 0.0502  137 GLU A CB  
1082 C  CG  . GLU A 137 ? 0.4815 0.3897 0.2552 0.1693  -0.0445 0.0536  137 GLU A CG  
1083 C  CD  . GLU A 137 ? 0.7939 0.5881 0.4354 0.2231  0.0326  -0.0663 137 GLU A CD  
1084 O  OE1 . GLU A 137 ? 0.9389 0.5782 0.4500 -0.0125 -0.0321 0.1520  137 GLU A OE1 
1085 O  OE2 . GLU A 137 ? 1.0432 0.7543 0.7009 0.3276  -0.0779 0.2717  137 GLU A OE2 
1086 N  N   . GLY A 138 ? 0.1992 0.2831 0.1798 0.0794  0.0488  0.1329  138 GLY A N   
1087 C  CA  . GLY A 138 ? 0.1844 0.2065 0.2563 0.0608  0.0188  0.1412  138 GLY A CA  
1088 C  C   . GLY A 138 ? 0.1564 0.2103 0.1489 -0.0039 -0.0063 0.0983  138 GLY A C   
1089 O  O   . GLY A 138 ? 0.1336 0.2338 0.3032 -0.0054 -0.0293 0.1307  138 GLY A O   
1090 N  N   . LEU A 139 ? 0.1234 0.2127 0.2002 0.0066  0.0071  0.0794  139 LEU A N   
1091 C  CA  . LEU A 139 ? 0.1491 0.1160 0.1837 0.0065  0.0041  0.0373  139 LEU A CA  
1092 C  C   . LEU A 139 ? 0.1430 0.1076 0.1732 0.0290  0.0027  0.0611  139 LEU A C   
1093 O  O   . LEU A 139 ? 0.1417 0.1202 0.1672 0.0183  0.0023  0.0616  139 LEU A O   
1094 C  CB  . LEU A 139 ? 0.1521 0.0861 0.2085 0.0283  -0.0044 0.0299  139 LEU A CB  
1095 C  CG  . LEU A 139 ? 0.1069 0.0690 0.2309 0.0303  -0.0079 0.0486  139 LEU A CG  
1096 C  CD1 . LEU A 139 ? 0.1298 0.1419 0.2559 0.0388  0.0027  0.0035  139 LEU A CD1 
1097 C  CD2 . LEU A 139 ? 0.1392 0.1790 0.2596 0.0315  -0.0395 0.0354  139 LEU A CD2 
1098 N  N   . ALA A 140 ? 0.0993 0.1474 0.1234 -0.0176 -0.0370 0.0639  140 ALA A N   
1099 C  CA  . ALA A 140 ? 0.1478 0.1415 0.1434 -0.0068 0.0201  0.0701  140 ALA A CA  
1100 C  C   . ALA A 140 ? 0.1320 0.0993 0.1243 -0.0125 -0.0030 0.0457  140 ALA A C   
1101 O  O   . ALA A 140 ? 0.1363 0.1234 0.1683 0.0015  -0.0276 0.0563  140 ALA A O   
1102 C  CB  . ALA A 140 ? 0.1096 0.1557 0.1864 -0.0095 0.0154  0.0436  140 ALA A CB  
1103 N  N   . VAL A 141 ? 0.1212 0.0906 0.1722 0.0087  0.0296  0.0519  141 VAL A N   
1104 C  CA  . VAL A 141 ? 0.1139 0.0771 0.1494 0.0098  0.0334  0.0419  141 VAL A CA  
1105 C  C   . VAL A 141 ? 0.1121 0.0893 0.1570 0.0103  -0.0032 0.0541  141 VAL A C   
1106 O  O   . VAL A 141 ? 0.1410 0.1115 0.1516 0.0179  -0.0011 0.0389  141 VAL A O   
1107 C  CB  . VAL A 141 ? 0.1546 0.0411 0.1478 0.0445  -0.0016 0.0222  141 VAL A CB  
1108 C  CG1 . VAL A 141 ? 0.1431 0.1780 0.1143 0.0348  -0.0110 0.0257  141 VAL A CG1 
1109 C  CG2 . VAL A 141 ? 0.1435 0.0507 0.1725 0.0229  -0.0157 -0.0140 141 VAL A CG2 
1110 N  N   . LEU A 142 ? 0.1157 0.0842 0.1345 0.0119  -0.0126 0.0354  142 LEU A N   
1111 C  CA  . LEU A 142 ? 0.1266 0.0838 0.1441 0.0197  0.0244  0.0458  142 LEU A CA  
1112 C  C   . LEU A 142 ? 0.1435 0.0539 0.1108 -0.0144 0.0148  0.0496  142 LEU A C   
1113 O  O   . LEU A 142 ? 0.1342 0.1263 0.1360 0.0118  0.0066  0.0001  142 LEU A O   
1114 C  CB  . LEU A 142 ? 0.1270 0.1014 0.1578 0.0236  -0.0004 0.0304  142 LEU A CB  
1115 C  CG  . LEU A 142 ? 0.1252 0.1678 0.1733 0.0697  0.0068  0.0073  142 LEU A CG  
1116 C  CD1 . LEU A 142 ? 0.1283 0.1293 0.2342 0.0397  -0.0133 0.0304  142 LEU A CD1 
1117 C  CD2 . LEU A 142 ? 0.1315 0.1521 0.1420 0.0315  0.0240  0.0320  142 LEU A CD2 
1118 N  N   . ALA A 143 ? 0.1162 0.0476 0.1707 0.0059  0.0168  0.0385  143 ALA A N   
1119 C  CA  . ALA A 143 ? 0.0961 0.1168 0.1355 -0.0087 -0.0038 0.0657  143 ALA A CA  
1120 C  C   . ALA A 143 ? 0.1205 0.0947 0.1212 -0.0031 -0.0071 0.0270  143 ALA A C   
1121 O  O   . ALA A 143 ? 0.1415 0.1187 0.1301 0.0055  0.0089  0.0358  143 ALA A O   
1122 C  CB  . ALA A 143 ? 0.1074 0.1403 0.1549 0.0121  -0.0117 0.0361  143 ALA A CB  
1123 N  N   . VAL A 144 ? 0.1115 0.0524 0.1331 0.0143  -0.0204 0.0565  144 VAL A N   
1124 C  CA  . VAL A 144 ? 0.1473 0.0513 0.1417 -0.0049 -0.0049 0.0475  144 VAL A CA  
1125 C  C   . VAL A 144 ? 0.1622 0.0873 0.1132 -0.0116 0.0077  0.0231  144 VAL A C   
1126 O  O   . VAL A 144 ? 0.1431 0.0566 0.1775 -0.0075 0.0138  0.0076  144 VAL A O   
1127 C  CB  . VAL A 144 ? 0.1232 0.0308 0.1841 0.0381  -0.0030 0.0387  144 VAL A CB  
1128 C  CG1 . VAL A 144 ? 0.2049 0.0446 0.2306 0.0204  -0.0013 0.0631  144 VAL A CG1 
1129 C  CG2 . VAL A 144 ? 0.1241 0.1190 0.1545 0.0388  0.0035  0.0376  144 VAL A CG2 
1130 N  N   . LEU A 145 ? 0.1291 0.0771 0.1629 0.0081  0.0008  0.0264  145 LEU A N   
1131 C  CA  . LEU A 145 ? 0.1595 0.0805 0.1643 -0.0173 0.0042  0.0440  145 LEU A CA  
1132 C  C   . LEU A 145 ? 0.1751 0.0374 0.1531 0.0370  0.0220  0.0218  145 LEU A C   
1133 O  O   . LEU A 145 ? 0.1739 0.0449 0.1830 0.0424  -0.0029 0.0264  145 LEU A O   
1134 C  CB  . LEU A 145 ? 0.1518 0.0780 0.1258 0.0145  -0.0055 0.0283  145 LEU A CB  
1135 C  CG  . LEU A 145 ? 0.1889 0.0936 0.1363 0.0234  -0.0035 0.0414  145 LEU A CG  
1136 C  CD1 . LEU A 145 ? 0.2236 0.1069 0.1537 0.0268  -0.0159 0.0152  145 LEU A CD1 
1137 C  CD2 . LEU A 145 ? 0.2398 0.0516 0.1977 0.0232  -0.0221 0.0301  145 LEU A CD2 
1138 N  N   . ILE A 146 ? 0.1625 0.0713 0.1570 0.0208  0.0274  0.0510  146 ILE A N   
1139 C  CA  . ILE A 146 ? 0.1631 0.0565 0.1510 0.0337  0.0157  0.0295  146 ILE A CA  
1140 C  C   . ILE A 146 ? 0.1548 0.0170 0.1803 0.0077  0.0026  0.0108  146 ILE A C   
1141 O  O   . ILE A 146 ? 0.1798 0.0947 0.1900 0.0462  0.0270  0.0468  146 ILE A O   
1142 C  CB  . ILE A 146 ? 0.1747 0.0629 0.1620 0.0164  0.0034  0.0281  146 ILE A CB  
1143 C  CG1 . ILE A 146 ? 0.1714 0.0703 0.2301 0.0174  0.0132  0.0218  146 ILE A CG1 
1144 C  CG2 . ILE A 146 ? 0.1823 0.1178 0.1757 0.0445  -0.0100 0.0524  146 ILE A CG2 
1145 C  CD1 . ILE A 146 ? 0.2009 0.0476 0.2205 0.0209  -0.0094 0.0420  146 ILE A CD1 
1146 N  N   . GLU A 147 ? 0.2083 0.0327 0.1846 -0.0253 0.0102  0.0408  147 GLU A N   
1147 C  CA  . GLU A 147 ? 0.1829 0.1295 0.1916 -0.0173 0.0194  0.0695  147 GLU A CA  
1148 C  C   . GLU A 147 ? 0.2121 0.0381 0.2110 0.0229  0.0194  0.0666  147 GLU A C   
1149 O  O   . GLU A 147 ? 0.2074 0.0491 0.2250 0.0092  0.0114  0.0601  147 GLU A O   
1150 C  CB  . GLU A 147 ? 0.2421 0.0475 0.2502 0.0030  0.0181  0.0728  147 GLU A CB  
1151 C  CG  . GLU A 147 ? 0.2005 0.0882 0.2503 -0.0093 0.0429  0.0317  147 GLU A CG  
1152 C  CD  . GLU A 147 ? 0.3008 0.0320 0.3079 -0.0276 -0.0030 0.0450  147 GLU A CD  
1153 O  OE1 . GLU A 147 ? 0.3256 0.1117 0.3046 0.0265  -0.0212 0.0088  147 GLU A OE1 
1154 O  OE2 . GLU A 147 ? 0.4135 0.0927 0.4191 0.0460  -0.0604 -0.0128 147 GLU A OE2 
1155 N  N   . MET A 148 ? 0.2254 0.1265 0.2042 0.0105  0.0319  0.0446  148 MET A N   
1156 C  CA  . MET A 148 ? 0.2256 0.1722 0.2196 0.0024  0.0214  0.0877  148 MET A CA  
1157 C  C   . MET A 148 ? 0.3005 0.1725 0.2275 -0.0109 0.0019  0.0859  148 MET A C   
1158 O  O   . MET A 148 ? 0.3948 0.1915 0.2600 -0.0091 -0.0468 0.0790  148 MET A O   
1159 C  CB  . MET A 148 ? 0.2092 0.2615 0.2291 -0.0230 0.0115  0.0954  148 MET A CB  
1160 C  CG  . MET A 148 ? 0.3387 0.2947 0.2212 -0.0736 -0.0148 -0.0181 148 MET A CG  
1161 S  SD  . MET A 148 ? 0.3745 0.3432 0.3168 -0.0472 0.0094  0.0970  148 MET A SD  
1162 N  N   . GLY A 149 ? 0.2816 0.1433 0.2608 -0.0104 0.0177  0.1535  149 GLY A N   
1163 C  CA  . GLY A 149 ? 0.2372 0.1772 0.2881 0.0168  -0.0111 0.1004  149 GLY A CA  
1164 C  C   . GLY A 149 ? 0.2221 0.2041 0.2621 0.0772  0.0315  0.1640  149 GLY A C   
1165 O  O   . GLY A 149 ? 0.2995 0.1033 0.2997 0.0201  0.0554  0.1144  149 GLY A O   
1166 N  N   . SER A 150 ? 0.2246 0.1888 0.3934 0.0951  0.0225  0.1556  150 SER A N   
1167 C  CA  . SER A 150 ? 0.2542 0.1981 0.3618 0.1231  0.0109  0.0873  150 SER A CA  
1168 C  C   . SER A 150 ? 0.2952 0.2753 0.2232 0.0791  0.0245  0.0780  150 SER A C   
1169 O  O   . SER A 150 ? 0.3080 0.2229 0.2643 0.0816  -0.0055 0.0893  150 SER A O   
1170 C  CB  . SER A 150 ? 0.3120 0.3269 0.4579 0.1640  0.0179  -0.0480 150 SER A CB  
1171 O  OG  . SER A 150 ? 0.3998 0.5001 0.5286 0.0662  0.0894  -0.1354 150 SER A OG  
1172 N  N   . PHE A 151 ? 0.2133 0.2374 0.2250 0.0685  0.0247  0.0772  151 PHE A N   
1173 C  CA  . PHE A 151 ? 0.2347 0.2498 0.2386 0.0260  0.0063  0.1227  151 PHE A CA  
1174 C  C   . PHE A 151 ? 0.2780 0.2240 0.1908 0.0848  0.0194  0.0851  151 PHE A C   
1175 O  O   . PHE A 151 ? 0.2972 0.2130 0.2799 0.1067  0.0366  0.1295  151 PHE A O   
1176 C  CB  . PHE A 151 ? 0.2678 0.2340 0.2142 0.0695  0.0091  0.0919  151 PHE A CB  
1177 C  CG  . PHE A 151 ? 0.2525 0.2999 0.2799 0.0762  -0.0422 0.0955  151 PHE A CG  
1178 C  CD1 . PHE A 151 ? 0.2746 0.2195 0.2335 0.0736  -0.0290 0.1405  151 PHE A CD1 
1179 C  CD2 . PHE A 151 ? 0.2380 0.2766 0.2542 0.0455  -0.0006 0.1314  151 PHE A CD2 
1180 C  CE1 . PHE A 151 ? 0.2664 0.3314 0.1909 0.0622  -0.0348 0.1147  151 PHE A CE1 
1181 C  CE2 . PHE A 151 ? 0.2789 0.3054 0.2340 0.0632  -0.0278 0.1286  151 PHE A CE2 
1182 C  CZ  . PHE A 151 ? 0.2692 0.3019 0.2494 0.0317  -0.0476 0.0954  151 PHE A CZ  
1183 N  N   . ASN A 152 ? 0.2152 0.2788 0.1751 0.0248  -0.0220 0.1474  152 ASN A N   
1184 C  CA  . ASN A 152 ? 0.1913 0.2886 0.2171 0.0392  -0.0082 0.1382  152 ASN A CA  
1185 C  C   . ASN A 152 ? 0.2150 0.2910 0.1798 0.0697  -0.0121 0.1441  152 ASN A C   
1186 O  O   . ASN A 152 ? 0.2273 0.3032 0.2048 0.0469  -0.0072 0.1005  152 ASN A O   
1187 C  CB  . ASN A 152 ? 0.2457 0.1718 0.2157 0.0705  0.0279  0.1216  152 ASN A CB  
1188 C  CG  . ASN A 152 ? 0.2019 0.1879 0.2099 0.0690  0.0026  0.1233  152 ASN A CG  
1189 O  OD1 . ASN A 152 ? 0.1999 0.1829 0.2173 0.0361  -0.0212 0.0789  152 ASN A OD1 
1190 N  ND2 . ASN A 152 ? 0.2304 0.1164 0.2346 0.0596  0.0132  0.0558  152 ASN A ND2 
1191 N  N   . PRO A 153 ? 0.1877 0.2462 0.2132 0.0532  0.0002  0.1275  153 PRO A N   
1192 C  CA  . PRO A 153 ? 0.2125 0.2557 0.2198 0.0620  -0.0171 0.1401  153 PRO A CA  
1193 C  C   . PRO A 153 ? 0.2610 0.2444 0.1967 0.0506  -0.0406 0.1315  153 PRO A C   
1194 O  O   . PRO A 153 ? 0.2743 0.2984 0.2541 0.0433  -0.0244 0.0618  153 PRO A O   
1195 C  CB  . PRO A 153 ? 0.2866 0.2460 0.3258 0.0998  -0.0554 0.1336  153 PRO A CB  
1196 C  CG  . PRO A 153 ? 0.2776 0.3057 0.4005 0.1042  -0.0751 0.0813  153 PRO A CG  
1197 C  CD  . PRO A 153 ? 0.2828 0.2696 0.2713 0.1525  -0.0162 0.1214  153 PRO A CD  
1198 N  N   . SER A 154 ? 0.2143 0.2913 0.1938 0.0994  0.0010  0.1370  154 SER A N   
1199 C  CA  . SER A 154 ? 0.2119 0.2557 0.2067 0.0732  -0.0122 0.1099  154 SER A CA  
1200 C  C   . SER A 154 ? 0.1683 0.2381 0.1787 0.0412  0.0089  0.0346  154 SER A C   
1201 O  O   . SER A 154 ? 0.1985 0.2544 0.1787 0.0458  -0.0386 0.0693  154 SER A O   
1202 C  CB  . SER A 154 ? 0.2225 0.2248 0.2037 0.0666  -0.0040 0.0993  154 SER A CB  
1203 O  OG  . SER A 154 ? 0.2579 0.2658 0.3120 0.1021  0.0491  0.0769  154 SER A OG  
1204 N  N   . TYR A 155 ? 0.1649 0.2268 0.1847 0.0726  -0.0198 0.1132  155 TYR A N   
1205 C  CA  . TYR A 155 ? 0.1701 0.1958 0.1676 0.0644  -0.0732 0.0613  155 TYR A CA  
1206 C  C   . TYR A 155 ? 0.1979 0.3397 0.1466 0.0580  -0.0530 0.0807  155 TYR A C   
1207 O  O   . TYR A 155 ? 0.2174 0.3118 0.1701 0.0387  -0.0318 0.0677  155 TYR A O   
1208 C  CB  . TYR A 155 ? 0.1884 0.2146 0.1567 0.0280  -0.0611 0.0729  155 TYR A CB  
1209 C  CG  . TYR A 155 ? 0.1584 0.2137 0.1301 0.0369  -0.0156 0.0490  155 TYR A CG  
1210 C  CD1 . TYR A 155 ? 0.1484 0.1498 0.1746 0.0298  0.0172  0.0616  155 TYR A CD1 
1211 C  CD2 . TYR A 155 ? 0.1624 0.1952 0.1286 0.0291  0.0010  0.0483  155 TYR A CD2 
1212 C  CE1 . TYR A 155 ? 0.1588 0.1270 0.1872 0.0288  -0.0230 0.0826  155 TYR A CE1 
1213 C  CE2 . TYR A 155 ? 0.1507 0.1586 0.1313 0.0041  -0.0207 0.0376  155 TYR A CE2 
1214 C  CZ  . TYR A 155 ? 0.1690 0.1169 0.1628 0.0307  0.0184  0.0870  155 TYR A CZ  
1215 O  OH  . TYR A 155 ? 0.1707 0.1347 0.1776 0.0398  -0.0124 0.0656  155 TYR A OH  
1216 N  N   . ASP A 156 ? 0.2149 0.3561 0.1302 0.0807  -0.0133 0.0886  156 ASP A N   
1217 C  CA  . ASP A 156 ? 0.1868 0.3115 0.1456 0.0206  -0.0307 0.0934  156 ASP A CA  
1218 C  C   . ASP A 156 ? 0.1622 0.2949 0.1234 0.0561  -0.0508 0.0871  156 ASP A C   
1219 O  O   . ASP A 156 ? 0.2303 0.3911 0.1392 0.0628  -0.0477 0.0444  156 ASP A O   
1220 C  CB  . ASP A 156 ? 0.2758 0.3711 0.1579 0.0248  -0.0296 0.1327  156 ASP A CB  
1221 C  CG  . ASP A 156 ? 0.2603 0.2649 0.1848 0.0329  -0.0299 0.1271  156 ASP A CG  
1222 O  OD1 . ASP A 156 ? 0.2770 0.2828 0.1927 0.0952  -0.0077 0.0922  156 ASP A OD1 
1223 O  OD2 . ASP A 156 ? 0.3668 0.3574 0.2117 0.0647  -0.0855 0.0775  156 ASP A OD2 
1224 N  N   . LYS A 157 ? 0.1629 0.3410 0.1851 0.0259  -0.0223 0.0845  157 LYS A N   
1225 C  CA  . LYS A 157 ? 0.2127 0.2789 0.2523 0.0089  -0.0104 0.1049  157 LYS A CA  
1226 C  C   . LYS A 157 ? 0.1962 0.2900 0.2653 0.0412  -0.0311 0.0605  157 LYS A C   
1227 O  O   . LYS A 157 ? 0.2028 0.3305 0.2805 0.0138  -0.0473 0.0610  157 LYS A O   
1228 C  CB  . LYS A 157 ? 0.2017 0.3082 0.2652 0.0265  -0.0351 0.0776  157 LYS A CB  
1229 C  CG  . LYS A 157 ? 0.1927 0.2834 0.2583 0.0075  -0.0071 0.0851  157 LYS A CG  
1230 C  CD  . LYS A 157 ? 0.2660 0.3246 0.2297 0.0703  -0.0359 0.0457  157 LYS A CD  
1231 C  CE  . LYS A 157 ? 0.2769 0.3560 0.2682 0.1239  -0.0392 0.0275  157 LYS A CE  
1232 N  NZ  . LYS A 157 ? 0.2143 0.3044 0.2842 0.0913  -0.0220 0.0537  157 LYS A NZ  
1233 N  N   . ILE A 158 ? 0.1882 0.2433 0.1961 0.0377  -0.0136 0.0712  158 ILE A N   
1234 C  CA  . ILE A 158 ? 0.2301 0.2340 0.1729 0.0458  -0.0167 0.0732  158 ILE A CA  
1235 C  C   . ILE A 158 ? 0.2002 0.3075 0.1683 0.0154  -0.0352 0.0613  158 ILE A C   
1236 O  O   . ILE A 158 ? 0.2599 0.2850 0.1629 0.0430  -0.0051 0.0414  158 ILE A O   
1237 C  CB  . ILE A 158 ? 0.2186 0.2904 0.2155 0.0939  -0.0331 0.0655  158 ILE A CB  
1238 C  CG1 . ILE A 158 ? 0.3147 0.3206 0.2205 0.1140  0.0052  0.1001  158 ILE A CG1 
1239 C  CG2 . ILE A 158 ? 0.2363 0.2161 0.1962 0.0489  -0.0270 0.0467  158 ILE A CG2 
1240 C  CD1 . ILE A 158 ? 0.3970 0.3141 0.2077 0.1002  0.0018  0.0864  158 ILE A CD1 
1241 N  N   . PHE A 159 ? 0.1767 0.3815 0.1891 0.0257  -0.0193 0.0961  159 PHE A N   
1242 C  CA  . PHE A 159 ? 0.1934 0.2854 0.1775 -0.0237 -0.0165 0.0231  159 PHE A CA  
1243 C  C   . PHE A 159 ? 0.2678 0.3323 0.1611 0.0361  -0.0418 0.1148  159 PHE A C   
1244 O  O   . PHE A 159 ? 0.2344 0.4260 0.1767 0.0051  -0.0412 0.0231  159 PHE A O   
1245 C  CB  . PHE A 159 ? 0.2097 0.2072 0.1567 -0.0038 -0.0295 0.0452  159 PHE A CB  
1246 C  CG  . PHE A 159 ? 0.1877 0.2167 0.1561 0.0023  -0.0253 0.0366  159 PHE A CG  
1247 C  CD1 . PHE A 159 ? 0.3064 0.3095 0.1740 0.0641  -0.0356 0.0763  159 PHE A CD1 
1248 C  CD2 . PHE A 159 ? 0.1888 0.2049 0.2028 0.0051  -0.0381 0.0334  159 PHE A CD2 
1249 C  CE1 . PHE A 159 ? 0.2527 0.2690 0.2200 0.0150  -0.0439 0.0613  159 PHE A CE1 
1250 C  CE2 . PHE A 159 ? 0.1794 0.3055 0.2094 0.0061  -0.0489 0.0460  159 PHE A CE2 
1251 C  CZ  . PHE A 159 ? 0.1941 0.2811 0.1826 0.0712  -0.0625 0.0204  159 PHE A CZ  
1252 N  N   . SER A 160 ? 0.2816 0.2363 0.1807 0.0320  -0.0502 0.1087  160 SER A N   
1253 C  CA  . SER A 160 ? 0.2674 0.3271 0.2173 0.0171  -0.0741 0.0454  160 SER A CA  
1254 C  C   . SER A 160 ? 0.2218 0.2908 0.1358 0.0890  -0.0826 0.0421  160 SER A C   
1255 O  O   . SER A 160 ? 0.3556 0.3625 0.1390 0.0337  -0.0710 0.0304  160 SER A O   
1256 C  CB  . SER A 160 ? 0.2367 0.3905 0.1696 0.0155  -0.0741 0.0794  160 SER A CB  
1257 O  OG  . SER A 160 ? 0.2483 0.3831 0.2281 0.0236  -0.0381 0.0820  160 SER A OG  
1258 N  N   . HIS A 161 ? 0.2884 0.2484 0.2329 0.0465  -0.1214 0.0850  161 HIS A N   
1259 C  CA  . HIS A 161 ? 0.2430 0.2454 0.1976 0.0413  -0.0761 0.0204  161 HIS A CA  
1260 C  C   . HIS A 161 ? 0.2539 0.3628 0.2775 0.0757  -0.0502 -0.0259 161 HIS A C   
1261 O  O   . HIS A 161 ? 0.2922 0.3401 0.2311 0.0557  -0.1164 -0.0203 161 HIS A O   
1262 C  CB  . HIS A 161 ? 0.2673 0.3145 0.2290 0.0832  -0.0311 0.0222  161 HIS A CB  
1263 C  CG  . HIS A 161 ? 0.2728 0.2808 0.2382 0.0701  -0.0692 0.0225  161 HIS A CG  
1264 N  ND1 . HIS A 161 ? 0.2602 0.3534 0.3239 0.0421  -0.1032 0.0259  161 HIS A ND1 
1265 C  CD2 . HIS A 161 ? 0.2876 0.2618 0.2653 0.0792  -0.0783 0.0389  161 HIS A CD2 
1266 C  CE1 . HIS A 161 ? 0.2849 0.3244 0.4455 0.0318  -0.0815 -0.0033 161 HIS A CE1 
1267 N  NE2 . HIS A 161 ? 0.2798 0.3800 0.2382 0.0743  -0.0663 0.0353  161 HIS A NE2 
1268 N  N   . LEU A 162 ? 0.2694 0.4111 0.1970 0.0502  -0.0807 -0.0368 162 LEU A N   
1269 C  CA  . LEU A 162 ? 0.3156 0.3960 0.2592 0.0532  -0.1184 -0.0819 162 LEU A CA  
1270 C  C   . LEU A 162 ? 0.3142 0.2976 0.2652 0.0428  -0.0670 -0.0456 162 LEU A C   
1271 O  O   . LEU A 162 ? 0.3624 0.2926 0.3335 0.0831  -0.1342 -0.1110 162 LEU A O   
1272 C  CB  . LEU A 162 ? 0.2839 0.3787 0.2928 0.1124  -0.1167 -0.1488 162 LEU A CB  
1273 C  CG  . LEU A 162 ? 0.3517 0.3725 0.2466 0.0555  -0.1448 -0.1120 162 LEU A CG  
1274 C  CD1 . LEU A 162 ? 0.3250 0.3268 0.4355 0.0963  -0.1386 -0.2053 162 LEU A CD1 
1275 C  CD2 . LEU A 162 ? 0.5759 0.3757 0.2457 0.1882  -0.1679 -0.0719 162 LEU A CD2 
1276 N  N   . GLN A 163 ? 0.3579 0.3968 0.2687 0.0443  -0.0741 -0.0059 163 GLN A N   
1277 C  CA  . GLN A 163 ? 0.4505 0.3447 0.3031 0.0636  -0.0425 -0.0256 163 GLN A CA  
1278 C  C   . GLN A 163 ? 0.3988 0.5065 0.2257 -0.0429 0.0060  -0.0590 163 GLN A C   
1279 O  O   . GLN A 163 ? 0.3012 0.5347 0.3402 -0.0568 0.0259  -0.1178 163 GLN A O   
1280 C  CB  . GLN A 163 ? 0.6692 0.3531 0.3550 -0.0231 -0.0015 0.0109  163 GLN A CB  
1281 C  CG  . GLN A 163 ? 0.7189 0.4401 0.6712 0.0468  -0.1176 0.0276  163 GLN A CG  
1282 C  CD  . GLN A 163 ? 0.9470 0.1039 0.5994 -0.1206 -0.0505 0.1072  163 GLN A CD  
1283 O  OE1 . GLN A 163 ? 0.9175 0.5576 0.7573 0.0894  -0.0264 0.2802  163 GLN A OE1 
1284 N  NE2 . GLN A 163 ? 0.9473 0.5806 0.5334 0.0281  -0.1008 0.2347  163 GLN A NE2 
1285 N  N   . HIS A 164 ? 0.3252 0.5394 0.1542 -0.0296 -0.0842 0.0729  164 HIS A N   
1286 C  CA  . HIS A 164 ? 0.2394 0.4620 0.2153 0.0766  -0.0932 -0.0739 164 HIS A CA  
1287 C  C   . HIS A 164 ? 0.2471 0.4839 0.1979 0.0705  -0.0732 -0.0800 164 HIS A C   
1288 O  O   . HIS A 164 ? 0.3024 0.4863 0.2755 0.0644  -0.0998 -0.0837 164 HIS A O   
1289 C  CB  . HIS A 164 ? 0.2254 0.3623 0.2380 0.0212  -0.0447 0.0280  164 HIS A CB  
1290 C  CG  . HIS A 164 ? 0.2074 0.3769 0.3098 0.0119  -0.0658 0.0570  164 HIS A CG  
1291 N  ND1 . HIS A 164 ? 0.2575 0.4290 0.3190 -0.0220 -0.1062 -0.0060 164 HIS A ND1 
1292 C  CD2 . HIS A 164 ? 0.2002 0.3128 0.4802 -0.0179 -0.0593 0.0564  164 HIS A CD2 
1293 C  CE1 . HIS A 164 ? 0.2558 0.3289 0.3683 -0.0719 -0.0650 0.0104  164 HIS A CE1 
1294 N  NE2 . HIS A 164 ? 0.3866 0.3682 0.4582 0.0425  -0.0619 0.0220  164 HIS A NE2 
1295 N  N   . VAL A 165 ? 0.2320 0.3775 0.2561 0.0438  -0.0858 -0.0735 165 VAL A N   
1296 C  CA  . VAL A 165 ? 0.2745 0.3407 0.2956 0.0879  -0.0860 -0.0907 165 VAL A CA  
1297 C  C   . VAL A 165 ? 0.2718 0.3450 0.2117 0.0692  -0.0792 -0.0833 165 VAL A C   
1298 O  O   . VAL A 165 ? 0.2632 0.4902 0.1988 0.1054  -0.0798 -0.1120 165 VAL A O   
1299 C  CB  . VAL A 165 ? 0.2446 0.3297 0.2973 0.0023  -0.0629 -0.0155 165 VAL A CB  
1300 C  CG1 . VAL A 165 ? 0.2378 0.3975 0.3488 0.0363  -0.0692 -0.1276 165 VAL A CG1 
1301 C  CG2 . VAL A 165 ? 0.2493 0.3872 0.3582 0.0117  -0.1468 -0.0793 165 VAL A CG2 
1302 N  N   . LYS A 166 ? 0.2429 0.3336 0.2707 0.0397  -0.0632 -0.0487 166 LYS A N   
1303 C  CA  . LYS A 166 ? 0.2380 0.2509 0.2873 0.0291  -0.0452 -0.0721 166 LYS A CA  
1304 C  C   . LYS A 166 ? 0.2669 0.3133 0.1988 0.0356  -0.1000 -0.0466 166 LYS A C   
1305 O  O   . LYS A 166 ? 0.2380 0.3048 0.2846 0.0458  -0.0959 -0.1417 166 LYS A O   
1306 C  CB  . LYS A 166 ? 0.3005 0.4562 0.2927 0.0067  -0.0967 -0.0398 166 LYS A CB  
1307 C  CG  . LYS A 166 ? 0.3531 0.3176 0.3495 0.0171  -0.0225 -0.1225 166 LYS A CG  
1308 C  CD  . LYS A 166 ? 0.4089 0.3468 0.4138 0.0058  0.0589  -0.0297 166 LYS A CD  
1309 C  CE  . LYS A 166 ? 0.7365 0.3560 0.2951 0.0477  0.0299  -0.0122 166 LYS A CE  
1310 N  NZ  . LYS A 166 ? 0.9314 0.6067 0.1133 0.0930  -0.1377 -0.0723 166 LYS A NZ  
1311 N  N   . TYR A 167 ? 0.2639 0.2620 0.2245 0.0201  -0.0329 -0.0439 167 TYR A N   
1312 C  CA  . TYR A 167 ? 0.3203 0.2734 0.1855 0.0681  -0.0273 -0.0383 167 TYR A CA  
1313 C  C   . TYR A 167 ? 0.2015 0.3031 0.2361 0.0236  -0.0494 -0.0465 167 TYR A C   
1314 O  O   . TYR A 167 ? 0.2164 0.4057 0.2155 0.0556  -0.0336 0.0106  167 TYR A O   
1315 C  CB  . TYR A 167 ? 0.2928 0.2358 0.1855 -0.0315 -0.0330 -0.0060 167 TYR A CB  
1316 C  CG  . TYR A 167 ? 0.3000 0.1804 0.1737 0.0092  -0.0331 -0.0299 167 TYR A CG  
1317 C  CD1 . TYR A 167 ? 0.2868 0.1934 0.2496 -0.0309 -0.0512 -0.0251 167 TYR A CD1 
1318 C  CD2 . TYR A 167 ? 0.3509 0.1318 0.2254 -0.0115 -0.0568 -0.0002 167 TYR A CD2 
1319 C  CE1 . TYR A 167 ? 0.3345 0.2160 0.2658 -0.0019 -0.0362 0.0199  167 TYR A CE1 
1320 C  CE2 . TYR A 167 ? 0.3790 0.2861 0.1857 -0.0111 -0.0855 0.0264  167 TYR A CE2 
1321 C  CZ  . TYR A 167 ? 0.3798 0.3192 0.3070 -0.0401 -0.0604 0.0866  167 TYR A CZ  
1322 O  OH  . TYR A 167 ? 0.4627 0.3212 0.3052 -0.1021 0.0460  -0.0330 167 TYR A OH  
1323 N  N   . LYS A 168 ? 0.2818 0.4012 0.2471 0.1450  -0.0040 -0.0286 168 LYS A N   
1324 C  CA  . LYS A 168 ? 0.3640 0.5102 0.2010 0.2046  0.0158  0.0663  168 LYS A CA  
1325 C  C   . LYS A 168 ? 0.4133 0.4489 0.3459 0.1582  0.0592  0.1054  168 LYS A C   
1326 O  O   . LYS A 168 ? 0.4236 0.5841 0.3669 0.1161  0.0673  0.0769  168 LYS A O   
1327 C  CB  . LYS A 168 ? 0.3882 0.6125 0.2137 0.2336  -0.0057 0.1234  168 LYS A CB  
1328 C  CG  . LYS A 168 ? 0.4441 0.6442 0.3833 0.1794  0.0769  0.1817  168 LYS A CG  
1329 C  CD  . LYS A 168 ? 0.4146 0.5031 0.4762 0.1088  0.0598  0.2037  168 LYS A CD  
1330 C  CE  . LYS A 168 ? 0.6432 0.3527 0.6792 -0.1725 0.1559  0.2103  168 LYS A CE  
1331 N  NZ  . LYS A 168 ? 0.3377 0.2544 0.9374 -0.0369 0.1560  0.2083  168 LYS A NZ  
1332 N  N   . GLY A 169 ? 0.3628 0.3778 0.4087 0.1489  0.0589  0.1942  169 GLY A N   
1333 C  CA  . GLY A 169 ? 0.4397 0.5360 0.4171 0.1102  0.0240  0.1361  169 GLY A CA  
1334 C  C   . GLY A 169 ? 0.4008 0.4774 0.4365 0.0606  -0.0100 0.1154  169 GLY A C   
1335 O  O   . GLY A 169 ? 0.3862 0.6113 0.6087 0.1470  0.0140  0.2617  169 GLY A O   
1336 N  N   . GLN A 170 ? 0.3115 0.2582 0.2998 0.1007  -0.0274 -0.0731 170 GLN A N   
1337 C  CA  . GLN A 170 ? 0.2455 0.3154 0.2368 0.0326  -0.0118 -0.0175 170 GLN A CA  
1338 C  C   . GLN A 170 ? 0.3251 0.4483 0.2010 0.0146  -0.0111 -0.0833 170 GLN A C   
1339 O  O   . GLN A 170 ? 0.2440 0.6421 0.2103 0.1131  -0.0388 -0.0644 170 GLN A O   
1340 C  CB  . GLN A 170 ? 0.2834 0.2620 0.2469 -0.0002 0.0133  -0.0367 170 GLN A CB  
1341 C  CG  . GLN A 170 ? 0.2975 0.2160 0.2394 0.0263  -0.0348 -0.0489 170 GLN A CG  
1342 C  CD  . GLN A 170 ? 0.3010 0.2559 0.2214 -0.0212 -0.0294 -0.0970 170 GLN A CD  
1343 O  OE1 . GLN A 170 ? 0.3365 0.2417 0.2921 0.0011  -0.0930 -0.0952 170 GLN A OE1 
1344 N  NE2 . GLN A 170 ? 0.2815 0.4123 0.2328 -0.0955 -0.0080 -0.1412 170 GLN A NE2 
1345 N  N   . GLU A 171 ? 0.2843 0.4903 0.2789 -0.0640 -0.0262 -0.1258 171 GLU A N   
1346 C  CA  . GLU A 171 ? 0.3406 0.4434 0.2335 -0.0001 -0.0325 -0.0619 171 GLU A CA  
1347 C  C   . GLU A 171 ? 0.2613 0.4501 0.2187 0.0061  -0.0772 -0.1284 171 GLU A C   
1348 O  O   . GLU A 171 ? 0.3028 0.7382 0.2202 0.0973  -0.1175 -0.1643 171 GLU A O   
1349 C  CB  . GLU A 171 ? 0.2811 0.4983 0.3600 -0.1229 -0.0250 -0.1409 171 GLU A CB  
1350 C  CG  . GLU A 171 ? 0.4571 0.4996 0.6258 -0.0581 0.1278  -0.1193 171 GLU A CG  
1351 C  CD  . GLU A 171 ? 0.3094 0.3304 0.7117 0.0660  0.1593  -0.1347 171 GLU A CD  
1352 O  OE1 . GLU A 171 ? 0.3318 0.5263 0.5926 -0.0116 -0.0075 -0.1428 171 GLU A OE1 
1353 O  OE2 . GLU A 171 ? 0.6928 0.1714 0.9256 0.0027  0.1261  0.0252  171 GLU A OE2 
1354 N  N   . ALA A 172 ? 0.2621 0.3639 0.2411 0.0384  -0.0751 -0.0569 172 ALA A N   
1355 C  CA  . ALA A 172 ? 0.1828 0.4932 0.2707 0.0247  -0.0810 0.0226  172 ALA A CA  
1356 C  C   . ALA A 172 ? 0.2099 0.4275 0.2095 0.0000  -0.0820 0.0161  172 ALA A C   
1357 O  O   . ALA A 172 ? 0.2770 0.4920 0.2044 0.0384  -0.1268 -0.0095 172 ALA A O   
1358 C  CB  . ALA A 172 ? 0.2037 0.4977 0.2446 0.0439  -0.0308 0.0519  172 ALA A CB  
1359 N  N   . PHE A 173 ? 0.1829 0.5860 0.2417 0.0620  -0.0571 0.0157  173 PHE A N   
1360 C  CA  . PHE A 173 ? 0.1783 0.4983 0.2530 0.0493  -0.0776 -0.0270 173 PHE A CA  
1361 C  C   . PHE A 173 ? 0.2732 0.5450 0.2617 -0.0271 -0.0472 -0.0111 173 PHE A C   
1362 O  O   . PHE A 173 ? 0.2995 0.6393 0.2306 0.0189  -0.0512 0.0046  173 PHE A O   
1363 C  CB  . PHE A 173 ? 0.2175 0.5100 0.2916 0.0065  -0.0906 -0.1031 173 PHE A CB  
1364 C  CG  . PHE A 173 ? 0.2345 0.4314 0.3109 0.1064  -0.0681 -0.1176 173 PHE A CG  
1365 C  CD1 . PHE A 173 ? 0.2750 0.5170 0.3553 0.0892  -0.1553 -0.0319 173 PHE A CD1 
1366 C  CD2 . PHE A 173 ? 0.4199 0.4243 0.3895 0.0980  -0.0343 -0.1490 173 PHE A CD2 
1367 C  CE1 . PHE A 173 ? 0.2755 0.5554 0.3700 0.1341  -0.1190 -0.0248 173 PHE A CE1 
1368 C  CE2 . PHE A 173 ? 0.2633 0.4770 0.4709 0.1845  -0.0795 -0.0334 173 PHE A CE2 
1369 C  CZ  . PHE A 173 ? 0.3401 0.5511 0.4713 0.0234  -0.1412 -0.0710 173 PHE A CZ  
1370 N  N   . VAL A 174 ? 0.2117 0.5104 0.2667 0.0545  -0.0983 -0.0163 174 VAL A N   
1371 C  CA  . VAL A 174 ? 0.1642 0.4817 0.2080 0.0439  -0.0525 0.0668  174 VAL A CA  
1372 C  C   . VAL A 174 ? 0.1675 0.3704 0.1877 0.0496  -0.0898 -0.0245 174 VAL A C   
1373 O  O   . VAL A 174 ? 0.2135 0.4196 0.2419 0.0790  -0.0807 0.0706  174 VAL A O   
1374 C  CB  . VAL A 174 ? 0.1884 0.3629 0.2602 -0.0253 -0.0608 0.0590  174 VAL A CB  
1375 C  CG1 . VAL A 174 ? 0.2861 0.3577 0.2509 0.0168  -0.0491 0.0469  174 VAL A CG1 
1376 C  CG2 . VAL A 174 ? 0.2228 0.3861 0.2525 0.0116  -0.0819 0.0207  174 VAL A CG2 
1377 N  N   . PRO A 175 ? 0.2189 0.4786 0.1647 0.0966  -0.0599 0.0337  175 PRO A N   
1378 C  CA  . PRO A 175 ? 0.1905 0.4875 0.2753 0.0899  -0.0409 0.0517  175 PRO A CA  
1379 C  C   . PRO A 175 ? 0.1729 0.4030 0.2791 0.0866  -0.0383 0.0734  175 PRO A C   
1380 O  O   . PRO A 175 ? 0.2428 0.3265 0.2425 0.0384  -0.0839 0.0454  175 PRO A O   
1381 C  CB  . PRO A 175 ? 0.2249 0.5508 0.2710 0.1300  -0.0544 0.0651  175 PRO A CB  
1382 C  CG  . PRO A 175 ? 0.2411 0.3711 0.3280 0.1668  -0.0092 0.0898  175 PRO A CG  
1383 C  CD  . PRO A 175 ? 0.2005 0.3746 0.2904 0.1146  -0.0005 0.1233  175 PRO A CD  
1384 N  N   . GLY A 176 ? 0.2010 0.3033 0.2443 0.0628  -0.0556 0.0622  176 GLY A N   
1385 C  CA  . GLY A 176 ? 0.1579 0.3493 0.2794 0.0125  -0.0329 0.0334  176 GLY A CA  
1386 C  C   . GLY A 176 ? 0.2059 0.3575 0.1725 -0.0256 -0.0747 0.0457  176 GLY A C   
1387 O  O   . GLY A 176 ? 0.2207 0.3781 0.2426 -0.0256 -0.1038 0.0726  176 GLY A O   
1388 N  N   . PHE A 177 ? 0.1965 0.3110 0.2173 0.0216  -0.0995 0.0136  177 PHE A N   
1389 C  CA  . PHE A 177 ? 0.1505 0.3134 0.2189 0.0147  -0.0361 0.0665  177 PHE A CA  
1390 C  C   . PHE A 177 ? 0.1699 0.2590 0.2259 0.0336  -0.0502 0.0530  177 PHE A C   
1391 O  O   . PHE A 177 ? 0.1582 0.3082 0.2547 0.0544  -0.0447 0.0937  177 PHE A O   
1392 C  CB  . PHE A 177 ? 0.1426 0.2920 0.2476 0.0031  -0.0464 0.1077  177 PHE A CB  
1393 C  CG  . PHE A 177 ? 0.1252 0.3170 0.2067 -0.0011 -0.0269 0.0820  177 PHE A CG  
1394 C  CD1 . PHE A 177 ? 0.1794 0.3431 0.1732 0.0693  -0.0232 0.0682  177 PHE A CD1 
1395 C  CD2 . PHE A 177 ? 0.1613 0.2407 0.2636 0.0025  -0.0427 0.0873  177 PHE A CD2 
1396 C  CE1 . PHE A 177 ? 0.1477 0.4370 0.1909 0.0307  -0.0254 0.0885  177 PHE A CE1 
1397 C  CE2 . PHE A 177 ? 0.1593 0.2745 0.1859 -0.0066 -0.0559 0.0458  177 PHE A CE2 
1398 C  CZ  . PHE A 177 ? 0.1779 0.3141 0.1828 0.0769  -0.0405 0.0643  177 PHE A CZ  
1399 N  N   . ASN A 178 ? 0.1417 0.2174 0.1926 0.0376  -0.0494 0.0936  178 ASN A N   
1400 C  CA  . ASN A 178 ? 0.1241 0.2132 0.1758 0.0636  -0.0577 0.0748  178 ASN A CA  
1401 C  C   . ASN A 178 ? 0.1187 0.1624 0.1857 0.0823  -0.0372 0.0218  178 ASN A C   
1402 O  O   . ASN A 178 ? 0.1525 0.2303 0.2275 0.0664  -0.0114 0.0666  178 ASN A O   
1403 C  CB  . ASN A 178 ? 0.1805 0.2426 0.2246 0.0952  -0.0370 0.0477  178 ASN A CB  
1404 C  CG  . ASN A 178 ? 0.2152 0.1948 0.2132 0.0237  -0.0166 0.0587  178 ASN A CG  
1405 O  OD1 . ASN A 178 ? 0.1747 0.2516 0.2132 0.0570  -0.0001 0.0803  178 ASN A OD1 
1406 N  ND2 . ASN A 178 ? 0.2286 0.2207 0.3312 0.0917  -0.0013 0.0708  178 ASN A ND2 
1407 N  N   . ILE A 179 ? 0.1514 0.1642 0.2299 0.0839  -0.0373 0.0552  179 ILE A N   
1408 C  CA  . ILE A 179 ? 0.1269 0.1603 0.2247 0.0275  -0.0432 0.0399  179 ILE A CA  
1409 C  C   . ILE A 179 ? 0.1377 0.1721 0.1954 0.0495  -0.0589 0.0442  179 ILE A C   
1410 O  O   . ILE A 179 ? 0.1397 0.1888 0.1703 0.0215  -0.0126 0.0621  179 ILE A O   
1411 C  CB  . ILE A 179 ? 0.1265 0.1855 0.1974 0.0294  -0.0406 0.0705  179 ILE A CB  
1412 C  CG1 . ILE A 179 ? 0.1618 0.1552 0.2010 0.0183  -0.0009 0.0488  179 ILE A CG1 
1413 C  CG2 . ILE A 179 ? 0.1428 0.1904 0.2119 0.0402  -0.0646 0.0753  179 ILE A CG2 
1414 C  CD1 . ILE A 179 ? 0.1466 0.1593 0.2020 0.0365  -0.0077 0.0351  179 ILE A CD1 
1415 N  N   . GLU A 180 ? 0.1703 0.1829 0.1778 0.0317  0.0000  0.0583  180 GLU A N   
1416 C  CA  . GLU A 180 ? 0.1772 0.1650 0.1712 0.0739  0.0193  0.0594  180 GLU A CA  
1417 C  C   . GLU A 180 ? 0.1455 0.2428 0.1654 0.0395  0.0247  0.0658  180 GLU A C   
1418 O  O   . GLU A 180 ? 0.1739 0.2243 0.2541 0.0633  -0.0097 0.0649  180 GLU A O   
1419 C  CB  . GLU A 180 ? 0.1560 0.2586 0.2153 0.0643  0.0212  -0.0072 180 GLU A CB  
1420 C  CG  . GLU A 180 ? 0.2579 0.4163 0.1927 0.0850  0.0013  -0.0194 180 GLU A CG  
1421 C  CD  . GLU A 180 ? 0.3388 0.3980 0.1773 0.1751  0.0136  0.0461  180 GLU A CD  
1422 O  OE1 . GLU A 180 ? 0.3380 0.3484 0.3118 0.1922  0.0564  0.0339  180 GLU A OE1 
1423 O  OE2 . GLU A 180 ? 0.3808 0.2939 0.2638 0.1259  0.0281  -0.0147 180 GLU A OE2 
1424 N  N   . GLU A 181 ? 0.1746 0.1478 0.1643 0.0591  0.0208  0.0632  181 GLU A N   
1425 C  CA  . GLU A 181 ? 0.1537 0.1940 0.1886 0.0230  0.0105  0.0590  181 GLU A CA  
1426 C  C   . GLU A 181 ? 0.1657 0.1330 0.2507 0.0348  0.0219  0.0783  181 GLU A C   
1427 O  O   . GLU A 181 ? 0.1692 0.1291 0.2381 0.0339  0.0201  0.0760  181 GLU A O   
1428 C  CB  . GLU A 181 ? 0.1672 0.1956 0.1873 0.1113  -0.0035 0.0789  181 GLU A CB  
1429 C  CG  . GLU A 181 ? 0.1464 0.2741 0.2627 0.0921  -0.0089 0.0974  181 GLU A CG  
1430 C  CD  . GLU A 181 ? 0.1898 0.2710 0.2730 0.0497  -0.0220 0.1324  181 GLU A CD  
1431 O  OE1 . GLU A 181 ? 0.1708 0.2983 0.2813 0.0597  -0.0451 0.0993  181 GLU A OE1 
1432 O  OE2 . GLU A 181 ? 0.1959 0.2490 0.3070 0.0746  -0.0284 0.0941  181 GLU A OE2 
1433 N  N   . LEU A 182 ? 0.1496 0.1128 0.1631 0.0528  -0.0198 0.0150  182 LEU A N   
1434 C  CA  . LEU A 182 ? 0.1387 0.1236 0.1653 0.0302  0.0051  0.0286  182 LEU A CA  
1435 C  C   . LEU A 182 ? 0.1679 0.1121 0.1561 0.0456  -0.0016 0.0263  182 LEU A C   
1436 O  O   . LEU A 182 ? 0.1627 0.1904 0.1566 0.0314  -0.0118 0.0396  182 LEU A O   
1437 C  CB  . LEU A 182 ? 0.1864 0.1166 0.1302 0.0419  -0.0038 0.0513  182 LEU A CB  
1438 C  CG  . LEU A 182 ? 0.2128 0.1085 0.1841 0.0405  -0.0230 0.0596  182 LEU A CG  
1439 C  CD1 . LEU A 182 ? 0.1613 0.0992 0.2241 0.0332  -0.0156 0.0155  182 LEU A CD1 
1440 C  CD2 . LEU A 182 ? 0.1560 0.1811 0.1505 0.0444  -0.0020 0.0334  182 LEU A CD2 
1441 N  N   . LEU A 183 ? 0.1693 0.1876 0.1166 0.0447  -0.0140 0.0290  183 LEU A N   
1442 C  CA  . LEU A 183 ? 0.1877 0.1424 0.1280 -0.0016 -0.0041 0.0132  183 LEU A CA  
1443 C  C   . LEU A 183 ? 0.1403 0.1381 0.2101 0.0425  0.0086  0.0432  183 LEU A C   
1444 O  O   . LEU A 183 ? 0.2052 0.1205 0.2304 0.0487  -0.0081 0.0480  183 LEU A O   
1445 C  CB  . LEU A 183 ? 0.1990 0.1507 0.1563 -0.0069 0.0100  0.0509  183 LEU A CB  
1446 C  CG  . LEU A 183 ? 0.1753 0.1473 0.1930 0.0011  0.0346  0.0633  183 LEU A CG  
1447 C  CD1 . LEU A 183 ? 0.2776 0.1640 0.2347 0.0034  0.0938  0.0012  183 LEU A CD1 
1448 C  CD2 . LEU A 183 ? 0.2192 0.1755 0.2067 0.0406  0.0312  0.0291  183 LEU A CD2 
1449 N  N   . PRO A 184 ? 0.1462 0.1046 0.1987 0.0392  -0.0138 0.0385  184 PRO A N   
1450 C  CA  . PRO A 184 ? 0.1963 0.1164 0.2049 0.0100  -0.0137 0.0617  184 PRO A CA  
1451 C  C   . PRO A 184 ? 0.2246 0.1013 0.2089 0.0452  -0.0262 0.0752  184 PRO A C   
1452 O  O   . PRO A 184 ? 0.2987 0.0746 0.2289 0.0298  0.0199  0.0455  184 PRO A O   
1453 C  CB  . PRO A 184 ? 0.2069 0.1360 0.1995 0.0065  -0.0239 0.0675  184 PRO A CB  
1454 C  CG  . PRO A 184 ? 0.1564 0.1018 0.2732 0.0002  -0.0150 0.0807  184 PRO A CG  
1455 C  CD  . PRO A 184 ? 0.2081 0.0719 0.1859 0.0462  0.0018  0.0347  184 PRO A CD  
1456 N  N   . GLU A 185 ? 0.2360 0.1239 0.2730 0.0299  -0.0297 0.0433  185 GLU A N   
1457 C  CA  . GLU A 185 ? 0.3550 0.0654 0.2507 0.0127  -0.0509 0.0340  185 GLU A CA  
1458 C  C   . GLU A 185 ? 0.2153 0.2060 0.2497 0.0569  -0.0074 0.0575  185 GLU A C   
1459 O  O   . GLU A 185 ? 0.2070 0.1014 0.2883 0.0252  -0.0161 0.0374  185 GLU A O   
1460 C  CB  . GLU A 185 ? 0.4756 0.0323 0.3072 0.0197  -0.0299 0.0168  185 GLU A CB  
1461 C  CG  . GLU A 185 ? 0.4035 0.2873 0.3330 0.1653  0.0062  0.1559  185 GLU A CG  
1462 C  CD  . GLU A 185 ? 0.4254 0.4996 0.4225 0.1424  -0.0032 -0.0089 185 GLU A CD  
1463 O  OE1 . GLU A 185 ? 0.5147 0.5061 0.4820 0.2648  0.0802  0.1208  185 GLU A OE1 
1464 O  OE2 . GLU A 185 ? 0.7508 0.8071 0.4584 0.0958  -0.1558 0.0057  185 GLU A OE2 
1465 N  N   . ARG A 186 ? 0.2268 0.0827 0.2561 0.0369  0.0158  0.0433  186 ARG A N   
1466 C  CA  . ARG A 186 ? 0.2834 0.1185 0.2776 0.0326  0.0204  0.0530  186 ARG A CA  
1467 C  C   . ARG A 186 ? 0.1474 0.0954 0.3093 0.0623  0.0050  0.0052  186 ARG A C   
1468 O  O   . ARG A 186 ? 0.1786 0.1180 0.2622 0.0379  -0.0086 0.0215  186 ARG A O   
1469 C  CB  . ARG A 186 ? 0.2998 0.0990 0.3679 0.0298  0.0385  0.0254  186 ARG A CB  
1470 C  CG  . ARG A 186 ? 0.4071 0.1245 0.4059 0.0179  -0.0405 0.1090  186 ARG A CG  
1471 C  CD  . ARG A 186 ? 0.3870 0.1714 0.4796 0.0000  0.0055  0.0050  186 ARG A CD  
1472 N  NE  . ARG A 186 ? 0.4173 0.2024 0.5664 0.0127  0.0452  0.0350  186 ARG A NE  
1473 C  CZ  . ARG A 186 ? 0.5263 0.3465 0.5690 0.0494  0.1331  -0.1869 186 ARG A CZ  
1474 N  NH1 . ARG A 186 ? 0.6575 0.3406 0.7727 -0.0136 -0.0494 -0.1348 186 ARG A NH1 
1475 N  NH2 . ARG A 186 ? 0.5216 0.1406 0.6707 0.0106  -0.0471 -0.0402 186 ARG A NH2 
1476 N  N   . THR A 187 ? 0.2127 0.0717 0.2676 0.0208  0.0251  -0.0179 187 THR A N   
1477 C  CA  . THR A 187 ? 0.1690 0.0913 0.1956 0.0625  0.0152  -0.0044 187 THR A CA  
1478 C  C   . THR A 187 ? 0.2024 0.1428 0.1787 0.0286  -0.0168 -0.0174 187 THR A C   
1479 O  O   . THR A 187 ? 0.1907 0.1334 0.2096 0.0086  -0.0013 0.0088  187 THR A O   
1480 C  CB  . THR A 187 ? 0.1782 0.1773 0.2247 0.0207  -0.0065 0.0042  187 THR A CB  
1481 O  OG1 . THR A 187 ? 0.1790 0.1990 0.2786 0.0242  0.0029  -0.0057 187 THR A OG1 
1482 C  CG2 . THR A 187 ? 0.2145 0.1897 0.2457 -0.0167 0.0240  -0.0013 187 THR A CG2 
1483 N  N   . ALA A 188 ? 0.2182 0.1568 0.1949 0.0222  0.0297  -0.0197 188 ALA A N   
1484 C  CA  . ALA A 188 ? 0.1916 0.1733 0.2088 0.0285  -0.0162 -0.0339 188 ALA A CA  
1485 C  C   . ALA A 188 ? 0.1812 0.1259 0.2317 0.0307  -0.0079 -0.0259 188 ALA A C   
1486 O  O   . ALA A 188 ? 0.1779 0.1961 0.2311 0.0611  -0.0083 -0.0343 188 ALA A O   
1487 C  CB  . ALA A 188 ? 0.2576 0.2176 0.2171 0.0767  -0.0109 -0.0491 188 ALA A CB  
1488 N  N   . GLU A 189 ? 0.1837 0.1139 0.2516 0.0288  -0.0096 -0.0332 189 GLU A N   
1489 C  CA  . GLU A 189 ? 0.1737 0.0758 0.2522 -0.0009 0.0172  -0.0059 189 GLU A CA  
1490 C  C   . GLU A 189 ? 0.1506 0.0967 0.1676 0.0160  -0.0260 -0.0078 189 GLU A C   
1491 O  O   . GLU A 189 ? 0.1822 0.1198 0.1712 0.0206  0.0247  0.0077  189 GLU A O   
1492 C  CB  . GLU A 189 ? 0.2555 0.0586 0.2636 0.0175  0.0402  0.0337  189 GLU A CB  
1493 C  CG  . GLU A 189 ? 0.3143 0.1017 0.3824 0.0414  0.0336  -0.0366 189 GLU A CG  
1494 C  CD  . GLU A 189 ? 0.3847 0.0405 0.4513 0.0534  0.0625  -0.0333 189 GLU A CD  
1495 O  OE1 . GLU A 189 ? 0.4588 0.1036 0.5443 0.0658  0.1116  0.0367  189 GLU A OE1 
1496 O  OE2 . GLU A 189 ? 0.6483 0.0759 0.5164 0.1508  0.0062  -0.0572 189 GLU A OE2 
1497 N  N   . TYR A 190 ? 0.1676 0.0685 0.2019 0.0323  0.0233  0.0179  190 TYR A N   
1498 C  CA  . TYR A 190 ? 0.1430 0.0540 0.1765 -0.0103 0.0077  -0.0105 190 TYR A CA  
1499 C  C   . TYR A 190 ? 0.1094 0.1150 0.1855 -0.0229 0.0044  -0.0294 190 TYR A C   
1500 O  O   . TYR A 190 ? 0.1954 0.0516 0.1804 -0.0104 -0.0023 -0.0013 190 TYR A O   
1501 C  CB  . TYR A 190 ? 0.1585 0.1141 0.1498 -0.0389 0.0234  -0.0212 190 TYR A CB  
1502 C  CG  . TYR A 190 ? 0.1548 0.0952 0.1613 -0.0029 0.0409  -0.0086 190 TYR A CG  
1503 C  CD1 . TYR A 190 ? 0.1573 0.0911 0.1934 0.0287  0.0433  -0.0016 190 TYR A CD1 
1504 C  CD2 . TYR A 190 ? 0.1550 0.1297 0.1699 0.0044  0.0325  -0.0042 190 TYR A CD2 
1505 C  CE1 . TYR A 190 ? 0.1474 0.1198 0.1973 -0.0022 0.0402  -0.0461 190 TYR A CE1 
1506 C  CE2 . TYR A 190 ? 0.1446 0.1410 0.1877 0.0049  0.0395  0.0050  190 TYR A CE2 
1507 C  CZ  . TYR A 190 ? 0.1471 0.1112 0.1858 -0.0006 0.0390  -0.0106 190 TYR A CZ  
1508 O  OH  . TYR A 190 ? 0.1834 0.1277 0.1850 0.0082  0.0458  -0.0239 190 TYR A OH  
1509 N  N   . TYR A 191 ? 0.1200 0.1039 0.1650 0.0151  0.0017  0.0138  191 TYR A N   
1510 C  CA  . TYR A 191 ? 0.1455 0.0714 0.1694 0.0110  0.0189  0.0207  191 TYR A CA  
1511 C  C   . TYR A 191 ? 0.1463 0.0577 0.1481 0.0127  -0.0107 0.0115  191 TYR A C   
1512 O  O   . TYR A 191 ? 0.1513 0.1280 0.1557 0.0147  -0.0104 0.0030  191 TYR A O   
1513 C  CB  . TYR A 191 ? 0.1218 0.0839 0.1715 -0.0122 0.0080  0.0035  191 TYR A CB  
1514 C  CG  . TYR A 191 ? 0.1076 0.1124 0.1886 -0.0084 0.0197  0.0163  191 TYR A CG  
1515 C  CD1 . TYR A 191 ? 0.1282 0.1107 0.1938 -0.0080 -0.0077 0.0086  191 TYR A CD1 
1516 C  CD2 . TYR A 191 ? 0.1682 0.0542 0.1941 0.0210  -0.0072 0.0070  191 TYR A CD2 
1517 C  CE1 . TYR A 191 ? 0.1397 0.1430 0.1933 -0.0160 0.0033  0.0086  191 TYR A CE1 
1518 C  CE2 . TYR A 191 ? 0.1313 0.1169 0.2223 -0.0034 0.0052  -0.0063 191 TYR A CE2 
1519 C  CZ  . TYR A 191 ? 0.1686 0.0807 0.2229 -0.0325 -0.0280 0.0414  191 TYR A CZ  
1520 O  OH  . TYR A 191 ? 0.1733 0.1416 0.2380 -0.0562 0.0209  0.0288  191 TYR A OH  
1521 N  N   . ARG A 192 ? 0.1764 0.1040 0.1355 -0.0002 0.0083  0.0193  192 ARG A N   
1522 C  CA  . ARG A 192 ? 0.1338 0.1221 0.1330 -0.0177 -0.0125 0.0141  192 ARG A CA  
1523 C  C   . ARG A 192 ? 0.1647 0.1600 0.1128 0.0072  -0.0042 -0.0004 192 ARG A C   
1524 O  O   . ARG A 192 ? 0.1826 0.1036 0.1495 0.0154  -0.0439 0.0046  192 ARG A O   
1525 C  CB  . ARG A 192 ? 0.1789 0.0848 0.1650 0.0185  0.0149  0.0219  192 ARG A CB  
1526 C  CG  . ARG A 192 ? 0.1737 0.1470 0.1528 -0.0184 -0.0086 0.0388  192 ARG A CG  
1527 C  CD  . ARG A 192 ? 0.1884 0.1239 0.1931 -0.0111 -0.0129 0.0293  192 ARG A CD  
1528 N  NE  . ARG A 192 ? 0.1471 0.1498 0.1656 -0.0263 0.0100  0.0141  192 ARG A NE  
1529 C  CZ  . ARG A 192 ? 0.1857 0.1302 0.1836 -0.0223 0.0513  0.0021  192 ARG A CZ  
1530 N  NH1 . ARG A 192 ? 0.2069 0.1184 0.1606 -0.0254 0.0130  -0.0212 192 ARG A NH1 
1531 N  NH2 . ARG A 192 ? 0.1772 0.1647 0.2010 -0.0141 0.0334  0.0053  192 ARG A NH2 
1532 N  N   . TYR A 193 ? 0.1372 0.1238 0.1280 0.0277  -0.0164 0.0153  193 TYR A N   
1533 C  CA  . TYR A 193 ? 0.1349 0.1033 0.1650 -0.0195 -0.0130 0.0549  193 TYR A CA  
1534 C  C   . TYR A 193 ? 0.1614 0.1191 0.0811 -0.0296 0.0092  0.0228  193 TYR A C   
1535 O  O   . TYR A 193 ? 0.1542 0.1288 0.1245 0.0119  -0.0237 0.0141  193 TYR A O   
1536 C  CB  . TYR A 193 ? 0.1336 0.1304 0.1492 0.0122  -0.0017 0.0149  193 TYR A CB  
1537 C  CG  . TYR A 193 ? 0.1390 0.1094 0.1582 0.0002  0.0076  0.0115  193 TYR A CG  
1538 C  CD1 . TYR A 193 ? 0.1439 0.0981 0.1596 0.0133  0.0030  0.0066  193 TYR A CD1 
1539 C  CD2 . TYR A 193 ? 0.1476 0.1178 0.1301 0.0245  -0.0145 0.0436  193 TYR A CD2 
1540 C  CE1 . TYR A 193 ? 0.1266 0.0861 0.1595 0.0277  0.0086  0.0094  193 TYR A CE1 
1541 C  CE2 . TYR A 193 ? 0.1399 0.0936 0.1207 -0.0034 -0.0013 0.0575  193 TYR A CE2 
1542 C  CZ  . TYR A 193 ? 0.1491 0.0568 0.1083 0.0054  -0.0242 0.0309  193 TYR A CZ  
1543 O  OH  . TYR A 193 ? 0.1453 0.1098 0.1223 0.0153  -0.0073 0.0261  193 TYR A OH  
1544 N  N   . ARG A 194 ? 0.1825 0.1035 0.1478 0.0072  0.0166  0.0319  194 ARG A N   
1545 C  CA  . ARG A 194 ? 0.1255 0.0954 0.1101 0.0110  0.0015  0.0351  194 ARG A CA  
1546 C  C   . ARG A 194 ? 0.1561 0.0791 0.1085 0.0266  0.0029  0.0509  194 ARG A C   
1547 O  O   . ARG A 194 ? 0.1635 0.1204 0.1509 0.0222  -0.0226 0.0183  194 ARG A O   
1548 C  CB  . ARG A 194 ? 0.2109 0.1467 0.1308 0.0107  0.0682  0.0511  194 ARG A CB  
1549 C  CG  . ARG A 194 ? 0.2064 0.3141 0.1604 0.0341  0.0648  0.0336  194 ARG A CG  
1550 C  CD  . ARG A 194 ? 0.3728 0.4322 0.2594 -0.0102 0.1421  0.1125  194 ARG A CD  
1551 N  NE  . ARG A 194 ? 0.4996 0.6713 0.4093 0.0710  0.1873  0.0190  194 ARG A NE  
1552 C  CZ  . ARG A 194 ? 0.4680 0.7885 0.4762 0.1082  0.1038  0.0140  194 ARG A CZ  
1553 N  NH1 . ARG A 194 ? 0.6416 0.8310 0.2349 -0.0190 -0.0524 0.1540  194 ARG A NH1 
1554 N  NH2 . ARG A 194 ? 0.5215 0.8989 0.5881 0.1062  0.2717  0.0621  194 ARG A NH2 
1555 N  N   . GLY A 195 ? 0.1574 0.1250 0.1216 0.0328  0.0027  0.0162  195 GLY A N   
1556 C  CA  . GLY A 195 ? 0.1254 0.1435 0.1282 0.0258  -0.0204 -0.0098 195 GLY A CA  
1557 C  C   . GLY A 195 ? 0.1087 0.0814 0.1446 0.0262  0.0201  0.0149  195 GLY A C   
1558 O  O   . GLY A 195 ? 0.1412 0.1076 0.1689 0.0188  0.0122  0.0706  195 GLY A O   
1559 N  N   . SER A 196 ? 0.1287 0.0697 0.1288 0.0201  -0.0050 0.0160  196 SER A N   
1560 C  CA  . SER A 196 ? 0.0976 0.0703 0.1516 0.0126  -0.0268 0.0143  196 SER A CA  
1561 C  C   . SER A 196 ? 0.0787 0.0629 0.1505 0.0089  -0.0260 0.0379  196 SER A C   
1562 O  O   . SER A 196 ? 0.1560 0.0563 0.1333 0.0292  -0.0034 0.0285  196 SER A O   
1563 C  CB  . SER A 196 ? 0.1053 0.0767 0.1920 0.0179  -0.0322 0.0545  196 SER A CB  
1564 O  OG  . SER A 196 ? 0.1216 0.0782 0.1733 0.0238  -0.0108 0.0277  196 SER A OG  
1565 N  N   . LEU A 197 ? 0.0920 0.1112 0.1220 0.0145  -0.0218 0.0066  197 LEU A N   
1566 C  CA  . LEU A 197 ? 0.1506 0.0629 0.1327 -0.0064 -0.0024 0.0310  197 LEU A CA  
1567 C  C   . LEU A 197 ? 0.1270 0.0640 0.1593 0.0116  -0.0141 0.0331  197 LEU A C   
1568 O  O   . LEU A 197 ? 0.1470 0.0559 0.1466 0.0150  -0.0251 0.0256  197 LEU A O   
1569 C  CB  . LEU A 197 ? 0.1311 0.0669 0.2188 -0.0423 0.0186  0.0273  197 LEU A CB  
1570 C  CG  . LEU A 197 ? 0.1485 0.0845 0.2728 -0.0453 -0.0471 0.0458  197 LEU A CG  
1571 C  CD1 . LEU A 197 ? 0.1455 0.2130 0.3335 -0.0281 0.0501  0.0223  197 LEU A CD1 
1572 C  CD2 . LEU A 197 ? 0.1690 0.1541 0.2624 -0.0452 -0.0664 0.0088  197 LEU A CD2 
1573 N  N   . THR A 198 ? 0.1284 0.0706 0.1398 0.0017  -0.0195 0.0244  198 THR A N   
1574 C  CA  . THR A 198 ? 0.1273 0.0196 0.1654 -0.0098 -0.0210 0.0407  198 THR A CA  
1575 C  C   . THR A 198 ? 0.1121 0.0737 0.1872 -0.0031 -0.0383 0.0205  198 THR A C   
1576 O  O   . THR A 198 ? 0.1305 0.0524 0.2013 -0.0063 -0.0179 0.0252  198 THR A O   
1577 C  CB  . THR A 198 ? 0.1448 0.0120 0.1431 -0.0218 -0.0416 0.0231  198 THR A CB  
1578 O  OG1 . THR A 198 ? 0.1345 0.0613 0.1437 0.0084  -0.0489 0.0099  198 THR A OG1 
1579 C  CG2 . THR A 198 ? 0.1636 0.0540 0.1499 -0.0095 -0.0194 -0.0006 198 THR A CG2 
1580 N  N   . THR A 199 ? 0.1421 0.0207 0.1491 -0.0069 -0.0194 0.0176  199 THR A N   
1581 C  CA  . THR A 199 ? 0.1403 0.0236 0.1900 0.0023  -0.0477 -0.0016 199 THR A CA  
1582 C  C   . THR A 199 ? 0.1284 0.0686 0.1943 -0.0192 -0.0234 0.0290  199 THR A C   
1583 O  O   . THR A 199 ? 0.1239 0.0970 0.1877 0.0061  -0.0378 0.0175  199 THR A O   
1584 C  CB  . THR A 199 ? 0.1309 0.0245 0.1861 -0.0005 -0.0397 0.0533  199 THR A CB  
1585 O  OG1 . THR A 199 ? 0.1362 0.0958 0.2353 -0.0190 -0.0257 0.0369  199 THR A OG1 
1586 C  CG2 . THR A 199 ? 0.2267 0.0226 0.1970 0.0072  -0.0707 0.0495  199 THR A CG2 
1587 N  N   . PRO A 200 ? 0.1740 0.0553 0.1561 -0.0223 -0.0498 0.0324  200 PRO A N   
1588 C  CA  . PRO A 200 ? 0.1295 0.0578 0.1466 -0.0289 -0.0573 0.0326  200 PRO A CA  
1589 C  C   . PRO A 200 ? 0.1550 0.0766 0.2232 0.0174  -0.0376 0.0179  200 PRO A C   
1590 O  O   . PRO A 200 ? 0.1597 0.0914 0.2180 -0.0206 -0.0542 0.0251  200 PRO A O   
1591 C  CB  . PRO A 200 ? 0.1692 0.1089 0.1643 -0.0255 -0.0281 0.0206  200 PRO A CB  
1592 C  CG  . PRO A 200 ? 0.1736 0.0107 0.2054 -0.0130 -0.0331 0.0282  200 PRO A CG  
1593 C  CD  . PRO A 200 ? 0.1814 0.0232 0.2174 0.0273  -0.0217 0.0141  200 PRO A CD  
1594 N  N   . PRO A 201 ? 0.1279 0.0649 0.2309 -0.0107 -0.0410 0.0256  201 PRO A N   
1595 C  CA  . PRO A 201 ? 0.1628 0.0547 0.2399 -0.0352 -0.0559 0.0326  201 PRO A CA  
1596 C  C   . PRO A 201 ? 0.1358 0.0265 0.2020 -0.0204 -0.0326 0.0281  201 PRO A C   
1597 O  O   . PRO A 201 ? 0.1653 0.1017 0.2094 -0.0093 -0.0310 0.0376  201 PRO A O   
1598 C  CB  . PRO A 201 ? 0.1191 0.0559 0.3009 -0.0428 -0.0662 0.0089  201 PRO A CB  
1599 C  CG  . PRO A 201 ? 0.2106 0.1280 0.2321 -0.0111 -0.0886 0.0589  201 PRO A CG  
1600 C  CD  . PRO A 201 ? 0.1514 0.0461 0.3335 -0.0567 -0.0379 -0.0110 201 PRO A CD  
1601 N  N   . CYS A 202 ? 0.1505 0.0241 0.1927 -0.0217 -0.0218 0.0084  202 CYS A N   
1602 C  CA  . CYS A 202 ? 0.1227 0.0742 0.1811 -0.0038 -0.0190 -0.0098 202 CYS A CA  
1603 C  C   . CYS A 202 ? 0.0927 0.1049 0.1854 0.0166  -0.0080 0.0216  202 CYS A C   
1604 O  O   . CYS A 202 ? 0.1262 0.0346 0.1947 0.0159  -0.0293 0.0353  202 CYS A O   
1605 C  CB  . CYS A 202 ? 0.1295 0.0787 0.1686 0.0181  -0.0121 -0.0258 202 CYS A CB  
1606 S  SG  . CYS A 202 ? 0.1441 0.0335 0.1947 -0.0003 -0.0158 0.0170  202 CYS A SG  
1607 N  N   . ASN A 203 ? 0.1094 0.0708 0.2131 0.0131  -0.0027 0.0159  203 ASN A N   
1608 C  CA  . ASN A 203 ? 0.1327 0.0850 0.2291 -0.0074 0.0088  0.0165  203 ASN A CA  
1609 C  C   . ASN A 203 ? 0.1643 0.0758 0.1485 0.0203  0.0245  0.0386  203 ASN A C   
1610 O  O   . ASN A 203 ? 0.1557 0.0740 0.1661 0.0022  -0.0115 0.0381  203 ASN A O   
1611 C  CB  . ASN A 203 ? 0.1807 0.1518 0.3112 -0.1038 -0.0116 -0.0158 203 ASN A CB  
1612 C  CG  . ASN A 203 ? 0.1681 0.0842 0.3711 -0.0834 -0.0292 0.0154  203 ASN A CG  
1613 O  OD1 . ASN A 203 ? 0.2098 0.1791 0.3942 0.0041  -0.0413 -0.0414 203 ASN A OD1 
1614 N  ND2 . ASN A 203 ? 0.1847 0.1446 0.4056 -0.0147 -0.0117 0.0878  203 ASN A ND2 
1615 N  N   . PRO A 204 ? 0.1564 0.1045 0.1869 0.0612  -0.0259 0.0536  204 PRO A N   
1616 C  CA  . PRO A 204 ? 0.1459 0.1076 0.1654 0.0110  0.0029  0.0497  204 PRO A CA  
1617 C  C   . PRO A 204 ? 0.1606 0.0932 0.1987 0.0197  0.0104  0.0489  204 PRO A C   
1618 O  O   . PRO A 204 ? 0.1947 0.2071 0.1865 0.0636  -0.0016 0.0507  204 PRO A O   
1619 C  CB  . PRO A 204 ? 0.1713 0.0868 0.2624 0.0639  -0.0296 0.0463  204 PRO A CB  
1620 C  CG  . PRO A 204 ? 0.1586 0.1002 0.2026 0.0396  -0.0321 0.0457  204 PRO A CG  
1621 C  CD  . PRO A 204 ? 0.2063 0.0442 0.2084 0.0331  -0.0260 0.0321  204 PRO A CD  
1622 N  N   . THR A 205 ? 0.1227 0.0895 0.2245 0.0150  0.0084  0.0431  205 THR A N   
1623 C  CA  . THR A 205 ? 0.1286 0.1315 0.2309 0.0359  0.0013  0.0369  205 THR A CA  
1624 C  C   . THR A 205 ? 0.1193 0.1090 0.2177 -0.0048 -0.0229 0.0443  205 THR A C   
1625 O  O   . THR A 205 ? 0.1331 0.0965 0.2069 0.0144  -0.0006 0.0314  205 THR A O   
1626 C  CB  . THR A 205 ? 0.1690 0.0737 0.2515 0.0410  0.0165  0.0556  205 THR A CB  
1627 O  OG1 . THR A 205 ? 0.1872 0.0803 0.2737 0.0051  0.0413  0.0344  205 THR A OG1 
1628 C  CG2 . THR A 205 ? 0.1495 0.0708 0.2865 0.0111  0.0353  0.0864  205 THR A CG2 
1629 N  N   . VAL A 206 ? 0.1374 0.1248 0.1859 0.0268  0.0220  0.0688  206 VAL A N   
1630 C  CA  . VAL A 206 ? 0.1160 0.1017 0.1676 -0.0021 -0.0239 0.0458  206 VAL A CA  
1631 C  C   . VAL A 206 ? 0.1502 0.1502 0.1352 0.0192  0.0223  0.0255  206 VAL A C   
1632 O  O   . VAL A 206 ? 0.1675 0.0911 0.2010 0.0083  -0.0184 0.0607  206 VAL A O   
1633 C  CB  . VAL A 206 ? 0.1505 0.0638 0.1801 0.0068  0.0218  0.0612  206 VAL A CB  
1634 C  CG1 . VAL A 206 ? 0.1416 0.1062 0.1625 0.0267  -0.0185 0.0788  206 VAL A CG1 
1635 C  CG2 . VAL A 206 ? 0.1115 0.1130 0.2121 0.0468  -0.0054 0.0222  206 VAL A CG2 
1636 N  N   . LEU A 207 ? 0.1184 0.0934 0.1596 0.0068  -0.0043 0.0502  207 LEU A N   
1637 C  CA  . LEU A 207 ? 0.1749 0.1015 0.1808 -0.0052 0.0050  0.0368  207 LEU A CA  
1638 C  C   . LEU A 207 ? 0.1502 0.1409 0.1182 -0.0226 -0.0073 0.0139  207 LEU A C   
1639 O  O   . LEU A 207 ? 0.1223 0.1097 0.1521 0.0143  -0.0075 0.0234  207 LEU A O   
1640 C  CB  . LEU A 207 ? 0.1513 0.1266 0.2092 -0.0011 -0.0154 0.0336  207 LEU A CB  
1641 C  CG  . LEU A 207 ? 0.2496 0.1843 0.2399 0.0545  -0.0331 -0.0252 207 LEU A CG  
1642 C  CD1 . LEU A 207 ? 0.2590 0.1739 0.2755 -0.0038 -0.0544 0.0022  207 LEU A CD1 
1643 C  CD2 . LEU A 207 ? 0.2508 0.3708 0.3824 0.0372  0.0268  -0.0381 207 LEU A CD2 
1644 N  N   . TRP A 208 ? 0.1298 0.0866 0.1482 0.0170  0.0276  0.0208  208 TRP A N   
1645 C  CA  . TRP A 208 ? 0.1096 0.1146 0.1372 0.0225  0.0195  0.0297  208 TRP A CA  
1646 C  C   . TRP A 208 ? 0.1306 0.1248 0.1141 0.0242  -0.0036 0.0239  208 TRP A C   
1647 O  O   . TRP A 208 ? 0.1683 0.0900 0.1300 0.0312  -0.0205 0.0230  208 TRP A O   
1648 C  CB  . TRP A 208 ? 0.1047 0.0830 0.1462 0.0037  0.0143  0.0152  208 TRP A CB  
1649 C  CG  . TRP A 208 ? 0.0977 0.0726 0.1416 0.0421  -0.0190 0.0303  208 TRP A CG  
1650 C  CD1 . TRP A 208 ? 0.1496 0.0598 0.1570 0.0172  0.0013  0.0594  208 TRP A CD1 
1651 C  CD2 . TRP A 208 ? 0.1264 0.0848 0.1338 0.0134  0.0095  0.0342  208 TRP A CD2 
1652 N  NE1 . TRP A 208 ? 0.1527 0.1381 0.1344 0.0245  -0.0140 0.0342  208 TRP A NE1 
1653 C  CE2 . TRP A 208 ? 0.1180 0.0670 0.1385 -0.0077 -0.0302 0.0228  208 TRP A CE2 
1654 C  CE3 . TRP A 208 ? 0.1053 0.1090 0.1119 0.0033  -0.0147 0.0199  208 TRP A CE3 
1655 C  CZ2 . TRP A 208 ? 0.1233 0.1101 0.1352 0.0013  -0.0154 0.0317  208 TRP A CZ2 
1656 C  CZ3 . TRP A 208 ? 0.1189 0.0902 0.1265 0.0355  0.0011  -0.0086 208 TRP A CZ3 
1657 C  CH2 . TRP A 208 ? 0.1119 0.0695 0.1367 0.0138  -0.0307 0.0013  208 TRP A CH2 
1658 N  N   . THR A 209 ? 0.1233 0.0362 0.1276 -0.0075 -0.0062 0.0366  209 THR A N   
1659 C  CA  . THR A 209 ? 0.1180 0.0387 0.1334 -0.0002 0.0058  0.0364  209 THR A CA  
1660 C  C   . THR A 209 ? 0.1251 0.0738 0.1227 -0.0060 -0.0083 0.0447  209 THR A C   
1661 O  O   . THR A 209 ? 0.1269 0.1088 0.1320 0.0001  -0.0138 0.0296  209 THR A O   
1662 C  CB  . THR A 209 ? 0.1218 0.0647 0.1252 0.0064  -0.0059 0.0147  209 THR A CB  
1663 O  OG1 . THR A 209 ? 0.1352 0.1341 0.1379 0.0154  0.0120  0.0319  209 THR A OG1 
1664 C  CG2 . THR A 209 ? 0.1807 0.0722 0.2009 0.0389  -0.0210 0.0317  209 THR A CG2 
1665 N  N   . VAL A 210 ? 0.1125 0.0863 0.1604 -0.0089 0.0198  0.0346  210 VAL A N   
1666 C  CA  . VAL A 210 ? 0.0875 0.0731 0.1530 0.0121  0.0052  0.0491  210 VAL A CA  
1667 C  C   . VAL A 210 ? 0.1362 0.0791 0.1596 0.0186  -0.0094 0.0216  210 VAL A C   
1668 O  O   . VAL A 210 ? 0.1527 0.0990 0.1525 -0.0064 -0.0226 0.0420  210 VAL A O   
1669 C  CB  . VAL A 210 ? 0.1001 0.0489 0.1728 0.0313  0.0143  0.0367  210 VAL A CB  
1670 C  CG1 . VAL A 210 ? 0.1385 0.1191 0.1456 0.0307  0.0223  0.0250  210 VAL A CG1 
1671 C  CG2 . VAL A 210 ? 0.1148 0.0507 0.1810 0.0453  -0.0215 0.0130  210 VAL A CG2 
1672 N  N   . PHE A 211 ? 0.1209 0.0868 0.1518 0.0222  -0.0021 0.0288  211 PHE A N   
1673 C  CA  . PHE A 211 ? 0.1391 0.0884 0.1895 0.0244  -0.0173 0.0051  211 PHE A CA  
1674 C  C   . PHE A 211 ? 0.1342 0.0320 0.1628 0.0318  -0.0095 -0.0016 211 PHE A C   
1675 O  O   . PHE A 211 ? 0.1645 0.0681 0.1877 0.0304  0.0044  0.0133  211 PHE A O   
1676 C  CB  . PHE A 211 ? 0.1640 0.0458 0.1909 0.0196  -0.0356 -0.0072 211 PHE A CB  
1677 C  CG  . PHE A 211 ? 0.1460 0.0817 0.1900 0.0099  -0.0417 0.0021  211 PHE A CG  
1678 C  CD1 . PHE A 211 ? 0.1582 0.0835 0.2078 0.0063  -0.0227 0.0354  211 PHE A CD1 
1679 C  CD2 . PHE A 211 ? 0.1420 0.0671 0.1887 -0.0331 -0.0280 0.0245  211 PHE A CD2 
1680 C  CE1 . PHE A 211 ? 0.1509 0.1719 0.2134 -0.0004 -0.0059 0.0467  211 PHE A CE1 
1681 C  CE2 . PHE A 211 ? 0.1270 0.0842 0.1879 -0.0075 -0.0332 0.0641  211 PHE A CE2 
1682 C  CZ  . PHE A 211 ? 0.1259 0.1369 0.2260 -0.0132 0.0013  0.0699  211 PHE A CZ  
1683 N  N   . ARG A 212 ? 0.1764 0.0523 0.1782 0.0072  -0.0093 -0.0244 212 ARG A N   
1684 C  CA  . ARG A 212 ? 0.1366 0.0832 0.1597 0.0195  -0.0244 -0.0016 212 ARG A CA  
1685 C  C   . ARG A 212 ? 0.1858 0.0943 0.1818 -0.0211 0.0001  0.0107  212 ARG A C   
1686 O  O   . ARG A 212 ? 0.2135 0.0353 0.2405 -0.0087 0.0119  0.0321  212 ARG A O   
1687 C  CB  . ARG A 212 ? 0.2435 0.0765 0.1779 -0.0789 0.0176  -0.0269 212 ARG A CB  
1688 C  CG  . ARG A 212 ? 0.2115 0.1186 0.2038 -0.0745 0.0310  -0.0189 212 ARG A CG  
1689 C  CD  . ARG A 212 ? 0.2960 0.2017 0.3022 -0.0501 0.0328  -0.1141 212 ARG A CD  
1690 N  NE  . ARG A 212 ? 0.3342 0.2163 0.3481 -0.1015 0.0328  -0.0991 212 ARG A NE  
1691 C  CZ  . ARG A 212 ? 0.4828 0.1754 0.3959 -0.0985 0.0935  -0.0831 212 ARG A CZ  
1692 N  NH1 . ARG A 212 ? 0.4192 0.2532 0.5246 -0.0355 0.0763  0.0345  212 ARG A NH1 
1693 N  NH2 . ARG A 212 ? 0.5581 0.2511 0.5989 -0.1769 0.0447  -0.1503 212 ARG A NH2 
1694 N  N   . ASN A 213 ? 0.2081 0.0705 0.1879 -0.0115 -0.0066 0.0354  213 ASN A N   
1695 C  CA  . ASN A 213 ? 0.2410 0.0916 0.1776 0.0464  0.0041  0.0283  213 ASN A CA  
1696 C  C   . ASN A 213 ? 0.1539 0.1121 0.1791 0.0347  -0.0103 0.0248  213 ASN A C   
1697 O  O   . ASN A 213 ? 0.1941 0.0837 0.2053 0.0245  -0.0029 0.0544  213 ASN A O   
1698 C  CB  . ASN A 213 ? 0.2185 0.1381 0.2196 0.0633  -0.0038 0.0440  213 ASN A CB  
1699 C  CG  . ASN A 213 ? 0.2763 0.1550 0.2454 0.0152  0.0345  0.0244  213 ASN A CG  
1700 O  OD1 . ASN A 213 ? 0.2945 0.1643 0.3810 -0.0097 0.0947  -0.0166 213 ASN A OD1 
1701 N  ND2 . ASN A 213 ? 0.2766 0.0810 0.2904 0.0407  0.0384  -0.0161 213 ASN A ND2 
1702 N  N   . PRO A 214 ? 0.1948 0.0758 0.1761 -0.0094 -0.0096 0.0168  214 PRO A N   
1703 C  CA  . PRO A 214 ? 0.1768 0.1635 0.1288 0.0257  -0.0089 0.0239  214 PRO A CA  
1704 C  C   . PRO A 214 ? 0.1780 0.0668 0.1764 0.0443  -0.0067 0.0318  214 PRO A C   
1705 O  O   . PRO A 214 ? 0.2297 0.0881 0.2166 0.0661  0.0030  0.0058  214 PRO A O   
1706 C  CB  . PRO A 214 ? 0.1972 0.0406 0.2394 -0.0019 0.0117  0.0571  214 PRO A CB  
1707 C  CG  . PRO A 214 ? 0.2506 0.0706 0.2429 -0.0526 0.0403  0.0350  214 PRO A CG  
1708 C  CD  . PRO A 214 ? 0.1668 0.1462 0.2494 -0.0203 0.0215  0.0062  214 PRO A CD  
1709 N  N   . VAL A 215 ? 0.1462 0.1284 0.1449 0.0193  0.0012  0.0336  215 VAL A N   
1710 C  CA  . VAL A 215 ? 0.1833 0.1247 0.1399 0.0381  -0.0005 0.0300  215 VAL A CA  
1711 C  C   . VAL A 215 ? 0.1908 0.1449 0.1701 0.0486  0.0159  0.0575  215 VAL A C   
1712 O  O   . VAL A 215 ? 0.1819 0.1523 0.1638 0.0502  0.0249  0.0450  215 VAL A O   
1713 C  CB  . VAL A 215 ? 0.2097 0.0766 0.1690 0.0247  0.0053  0.0482  215 VAL A CB  
1714 C  CG1 . VAL A 215 ? 0.1816 0.1441 0.2015 0.0422  0.0178  0.0231  215 VAL A CG1 
1715 C  CG2 . VAL A 215 ? 0.1848 0.0952 0.1764 0.0328  -0.0068 0.0247  215 VAL A CG2 
1716 N  N   . GLN A 216 ? 0.2157 0.1595 0.1760 0.0315  0.0392  0.0954  216 GLN A N   
1717 C  CA  . GLN A 216 ? 0.1938 0.1597 0.1527 0.0383  0.0141  0.0829  216 GLN A CA  
1718 C  C   . GLN A 216 ? 0.1986 0.1907 0.1844 0.0217  0.0242  0.0675  216 GLN A C   
1719 O  O   . GLN A 216 ? 0.1785 0.2064 0.2127 0.0534  0.0207  0.0763  216 GLN A O   
1720 C  CB  . GLN A 216 ? 0.2196 0.1747 0.2077 0.0219  0.0097  0.0926  216 GLN A CB  
1721 C  CG  . GLN A 216 ? 0.2326 0.0714 0.2301 0.0385  0.0043  0.0727  216 GLN A CG  
1722 C  CD  . GLN A 216 ? 0.2748 0.1130 0.3104 -0.0168 -0.0004 0.0881  216 GLN A CD  
1723 O  OE1 . GLN A 216 ? 0.2828 0.1399 0.2815 0.0179  0.0262  0.0488  216 GLN A OE1 
1724 N  NE2 . GLN A 216 ? 0.3730 0.2782 0.3285 -0.0308 -0.0166 0.0207  216 GLN A NE2 
1725 N  N   . ILE A 217 ? 0.2240 0.1518 0.2002 0.0530  0.0414  0.0721  217 ILE A N   
1726 C  CA  . ILE A 217 ? 0.2339 0.1240 0.1865 0.0836  0.0381  0.0732  217 ILE A CA  
1727 C  C   . ILE A 217 ? 0.2538 0.1861 0.1848 0.0435  0.0348  0.0526  217 ILE A C   
1728 O  O   . ILE A 217 ? 0.2491 0.1252 0.2342 0.0441  0.0149  0.0861  217 ILE A O   
1729 C  CB  . ILE A 217 ? 0.2035 0.1284 0.1771 0.0710  0.0390  0.0647  217 ILE A CB  
1730 C  CG1 . ILE A 217 ? 0.2232 0.0884 0.2404 0.0892  0.0369  0.0539  217 ILE A CG1 
1731 C  CG2 . ILE A 217 ? 0.1642 0.1821 0.2076 0.0232  -0.0012 0.0886  217 ILE A CG2 
1732 C  CD1 . ILE A 217 ? 0.1841 0.1013 0.1537 0.0554  0.0141  0.0290  217 ILE A CD1 
1733 N  N   . SER A 218 ? 0.2218 0.2010 0.1640 0.0575  0.0468  0.0705  218 SER A N   
1734 C  CA  . SER A 218 ? 0.1852 0.2138 0.1898 0.0480  0.0331  0.0932  218 SER A CA  
1735 C  C   . SER A 218 ? 0.2078 0.2289 0.1865 0.0479  0.0559  0.0592  218 SER A C   
1736 O  O   . SER A 218 ? 0.1981 0.2300 0.1739 0.0326  0.0197  0.0846  218 SER A O   
1737 C  CB  . SER A 218 ? 0.3009 0.1920 0.1801 0.0929  0.0218  0.0990  218 SER A CB  
1738 O  OG  . SER A 218 ? 0.2537 0.1779 0.2105 0.0693  0.0597  0.0806  218 SER A OG  
1739 N  N   . GLN A 219 ? 0.2073 0.2035 0.2105 0.0407  0.0615  0.0496  219 GLN A N   
1740 C  CA  . GLN A 219 ? 0.2028 0.2552 0.1888 0.0548  0.0507  0.0447  219 GLN A CA  
1741 C  C   . GLN A 219 ? 0.2120 0.2123 0.2351 0.0644  0.0535  0.0686  219 GLN A C   
1742 O  O   . GLN A 219 ? 0.2433 0.1574 0.2239 0.0179  0.0218  0.0769  219 GLN A O   
1743 C  CB  . GLN A 219 ? 0.2820 0.2222 0.2922 0.0315  0.1010  0.0476  219 GLN A CB  
1744 C  CG  . GLN A 219 ? 0.3905 0.3498 0.2549 0.0205  0.0703  0.0484  219 GLN A CG  
1745 C  CD  . GLN A 219 ? 0.5175 0.1205 0.4097 0.0414  0.1919  0.0604  219 GLN A CD  
1746 O  OE1 . GLN A 219 ? 0.7278 0.3296 0.7823 -0.1578 0.1690  -0.1667 219 GLN A OE1 
1747 N  NE2 . GLN A 219 ? 0.6759 0.3428 0.6306 0.2483  0.1280  -0.1292 219 GLN A NE2 
1748 N  N   . GLU A 220 ? 0.2260 0.1370 0.2041 0.0419  0.0299  0.0813  220 GLU A N   
1749 C  CA  . GLU A 220 ? 0.2272 0.2664 0.1410 0.0297  0.0375  0.0771  220 GLU A CA  
1750 C  C   . GLU A 220 ? 0.2632 0.2524 0.1144 0.0314  0.0274  0.0726  220 GLU A C   
1751 O  O   . GLU A 220 ? 0.1882 0.2529 0.1622 0.0392  -0.0178 -0.0022 220 GLU A O   
1752 C  CB  . GLU A 220 ? 0.2938 0.3199 0.2060 0.1037  0.0510  0.1476  220 GLU A CB  
1753 C  CG  . GLU A 220 ? 0.3182 0.2401 0.2825 0.0551  0.0739  0.0862  220 GLU A CG  
1754 C  CD  . GLU A 220 ? 0.4264 0.2372 0.3026 0.0395  0.0468  0.1239  220 GLU A CD  
1755 O  OE1 . GLU A 220 ? 0.4513 0.2218 0.2832 0.1018  0.0296  0.1288  220 GLU A OE1 
1756 O  OE2 . GLU A 220 ? 0.4934 0.3251 0.3685 0.0938  0.1357  0.1932  220 GLU A OE2 
1757 N  N   . GLN A 221 ? 0.2358 0.2639 0.1038 0.0078  0.0272  0.0784  221 GLN A N   
1758 C  CA  . GLN A 221 ? 0.1722 0.2085 0.1288 0.0253  -0.0013 0.0559  221 GLN A CA  
1759 C  C   . GLN A 221 ? 0.1834 0.2117 0.1528 0.0218  -0.0113 0.0756  221 GLN A C   
1760 O  O   . GLN A 221 ? 0.1814 0.2157 0.1474 0.0035  -0.0018 0.0850  221 GLN A O   
1761 C  CB  . GLN A 221 ? 0.1905 0.2306 0.1311 0.0546  0.0262  0.0728  221 GLN A CB  
1762 C  CG  . GLN A 221 ? 0.1970 0.2901 0.1797 0.0653  0.0134  0.0756  221 GLN A CG  
1763 C  CD  . GLN A 221 ? 0.1945 0.1952 0.1596 0.0274  0.0080  0.0715  221 GLN A CD  
1764 O  OE1 . GLN A 221 ? 0.2235 0.2019 0.1879 0.0460  -0.0052 0.0813  221 GLN A OE1 
1765 N  NE2 . GLN A 221 ? 0.1828 0.2755 0.1937 0.0494  0.0111  0.0892  221 GLN A NE2 
1766 N  N   . LEU A 222 ? 0.1959 0.2928 0.1031 0.0172  -0.0199 0.0653  222 LEU A N   
1767 C  CA  . LEU A 222 ? 0.2171 0.2257 0.1227 0.0068  -0.0351 0.0505  222 LEU A CA  
1768 C  C   . LEU A 222 ? 0.2368 0.2444 0.1527 0.0233  -0.0184 0.0646  222 LEU A C   
1769 O  O   . LEU A 222 ? 0.1699 0.2406 0.1338 0.0122  -0.0225 0.0820  222 LEU A O   
1770 C  CB  . LEU A 222 ? 0.2070 0.2561 0.1385 -0.0129 -0.0424 0.0722  222 LEU A CB  
1771 C  CG  . LEU A 222 ? 0.1902 0.1808 0.1518 0.0066  -0.0265 0.0122  222 LEU A CG  
1772 C  CD1 . LEU A 222 ? 0.2272 0.1782 0.1489 0.0143  -0.0177 0.0369  222 LEU A CD1 
1773 C  CD2 . LEU A 222 ? 0.1850 0.2435 0.2207 -0.0212 -0.0033 -0.0472 222 LEU A CD2 
1774 N  N   . LEU A 223 ? 0.2028 0.1715 0.1668 0.0190  -0.0065 0.0560  223 LEU A N   
1775 C  CA  . LEU A 223 ? 0.1877 0.2263 0.1550 -0.0138 0.0137  0.0553  223 LEU A CA  
1776 C  C   . LEU A 223 ? 0.2066 0.1897 0.1679 0.0110  0.0001  0.0537  223 LEU A C   
1777 O  O   . LEU A 223 ? 0.2507 0.1514 0.1485 -0.0187 -0.0174 0.0389  223 LEU A O   
1778 C  CB  . LEU A 223 ? 0.2623 0.2310 0.1658 0.0144  0.0428  0.0675  223 LEU A CB  
1779 C  CG  . LEU A 223 ? 0.2005 0.2304 0.2005 -0.0260 0.0389  0.0491  223 LEU A CG  
1780 C  CD1 . LEU A 223 ? 0.2035 0.3464 0.2376 0.0464  0.0960  0.0705  223 LEU A CD1 
1781 C  CD2 . LEU A 223 ? 0.3139 0.3319 0.1841 -0.0192 0.0913  0.0729  223 LEU A CD2 
1782 N  N   . ALA A 224 ? 0.1947 0.1611 0.1761 0.0124  -0.0085 0.0554  224 ALA A N   
1783 C  CA  . ALA A 224 ? 0.2171 0.2259 0.1381 -0.0121 -0.0203 0.0552  224 ALA A CA  
1784 C  C   . ALA A 224 ? 0.2550 0.2496 0.1397 0.0127  -0.0147 0.0664  224 ALA A C   
1785 O  O   . ALA A 224 ? 0.1735 0.2149 0.2076 0.0236  -0.0318 0.0380  224 ALA A O   
1786 C  CB  . ALA A 224 ? 0.1886 0.2801 0.2095 -0.0413 -0.0583 0.0913  224 ALA A CB  
1787 N  N   . LEU A 225 ? 0.1760 0.2876 0.1090 -0.0134 -0.0026 0.0841  225 LEU A N   
1788 C  CA  . LEU A 225 ? 0.1668 0.2080 0.1517 0.0194  0.0043  0.0683  225 LEU A CA  
1789 C  C   . LEU A 225 ? 0.1843 0.1854 0.2114 0.0232  0.0053  0.0625  225 LEU A C   
1790 O  O   . LEU A 225 ? 0.2689 0.1722 0.1834 0.0054  -0.0390 0.0524  225 LEU A O   
1791 C  CB  . LEU A 225 ? 0.2260 0.2655 0.1026 0.0279  -0.0115 0.0772  225 LEU A CB  
1792 C  CG  . LEU A 225 ? 0.1791 0.1757 0.1747 -0.0111 -0.0098 0.0812  225 LEU A CG  
1793 C  CD1 . LEU A 225 ? 0.2329 0.2015 0.2353 -0.0624 -0.0194 0.0895  225 LEU A CD1 
1794 C  CD2 . LEU A 225 ? 0.2231 0.2743 0.1355 0.0270  -0.0200 0.0795  225 LEU A CD2 
1795 N  N   . GLU A 226 ? 0.1288 0.2753 0.1204 0.0266  -0.0051 0.0454  226 GLU A N   
1796 C  CA  . GLU A 226 ? 0.1805 0.2430 0.1758 0.0553  -0.0010 0.0359  226 GLU A CA  
1797 C  C   . GLU A 226 ? 0.1801 0.2883 0.1999 0.0536  -0.0313 0.0096  226 GLU A C   
1798 O  O   . GLU A 226 ? 0.2299 0.2907 0.2352 0.0789  -0.0423 0.0310  226 GLU A O   
1799 C  CB  . GLU A 226 ? 0.1575 0.2661 0.1589 0.0639  0.0170  0.0124  226 GLU A CB  
1800 C  CG  . GLU A 226 ? 0.1708 0.1448 0.1503 0.0176  0.0212  0.0414  226 GLU A CG  
1801 C  CD  . GLU A 226 ? 0.2182 0.1341 0.1215 0.0210  0.0352  0.0173  226 GLU A CD  
1802 O  OE1 . GLU A 226 ? 0.2614 0.2132 0.1057 -0.0047 0.0175  0.0232  226 GLU A OE1 
1803 O  OE2 . GLU A 226 ? 0.2234 0.1693 0.1222 0.0093  0.0108  0.0380  226 GLU A OE2 
1804 N  N   . THR A 227 ? 0.1733 0.2666 0.1743 0.0083  -0.0161 0.0252  227 THR A N   
1805 C  CA  . THR A 227 ? 0.2437 0.2691 0.1625 -0.0142 -0.0155 0.0377  227 THR A CA  
1806 C  C   . THR A 227 ? 0.2628 0.2771 0.2108 -0.0042 -0.0350 -0.0029 227 THR A C   
1807 O  O   . THR A 227 ? 0.3601 0.2987 0.2358 0.0602  -0.0212 -0.0377 227 THR A O   
1808 C  CB  . THR A 227 ? 0.2532 0.3116 0.1409 0.0507  0.0147  0.0624  227 THR A CB  
1809 O  OG1 . THR A 227 ? 0.2981 0.2728 0.1499 0.0533  -0.0184 0.0573  227 THR A OG1 
1810 C  CG2 . THR A 227 ? 0.3103 0.3466 0.1764 -0.0102 0.0684  -0.0249 227 THR A CG2 
1811 N  N   . ALA A 228 ? 0.2151 0.2541 0.2205 -0.0162 -0.0729 0.0244  228 ALA A N   
1812 C  CA  . ALA A 228 ? 0.2372 0.1323 0.2576 -0.0025 -0.0816 0.0127  228 ALA A CA  
1813 C  C   . ALA A 228 ? 0.2936 0.1294 0.2296 -0.0089 -0.1091 0.0251  228 ALA A C   
1814 O  O   . ALA A 228 ? 0.3983 0.3251 0.2198 -0.0190 -0.1518 -0.0533 228 ALA A O   
1815 C  CB  . ALA A 228 ? 0.2657 0.1798 0.3617 -0.0050 -0.0589 -0.0552 228 ALA A CB  
1816 N  N   . LEU A 229 ? 0.2733 0.1704 0.1803 -0.0134 -0.0908 -0.0067 229 LEU A N   
1817 C  CA  . LEU A 229 ? 0.2460 0.1592 0.2253 -0.0115 -0.0677 0.0082  229 LEU A CA  
1818 C  C   . LEU A 229 ? 0.2705 0.2146 0.2593 -0.0015 -0.0532 -0.0885 229 LEU A C   
1819 O  O   . LEU A 229 ? 0.2688 0.1782 0.2196 -0.0160 -0.0724 -0.0063 229 LEU A O   
1820 C  CB  . LEU A 229 ? 0.2185 0.2073 0.2275 0.0377  -0.0583 0.0364  229 LEU A CB  
1821 C  CG  . LEU A 229 ? 0.1864 0.2672 0.2017 0.0452  -0.0644 0.0026  229 LEU A CG  
1822 C  CD1 . LEU A 229 ? 0.2209 0.2780 0.2034 0.0268  -0.0886 -0.0073 229 LEU A CD1 
1823 C  CD2 . LEU A 229 ? 0.2231 0.2339 0.4183 0.0284  -0.1302 -0.0800 229 LEU A CD2 
1824 N  N   . TYR A 230 ? 0.2483 0.2131 0.1780 -0.0322 -0.0651 -0.0332 230 TYR A N   
1825 C  CA  . TYR A 230 ? 0.3006 0.2903 0.1600 0.0320  -0.0537 -0.0589 230 TYR A CA  
1826 C  C   . TYR A 230 ? 0.2514 0.2556 0.2222 0.0384  -0.0509 -0.0289 230 TYR A C   
1827 O  O   . TYR A 230 ? 0.2578 0.2715 0.2540 0.0219  -0.0478 -0.0619 230 TYR A O   
1828 C  CB  . TYR A 230 ? 0.2893 0.2315 0.2529 0.0145  -0.0873 -0.1124 230 TYR A CB  
1829 C  CG  . TYR A 230 ? 0.3049 0.3863 0.2153 0.0666  -0.0734 -0.0950 230 TYR A CG  
1830 C  CD1 . TYR A 230 ? 0.4343 0.3575 0.3825 0.1447  0.0167  -0.0600 230 TYR A CD1 
1831 C  CD2 . TYR A 230 ? 0.3968 0.4537 0.2691 0.1340  0.0165  -0.0685 230 TYR A CD2 
1832 C  CE1 . TYR A 230 ? 0.5600 0.4314 0.5402 0.1395  0.1678  -0.0290 230 TYR A CE1 
1833 C  CE2 . TYR A 230 ? 0.5740 0.2873 0.4127 0.0655  0.1539  -0.1694 230 TYR A CE2 
1834 C  CZ  . TYR A 230 ? 0.5646 0.3672 0.4848 0.0547  0.2155  -0.0770 230 TYR A CZ  
1835 O  OH  . TYR A 230 ? 0.9033 0.5616 0.5068 -0.1000 0.2730  -0.0626 230 TYR A OH  
1836 N  N   . CYS A 231 ? 0.2977 0.1981 0.2058 0.0820  -0.0383 -0.0571 231 CYS A N   
1837 C  CA  . CYS A 231 ? 0.2924 0.3330 0.1800 0.0514  -0.0119 -0.0150 231 CYS A CA  
1838 C  C   . CYS A 231 ? 0.3500 0.3386 0.1722 0.0913  -0.0126 -0.0708 231 CYS A C   
1839 O  O   . CYS A 231 ? 0.3939 0.3495 0.1692 0.0905  0.0000  -0.0424 231 CYS A O   
1840 C  CB  . CYS A 231 ? 0.2638 0.2194 0.3150 0.0434  -0.0464 -0.0279 231 CYS A CB  
1841 S  SG  . CYS A 231 ? 0.3225 0.2530 0.2572 0.0643  -0.0482 -0.0458 231 CYS A SG  
1842 N  N   . THR A 232 ? 0.3838 0.2627 0.1773 0.0774  -0.0002 -0.0738 232 THR A N   
1843 C  CA  . THR A 232 ? 0.3415 0.2442 0.2243 0.0806  -0.0110 -0.0820 232 THR A CA  
1844 C  C   . THR A 232 ? 0.3574 0.1665 0.2570 0.0243  -0.0302 0.0136  232 THR A C   
1845 O  O   . THR A 232 ? 0.3528 0.1931 0.2261 0.0373  -0.0331 -0.0100 232 THR A O   
1846 C  CB  . THR A 232 ? 0.3041 0.2368 0.2462 0.1082  -0.0363 -0.0158 232 THR A CB  
1847 O  OG1 . THR A 232 ? 0.3166 0.2304 0.2157 0.0520  -0.0240 -0.0867 232 THR A OG1 
1848 C  CG2 . THR A 232 ? 0.2894 0.3211 0.3064 0.1744  -0.0053 -0.0228 232 THR A CG2 
1849 N  N   . HIS A 233 ? 0.3288 0.1920 0.1783 -0.0223 0.0031  0.0015  233 HIS A N   
1850 C  CA  . HIS A 233 ? 0.4573 0.1791 0.2824 -0.0264 -0.0719 -0.0442 233 HIS A CA  
1851 C  C   . HIS A 233 ? 0.4866 0.2539 0.2709 -0.0681 -0.0305 -0.0403 233 HIS A C   
1852 O  O   . HIS A 233 ? 0.5370 0.1682 0.2256 -0.0178 -0.0040 -0.0431 233 HIS A O   
1853 C  CB  . HIS A 233 ? 0.4534 0.1420 0.4647 0.0279  -0.0961 -0.0172 233 HIS A CB  
1854 C  CG  . HIS A 233 ? 0.6170 0.4257 0.7461 -0.0756 0.0057  0.0929  233 HIS A CG  
1855 N  ND1 . HIS A 233 ? 0.6024 0.5425 0.7805 0.0162  -0.2974 -0.0639 233 HIS A ND1 
1856 C  CD2 . HIS A 233 ? 0.6330 0.2978 1.1257 0.1798  0.0146  0.0439  233 HIS A CD2 
1857 C  CE1 . HIS A 233 ? 0.6596 0.7233 0.8536 0.1370  -0.2431 0.1259  233 HIS A CE1 
1858 N  NE2 . HIS A 233 ? 0.3644 0.7270 1.0020 -0.0089 -0.0380 0.0869  233 HIS A NE2 
1859 N  N   . MET A 234 ? 0.5165 0.1983 0.3106 -0.0460 -0.0465 -0.0512 234 MET A N   
1860 C  CA  . MET A 234 ? 0.6128 0.1744 0.3249 -0.0527 -0.0439 -0.0669 234 MET A CA  
1861 C  C   . MET A 234 ? 0.3862 0.3524 0.2811 -0.0212 -0.1227 -0.0245 234 MET A C   
1862 O  O   . MET A 234 ? 0.5202 0.3386 0.2785 -0.1003 -0.0712 -0.0568 234 MET A O   
1863 C  CB  . MET A 234 ? 0.6132 0.4462 0.4484 0.1588  -0.0301 -0.0206 234 MET A CB  
1864 C  CG  . MET A 234 ? 0.5359 0.5051 0.4609 0.1650  -0.0055 0.0074  234 MET A CG  
1865 S  SD  . MET A 234 ? 0.4235 0.9112 0.6766 -0.0741 -0.2146 -0.0734 234 MET A SD  
1866 C  CE  . MET A 234 ? 0.5873 0.7595 0.5682 0.1145  0.0963  -0.0947 234 MET A CE  
1867 N  N   . ASP A 235 ? 0.4331 0.2715 0.3063 -0.0583 -0.0496 -0.1251 235 ASP A N   
1868 C  CA  . ASP A 235 ? 0.6024 0.1370 0.3615 -0.0501 0.0134  -0.0956 235 ASP A CA  
1869 C  C   . ASP A 235 ? 0.5461 0.1764 0.3926 -0.1226 -0.0493 -0.0716 235 ASP A C   
1870 O  O   . ASP A 235 ? 0.5977 0.4032 0.3766 -0.1205 -0.0060 -0.2087 235 ASP A O   
1871 C  CB  . ASP A 235 ? 0.6294 0.3085 0.6596 -0.0778 -0.1550 -0.1037 235 ASP A CB  
1872 C  CG  . ASP A 235 ? 0.9138 0.0990 0.6769 -0.0833 0.0229  -0.0223 235 ASP A CG  
1873 O  OD2 . ASP A 235 ? 1.1572 0.7805 0.3893 -0.1004 -0.2731 -0.1993 235 ASP A OD2 
1874 N  N   . ASP A 236 ? 0.4011 0.2904 0.3258 -0.1420 0.0595  -0.0946 236 ASP A N   
1875 C  CA  . ASP A 236 ? 0.4745 0.3231 0.3653 -0.0357 0.0644  -0.1566 236 ASP A CA  
1876 C  C   . ASP A 236 ? 0.4988 0.3143 0.4028 -0.0587 0.0433  -0.1025 236 ASP A C   
1877 O  O   . ASP A 236 ? 0.4671 0.3309 0.3480 -0.0201 0.0849  -0.1327 236 ASP A O   
1878 C  CB  . ASP A 236 ? 0.3455 0.4817 0.3503 -0.0063 0.0842  -0.1723 236 ASP A CB  
1879 C  CG  . ASP A 236 ? 0.4487 0.3058 0.5006 0.1015  0.0505  -0.1771 236 ASP A CG  
1880 O  OD1 . ASP A 236 ? 0.3802 0.5392 0.5580 0.0841  0.0285  -0.2291 236 ASP A OD1 
1881 O  OD2 . ASP A 236 ? 0.5597 0.2825 0.5534 0.1741  0.0958  -0.1156 236 ASP A OD2 
1882 N  N   . PRO A 237 ? 0.6276 0.2732 0.5533 -0.1061 0.0936  -0.1981 237 PRO A N   
1883 C  CA  . PRO A 237 ? 0.7274 0.0974 0.5600 0.0787  0.1714  -0.0833 237 PRO A CA  
1884 C  C   . PRO A 237 ? 0.8235 0.4866 0.4448 -0.0168 0.1562  -0.1890 237 PRO A C   
1885 O  O   . PRO A 237 ? 0.7397 0.2800 0.4131 0.1733  0.1061  -0.0747 237 PRO A O   
1886 C  CB  . PRO A 237 ? 0.6049 0.0749 0.7848 0.0536  0.1453  -0.1089 237 PRO A CB  
1887 C  CG  . PRO A 237 ? 0.6366 0.4442 0.6894 0.0297  0.1896  -0.0441 237 PRO A CG  
1888 C  CD  . PRO A 237 ? 0.5834 0.2381 0.7393 0.0811  0.0611  -0.1988 237 PRO A CD  
1889 N  N   . SER A 238 ? 0.5378 0.3282 0.4383 0.0969  0.0107  -0.1241 238 SER A N   
1890 C  CA  . SER A 238 ? 0.5169 0.3475 0.3290 0.1077  0.0442  -0.1377 238 SER A CA  
1891 C  C   . SER A 238 ? 0.4314 0.3955 0.3695 0.0894  0.0114  -0.1857 238 SER A C   
1892 O  O   . SER A 238 ? 0.3898 0.5042 0.3940 0.1230  -0.0231 -0.1925 238 SER A O   
1893 C  CB  . SER A 238 ? 0.9538 0.4062 0.4032 0.0310  -0.2050 0.2148  238 SER A CB  
1894 O  OG  . SER A 238 ? 0.9109 0.4303 0.5395 0.0978  0.2367  -0.1613 238 SER A OG  
1895 N  N   . PRO A 239 ? 0.3476 0.4121 0.3190 0.0116  -0.0119 -0.1772 239 PRO A N   
1896 C  CA  . PRO A 239 ? 0.3875 0.4767 0.2491 0.0352  0.0016  -0.1768 239 PRO A CA  
1897 C  C   . PRO A 239 ? 0.2412 0.4870 0.3114 0.0153  0.0390  -0.1632 239 PRO A C   
1898 O  O   . PRO A 239 ? 0.2535 0.4898 0.4099 -0.0146 0.0666  -0.2459 239 PRO A O   
1899 C  CB  . PRO A 239 ? 0.4271 0.3107 0.2699 -0.0129 0.0129  -0.1786 239 PRO A CB  
1900 C  CG  . PRO A 239 ? 0.5705 0.3990 0.3875 0.0461  0.1277  -0.1333 239 PRO A CG  
1901 C  CD  . PRO A 239 ? 0.4412 0.3035 0.3215 -0.1092 0.0680  -0.1790 239 PRO A CD  
1902 N  N   . ARG A 240 ? 0.2272 0.3932 0.2757 0.0895  -0.0155 -0.1707 240 ARG A N   
1903 C  CA  . ARG A 240 ? 0.2763 0.2861 0.2791 0.0555  -0.0212 -0.1315 240 ARG A CA  
1904 C  C   . ARG A 240 ? 0.2444 0.3069 0.2247 0.0820  -0.0706 -0.0697 240 ARG A C   
1905 O  O   . ARG A 240 ? 0.2630 0.3394 0.2726 0.0657  -0.0370 -0.1160 240 ARG A O   
1906 C  CB  . ARG A 240 ? 0.3104 0.3506 0.3375 0.0779  -0.0268 -0.1031 240 ARG A CB  
1907 C  CG  . ARG A 240 ? 0.3527 0.3524 0.4302 0.0922  -0.0260 -0.0494 240 ARG A CG  
1908 C  CD  . ARG A 240 ? 0.3217 0.3671 0.4084 0.0183  -0.0859 -0.0741 240 ARG A CD  
1909 N  NE  . ARG A 240 ? 0.2883 0.3776 0.6850 0.0089  -0.0954 -0.1919 240 ARG A NE  
1910 C  CZ  . ARG A 240 ? 0.3279 0.5348 0.4342 -0.0199 -0.1938 -0.1213 240 ARG A CZ  
1911 N  NH1 . ARG A 240 ? 0.4484 0.4882 0.3694 0.0441  -0.1374 -0.0818 240 ARG A NH1 
1912 N  NH2 . ARG A 240 ? 0.4045 0.5274 0.3557 -0.0225 -0.0836 0.0005  240 ARG A NH2 
1913 N  N   . GLU A 241 ? 0.3014 0.3237 0.2125 0.0768  -0.0386 -0.0941 241 GLU A N   
1914 C  CA  . GLU A 241 ? 0.2218 0.2430 0.2217 0.0356  -0.0548 -0.0058 241 GLU A CA  
1915 C  C   . GLU A 241 ? 0.2386 0.2290 0.2356 0.0295  -0.0348 -0.0350 241 GLU A C   
1916 O  O   . GLU A 241 ? 0.2764 0.1889 0.2375 0.0731  -0.0226 -0.0434 241 GLU A O   
1917 C  CB  . GLU A 241 ? 0.2665 0.2565 0.2545 -0.0111 0.0031  -0.0358 241 GLU A CB  
1918 C  CG  . GLU A 241 ? 0.2830 0.2884 0.2518 0.0727  -0.0223 -0.0046 241 GLU A CG  
1919 C  CD  . GLU A 241 ? 0.3692 0.5867 0.3154 -0.0687 0.1441  -0.0042 241 GLU A CD  
1920 O  OE1 . GLU A 241 ? 0.5237 0.7946 0.4271 -0.1751 0.0425  0.0871  241 GLU A OE1 
1921 O  OE2 . GLU A 241 ? 0.6064 0.6771 0.3370 -0.0231 -0.0148 -0.0100 241 GLU A OE2 
1922 N  N   . MET A 242 ? 0.2398 0.1805 0.1987 0.0006  -0.0122 -0.0837 242 MET A N   
1923 C  CA  . MET A 242 ? 0.2114 0.1737 0.1571 0.0128  -0.0361 -0.0367 242 MET A CA  
1924 C  C   . MET A 242 ? 0.1938 0.1537 0.1724 0.0462  -0.0233 -0.0367 242 MET A C   
1925 O  O   . MET A 242 ? 0.2265 0.1567 0.1819 0.0551  -0.0614 -0.0458 242 MET A O   
1926 C  CB  . MET A 242 ? 0.2272 0.1679 0.1611 0.0238  -0.0170 -0.0381 242 MET A CB  
1927 C  CG  . MET A 242 ? 0.2561 0.1984 0.1571 0.0157  -0.0193 -0.0435 242 MET A CG  
1928 S  SD  . MET A 242 ? 0.2579 0.2044 0.2173 0.0494  -0.0521 -0.0504 242 MET A SD  
1929 C  CE  . MET A 242 ? 0.1632 0.2038 0.2286 0.0055  -0.0324 -0.0402 242 MET A CE  
1930 N  N   . ILE A 243 ? 0.1847 0.1531 0.1550 0.0314  -0.0326 -0.0595 243 ILE A N   
1931 C  CA  . ILE A 243 ? 0.1769 0.1438 0.1370 0.0259  -0.0296 -0.0259 243 ILE A CA  
1932 C  C   . ILE A 243 ? 0.1663 0.1507 0.1500 0.0286  -0.0373 -0.0172 243 ILE A C   
1933 O  O   . ILE A 243 ? 0.1683 0.1391 0.1703 0.0159  -0.0032 0.0156  243 ILE A O   
1934 C  CB  . ILE A 243 ? 0.2063 0.2271 0.1546 0.1015  0.0113  -0.0016 243 ILE A CB  
1935 C  CG1 . ILE A 243 ? 0.2133 0.1907 0.1607 0.0880  0.0035  0.0111  243 ILE A CG1 
1936 C  CG2 . ILE A 243 ? 0.2497 0.2825 0.1722 -0.0310 -0.0236 0.0707  243 ILE A CG2 
1937 C  CD1 . ILE A 243 ? 0.2514 0.2505 0.1966 0.1029  0.0695  -0.0044 243 ILE A CD1 
1938 N  N   . ASN A 244 ? 0.1640 0.0952 0.1072 0.0243  0.0017  0.0129  244 ASN A N   
1939 C  CA  . ASN A 244 ? 0.1545 0.1391 0.1038 0.0233  0.0137  0.0081  244 ASN A CA  
1940 C  C   . ASN A 244 ? 0.1316 0.0794 0.1294 -0.0037 -0.0255 -0.0019 244 ASN A C   
1941 O  O   . ASN A 244 ? 0.1591 0.0715 0.1816 0.0085  -0.0221 0.0150  244 ASN A O   
1942 C  CB  . ASN A 244 ? 0.1406 0.1094 0.1740 0.0120  0.0011  0.0071  244 ASN A CB  
1943 C  CG  . ASN A 244 ? 0.1452 0.1534 0.1456 0.0266  0.0038  0.0129  244 ASN A CG  
1944 O  OD1 . ASN A 244 ? 0.1987 0.1369 0.2393 0.0328  0.0261  0.0358  244 ASN A OD1 
1945 N  ND2 . ASN A 244 ? 0.1744 0.2010 0.2067 0.0130  0.0314  -0.0329 244 ASN A ND2 
1946 N  N   . ASN A 245 ? 0.1294 0.0627 0.1390 0.0054  0.0010  -0.0047 245 ASN A N   
1947 C  CA  . ASN A 245 ? 0.1374 0.1236 0.1330 0.0013  -0.0099 0.0186  245 ASN A CA  
1948 C  C   . ASN A 245 ? 0.1352 0.0665 0.1413 -0.0078 -0.0104 0.0042  245 ASN A C   
1949 O  O   . ASN A 245 ? 0.1467 0.0584 0.1597 -0.0046 0.0025  0.0047  245 ASN A O   
1950 C  CB  . ASN A 245 ? 0.1295 0.1305 0.1568 0.0151  -0.0177 0.0029  245 ASN A CB  
1951 C  CG  . ASN A 245 ? 0.1072 0.0796 0.1509 -0.0364 -0.0359 0.0287  245 ASN A CG  
1952 O  OD1 . ASN A 245 ? 0.1611 0.0598 0.2279 -0.0268 -0.0384 0.0054  245 ASN A OD1 
1953 N  ND2 . ASN A 245 ? 0.1074 0.1500 0.2232 -0.0284 -0.0416 0.0388  245 ASN A ND2 
1954 N  N   . PHE A 246 ? 0.1496 0.0542 0.1273 -0.0096 -0.0175 0.0166  246 PHE A N   
1955 C  CA  . PHE A 246 ? 0.1506 0.0362 0.1045 -0.0037 -0.0435 0.0385  246 PHE A CA  
1956 C  C   . PHE A 246 ? 0.1215 0.0192 0.1326 -0.0047 -0.0217 0.0402  246 PHE A C   
1957 O  O   . PHE A 246 ? 0.1541 0.0115 0.1737 0.0100  -0.0044 0.0089  246 PHE A O   
1958 C  CB  . PHE A 246 ? 0.1354 0.0361 0.1532 -0.0040 -0.0030 0.0274  246 PHE A CB  
1959 C  CG  . PHE A 246 ? 0.1569 0.0091 0.1590 0.0055  0.0109  0.0202  246 PHE A CG  
1960 C  CD1 . PHE A 246 ? 0.1447 0.0099 0.1583 -0.0155 0.0190  0.0143  246 PHE A CD1 
1961 C  CD2 . PHE A 246 ? 0.1756 0.0077 0.2252 0.0076  -0.0327 0.0136  246 PHE A CD2 
1962 C  CE1 . PHE A 246 ? 0.1057 0.0354 0.2228 -0.0243 -0.0126 -0.0118 246 PHE A CE1 
1963 C  CE2 . PHE A 246 ? 0.2046 0.0082 0.1887 0.0071  -0.0187 -0.0180 246 PHE A CE2 
1964 C  CZ  . PHE A 246 ? 0.1348 0.0507 0.1776 -0.0134 -0.0148 -0.0021 246 PHE A CZ  
1965 N  N   . ARG A 247 ? 0.1439 0.0192 0.1081 -0.0107 -0.0445 0.0359  247 ARG A N   
1966 C  CA  . ARG A 247 ? 0.1169 0.0757 0.1291 0.0055  -0.0386 0.0480  247 ARG A CA  
1967 C  C   . ARG A 247 ? 0.1403 0.0405 0.1161 0.0348  -0.0400 0.0067  247 ARG A C   
1968 O  O   . ARG A 247 ? 0.1331 0.0466 0.1557 0.0408  -0.0168 0.0053  247 ARG A O   
1969 C  CB  . ARG A 247 ? 0.1588 0.0277 0.1288 -0.0120 -0.0434 0.0424  247 ARG A CB  
1970 C  CG  . ARG A 247 ? 0.1773 0.0352 0.1187 0.0283  -0.0053 0.0441  247 ARG A CG  
1971 C  CD  . ARG A 247 ? 0.1323 0.0704 0.1288 0.0025  -0.0378 0.0677  247 ARG A CD  
1972 N  NE  . ARG A 247 ? 0.1308 0.0336 0.1254 0.0205  -0.0041 0.0290  247 ARG A NE  
1973 C  CZ  . ARG A 247 ? 0.1137 0.0817 0.1435 0.0095  -0.0095 0.0621  247 ARG A CZ  
1974 N  NH1 . ARG A 247 ? 0.1319 0.0356 0.1665 0.0225  -0.0184 0.0214  247 ARG A NH1 
1975 N  NH2 . ARG A 247 ? 0.1385 0.0319 0.1719 0.0002  -0.0131 0.0258  247 ARG A NH2 
1976 N  N   . GLN A 248 ? 0.1144 0.0438 0.1441 -0.0142 -0.0321 -0.0005 248 GLN A N   
1977 C  CA  . GLN A 248 ? 0.1064 0.0065 0.1229 -0.0037 -0.0076 -0.0030 248 GLN A CA  
1978 C  C   . GLN A 248 ? 0.1234 0.0469 0.0997 -0.0113 -0.0214 0.0011  248 GLN A C   
1979 O  O   . GLN A 248 ? 0.1500 0.0522 0.1344 0.0139  -0.0079 0.0362  248 GLN A O   
1980 C  CB  . GLN A 248 ? 0.0830 0.0527 0.1818 -0.0158 -0.0234 -0.0008 248 GLN A CB  
1981 C  CG  . GLN A 248 ? 0.1286 0.0353 0.1653 0.0042  -0.0121 0.0275  248 GLN A CG  
1982 C  CD  . GLN A 248 ? 0.1803 0.0415 0.1159 -0.0427 -0.0302 0.0025  248 GLN A CD  
1983 O  OE1 . GLN A 248 ? 0.1600 0.0433 0.1610 -0.0145 -0.0383 0.0188  248 GLN A OE1 
1984 N  NE2 . GLN A 248 ? 0.1505 0.0697 0.1596 -0.0070 -0.0428 0.0078  248 GLN A NE2 
1985 N  N   . VAL A 249 ? 0.1326 0.0226 0.1230 0.0168  -0.0282 0.0068  249 VAL A N   
1986 C  CA  . VAL A 249 ? 0.1405 0.0081 0.1365 0.0076  -0.0126 0.0033  249 VAL A CA  
1987 C  C   . VAL A 249 ? 0.1356 0.0276 0.1535 0.0196  -0.0053 0.0171  249 VAL A C   
1988 O  O   . VAL A 249 ? 0.1240 0.0437 0.1703 0.0178  -0.0042 0.0274  249 VAL A O   
1989 C  CB  . VAL A 249 ? 0.2036 0.0116 0.2266 0.0314  -0.0217 0.0040  249 VAL A CB  
1990 C  CG1 . VAL A 249 ? 0.1983 0.0346 0.1787 0.0336  -0.0218 0.0231  249 VAL A CG1 
1991 C  CG2 . VAL A 249 ? 0.2038 0.0250 0.2078 0.0337  -0.0143 -0.0006 249 VAL A CG2 
1992 N  N   . GLN A 250 ? 0.1541 0.0452 0.1044 0.0269  -0.0319 0.0027  250 GLN A N   
1993 C  CA  . GLN A 250 ? 0.1288 0.0717 0.1214 0.0329  -0.0157 0.0284  250 GLN A CA  
1994 C  C   . GLN A 250 ? 0.1652 0.0796 0.1166 0.0434  -0.0350 0.0182  250 GLN A C   
1995 O  O   . GLN A 250 ? 0.1692 0.0861 0.1755 0.0392  -0.0249 -0.0027 250 GLN A O   
1996 C  CB  . GLN A 250 ? 0.1555 0.0460 0.1582 -0.0050 -0.0326 0.0537  250 GLN A CB  
1997 C  CG  . GLN A 250 ? 0.1675 0.0399 0.1464 0.0320  -0.0374 0.0408  250 GLN A CG  
1998 C  CD  . GLN A 250 ? 0.1683 0.0591 0.1175 0.0227  -0.0705 0.0116  250 GLN A CD  
1999 O  OE1 . GLN A 250 ? 0.1679 0.0559 0.1634 0.0277  0.0081  0.0418  250 GLN A OE1 
2000 N  NE2 . GLN A 250 ? 0.1500 0.0281 0.1342 0.0012  -0.0524 0.0419  250 GLN A NE2 
2001 N  N   . LYS A 251 ? 0.1525 0.1074 0.1035 0.0440  -0.0110 0.0416  251 LYS A N   
2002 C  CA  . LYS A 251 ? 0.1355 0.1865 0.1135 0.0547  -0.0147 0.0179  251 LYS A CA  
2003 C  C   . LYS A 251 ? 0.1175 0.1707 0.1273 0.0538  -0.0186 -0.0260 251 LYS A C   
2004 O  O   . LYS A 251 ? 0.1410 0.2035 0.1785 0.0161  -0.0004 0.0289  251 LYS A O   
2005 C  CB  . LYS A 251 ? 0.1266 0.2137 0.1363 0.0749  -0.0109 0.0098  251 LYS A CB  
2006 C  CG  . LYS A 251 ? 0.1345 0.2436 0.1520 0.0597  -0.0005 -0.0218 251 LYS A CG  
2007 C  CD  . LYS A 251 ? 0.1279 0.3019 0.1197 0.0565  0.0173  0.0620  251 LYS A CD  
2008 C  CE  . LYS A 251 ? 0.1286 0.1381 0.1222 0.0027  -0.0158 0.0061  251 LYS A CE  
2009 N  NZ  . LYS A 251 ? 0.1103 0.0756 0.1272 0.0230  -0.0160 0.0264  251 LYS A NZ  
2010 N  N   . PHE A 252 ? 0.1956 0.1694 0.1510 0.0241  -0.0155 -0.0260 252 PHE A N   
2011 C  CA  . PHE A 252 ? 0.2570 0.1103 0.1796 0.0662  0.0223  -0.0222 252 PHE A CA  
2012 C  C   . PHE A 252 ? 0.3128 0.2955 0.2471 0.1465  -0.0582 -0.0913 252 PHE A C   
2013 O  O   . PHE A 252 ? 0.4850 0.3916 0.3982 0.1008  -0.1811 -0.1650 252 PHE A O   
2014 C  CB  . PHE A 252 ? 0.2320 0.1758 0.2065 0.0652  -0.0091 0.0024  252 PHE A CB  
2015 C  CG  . PHE A 252 ? 0.1956 0.1986 0.2211 0.1033  -0.0462 0.0307  252 PHE A CG  
2016 C  CD1 . PHE A 252 ? 0.1552 0.3143 0.2008 0.0682  -0.0431 0.0768  252 PHE A CD1 
2017 C  CD2 . PHE A 252 ? 0.3024 0.2909 0.2436 0.1111  -0.0223 -0.0279 252 PHE A CD2 
2018 C  CE1 . PHE A 252 ? 0.2229 0.3766 0.1980 0.1487  -0.0317 0.0816  252 PHE A CE1 
2019 C  CE2 . PHE A 252 ? 0.2859 0.3643 0.1812 0.1406  -0.0713 -0.0096 252 PHE A CE2 
2020 C  CZ  . PHE A 252 ? 0.2627 0.4336 0.1760 0.0895  -0.0414 -0.0051 252 PHE A CZ  
2021 N  N   . ASP A 253 ? 0.4399 0.3310 0.2701 0.0597  -0.0498 -0.0363 253 ASP A N   
2022 C  CA  . ASP A 253 ? 0.4507 0.5508 0.1865 0.1868  -0.1017 0.0849  253 ASP A CA  
2023 C  C   . ASP A 253 ? 0.2958 0.4593 0.2313 0.0972  -0.0790 -0.0027 253 ASP A C   
2024 O  O   . ASP A 253 ? 0.3697 0.4190 0.3380 0.0221  -0.0300 -0.0076 253 ASP A O   
2025 C  CB  . ASP A 253 ? 0.4090 0.5759 0.2225 0.1662  -0.0620 0.0403  253 ASP A CB  
2026 C  CG  . ASP A 253 ? 0.4205 0.6466 0.4480 0.0167  -0.1114 0.1594  253 ASP A CG  
2027 O  OD1 . ASP A 253 ? 0.3274 0.6372 0.5404 0.0500  -0.0336 0.2289  253 ASP A OD1 
2028 O  OD2 . ASP A 253 ? 0.4492 0.6991 0.3794 0.1196  0.0022  0.1632  253 ASP A OD2 
2029 N  N   . GLU A 254 ? 0.2867 0.4722 0.2922 0.0566  -0.0425 0.0784  254 GLU A N   
2030 C  CA  . GLU A 254 ? 0.2800 0.5032 0.3190 0.0214  -0.0200 0.1175  254 GLU A CA  
2031 C  C   . GLU A 254 ? 0.2921 0.4886 0.3131 0.0414  -0.1066 0.1452  254 GLU A C   
2032 O  O   . GLU A 254 ? 0.4758 0.6048 0.3403 -0.0450 -0.0529 0.1842  254 GLU A O   
2033 C  CB  . GLU A 254 ? 0.2313 0.4401 0.3072 -0.0098 -0.0249 0.0922  254 GLU A CB  
2034 C  CG  . GLU A 254 ? 0.2382 0.4252 0.4771 0.0905  -0.0551 0.0192  254 GLU A CG  
2035 C  CD  . GLU A 254 ? 0.4561 0.4901 0.4952 0.0419  -0.1483 0.0555  254 GLU A CD  
2036 O  OE1 . GLU A 254 ? 0.5173 0.5716 0.4751 -0.1154 -0.1021 0.2345  254 GLU A OE1 
2037 O  OE2 . GLU A 254 ? 0.5796 0.4343 0.4594 0.0881  -0.1521 -0.1662 254 GLU A OE2 
2038 N  N   . ARG A 255 ? 0.3137 0.5598 0.2570 0.1368  -0.0501 0.1329  255 ARG A N   
2039 C  CA  . ARG A 255 ? 0.2827 0.2672 0.2883 0.1099  -0.0337 -0.0304 255 ARG A CA  
2040 C  C   . ARG A 255 ? 0.3024 0.3711 0.2876 0.1817  0.0201  0.0731  255 ARG A C   
2041 O  O   . ARG A 255 ? 0.3133 0.5011 0.2632 0.0399  0.0005  -0.0190 255 ARG A O   
2042 C  CB  . ARG A 255 ? 0.3405 0.2275 0.3524 0.1004  -0.0115 -0.0719 255 ARG A CB  
2043 C  CG  . ARG A 255 ? 0.4906 0.2062 0.3350 0.1434  -0.0553 -0.1208 255 ARG A CG  
2044 C  CD  . ARG A 255 ? 0.3015 0.2899 0.3608 0.0611  -0.1189 -0.0842 255 ARG A CD  
2045 N  NE  . ARG A 255 ? 0.2561 0.4821 0.3173 -0.0719 -0.1241 0.1014  255 ARG A NE  
2046 C  CZ  . ARG A 255 ? 0.2337 0.4016 0.3220 -0.0132 -0.0683 -0.0051 255 ARG A CZ  
2047 N  NH1 . ARG A 255 ? 0.3186 0.4191 0.3977 0.0208  -0.0693 -0.1361 255 ARG A NH1 
2048 N  NH2 . ARG A 255 ? 0.2311 0.2903 0.2070 0.0297  -0.0634 -0.0141 255 ARG A NH2 
2049 N  N   . LEU A 256 ? 0.2982 0.3837 0.2694 0.1780  -0.0013 0.0352  256 LEU A N   
2050 C  CA  . LEU A 256 ? 0.2798 0.3511 0.2228 0.1053  -0.0103 0.0643  256 LEU A CA  
2051 C  C   . LEU A 256 ? 0.2692 0.1834 0.2017 0.0976  0.0188  0.0068  256 LEU A C   
2052 O  O   . LEU A 256 ? 0.3277 0.3104 0.2472 0.0549  -0.0675 -0.0122 256 LEU A O   
2053 C  CB  . LEU A 256 ? 0.3536 0.4343 0.1553 0.0049  -0.0109 0.0089  256 LEU A CB  
2054 C  CG  . LEU A 256 ? 0.3494 0.4733 0.2164 0.0108  -0.0704 0.1154  256 LEU A CG  
2055 C  CD1 . LEU A 256 ? 0.5524 0.4552 0.2199 0.0664  -0.1051 0.0022  256 LEU A CD1 
2056 C  CD2 . LEU A 256 ? 0.4436 0.6043 0.2998 -0.0584 -0.0037 0.1344  256 LEU A CD2 
2057 N  N   . VAL A 257 ? 0.2523 0.3306 0.2107 0.0944  0.0027  0.0924  257 VAL A N   
2058 C  CA  . VAL A 257 ? 0.2640 0.1877 0.1872 0.0509  -0.0300 0.0143  257 VAL A CA  
2059 C  C   . VAL A 257 ? 0.2229 0.2385 0.1961 0.0261  0.0064  -0.0346 257 VAL A C   
2060 O  O   . VAL A 257 ? 0.2115 0.2588 0.2603 0.0080  -0.0040 -0.0262 257 VAL A O   
2061 C  CB  . VAL A 257 ? 0.2263 0.1699 0.1740 0.0284  -0.0173 -0.0279 257 VAL A CB  
2062 C  CG1 . VAL A 257 ? 0.2250 0.0920 0.1898 -0.0182 -0.0146 0.0172  257 VAL A CG1 
2063 C  CG2 . VAL A 257 ? 0.2417 0.1674 0.2117 0.0593  -0.0006 -0.0027 257 VAL A CG2 
2064 N  N   . TYR A 258 ? 0.2225 0.1212 0.2142 0.0240  -0.0179 -0.0461 258 TYR A N   
2065 C  CA  . TYR A 258 ? 0.1999 0.1272 0.2023 0.0494  0.0067  -0.0022 258 TYR A CA  
2066 C  C   . TYR A 258 ? 0.2351 0.1477 0.1591 0.0337  0.0018  -0.0113 258 TYR A C   
2067 O  O   . TYR A 258 ? 0.2804 0.0898 0.2128 0.0010  -0.0268 0.0041  258 TYR A O   
2068 C  CB  . TYR A 258 ? 0.2200 0.2877 0.1495 0.0078  0.0147  -0.0111 258 TYR A CB  
2069 C  CG  . TYR A 258 ? 0.2614 0.3084 0.2153 0.0099  -0.0061 0.0217  258 TYR A CG  
2070 C  CD1 . TYR A 258 ? 0.2790 0.3963 0.1889 0.0450  -0.0351 0.0190  258 TYR A CD1 
2071 C  CD2 . TYR A 258 ? 0.2469 0.2899 0.2328 -0.0308 -0.0251 0.0269  258 TYR A CD2 
2072 C  CE1 . TYR A 258 ? 0.4159 0.2854 0.2863 0.0296  -0.0466 0.0479  258 TYR A CE1 
2073 C  CE2 . TYR A 258 ? 0.4674 0.3124 0.2416 0.0044  -0.0483 0.0485  258 TYR A CE2 
2074 C  CZ  . TYR A 258 ? 0.3728 0.3106 0.2085 0.0770  -0.0357 0.0397  258 TYR A CZ  
2075 O  OH  . TYR A 258 ? 0.6020 0.4211 0.2931 0.0498  -0.1377 0.1171  258 TYR A OH  
2076 N  N   . THR A 259 ? 0.2308 0.1374 0.1844 0.0171  -0.0077 0.0035  259 THR A N   
2077 C  CA  . THR A 259 ? 0.1731 0.1566 0.1775 -0.0230 -0.0179 0.0172  259 THR A CA  
2078 C  C   . THR A 259 ? 0.1726 0.1008 0.1578 -0.0581 -0.0058 0.0252  259 THR A C   
2079 O  O   . THR A 259 ? 0.2358 0.1039 0.1663 0.0223  -0.0129 0.0021  259 THR A O   
2080 C  CB  . THR A 259 ? 0.1694 0.1539 0.1927 -0.0348 0.0167  -0.0497 259 THR A CB  
2081 O  OG1 . THR A 259 ? 0.2155 0.1810 0.2483 -0.0431 -0.0058 -0.0806 259 THR A OG1 
2082 C  CG2 . THR A 259 ? 0.1834 0.2012 0.1772 0.0320  -0.0004 -0.0150 259 THR A CG2 
2083 N  N   . SER A 260 ? 0.1632 0.1374 0.1850 -0.0111 -0.0234 0.0075  260 SER A N   
2084 C  CA  . SER A 260 ? 0.1714 0.1442 0.1737 -0.0044 -0.0152 0.0029  260 SER A CA  
2085 C  C   . SER A 260 ? 0.2275 0.1280 0.2074 0.0152  0.0313  -0.0517 260 SER A C   
2086 O  O   . SER A 260 ? 0.2623 0.0708 0.3362 0.0320  0.0219  -0.0449 260 SER A O   
2087 C  CB  . SER A 260 ? 0.1837 0.1593 0.1636 0.0188  -0.0230 -0.0107 260 SER A CB  
2088 O  OG  . SER A 260 ? 0.1803 0.1449 0.1588 0.0125  -0.0176 -0.0322 260 SER A OG  
2089 N  N   . PHE A 261 ? 0.2260 0.0774 0.2578 -0.0209 -0.0005 -0.0565 261 PHE A N   
2090 C  CA  . PHE A 261 ? 0.2388 0.0935 0.2803 -0.0375 0.0198  0.0031  261 PHE A CA  
2091 C  C   . PHE A 261 ? 0.2455 0.1042 0.2789 -0.0535 -0.0020 -0.0447 261 PHE A C   
2092 O  O   . PHE A 261 ? 0.2762 0.2340 0.2336 0.0385  -0.0526 -0.0163 261 PHE A O   
2093 C  CB  . PHE A 261 ? 0.2292 0.0459 0.2849 -0.0564 0.0343  -0.0135 261 PHE A CB  
2094 C  CG  . PHE A 261 ? 0.2153 0.1780 0.2277 0.0004  0.0093  -0.0049 261 PHE A CG  
2095 C  CD1 . PHE A 261 ? 0.1859 0.1663 0.1983 -0.0033 -0.0051 0.0256  261 PHE A CD1 
2096 C  CD2 . PHE A 261 ? 0.2315 0.1318 0.3444 -0.0302 0.0421  -0.0183 261 PHE A CD2 
2097 C  CE1 . PHE A 261 ? 0.1758 0.2440 0.2178 0.0303  0.0122  0.0408  261 PHE A CE1 
2098 C  CE2 . PHE A 261 ? 0.3010 0.1948 0.3514 -0.0127 0.0325  -0.0706 261 PHE A CE2 
2099 C  CZ  . PHE A 261 ? 0.1977 0.1596 0.2478 -0.0053 0.0425  -0.0108 261 PHE A CZ  
2100 N  N   . SER A 262 ? 0.3955 0.0821 0.4260 -0.0736 -0.0339 -0.0240 262 SER A N   
2101 C  CA  . SER A 262 ? 0.4480 0.2444 0.4709 -0.0899 -0.0391 -0.1408 262 SER A CA  
2102 C  C   . SER A 262 ? 0.5738 0.1755 0.6307 -0.0080 0.1905  -0.1574 262 SER A C   
2103 O  O   . SER A 262 ? 0.5707 0.5424 0.5658 -0.1896 0.1199  -0.2043 262 SER A O   
2104 C  CB  . SER A 262 ? 0.6863 0.0986 0.6848 -0.0949 0.0763  -0.2407 262 SER A CB  
2105 O  OG  . SER A 262 ? 0.8318 0.3643 0.6560 0.0697  0.0330  -0.1095 262 SER A OG  
2106 N  N   . LYS B 3   ? 0.6052 0.2737 0.6269 0.1465  0.1184  0.1775  3   LYS B N   
2107 C  CA  . LYS B 3   ? 0.5332 0.1754 0.6585 -0.0038 0.0259  0.1951  3   LYS B CA  
2108 C  C   . LYS B 3   ? 0.3342 0.1812 0.3297 0.0303  0.0670  0.0668  3   LYS B C   
2109 O  O   . LYS B 3   ? 0.4087 0.1175 0.2934 -0.0156 0.0806  0.0381  3   LYS B O   
2110 C  CB  . LYS B 3   ? 0.5455 0.2900 0.7514 -0.0545 0.1069  0.1416  3   LYS B CB  
2111 C  CG  . LYS B 3   ? 0.3910 0.0635 0.9374 0.0575  0.1496  0.2282  3   LYS B CG  
2112 C  CD  . LYS B 3   ? 0.5082 0.4121 1.0216 0.2995  0.1036  -0.0240 3   LYS B CD  
2113 C  CE  . LYS B 3   ? 0.8512 0.4667 1.0412 0.3109  0.2376  0.1595  3   LYS B CE  
2114 N  NZ  . LYS B 3   ? 0.8734 0.5070 0.5349 0.3465  0.0858  0.0277  3   LYS B NZ  
2115 N  N   . TRP B 4   ? 0.2852 0.0419 0.2940 0.0189  0.0363  0.0458  4   TRP B N   
2116 C  CA  . TRP B 4   ? 0.2128 0.0431 0.2379 0.0008  -0.0175 0.0152  4   TRP B CA  
2117 C  C   . TRP B 4   ? 0.2687 0.0871 0.1420 0.0333  -0.0553 0.0149  4   TRP B C   
2118 O  O   . TRP B 4   ? 0.2060 0.0731 0.2369 -0.0469 -0.0316 0.0714  4   TRP B O   
2119 C  CB  . TRP B 4   ? 0.1833 0.0787 0.2293 0.0017  -0.0187 0.0023  4   TRP B CB  
2120 C  CG  . TRP B 4   ? 0.1703 0.0893 0.1392 -0.0006 -0.0295 0.0229  4   TRP B CG  
2121 C  CD1 . TRP B 4   ? 0.1895 0.0965 0.1392 -0.0018 -0.0259 0.0229  4   TRP B CD1 
2122 C  CD2 . TRP B 4   ? 0.1729 0.0660 0.1791 0.0284  -0.0506 0.0297  4   TRP B CD2 
2123 N  NE1 . TRP B 4   ? 0.1678 0.0591 0.2060 0.0421  -0.0227 0.0373  4   TRP B NE1 
2124 C  CE2 . TRP B 4   ? 0.1658 0.0602 0.1269 0.0139  -0.0366 -0.0058 4   TRP B CE2 
2125 C  CE3 . TRP B 4   ? 0.2116 0.0478 0.1286 0.0070  -0.0196 0.0383  4   TRP B CE3 
2126 C  CZ2 . TRP B 4   ? 0.1884 0.0936 0.1956 -0.0119 -0.0394 0.0058  4   TRP B CZ2 
2127 C  CZ3 . TRP B 4   ? 0.1947 0.0660 0.1632 -0.0067 -0.0444 0.0254  4   TRP B CZ3 
2128 C  CH2 . TRP B 4   ? 0.2074 0.1273 0.1305 0.0196  -0.0251 -0.0013 4   TRP B CH2 
2129 N  N   . THR B 5   ? 0.1410 0.0363 0.2342 -0.0498 -0.0331 0.0348  5   THR B N   
2130 C  CA  . THR B 5   ? 0.2012 0.0313 0.2077 -0.0496 0.0010  0.0498  5   THR B CA  
2131 C  C   . THR B 5   ? 0.1697 0.0361 0.1575 -0.0247 -0.0259 0.0093  5   THR B C   
2132 O  O   . THR B 5   ? 0.1864 0.0347 0.1606 -0.0116 -0.0328 0.0192  5   THR B O   
2133 C  CB  . THR B 5   ? 0.1913 0.0549 0.2189 -0.0039 -0.0096 0.0826  5   THR B CB  
2134 O  OG1 . THR B 5   ? 0.1728 0.1067 0.2196 -0.0013 0.0150  0.0560  5   THR B OG1 
2135 C  CG2 . THR B 5   ? 0.2765 0.0177 0.2575 -0.0221 0.0233  0.0469  5   THR B CG2 
2136 N  N   . TYR B 6   ? 0.2019 0.0464 0.1611 -0.0262 0.0011  0.0049  6   TYR B N   
2137 C  CA  . TYR B 6   ? 0.1703 0.0349 0.1536 -0.0539 -0.0091 0.0053  6   TYR B CA  
2138 C  C   . TYR B 6   ? 0.1847 0.0610 0.1410 0.0041  -0.0044 0.0113  6   TYR B C   
2139 O  O   . TYR B 6   ? 0.1796 0.0841 0.2121 0.0060  -0.0392 0.0384  6   TYR B O   
2140 C  CB  . TYR B 6   ? 0.1306 0.0523 0.1815 -0.0435 -0.0035 -0.0312 6   TYR B CB  
2141 C  CG  . TYR B 6   ? 0.1527 0.0384 0.1609 -0.0249 0.0122  0.0120  6   TYR B CG  
2142 C  CD1 . TYR B 6   ? 0.1894 0.0084 0.1606 -0.0179 0.0050  0.0066  6   TYR B CD1 
2143 C  CD2 . TYR B 6   ? 0.2109 0.0077 0.1538 -0.0164 0.0029  -0.0042 6   TYR B CD2 
2144 C  CE1 . TYR B 6   ? 0.1868 0.0087 0.1648 0.0002  -0.0059 -0.0194 6   TYR B CE1 
2145 C  CE2 . TYR B 6   ? 0.1842 0.0081 0.2070 0.0001  0.0080  -0.0189 6   TYR B CE2 
2146 C  CZ  . TYR B 6   ? 0.1898 0.0080 0.1895 -0.0172 0.0075  0.0020  6   TYR B CZ  
2147 O  OH  . TYR B 6   ? 0.1996 0.0088 0.1940 0.0062  0.0026  -0.0206 6   TYR B OH  
2148 N  N   . PHE B 7   ? 0.1324 0.0929 0.2186 -0.0203 0.0076  0.0287  7   PHE B N   
2149 C  CA  . PHE B 7   ? 0.1890 0.0679 0.2588 0.0044  0.0336  0.0030  7   PHE B CA  
2150 C  C   . PHE B 7   ? 0.1379 0.1392 0.2218 -0.0161 -0.0050 0.0685  7   PHE B C   
2151 O  O   . PHE B 7   ? 0.1667 0.0969 0.2417 0.0098  0.0073  0.0555  7   PHE B O   
2152 C  CB  . PHE B 7   ? 0.3107 0.1785 0.3010 -0.0008 0.0185  -0.0442 7   PHE B CB  
2153 C  CG  . PHE B 7   ? 0.4379 0.0632 0.3182 0.0009  0.1051  -0.0259 7   PHE B CG  
2154 C  CD1 . PHE B 7   ? 0.4221 0.1367 0.4446 0.0220  0.1615  0.0471  7   PHE B CD1 
2155 C  CD2 . PHE B 7   ? 0.6117 0.2148 0.6013 -0.0578 0.2143  0.1896  7   PHE B CD2 
2156 C  CE1 . PHE B 7   ? 0.5014 0.1128 0.6397 0.0901  0.2536  0.0374  7   PHE B CE1 
2157 C  CE2 . PHE B 7   ? 0.6882 0.2408 0.7361 -0.1031 0.3466  0.2444  7   PHE B CE2 
2158 C  CZ  . PHE B 7   ? 0.6328 0.4738 0.7776 -0.0074 0.3231  0.1949  7   PHE B CZ  
2159 N  N   . GLY B 8   ? 0.1586 0.1941 0.2476 -0.0558 -0.0084 0.0652  8   GLY B N   
2160 C  CA  . GLY B 8   ? 0.1898 0.2076 0.2365 -0.1038 -0.0329 0.0465  8   GLY B CA  
2161 C  C   . GLY B 8   ? 0.1851 0.2624 0.2387 -0.0410 -0.0310 0.0412  8   GLY B C   
2162 O  O   . GLY B 8   ? 0.2249 0.2181 0.2139 -0.0402 -0.0501 0.0322  8   GLY B O   
2163 N  N   . PRO B 9   ? 0.1886 0.2333 0.2752 0.0208  -0.0260 0.0924  9   PRO B N   
2164 C  CA  . PRO B 9   ? 0.2157 0.2358 0.3494 -0.0493 0.0234  0.0701  9   PRO B CA  
2165 C  C   . PRO B 9   ? 0.1859 0.1266 0.2166 -0.0670 -0.0440 0.0541  9   PRO B C   
2166 O  O   . PRO B 9   ? 0.2552 0.1775 0.2213 -0.0251 -0.0905 0.0332  9   PRO B O   
2167 C  CB  . PRO B 9   ? 0.2394 0.3097 0.3868 -0.0929 0.0475  0.1327  9   PRO B CB  
2168 C  CG  . PRO B 9   ? 0.5141 0.0369 0.5017 0.0085  0.1128  0.1215  9   PRO B CG  
2169 C  CD  . PRO B 9   ? 0.2855 0.2407 0.3052 -0.0683 -0.0163 0.1012  9   PRO B CD  
2170 N  N   . ASP B 10  ? 0.1743 0.0913 0.2564 -0.0621 -0.0358 0.0905  10  ASP B N   
2171 C  CA  . ASP B 10  ? 0.1875 0.0581 0.2446 -0.0444 -0.0639 0.0595  10  ASP B CA  
2172 C  C   . ASP B 10  ? 0.2180 0.0584 0.1652 -0.0326 -0.0301 0.0353  10  ASP B C   
2173 O  O   . ASP B 10  ? 0.1888 0.0173 0.2203 -0.0309 -0.0311 0.0398  10  ASP B O   
2174 C  CB  . ASP B 10  ? 0.2594 0.0758 0.2407 -0.0236 -0.0540 0.1125  10  ASP B CB  
2175 C  CG  . ASP B 10  ? 0.2860 0.0656 0.3201 -0.0512 -0.0684 0.1021  10  ASP B CG  
2176 O  OD1 . ASP B 10  ? 0.5309 0.1179 0.3480 -0.1108 -0.0955 0.0577  10  ASP B OD1 
2177 O  OD2 . ASP B 10  ? 0.5006 0.1324 0.3158 -0.0445 -0.0354 0.0941  10  ASP B OD2 
2178 N  N   . GLY B 11  ? 0.1754 0.0383 0.1568 -0.0547 -0.0566 0.0179  11  GLY B N   
2179 C  CA  . GLY B 11  ? 0.1690 0.0207 0.1665 -0.0219 -0.0258 0.0127  11  GLY B CA  
2180 C  C   . GLY B 11  ? 0.1336 0.0611 0.1581 -0.0139 -0.0165 0.0313  11  GLY B C   
2181 O  O   . GLY B 11  ? 0.1247 0.0538 0.1722 0.0159  -0.0418 0.0287  11  GLY B O   
2182 N  N   . GLU B 12  ? 0.1478 0.0534 0.1456 0.0058  -0.0255 0.0333  12  GLU B N   
2183 C  CA  . GLU B 12  ? 0.1171 0.0299 0.1434 -0.0179 -0.0227 0.0387  12  GLU B CA  
2184 C  C   . GLU B 12  ? 0.1252 0.0466 0.1398 -0.0068 -0.0194 0.0359  12  GLU B C   
2185 O  O   . GLU B 12  ? 0.1463 0.0159 0.1306 0.0031  -0.0174 0.0277  12  GLU B O   
2186 C  CB  . GLU B 12  ? 0.1549 0.0139 0.1994 0.0224  -0.0079 0.0271  12  GLU B CB  
2187 C  CG  . GLU B 12  ? 0.1105 0.0150 0.2235 0.0188  -0.0242 0.0208  12  GLU B CG  
2188 C  CD  . GLU B 12  ? 0.1172 0.0304 0.2060 0.0029  -0.0487 0.0219  12  GLU B CD  
2189 O  OE1 . GLU B 12  ? 0.1732 0.0097 0.1776 0.0222  -0.0266 -0.0118 12  GLU B OE1 
2190 O  OE2 . GLU B 12  ? 0.1644 0.0190 0.1805 -0.0210 -0.0302 0.0447  12  GLU B OE2 
2191 N  N   . ASN B 13  ? 0.1122 0.0079 0.2000 -0.0103 -0.0443 0.0145  13  ASN B N   
2192 C  CA  . ASN B 13  ? 0.0791 0.0292 0.2232 -0.0370 -0.0381 0.0237  13  ASN B CA  
2193 C  C   . ASN B 13  ? 0.1054 0.0282 0.1900 -0.0126 -0.0199 0.0358  13  ASN B C   
2194 O  O   . ASN B 13  ? 0.2139 0.0073 0.2299 -0.0098 -0.0496 0.0126  13  ASN B O   
2195 C  CB  . ASN B 13  ? 0.1196 0.0133 0.2042 0.0044  -0.0441 -0.0150 13  ASN B CB  
2196 C  CG  . ASN B 13  ? 0.1442 0.0158 0.1524 -0.0158 -0.0203 0.0092  13  ASN B CG  
2197 O  OD1 . ASN B 13  ? 0.1277 0.0629 0.1895 0.0031  0.0108  0.0179  13  ASN B OD1 
2198 N  ND2 . ASN B 13  ? 0.1452 0.0388 0.1890 0.0031  -0.0181 0.0292  13  ASN B ND2 
2199 N  N   . SER B 14  ? 0.1259 0.0081 0.1761 -0.0114 -0.0109 0.0120  14  SER B N   
2200 C  CA  . SER B 14  ? 0.1622 0.0129 0.1690 -0.0005 -0.0128 0.0326  14  SER B CA  
2201 C  C   . SER B 14  ? 0.1566 0.0109 0.1771 -0.0179 -0.0046 0.0210  14  SER B C   
2202 O  O   . SER B 14  ? 0.1362 0.0082 0.1840 -0.0148 -0.0242 0.0087  14  SER B O   
2203 C  CB  . SER B 14  ? 0.1392 0.0428 0.1992 0.0011  0.0047  0.0402  14  SER B CB  
2204 O  OG  . SER B 14  ? 0.1507 0.0338 0.2010 0.0130  -0.0037 0.0199  14  SER B OG  
2205 N  N   . TRP B 15  ? 0.1245 0.0095 0.1850 -0.0076 -0.0152 0.0231  15  TRP B N   
2206 C  CA  . TRP B 15  ? 0.1294 0.0116 0.1951 -0.0245 -0.0115 0.0099  15  TRP B CA  
2207 C  C   . TRP B 15  ? 0.1143 0.0082 0.2110 -0.0134 -0.0232 0.0094  15  TRP B C   
2208 O  O   . TRP B 15  ? 0.1632 0.0075 0.2087 0.0000  -0.0228 0.0154  15  TRP B O   
2209 C  CB  . TRP B 15  ? 0.1500 0.0207 0.1848 -0.0425 -0.0013 0.0079  15  TRP B CB  
2210 C  CG  . TRP B 15  ? 0.1488 0.0077 0.1776 0.0142  -0.0150 -0.0013 15  TRP B CG  
2211 C  CD1 . TRP B 15  ? 0.1529 0.0083 0.1973 0.0156  -0.0190 -0.0095 15  TRP B CD1 
2212 C  CD2 . TRP B 15  ? 0.1589 0.0193 0.2164 -0.0003 -0.0295 0.0515  15  TRP B CD2 
2213 N  NE1 . TRP B 15  ? 0.1502 0.0167 0.1681 0.0197  -0.0369 0.0009  15  TRP B NE1 
2214 C  CE2 . TRP B 15  ? 0.1373 0.0120 0.2047 0.0191  -0.0413 0.0171  15  TRP B CE2 
2215 C  CE3 . TRP B 15  ? 0.1275 0.0063 0.1911 -0.0004 -0.0030 0.0005  15  TRP B CE3 
2216 C  CZ2 . TRP B 15  ? 0.0888 0.0157 0.1941 0.0135  -0.0396 0.0281  15  TRP B CZ2 
2217 C  CZ3 . TRP B 15  ? 0.1092 0.0066 0.1854 0.0051  -0.0486 -0.0040 15  TRP B CZ3 
2218 C  CH2 . TRP B 15  ? 0.1429 0.0108 0.1677 0.0123  -0.0238 0.0207  15  TRP B CH2 
2219 N  N   . SER B 16  ? 0.1617 0.0128 0.1964 -0.0267 -0.0426 0.0258  16  SER B N   
2220 C  CA  . SER B 16  ? 0.1708 0.0109 0.2113 -0.0275 -0.0533 0.0089  16  SER B CA  
2221 C  C   . SER B 16  ? 0.1306 0.0090 0.2029 -0.0133 -0.0247 0.0179  16  SER B C   
2222 O  O   . SER B 16  ? 0.1820 0.0072 0.2446 -0.0118 -0.0297 0.0077  16  SER B O   
2223 C  CB  . SER B 16  ? 0.1481 0.0147 0.2632 -0.0027 -0.0442 0.0353  16  SER B CB  
2224 O  OG  . SER B 16  ? 0.1877 0.0981 0.2798 -0.0034 -0.0188 0.0127  16  SER B OG  
2225 N  N   . LYS B 17  ? 0.1667 0.0083 0.2469 -0.0176 -0.0198 0.0068  17  LYS B N   
2226 C  CA  . LYS B 17  ? 0.1392 0.0104 0.1873 -0.0219 -0.0326 -0.0042 17  LYS B CA  
2227 C  C   . LYS B 17  ? 0.1564 0.0098 0.2515 -0.0158 -0.0156 -0.0194 17  LYS B C   
2228 O  O   . LYS B 17  ? 0.1662 0.0070 0.2989 -0.0080 -0.0246 -0.0082 17  LYS B O   
2229 C  CB  . LYS B 17  ? 0.1395 0.0103 0.2200 -0.0216 -0.0209 -0.0073 17  LYS B CB  
2230 C  CG  . LYS B 17  ? 0.1701 0.0323 0.2483 0.0107  0.0152  -0.0082 17  LYS B CG  
2231 C  CD  . LYS B 17  ? 0.2267 0.0119 0.2270 0.0348  0.0160  0.0062  17  LYS B CD  
2232 C  CE  . LYS B 17  ? 0.1524 0.0072 0.2228 -0.0063 -0.0030 -0.0111 17  LYS B CE  
2233 N  NZ  . LYS B 17  ? 0.1661 0.0119 0.2388 0.0006  -0.0099 -0.0100 17  LYS B NZ  
2234 N  N   . LYS B 18  ? 0.1553 0.0094 0.2627 -0.0187 -0.0199 0.0161  18  LYS B N   
2235 C  CA  . LYS B 18  ? 0.1205 0.0355 0.2657 -0.0257 -0.0168 0.0155  18  LYS B CA  
2236 C  C   . LYS B 18  ? 0.1739 0.0141 0.2412 -0.0035 -0.0009 0.0425  18  LYS B C   
2237 O  O   . LYS B 18  ? 0.1898 0.0090 0.3838 -0.0173 0.0353  0.0161  18  LYS B O   
2238 C  CB  . LYS B 18  ? 0.2417 0.0848 0.2476 -0.0760 -0.0244 0.0384  18  LYS B CB  
2239 C  CG  . LYS B 18  ? 0.2657 0.2613 0.2683 -0.1131 -0.0425 0.1147  18  LYS B CG  
2240 C  CD  . LYS B 18  ? 0.4157 0.1676 0.2763 -0.0586 -0.0760 0.0999  18  LYS B CD  
2241 C  CE  . LYS B 18  ? 0.3463 0.5468 0.2027 -0.1155 -0.1213 0.1444  18  LYS B CE  
2242 N  NZ  . LYS B 18  ? 0.4440 0.7900 0.2597 -0.2658 -0.1044 -0.0141 18  LYS B NZ  
2243 N  N   . TYR B 19  ? 0.1881 0.0152 0.1772 -0.0268 -0.0175 0.0314  19  TYR B N   
2244 C  CA  . TYR B 19  ? 0.1621 0.0136 0.2479 -0.0234 0.0032  -0.0304 19  TYR B CA  
2245 C  C   . TYR B 19  ? 0.2351 0.0066 0.2400 -0.0013 -0.0084 -0.0083 19  TYR B C   
2246 O  O   . TYR B 19  ? 0.1844 0.0115 0.2158 -0.0251 -0.0257 0.0219  19  TYR B O   
2247 C  CB  . TYR B 19  ? 0.1981 0.0176 0.2447 0.0137  -0.0151 -0.0505 19  TYR B CB  
2248 C  CG  . TYR B 19  ? 0.1886 0.0068 0.2666 -0.0078 -0.0167 -0.0052 19  TYR B CG  
2249 C  CD1 . TYR B 19  ? 0.1649 0.0616 0.2358 -0.0240 -0.0306 0.0011  19  TYR B CD1 
2250 C  CD2 . TYR B 19  ? 0.2045 0.0207 0.2381 -0.0446 -0.0416 0.0403  19  TYR B CD2 
2251 C  CE1 . TYR B 19  ? 0.2527 0.0533 0.2338 -0.0284 -0.0666 -0.0087 19  TYR B CE1 
2252 C  CE2 . TYR B 19  ? 0.2226 0.0076 0.2308 -0.0148 -0.0634 -0.0036 19  TYR B CE2 
2253 C  CZ  . TYR B 19  ? 0.2351 0.0150 0.2480 -0.0055 -0.0725 0.0021  19  TYR B CZ  
2254 O  OH  . TYR B 19  ? 0.2780 0.1711 0.2465 0.0296  -0.0827 0.0147  19  TYR B OH  
2255 N  N   . PRO B 20  ? 0.2379 0.0096 0.2152 -0.0158 -0.0261 0.0230  20  PRO B N   
2256 C  CA  . PRO B 20  ? 0.2507 0.0103 0.2425 -0.0305 -0.0529 0.0133  20  PRO B CA  
2257 C  C   . PRO B 20  ? 0.2268 0.0214 0.1824 -0.0502 -0.0310 -0.0178 20  PRO B C   
2258 O  O   . PRO B 20  ? 0.2457 0.0092 0.2827 -0.0151 -0.0486 -0.0196 20  PRO B O   
2259 C  CB  . PRO B 20  ? 0.3395 0.0329 0.2670 0.0081  -0.0882 -0.0194 20  PRO B CB  
2260 C  CG  . PRO B 20  ? 0.4190 0.0841 0.2083 0.0077  -0.0658 0.0118  20  PRO B CG  
2261 C  CD  . PRO B 20  ? 0.3185 0.0067 0.2271 -0.0037 -0.0572 0.0090  20  PRO B CD  
2262 N  N   . SER B 21  ? 0.2226 0.0102 0.1625 -0.0291 -0.0252 0.0024  21  SER B N   
2263 C  CA  . SER B 21  ? 0.2337 0.0085 0.1879 -0.0222 0.0072  0.0017  21  SER B CA  
2264 C  C   . SER B 21  ? 0.2161 0.0327 0.1600 0.0168  0.0027  0.0183  21  SER B C   
2265 O  O   . SER B 21  ? 0.2277 0.0140 0.1913 -0.0411 -0.0285 0.0073  21  SER B O   
2266 C  CB  . SER B 21  ? 0.2257 0.0077 0.2552 -0.0176 0.0198  -0.0053 21  SER B CB  
2267 O  OG  . SER B 21  ? 0.2777 0.0313 0.2618 -0.0005 -0.0063 -0.0398 21  SER B OG  
2268 N  N   . CYS B 22  ? 0.2051 0.0071 0.1506 -0.0067 -0.0273 -0.0082 22  CYS B N   
2269 C  CA  . CYS B 22  ? 0.1712 0.0074 0.1496 0.0015  -0.0317 -0.0122 22  CYS B CA  
2270 C  C   . CYS B 22  ? 0.1887 0.0076 0.1750 0.0123  -0.0452 0.0058  22  CYS B C   
2271 O  O   . CYS B 22  ? 0.1830 0.0091 0.2191 0.0147  -0.0467 0.0137  22  CYS B O   
2272 C  CB  . CYS B 22  ? 0.1920 0.0104 0.1477 -0.0270 -0.0271 0.0000  22  CYS B CB  
2273 S  SG  . CYS B 22  ? 0.1949 0.0065 0.1711 0.0045  -0.0371 0.0031  22  CYS B SG  
2274 N  N   . GLY B 23  ? 0.1447 0.0164 0.2593 -0.0369 -0.0678 0.0244  23  GLY B N   
2275 C  CA  . GLY B 23  ? 0.1941 0.0180 0.1919 0.0336  -0.0641 -0.0281 23  GLY B CA  
2276 C  C   . GLY B 23  ? 0.2138 0.0071 0.2042 0.0090  -0.0357 -0.0106 23  GLY B C   
2277 O  O   . GLY B 23  ? 0.2386 0.0403 0.2371 0.0035  -0.0697 0.0074  23  GLY B O   
2278 N  N   . GLY B 24  ? 0.2128 0.0121 0.2228 -0.0222 -0.0168 -0.0250 24  GLY B N   
2279 C  CA  . GLY B 24  ? 0.2796 0.0742 0.2153 -0.1137 -0.0131 -0.0039 24  GLY B CA  
2280 C  C   . GLY B 24  ? 0.4238 0.0906 0.1905 -0.1728 -0.0413 -0.0307 24  GLY B C   
2281 O  O   . GLY B 24  ? 0.4659 0.0670 0.1879 -0.0922 -0.0716 0.0207  24  GLY B O   
2282 N  N   . LEU B 25  ? 0.4377 0.0419 0.1894 -0.0702 -0.0003 0.0504  25  LEU B N   
2283 C  CA  . LEU B 25  ? 0.4236 0.0954 0.2074 -0.1708 -0.0525 0.0779  25  LEU B CA  
2284 C  C   . LEU B 25  ? 0.3704 0.1130 0.1356 -0.0810 -0.0661 0.0188  25  LEU B C   
2285 O  O   . LEU B 25  ? 0.3115 0.0798 0.1604 -0.0560 -0.0147 0.0033  25  LEU B O   
2286 C  CB  . LEU B 25  ? 0.6330 0.3079 0.2222 -0.2679 -0.0553 0.0485  25  LEU B CB  
2287 C  CG  . LEU B 25  ? 0.6703 0.3269 0.4001 -0.2193 -0.1195 -0.0847 25  LEU B CG  
2288 C  CD1 . LEU B 25  ? 0.9755 0.1868 0.3788 -0.1967 -0.0699 -0.0427 25  LEU B CD1 
2289 C  CD2 . LEU B 25  ? 0.7381 0.4734 0.5264 -0.0829 -0.1078 0.0990  25  LEU B CD2 
2290 N  N   . LEU B 26  ? 0.3761 0.1128 0.1952 -0.1586 -0.0346 0.0011  26  LEU B N   
2291 C  CA  . LEU B 26  ? 0.3208 0.0398 0.1905 -0.0979 -0.0312 -0.0093 26  LEU B CA  
2292 C  C   . LEU B 26  ? 0.2414 0.0252 0.1789 -0.0659 -0.0136 -0.0040 26  LEU B C   
2293 O  O   . LEU B 26  ? 0.1789 0.0367 0.2225 -0.0204 0.0208  0.0003  26  LEU B O   
2294 C  CB  . LEU B 26  ? 0.4385 0.1682 0.2495 -0.0181 0.0352  -0.0216 26  LEU B CB  
2295 C  CG  . LEU B 26  ? 0.5173 0.1525 0.3067 0.0533  0.0886  0.0615  26  LEU B CG  
2296 C  CD1 . LEU B 26  ? 0.5671 0.2749 0.3776 0.1624  0.1474  0.0241  26  LEU B CD1 
2297 C  CD2 . LEU B 26  ? 0.4823 0.0900 0.2661 -0.0103 0.0336  0.0103  26  LEU B CD2 
2298 N  N   . GLN B 27  ? 0.2103 0.0135 0.1508 -0.0158 -0.0398 0.0316  27  GLN B N   
2299 C  CA  . GLN B 27  ? 0.1485 0.0223 0.1449 -0.0211 -0.0316 0.0040  27  GLN B CA  
2300 C  C   . GLN B 27  ? 0.2101 0.0086 0.1360 0.0061  -0.0175 0.0160  27  GLN B C   
2301 O  O   . GLN B 27  ? 0.1694 0.0191 0.1888 0.0103  -0.0403 0.0389  27  GLN B O   
2302 C  CB  . GLN B 27  ? 0.1694 0.0127 0.1833 -0.0322 -0.0404 0.0084  27  GLN B CB  
2303 C  CG  . GLN B 27  ? 0.1961 0.0101 0.1249 -0.0250 -0.0505 0.0135  27  GLN B CG  
2304 C  CD  . GLN B 27  ? 0.1719 0.0167 0.1440 -0.0213 -0.0420 -0.0256 27  GLN B CD  
2305 O  OE1 . GLN B 27  ? 0.1879 0.0069 0.1524 0.0034  -0.0339 -0.0098 27  GLN B OE1 
2306 N  NE2 . GLN B 27  ? 0.2246 0.0169 0.1682 -0.0281 -0.0113 -0.0319 27  GLN B NE2 
2307 N  N   . SER B 28  ? 0.1187 0.0225 0.1408 -0.0181 -0.0073 -0.0411 28  SER B N   
2308 C  CA  . SER B 28  ? 0.1220 0.0119 0.1256 -0.0081 -0.0302 -0.0214 28  SER B CA  
2309 C  C   . SER B 28  ? 0.1394 0.0647 0.1251 -0.0088 -0.0105 0.0109  28  SER B C   
2310 O  O   . SER B 28  ? 0.0873 0.0688 0.1282 -0.0118 0.0020  0.0190  28  SER B O   
2311 C  CB  . SER B 28  ? 0.1278 0.0081 0.1377 -0.0075 -0.0211 -0.0117 28  SER B CB  
2312 O  OG  . SER B 28  ? 0.1560 0.0244 0.1349 0.0026  0.0004  -0.0220 28  SER B OG  
2313 N  N   . PRO B 29  ? 0.1207 0.0174 0.1573 0.0122  0.0022  0.0388  29  PRO B N   
2314 C  CA  . PRO B 29  ? 0.1302 0.0104 0.1498 -0.0107 -0.0369 0.0237  29  PRO B CA  
2315 C  C   . PRO B 29  ? 0.1060 0.0256 0.1449 0.0034  -0.0143 0.0281  29  PRO B C   
2316 O  O   . PRO B 29  ? 0.1666 0.0089 0.1639 -0.0146 -0.0499 0.0180  29  PRO B O   
2317 C  CB  . PRO B 29  ? 0.1581 0.0118 0.1341 0.0207  -0.0036 0.0095  29  PRO B CB  
2318 C  CG  . PRO B 29  ? 0.1484 0.0067 0.1830 0.0042  0.0028  -0.0064 29  PRO B CG  
2319 C  CD  . PRO B 29  ? 0.1174 0.0064 0.1439 0.0030  -0.0271 0.0005  29  PRO B CD  
2320 N  N   . ILE B 30  ? 0.1290 0.0308 0.1173 -0.0166 -0.0258 0.0228  30  ILE B N   
2321 C  CA  . ILE B 30  ? 0.1358 0.0126 0.1329 -0.0028 -0.0103 0.0282  30  ILE B CA  
2322 C  C   . ILE B 30  ? 0.1049 0.0186 0.1557 0.0051  -0.0031 0.0015  30  ILE B C   
2323 O  O   . ILE B 30  ? 0.1238 0.0126 0.1763 0.0021  -0.0165 0.0319  30  ILE B O   
2324 C  CB  . ILE B 30  ? 0.1796 0.0103 0.1421 -0.0194 -0.0065 0.0166  30  ILE B CB  
2325 C  CG1 . ILE B 30  ? 0.1574 0.0098 0.1516 0.0220  0.0204  0.0088  30  ILE B CG1 
2326 C  CG2 . ILE B 30  ? 0.2248 0.0074 0.1037 0.0078  -0.0244 0.0079  30  ILE B CG2 
2327 C  CD1 . ILE B 30  ? 0.1952 0.0844 0.1604 0.0300  0.0193  0.0287  30  ILE B CD1 
2328 N  N   . ASP B 31  ? 0.1092 0.0088 0.1489 0.0151  0.0034  0.0063  31  ASP B N   
2329 C  CA  . ASP B 31  ? 0.1323 0.0074 0.1709 0.0064  0.0341  0.0129  31  ASP B CA  
2330 C  C   . ASP B 31  ? 0.1438 0.0590 0.1500 -0.0220 0.0107  0.0162  31  ASP B C   
2331 O  O   . ASP B 31  ? 0.1791 0.0468 0.1736 -0.0286 -0.0193 0.0301  31  ASP B O   
2332 C  CB  . ASP B 31  ? 0.1238 0.0136 0.1800 0.0117  0.0375  0.0289  31  ASP B CB  
2333 C  CG  . ASP B 31  ? 0.1864 0.0189 0.1642 0.0051  -0.0192 -0.0168 31  ASP B CG  
2334 O  OD1 . ASP B 31  ? 0.1865 0.0593 0.1747 0.0051  -0.0545 0.0033  31  ASP B OD1 
2335 O  OD2 . ASP B 31  ? 0.2370 0.0592 0.1936 0.0229  -0.0375 0.0118  31  ASP B OD2 
2336 N  N   . LEU B 32  ? 0.1395 0.0144 0.1743 -0.0124 0.0268  0.0220  32  LEU B N   
2337 C  CA  . LEU B 32  ? 0.2338 0.0320 0.1356 -0.0326 -0.0301 0.0557  32  LEU B CA  
2338 C  C   . LEU B 32  ? 0.2095 0.0310 0.1625 -0.0315 -0.0145 0.0163  32  LEU B C   
2339 O  O   . LEU B 32  ? 0.3588 0.0108 0.1674 -0.0076 -0.0565 0.0267  32  LEU B O   
2340 C  CB  . LEU B 32  ? 0.2056 0.0090 0.1825 -0.0200 -0.0016 0.0110  32  LEU B CB  
2341 C  CG  . LEU B 32  ? 0.1918 0.0390 0.2117 -0.0144 -0.0289 0.0067  32  LEU B CG  
2342 C  CD1 . LEU B 32  ? 0.1676 0.1148 0.2248 -0.0061 -0.0447 0.0441  32  LEU B CD1 
2343 C  CD2 . LEU B 32  ? 0.2768 0.1399 0.1923 -0.0237 -0.0400 -0.0243 32  LEU B CD2 
2344 N  N   . HIS B 33  ? 0.2372 0.0262 0.1695 -0.0207 -0.0184 0.0556  33  HIS B N   
2345 C  CA  . HIS B 33  ? 0.2004 0.0546 0.1758 -0.0002 0.0038  0.0620  33  HIS B CA  
2346 C  C   . HIS B 33  ? 0.1773 0.0398 0.1627 -0.0069 0.0097  0.0472  33  HIS B C   
2347 O  O   . HIS B 33  ? 0.1798 0.0830 0.1591 0.0200  0.0110  0.0340  33  HIS B O   
2348 C  CB  . HIS B 33  ? 0.1891 0.0619 0.1876 -0.0027 0.0052  0.0577  33  HIS B CB  
2349 C  CG  . HIS B 33  ? 0.2146 0.1331 0.1338 -0.0591 0.0095  0.0613  33  HIS B CG  
2350 N  ND1 . HIS B 33  ? 0.2915 0.1435 0.1947 -0.0829 -0.0850 0.0913  33  HIS B ND1 
2351 C  CD2 . HIS B 33  ? 0.1715 0.1312 0.1679 -0.0047 -0.0024 0.0527  33  HIS B CD2 
2352 C  CE1 . HIS B 33  ? 0.2982 0.2360 0.1417 -0.0744 -0.0714 0.0387  33  HIS B CE1 
2353 N  NE2 . HIS B 33  ? 0.1833 0.1549 0.1430 -0.0387 -0.0022 0.0305  33  HIS B NE2 
2354 N  N   . SER B 34  ? 0.1916 0.0540 0.2031 -0.0005 0.0038  0.0728  34  SER B N   
2355 C  CA  . SER B 34  ? 0.2016 0.0436 0.1934 0.0261  0.0223  0.0564  34  SER B CA  
2356 C  C   . SER B 34  ? 0.1654 0.1142 0.2092 0.0275  0.0232  0.0226  34  SER B C   
2357 O  O   . SER B 34  ? 0.1846 0.1126 0.1880 0.0168  0.0086  0.0455  34  SER B O   
2358 C  CB  . SER B 34  ? 0.2364 0.0408 0.2813 0.0218  -0.0055 0.0914  34  SER B CB  
2359 O  OG  . SER B 34  ? 0.2473 0.1413 0.3653 0.0305  -0.0124 0.0581  34  SER B OG  
2360 N  N   . ASP B 35  ? 0.1778 0.1209 0.1776 0.0199  -0.0378 0.0619  35  ASP B N   
2361 C  CA  . ASP B 35  ? 0.1464 0.1363 0.2290 0.0154  -0.0332 0.0336  35  ASP B CA  
2362 C  C   . ASP B 35  ? 0.1719 0.0848 0.2070 -0.0089 -0.0454 0.0206  35  ASP B C   
2363 O  O   . ASP B 35  ? 0.2314 0.1949 0.2042 0.0296  -0.0323 0.0059  35  ASP B O   
2364 C  CB  . ASP B 35  ? 0.1406 0.1888 0.3140 0.0187  -0.0088 0.0118  35  ASP B CB  
2365 C  CG  . ASP B 35  ? 0.1322 0.1649 0.2979 -0.0161 -0.0159 -0.0120 35  ASP B CG  
2366 O  OD1 . ASP B 35  ? 0.2016 0.1403 0.2469 0.0151  -0.0074 0.0580  35  ASP B OD1 
2367 O  OD2 . ASP B 35  ? 0.1810 0.2103 0.2487 -0.0057 -0.0249 0.0342  35  ASP B OD2 
2368 N  N   . ILE B 36  ? 0.1729 0.0803 0.2081 0.0220  -0.0303 0.0022  36  ILE B N   
2369 C  CA  . ILE B 36  ? 0.1933 0.0638 0.2044 0.0215  0.0104  0.0187  36  ILE B CA  
2370 C  C   . ILE B 36  ? 0.1701 0.0499 0.1707 0.0096  -0.0305 0.0091  36  ILE B C   
2371 O  O   . ILE B 36  ? 0.2117 0.1044 0.2046 0.0500  -0.0025 0.0077  36  ILE B O   
2372 C  CB  . ILE B 36  ? 0.2540 0.0784 0.2586 -0.0582 0.0243  0.0136  36  ILE B CB  
2373 C  CG1 . ILE B 36  ? 0.3170 0.0986 0.2110 0.0615  0.0465  0.1051  36  ILE B CG1 
2374 C  CG2 . ILE B 36  ? 0.2242 0.1908 0.3151 -0.0491 0.0662  0.0138  36  ILE B CG2 
2375 C  CD1 . ILE B 36  ? 0.2236 0.2799 0.3755 0.1280  0.0256  -0.0895 36  ILE B CD1 
2376 N  N   . LEU B 37  ? 0.1798 0.0519 0.1808 -0.0021 -0.0071 0.0348  37  LEU B N   
2377 C  CA  . LEU B 37  ? 0.1670 0.0793 0.1755 0.0159  -0.0066 0.0362  37  LEU B CA  
2378 C  C   . LEU B 37  ? 0.1581 0.1433 0.2127 0.0397  0.0234  0.0805  37  LEU B C   
2379 O  O   . LEU B 37  ? 0.2173 0.2360 0.2442 0.0559  -0.0065 0.1354  37  LEU B O   
2380 C  CB  . LEU B 37  ? 0.1922 0.0643 0.1981 0.0495  -0.0105 0.0311  37  LEU B CB  
2381 C  CG  . LEU B 37  ? 0.1452 0.0959 0.1755 0.0440  -0.0315 -0.0078 37  LEU B CG  
2382 C  CD1 . LEU B 37  ? 0.2026 0.1548 0.2928 -0.0306 -0.0806 -0.0666 37  LEU B CD1 
2383 C  CD2 . LEU B 37  ? 0.1821 0.1212 0.2109 0.0291  -0.0258 0.0653  37  LEU B CD2 
2384 N  N   . GLN B 38  ? 0.1482 0.1264 0.1816 0.0055  0.0259  0.0396  38  GLN B N   
2385 C  CA  . GLN B 38  ? 0.1631 0.1749 0.1963 0.0201  0.0462  0.0523  38  GLN B CA  
2386 C  C   . GLN B 38  ? 0.1715 0.1391 0.2071 0.0110  0.0079  0.1185  38  GLN B C   
2387 O  O   . GLN B 38  ? 0.1976 0.0832 0.1790 0.0201  0.0005  0.0630  38  GLN B O   
2388 C  CB  . GLN B 38  ? 0.1801 0.3679 0.1967 -0.0450 0.0256  -0.0401 38  GLN B CB  
2389 C  CG  . GLN B 38  ? 0.1980 0.4484 0.2396 -0.0845 0.0111  0.0221  38  GLN B CG  
2390 C  CD  . GLN B 38  ? 0.3860 0.4360 0.2351 0.0053  -0.0801 0.0361  38  GLN B CD  
2391 O  OE1 . GLN B 38  ? 0.4092 0.7875 0.3617 -0.0198 -0.0232 -0.0021 38  GLN B OE1 
2392 N  NE2 . GLN B 38  ? 0.4405 0.3730 0.4084 -0.0697 0.0491  0.0207  38  GLN B NE2 
2393 N  N   . TYR B 39  ? 0.2170 0.0882 0.1873 0.0143  0.0302  0.0564  39  TYR B N   
2394 C  CA  . TYR B 39  ? 0.2181 0.0239 0.2067 0.0411  0.0316  0.0494  39  TYR B CA  
2395 C  C   . TYR B 39  ? 0.2146 0.0586 0.1697 0.0539  0.0078  0.0368  39  TYR B C   
2396 O  O   . TYR B 39  ? 0.2285 0.0742 0.1823 0.0264  0.0117  0.0211  39  TYR B O   
2397 C  CB  . TYR B 39  ? 0.2283 0.0230 0.1889 0.0030  0.0418  0.0467  39  TYR B CB  
2398 C  CG  . TYR B 39  ? 0.2286 0.0553 0.1829 -0.0115 0.0334  0.0324  39  TYR B CG  
2399 C  CD1 . TYR B 39  ? 0.2318 0.0290 0.1931 -0.0050 0.0223  0.0333  39  TYR B CD1 
2400 C  CD2 . TYR B 39  ? 0.2387 0.0505 0.2236 -0.0283 0.0423  0.0741  39  TYR B CD2 
2401 C  CE1 . TYR B 39  ? 0.2453 0.0511 0.2436 0.0121  0.0487  0.0637  39  TYR B CE1 
2402 C  CE2 . TYR B 39  ? 0.2282 0.0471 0.2550 -0.0304 0.0133  0.0418  39  TYR B CE2 
2403 C  CZ  . TYR B 39  ? 0.2283 0.0705 0.2370 -0.0234 0.0287  0.0668  39  TYR B CZ  
2404 O  OH  . TYR B 39  ? 0.2152 0.0929 0.2633 -0.0248 0.0074  0.0374  39  TYR B OH  
2405 N  N   . ASP B 40  ? 0.1905 0.0480 0.1967 0.0465  0.0359  0.0370  40  ASP B N   
2406 C  CA  . ASP B 40  ? 0.1915 0.0147 0.2083 0.0348  0.0282  0.0241  40  ASP B CA  
2407 C  C   . ASP B 40  ? 0.1826 0.1096 0.1754 0.0150  0.0348  0.0518  40  ASP B C   
2408 O  O   . ASP B 40  ? 0.1733 0.0735 0.1981 0.0377  0.0285  0.0414  40  ASP B O   
2409 C  CB  . ASP B 40  ? 0.2902 0.0327 0.1911 0.0731  0.0478  0.0488  40  ASP B CB  
2410 C  CG  . ASP B 40  ? 0.3503 0.0794 0.1985 0.0548  0.0640  -0.0403 40  ASP B CG  
2411 O  OD1 . ASP B 40  ? 0.1882 0.1301 0.2740 0.0905  0.0212  -0.0400 40  ASP B OD1 
2412 O  OD2 . ASP B 40  ? 0.2933 0.0754 0.3441 0.0164  0.0018  -0.0705 40  ASP B OD2 
2413 N  N   . ALA B 41  ? 0.2042 0.0841 0.1931 -0.0109 0.0433  0.0427  41  ALA B N   
2414 C  CA  . ALA B 41  ? 0.1710 0.0886 0.1986 0.0201  0.0384  0.0680  41  ALA B CA  
2415 C  C   . ALA B 41  ? 0.1915 0.0749 0.2218 0.0293  0.0530  0.0501  41  ALA B C   
2416 O  O   . ALA B 41  ? 0.1999 0.1794 0.2444 0.0030  0.0591  -0.0047 41  ALA B O   
2417 C  CB  . ALA B 41  ? 0.2300 0.0979 0.2126 -0.0417 0.0293  0.0697  41  ALA B CB  
2418 N  N   A SER B 42  ? 0.2546 0.0722 0.2362 0.0318  0.0275  0.0544  42  SER B N   
2419 N  N   B SER B 42  ? 0.2390 0.0757 0.2329 0.0287  0.0357  0.0510  42  SER B N   
2420 C  CA  A SER B 42  ? 0.2390 0.1006 0.2292 0.0379  0.0174  0.0008  42  SER B CA  
2421 C  CA  B SER B 42  ? 0.2182 0.1128 0.2196 0.0359  0.0358  0.0095  42  SER B CA  
2422 C  C   A SER B 42  ? 0.2408 0.1388 0.2340 0.0486  0.0308  0.0053  42  SER B C   
2423 C  C   B SER B 42  ? 0.1915 0.1270 0.2360 0.0207  0.0234  0.0139  42  SER B C   
2424 O  O   A SER B 42  ? 0.2746 0.1693 0.2401 0.0845  0.0012  -0.0211 42  SER B O   
2425 O  O   B SER B 42  ? 0.2177 0.1362 0.3628 0.0405  -0.0184 -0.0199 42  SER B O   
2426 C  CB  A SER B 42  ? 0.2540 0.0886 0.2882 0.0179  -0.0062 -0.0017 42  SER B CB  
2427 C  CB  B SER B 42  ? 0.2148 0.1056 0.1873 0.0680  0.0368  0.0122  42  SER B CB  
2428 O  OG  A SER B 42  ? 0.1632 0.1940 0.2056 0.0226  -0.0301 -0.0337 42  SER B OG  
2429 O  OG  B SER B 42  ? 0.2877 0.1617 0.1416 0.0539  0.0632  -0.0325 42  SER B OG  
2430 N  N   . LEU B 43  ? 0.2509 0.0978 0.1746 0.0006  0.0288  -0.0005 43  LEU B N   
2431 C  CA  . LEU B 43  ? 0.1959 0.1176 0.1954 0.0029  0.0167  0.0249  43  LEU B CA  
2432 C  C   . LEU B 43  ? 0.2134 0.0835 0.2214 0.0304  -0.0001 0.0323  43  LEU B C   
2433 O  O   . LEU B 43  ? 0.2174 0.0796 0.2746 0.0081  -0.0016 0.0174  43  LEU B O   
2434 C  CB  . LEU B 43  ? 0.2265 0.0208 0.1697 0.0275  0.0133  -0.0069 43  LEU B CB  
2435 C  CG  . LEU B 43  ? 0.2164 0.0181 0.2181 0.0160  0.0217  0.0450  43  LEU B CG  
2436 C  CD1 . LEU B 43  ? 0.2254 0.0478 0.2293 0.0522  0.0100  0.0039  43  LEU B CD1 
2437 C  CD2 . LEU B 43  ? 0.1670 0.0238 0.2318 0.0251  0.0091  0.0245  43  LEU B CD2 
2438 N  N   . THR B 44  ? 0.2028 0.1315 0.2739 0.0008  0.0524  0.0356  44  THR B N   
2439 C  CA  . THR B 44  ? 0.1948 0.1715 0.2723 -0.0181 0.0411  0.0600  44  THR B CA  
2440 C  C   . THR B 44  ? 0.1356 0.1421 0.2924 -0.0238 -0.0003 0.0628  44  THR B C   
2441 O  O   . THR B 44  ? 0.1697 0.0929 0.3334 -0.0106 -0.0218 0.0840  44  THR B O   
2442 C  CB  . THR B 44  ? 0.1872 0.2660 0.3039 0.0188  0.0537  0.0932  44  THR B CB  
2443 O  OG1 . THR B 44  ? 0.2480 0.2701 0.4458 0.0662  0.0954  0.1483  44  THR B OG1 
2444 C  CG2 . THR B 44  ? 0.3394 0.2545 0.2336 -0.1254 0.0240  0.0436  44  THR B CG2 
2445 N  N   . PRO B 45  ? 0.1708 0.1245 0.2533 -0.0325 -0.0353 0.1046  45  PRO B N   
2446 C  CA  . PRO B 45  ? 0.1611 0.1747 0.2621 0.0161  -0.0390 0.0920  45  PRO B CA  
2447 C  C   . PRO B 45  ? 0.1269 0.1424 0.2565 0.0013  0.0017  0.0634  45  PRO B C   
2448 O  O   . PRO B 45  ? 0.1981 0.1548 0.3257 0.0373  0.0407  0.0969  45  PRO B O   
2449 C  CB  . PRO B 45  ? 0.2181 0.1685 0.3587 -0.0009 -0.0195 0.1046  45  PRO B CB  
2450 C  CG  . PRO B 45  ? 0.2901 0.2476 0.3032 -0.0070 -0.0222 0.1073  45  PRO B CG  
2451 C  CD  . PRO B 45  ? 0.2343 0.1640 0.2947 -0.0255 0.0367  0.1384  45  PRO B CD  
2452 N  N   . LEU B 46  ? 0.1646 0.1254 0.2203 0.0240  -0.0170 0.0432  46  LEU B N   
2453 C  CA  . LEU B 46  ? 0.1711 0.1316 0.2369 0.0185  -0.0247 0.0504  46  LEU B CA  
2454 C  C   . LEU B 46  ? 0.1492 0.1654 0.2152 0.0609  -0.0232 0.0127  46  LEU B C   
2455 O  O   . LEU B 46  ? 0.2052 0.1280 0.2715 0.0232  -0.0032 0.0321  46  LEU B O   
2456 C  CB  . LEU B 46  ? 0.1531 0.0444 0.2625 0.0030  -0.0125 0.0041  46  LEU B CB  
2457 C  CG  . LEU B 46  ? 0.1611 0.1555 0.2816 -0.0120 -0.0006 -0.0289 46  LEU B CG  
2458 C  CD1 . LEU B 46  ? 0.1854 0.1535 0.3017 -0.0071 -0.0097 0.0478  46  LEU B CD1 
2459 C  CD2 . LEU B 46  ? 0.3004 0.2868 0.3097 0.0403  -0.0488 -0.1188 46  LEU B CD2 
2460 N  N   . GLU B 47  ? 0.1674 0.0632 0.2415 0.0184  -0.0032 0.0644  47  GLU B N   
2461 C  CA  . GLU B 47  ? 0.2016 0.1800 0.1744 0.0083  -0.0124 0.0544  47  GLU B CA  
2462 C  C   . GLU B 47  ? 0.2380 0.1692 0.1773 0.0269  0.0188  0.0539  47  GLU B C   
2463 O  O   . GLU B 47  ? 0.1922 0.1740 0.2477 -0.0078 0.0380  0.0528  47  GLU B O   
2464 C  CB  . GLU B 47  ? 0.2016 0.1970 0.2155 -0.0059 0.0087  0.0981  47  GLU B CB  
2465 C  CG  . GLU B 47  ? 0.2283 0.3138 0.2816 -0.0071 0.0460  0.1842  47  GLU B CG  
2466 C  CD  . GLU B 47  ? 0.2653 0.4592 0.3952 0.0312  0.1158  0.1867  47  GLU B CD  
2467 O  OE1 . GLU B 47  ? 0.3195 0.5470 0.3389 0.1274  0.1045  0.1221  47  GLU B OE1 
2468 O  OE2 . GLU B 47  ? 0.3410 0.6456 0.4710 0.0620  0.0724  0.2066  47  GLU B OE2 
2469 N  N   . PHE B 48  ? 0.2157 0.0467 0.2173 0.0242  -0.0212 0.0473  48  PHE B N   
2470 C  CA  . PHE B 48  ? 0.1918 0.0538 0.2130 0.0174  0.0022  0.0417  48  PHE B CA  
2471 C  C   . PHE B 48  ? 0.1866 0.1324 0.1772 0.0192  -0.0046 0.0164  48  PHE B C   
2472 O  O   . PHE B 48  ? 0.2339 0.0942 0.3249 0.0421  -0.0802 -0.0142 48  PHE B O   
2473 C  CB  . PHE B 48  ? 0.1729 0.1069 0.2636 0.0376  0.0288  0.0440  48  PHE B CB  
2474 C  CG  . PHE B 48  ? 0.1962 0.0780 0.2699 0.0067  -0.0185 0.0539  48  PHE B CG  
2475 C  CD1 . PHE B 48  ? 0.1949 0.0222 0.2694 0.0212  -0.0003 0.0266  48  PHE B CD1 
2476 C  CD2 . PHE B 48  ? 0.2579 0.0920 0.2102 0.0513  0.0002  0.0758  48  PHE B CD2 
2477 C  CE1 . PHE B 48  ? 0.2081 0.0780 0.2142 0.0646  0.0493  0.1093  48  PHE B CE1 
2478 C  CE2 . PHE B 48  ? 0.2133 0.1301 0.2473 0.0379  0.0273  0.0730  48  PHE B CE2 
2479 C  CZ  . PHE B 48  ? 0.2141 0.0654 0.2690 0.0482  0.0469  0.0521  48  PHE B CZ  
2480 N  N   . GLN B 49  ? 0.1509 0.1164 0.2178 0.0076  0.0359  0.0337  49  GLN B N   
2481 C  CA  . GLN B 49  ? 0.1773 0.0765 0.2015 0.0241  0.0342  0.0215  49  GLN B CA  
2482 C  C   . GLN B 49  ? 0.1121 0.1076 0.2107 0.0176  0.0240  0.0477  49  GLN B C   
2483 O  O   . GLN B 49  ? 0.1549 0.1011 0.2228 -0.0029 0.0274  0.0307  49  GLN B O   
2484 C  CB  . GLN B 49  ? 0.2123 0.1252 0.1645 -0.0065 0.0218  0.0032  49  GLN B CB  
2485 C  CG  . GLN B 49  ? 0.2929 0.1552 0.2020 0.0061  0.0428  0.0423  49  GLN B CG  
2486 C  CD  . GLN B 49  ? 0.2318 0.2004 0.2689 0.0121  0.0187  0.1082  49  GLN B CD  
2487 O  OE1 . GLN B 49  ? 0.2547 0.1708 0.4737 -0.0096 -0.0703 0.0968  49  GLN B OE1 
2488 N  NE2 . GLN B 49  ? 0.2081 0.3412 0.3464 0.0069  0.0189  0.0622  49  GLN B NE2 
2489 N  N   . GLY B 50  ? 0.1679 0.0749 0.2173 0.0276  0.0098  0.0250  50  GLY B N   
2490 C  CA  . GLY B 50  ? 0.1643 0.1236 0.1732 0.0815  0.0322  0.0212  50  GLY B CA  
2491 C  C   . GLY B 50  ? 0.1265 0.0999 0.2031 0.0439  0.0300  0.0271  50  GLY B C   
2492 O  O   . GLY B 50  ? 0.1354 0.1458 0.2048 0.0204  0.0010  0.0506  50  GLY B O   
2493 N  N   . TYR B 51  ? 0.1020 0.0988 0.1988 0.0323  -0.0021 0.0356  51  TYR B N   
2494 C  CA  . TYR B 51  ? 0.0996 0.1080 0.2102 0.0053  -0.0068 0.0193  51  TYR B CA  
2495 C  C   . TYR B 51  ? 0.1189 0.0654 0.2138 0.0094  -0.0079 0.0320  51  TYR B C   
2496 O  O   . TYR B 51  ? 0.1514 0.0236 0.2253 0.0029  0.0106  -0.0006 51  TYR B O   
2497 C  CB  . TYR B 51  ? 0.1435 0.0746 0.2077 0.0001  -0.0200 0.0336  51  TYR B CB  
2498 C  CG  . TYR B 51  ? 0.1288 0.0505 0.1861 0.0074  -0.0009 0.0274  51  TYR B CG  
2499 C  CD1 . TYR B 51  ? 0.1451 0.0660 0.2124 -0.0012 0.0229  0.0024  51  TYR B CD1 
2500 C  CD2 . TYR B 51  ? 0.1257 0.0480 0.2313 0.0139  -0.0027 0.0423  51  TYR B CD2 
2501 C  CE1 . TYR B 51  ? 0.1428 0.0841 0.2034 0.0019  0.0150  0.0265  51  TYR B CE1 
2502 C  CE2 . TYR B 51  ? 0.1713 0.0267 0.1948 -0.0080 0.0120  0.0214  51  TYR B CE2 
2503 C  CZ  . TYR B 51  ? 0.1269 0.0566 0.2210 -0.0304 0.0082  -0.0125 51  TYR B CZ  
2504 O  OH  . TYR B 51  ? 0.1618 0.0600 0.2354 -0.0088 -0.0331 -0.0029 51  TYR B OH  
2505 N  N   . ASN B 52  ? 0.1171 0.0763 0.2092 0.0134  0.0029  0.0419  52  ASN B N   
2506 C  CA  . ASN B 52  ? 0.1514 0.0997 0.2308 -0.0258 -0.0398 0.0890  52  ASN B CA  
2507 C  C   . ASN B 52  ? 0.1401 0.1266 0.1905 0.0629  -0.0064 0.0380  52  ASN B C   
2508 O  O   . ASN B 52  ? 0.1166 0.1358 0.2779 0.0267  -0.0067 0.0673  52  ASN B O   
2509 C  CB  . ASN B 52  ? 0.2024 0.0868 0.2500 -0.0577 -0.0167 0.0585  52  ASN B CB  
2510 C  CG  . ASN B 52  ? 0.2038 0.1985 0.3120 -0.0680 -0.0422 0.0099  52  ASN B CG  
2511 O  OD1 . ASN B 52  ? 0.2442 0.3587 0.3292 -0.1127 -0.0199 0.0173  52  ASN B OD1 
2512 N  ND2 . ASN B 52  ? 0.1902 0.1683 0.4189 -0.0434 -0.0290 0.0216  52  ASN B ND2 
2513 N  N   . LEU B 53  ? 0.1927 0.0936 0.1617 0.0088  -0.0324 0.0186  53  LEU B N   
2514 C  CA  . LEU B 53  ? 0.1324 0.0875 0.2362 0.0022  -0.0168 0.0336  53  LEU B CA  
2515 C  C   . LEU B 53  ? 0.1254 0.1288 0.1549 0.0457  0.0179  -0.0217 53  LEU B C   
2516 O  O   . LEU B 53  ? 0.1502 0.1247 0.2065 0.0245  -0.0098 -0.0525 53  LEU B O   
2517 C  CB  . LEU B 53  ? 0.1312 0.0248 0.2583 -0.0006 -0.0362 0.0456  53  LEU B CB  
2518 C  CG  . LEU B 53  ? 0.1266 0.0974 0.2615 -0.0162 -0.0205 0.0036  53  LEU B CG  
2519 C  CD1 . LEU B 53  ? 0.1308 0.1247 0.3095 -0.0234 -0.0545 0.0908  53  LEU B CD1 
2520 C  CD2 . LEU B 53  ? 0.1913 0.1858 0.2433 0.0864  -0.0737 -0.0194 53  LEU B CD2 
2521 N  N   . SER B 54  ? 0.1074 0.1150 0.2283 0.0064  -0.0122 0.0260  54  SER B N   
2522 C  CA  . SER B 54  ? 0.1176 0.1767 0.1916 -0.0122 0.0020  0.0047  54  SER B CA  
2523 C  C   . SER B 54  ? 0.1305 0.1507 0.1778 -0.0368 0.0043  -0.0152 54  SER B C   
2524 O  O   . SER B 54  ? 0.1581 0.1434 0.1858 -0.0198 -0.0201 0.0451  54  SER B O   
2525 C  CB  . SER B 54  ? 0.1681 0.1421 0.1879 0.0062  -0.0181 0.0412  54  SER B CB  
2526 O  OG  . SER B 54  ? 0.1916 0.2178 0.1887 -0.0096 -0.0234 0.0115  54  SER B OG  
2527 N  N   . ALA B 55  ? 0.1969 0.1453 0.1908 -0.0264 -0.0381 -0.0008 55  ALA B N   
2528 C  CA  . ALA B 55  ? 0.1913 0.2166 0.1991 0.0122  -0.0564 -0.0611 55  ALA B CA  
2529 C  C   . ALA B 55  ? 0.1478 0.1882 0.2214 -0.0700 -0.0031 0.0046  55  ALA B C   
2530 O  O   . ALA B 55  ? 0.2924 0.3143 0.2077 -0.0162 0.0190  0.0073  55  ALA B O   
2531 C  CB  . ALA B 55  ? 0.3013 0.2504 0.2990 -0.0534 -0.0797 -0.0672 55  ALA B CB  
2532 N  N   . ASN B 56  ? 0.1294 0.2286 0.2247 -0.0122 -0.0419 0.0478  56  ASN B N   
2533 C  CA  . ASN B 56  ? 0.1426 0.1951 0.2850 0.0031  -0.0250 0.0374  56  ASN B CA  
2534 C  C   . ASN B 56  ? 0.0886 0.2128 0.2878 -0.0281 -0.0194 0.0469  56  ASN B C   
2535 O  O   . ASN B 56  ? 0.2392 0.3160 0.3107 -0.0165 -0.0820 0.1084  56  ASN B O   
2536 C  CB  . ASN B 56  ? 0.1336 0.2587 0.2443 -0.0469 -0.0495 0.0572  56  ASN B CB  
2537 C  CG  . ASN B 56  ? 0.1933 0.2514 0.3418 -0.0414 -0.0200 0.0256  56  ASN B CG  
2538 O  OD1 . ASN B 56  ? 0.2895 0.3294 0.3278 0.0163  -0.0609 -0.0069 56  ASN B OD1 
2539 N  ND2 . ASN B 56  ? 0.2500 0.4564 0.4737 -0.1163 0.0714  -0.1135 56  ASN B ND2 
2540 N  N   . LYS B 57  ? 0.0839 0.2274 0.2621 -0.0290 -0.0077 0.0705  57  LYS B N   
2541 C  CA  . LYS B 57  ? 0.1099 0.2144 0.1936 -0.0394 -0.0004 0.0725  57  LYS B CA  
2542 C  C   . LYS B 57  ? 0.1259 0.1376 0.2150 0.0000  0.0136  0.0559  57  LYS B C   
2543 O  O   . LYS B 57  ? 0.1507 0.1409 0.2548 -0.0005 -0.0227 0.0200  57  LYS B O   
2544 C  CB  . LYS B 57  ? 0.1437 0.2733 0.2261 0.0353  -0.0245 -0.0234 57  LYS B CB  
2545 C  CG  . LYS B 57  ? 0.1329 0.2984 0.2352 0.0352  0.0018  0.0452  57  LYS B CG  
2546 C  CD  . LYS B 57  ? 0.3068 0.4658 0.2711 0.0212  0.0861  -0.0569 57  LYS B CD  
2547 C  CE  . LYS B 57  ? 0.3651 0.4841 0.4492 0.0692  0.0893  -0.0406 57  LYS B CE  
2548 N  NZ  . LYS B 57  ? 0.3037 0.4864 0.4968 0.1080  0.0380  -0.0797 57  LYS B NZ  
2549 N  N   A GLN B 58  ? 0.1197 0.1812 0.2173 -0.0484 -0.0332 0.0696  58  GLN B N   
2550 N  N   B GLN B 58  ? 0.0988 0.1819 0.2182 -0.0516 -0.0403 0.0341  58  GLN B N   
2551 C  CA  A GLN B 58  ? 0.1287 0.1359 0.2284 -0.0228 -0.0223 0.0846  58  GLN B CA  
2552 C  CA  B GLN B 58  ? 0.0999 0.1571 0.2193 -0.0444 -0.0447 0.0364  58  GLN B CA  
2553 C  C   A GLN B 58  ? 0.1306 0.0787 0.1877 -0.0356 0.0111  0.0862  58  GLN B C   
2554 C  C   B GLN B 58  ? 0.1169 0.0809 0.2008 -0.0378 -0.0238 0.0468  58  GLN B C   
2555 O  O   A GLN B 58  ? 0.1212 0.1094 0.2349 0.0009  0.0139  0.0623  58  GLN B O   
2556 O  O   B GLN B 58  ? 0.1434 0.1200 0.2732 0.0762  -0.0096 0.0829  58  GLN B O   
2557 C  CB  A GLN B 58  ? 0.2455 0.1215 0.2478 -0.1181 0.0127  0.1107  58  GLN B CB  
2558 C  CB  B GLN B 58  ? 0.1707 0.2138 0.1949 -0.0476 -0.0418 0.0190  58  GLN B CB  
2559 C  CG  A GLN B 58  ? 0.3001 0.1638 0.2860 -0.0501 -0.0486 0.0122  58  GLN B CG  
2560 C  CG  B GLN B 58  ? 0.2010 0.2713 0.1561 -0.0558 -0.0725 0.0495  58  GLN B CG  
2561 C  CD  A GLN B 58  ? 0.3754 0.2497 0.2812 -0.0693 -0.1336 -0.0035 58  GLN B CD  
2562 C  CD  B GLN B 58  ? 0.2622 0.2890 0.1954 -0.0211 -0.0268 0.0961  58  GLN B CD  
2563 O  OE1 A GLN B 58  ? 0.4530 0.4047 0.1466 0.0329  -0.0871 0.0652  58  GLN B OE1 
2564 O  OE1 B GLN B 58  ? 0.3177 0.3076 0.4039 0.0714  0.0442  0.0520  58  GLN B OE1 
2565 N  NE2 A GLN B 58  ? 0.3502 0.2669 0.3434 0.0155  -0.1441 0.0606  58  GLN B NE2 
2566 N  NE2 B GLN B 58  ? 0.2627 0.2660 0.1146 -0.1017 -0.0222 0.1031  58  GLN B NE2 
2567 N  N   . PHE B 59  ? 0.1157 0.1557 0.2204 -0.0346 -0.0372 0.1091  59  PHE B N   
2568 C  CA  . PHE B 59  ? 0.1543 0.0658 0.2037 -0.0005 -0.0230 0.0599  59  PHE B CA  
2569 C  C   . PHE B 59  ? 0.1363 0.0719 0.1798 0.0139  -0.0221 0.0365  59  PHE B C   
2570 O  O   . PHE B 59  ? 0.1617 0.1110 0.1754 0.0041  -0.0139 0.0346  59  PHE B O   
2571 C  CB  . PHE B 59  ? 0.1582 0.0604 0.1934 0.0094  -0.0136 0.0525  59  PHE B CB  
2572 C  CG  . PHE B 59  ? 0.1606 0.0692 0.1976 0.0034  0.0100  0.0152  59  PHE B CG  
2573 C  CD1 . PHE B 59  ? 0.1676 0.0449 0.1909 -0.0075 0.0116  0.0432  59  PHE B CD1 
2574 C  CD2 . PHE B 59  ? 0.1441 0.0674 0.2455 0.0391  0.0122  -0.0044 59  PHE B CD2 
2575 C  CE1 . PHE B 59  ? 0.1697 0.0568 0.2009 -0.0006 0.0047  0.0361  59  PHE B CE1 
2576 C  CE2 . PHE B 59  ? 0.1272 0.1808 0.2614 -0.0088 -0.0089 0.0184  59  PHE B CE2 
2577 C  CZ  . PHE B 59  ? 0.1434 0.1146 0.2152 0.0281  -0.0069 0.0228  59  PHE B CZ  
2578 N  N   . LEU B 60  ? 0.1270 0.0762 0.2130 -0.0130 -0.0425 0.0485  60  LEU B N   
2579 C  CA  . LEU B 60  ? 0.1696 0.0800 0.2213 0.0406  0.0236  0.0535  60  LEU B CA  
2580 C  C   . LEU B 60  ? 0.1435 0.0776 0.1682 -0.0120 -0.0071 0.0460  60  LEU B C   
2581 O  O   . LEU B 60  ? 0.1934 0.0882 0.1797 -0.0013 -0.0329 0.0208  60  LEU B O   
2582 C  CB  . LEU B 60  ? 0.1882 0.0577 0.2619 0.0390  -0.0394 0.0680  60  LEU B CB  
2583 C  CG  . LEU B 60  ? 0.2896 0.0291 0.3243 -0.0018 -0.0396 0.0810  60  LEU B CG  
2584 C  CD1 . LEU B 60  ? 0.2775 0.2148 0.2861 0.0499  0.0212  0.0615  60  LEU B CD1 
2585 C  CD2 . LEU B 60  ? 0.1949 0.0668 0.3895 0.0185  -0.0506 0.0142  60  LEU B CD2 
2586 N  N   . LEU B 61  ? 0.1254 0.1516 0.1527 0.0020  -0.0185 0.0434  61  LEU B N   
2587 C  CA  . LEU B 61  ? 0.1125 0.1394 0.2101 -0.0132 -0.0094 0.0383  61  LEU B CA  
2588 C  C   . LEU B 61  ? 0.1287 0.1139 0.1822 -0.0166 -0.0527 0.0391  61  LEU B C   
2589 O  O   . LEU B 61  ? 0.1606 0.1699 0.1850 -0.0333 -0.0362 0.0741  61  LEU B O   
2590 C  CB  . LEU B 61  ? 0.1818 0.1988 0.1563 0.0348  -0.0321 0.0423  61  LEU B CB  
2591 C  CG  . LEU B 61  ? 0.1778 0.1322 0.1682 0.0100  -0.0034 0.0195  61  LEU B CG  
2592 C  CD1 . LEU B 61  ? 0.2035 0.1700 0.1963 0.0375  -0.0309 0.0446  61  LEU B CD1 
2593 C  CD2 . LEU B 61  ? 0.1683 0.1707 0.1791 -0.0136 0.0105  0.0069  61  LEU B CD2 
2594 N  N   A THR B 62  ? 0.1038 0.1523 0.2518 -0.0411 -0.0335 0.0454  62  THR B N   
2595 N  N   B THR B 62  ? 0.0866 0.1298 0.2056 0.0073  -0.0353 0.0366  62  THR B N   
2596 C  CA  A THR B 62  ? 0.1513 0.1239 0.2352 -0.0348 -0.0558 0.0620  62  THR B CA  
2597 C  CA  B THR B 62  ? 0.1315 0.0857 0.1712 0.0064  -0.0653 0.0311  62  THR B CA  
2598 C  C   A THR B 62  ? 0.1620 0.2049 0.2052 -0.0064 -0.0104 0.0908  62  THR B C   
2599 C  C   B THR B 62  ? 0.1319 0.1654 0.1797 0.0089  -0.0178 0.0629  62  THR B C   
2600 O  O   A THR B 62  ? 0.1315 0.2037 0.1732 0.0055  -0.0185 0.0600  62  THR B O   
2601 O  O   B THR B 62  ? 0.1088 0.1172 0.1907 0.0113  -0.0445 0.0270  62  THR B O   
2602 C  CB  A THR B 62  ? 0.2951 0.1660 0.3292 -0.0150 -0.0129 0.0182  62  THR B CB  
2603 C  CB  B THR B 62  ? 0.1801 0.1063 0.1823 0.0306  -0.0545 0.0209  62  THR B CB  
2604 O  OG1 A THR B 62  ? 0.3211 0.2799 0.3582 -0.0346 -0.1079 0.0204  62  THR B OG1 
2605 O  OG1 B THR B 62  ? 0.0999 0.0847 0.1855 0.0148  -0.0693 0.0062  62  THR B OG1 
2606 C  CG2 A THR B 62  ? 0.2899 0.1812 0.4235 -0.0124 0.0272  0.0751  62  THR B CG2 
2607 C  CG2 B THR B 62  ? 0.1949 0.1251 0.1841 0.0385  -0.0381 0.0044  62  THR B CG2 
2608 N  N   . ASN B 63  ? 0.1548 0.1221 0.2070 -0.0062 -0.0167 0.0672  63  ASN B N   
2609 C  CA  . ASN B 63  ? 0.1557 0.1126 0.1715 -0.0238 0.0110  0.0239  63  ASN B CA  
2610 C  C   . ASN B 63  ? 0.1258 0.1060 0.1778 -0.0159 0.0100  0.0251  63  ASN B C   
2611 O  O   . ASN B 63  ? 0.1983 0.1230 0.2353 0.0085  0.0230  0.0485  63  ASN B O   
2612 C  CB  . ASN B 63  ? 0.1521 0.1808 0.1550 -0.0067 -0.0232 -0.0031 63  ASN B CB  
2613 C  CG  . ASN B 63  ? 0.1592 0.1146 0.1798 0.0335  -0.0594 0.0381  63  ASN B CG  
2614 O  OD1 . ASN B 63  ? 0.1778 0.1628 0.1703 0.0108  -0.0383 -0.0125 63  ASN B OD1 
2615 N  ND2 . ASN B 63  ? 0.1690 0.0830 0.2229 -0.0301 0.0044  0.0359  63  ASN B ND2 
2616 N  N   . ASN B 64  ? 0.2072 0.0472 0.2065 -0.0135 0.0167  -0.0159 64  ASN B N   
2617 C  CA  . ASN B 64  ? 0.1815 0.0366 0.2161 0.0075  0.0095  -0.0193 64  ASN B CA  
2618 C  C   . ASN B 64  ? 0.1812 0.0744 0.3107 -0.0154 0.0214  0.0131  64  ASN B C   
2619 O  O   . ASN B 64  ? 0.2453 0.1056 0.2921 -0.0625 -0.0322 0.0524  64  ASN B O   
2620 C  CB  . ASN B 64  ? 0.2491 0.0627 0.2001 -0.0066 0.0039  -0.0118 64  ASN B CB  
2621 C  CG  . ASN B 64  ? 0.2085 0.1154 0.1690 -0.0018 -0.0040 -0.0322 64  ASN B CG  
2622 O  OD1 . ASN B 64  ? 0.2513 0.0532 0.2322 -0.0208 0.0460  -0.0186 64  ASN B OD1 
2623 N  ND2 . ASN B 64  ? 0.2535 0.2041 0.1861 0.0029  0.0149  -0.0326 64  ASN B ND2 
2624 N  N   . GLY B 65  ? 0.1473 0.1182 0.2178 -0.0043 0.0210  0.0162  65  GLY B N   
2625 C  CA  . GLY B 65  ? 0.1446 0.2707 0.2263 0.0042  0.0004  0.0591  65  GLY B CA  
2626 C  C   . GLY B 65  ? 0.1245 0.1988 0.2006 -0.0727 -0.0182 0.0483  65  GLY B C   
2627 O  O   . GLY B 65  ? 0.1597 0.2398 0.1783 -0.0064 0.0231  0.0281  65  GLY B O   
2628 N  N   . HIS B 66  ? 0.1758 0.2429 0.1830 -0.0254 -0.0057 0.0350  66  HIS B N   
2629 C  CA  . HIS B 66  ? 0.2008 0.0938 0.1712 -0.0335 0.0033  0.0125  66  HIS B CA  
2630 C  C   . HIS B 66  ? 0.2035 0.0403 0.2711 -0.0075 -0.0145 0.0078  66  HIS B C   
2631 O  O   . HIS B 66  ? 0.1984 0.1150 0.2268 0.0450  -0.0002 0.0209  66  HIS B O   
2632 C  CB  . HIS B 66  ? 0.2453 0.0830 0.1923 -0.0206 -0.0340 -0.0037 66  HIS B CB  
2633 C  CG  . HIS B 66  ? 0.2234 0.0635 0.1893 0.0124  -0.0405 0.0156  66  HIS B CG  
2634 N  ND1 . HIS B 66  ? 0.2230 0.1525 0.1699 -0.0347 -0.0289 0.0198  66  HIS B ND1 
2635 C  CD2 . HIS B 66  ? 0.2090 0.0622 0.2048 0.0152  -0.0340 0.0092  66  HIS B CD2 
2636 C  CE1 . HIS B 66  ? 0.2275 0.1492 0.1880 -0.0337 -0.0195 0.0105  66  HIS B CE1 
2637 N  NE2 . HIS B 66  ? 0.2472 0.1141 0.2572 -0.0377 -0.0352 -0.0016 66  HIS B NE2 
2638 N  N   . SER B 67  ? 0.2273 0.0435 0.2192 -0.0417 -0.0128 0.0351  67  SER B N   
2639 C  CA  . SER B 67  ? 0.2105 0.0111 0.2746 -0.0296 -0.0335 0.0171  67  SER B CA  
2640 C  C   . SER B 67  ? 0.2236 0.0200 0.3323 -0.0065 -0.0655 -0.0022 67  SER B C   
2641 O  O   . SER B 67  ? 0.2596 0.0356 0.4674 0.0193  -0.1430 0.0017  67  SER B O   
2642 C  CB  . SER B 67  ? 0.2279 0.0441 0.2567 -0.0077 0.0329  0.0462  67  SER B CB  
2643 O  OG  . SER B 67  ? 0.2128 0.0792 0.2996 -0.0408 0.0127  0.0309  67  SER B OG  
2644 N  N   . VAL B 68  ? 0.1805 0.0911 0.2106 -0.0118 -0.0847 -0.0158 68  VAL B N   
2645 C  CA  . VAL B 68  ? 0.1085 0.1599 0.1279 0.0475  -0.0030 -0.0055 68  VAL B CA  
2646 C  C   . VAL B 68  ? 0.1696 0.1801 0.1374 0.0146  0.0128  0.0047  68  VAL B C   
2647 O  O   . VAL B 68  ? 0.1180 0.2175 0.1913 -0.0006 -0.0035 0.0435  68  VAL B O   
2648 C  CB  . VAL B 68  ? 0.1628 0.1168 0.1155 0.0343  -0.0260 0.0122  68  VAL B CB  
2649 C  CG1 . VAL B 68  ? 0.1771 0.1624 0.1746 0.0558  -0.0595 -0.0037 68  VAL B CG1 
2650 C  CG2 . VAL B 68  ? 0.2561 0.1703 0.1959 -0.0543 0.0140  0.0146  68  VAL B CG2 
2651 N  N   . LYS B 69  ? 0.1212 0.1585 0.1306 -0.0073 -0.0233 0.0162  69  LYS B N   
2652 C  CA  . LYS B 69  ? 0.1032 0.0773 0.1570 0.0113  -0.0037 0.0039  69  LYS B CA  
2653 C  C   . LYS B 69  ? 0.1128 0.0841 0.1685 -0.0211 -0.0275 0.0637  69  LYS B C   
2654 O  O   . LYS B 69  ? 0.1449 0.1614 0.1487 -0.0154 -0.0369 0.0610  69  LYS B O   
2655 C  CB  . LYS B 69  ? 0.1593 0.0965 0.2189 -0.0105 -0.0486 -0.0317 69  LYS B CB  
2656 C  CG  . LYS B 69  ? 0.1494 0.0475 0.2144 0.0008  -0.0373 -0.0082 69  LYS B CG  
2657 C  CD  . LYS B 69  ? 0.1740 0.0231 0.2256 -0.0137 -0.0253 0.0107  69  LYS B CD  
2658 C  CE  . LYS B 69  ? 0.1643 0.0398 0.2092 -0.0010 -0.0301 -0.0104 69  LYS B CE  
2659 N  NZ  . LYS B 69  ? 0.2028 0.0367 0.2337 -0.0273 -0.0285 -0.0163 69  LYS B NZ  
2660 N  N   . LEU B 70  ? 0.1031 0.0498 0.1631 0.0077  0.0040  0.0395  70  LEU B N   
2661 C  CA  . LEU B 70  ? 0.1099 0.0083 0.1733 -0.0042 -0.0109 0.0175  70  LEU B CA  
2662 C  C   . LEU B 70  ? 0.1266 0.0518 0.1715 0.0081  -0.0290 0.0275  70  LEU B C   
2663 O  O   . LEU B 70  ? 0.1564 0.0273 0.1719 0.0012  -0.0248 0.0288  70  LEU B O   
2664 C  CB  . LEU B 70  ? 0.1308 0.0073 0.2191 0.0034  -0.0179 0.0130  70  LEU B CB  
2665 C  CG  . LEU B 70  ? 0.1283 0.0167 0.1766 -0.0190 -0.0278 0.0391  70  LEU B CG  
2666 C  CD1 . LEU B 70  ? 0.1692 0.0929 0.1807 0.0168  -0.0541 0.0206  70  LEU B CD1 
2667 C  CD2 . LEU B 70  ? 0.1830 0.0266 0.2376 -0.0499 -0.0142 0.0368  70  LEU B CD2 
2668 N  N   A ASN B 71  ? 0.1707 0.0489 0.1769 0.0291  0.0070  0.0425  71  ASN B N   
2669 N  N   B ASN B 71  ? 0.1758 0.0507 0.1765 0.0297  0.0087  0.0433  71  ASN B N   
2670 C  CA  A ASN B 71  ? 0.1564 0.0564 0.1902 0.0308  -0.0137 0.0352  71  ASN B CA  
2671 C  CA  B ASN B 71  ? 0.1555 0.0597 0.1956 0.0308  -0.0134 0.0295  71  ASN B CA  
2672 C  C   A ASN B 71  ? 0.1539 0.1040 0.1936 0.0295  0.0253  0.0113  71  ASN B C   
2673 C  C   B ASN B 71  ? 0.1584 0.1036 0.1959 0.0292  0.0253  0.0105  71  ASN B C   
2674 O  O   A ASN B 71  ? 0.2020 0.1128 0.2206 -0.0176 0.0027  0.0496  71  ASN B O   
2675 O  O   B ASN B 71  ? 0.2046 0.1133 0.2214 -0.0174 0.0009  0.0489  71  ASN B O   
2676 C  CB  A ASN B 71  ? 0.2137 0.0295 0.2461 0.0617  0.0259  0.0002  71  ASN B CB  
2677 C  CB  B ASN B 71  ? 0.2214 0.0305 0.2512 0.0626  0.0315  -0.0055 71  ASN B CB  
2678 C  CG  A ASN B 71  ? 0.2906 0.0171 0.3407 0.0293  -0.0501 0.0406  71  ASN B CG  
2679 C  CG  B ASN B 71  ? 0.3054 0.0721 0.4115 -0.0188 -0.0326 -0.0002 71  ASN B CG  
2680 O  OD1 A ASN B 71  ? 0.3430 0.1297 0.3132 -0.0321 -0.1029 0.1918  71  ASN B OD1 
2681 O  OD1 B ASN B 71  ? 0.3210 0.1269 0.4819 -0.0225 -0.0325 -0.0072 71  ASN B OD1 
2682 N  ND2 A ASN B 71  ? 0.2963 0.0888 0.4228 0.0944  -0.0424 0.1005  71  ASN B ND2 
2683 N  ND2 B ASN B 71  ? 0.4401 0.2943 0.4199 -0.0803 0.0398  -0.1195 71  ASN B ND2 
2684 N  N   . LEU B 72  ? 0.1579 0.0319 0.1841 0.0050  -0.0002 0.0440  72  LEU B N   
2685 C  CA  . LEU B 72  ? 0.1139 0.0285 0.1979 0.0119  0.0049  0.0155  72  LEU B CA  
2686 C  C   . LEU B 72  ? 0.1315 0.0785 0.2311 0.0308  0.0017  -0.0220 72  LEU B C   
2687 O  O   . LEU B 72  ? 0.1997 0.0914 0.1977 -0.0091 -0.0292 0.0040  72  LEU B O   
2688 C  CB  . LEU B 72  ? 0.1647 0.0425 0.1994 0.0394  -0.0234 -0.0024 72  LEU B CB  
2689 C  CG  . LEU B 72  ? 0.1573 0.0436 0.1674 0.0176  -0.0219 -0.0164 72  LEU B CG  
2690 C  CD1 . LEU B 72  ? 0.1478 0.0580 0.2130 -0.0166 -0.0414 0.0227  72  LEU B CD1 
2691 C  CD2 . LEU B 72  ? 0.1538 0.0480 0.2173 0.0198  -0.0497 -0.0141 72  LEU B CD2 
2692 N  N   . PRO B 73  ? 0.1306 0.0586 0.1927 0.0232  -0.0104 -0.0117 73  PRO B N   
2693 C  CA  . PRO B 73  ? 0.1883 0.0281 0.2144 0.0439  0.0017  -0.0201 73  PRO B CA  
2694 C  C   . PRO B 73  ? 0.1850 0.0721 0.2286 0.0432  0.0130  -0.0189 73  PRO B C   
2695 O  O   . PRO B 73  ? 0.1963 0.0811 0.2515 0.0326  0.0223  0.0017  73  PRO B O   
2696 C  CB  . PRO B 73  ? 0.1794 0.0357 0.2716 0.0425  0.0000  0.0049  73  PRO B CB  
2697 C  CG  . PRO B 73  ? 0.1671 0.0259 0.2769 0.0211  0.0034  0.0206  73  PRO B CG  
2698 C  CD  . PRO B 73  ? 0.1402 0.0751 0.2606 0.0001  -0.0317 -0.0160 73  PRO B CD  
2699 N  N   A SER B 74  ? 0.2778 0.0649 0.2241 0.0544  0.0262  -0.0142 74  SER B N   
2700 N  N   B SER B 74  ? 0.2907 0.0801 0.2098 0.0567  0.0392  -0.0179 74  SER B N   
2701 C  CA  A SER B 74  ? 0.2358 0.0844 0.2274 0.0330  0.0339  -0.0394 74  SER B CA  
2702 C  CA  B SER B 74  ? 0.2757 0.0701 0.2170 0.0411  0.0356  -0.0222 74  SER B CA  
2703 C  C   A SER B 74  ? 0.2667 0.1029 0.1825 0.0073  -0.0078 0.0070  74  SER B C   
2704 C  C   B SER B 74  ? 0.2304 0.0714 0.2511 0.0185  0.0010  -0.0199 74  SER B C   
2705 O  O   A SER B 74  ? 0.2972 0.1245 0.1819 -0.0420 0.0370  -0.0146 74  SER B O   
2706 O  O   B SER B 74  ? 0.1923 0.0550 0.2620 0.0746  0.0367  -0.0174 74  SER B O   
2707 C  CB  A SER B 74  ? 0.1893 0.0818 0.3203 0.0317  0.0109  -0.0577 74  SER B CB  
2708 C  CB  B SER B 74  ? 0.3263 0.0785 0.3025 0.0036  0.0081  -0.0873 74  SER B CB  
2709 O  OG  A SER B 74  ? 0.1850 0.0907 0.2983 0.0469  0.0305  -0.0686 74  SER B OG  
2710 O  OG  B SER B 74  ? 0.3726 0.1707 0.3934 -0.0548 0.0133  -0.0153 74  SER B OG  
2711 N  N   . ASP B 75  ? 0.1873 0.0915 0.2678 0.0348  0.0069  0.0237  75  ASP B N   
2712 C  CA  . ASP B 75  ? 0.1873 0.0977 0.3124 0.0394  0.0159  0.0275  75  ASP B CA  
2713 C  C   . ASP B 75  ? 0.1423 0.1340 0.2624 0.0520  0.0309  0.0678  75  ASP B C   
2714 O  O   . ASP B 75  ? 0.2037 0.1164 0.3406 0.0483  0.0723  0.0895  75  ASP B O   
2715 C  CB  . ASP B 75  ? 0.2406 0.1571 0.2552 0.0701  -0.0700 -0.0211 75  ASP B CB  
2716 C  CG  . ASP B 75  ? 0.3953 0.4749 0.2767 0.0275  -0.0165 -0.0241 75  ASP B CG  
2717 O  OD1 . ASP B 75  ? 0.3488 0.4631 0.3579 -0.0879 0.0400  0.0111  75  ASP B OD1 
2718 O  OD2 . ASP B 75  ? 0.4135 0.6740 0.7426 -0.1227 -0.2518 -0.0719 75  ASP B OD2 
2719 N  N   . MET B 76  ? 0.1532 0.1128 0.2250 0.0613  0.0212  0.0311  76  MET B N   
2720 C  CA  . MET B 76  ? 0.1439 0.0572 0.2117 0.0196  0.0020  0.0042  76  MET B CA  
2721 C  C   . MET B 76  ? 0.1868 0.0505 0.1861 0.0449  0.0157  0.0051  76  MET B C   
2722 O  O   . MET B 76  ? 0.1846 0.0581 0.2640 0.0285  0.0110  0.0551  76  MET B O   
2723 C  CB  . MET B 76  ? 0.1514 0.0715 0.2139 0.0348  0.0104  0.0140  76  MET B CB  
2724 C  CG  . MET B 76  ? 0.1857 0.0428 0.2103 0.0368  0.0071  -0.0024 76  MET B CG  
2725 S  SD  . MET B 76  ? 0.1708 0.0636 0.1967 0.0152  0.0030  -0.0072 76  MET B SD  
2726 C  CE  . MET B 76  ? 0.1908 0.0137 0.2080 0.0355  0.0051  0.0109  76  MET B CE  
2727 N  N   . HIS B 77  ? 0.1981 0.0724 0.1708 0.0462  0.0200  0.0158  77  HIS B N   
2728 C  CA  . HIS B 77  ? 0.1902 0.0656 0.1987 0.0740  0.0198  0.0285  77  HIS B CA  
2729 C  C   . HIS B 77  ? 0.1295 0.0785 0.1604 0.0376  0.0099  0.0445  77  HIS B C   
2730 O  O   . HIS B 77  ? 0.2272 0.1053 0.1904 -0.0077 0.0068  -0.0047 77  HIS B O   
2731 C  CB  . HIS B 77  ? 0.1762 0.1081 0.2108 0.0430  0.0367  0.0036  77  HIS B CB  
2732 C  CG  . HIS B 77  ? 0.1722 0.1453 0.2418 0.0410  0.0423  0.0089  77  HIS B CG  
2733 N  ND1 . HIS B 77  ? 0.1706 0.1718 0.2437 0.0187  0.0269  -0.0261 77  HIS B ND1 
2734 C  CD2 . HIS B 77  ? 0.2622 0.1180 0.2503 0.0479  0.0366  0.0117  77  HIS B CD2 
2735 C  CE1 . HIS B 77  ? 0.1776 0.2010 0.2462 0.0545  0.0346  0.0004  77  HIS B CE1 
2736 N  NE2 . HIS B 77  ? 0.2700 0.2327 0.2493 0.0046  -0.0005 0.0179  77  HIS B NE2 
2737 N  N   . ILE B 78  ? 0.1636 0.0419 0.1876 0.0697  -0.0104 0.0182  78  ILE B N   
2738 C  CA  . ILE B 78  ? 0.1790 0.0508 0.1986 0.0783  -0.0291 0.0168  78  ILE B CA  
2739 C  C   . ILE B 78  ? 0.2103 0.1106 0.2151 0.0915  0.0190  0.0472  78  ILE B C   
2740 O  O   . ILE B 78  ? 0.2281 0.1166 0.2319 0.0424  0.0271  0.0370  78  ILE B O   
2741 C  CB  . ILE B 78  ? 0.1652 0.1379 0.2212 0.1037  -0.0010 0.0540  78  ILE B CB  
2742 C  CG1 . ILE B 78  ? 0.1909 0.2304 0.2369 0.0332  0.0396  0.0592  78  ILE B CG1 
2743 C  CG2 . ILE B 78  ? 0.2360 0.1280 0.2564 0.0897  -0.0317 0.0636  78  ILE B CG2 
2744 C  CD1 . ILE B 78  ? 0.1872 0.0827 0.2964 0.0517  0.0475  0.0734  78  ILE B CD1 
2745 N  N   . GLN B 79  ? 0.2256 0.1003 0.2241 0.0883  -0.0036 0.0290  79  GLN B N   
2746 C  CA  . GLN B 79  ? 0.2308 0.1451 0.2261 0.0988  0.0162  0.0384  79  GLN B CA  
2747 C  C   . GLN B 79  ? 0.3131 0.1344 0.2308 0.0982  -0.0133 0.0540  79  GLN B C   
2748 O  O   . GLN B 79  ? 0.2908 0.1022 0.2909 0.0732  -0.0649 -0.0006 79  GLN B O   
2749 C  CB  . GLN B 79  ? 0.3037 0.2736 0.2509 -0.0258 0.0600  0.0548  79  GLN B CB  
2750 C  CG  . GLN B 79  ? 0.3358 0.3688 0.2754 -0.0562 0.0877  0.0577  79  GLN B CG  
2751 C  CD  . GLN B 79  ? 0.5237 0.4963 0.2745 -0.0308 0.0644  -0.0081 79  GLN B CD  
2752 O  OE1 . GLN B 79  ? 0.3811 0.4556 0.3751 -0.1441 0.0637  0.0522  79  GLN B OE1 
2753 N  NE2 . GLN B 79  ? 0.4616 0.6675 0.2962 -0.3072 0.0307  0.0675  79  GLN B NE2 
2754 N  N   . GLY B 80  ? 0.2609 0.1879 0.2329 0.0505  -0.0282 0.0402  80  GLY B N   
2755 C  CA  . GLY B 80  ? 0.2820 0.1270 0.2010 0.0537  -0.0284 0.0196  80  GLY B CA  
2756 C  C   . GLY B 80  ? 0.2423 0.1907 0.2105 0.0227  0.0273  0.0532  80  GLY B C   
2757 O  O   . GLY B 80  ? 0.2728 0.3124 0.2810 0.0994  -0.0099 0.0806  80  GLY B O   
2758 N  N   . LEU B 81  ? 0.2363 0.1908 0.2419 0.0257  0.0098  0.0847  81  LEU B N   
2759 C  CA  . LEU B 81  ? 0.2852 0.2065 0.1837 0.0911  -0.0158 0.0168  81  LEU B CA  
2760 C  C   . LEU B 81  ? 0.2487 0.2497 0.2582 0.1135  0.0089  -0.0242 81  LEU B C   
2761 O  O   . LEU B 81  ? 0.2600 0.2625 0.2514 0.0440  -0.0053 -0.0070 81  LEU B O   
2762 C  CB  . LEU B 81  ? 0.3046 0.1532 0.2103 0.1090  0.0359  -0.0072 81  LEU B CB  
2763 C  CG  . LEU B 81  ? 0.2697 0.1298 0.1916 0.1091  0.0234  0.0126  81  LEU B CG  
2764 C  CD1 . LEU B 81  ? 0.3231 0.1243 0.1974 0.0961  0.0400  0.0170  81  LEU B CD1 
2765 C  CD2 . LEU B 81  ? 0.2734 0.1822 0.2662 0.0903  0.0079  0.1011  81  LEU B CD2 
2766 N  N   . GLN B 82  ? 0.3310 0.2547 0.2430 0.1123  -0.0249 -0.0155 82  GLN B N   
2767 C  CA  . GLN B 82  ? 0.2799 0.2912 0.3050 0.1008  -0.0176 -0.0535 82  GLN B CA  
2768 C  C   . GLN B 82  ? 0.3023 0.2378 0.1656 0.0889  0.0044  -0.0490 82  GLN B C   
2769 O  O   . GLN B 82  ? 0.4149 0.2621 0.1962 0.1606  0.0023  -0.0641 82  GLN B O   
2770 C  CB  . GLN B 82  ? 0.3007 0.2798 0.2825 0.0649  -0.0362 -0.0086 82  GLN B CB  
2771 C  CG  . GLN B 82  ? 0.2920 0.2331 0.3134 0.0477  -0.0249 -0.0003 82  GLN B CG  
2772 C  CD  . GLN B 82  ? 0.3746 0.3689 0.4780 -0.1209 0.0119  0.0759  82  GLN B CD  
2773 O  OE1 . GLN B 82  ? 0.5655 0.3180 0.6100 -0.0752 0.0362  0.0002  82  GLN B OE1 
2774 N  NE2 . GLN B 82  ? 0.3672 0.2411 0.3836 -0.0554 -0.1009 0.1531  82  GLN B NE2 
2775 N  N   . SER B 83  ? 0.2321 0.1729 0.2072 0.0638  -0.0094 -0.0061 83  SER B N   
2776 C  CA  . SER B 83  ? 0.2180 0.1713 0.2478 0.0256  -0.0592 0.0006  83  SER B CA  
2777 C  C   . SER B 83  ? 0.1794 0.1254 0.2133 0.0335  0.0044  0.0015  83  SER B C   
2778 O  O   . SER B 83  ? 0.2272 0.1665 0.2114 0.0776  -0.0114 -0.0151 83  SER B O   
2779 C  CB  . SER B 83  ? 0.2115 0.1761 0.3437 -0.0533 -0.1243 -0.0416 83  SER B CB  
2780 O  OG  . SER B 83  ? 0.3638 0.2162 0.2644 -0.0181 -0.0631 -0.0411 83  SER B OG  
2781 N  N   . ARG B 84  ? 0.1821 0.1877 0.1925 0.0086  -0.0103 0.0291  84  ARG B N   
2782 C  CA  . ARG B 84  ? 0.1658 0.1873 0.1869 0.0290  0.0074  -0.0040 84  ARG B CA  
2783 C  C   . ARG B 84  ? 0.1965 0.1391 0.1995 0.0822  0.0535  -0.0234 84  ARG B C   
2784 O  O   . ARG B 84  ? 0.2740 0.1258 0.2225 0.0862  0.0111  0.0003  84  ARG B O   
2785 C  CB  . ARG B 84  ? 0.1855 0.1300 0.2575 0.0476  0.0027  -0.0106 84  ARG B CB  
2786 C  CG  . ARG B 84  ? 0.2066 0.2178 0.2656 0.0857  0.0311  0.0002  84  ARG B CG  
2787 C  CD  . ARG B 84  ? 0.2284 0.2898 0.2759 0.1729  0.0073  0.0226  84  ARG B CD  
2788 N  NE  . ARG B 84  ? 0.2657 0.1760 0.3212 0.0826  -0.0140 0.0407  84  ARG B NE  
2789 C  CZ  . ARG B 84  ? 0.2692 0.2121 0.2232 0.0412  -0.0024 -0.0534 84  ARG B CZ  
2790 N  NH1 . ARG B 84  ? 0.2325 0.3438 0.4066 0.1263  0.0304  0.0485  84  ARG B NH1 
2791 N  NH2 . ARG B 84  ? 0.2893 0.2712 0.2382 0.0127  0.0005  0.0044  84  ARG B NH2 
2792 N  N   . TYR B 85  ? 0.1537 0.1967 0.1546 0.0856  0.0179  -0.0500 85  TYR B N   
2793 C  CA  . TYR B 85  ? 0.1800 0.0911 0.1672 0.0672  0.0034  -0.0298 85  TYR B CA  
2794 C  C   . TYR B 85  ? 0.1925 0.0654 0.1672 0.0436  0.0073  -0.0262 85  TYR B C   
2795 O  O   . TYR B 85  ? 0.2042 0.0617 0.2171 0.0148  -0.0231 -0.0041 85  TYR B O   
2796 C  CB  . TYR B 85  ? 0.1660 0.1643 0.1591 0.0719  -0.0022 -0.0386 85  TYR B CB  
2797 C  CG  . TYR B 85  ? 0.1986 0.0530 0.1760 0.0612  -0.0133 -0.0104 85  TYR B CG  
2798 C  CD1 . TYR B 85  ? 0.2207 0.0626 0.1729 0.0452  -0.0138 -0.0201 85  TYR B CD1 
2799 C  CD2 . TYR B 85  ? 0.2487 0.0247 0.2311 0.0595  0.0098  -0.0265 85  TYR B CD2 
2800 C  CE1 . TYR B 85  ? 0.2267 0.0638 0.2046 -0.0032 -0.0002 -0.0519 85  TYR B CE1 
2801 C  CE2 . TYR B 85  ? 0.2221 0.0875 0.2170 0.0683  0.0221  -0.0276 85  TYR B CE2 
2802 C  CZ  . TYR B 85  ? 0.2030 0.0723 0.2085 0.0174  0.0227  -0.0388 85  TYR B CZ  
2803 O  OH  . TYR B 85  ? 0.2730 0.1276 0.2304 0.0366  -0.0348 -0.0367 85  TYR B OH  
2804 N  N   . SER B 86  ? 0.2072 0.0897 0.2022 0.0704  0.0293  0.0149  86  SER B N   
2805 C  CA  . SER B 86  ? 0.1925 0.0801 0.1773 0.0749  0.0160  0.0088  86  SER B CA  
2806 C  C   . SER B 86  ? 0.1747 0.0469 0.1622 0.0348  -0.0016 -0.0022 86  SER B C   
2807 O  O   . SER B 86  ? 0.1791 0.0496 0.2034 0.0281  0.0027  -0.0161 86  SER B O   
2808 C  CB  . SER B 86  ? 0.2099 0.0981 0.1962 0.0890  0.0152  0.0274  86  SER B CB  
2809 O  OG  . SER B 86  ? 0.1649 0.1553 0.2502 0.0612  0.0118  -0.0096 86  SER B OG  
2810 N  N   . ALA B 87  ? 0.1941 0.0660 0.1505 0.0441  0.0044  0.0032  87  ALA B N   
2811 C  CA  . ALA B 87  ? 0.1665 0.0516 0.1785 0.0166  0.0047  -0.0201 87  ALA B CA  
2812 C  C   . ALA B 87  ? 0.1305 0.0645 0.1516 0.0154  0.0243  -0.0157 87  ALA B C   
2813 O  O   . ALA B 87  ? 0.1650 0.0740 0.2223 0.0300  0.0186  -0.0185 87  ALA B O   
2814 C  CB  . ALA B 87  ? 0.2072 0.0665 0.2834 -0.0013 -0.0087 -0.0640 87  ALA B CB  
2815 N  N   . THR B 88  ? 0.1243 0.0296 0.1779 0.0296  0.0131  -0.0082 88  THR B N   
2816 C  CA  . THR B 88  ? 0.1660 0.0485 0.1976 0.0001  0.0083  0.0036  88  THR B CA  
2817 C  C   . THR B 88  ? 0.1031 0.0557 0.1933 0.0288  -0.0108 0.0070  88  THR B C   
2818 O  O   . THR B 88  ? 0.1588 0.0437 0.1985 0.0254  -0.0223 0.0089  88  THR B O   
2819 C  CB  . THR B 88  ? 0.1894 0.0205 0.2265 0.0250  -0.0446 0.0037  88  THR B CB  
2820 O  OG1 . THR B 88  ? 0.3488 0.0679 0.2788 0.0379  -0.0988 0.0536  88  THR B OG1 
2821 C  CG2 . THR B 88  ? 0.1604 0.0859 0.3057 0.0048  -0.0174 0.0009  88  THR B CG2 
2822 N  N   . GLN B 89  ? 0.0975 0.0106 0.1924 -0.0032 0.0181  0.0268  89  GLN B N   
2823 C  CA  . GLN B 89  ? 0.1732 0.0095 0.1872 0.0102  0.0131  0.0221  89  GLN B CA  
2824 C  C   . GLN B 89  ? 0.1327 0.0072 0.1421 0.0096  -0.0201 0.0027  89  GLN B C   
2825 O  O   . GLN B 89  ? 0.1431 0.0121 0.1492 0.0217  -0.0136 0.0040  89  GLN B O   
2826 C  CB  . GLN B 89  ? 0.1294 0.0100 0.2343 -0.0074 -0.0219 0.0281  89  GLN B CB  
2827 C  CG  . GLN B 89  ? 0.1306 0.0077 0.2273 -0.0099 -0.0030 0.0119  89  GLN B CG  
2828 C  CD  . GLN B 89  ? 0.1370 0.0327 0.1821 0.0312  -0.0381 -0.0071 89  GLN B CD  
2829 O  OE1 . GLN B 89  ? 0.1847 0.0285 0.2088 0.0395  0.0093  0.0010  89  GLN B OE1 
2830 N  NE2 . GLN B 89  ? 0.1726 0.0823 0.2148 -0.0064 0.0082  0.0427  89  GLN B NE2 
2831 N  N   . LEU B 90  ? 0.1155 0.0369 0.1514 0.0109  0.0172  -0.0033 90  LEU B N   
2832 C  CA  . LEU B 90  ? 0.1103 0.0068 0.1502 -0.0064 -0.0063 0.0037  90  LEU B CA  
2833 C  C   . LEU B 90  ? 0.1024 0.0125 0.1381 0.0001  -0.0201 0.0038  90  LEU B C   
2834 O  O   . LEU B 90  ? 0.1281 0.0096 0.1497 0.0169  -0.0228 0.0079  90  LEU B O   
2835 C  CB  . LEU B 90  ? 0.1294 0.0100 0.1747 -0.0212 -0.0270 0.0044  90  LEU B CB  
2836 C  CG  . LEU B 90  ? 0.1323 0.0147 0.1682 -0.0210 -0.0141 0.0024  90  LEU B CG  
2837 C  CD1 . LEU B 90  ? 0.1388 0.0172 0.1595 0.0055  -0.0187 0.0190  90  LEU B CD1 
2838 C  CD2 . LEU B 90  ? 0.1227 0.0220 0.2056 -0.0242 0.0055  -0.0137 90  LEU B CD2 
2839 N  N   . HIS B 91  ? 0.1015 0.0063 0.1710 -0.0001 -0.0118 -0.0029 91  HIS B N   
2840 C  CA  . HIS B 91  ? 0.0997 0.0065 0.1623 0.0033  -0.0045 0.0031  91  HIS B CA  
2841 C  C   . HIS B 91  ? 0.0981 0.0096 0.1316 0.0164  0.0039  0.0068  91  HIS B C   
2842 O  O   . HIS B 91  ? 0.1495 0.0084 0.1481 0.0065  -0.0061 0.0159  91  HIS B O   
2843 C  CB  . HIS B 91  ? 0.1082 0.0089 0.1358 -0.0149 -0.0075 0.0083  91  HIS B CB  
2844 C  CG  . HIS B 91  ? 0.1190 0.0082 0.1447 -0.0117 -0.0169 0.0112  91  HIS B CG  
2845 N  ND1 . HIS B 91  ? 0.1239 0.0247 0.1374 0.0075  -0.0217 0.0270  91  HIS B ND1 
2846 C  CD2 . HIS B 91  ? 0.1315 0.0148 0.1582 -0.0296 -0.0492 0.0255  91  HIS B CD2 
2847 C  CE1 . HIS B 91  ? 0.1283 0.0121 0.1372 -0.0067 -0.0212 0.0276  91  HIS B CE1 
2848 N  NE2 . HIS B 91  ? 0.1247 0.0122 0.1600 -0.0064 -0.0256 0.0300  91  HIS B NE2 
2849 N  N   . LEU B 92  ? 0.1017 0.0112 0.1500 0.0217  0.0004  0.0012  92  LEU B N   
2850 C  CA  . LEU B 92  ? 0.0990 0.0122 0.1592 0.0186  0.0108  -0.0162 92  LEU B CA  
2851 C  C   . LEU B 92  ? 0.1218 0.0313 0.1481 0.0043  0.0222  0.0302  92  LEU B C   
2852 O  O   . LEU B 92  ? 0.1218 0.0160 0.1678 0.0027  -0.0089 0.0237  92  LEU B O   
2853 C  CB  . LEU B 92  ? 0.1349 0.0365 0.1920 -0.0197 -0.0029 -0.0411 92  LEU B CB  
2854 C  CG  . LEU B 92  ? 0.1071 0.0285 0.1675 -0.0006 -0.0150 -0.0417 92  LEU B CG  
2855 C  CD1 . LEU B 92  ? 0.1275 0.1094 0.2683 0.0131  -0.0500 -0.0237 92  LEU B CD1 
2856 C  CD2 . LEU B 92  ? 0.1922 0.0110 0.2455 -0.0055 -0.0219 -0.0154 92  LEU B CD2 
2857 N  N   . HIS B 93  ? 0.1021 0.0472 0.1464 0.0016  -0.0070 0.0016  93  HIS B N   
2858 C  CA  . HIS B 93  ? 0.0895 0.0703 0.0923 0.0230  0.0087  -0.0053 93  HIS B CA  
2859 C  C   . HIS B 93  ? 0.0858 0.0119 0.1272 -0.0043 -0.0015 0.0255  93  HIS B C   
2860 O  O   . HIS B 93  ? 0.1380 0.0130 0.1501 -0.0066 0.0124  0.0294  93  HIS B O   
2861 C  CB  . HIS B 93  ? 0.1416 0.0295 0.1045 0.0184  0.0040  -0.0018 93  HIS B CB  
2862 C  CG  . HIS B 93  ? 0.1298 0.0108 0.1294 0.0228  -0.0154 0.0027  93  HIS B CG  
2863 N  ND1 . HIS B 93  ? 0.1085 0.0319 0.1143 0.0050  -0.0026 0.0449  93  HIS B ND1 
2864 C  CD2 . HIS B 93  ? 0.1627 0.0230 0.1137 0.0319  0.0021  -0.0162 93  HIS B CD2 
2865 C  CE1 . HIS B 93  ? 0.1013 0.0690 0.1270 0.0206  -0.0319 0.0138  93  HIS B CE1 
2866 N  NE2 . HIS B 93  ? 0.1164 0.0271 0.1004 0.0453  -0.0089 -0.0175 93  HIS B NE2 
2867 N  N   . TRP B 94  ? 0.1026 0.0180 0.1142 0.0201  0.0091  0.0124  94  TRP B N   
2868 C  CA  . TRP B 94  ? 0.1036 0.0222 0.1058 -0.0005 0.0103  -0.0010 94  TRP B CA  
2869 C  C   . TRP B 94  ? 0.0988 0.0365 0.1144 -0.0052 -0.0027 0.0211  94  TRP B C   
2870 O  O   . TRP B 94  ? 0.0895 0.0311 0.1500 -0.0085 -0.0078 0.0318  94  TRP B O   
2871 C  CB  . TRP B 94  ? 0.1311 0.0145 0.1354 -0.0135 -0.0168 0.0237  94  TRP B CB  
2872 C  CG  . TRP B 94  ? 0.1173 0.0105 0.1473 0.0084  0.0056  0.0226  94  TRP B CG  
2873 C  CD1 . TRP B 94  ? 0.1471 0.0076 0.1239 0.0109  0.0036  0.0076  94  TRP B CD1 
2874 C  CD2 . TRP B 94  ? 0.1270 0.0110 0.1106 0.0174  -0.0086 0.0117  94  TRP B CD2 
2875 N  NE1 . TRP B 94  ? 0.1136 0.0129 0.1740 0.0228  0.0230  0.0220  94  TRP B NE1 
2876 C  CE2 . TRP B 94  ? 0.1137 0.0264 0.1223 0.0304  0.0052  0.0201  94  TRP B CE2 
2877 C  CE3 . TRP B 94  ? 0.1076 0.0190 0.1499 0.0251  -0.0117 0.0072  94  TRP B CE3 
2878 C  CZ2 . TRP B 94  ? 0.1347 0.0172 0.1700 0.0354  0.0163  0.0176  94  TRP B CZ2 
2879 C  CZ3 . TRP B 94  ? 0.1554 0.0189 0.1306 0.0432  0.0143  0.0069  94  TRP B CZ3 
2880 C  CH2 . TRP B 94  ? 0.1288 0.0445 0.1460 0.0283  0.0052  0.0263  94  TRP B CH2 
2881 N  N   . GLY B 95  ? 0.1239 0.0469 0.1345 0.0041  0.0129  0.0186  95  GLY B N   
2882 C  CA  . GLY B 95  ? 0.1230 0.0606 0.1442 0.0083  0.0148  0.0240  95  GLY B CA  
2883 C  C   . GLY B 95  ? 0.1234 0.0769 0.1094 0.0219  -0.0425 -0.0122 95  GLY B C   
2884 O  O   . GLY B 95  ? 0.1341 0.0870 0.1269 0.0210  0.0119  0.0367  95  GLY B O   
2885 N  N   . ASN B 96  ? 0.1355 0.0575 0.1361 -0.0084 0.0296  0.0097  96  ASN B N   
2886 C  CA  . ASN B 96  ? 0.1295 0.1110 0.1262 0.0162  0.0171  0.0055  96  ASN B CA  
2887 C  C   . ASN B 96  ? 0.1676 0.0976 0.1484 0.0287  0.0243  0.0216  96  ASN B C   
2888 O  O   . ASN B 96  ? 0.1857 0.0733 0.1420 -0.0004 0.0068  0.0133  96  ASN B O   
2889 C  CB  . ASN B 96  ? 0.1550 0.1033 0.1834 0.0057  0.0346  0.0514  96  ASN B CB  
2890 C  CG  . ASN B 96  ? 0.1205 0.0929 0.2795 -0.0193 0.0791  0.0092  96  ASN B CG  
2891 O  OD1 . ASN B 96  ? 0.2315 0.1568 0.3797 -0.0429 0.1454  -0.0507 96  ASN B OD1 
2892 N  ND2 . ASN B 96  ? 0.1875 0.0531 0.3862 0.0221  -0.0094 0.0087  96  ASN B ND2 
2893 N  N   . PRO B 97  ? 0.1527 0.1397 0.1381 0.0633  0.0071  0.0271  97  PRO B N   
2894 C  CA  . PRO B 97  ? 0.1798 0.1352 0.1740 0.0499  0.0001  0.0156  97  PRO B CA  
2895 C  C   . PRO B 97  ? 0.1301 0.1207 0.1807 0.0209  0.0330  0.0099  97  PRO B C   
2896 O  O   . PRO B 97  ? 0.2268 0.1182 0.2538 -0.0086 0.0293  -0.0026 97  PRO B O   
2897 C  CB  . PRO B 97  ? 0.2284 0.2376 0.1649 0.1100  0.0161  0.0098  97  PRO B CB  
2898 C  CG  . PRO B 97  ? 0.2133 0.2103 0.1823 0.0871  0.0153  0.0243  97  PRO B CG  
2899 C  CD  . PRO B 97  ? 0.1780 0.1990 0.1869 0.0847  -0.0060 0.0767  97  PRO B CD  
2900 N  N   . ASN B 98  ? 0.1103 0.1643 0.1428 0.0325  0.0192  0.0242  98  ASN B N   
2901 C  CA  . ASN B 98  ? 0.1186 0.1301 0.1833 0.0181  0.0293  0.0423  98  ASN B CA  
2902 C  C   . ASN B 98  ? 0.1712 0.1211 0.1815 0.0063  0.0598  0.0604  98  ASN B C   
2903 O  O   . ASN B 98  ? 0.2585 0.2520 0.2342 0.1110  0.0342  0.0578  98  ASN B O   
2904 C  CB  . ASN B 98  ? 0.1611 0.0817 0.1743 -0.0053 0.0487  0.0052  98  ASN B CB  
2905 C  CG  . ASN B 98  ? 0.1744 0.1119 0.1715 0.0591  0.0181  0.0084  98  ASN B CG  
2906 O  OD1 . ASN B 98  ? 0.2657 0.0872 0.2077 0.0319  0.0129  0.0270  98  ASN B OD1 
2907 N  ND2 . ASN B 98  ? 0.2383 0.1287 0.2248 -0.0096 0.0375  0.0461  98  ASN B ND2 
2908 N  N   . ASP B 99  ? 0.1746 0.1399 0.1409 -0.0065 0.0447  0.0281  99  ASP B N   
2909 C  CA  . ASP B 99  ? 0.1819 0.1139 0.1531 -0.0040 0.0220  0.0203  99  ASP B CA  
2910 C  C   . ASP B 99  ? 0.1866 0.1222 0.1582 0.0055  0.0252  0.0063  99  ASP B C   
2911 O  O   . ASP B 99  ? 0.1492 0.0677 0.1370 0.0058  0.0055  0.0406  99  ASP B O   
2912 C  CB  . ASP B 99  ? 0.1895 0.1688 0.1805 -0.0256 -0.0221 0.0296  99  ASP B CB  
2913 C  CG  . ASP B 99  ? 0.2137 0.2340 0.2132 -0.0100 -0.0747 0.0657  99  ASP B CG  
2914 O  OD1 . ASP B 99  ? 0.2904 0.2870 0.2376 0.0076  -0.0333 0.0945  99  ASP B OD1 
2915 O  OD2 . ASP B 99  ? 0.3225 0.3847 0.3045 -0.0983 -0.1701 0.0460  99  ASP B OD2 
2916 N  N   . PRO B 100 ? 0.1609 0.0437 0.1452 0.0430  0.0076  -0.0135 100 PRO B N   
2917 C  CA  . PRO B 100 ? 0.1318 0.0435 0.1686 0.0069  -0.0116 0.0128  100 PRO B CA  
2918 C  C   . PRO B 100 ? 0.1760 0.0480 0.1779 -0.0082 -0.0047 0.0311  100 PRO B C   
2919 O  O   . PRO B 100 ? 0.2138 0.0345 0.1846 -0.0303 0.0337  -0.0199 100 PRO B O   
2920 C  CB  . PRO B 100 ? 0.1985 0.0319 0.1952 0.0026  0.0043  -0.0205 100 PRO B CB  
2921 C  CG  . PRO B 100 ? 0.1900 0.0241 0.1963 -0.0055 0.0099  -0.0219 100 PRO B CG  
2922 C  CD  . PRO B 100 ? 0.2040 0.0253 0.1567 0.0107  0.0359  -0.0054 100 PRO B CD  
2923 N  N   . HIS B 101 ? 0.1791 0.0701 0.1351 0.0052  0.0005  0.0039  101 HIS B N   
2924 C  CA  . HIS B 101 ? 0.1818 0.0473 0.1517 0.0212  0.0038  -0.0201 101 HIS B CA  
2925 C  C   . HIS B 101 ? 0.1408 0.0435 0.1503 -0.0137 0.0332  -0.0168 101 HIS B C   
2926 O  O   . HIS B 101 ? 0.1891 0.1419 0.2940 -0.0234 -0.0457 -0.0253 101 HIS B O   
2927 C  CB  . HIS B 101 ? 0.1549 0.1430 0.1646 0.0226  -0.0124 0.0006  101 HIS B CB  
2928 C  CG  . HIS B 101 ? 0.1895 0.0803 0.2552 0.0149  -0.0443 0.0392  101 HIS B CG  
2929 N  ND1 . HIS B 101 ? 0.2161 0.0909 0.3614 0.0350  -0.0173 0.0671  101 HIS B ND1 
2930 C  CD2 . HIS B 101 ? 0.1737 0.0301 0.2606 0.0502  -0.0411 0.0238  101 HIS B CD2 
2931 C  CE1 . HIS B 101 ? 0.2812 0.0598 0.4750 0.0403  0.0074  0.0502  101 HIS B CE1 
2932 N  NE2 . HIS B 101 ? 0.3650 0.0433 0.4257 0.0122  -0.0006 0.0041  101 HIS B NE2 
2933 N  N   . GLY B 102 ? 0.1678 0.0381 0.1638 -0.0129 0.0206  -0.0026 102 GLY B N   
2934 C  CA  . GLY B 102 ? 0.1333 0.0264 0.1388 -0.0271 0.0114  0.0075  102 GLY B CA  
2935 C  C   . GLY B 102 ? 0.0985 0.0353 0.1694 0.0106  0.0013  0.0303  102 GLY B C   
2936 O  O   . GLY B 102 ? 0.1482 0.0122 0.1602 -0.0076 0.0196  -0.0058 102 GLY B O   
2937 N  N   . SER B 103 ? 0.1327 0.0064 0.1352 -0.0040 0.0060  -0.0012 103 SER B N   
2938 C  CA  . SER B 103 ? 0.1080 0.0145 0.1471 -0.0194 0.0081  0.0237  103 SER B CA  
2939 C  C   . SER B 103 ? 0.1322 0.0195 0.1680 -0.0355 0.0124  0.0189  103 SER B C   
2940 O  O   . SER B 103 ? 0.1252 0.0380 0.1911 0.0022  0.0089  -0.0044 103 SER B O   
2941 C  CB  . SER B 103 ? 0.1271 0.0155 0.1478 -0.0182 -0.0239 0.0332  103 SER B CB  
2942 O  OG  . SER B 103 ? 0.1309 0.0162 0.1500 -0.0015 -0.0309 0.0021  103 SER B OG  
2943 N  N   . GLU B 104 ? 0.1414 0.0074 0.1413 0.0069  -0.0334 0.0081  104 GLU B N   
2944 C  CA  . GLU B 104 ? 0.1557 0.0101 0.1379 -0.0159 0.0020  -0.0140 104 GLU B CA  
2945 C  C   . GLU B 104 ? 0.1585 0.0102 0.1482 -0.0149 -0.0270 -0.0158 104 GLU B C   
2946 O  O   . GLU B 104 ? 0.1542 0.0075 0.1545 -0.0022 -0.0038 0.0131  104 GLU B O   
2947 C  CB  . GLU B 104 ? 0.1459 0.0534 0.1356 0.0245  -0.0186 0.0222  104 GLU B CB  
2948 C  CG  . GLU B 104 ? 0.1988 0.0230 0.1376 0.0557  -0.0140 0.0039  104 GLU B CG  
2949 C  CD  . GLU B 104 ? 0.1221 0.0084 0.1116 0.0149  0.0055  -0.0036 104 GLU B CD  
2950 O  OE1 . GLU B 104 ? 0.1235 0.0064 0.1992 -0.0022 0.0187  -0.0040 104 GLU B OE1 
2951 O  OE2 . GLU B 104 ? 0.1273 0.0173 0.1460 0.0121  -0.0034 0.0073  104 GLU B OE2 
2952 N  N   . HIS B 105 ? 0.1832 0.0127 0.1227 0.0044  -0.0140 0.0052  105 HIS B N   
2953 C  CA  . HIS B 105 ? 0.1323 0.0101 0.1549 0.0190  -0.0232 0.0076  105 HIS B CA  
2954 C  C   . HIS B 105 ? 0.1618 0.0127 0.1604 0.0131  -0.0236 -0.0164 105 HIS B C   
2955 O  O   . HIS B 105 ? 0.1735 0.0088 0.1629 -0.0087 -0.0347 0.0191  105 HIS B O   
2956 C  CB  . HIS B 105 ? 0.1337 0.0117 0.1790 0.0209  -0.0087 0.0168  105 HIS B CB  
2957 C  CG  . HIS B 105 ? 0.1252 0.0084 0.1614 0.0032  -0.0212 -0.0162 105 HIS B CG  
2958 N  ND1 . HIS B 105 ? 0.1237 0.0069 0.1729 0.0038  -0.0045 -0.0088 105 HIS B ND1 
2959 C  CD2 . HIS B 105 ? 0.1477 0.0065 0.1525 -0.0032 0.0026  0.0038  105 HIS B CD2 
2960 C  CE1 . HIS B 105 ? 0.1361 0.0075 0.1368 0.0093  -0.0255 0.0060  105 HIS B CE1 
2961 N  NE2 . HIS B 105 ? 0.1707 0.0072 0.1551 0.0067  -0.0325 0.0082  105 HIS B NE2 
2962 N  N   . THR B 106 ? 0.1531 0.0098 0.1683 0.0227  -0.0142 -0.0011 106 THR B N   
2963 C  CA  . THR B 106 ? 0.1509 0.0262 0.1981 0.0491  -0.0179 0.0189  106 THR B CA  
2964 C  C   . THR B 106 ? 0.1566 0.0478 0.1266 0.0234  -0.0447 -0.0019 106 THR B C   
2965 O  O   . THR B 106 ? 0.1927 0.0243 0.1463 0.0242  -0.0535 0.0054  106 THR B O   
2966 C  CB  . THR B 106 ? 0.1665 0.0674 0.1398 0.0120  0.0006  -0.0297 106 THR B CB  
2967 O  OG1 . THR B 106 ? 0.1663 0.0477 0.1676 0.0286  -0.0122 -0.0430 106 THR B OG1 
2968 C  CG2 . THR B 106 ? 0.1333 0.1036 0.1755 0.0354  0.0102  0.0158  106 THR B CG2 
2969 N  N   . VAL B 107 ? 0.2220 0.0335 0.1995 0.0228  -0.0357 0.0210  107 VAL B N   
2970 C  CA  . VAL B 107 ? 0.2267 0.0766 0.2333 0.0052  -0.0724 0.0569  107 VAL B CA  
2971 C  C   . VAL B 107 ? 0.2013 0.0805 0.2223 0.0050  -0.0425 0.0106  107 VAL B C   
2972 O  O   . VAL B 107 ? 0.2586 0.0469 0.2077 0.0416  -0.0482 0.0289  107 VAL B O   
2973 C  CB  . VAL B 107 ? 0.2321 0.0379 0.2527 0.0055  -0.0776 0.0640  107 VAL B CB  
2974 C  CG1 . VAL B 107 ? 0.3711 0.0541 0.2746 -0.0361 -0.0474 0.0812  107 VAL B CG1 
2975 C  CG2 . VAL B 107 ? 0.2869 0.0505 0.3142 0.0616  -0.0729 -0.0022 107 VAL B CG2 
2976 N  N   . SER B 108 ? 0.2486 0.0503 0.2368 0.0315  -0.0649 0.0320  108 SER B N   
2977 C  CA  . SER B 108 ? 0.2310 0.0192 0.2910 0.0240  -0.0579 0.0215  108 SER B CA  
2978 C  C   . SER B 108 ? 0.2405 0.1347 0.1920 0.1076  -0.0536 0.0083  108 SER B C   
2979 O  O   . SER B 108 ? 0.2517 0.1218 0.2711 0.0803  -0.0243 -0.0076 108 SER B O   
2980 C  CB  . SER B 108 ? 0.3827 0.0288 0.3502 0.0039  -0.0603 0.0591  108 SER B CB  
2981 O  OG  . SER B 108 ? 0.4125 0.0853 0.3373 0.0499  -0.0512 0.1018  108 SER B OG  
2982 N  N   . GLY B 109 ? 0.1780 0.1470 0.2342 -0.0016 -0.0391 0.0113  109 GLY B N   
2983 C  CA  . GLY B 109 ? 0.1549 0.1556 0.2239 0.0501  -0.0453 -0.0001 109 GLY B CA  
2984 C  C   . GLY B 109 ? 0.1999 0.2865 0.2304 0.1017  -0.0475 0.0182  109 GLY B C   
2985 O  O   . GLY B 109 ? 0.2291 0.4254 0.2300 0.1478  0.0125  0.0566  109 GLY B O   
2986 N  N   . GLN B 110 ? 0.2261 0.1948 0.2089 0.0964  -0.0740 0.0020  110 GLN B N   
2987 C  CA  . GLN B 110 ? 0.2592 0.1557 0.2092 0.0923  -0.0607 -0.0151 110 GLN B CA  
2988 C  C   . GLN B 110 ? 0.1876 0.0584 0.1916 0.0182  -0.0107 0.0161  110 GLN B C   
2989 O  O   . GLN B 110 ? 0.1913 0.0095 0.1817 0.0108  -0.0202 0.0197  110 GLN B O   
2990 C  CB  . GLN B 110 ? 0.4349 0.0814 0.3495 0.1262  -0.1096 -0.0084 110 GLN B CB  
2991 C  CG  . GLN B 110 ? 0.3208 0.1773 0.3327 0.1124  -0.0489 0.0649  110 GLN B CG  
2992 C  CD  . GLN B 110 ? 0.3096 0.4550 0.3462 0.1317  -0.0518 -0.0179 110 GLN B CD  
2993 O  OE1 . GLN B 110 ? 0.6253 0.5816 0.3802 0.2658  -0.0838 -0.1109 110 GLN B OE1 
2994 N  NE2 . GLN B 110 ? 0.4169 0.3564 0.4027 0.0342  -0.0879 0.0156  110 GLN B NE2 
2995 N  N   . HIS B 111 ? 0.1850 0.0873 0.1685 0.0182  -0.0132 0.0057  111 HIS B N   
2996 C  CA  . HIS B 111 ? 0.1714 0.1024 0.1743 0.0018  -0.0105 0.0228  111 HIS B CA  
2997 C  C   . HIS B 111 ? 0.1577 0.0162 0.1390 0.0381  -0.0025 0.0051  111 HIS B C   
2998 O  O   . HIS B 111 ? 0.1808 0.0855 0.2966 0.0612  -0.0159 -0.0976 111 HIS B O   
2999 C  CB  . HIS B 111 ? 0.2156 0.0935 0.1600 -0.0311 0.0165  -0.0099 111 HIS B CB  
3000 C  CG  . HIS B 111 ? 0.1800 0.0191 0.1829 0.0168  0.0223  0.0239  111 HIS B CG  
3001 N  ND1 . HIS B 111 ? 0.1610 0.0965 0.2009 0.0622  0.0388  -0.0216 111 HIS B ND1 
3002 C  CD2 . HIS B 111 ? 0.1933 0.0180 0.3067 -0.0035 0.0176  0.0212  111 HIS B CD2 
3003 C  CE1 . HIS B 111 ? 0.2550 0.1550 0.1537 -0.0030 0.0094  0.0337  111 HIS B CE1 
3004 N  NE2 . HIS B 111 ? 0.2522 0.0428 0.2525 -0.0026 0.0601  -0.0271 111 HIS B NE2 
3005 N  N   . PHE B 112 ? 0.1588 0.0362 0.1518 0.0208  0.0006  0.0250  112 PHE B N   
3006 C  CA  . PHE B 112 ? 0.1555 0.0426 0.1442 0.0227  -0.0047 0.0179  112 PHE B CA  
3007 C  C   . PHE B 112 ? 0.1349 0.0180 0.1385 -0.0075 0.0039  0.0068  112 PHE B C   
3008 O  O   . PHE B 112 ? 0.1304 0.0303 0.1530 -0.0187 -0.0165 0.0248  112 PHE B O   
3009 C  CB  . PHE B 112 ? 0.1803 0.0164 0.1765 0.0245  0.0269  0.0353  112 PHE B CB  
3010 C  CG  . PHE B 112 ? 0.2040 0.0440 0.1895 -0.0035 0.0071  0.0520  112 PHE B CG  
3011 C  CD1 . PHE B 112 ? 0.1958 0.1218 0.2214 0.0429  0.0027  0.0695  112 PHE B CD1 
3012 C  CD2 . PHE B 112 ? 0.2186 0.0355 0.2630 -0.0122 0.0529  0.0560  112 PHE B CD2 
3013 C  CE1 . PHE B 112 ? 0.3314 0.2109 0.2290 0.0030  0.0125  0.1060  112 PHE B CE1 
3014 C  CE2 . PHE B 112 ? 0.3377 0.0923 0.3087 0.0454  0.0510  0.1108  112 PHE B CE2 
3015 C  CZ  . PHE B 112 ? 0.2541 0.1150 0.2909 0.0785  0.0650  0.1603  112 PHE B CZ  
3016 N  N   . ALA B 113 ? 0.1416 0.0077 0.1490 -0.0135 0.0080  0.0010  113 ALA B N   
3017 C  CA  . ALA B 113 ? 0.1579 0.0279 0.1155 0.0256  -0.0035 -0.0204 113 ALA B CA  
3018 C  C   . ALA B 113 ? 0.1172 0.0204 0.1259 0.0081  0.0220  0.0015  113 ALA B C   
3019 O  O   . ALA B 113 ? 0.1478 0.0198 0.1670 -0.0283 0.0035  0.0121  113 ALA B O   
3020 C  CB  . ALA B 113 ? 0.1449 0.0636 0.1622 0.0176  -0.0116 -0.0323 113 ALA B CB  
3021 N  N   . ALA B 114 ? 0.1492 0.0221 0.1277 0.0231  0.0129  -0.0358 114 ALA B N   
3022 C  CA  . ALA B 114 ? 0.1510 0.0105 0.1043 0.0221  -0.0037 -0.0092 114 ALA B CA  
3023 C  C   . ALA B 114 ? 0.1138 0.0072 0.1627 0.0065  0.0202  0.0098  114 ALA B C   
3024 O  O   . ALA B 114 ? 0.1426 0.0073 0.1472 0.0098  0.0025  -0.0060 114 ALA B O   
3025 C  CB  . ALA B 114 ? 0.1562 0.0066 0.1697 -0.0031 -0.0355 0.0063  114 ALA B CB  
3026 N  N   . GLU B 115 ? 0.1291 0.0063 0.1430 -0.0004 0.0066  -0.0017 115 GLU B N   
3027 C  CA  . GLU B 115 ? 0.1119 0.0075 0.1484 -0.0079 -0.0045 0.0098  115 GLU B CA  
3028 C  C   . GLU B 115 ? 0.1252 0.0121 0.1385 0.0118  0.0261  0.0193  115 GLU B C   
3029 O  O   . GLU B 115 ? 0.1099 0.0443 0.1563 -0.0026 0.0130  0.0482  115 GLU B O   
3030 C  CB  . GLU B 115 ? 0.1112 0.0093 0.1311 0.0072  -0.0126 0.0168  115 GLU B CB  
3031 C  CG  . GLU B 115 ? 0.1521 0.0441 0.1284 -0.0097 -0.0082 0.0145  115 GLU B CG  
3032 C  CD  . GLU B 115 ? 0.1284 0.0121 0.1504 -0.0077 -0.0037 0.0278  115 GLU B CD  
3033 O  OE1 . GLU B 115 ? 0.1238 0.0087 0.1693 -0.0164 -0.0047 -0.0037 115 GLU B OE1 
3034 O  OE2 . GLU B 115 ? 0.1403 0.0082 0.1653 0.0099  -0.0219 0.0117  115 GLU B OE2 
3035 N  N   . LEU B 116 ? 0.1094 0.0068 0.1302 0.0020  0.0088  -0.0077 116 LEU B N   
3036 C  CA  . LEU B 116 ? 0.0956 0.0104 0.1270 -0.0044 0.0070  0.0069  116 LEU B CA  
3037 C  C   . LEU B 116 ? 0.1216 0.0083 0.1119 0.0025  -0.0153 0.0138  116 LEU B C   
3038 O  O   . LEU B 116 ? 0.1469 0.0118 0.1032 -0.0013 -0.0132 0.0132  116 LEU B O   
3039 C  CB  . LEU B 116 ? 0.0922 0.0217 0.1606 -0.0055 -0.0041 -0.0079 116 LEU B CB  
3040 C  CG  . LEU B 116 ? 0.0947 0.0406 0.1736 -0.0034 -0.0051 0.0444  116 LEU B CG  
3041 C  CD1 . LEU B 116 ? 0.1621 0.0259 0.1492 -0.0117 -0.0193 0.0254  116 LEU B CD1 
3042 C  CD2 . LEU B 116 ? 0.1460 0.0440 0.1994 -0.0405 -0.0004 0.0268  116 LEU B CD2 
3043 N  N   . HIS B 117 ? 0.1107 0.0097 0.1444 0.0040  0.0010  0.0211  117 HIS B N   
3044 C  CA  . HIS B 117 ? 0.1051 0.0304 0.1570 -0.0458 -0.0154 -0.0120 117 HIS B CA  
3045 C  C   . HIS B 117 ? 0.1257 0.0083 0.1228 -0.0141 -0.0081 -0.0054 117 HIS B C   
3046 O  O   . HIS B 117 ? 0.1236 0.0187 0.1437 -0.0005 0.0002  0.0204  117 HIS B O   
3047 C  CB  . HIS B 117 ? 0.1094 0.0179 0.2197 -0.0223 -0.0079 0.0394  117 HIS B CB  
3048 C  CG  . HIS B 117 ? 0.1144 0.0129 0.1487 -0.0222 -0.0132 0.0199  117 HIS B CG  
3049 N  ND1 . HIS B 117 ? 0.1456 0.0140 0.2059 -0.0321 -0.0443 0.0169  117 HIS B ND1 
3050 C  CD2 . HIS B 117 ? 0.0993 0.0139 0.1653 -0.0012 -0.0292 0.0220  117 HIS B CD2 
3051 C  CE1 . HIS B 117 ? 0.1074 0.0554 0.1931 -0.0571 -0.0244 0.0262  117 HIS B CE1 
3052 N  NE2 . HIS B 117 ? 0.0945 0.0069 0.1411 0.0059  -0.0142 0.0037  117 HIS B NE2 
3053 N  N   . ILE B 118 ? 0.1153 0.0092 0.1593 0.0164  0.0010  0.0079  118 ILE B N   
3054 C  CA  . ILE B 118 ? 0.1176 0.0177 0.1162 0.0193  0.0161  0.0240  118 ILE B CA  
3055 C  C   . ILE B 118 ? 0.1337 0.0129 0.1289 0.0223  0.0014  0.0183  118 ILE B C   
3056 O  O   . ILE B 118 ? 0.1692 0.0086 0.1368 0.0088  0.0029  0.0156  118 ILE B O   
3057 C  CB  . ILE B 118 ? 0.1045 0.0217 0.1460 0.0158  0.0060  -0.0096 118 ILE B CB  
3058 C  CG1 . ILE B 118 ? 0.1952 0.0101 0.1696 -0.0265 0.0195  -0.0050 118 ILE B CG1 
3059 C  CG2 . ILE B 118 ? 0.0997 0.0423 0.1936 0.0172  -0.0148 0.0042  118 ILE B CG2 
3060 C  CD1 . ILE B 118 ? 0.1817 0.0123 0.1923 -0.0255 0.0143  0.0183  118 ILE B CD1 
3061 N  N   . VAL B 119 ? 0.1038 0.0180 0.1430 0.0254  -0.0064 0.0245  119 VAL B N   
3062 C  CA  . VAL B 119 ? 0.1100 0.0413 0.1588 0.0013  0.0233  -0.0117 119 VAL B CA  
3063 C  C   . VAL B 119 ? 0.1096 0.0135 0.1741 0.0259  -0.0028 0.0099  119 VAL B C   
3064 O  O   . VAL B 119 ? 0.1359 0.0242 0.1830 0.0474  -0.0080 0.0059  119 VAL B O   
3065 C  CB  . VAL B 119 ? 0.1269 0.0116 0.1453 0.0171  0.0018  -0.0196 119 VAL B CB  
3066 C  CG1 . VAL B 119 ? 0.1758 0.0303 0.1686 0.0294  0.0117  -0.0531 119 VAL B CG1 
3067 C  CG2 . VAL B 119 ? 0.1410 0.0537 0.1776 0.0229  0.0275  -0.0158 119 VAL B CG2 
3068 N  N   . HIS B 120 ? 0.1295 0.0189 0.1664 0.0387  -0.0166 -0.0133 120 HIS B N   
3069 C  CA  . HIS B 120 ? 0.1412 0.0272 0.1636 0.0134  -0.0039 -0.0187 120 HIS B CA  
3070 C  C   . HIS B 120 ? 0.1672 0.0597 0.1381 0.0303  -0.0137 -0.0278 120 HIS B C   
3071 O  O   . HIS B 120 ? 0.1796 0.0230 0.1861 0.0377  -0.0233 0.0109  120 HIS B O   
3072 C  CB  . HIS B 120 ? 0.2186 0.0728 0.1725 -0.0182 0.0170  -0.0157 120 HIS B CB  
3073 C  CG  . HIS B 120 ? 0.1460 0.0678 0.1412 0.0353  -0.0182 -0.0204 120 HIS B CG  
3074 N  ND1 . HIS B 120 ? 0.1431 0.0208 0.1502 0.0126  0.0098  0.0094  120 HIS B ND1 
3075 C  CD2 . HIS B 120 ? 0.1123 0.0710 0.1635 0.0603  0.0124  -0.0197 120 HIS B CD2 
3076 C  CE1 . HIS B 120 ? 0.1308 0.0688 0.1458 -0.0005 -0.0128 -0.0012 120 HIS B CE1 
3077 N  NE2 . HIS B 120 ? 0.1420 0.0507 0.1366 0.0408  0.0240  0.0023  120 HIS B NE2 
3078 N  N   . TYR B 121 ? 0.1617 0.0708 0.1945 0.0266  0.0040  -0.0234 121 TYR B N   
3079 C  CA  . TYR B 121 ? 0.1945 0.0505 0.1882 0.0339  0.0100  -0.0173 121 TYR B CA  
3080 C  C   . TYR B 121 ? 0.2238 0.0882 0.1791 0.0675  0.0060  -0.0266 121 TYR B C   
3081 O  O   . TYR B 121 ? 0.2651 0.0464 0.2187 0.0708  0.0211  -0.0391 121 TYR B O   
3082 C  CB  . TYR B 121 ? 0.2238 0.0353 0.2016 0.0776  -0.0201 -0.0224 121 TYR B CB  
3083 C  CG  . TYR B 121 ? 0.2146 0.0638 0.2182 0.0559  -0.0201 -0.0006 121 TYR B CG  
3084 C  CD1 . TYR B 121 ? 0.1692 0.1658 0.1990 0.0194  -0.0190 0.0061  121 TYR B CD1 
3085 C  CD2 . TYR B 121 ? 0.2214 0.0759 0.2592 0.0870  -0.0117 0.0165  121 TYR B CD2 
3086 C  CE1 . TYR B 121 ? 0.2002 0.0886 0.2568 0.0425  -0.0005 0.0585  121 TYR B CE1 
3087 C  CE2 . TYR B 121 ? 0.2582 0.1622 0.2748 0.0930  -0.0378 0.0469  121 TYR B CE2 
3088 C  CZ  . TYR B 121 ? 0.1952 0.1456 0.2943 0.0487  -0.0030 0.0290  121 TYR B CZ  
3089 O  OH  . TYR B 121 ? 0.2532 0.1916 0.4322 0.0878  -0.0372 0.0833  121 TYR B OH  
3090 N  N   . ASN B 122 ? 0.1852 0.0402 0.2107 0.0607  0.0077  -0.0341 122 ASN B N   
3091 C  CA  . ASN B 122 ? 0.1674 0.1575 0.2218 0.0687  0.0065  -0.0848 122 ASN B CA  
3092 C  C   . ASN B 122 ? 0.1997 0.1460 0.2331 0.0840  -0.0488 -0.1098 122 ASN B C   
3093 O  O   . ASN B 122 ? 0.1992 0.1358 0.2180 0.0294  0.0075  -0.0640 122 ASN B O   
3094 C  CB  . ASN B 122 ? 0.2925 0.1071 0.1732 0.0682  -0.0013 -0.0514 122 ASN B CB  
3095 C  CG  . ASN B 122 ? 0.2394 0.1304 0.1743 0.0670  -0.0233 -0.0264 122 ASN B CG  
3096 O  OD1 . ASN B 122 ? 0.2376 0.0650 0.3292 0.0627  0.0260  -0.0440 122 ASN B OD1 
3097 N  ND2 . ASN B 122 ? 0.3139 0.1471 0.2002 0.0453  -0.0649 0.0019  122 ASN B ND2 
3098 N  N   . SER B 123 ? 0.1931 0.1276 0.1625 0.0763  -0.0461 -0.0172 123 SER B N   
3099 C  CA  . SER B 123 ? 0.1225 0.1737 0.1925 0.0609  -0.0134 -0.0142 123 SER B CA  
3100 C  C   . SER B 123 ? 0.1818 0.1383 0.2070 0.0526  -0.0033 -0.0270 123 SER B C   
3101 O  O   . SER B 123 ? 0.1941 0.2593 0.2685 0.1175  -0.0194 -0.0570 123 SER B O   
3102 C  CB  . SER B 123 ? 0.2099 0.1333 0.2998 0.0372  -0.0604 -0.0162 123 SER B CB  
3103 O  OG  . SER B 123 ? 0.2368 0.1536 0.1951 0.0621  0.0096  -0.0037 123 SER B OG  
3104 N  N   . ASP B 124 ? 0.2494 0.1923 0.2053 0.1259  -0.0021 -0.0341 124 ASP B N   
3105 C  CA  . ASP B 124 ? 0.2205 0.1796 0.2296 0.0820  -0.0065 -0.0142 124 ASP B CA  
3106 C  C   . ASP B 124 ? 0.2573 0.1923 0.2802 0.1250  -0.0463 -0.0938 124 ASP B C   
3107 O  O   . ASP B 124 ? 0.3094 0.2253 0.2367 0.1486  0.0458  -0.0189 124 ASP B O   
3108 C  CB  . ASP B 124 ? 0.2848 0.1859 0.2755 0.1131  0.0291  0.0283  124 ASP B CB  
3109 C  CG  . ASP B 124 ? 0.3360 0.2745 0.1897 0.0494  0.0185  -0.0538 124 ASP B CG  
3110 O  OD1 . ASP B 124 ? 0.3294 0.1356 0.2399 0.0427  -0.0023 -0.0158 124 ASP B OD1 
3111 O  OD2 . ASP B 124 ? 0.3643 0.2718 0.1980 0.0651  0.0345  -0.0447 124 ASP B OD2 
3112 N  N   . LEU B 125 ? 0.2289 0.2389 0.3091 0.0910  -0.0679 -0.0609 125 LEU B N   
3113 C  CA  . LEU B 125 ? 0.3420 0.1785 0.2523 0.1043  -0.0633 -0.0432 125 LEU B CA  
3114 C  C   . LEU B 125 ? 0.3673 0.2010 0.2390 0.1312  0.0293  -0.0768 125 LEU B C   
3115 O  O   . LEU B 125 ? 0.4909 0.2135 0.3036 0.0894  0.0312  -0.0988 125 LEU B O   
3116 C  CB  . LEU B 125 ? 0.3419 0.1865 0.2399 0.0522  -0.0820 -0.0182 125 LEU B CB  
3117 C  CG  . LEU B 125 ? 0.3510 0.1929 0.1672 0.0295  -0.0638 -0.0735 125 LEU B CG  
3118 C  CD1 . LEU B 125 ? 0.3580 0.2642 0.2753 0.0773  -0.0944 -0.1269 125 LEU B CD1 
3119 C  CD2 . LEU B 125 ? 0.3836 0.2485 0.1786 0.0668  -0.0727 -0.1112 125 LEU B CD2 
3120 N  N   . TYR B 126 ? 0.4259 0.1469 0.2164 0.1764  -0.0168 -0.0306 126 TYR B N   
3121 C  CA  . TYR B 126 ? 0.3581 0.2049 0.2278 0.1816  -0.0127 -0.0055 126 TYR B CA  
3122 C  C   . TYR B 126 ? 0.3751 0.2066 0.2490 0.1347  -0.0337 0.0032  126 TYR B C   
3123 O  O   . TYR B 126 ? 0.3889 0.2133 0.2673 0.1599  -0.0613 -0.0220 126 TYR B O   
3124 C  CB  . TYR B 126 ? 0.2266 0.2031 0.3071 -0.0400 0.0153  -0.0948 126 TYR B CB  
3125 C  CG  . TYR B 126 ? 0.3342 0.1359 0.2507 0.1547  0.0264  -0.0663 126 TYR B CG  
3126 C  CD1 . TYR B 126 ? 0.3882 0.1704 0.3063 0.1817  -0.1014 -0.0920 126 TYR B CD1 
3127 C  CD2 . TYR B 126 ? 0.3130 0.0872 0.3916 0.0960  -0.0094 -0.0539 126 TYR B CD2 
3128 C  CE1 . TYR B 126 ? 0.3162 0.2521 0.4026 0.1066  -0.1565 -0.0280 126 TYR B CE1 
3129 C  CE2 . TYR B 126 ? 0.3517 0.2627 0.3688 0.1014  -0.0155 -0.0551 126 TYR B CE2 
3130 C  CZ  . TYR B 126 ? 0.3822 0.2252 0.4540 0.1306  -0.1562 -0.0672 126 TYR B CZ  
3131 O  OH  . TYR B 126 ? 0.4400 0.2216 0.3568 0.0653  -0.1251 -0.1095 126 TYR B OH  
3132 N  N   . PRO B 127 ? 0.5468 0.1829 0.3114 0.1473  -0.0524 0.0190  127 PRO B N   
3133 C  CA  . PRO B 127 ? 0.5130 0.1889 0.3730 0.0879  -0.0985 0.0550  127 PRO B CA  
3134 C  C   . PRO B 127 ? 0.3715 0.2521 0.3522 0.0075  -0.1001 0.0653  127 PRO B C   
3135 O  O   . PRO B 127 ? 0.5144 0.4839 0.3292 -0.0691 -0.1271 0.0613  127 PRO B O   
3136 C  CB  . PRO B 127 ? 0.5735 0.1999 0.5069 0.1212  -0.1448 0.0818  127 PRO B CB  
3137 C  CG  . PRO B 127 ? 0.5938 0.0785 0.4167 0.0634  -0.0889 0.0344  127 PRO B CG  
3138 C  CD  . PRO B 127 ? 0.5189 0.2149 0.3022 0.1307  -0.0851 -0.0129 127 PRO B CD  
3139 N  N   . ASP B 128 ? 0.3633 0.3213 0.2689 0.0204  -0.0851 0.0238  128 ASP B N   
3140 C  CA  . ASP B 128 ? 0.3651 0.2097 0.2396 -0.0114 -0.1020 0.0379  128 ASP B CA  
3141 C  C   . ASP B 128 ? 0.3732 0.1786 0.2658 -0.0272 -0.1185 0.0337  128 ASP B C   
3142 O  O   . ASP B 128 ? 0.4149 0.1370 0.3134 0.0037  -0.1579 -0.0567 128 ASP B O   
3143 C  CB  . ASP B 128 ? 0.4075 0.2710 0.4039 -0.1176 -0.1359 0.1430  128 ASP B CB  
3144 C  CG  . ASP B 128 ? 0.4230 0.1489 0.4903 -0.0214 -0.0302 -0.0450 128 ASP B CG  
3145 O  OD1 . ASP B 128 ? 0.7127 0.3175 0.5230 -0.2140 -0.3910 0.1355  128 ASP B OD1 
3146 O  OD2 . ASP B 128 ? 0.4439 0.3104 0.6210 0.0462  0.0023  0.0744  128 ASP B OD2 
3147 N  N   . ALA B 129 ? 0.4219 0.1444 0.3543 -0.0095 -0.0653 0.0173  129 ALA B N   
3148 C  CA  . ALA B 129 ? 0.3977 0.0812 0.3134 -0.0153 0.0027  -0.0714 129 ALA B CA  
3149 C  C   . ALA B 129 ? 0.3955 0.0550 0.2876 0.0011  -0.0712 -0.0161 129 ALA B C   
3150 O  O   . ALA B 129 ? 0.4120 0.0584 0.3044 0.0001  -0.0522 -0.0102 129 ALA B O   
3151 C  CB  . ALA B 129 ? 0.5643 0.0762 0.3001 0.0378  0.0530  -0.0488 129 ALA B CB  
3152 N  N   A SER B 130 ? 0.4443 0.0452 0.2523 -0.0233 -0.0641 -0.0260 130 SER B N   
3153 N  N   B SER B 130 ? 0.4071 0.0244 0.3160 -0.0453 -0.0273 -0.0040 130 SER B N   
3154 C  CA  A SER B 130 ? 0.3994 0.0089 0.2909 0.0162  -0.0291 -0.0246 130 SER B CA  
3155 C  CA  B SER B 130 ? 0.3781 0.0082 0.3644 -0.0125 0.0501  0.0207  130 SER B CA  
3156 C  C   A SER B 130 ? 0.4245 0.0447 0.2439 -0.0133 -0.0021 0.0254  130 SER B C   
3157 C  C   B SER B 130 ? 0.4034 0.0663 0.3392 -0.0892 0.0458  0.0303  130 SER B C   
3158 O  O   A SER B 130 ? 0.3756 0.0384 0.4424 0.0633  0.0153  0.0987  130 SER B O   
3159 O  O   B SER B 130 ? 0.3844 0.0495 0.5112 -0.0362 0.0330  -0.0835 130 SER B O   
3160 C  CB  A SER B 130 ? 0.4275 0.1003 0.1592 -0.0037 -0.1375 -0.0250 130 SER B CB  
3161 C  CB  B SER B 130 ? 0.3382 0.0359 0.6232 -0.0367 0.0648  0.1169  130 SER B CB  
3162 O  OG  A SER B 130 ? 0.4598 0.1399 0.2688 -0.0433 -0.1007 0.0240  130 SER B OG  
3163 O  OG  B SER B 130 ? 0.2788 0.3321 0.7090 -0.0872 0.0118  0.0763  130 SER B OG  
3164 N  N   . THR B 131 ? 0.4591 0.0699 0.2595 0.0326  -0.0141 -0.0013 131 THR B N   
3165 C  CA  . THR B 131 ? 0.5380 0.0697 0.3415 0.1403  -0.0196 -0.0992 131 THR B CA  
3166 C  C   . THR B 131 ? 0.3062 0.0864 0.3195 0.1009  -0.0611 -0.1384 131 THR B C   
3167 O  O   . THR B 131 ? 0.2560 0.1503 0.3959 0.0315  -0.0927 -0.0354 131 THR B O   
3168 C  CB  . THR B 131 ? 0.5043 0.1668 0.3086 0.1467  -0.0334 -0.0345 131 THR B CB  
3169 O  OG1 . THR B 131 ? 0.4085 0.1349 0.4968 0.0838  -0.0922 0.0098  131 THR B OG1 
3170 C  CG2 . THR B 131 ? 0.3102 0.2487 0.3154 0.1877  -0.0582 -0.1092 131 THR B CG2 
3171 N  N   . ALA B 132 ? 0.4185 0.0590 0.2511 0.0886  -0.0844 -0.0906 132 ALA B N   
3172 C  CA  . ALA B 132 ? 0.3192 0.0739 0.3201 0.0875  -0.0893 -0.0593 132 ALA B CA  
3173 C  C   . ALA B 132 ? 0.3167 0.1171 0.2973 0.0908  -0.0232 -0.1039 132 ALA B C   
3174 O  O   . ALA B 132 ? 0.2302 0.1340 0.3237 0.0679  0.0078  -0.0300 132 ALA B O   
3175 C  CB  . ALA B 132 ? 0.2637 0.1190 0.1970 0.0488  -0.0490 -0.0293 132 ALA B CB  
3176 N  N   . SER B 133 ? 0.2896 0.0837 0.3353 0.0436  -0.0046 -0.0701 133 SER B N   
3177 C  CA  . SER B 133 ? 0.2717 0.0540 0.3024 0.0533  -0.0087 0.0220  133 SER B CA  
3178 C  C   . SER B 133 ? 0.3344 0.1961 0.3537 0.0089  -0.0583 -0.0103 133 SER B C   
3179 O  O   . SER B 133 ? 0.3457 0.0223 0.4382 0.0128  -0.0020 0.0592  133 SER B O   
3180 C  CB  . SER B 133 ? 0.3587 0.0844 0.3201 0.0491  -0.0002 0.0216  133 SER B CB  
3181 O  OG  . SER B 133 ? 0.4027 0.0694 0.4501 0.1197  0.0530  0.0331  133 SER B OG  
3182 N  N   . ASN B 134 ? 0.5533 0.0544 0.3212 -0.0693 -0.0556 0.0643  134 ASN B N   
3183 C  CA  . ASN B 134 ? 0.3416 0.1507 0.5031 -0.0181 -0.0524 0.0308  134 ASN B CA  
3184 C  C   . ASN B 134 ? 0.3867 0.0575 0.4665 -0.0255 -0.1426 -0.0483 134 ASN B C   
3185 O  O   . ASN B 134 ? 0.4597 0.2397 0.5507 0.0055  -0.2142 -0.1805 134 ASN B O   
3186 C  CB  . ASN B 134 ? 0.5301 0.1148 0.5351 -0.0673 0.1482  -0.0200 134 ASN B CB  
3187 C  CG  . ASN B 134 ? 0.4283 0.1098 0.5161 -0.0673 0.0991  0.0048  134 ASN B CG  
3188 O  OD1 . ASN B 134 ? 0.4169 0.1880 0.4830 -0.0365 0.1087  -0.0554 134 ASN B OD1 
3189 N  ND2 . ASN B 134 ? 0.6153 0.2773 0.6668 0.0708  -0.0290 -0.1549 134 ASN B ND2 
3190 N  N   . LYS B 135 ? 0.3438 0.0747 0.4879 0.0787  0.0873  0.0081  135 LYS B N   
3191 C  CA  . LYS B 135 ? 0.4354 0.0963 0.4130 0.0098  -0.0297 -0.0741 135 LYS B CA  
3192 C  C   . LYS B 135 ? 0.3870 0.1121 0.2904 0.0355  0.0578  -0.0648 135 LYS B C   
3193 O  O   . LYS B 135 ? 0.3119 0.1658 0.2478 0.0254  -0.0376 -0.0620 135 LYS B O   
3194 C  CB  . LYS B 135 ? 0.4834 0.1600 0.6512 0.0538  0.1773  0.0236  135 LYS B CB  
3195 N  N   . SER B 136 ? 0.4954 0.1448 0.3165 -0.0779 -0.0690 -0.0146 136 SER B N   
3196 C  CA  . SER B 136 ? 0.5058 0.1844 0.2988 -0.0406 -0.1145 -0.0117 136 SER B CA  
3197 C  C   . SER B 136 ? 0.4475 0.0821 0.2619 0.0352  -0.1513 -0.0290 136 SER B C   
3198 O  O   . SER B 136 ? 0.4480 0.3224 0.2495 0.0310  -0.0478 -0.0420 136 SER B O   
3199 C  CB  . SER B 136 ? 0.6127 0.4490 0.2512 -0.1317 -0.0392 -0.1399 136 SER B CB  
3200 O  OG  . SER B 136 ? 0.7482 0.6657 0.4447 -0.0245 0.1043  -0.1179 136 SER B OG  
3201 N  N   . GLU B 137 ? 0.3240 0.0380 0.4263 0.0387  -0.0591 -0.0017 137 GLU B N   
3202 C  CA  . GLU B 137 ? 0.2776 0.1742 0.3191 0.0245  -0.0945 -0.0917 137 GLU B CA  
3203 C  C   . GLU B 137 ? 0.2654 0.1370 0.2590 0.0418  -0.0110 -0.0025 137 GLU B C   
3204 O  O   . GLU B 137 ? 0.3261 0.2067 0.2719 -0.0721 -0.0688 0.0776  137 GLU B O   
3205 C  CB  . GLU B 137 ? 0.3565 0.2121 0.3371 0.0412  -0.1055 0.0034  137 GLU B CB  
3206 C  CG  . GLU B 137 ? 0.5535 0.1272 0.4213 0.0087  -0.2190 0.0366  137 GLU B CG  
3207 N  N   . GLY B 138 ? 0.2967 0.1006 0.2834 0.0297  -0.0749 -0.0128 138 GLY B N   
3208 C  CA  . GLY B 138 ? 0.2469 0.1042 0.2094 0.0591  -0.0259 -0.0700 138 GLY B CA  
3209 C  C   . GLY B 138 ? 0.2088 0.0683 0.2260 0.0296  -0.0116 -0.0624 138 GLY B C   
3210 O  O   . GLY B 138 ? 0.2148 0.1123 0.2408 0.0526  -0.0282 -0.0744 138 GLY B O   
3211 N  N   . LEU B 139 ? 0.2224 0.0139 0.1797 0.0170  -0.0181 -0.0341 139 LEU B N   
3212 C  CA  . LEU B 139 ? 0.1477 0.0126 0.1273 0.0277  0.0024  -0.0096 139 LEU B CA  
3213 C  C   . LEU B 139 ? 0.1631 0.0168 0.1674 0.0297  -0.0125 0.0089  139 LEU B C   
3214 O  O   . LEU B 139 ? 0.1703 0.0338 0.2263 0.0201  -0.0288 0.0161  139 LEU B O   
3215 C  CB  . LEU B 139 ? 0.1892 0.0113 0.1985 0.0275  0.0437  0.0186  139 LEU B CB  
3216 C  CG  . LEU B 139 ? 0.2293 0.0416 0.2024 0.0644  0.0429  0.0682  139 LEU B CG  
3217 C  CD1 . LEU B 139 ? 0.2389 0.0151 0.2970 0.0126  0.0832  0.0444  139 LEU B CD1 
3218 C  CD2 . LEU B 139 ? 0.2242 0.0787 0.2426 0.0525  -0.0026 0.0173  139 LEU B CD2 
3219 N  N   . ALA B 140 ? 0.1787 0.0226 0.1845 0.0517  -0.0314 0.0020  140 ALA B N   
3220 C  CA  . ALA B 140 ? 0.1995 0.0161 0.1524 0.0427  0.0237  -0.0014 140 ALA B CA  
3221 C  C   . ALA B 140 ? 0.1549 0.0079 0.1564 0.0146  0.0047  -0.0048 140 ALA B C   
3222 O  O   . ALA B 140 ? 0.1732 0.0335 0.1873 0.0378  -0.0132 -0.0104 140 ALA B O   
3223 C  CB  . ALA B 140 ? 0.2286 0.0265 0.1561 0.0369  0.0491  -0.0145 140 ALA B CB  
3224 N  N   . VAL B 141 ? 0.1512 0.0069 0.1633 0.0091  0.0038  0.0002  141 VAL B N   
3225 C  CA  . VAL B 141 ? 0.1381 0.0176 0.1363 0.0348  0.0464  0.0274  141 VAL B CA  
3226 C  C   . VAL B 141 ? 0.1468 0.0119 0.1382 0.0265  0.0071  0.0098  141 VAL B C   
3227 O  O   . VAL B 141 ? 0.1518 0.0092 0.1530 0.0204  -0.0201 -0.0016 141 VAL B O   
3228 C  CB  . VAL B 141 ? 0.1478 0.0101 0.1444 -0.0062 0.0302  0.0204  141 VAL B CB  
3229 C  CG1 . VAL B 141 ? 0.1805 0.0754 0.1514 -0.0100 0.0219  -0.0071 141 VAL B CG1 
3230 C  CG2 . VAL B 141 ? 0.1593 0.0352 0.2388 -0.0066 -0.0377 0.0815  141 VAL B CG2 
3231 N  N   . LEU B 142 ? 0.1677 0.0144 0.1130 0.0349  0.0098  0.0094  142 LEU B N   
3232 C  CA  . LEU B 142 ? 0.1146 0.0079 0.1433 0.0114  0.0025  0.0075  142 LEU B CA  
3233 C  C   . LEU B 142 ? 0.1157 0.0250 0.1320 -0.0096 0.0078  0.0084  142 LEU B C   
3234 O  O   . LEU B 142 ? 0.1859 0.0078 0.1426 0.0058  0.0095  0.0138  142 LEU B O   
3235 C  CB  . LEU B 142 ? 0.1103 0.0283 0.1927 -0.0049 0.0151  0.0096  142 LEU B CB  
3236 C  CG  . LEU B 142 ? 0.1216 0.0686 0.1672 0.0031  0.0055  -0.0067 142 LEU B CG  
3237 C  CD1 . LEU B 142 ? 0.1295 0.0334 0.2693 -0.0251 0.0201  -0.0171 142 LEU B CD1 
3238 C  CD2 . LEU B 142 ? 0.1769 0.0792 0.1938 0.0094  -0.0174 0.0342  142 LEU B CD2 
3239 N  N   . ALA B 143 ? 0.1155 0.0094 0.1625 -0.0117 -0.0126 -0.0155 143 ALA B N   
3240 C  CA  . ALA B 143 ? 0.1056 0.0120 0.1974 0.0036  0.0015  -0.0324 143 ALA B CA  
3241 C  C   . ALA B 143 ? 0.1437 0.0075 0.1485 -0.0119 -0.0062 0.0063  143 ALA B C   
3242 O  O   . ALA B 143 ? 0.1717 0.0077 0.1290 0.0151  -0.0074 0.0009  143 ALA B O   
3243 C  CB  . ALA B 143 ? 0.1403 0.0076 0.1710 -0.0019 -0.0260 0.0146  143 ALA B CB  
3244 N  N   . VAL B 144 ? 0.1117 0.0064 0.1313 0.0004  -0.0111 -0.0033 144 VAL B N   
3245 C  CA  . VAL B 144 ? 0.1035 0.0088 0.1619 0.0084  0.0048  -0.0161 144 VAL B CA  
3246 C  C   . VAL B 144 ? 0.1351 0.0144 0.1366 0.0201  0.0212  -0.0026 144 VAL B C   
3247 O  O   . VAL B 144 ? 0.1402 0.0066 0.1429 0.0044  0.0075  0.0048  144 VAL B O   
3248 C  CB  . VAL B 144 ? 0.1132 0.0075 0.1583 -0.0074 -0.0103 -0.0096 144 VAL B CB  
3249 C  CG1 . VAL B 144 ? 0.1673 0.0120 0.2106 -0.0290 0.0028  -0.0102 144 VAL B CG1 
3250 C  CG2 . VAL B 144 ? 0.1464 0.0362 0.1618 0.0064  -0.0061 0.0121  144 VAL B CG2 
3251 N  N   . LEU B 145 ? 0.1245 0.0075 0.1823 0.0022  0.0078  -0.0138 145 LEU B N   
3252 C  CA  . LEU B 145 ? 0.1250 0.0361 0.1381 0.0126  -0.0079 -0.0066 145 LEU B CA  
3253 C  C   . LEU B 145 ? 0.1256 0.0064 0.1404 0.0026  -0.0030 0.0032  145 LEU B C   
3254 O  O   . LEU B 145 ? 0.1435 0.0108 0.1505 -0.0096 0.0114  -0.0030 145 LEU B O   
3255 C  CB  . LEU B 145 ? 0.1596 0.0322 0.1345 0.0233  -0.0051 0.0092  145 LEU B CB  
3256 C  CG  . LEU B 145 ? 0.1933 0.0067 0.1678 0.0071  -0.0188 0.0044  145 LEU B CG  
3257 C  CD1 . LEU B 145 ? 0.2358 0.0524 0.1713 0.0364  -0.0436 0.0102  145 LEU B CD1 
3258 C  CD2 . LEU B 145 ? 0.2832 0.0589 0.2361 -0.0650 -0.0168 0.0317  145 LEU B CD2 
3259 N  N   . ILE B 146 ? 0.1668 0.0105 0.1304 0.0081  0.0045  -0.0213 146 ILE B N   
3260 C  CA  . ILE B 146 ? 0.1714 0.0520 0.0889 0.0020  0.0218  -0.0047 146 ILE B CA  
3261 C  C   . ILE B 146 ? 0.1345 0.0161 0.1234 -0.0068 -0.0065 0.0041  146 ILE B C   
3262 O  O   . ILE B 146 ? 0.1320 0.0327 0.1743 0.0080  0.0204  -0.0134 146 ILE B O   
3263 C  CB  . ILE B 146 ? 0.1388 0.0300 0.1448 0.0155  0.0057  -0.0105 146 ILE B CB  
3264 C  CG1 . ILE B 146 ? 0.1570 0.0128 0.2106 0.0304  -0.0064 0.0066  146 ILE B CG1 
3265 C  CG2 . ILE B 146 ? 0.1778 0.0350 0.1719 -0.0370 -0.0065 -0.0230 146 ILE B CG2 
3266 C  CD1 . ILE B 146 ? 0.1689 0.0135 0.2370 0.0306  0.0029  0.0185  146 ILE B CD1 
3267 N  N   . GLU B 147 ? 0.1733 0.0154 0.1326 0.0091  -0.0337 -0.0098 147 GLU B N   
3268 C  CA  . GLU B 147 ? 0.1582 0.0498 0.1561 0.0070  -0.0240 -0.0089 147 GLU B CA  
3269 C  C   . GLU B 147 ? 0.1485 0.0095 0.1640 0.0065  -0.0132 -0.0221 147 GLU B C   
3270 O  O   . GLU B 147 ? 0.1456 0.0108 0.1824 0.0115  -0.0073 -0.0255 147 GLU B O   
3271 C  CB  . GLU B 147 ? 0.2725 0.0471 0.2174 0.0829  -0.0234 -0.0019 147 GLU B CB  
3272 C  CG  . GLU B 147 ? 0.3299 0.2401 0.2623 0.0089  -0.0581 0.0507  147 GLU B CG  
3273 C  CD  . GLU B 147 ? 0.5065 0.2193 0.3854 0.1007  -0.1258 0.0661  147 GLU B CD  
3274 O  OE1 . GLU B 147 ? 0.4175 0.1728 0.3133 0.1009  -0.0540 0.0752  147 GLU B OE1 
3275 O  OE2 . GLU B 147 ? 0.5441 0.2509 0.4187 0.1485  -0.2150 -0.0982 147 GLU B OE2 
3276 N  N   . MET B 148 ? 0.1929 0.0094 0.1823 0.0073  0.0213  -0.0213 148 MET B N   
3277 C  CA  . MET B 148 ? 0.1557 0.0225 0.1834 -0.0218 0.0168  -0.0298 148 MET B CA  
3278 C  C   . MET B 148 ? 0.0954 0.0091 0.2375 0.0156  0.0025  0.0017  148 MET B C   
3279 O  O   . MET B 148 ? 0.1424 0.0468 0.2125 0.0002  -0.0569 0.0022  148 MET B O   
3280 C  CB  . MET B 148 ? 0.1438 0.0234 0.1769 -0.0106 0.0110  -0.0051 148 MET B CB  
3281 C  CG  . MET B 148 ? 0.1999 0.0407 0.1900 -0.0037 0.0144  -0.0436 148 MET B CG  
3282 S  SD  . MET B 148 ? 0.2128 0.0171 0.2638 -0.0164 0.0405  -0.0315 148 MET B SD  
3283 C  CE  . MET B 148 ? 0.3726 0.0353 0.3010 0.0181  -0.0897 -0.0919 148 MET B CE  
3284 N  N   . GLY B 149 ? 0.1270 0.0116 0.2022 -0.0186 -0.0118 -0.0197 149 GLY B N   
3285 C  CA  . GLY B 149 ? 0.1630 0.0111 0.2078 -0.0273 -0.0457 0.0059  149 GLY B CA  
3286 C  C   . GLY B 149 ? 0.1626 0.0099 0.1699 0.0137  -0.0170 -0.0209 149 GLY B C   
3287 O  O   . GLY B 149 ? 0.1500 0.0063 0.1871 -0.0002 -0.0064 -0.0002 149 GLY B O   
3288 N  N   . SER B 150 ? 0.1421 0.0109 0.2365 0.0140  -0.0197 -0.0286 150 SER B N   
3289 C  CA  . SER B 150 ? 0.1451 0.0136 0.1680 0.0316  -0.0054 0.0008  150 SER B CA  
3290 C  C   . SER B 150 ? 0.1542 0.0100 0.1826 0.0203  -0.0368 -0.0171 150 SER B C   
3291 O  O   . SER B 150 ? 0.1693 0.0091 0.1564 0.0011  -0.0287 -0.0201 150 SER B O   
3292 C  CB  . SER B 150 ? 0.1049 0.0102 0.1904 0.0179  -0.0103 -0.0126 150 SER B CB  
3293 O  OG  . SER B 150 ? 0.1661 0.0108 0.2114 0.0262  -0.0098 -0.0075 150 SER B OG  
3294 N  N   . PHE B 151 ? 0.1632 0.0096 0.1861 0.0212  -0.0427 -0.0137 151 PHE B N   
3295 C  CA  . PHE B 151 ? 0.1575 0.0136 0.2073 0.0281  -0.0439 0.0119  151 PHE B CA  
3296 C  C   . PHE B 151 ? 0.2010 0.0097 0.2134 0.0039  -0.0142 -0.0264 151 PHE B C   
3297 O  O   . PHE B 151 ? 0.1891 0.0082 0.2438 0.0095  0.0112  -0.0178 151 PHE B O   
3298 C  CB  . PHE B 151 ? 0.1722 0.0390 0.2002 0.0209  -0.0412 -0.0128 151 PHE B CB  
3299 C  CG  . PHE B 151 ? 0.1697 0.0320 0.2046 0.0188  -0.0125 0.0035  151 PHE B CG  
3300 C  CD1 . PHE B 151 ? 0.1931 0.0453 0.1789 0.0000  -0.0408 0.0069  151 PHE B CD1 
3301 C  CD2 . PHE B 151 ? 0.1742 0.0440 0.1833 -0.0060 -0.0493 -0.0137 151 PHE B CD2 
3302 C  CE1 . PHE B 151 ? 0.1969 0.0690 0.2412 0.0234  -0.0636 0.0037  151 PHE B CE1 
3303 C  CE2 . PHE B 151 ? 0.1606 0.1082 0.2117 0.0347  -0.0316 0.0108  151 PHE B CE2 
3304 C  CZ  . PHE B 151 ? 0.1907 0.0911 0.1958 0.0131  -0.0657 0.0076  151 PHE B CZ  
3305 N  N   . ASN B 152 ? 0.1602 0.0183 0.1604 0.0030  -0.0422 -0.0420 152 ASN B N   
3306 C  CA  . ASN B 152 ? 0.1058 0.0569 0.1665 -0.0070 -0.0447 -0.0060 152 ASN B CA  
3307 C  C   . ASN B 152 ? 0.1481 0.0076 0.2001 0.0121  -0.0214 -0.0086 152 ASN B C   
3308 O  O   . ASN B 152 ? 0.1556 0.0067 0.2044 0.0077  -0.0348 -0.0013 152 ASN B O   
3309 C  CB  . ASN B 152 ? 0.1757 0.0092 0.1478 -0.0074 -0.0135 -0.0183 152 ASN B CB  
3310 C  CG  . ASN B 152 ? 0.1229 0.0176 0.1709 -0.0272 -0.0230 -0.0225 152 ASN B CG  
3311 O  OD1 . ASN B 152 ? 0.1320 0.0072 0.2110 -0.0104 -0.0228 -0.0020 152 ASN B OD1 
3312 N  ND2 . ASN B 152 ? 0.1768 0.0065 0.1832 -0.0008 -0.0373 -0.0052 152 ASN B ND2 
3313 N  N   . PRO B 153 ? 0.1542 0.0066 0.2321 -0.0052 -0.0518 0.0070  153 PRO B N   
3314 C  CA  . PRO B 153 ? 0.1374 0.0433 0.1995 0.0000  -0.0499 -0.0234 153 PRO B CA  
3315 C  C   . PRO B 153 ? 0.1920 0.0553 0.1857 -0.0063 -0.0094 -0.0321 153 PRO B C   
3316 O  O   . PRO B 153 ? 0.2256 0.0532 0.2092 -0.0178 -0.0150 -0.0208 153 PRO B O   
3317 C  CB  . PRO B 153 ? 0.1342 0.0316 0.2926 -0.0026 -0.0400 -0.0006 153 PRO B CB  
3318 C  CG  . PRO B 153 ? 0.1791 0.0196 0.3870 -0.0021 -0.0672 0.0536  153 PRO B CG  
3319 C  CD  . PRO B 153 ? 0.1349 0.0066 0.3051 -0.0061 -0.0219 0.0052  153 PRO B CD  
3320 N  N   . SER B 154 ? 0.1706 0.0157 0.2028 -0.0225 -0.0169 -0.0325 154 SER B N   
3321 C  CA  . SER B 154 ? 0.1421 0.0250 0.1710 -0.0084 -0.0251 -0.0307 154 SER B CA  
3322 C  C   . SER B 154 ? 0.1627 0.0102 0.1997 0.0004  -0.0547 0.0022  154 SER B C   
3323 O  O   . SER B 154 ? 0.1579 0.0214 0.2223 0.0171  -0.0151 0.0223  154 SER B O   
3324 C  CB  . SER B 154 ? 0.2046 0.0461 0.2084 -0.0496 0.0075  -0.0232 154 SER B CB  
3325 O  OG  . SER B 154 ? 0.2513 0.0621 0.2705 -0.0788 0.0474  -0.0353 154 SER B OG  
3326 N  N   . TYR B 155 ? 0.1273 0.0510 0.1487 -0.0118 -0.0061 -0.0290 155 TYR B N   
3327 C  CA  . TYR B 155 ? 0.1481 0.0113 0.1593 -0.0004 -0.0378 -0.0114 155 TYR B CA  
3328 C  C   . TYR B 155 ? 0.1664 0.0066 0.1558 0.0021  -0.0252 -0.0068 155 TYR B C   
3329 O  O   . TYR B 155 ? 0.1623 0.0084 0.2008 0.0180  -0.0305 -0.0005 155 TYR B O   
3330 C  CB  . TYR B 155 ? 0.1401 0.0134 0.1769 0.0095  -0.0342 -0.0345 155 TYR B CB  
3331 C  CG  . TYR B 155 ? 0.1312 0.0173 0.1742 -0.0043 -0.0096 -0.0155 155 TYR B CG  
3332 C  CD1 . TYR B 155 ? 0.1488 0.0072 0.2067 0.0073  -0.0060 -0.0102 155 TYR B CD1 
3333 C  CD2 . TYR B 155 ? 0.1800 0.0125 0.1970 -0.0283 -0.0304 0.0049  155 TYR B CD2 
3334 C  CE1 . TYR B 155 ? 0.1555 0.0090 0.2223 0.0120  -0.0403 0.0141  155 TYR B CE1 
3335 C  CE2 . TYR B 155 ? 0.1215 0.0234 0.2040 -0.0055 -0.0323 0.0027  155 TYR B CE2 
3336 C  CZ  . TYR B 155 ? 0.1834 0.0383 0.1636 -0.0038 -0.0187 -0.0061 155 TYR B CZ  
3337 O  OH  . TYR B 155 ? 0.1546 0.0074 0.1699 0.0085  -0.0241 0.0089  155 TYR B OH  
3338 N  N   . ASP B 156 ? 0.1458 0.0145 0.1597 0.0102  -0.0150 -0.0236 156 ASP B N   
3339 C  CA  . ASP B 156 ? 0.1773 0.0285 0.1487 0.0107  0.0074  -0.0378 156 ASP B CA  
3340 C  C   . ASP B 156 ? 0.1629 0.0311 0.1342 -0.0071 -0.0266 -0.0052 156 ASP B C   
3341 O  O   . ASP B 156 ? 0.1955 0.0491 0.1484 0.0032  -0.0271 0.0130  156 ASP B O   
3342 C  CB  . ASP B 156 ? 0.2271 0.0242 0.1611 0.0093  -0.0150 -0.0381 156 ASP B CB  
3343 C  CG  . ASP B 156 ? 0.2536 0.0514 0.1769 0.0201  -0.0291 0.0285  156 ASP B CG  
3344 O  OD1 . ASP B 156 ? 0.2314 0.0188 0.1675 0.0505  -0.0039 0.0062  156 ASP B OD1 
3345 O  OD2 . ASP B 156 ? 0.2175 0.1801 0.2155 -0.0273 -0.0816 0.0539  156 ASP B OD2 
3346 N  N   . LYS B 157 ? 0.1470 0.0266 0.1965 0.0131  -0.0244 -0.0227 157 LYS B N   
3347 C  CA  . LYS B 157 ? 0.1492 0.0285 0.2509 0.0111  0.0097  -0.0095 157 LYS B CA  
3348 C  C   . LYS B 157 ? 0.1706 0.0559 0.2052 -0.0239 -0.0566 0.0168  157 LYS B C   
3349 O  O   . LYS B 157 ? 0.1527 0.0862 0.3482 0.0280  -0.0373 0.0440  157 LYS B O   
3350 C  CB  . LYS B 157 ? 0.1494 0.0092 0.2248 -0.0176 -0.0032 -0.0127 157 LYS B CB  
3351 C  CG  . LYS B 157 ? 0.1414 0.0099 0.3120 -0.0219 0.0147  -0.0048 157 LYS B CG  
3352 C  CD  . LYS B 157 ? 0.1552 0.0721 0.2964 -0.0562 0.0084  -0.0083 157 LYS B CD  
3353 C  CE  . LYS B 157 ? 0.2156 0.0960 0.3231 -0.0922 0.0069  -0.0296 157 LYS B CE  
3354 N  NZ  . LYS B 157 ? 0.2297 0.2157 0.2549 -0.0963 0.0164  -0.0413 157 LYS B NZ  
3355 N  N   . ILE B 158 ? 0.1603 0.0313 0.1762 -0.0137 -0.0380 0.0039  158 ILE B N   
3356 C  CA  . ILE B 158 ? 0.2363 0.0093 0.1598 -0.0140 -0.0251 -0.0163 158 ILE B CA  
3357 C  C   . ILE B 158 ? 0.2311 0.0094 0.1582 -0.0025 -0.0042 -0.0217 158 ILE B C   
3358 O  O   . ILE B 158 ? 0.2044 0.0390 0.1984 -0.0083 -0.0088 0.0074  158 ILE B O   
3359 C  CB  . ILE B 158 ? 0.2003 0.0074 0.1639 -0.0127 -0.0235 0.0074  158 ILE B CB  
3360 C  CG1 . ILE B 158 ? 0.2679 0.0431 0.1743 -0.0462 0.0163  -0.0031 158 ILE B CG1 
3361 C  CG2 . ILE B 158 ? 0.3051 0.0093 0.2315 -0.0284 -0.0592 -0.0017 158 ILE B CG2 
3362 C  CD1 . ILE B 158 ? 0.2875 0.0963 0.1696 -0.0037 0.0244  -0.0268 158 ILE B CD1 
3363 N  N   . PHE B 159 ? 0.1647 0.0487 0.1848 -0.0016 -0.0039 -0.0323 159 PHE B N   
3364 C  CA  . PHE B 159 ? 0.1787 0.0660 0.1912 0.0063  0.0105  -0.0290 159 PHE B CA  
3365 C  C   . PHE B 159 ? 0.1634 0.0708 0.1890 -0.0038 0.0243  -0.0077 159 PHE B C   
3366 O  O   . PHE B 159 ? 0.2592 0.1247 0.2619 -0.0588 0.0623  0.0269  159 PHE B O   
3367 C  CB  . PHE B 159 ? 0.1755 0.0383 0.2583 -0.0168 -0.0253 -0.0102 159 PHE B CB  
3368 C  CG  . PHE B 159 ? 0.1362 0.0101 0.2621 -0.0133 -0.0209 -0.0201 159 PHE B CG  
3369 C  CD1 . PHE B 159 ? 0.1326 0.1428 0.2561 -0.0486 -0.0149 -0.0800 159 PHE B CD1 
3370 C  CD2 . PHE B 159 ? 0.1869 0.0201 0.2515 0.0068  -0.0046 -0.0099 159 PHE B CD2 
3371 C  CE1 . PHE B 159 ? 0.1395 0.0578 0.2554 -0.0323 0.0179  -0.0348 159 PHE B CE1 
3372 C  CE2 . PHE B 159 ? 0.1757 0.0753 0.2455 -0.0017 0.0126  -0.0392 159 PHE B CE2 
3373 C  CZ  . PHE B 159 ? 0.2290 0.0753 0.2274 -0.0089 0.0278  -0.0421 159 PHE B CZ  
3374 N  N   . SER B 160 ? 0.1712 0.0979 0.1761 -0.0245 0.0004  0.0086  160 SER B N   
3375 C  CA  . SER B 160 ? 0.2782 0.1323 0.1869 -0.1128 -0.0277 0.0260  160 SER B CA  
3376 C  C   . SER B 160 ? 0.2207 0.1607 0.1643 -0.0597 -0.0523 0.0278  160 SER B C   
3377 O  O   . SER B 160 ? 0.3228 0.2134 0.1631 -0.0614 -0.0736 0.0049  160 SER B O   
3378 C  CB  . SER B 160 ? 0.3181 0.1471 0.2295 -0.1360 -0.0601 0.0119  160 SER B CB  
3379 O  OG  . SER B 160 ? 0.2699 0.2538 0.2286 -0.0863 -0.0608 0.0454  160 SER B OG  
3380 N  N   . HIS B 161 ? 0.1833 0.1708 0.1805 -0.0749 -0.0269 0.0067  161 HIS B N   
3381 C  CA  . HIS B 161 ? 0.1726 0.2037 0.2153 -0.0392 -0.0129 0.0652  161 HIS B CA  
3382 C  C   . HIS B 161 ? 0.2503 0.1815 0.1938 -0.0663 -0.0390 0.0032  161 HIS B C   
3383 O  O   . HIS B 161 ? 0.2711 0.1765 0.1869 -0.0355 -0.0155 0.0326  161 HIS B O   
3384 C  CB  . HIS B 161 ? 0.1919 0.1409 0.2569 -0.0384 -0.0449 0.0129  161 HIS B CB  
3385 C  CG  . HIS B 161 ? 0.1764 0.1415 0.2714 -0.0293 -0.0429 0.0127  161 HIS B CG  
3386 N  ND1 . HIS B 161 ? 0.2485 0.2875 0.2478 -0.0314 -0.0454 0.0683  161 HIS B ND1 
3387 C  CD2 . HIS B 161 ? 0.1987 0.1743 0.3112 -0.0343 0.0259  -0.0111 161 HIS B CD2 
3388 C  CE1 . HIS B 161 ? 0.3661 0.1909 0.2782 -0.0876 0.0166  -0.0372 161 HIS B CE1 
3389 N  NE2 . HIS B 161 ? 0.2309 0.1480 0.3494 0.0015  -0.0170 -0.0462 161 HIS B NE2 
3390 N  N   . LEU B 162 ? 0.2096 0.0848 0.2806 -0.0552 0.0044  0.0136  162 LEU B N   
3391 C  CA  . LEU B 162 ? 0.2306 0.0890 0.2535 -0.0651 0.0175  -0.0220 162 LEU B CA  
3392 C  C   . LEU B 162 ? 0.1696 0.2552 0.2603 -0.0467 0.0435  0.0263  162 LEU B C   
3393 O  O   . LEU B 162 ? 0.2195 0.1818 0.2344 -0.0297 0.0146  0.0188  162 LEU B O   
3394 C  CB  . LEU B 162 ? 0.2435 0.1649 0.3518 0.0093  0.0381  -0.0062 162 LEU B CB  
3395 C  CG  . LEU B 162 ? 0.1798 0.0920 0.3531 0.0209  -0.0207 0.0082  162 LEU B CG  
3396 C  CD1 . LEU B 162 ? 0.1604 0.1591 0.4802 0.0084  -0.1053 0.0124  162 LEU B CD1 
3397 C  CD2 . LEU B 162 ? 0.1602 0.1200 0.3807 0.0075  -0.0269 -0.0234 162 LEU B CD2 
3398 N  N   . GLN B 163 ? 0.2435 0.2825 0.2314 -0.0151 -0.0163 0.0575  163 GLN B N   
3399 C  CA  . GLN B 163 ? 0.2193 0.1875 0.2263 -0.0133 -0.0754 0.0575  163 GLN B CA  
3400 C  C   . GLN B 163 ? 0.2435 0.2369 0.2146 0.0173  -0.0368 -0.0258 163 GLN B C   
3401 O  O   . GLN B 163 ? 0.2935 0.2597 0.2904 0.0740  0.0494  0.0765  163 GLN B O   
3402 C  CB  . GLN B 163 ? 0.2552 0.3435 0.2468 -0.0020 -0.0436 0.0011  163 GLN B CB  
3403 C  CG  . GLN B 163 ? 0.2709 0.4214 0.2784 0.0096  -0.0961 -0.0453 163 GLN B CG  
3404 C  CD  . GLN B 163 ? 0.4918 0.4030 0.2453 -0.0161 -0.1447 0.0050  163 GLN B CD  
3405 O  OE1 . GLN B 163 ? 0.2640 0.3881 0.5337 0.0705  -0.0231 0.0368  163 GLN B OE1 
3406 N  NE2 . GLN B 163 ? 0.5905 0.3420 0.2791 0.0587  -0.1714 -0.0293 163 GLN B NE2 
3407 N  N   . HIS B 164 ? 0.1657 0.1891 0.1991 0.0023  -0.0529 0.0300  164 HIS B N   
3408 C  CA  . HIS B 164 ? 0.2421 0.2390 0.2637 0.0551  0.0032  0.0559  164 HIS B CA  
3409 C  C   . HIS B 164 ? 0.1442 0.2505 0.2632 -0.0048 -0.0052 0.1157  164 HIS B C   
3410 O  O   . HIS B 164 ? 0.2198 0.2831 0.2095 0.0203  -0.0400 0.0766  164 HIS B O   
3411 C  CB  . HIS B 164 ? 0.2254 0.1390 0.2340 0.0526  -0.0384 0.0027  164 HIS B CB  
3412 C  CG  . HIS B 164 ? 0.1731 0.2411 0.2706 0.0594  -0.0655 -0.0423 164 HIS B CG  
3413 N  ND1 . HIS B 164 ? 0.2840 0.2901 0.2713 0.0696  -0.0579 -0.0204 164 HIS B ND1 
3414 C  CD2 . HIS B 164 ? 0.3432 0.2178 0.3239 0.0737  -0.0580 -0.0245 164 HIS B CD2 
3415 C  CE1 . HIS B 164 ? 0.4327 0.3531 0.2376 -0.0033 -0.0511 -0.0712 164 HIS B CE1 
3416 N  NE2 . HIS B 164 ? 0.3855 0.3071 0.3015 0.0750  -0.0872 -0.0405 164 HIS B NE2 
3417 N  N   . VAL B 165 ? 0.1607 0.2146 0.2437 -0.0660 -0.0372 0.1183  165 VAL B N   
3418 C  CA  . VAL B 165 ? 0.1534 0.1500 0.2643 -0.0527 0.0292  0.0337  165 VAL B CA  
3419 C  C   . VAL B 165 ? 0.1485 0.0803 0.1561 -0.0070 -0.0204 0.0250  165 VAL B C   
3420 O  O   . VAL B 165 ? 0.1643 0.0924 0.1494 -0.0399 -0.0304 0.0264  165 VAL B O   
3421 C  CB  . VAL B 165 ? 0.1750 0.1096 0.2524 0.0088  0.0423  0.0719  165 VAL B CB  
3422 C  CG1 . VAL B 165 ? 0.1574 0.1672 0.2531 -0.0006 -0.0052 0.1183  165 VAL B CG1 
3423 C  CG2 . VAL B 165 ? 0.1891 0.1316 0.1713 -0.0083 -0.0096 0.0825  165 VAL B CG2 
3424 N  N   . LYS B 166 ? 0.1937 0.0574 0.1713 -0.0441 -0.0113 0.0201  166 LYS B N   
3425 C  CA  . LYS B 166 ? 0.2155 0.0343 0.1764 -0.0118 -0.0105 0.0076  166 LYS B CA  
3426 C  C   . LYS B 166 ? 0.1859 0.0318 0.1539 -0.0027 -0.0136 0.0242  166 LYS B C   
3427 O  O   . LYS B 166 ? 0.1512 0.0956 0.2081 -0.0142 -0.0079 0.0347  166 LYS B O   
3428 C  CB  . LYS B 166 ? 0.2614 0.0909 0.1816 -0.0441 -0.0207 -0.0374 166 LYS B CB  
3429 C  CG  . LYS B 166 ? 0.2506 0.0611 0.1567 0.0159  -0.0554 0.0087  166 LYS B CG  
3430 C  CD  . LYS B 166 ? 0.3682 0.1496 0.1962 -0.0067 -0.0031 -0.0519 166 LYS B CD  
3431 C  CE  . LYS B 166 ? 0.4419 0.2205 0.3503 0.1102  0.0354  -0.0886 166 LYS B CE  
3432 N  N   . TYR B 167 ? 0.1482 0.0399 0.1588 0.0004  -0.0050 0.0418  167 TYR B N   
3433 C  CA  . TYR B 167 ? 0.1433 0.0675 0.1527 -0.0158 0.0381  0.0152  167 TYR B CA  
3434 C  C   . TYR B 167 ? 0.1453 0.0201 0.1588 -0.0131 0.0153  0.0215  167 TYR B C   
3435 O  O   . TYR B 167 ? 0.1514 0.0610 0.1956 0.0122  0.0122  0.0230  167 TYR B O   
3436 C  CB  . TYR B 167 ? 0.1936 0.0349 0.1537 0.0216  0.0270  0.0109  167 TYR B CB  
3437 C  CG  . TYR B 167 ? 0.1999 0.0217 0.1701 -0.0114 0.0434  0.0013  167 TYR B CG  
3438 C  CD1 . TYR B 167 ? 0.2081 0.0381 0.1851 0.0261  0.0422  -0.0097 167 TYR B CD1 
3439 C  CD2 . TYR B 167 ? 0.2362 0.0066 0.1862 -0.0080 0.0109  -0.0027 167 TYR B CD2 
3440 C  CE1 . TYR B 167 ? 0.2568 0.0449 0.1726 -0.0174 0.0105  -0.0423 167 TYR B CE1 
3441 C  CE2 . TYR B 167 ? 0.2810 0.0113 0.2375 0.0312  0.0635  -0.0101 167 TYR B CE2 
3442 C  CZ  . TYR B 167 ? 0.2455 0.1198 0.1613 -0.0181 0.0365  -0.0215 167 TYR B CZ  
3443 O  OH  . TYR B 167 ? 0.2541 0.1451 0.1920 -0.0107 0.0335  -0.0491 167 TYR B OH  
3444 N  N   . LYS B 168 ? 0.1534 0.0760 0.2012 -0.0507 0.0425  -0.0334 168 LYS B N   
3445 C  CA  . LYS B 168 ? 0.1613 0.0533 0.2263 -0.0012 -0.0020 -0.0348 168 LYS B CA  
3446 C  C   . LYS B 168 ? 0.1549 0.0814 0.2234 -0.0026 0.0326  0.0167  168 LYS B C   
3447 O  O   . LYS B 168 ? 0.2352 0.0780 0.2321 -0.0047 0.0309  0.0049  168 LYS B O   
3448 C  CB  . LYS B 168 ? 0.1854 0.0724 0.2231 -0.0289 0.0226  -0.0247 168 LYS B CB  
3449 C  CG  . LYS B 168 ? 0.2242 0.0434 0.2789 0.0035  0.0103  -0.0436 168 LYS B CG  
3450 C  CD  . LYS B 168 ? 0.2743 0.0968 0.3222 -0.0657 0.0188  -0.0332 168 LYS B CD  
3451 C  CE  . LYS B 168 ? 0.3405 0.0780 0.3599 0.0512  -0.0505 -0.0173 168 LYS B CE  
3452 N  NZ  . LYS B 168 ? 0.3890 0.3446 0.4484 -0.0423 -0.1203 0.0241  168 LYS B NZ  
3453 N  N   . GLY B 169 ? 0.1852 0.1022 0.2531 0.0175  0.0451  -0.0161 169 GLY B N   
3454 C  CA  . GLY B 169 ? 0.1949 0.0882 0.3491 0.0154  0.0472  -0.0132 169 GLY B CA  
3455 C  C   . GLY B 169 ? 0.1764 0.1112 0.2911 0.0454  0.0265  0.0389  169 GLY B C   
3456 O  O   . GLY B 169 ? 0.2227 0.2102 0.4027 0.1043  -0.0183 0.0237  169 GLY B O   
3457 N  N   . GLN B 170 ? 0.1556 0.1132 0.2275 0.0177  0.0183  0.0189  170 GLN B N   
3458 C  CA  . GLN B 170 ? 0.1485 0.1546 0.1947 0.0092  0.0141  0.0313  170 GLN B CA  
3459 C  C   . GLN B 170 ? 0.1446 0.1408 0.1597 0.0133  -0.0002 0.0182  170 GLN B C   
3460 O  O   . GLN B 170 ? 0.1956 0.2239 0.1746 0.0111  -0.0257 0.0209  170 GLN B O   
3461 C  CB  . GLN B 170 ? 0.1830 0.1220 0.1787 0.0111  0.0114  0.0368  170 GLN B CB  
3462 C  CG  . GLN B 170 ? 0.1918 0.1534 0.1999 0.0185  0.0071  0.0721  170 GLN B CG  
3463 C  CD  . GLN B 170 ? 0.1793 0.1933 0.1819 0.0933  0.0168  0.0688  170 GLN B CD  
3464 O  OE1 . GLN B 170 ? 0.2081 0.1711 0.1927 0.0509  -0.0429 0.0624  170 GLN B OE1 
3465 N  NE2 . GLN B 170 ? 0.2834 0.3031 0.1794 0.0905  -0.0013 0.0792  170 GLN B NE2 
3466 N  N   . GLU B 171 ? 0.1581 0.2006 0.1988 -0.0313 -0.0323 0.0900  171 GLU B N   
3467 C  CA  . GLU B 171 ? 0.1915 0.2597 0.2138 -0.0205 0.0020  0.0989  171 GLU B CA  
3468 C  C   . GLU B 171 ? 0.1643 0.2900 0.1891 -0.0181 -0.0136 0.1248  171 GLU B C   
3469 O  O   . GLU B 171 ? 0.1905 0.3626 0.2010 -0.0313 -0.0476 0.1221  171 GLU B O   
3470 C  CB  . GLU B 171 ? 0.2273 0.3190 0.3840 -0.1220 0.1271  -0.0143 171 GLU B CB  
3471 C  CG  . GLU B 171 ? 0.2288 0.3920 0.3743 -0.0610 0.0458  -0.0157 171 GLU B CG  
3472 C  CD  . GLU B 171 ? 0.4163 0.3415 0.5752 -0.0436 0.0956  -0.0106 171 GLU B CD  
3473 O  OE1 . GLU B 171 ? 0.4199 0.1446 0.6718 0.0738  0.2108  0.0723  171 GLU B OE1 
3474 O  OE2 . GLU B 171 ? 0.5460 0.2958 0.5026 -0.0023 0.1243  -0.0718 171 GLU B OE2 
3475 N  N   . ALA B 172 ? 0.1373 0.2606 0.1861 -0.0414 -0.0194 0.0713  172 ALA B N   
3476 C  CA  . ALA B 172 ? 0.1348 0.3043 0.1643 -0.0514 -0.0172 0.0718  172 ALA B CA  
3477 C  C   . ALA B 172 ? 0.1252 0.2207 0.1564 -0.0411 -0.0012 0.0282  172 ALA B C   
3478 O  O   . ALA B 172 ? 0.1886 0.3346 0.1581 -0.0466 -0.0053 0.0458  172 ALA B O   
3479 C  CB  . ALA B 172 ? 0.1561 0.4110 0.1553 -0.0486 0.0204  0.0288  172 ALA B CB  
3480 N  N   . PHE B 173 ? 0.1707 0.2324 0.2404 -0.0963 -0.0168 0.0536  173 PHE B N   
3481 C  CA  . PHE B 173 ? 0.1476 0.1866 0.2639 -0.0603 -0.0092 0.0748  173 PHE B CA  
3482 C  C   . PHE B 173 ? 0.1791 0.2072 0.1804 -0.0474 -0.0519 0.0458  173 PHE B C   
3483 O  O   . PHE B 173 ? 0.3100 0.3206 0.1676 -0.0540 -0.0243 0.0240  173 PHE B O   
3484 C  CB  . PHE B 173 ? 0.1805 0.2309 0.3678 -0.0410 -0.0526 0.0710  173 PHE B CB  
3485 C  CG  . PHE B 173 ? 0.1494 0.1789 0.3623 -0.0442 -0.0485 0.1050  173 PHE B CG  
3486 C  CD1 . PHE B 173 ? 0.2834 0.1360 0.3668 -0.0051 -0.0048 0.0599  173 PHE B CD1 
3487 C  CD2 . PHE B 173 ? 0.3882 0.2403 0.4211 0.0520  0.0347  0.1585  173 PHE B CD2 
3488 C  CE1 . PHE B 173 ? 0.2561 0.1298 0.5183 0.0109  -0.1061 0.0042  173 PHE B CE1 
3489 C  CE2 . PHE B 173 ? 0.4314 0.3017 0.5126 -0.0048 0.0915  0.0390  173 PHE B CE2 
3490 C  CZ  . PHE B 173 ? 0.4796 0.2389 0.5120 0.0195  -0.0420 0.0913  173 PHE B CZ  
3491 N  N   . VAL B 174 ? 0.1694 0.1338 0.1758 -0.0547 -0.0140 0.0355  174 VAL B N   
3492 C  CA  . VAL B 174 ? 0.1782 0.1430 0.2342 -0.0582 -0.0036 0.0656  174 VAL B CA  
3493 C  C   . VAL B 174 ? 0.1834 0.2037 0.2410 -0.0780 0.0086  0.0231  174 VAL B C   
3494 O  O   . VAL B 174 ? 0.1333 0.2135 0.3010 -0.0257 -0.0095 -0.0155 174 VAL B O   
3495 C  CB  . VAL B 174 ? 0.1349 0.0925 0.2555 -0.0073 0.0136  0.0370  174 VAL B CB  
3496 C  CG1 . VAL B 174 ? 0.2358 0.0851 0.2564 -0.0129 0.0150  0.0116  174 VAL B CG1 
3497 C  CG2 . VAL B 174 ? 0.1548 0.1812 0.2576 -0.0619 0.0149  -0.0142 174 VAL B CG2 
3498 N  N   . PRO B 175 ? 0.1146 0.1649 0.2078 -0.0093 -0.0065 0.0168  175 PRO B N   
3499 C  CA  . PRO B 175 ? 0.1808 0.1245 0.1683 -0.0644 -0.0025 0.0280  175 PRO B CA  
3500 C  C   . PRO B 175 ? 0.1420 0.1322 0.1622 -0.0018 -0.0040 0.0223  175 PRO B C   
3501 O  O   . PRO B 175 ? 0.1356 0.1241 0.2340 -0.0139 0.0042  0.0369  175 PRO B O   
3502 C  CB  . PRO B 175 ? 0.2092 0.1096 0.2682 -0.1037 -0.0116 0.0140  175 PRO B CB  
3503 C  CG  . PRO B 175 ? 0.1492 0.2067 0.2604 -0.0634 -0.0079 0.0388  175 PRO B CG  
3504 C  CD  . PRO B 175 ? 0.1543 0.2020 0.2193 -0.0627 -0.0072 0.0049  175 PRO B CD  
3505 N  N   . GLY B 176 ? 0.1573 0.1144 0.1833 -0.0122 0.0225  0.0447  176 GLY B N   
3506 C  CA  . GLY B 176 ? 0.1665 0.0692 0.1733 0.0296  0.0219  0.0400  176 GLY B CA  
3507 C  C   . GLY B 176 ? 0.1044 0.0717 0.2161 0.0050  -0.0181 0.0084  176 GLY B C   
3508 O  O   . GLY B 176 ? 0.1563 0.1130 0.2394 -0.0096 -0.0608 0.0116  176 GLY B O   
3509 N  N   . PHE B 177 ? 0.1383 0.0318 0.2439 -0.0027 -0.0275 0.0526  177 PHE B N   
3510 C  CA  . PHE B 177 ? 0.2200 0.0231 0.2010 0.0092  -0.0215 0.0184  177 PHE B CA  
3511 C  C   . PHE B 177 ? 0.1236 0.0534 0.2091 -0.0027 -0.0354 0.0480  177 PHE B C   
3512 O  O   . PHE B 177 ? 0.1148 0.0908 0.1847 0.0000  -0.0315 0.0051  177 PHE B O   
3513 C  CB  . PHE B 177 ? 0.1441 0.0549 0.2254 -0.0108 -0.0352 -0.0121 177 PHE B CB  
3514 C  CG  . PHE B 177 ? 0.1456 0.0977 0.2067 -0.0111 -0.0236 -0.0081 177 PHE B CG  
3515 C  CD1 . PHE B 177 ? 0.1209 0.1014 0.2191 0.0039  0.0240  0.0019  177 PHE B CD1 
3516 C  CD2 . PHE B 177 ? 0.1363 0.1661 0.2311 0.0192  -0.0342 -0.0160 177 PHE B CD2 
3517 C  CE1 . PHE B 177 ? 0.1200 0.2002 0.1530 0.0223  0.0078  -0.0070 177 PHE B CE1 
3518 C  CE2 . PHE B 177 ? 0.1392 0.1537 0.1794 0.0280  -0.0380 0.0058  177 PHE B CE2 
3519 C  CZ  . PHE B 177 ? 0.1421 0.1865 0.2593 0.0270  0.0148  0.0288  177 PHE B CZ  
3520 N  N   . ASN B 178 ? 0.1821 0.0525 0.2178 -0.0306 -0.0129 0.0525  178 ASN B N   
3521 C  CA  . ASN B 178 ? 0.1458 0.0747 0.2248 -0.0543 -0.0296 0.0421  178 ASN B CA  
3522 C  C   . ASN B 178 ? 0.1401 0.0481 0.1749 -0.0375 -0.0156 -0.0131 178 ASN B C   
3523 O  O   . ASN B 178 ? 0.1660 0.0566 0.2171 -0.0137 -0.0285 -0.0153 178 ASN B O   
3524 C  CB  . ASN B 178 ? 0.1791 0.0722 0.2693 -0.0646 -0.0262 0.0337  178 ASN B CB  
3525 C  CG  . ASN B 178 ? 0.1615 0.0839 0.2596 -0.0390 -0.0060 0.0418  178 ASN B CG  
3526 O  OD1 . ASN B 178 ? 0.1685 0.0944 0.2284 -0.0293 0.0026  0.0223  178 ASN B OD1 
3527 N  ND2 . ASN B 178 ? 0.2234 0.0851 0.3651 -0.0740 0.0461  0.0185  178 ASN B ND2 
3528 N  N   . ILE B 179 ? 0.1191 0.0452 0.1525 -0.0445 -0.0197 0.0003  179 ILE B N   
3529 C  CA  . ILE B 179 ? 0.1345 0.0512 0.1841 -0.0092 -0.0438 -0.0083 179 ILE B CA  
3530 C  C   . ILE B 179 ? 0.1484 0.0331 0.1970 -0.0128 -0.0093 0.0069  179 ILE B C   
3531 O  O   . ILE B 179 ? 0.1747 0.0314 0.1981 0.0155  -0.0187 -0.0019 179 ILE B O   
3532 C  CB  . ILE B 179 ? 0.1065 0.0446 0.2005 0.0094  -0.0069 -0.0212 179 ILE B CB  
3533 C  CG1 . ILE B 179 ? 0.1506 0.0147 0.2013 0.0147  0.0046  -0.0321 179 ILE B CG1 
3534 C  CG2 . ILE B 179 ? 0.1139 0.1298 0.2059 -0.0199 0.0029  -0.0644 179 ILE B CG2 
3535 C  CD1 . ILE B 179 ? 0.1790 0.0913 0.1920 0.0582  -0.0080 -0.0446 179 ILE B CD1 
3536 N  N   . GLU B 180 ? 0.1848 0.0231 0.2006 -0.0131 -0.0091 0.0329  180 GLU B N   
3537 C  CA  . GLU B 180 ? 0.1979 0.0383 0.1768 0.0139  0.0097  0.0229  180 GLU B CA  
3538 C  C   . GLU B 180 ? 0.1470 0.0612 0.1668 -0.0052 0.0046  -0.0011 180 GLU B C   
3539 O  O   . GLU B 180 ? 0.1290 0.0920 0.2371 -0.0138 -0.0015 0.0359  180 GLU B O   
3540 C  CB  . GLU B 180 ? 0.1751 0.0793 0.2845 -0.0196 0.0072  0.0853  180 GLU B CB  
3541 C  CG  . GLU B 180 ? 0.2185 0.2207 0.3098 0.0554  0.0498  0.1441  180 GLU B CG  
3542 C  CD  . GLU B 180 ? 0.2162 0.1561 0.4026 -0.0966 0.0403  0.1835  180 GLU B CD  
3543 O  OE1 . GLU B 180 ? 0.2073 0.3097 0.3295 -0.0539 0.0294  0.0282  180 GLU B OE1 
3544 O  OE2 . GLU B 180 ? 0.4027 0.3618 0.3931 0.0004  0.0506  0.2318  180 GLU B OE2 
3545 N  N   . GLU B 181 ? 0.1266 0.0652 0.1804 0.0009  0.0055  0.0043  181 GLU B N   
3546 C  CA  . GLU B 181 ? 0.1298 0.0505 0.1973 -0.0089 0.0136  0.0017  181 GLU B CA  
3547 C  C   . GLU B 181 ? 0.1395 0.0173 0.1976 -0.0251 0.0156  -0.0106 181 GLU B C   
3548 O  O   . GLU B 181 ? 0.1755 0.0274 0.2782 0.0084  -0.0026 -0.0358 181 GLU B O   
3549 C  CB  . GLU B 181 ? 0.1589 0.0469 0.2150 -0.0116 -0.0147 -0.0024 181 GLU B CB  
3550 C  CG  . GLU B 181 ? 0.1588 0.1133 0.2582 -0.0392 0.0061  0.0120  181 GLU B CG  
3551 C  CD  . GLU B 181 ? 0.1760 0.0977 0.2699 0.0264  0.0065  -0.0389 181 GLU B CD  
3552 O  OE1 . GLU B 181 ? 0.1640 0.2479 0.2618 -0.0396 -0.0070 -0.0507 181 GLU B OE1 
3553 O  OE2 . GLU B 181 ? 0.1854 0.2020 0.3331 -0.0147 -0.0342 -0.0518 181 GLU B OE2 
3554 N  N   . LEU B 182 ? 0.1146 0.0251 0.1488 -0.0368 -0.0267 0.0257  182 LEU B N   
3555 C  CA  . LEU B 182 ? 0.1299 0.0223 0.1973 -0.0375 -0.0266 0.0370  182 LEU B CA  
3556 C  C   . LEU B 182 ? 0.1397 0.0084 0.1634 -0.0154 -0.0228 -0.0045 182 LEU B C   
3557 O  O   . LEU B 182 ? 0.1549 0.0074 0.2008 -0.0054 -0.0075 0.0067  182 LEU B O   
3558 C  CB  . LEU B 182 ? 0.1345 0.0230 0.2041 -0.0383 -0.0262 0.0394  182 LEU B CB  
3559 C  CG  . LEU B 182 ? 0.1914 0.0091 0.1958 0.0198  -0.0384 -0.0152 182 LEU B CG  
3560 C  CD1 . LEU B 182 ? 0.1306 0.0270 0.2522 -0.0234 -0.0368 0.0598  182 LEU B CD1 
3561 C  CD2 . LEU B 182 ? 0.1460 0.0551 0.2005 0.0146  0.0039  -0.0025 182 LEU B CD2 
3562 N  N   . LEU B 183 ? 0.1550 0.0080 0.1613 0.0027  -0.0212 0.0132  183 LEU B N   
3563 C  CA  . LEU B 183 ? 0.1370 0.0349 0.1503 0.0190  0.0013  0.0538  183 LEU B CA  
3564 C  C   . LEU B 183 ? 0.1586 0.0258 0.1654 -0.0122 -0.0082 0.0103  183 LEU B C   
3565 O  O   . LEU B 183 ? 0.1815 0.0459 0.2399 -0.0089 -0.0433 -0.0113 183 LEU B O   
3566 C  CB  . LEU B 183 ? 0.1790 0.0252 0.1834 0.0170  0.0006  0.0352  183 LEU B CB  
3567 C  CG  . LEU B 183 ? 0.1886 0.0286 0.1988 0.0198  0.0104  0.0168  183 LEU B CG  
3568 C  CD1 . LEU B 183 ? 0.2889 0.0850 0.2146 0.0704  0.0411  0.0293  183 LEU B CD1 
3569 C  CD2 . LEU B 183 ? 0.1764 0.0868 0.3010 0.0017  -0.0410 0.0272  183 LEU B CD2 
3570 N  N   . PRO B 184 ? 0.1690 0.0076 0.2035 -0.0100 -0.0258 0.0136  184 PRO B N   
3571 C  CA  . PRO B 184 ? 0.1674 0.0068 0.2457 0.0028  -0.0013 0.0109  184 PRO B CA  
3572 C  C   . PRO B 184 ? 0.2131 0.0305 0.2101 0.0120  0.0017  0.0228  184 PRO B C   
3573 O  O   . PRO B 184 ? 0.2505 0.0681 0.2295 -0.0148 0.0458  -0.0122 184 PRO B O   
3574 C  CB  . PRO B 184 ? 0.1904 0.0778 0.1879 0.0330  -0.0359 -0.0257 184 PRO B CB  
3575 C  CG  . PRO B 184 ? 0.1611 0.0498 0.1668 0.0027  -0.0035 -0.0049 184 PRO B CG  
3576 C  CD  . PRO B 184 ? 0.1916 0.0411 0.1555 -0.0311 -0.0305 0.0190  184 PRO B CD  
3577 N  N   . GLU B 185 ? 0.2214 0.0313 0.2460 0.0162  0.0109  0.0299  185 GLU B N   
3578 C  CA  . GLU B 185 ? 0.2876 0.0121 0.2323 0.0033  -0.0124 0.0359  185 GLU B CA  
3579 C  C   . GLU B 185 ? 0.2109 0.0279 0.2426 -0.0011 0.0114  -0.0085 185 GLU B C   
3580 O  O   . GLU B 185 ? 0.2383 0.0516 0.2422 -0.0381 0.0013  0.0164  185 GLU B O   
3581 C  CB  . GLU B 185 ? 0.4068 0.0092 0.2832 -0.0070 -0.0354 -0.0269 185 GLU B CB  
3582 C  CG  . GLU B 185 ? 0.3833 0.0722 0.3089 0.0006  -0.0619 -0.0348 185 GLU B CG  
3583 C  CD  . GLU B 185 ? 0.4907 0.0487 0.6185 -0.0991 0.1370  -0.0546 185 GLU B CD  
3584 O  OE1 . GLU B 185 ? 0.5551 0.3434 0.7004 0.0161  0.1243  0.0544  185 GLU B OE1 
3585 O  OE2 . GLU B 185 ? 0.5723 0.4796 0.7939 -0.2760 0.1706  -0.0760 185 GLU B OE2 
3586 N  N   . ARG B 186 ? 0.2067 0.0419 0.2195 -0.0295 -0.0029 0.0282  186 ARG B N   
3587 C  CA  . ARG B 186 ? 0.2739 0.0227 0.2441 -0.0287 -0.0052 0.0208  186 ARG B CA  
3588 C  C   . ARG B 186 ? 0.2017 0.0124 0.2685 -0.0145 -0.0110 0.0369  186 ARG B C   
3589 O  O   . ARG B 186 ? 0.2069 0.0356 0.2552 -0.0147 -0.0177 0.0328  186 ARG B O   
3590 C  CB  . ARG B 186 ? 0.2543 0.0462 0.2953 -0.0384 -0.0334 0.0322  186 ARG B CB  
3591 C  CG  . ARG B 186 ? 0.3495 0.0710 0.4105 -0.0924 -0.0540 0.0685  186 ARG B CG  
3592 C  CD  . ARG B 186 ? 0.3486 0.1115 0.3590 0.0083  0.0348  0.0458  186 ARG B CD  
3593 N  NE  . ARG B 186 ? 0.3710 0.1273 0.4424 0.0514  0.0633  0.0622  186 ARG B NE  
3594 C  CZ  . ARG B 186 ? 0.5396 0.2342 0.4623 -0.0917 0.1359  0.0959  186 ARG B CZ  
3595 N  NH1 . ARG B 186 ? 0.5565 0.1689 0.5974 0.0989  -0.0096 -0.0179 186 ARG B NH1 
3596 N  NH2 . ARG B 186 ? 0.4448 0.3391 0.7936 -0.0954 0.0888  0.0388  186 ARG B NH2 
3597 N  N   . THR B 187 ? 0.1690 0.0268 0.2770 -0.0211 0.0082  0.0630  187 THR B N   
3598 C  CA  . THR B 187 ? 0.1647 0.0394 0.2148 -0.0359 -0.0162 0.0606  187 THR B CA  
3599 C  C   . THR B 187 ? 0.1622 0.0364 0.2191 -0.0373 -0.0178 0.0325  187 THR B C   
3600 O  O   . THR B 187 ? 0.1694 0.0615 0.2196 -0.0595 -0.0332 0.0403  187 THR B O   
3601 C  CB  . THR B 187 ? 0.1862 0.0586 0.2344 0.0207  0.0173  0.0356  187 THR B CB  
3602 O  OG1 . THR B 187 ? 0.1912 0.0428 0.2894 -0.0024 -0.0057 0.0275  187 THR B OG1 
3603 C  CG2 . THR B 187 ? 0.1900 0.0498 0.2460 0.0313  0.0186  0.0381  187 THR B CG2 
3604 N  N   . ALA B 188 ? 0.1582 0.0945 0.1981 -0.0304 0.0089  0.0412  188 ALA B N   
3605 C  CA  . ALA B 188 ? 0.1803 0.0435 0.2096 -0.0179 0.0073  0.0754  188 ALA B CA  
3606 C  C   . ALA B 188 ? 0.1848 0.0562 0.2117 -0.0145 0.0058  0.0598  188 ALA B C   
3607 O  O   . ALA B 188 ? 0.1882 0.0571 0.2149 -0.0145 0.0273  0.0350  188 ALA B O   
3608 C  CB  . ALA B 188 ? 0.1934 0.1298 0.2164 -0.0707 -0.0010 0.0945  188 ALA B CB  
3609 N  N   A GLU B 189 ? 0.1601 0.0224 0.2402 -0.0123 0.0038  0.0590  189 GLU B N   
3610 N  N   B GLU B 189 ? 0.1607 0.0217 0.2415 -0.0125 0.0038  0.0577  189 GLU B N   
3611 C  CA  A GLU B 189 ? 0.1670 0.0198 0.2170 -0.0021 -0.0132 0.0265  189 GLU B CA  
3612 C  CA  B GLU B 189 ? 0.1679 0.0179 0.2178 -0.0024 -0.0138 0.0259  189 GLU B CA  
3613 C  C   A GLU B 189 ? 0.1988 0.0089 0.1948 0.0143  -0.0072 0.0162  189 GLU B C   
3614 C  C   B GLU B 189 ? 0.1995 0.0087 0.1956 0.0126  -0.0083 0.0165  189 GLU B C   
3615 O  O   A GLU B 189 ? 0.1992 0.0229 0.1909 -0.0127 0.0103  0.0047  189 GLU B O   
3616 O  O   B GLU B 189 ? 0.1998 0.0223 0.1931 -0.0118 0.0114  0.0049  189 GLU B O   
3617 C  CB  A GLU B 189 ? 0.2115 0.0232 0.2726 -0.0227 0.0301  0.0103  189 GLU B CB  
3618 C  CB  B GLU B 189 ? 0.2184 0.0275 0.2694 -0.0187 0.0303  0.0071  189 GLU B CB  
3619 C  CG  A GLU B 189 ? 0.1854 0.0134 0.2967 0.0047  0.0020  0.0449  189 GLU B CG  
3620 C  CG  B GLU B 189 ? 0.2115 0.0112 0.3014 0.0022  -0.0066 0.0381  189 GLU B CG  
3621 C  CD  A GLU B 189 ? 0.2789 0.0371 0.3458 0.0228  0.0541  0.1019  189 GLU B CD  
3622 C  CD  B GLU B 189 ? 0.3190 0.0100 0.4094 0.0066  0.0474  0.0387  189 GLU B CD  
3623 O  OE1 A GLU B 189 ? 0.2854 0.0230 0.5120 -0.0670 0.0922  -0.0059 189 GLU B OE1 
3624 O  OE1 B GLU B 189 ? 0.2976 0.1121 0.4815 -0.0135 0.0347  -0.0047 189 GLU B OE1 
3625 O  OE2 A GLU B 189 ? 0.3046 0.1013 0.4938 -0.0806 0.0814  0.0780  189 GLU B OE2 
3626 O  OE2 B GLU B 189 ? 0.4025 0.1918 0.4836 0.0165  0.0480  -0.0673 189 GLU B OE2 
3627 N  N   . TYR B 190 ? 0.1859 0.0296 0.1618 -0.0284 0.0049  0.0301  190 TYR B N   
3628 C  CA  . TYR B 190 ? 0.2211 0.0138 0.2025 0.0014  -0.0222 0.0378  190 TYR B CA  
3629 C  C   . TYR B 190 ? 0.1624 0.0161 0.1830 0.0195  0.0046  0.0365  190 TYR B C   
3630 O  O   . TYR B 190 ? 0.1661 0.0135 0.1815 -0.0027 -0.0023 0.0354  190 TYR B O   
3631 C  CB  . TYR B 190 ? 0.1338 0.0481 0.1819 0.0209  0.0111  0.0097  190 TYR B CB  
3632 C  CG  . TYR B 190 ? 0.1420 0.0207 0.1632 -0.0021 0.0183  0.0286  190 TYR B CG  
3633 C  CD1 . TYR B 190 ? 0.1712 0.0161 0.1808 0.0401  0.0191  0.0046  190 TYR B CD1 
3634 C  CD2 . TYR B 190 ? 0.1722 0.0301 0.2024 -0.0148 0.0477  0.0597  190 TYR B CD2 
3635 C  CE1 . TYR B 190 ? 0.1479 0.0145 0.2044 0.0148  0.0434  0.0394  190 TYR B CE1 
3636 C  CE2 . TYR B 190 ? 0.1690 0.0533 0.1660 0.0263  -0.0055 0.0412  190 TYR B CE2 
3637 C  CZ  . TYR B 190 ? 0.1535 0.0751 0.1708 0.0107  0.0345  0.0394  190 TYR B CZ  
3638 O  OH  . TYR B 190 ? 0.1758 0.0697 0.1452 0.0117  0.0243  0.0444  190 TYR B OH  
3639 N  N   . TYR B 191 ? 0.1380 0.0265 0.1530 -0.0064 -0.0059 0.0076  191 TYR B N   
3640 C  CA  . TYR B 191 ? 0.1275 0.0251 0.1618 0.0003  0.0006  0.0062  191 TYR B CA  
3641 C  C   . TYR B 191 ? 0.1345 0.0401 0.1202 0.0257  0.0198  0.0268  191 TYR B C   
3642 O  O   . TYR B 191 ? 0.1689 0.0546 0.1171 0.0000  -0.0143 0.0060  191 TYR B O   
3643 C  CB  . TYR B 191 ? 0.1403 0.0192 0.1560 0.0363  0.0031  0.0201  191 TYR B CB  
3644 C  CG  . TYR B 191 ? 0.1397 0.0079 0.1787 0.0107  0.0044  0.0112  191 TYR B CG  
3645 C  CD1 . TYR B 191 ? 0.1561 0.0196 0.2001 0.0312  -0.0013 0.0234  191 TYR B CD1 
3646 C  CD2 . TYR B 191 ? 0.1662 0.0073 0.1637 0.0025  0.0071  0.0121  191 TYR B CD2 
3647 C  CE1 . TYR B 191 ? 0.1631 0.0074 0.1916 0.0062  -0.0005 0.0126  191 TYR B CE1 
3648 C  CE2 . TYR B 191 ? 0.1727 0.0065 0.1946 0.0059  0.0038  0.0016  191 TYR B CE2 
3649 C  CZ  . TYR B 191 ? 0.2044 0.0178 0.1606 0.0284  0.0072  0.0114  191 TYR B CZ  
3650 O  OH  . TYR B 191 ? 0.2128 0.0373 0.2618 0.0252  -0.0037 -0.0396 191 TYR B OH  
3651 N  N   . ARG B 192 ? 0.1679 0.0080 0.1588 0.0115  0.0000  0.0114  192 ARG B N   
3652 C  CA  . ARG B 192 ? 0.1613 0.0266 0.1280 0.0348  -0.0018 0.0035  192 ARG B CA  
3653 C  C   . ARG B 192 ? 0.1645 0.0318 0.1015 -0.0031 0.0284  0.0242  192 ARG B C   
3654 O  O   . ARG B 192 ? 0.2101 0.0171 0.1485 0.0031  -0.0083 0.0139  192 ARG B O   
3655 C  CB  . ARG B 192 ? 0.1929 0.0220 0.1395 0.0310  0.0295  0.0148  192 ARG B CB  
3656 C  CG  . ARG B 192 ? 0.2017 0.0760 0.1635 0.0877  -0.0039 -0.0219 192 ARG B CG  
3657 C  CD  . ARG B 192 ? 0.2304 0.0216 0.1858 0.0297  -0.0163 0.0070  192 ARG B CD  
3658 N  NE  . ARG B 192 ? 0.1713 0.0915 0.1790 0.0484  0.0069  0.0009  192 ARG B NE  
3659 C  CZ  . ARG B 192 ? 0.1785 0.0496 0.1912 0.0768  -0.0008 0.0391  192 ARG B CZ  
3660 N  NH1 . ARG B 192 ? 0.2597 0.0553 0.1929 0.0596  0.0343  0.0417  192 ARG B NH1 
3661 N  NH2 . ARG B 192 ? 0.1890 0.0559 0.2110 0.0628  0.0013  0.0049  192 ARG B NH2 
3662 N  N   . TYR B 193 ? 0.2052 0.0274 0.1107 0.0067  -0.0006 0.0299  193 TYR B N   
3663 C  CA  . TYR B 193 ? 0.2060 0.0347 0.1814 0.0168  -0.0085 -0.0225 193 TYR B CA  
3664 C  C   . TYR B 193 ? 0.1597 0.0378 0.0864 0.0142  -0.0054 -0.0255 193 TYR B C   
3665 O  O   . TYR B 193 ? 0.1780 0.0138 0.1392 0.0027  -0.0172 0.0026  193 TYR B O   
3666 C  CB  . TYR B 193 ? 0.1826 0.0538 0.1302 -0.0215 -0.0244 0.0065  193 TYR B CB  
3667 C  CG  . TYR B 193 ? 0.1456 0.0068 0.1449 0.0081  -0.0066 0.0023  193 TYR B CG  
3668 C  CD1 . TYR B 193 ? 0.1658 0.0111 0.1399 0.0118  -0.0133 0.0001  193 TYR B CD1 
3669 C  CD2 . TYR B 193 ? 0.1603 0.0331 0.1417 -0.0172 0.0032  0.0142  193 TYR B CD2 
3670 C  CE1 . TYR B 193 ? 0.1365 0.0075 0.1680 0.0014  -0.0010 0.0139  193 TYR B CE1 
3671 C  CE2 . TYR B 193 ? 0.1775 0.0071 0.1294 0.0070  -0.0064 -0.0083 193 TYR B CE2 
3672 C  CZ  . TYR B 193 ? 0.1119 0.0199 0.1207 -0.0153 -0.0212 0.0190  193 TYR B CZ  
3673 O  OH  . TYR B 193 ? 0.1714 0.0069 0.1374 -0.0094 -0.0013 0.0033  193 TYR B OH  
3674 N  N   . ARG B 194 ? 0.2037 0.0117 0.1582 -0.0308 -0.0276 0.0132  194 ARG B N   
3675 C  CA  . ARG B 194 ? 0.2472 0.0074 0.1627 0.0035  0.0294  -0.0032 194 ARG B CA  
3676 C  C   . ARG B 194 ? 0.1981 0.0145 0.1732 0.0078  -0.0122 -0.0047 194 ARG B C   
3677 O  O   . ARG B 194 ? 0.2319 0.0076 0.2096 -0.0138 -0.0675 0.0122  194 ARG B O   
3678 C  CB  . ARG B 194 ? 0.3522 0.0749 0.1808 -0.0301 0.0185  -0.0316 194 ARG B CB  
3679 C  CG  . ARG B 194 ? 0.4331 0.2618 0.2313 -0.1040 0.0926  -0.0590 194 ARG B CG  
3680 C  CD  . ARG B 194 ? 0.5200 0.4197 0.2404 -0.0035 0.1486  -0.0604 194 ARG B CD  
3681 N  NE  . ARG B 194 ? 0.4954 0.5996 0.4987 0.0127  0.1646  -0.0005 194 ARG B NE  
3682 C  CZ  . ARG B 194 ? 0.4290 0.6979 0.6989 -0.0640 0.1463  0.1106  194 ARG B CZ  
3683 N  NH1 . ARG B 194 ? 0.5208 0.8273 0.8655 0.0833  0.1465  0.0677  194 ARG B NH1 
3684 N  NH2 . ARG B 194 ? 0.2906 0.7322 0.6519 -0.0326 0.0249  0.1976  194 ARG B NH2 
3685 N  N   . GLY B 195 ? 0.1929 0.0238 0.1464 -0.0168 -0.0155 -0.0072 195 GLY B N   
3686 C  CA  . GLY B 195 ? 0.1692 0.0104 0.2019 -0.0095 -0.0090 0.0268  195 GLY B CA  
3687 C  C   . GLY B 195 ? 0.1732 0.0064 0.1631 -0.0023 -0.0145 -0.0021 195 GLY B C   
3688 O  O   . GLY B 195 ? 0.1622 0.0065 0.2102 -0.0011 -0.0022 -0.0057 195 GLY B O   
3689 N  N   . SER B 196 ? 0.1869 0.0151 0.1546 -0.0335 -0.0197 0.0229  196 SER B N   
3690 C  CA  . SER B 196 ? 0.1805 0.0168 0.1505 -0.0190 -0.0005 0.0347  196 SER B CA  
3691 C  C   . SER B 196 ? 0.1732 0.0063 0.1473 -0.0018 -0.0148 0.0007  196 SER B C   
3692 O  O   . SER B 196 ? 0.1572 0.0066 0.1667 -0.0048 -0.0107 -0.0043 196 SER B O   
3693 C  CB  . SER B 196 ? 0.1452 0.0110 0.1811 -0.0089 -0.0381 -0.0082 196 SER B CB  
3694 O  OG  . SER B 196 ? 0.1572 0.0077 0.2273 0.0023  -0.0083 0.0174  196 SER B OG  
3695 N  N   . LEU B 197 ? 0.1764 0.0097 0.1245 -0.0105 0.0142  0.0168  197 LEU B N   
3696 C  CA  . LEU B 197 ? 0.1465 0.0135 0.1218 -0.0146 -0.0162 0.0270  197 LEU B CA  
3697 C  C   . LEU B 197 ? 0.1571 0.0267 0.1570 0.0015  -0.0141 -0.0138 197 LEU B C   
3698 O  O   . LEU B 197 ? 0.1379 0.0093 0.1758 0.0195  -0.0069 -0.0061 197 LEU B O   
3699 C  CB  . LEU B 197 ? 0.1761 0.0224 0.1889 0.0404  0.0006  0.0344  197 LEU B CB  
3700 C  CG  . LEU B 197 ? 0.1722 0.0590 0.2595 0.0117  0.0104  0.0595  197 LEU B CG  
3701 C  CD1 . LEU B 197 ? 0.2484 0.0765 0.2453 0.0340  0.0314  0.0957  197 LEU B CD1 
3702 C  CD2 . LEU B 197 ? 0.2019 0.1103 0.3010 0.0617  0.0245  0.1287  197 LEU B CD2 
3703 N  N   . THR B 198 ? 0.1304 0.0074 0.1332 0.0007  -0.0096 0.0119  198 THR B N   
3704 C  CA  . THR B 198 ? 0.1042 0.0104 0.1318 -0.0076 -0.0189 -0.0194 198 THR B CA  
3705 C  C   . THR B 198 ? 0.1114 0.0095 0.1846 -0.0182 -0.0115 0.0000  198 THR B C   
3706 O  O   . THR B 198 ? 0.1464 0.0074 0.1817 -0.0023 0.0005  0.0138  198 THR B O   
3707 C  CB  . THR B 198 ? 0.1717 0.0065 0.1455 -0.0044 -0.0561 -0.0009 198 THR B CB  
3708 O  OG1 . THR B 198 ? 0.1358 0.0166 0.1796 -0.0289 -0.0615 0.0371  198 THR B OG1 
3709 C  CG2 . THR B 198 ? 0.1657 0.0142 0.1301 0.0299  -0.0264 0.0114  198 THR B CG2 
3710 N  N   . THR B 199 ? 0.1873 0.0071 0.1327 0.0011  -0.0106 0.0098  199 THR B N   
3711 C  CA  . THR B 199 ? 0.1241 0.0133 0.1557 -0.0157 -0.0277 0.0237  199 THR B CA  
3712 C  C   . THR B 199 ? 0.0789 0.0361 0.1815 0.0012  -0.0221 -0.0079 199 THR B C   
3713 O  O   . THR B 199 ? 0.1647 0.0145 0.1901 -0.0193 -0.0127 -0.0062 199 THR B O   
3714 C  CB  . THR B 199 ? 0.1136 0.0095 0.1664 0.0042  -0.0373 -0.0224 199 THR B CB  
3715 O  OG1 . THR B 199 ? 0.1419 0.0139 0.2067 -0.0200 -0.0144 0.0219  199 THR B OG1 
3716 C  CG2 . THR B 199 ? 0.1781 0.0135 0.1641 -0.0280 -0.0204 -0.0168 199 THR B CG2 
3717 N  N   . PRO B 200 ? 0.1188 0.0089 0.1525 0.0169  -0.0267 -0.0030 200 PRO B N   
3718 C  CA  . PRO B 200 ? 0.1362 0.0110 0.1550 0.0239  -0.0401 -0.0113 200 PRO B CA  
3719 C  C   . PRO B 200 ? 0.1586 0.0249 0.2081 0.0241  -0.0209 0.0086  200 PRO B C   
3720 O  O   . PRO B 200 ? 0.1683 0.0146 0.2144 0.0241  -0.0339 0.0064  200 PRO B O   
3721 C  CB  . PRO B 200 ? 0.1173 0.0548 0.2200 -0.0051 -0.0108 -0.0067 200 PRO B CB  
3722 C  CG  . PRO B 200 ? 0.1350 0.0112 0.1643 -0.0086 0.0000  0.0261  200 PRO B CG  
3723 C  CD  . PRO B 200 ? 0.1257 0.0174 0.1796 -0.0163 -0.0048 0.0072  200 PRO B CD  
3724 N  N   A PRO B 201 ? 0.1814 0.0081 0.2072 0.0155  -0.0429 0.0052  201 PRO B N   
3725 N  N   B PRO B 201 ? 0.1719 0.0090 0.1955 0.0163  -0.0366 0.0101  201 PRO B N   
3726 C  CA  A PRO B 201 ? 0.1773 0.0128 0.1972 0.0054  -0.0256 -0.0148 201 PRO B CA  
3727 C  CA  B PRO B 201 ? 0.1600 0.0164 0.1819 0.0236  -0.0173 -0.0210 201 PRO B CA  
3728 C  C   A PRO B 201 ? 0.1706 0.0132 0.1922 -0.0254 -0.0281 -0.0025 201 PRO B C   
3729 C  C   B PRO B 201 ? 0.1708 0.0081 0.1697 -0.0133 -0.0182 -0.0087 201 PRO B C   
3730 O  O   A PRO B 201 ? 0.1465 0.0259 0.2026 -0.0518 -0.0169 0.0148  201 PRO B O   
3731 O  O   B PRO B 201 ? 0.1356 0.0216 0.1880 0.0093  -0.0150 -0.0163 201 PRO B O   
3732 C  CB  A PRO B 201 ? 0.2165 0.0071 0.2767 -0.0007 -0.0392 0.0150  201 PRO B CB  
3733 C  CB  B PRO B 201 ? 0.1645 0.0065 0.2125 0.0041  -0.0202 -0.0052 201 PRO B CB  
3734 C  CG  A PRO B 201 ? 0.2177 0.0189 0.2231 -0.0411 -0.0441 -0.0209 201 PRO B CG  
3735 C  CG  B PRO B 201 ? 0.1277 0.0569 0.1717 0.0242  -0.0231 -0.0005 201 PRO B CG  
3736 C  CD  A PRO B 201 ? 0.1563 0.0067 0.2100 -0.0015 -0.0254 -0.0088 201 PRO B CD  
3737 C  CD  B PRO B 201 ? 0.1711 0.0086 0.2040 0.0167  -0.0072 -0.0114 201 PRO B CD  
3738 N  N   . CYS B 202 ? 0.1597 0.0064 0.1656 0.0034  -0.0144 0.0027  202 CYS B N   
3739 C  CA  . CYS B 202 ? 0.1719 0.0067 0.1600 0.0078  -0.0206 -0.0008 202 CYS B CA  
3740 C  C   . CYS B 202 ? 0.1619 0.0075 0.1801 -0.0136 0.0050  0.0004  202 CYS B C   
3741 O  O   . CYS B 202 ? 0.1848 0.0128 0.1842 -0.0303 -0.0228 -0.0111 202 CYS B O   
3742 C  CB  . CYS B 202 ? 0.1807 0.0111 0.1899 -0.0283 -0.0219 -0.0024 202 CYS B CB  
3743 S  SG  . CYS B 202 ? 0.1636 0.0070 0.1808 -0.0050 -0.0264 0.0106  202 CYS B SG  
3744 N  N   A ASN B 203 ? 0.1891 0.0072 0.1924 0.0124  0.0132  0.0044  203 ASN B N   
3745 N  N   B ASN B 203 ? 0.1756 0.0068 0.1929 -0.0008 0.0139  -0.0096 203 ASN B N   
3746 C  CA  A ASN B 203 ? 0.2049 0.0266 0.1902 0.0187  0.0129  -0.0145 203 ASN B CA  
3747 C  CA  B ASN B 203 ? 0.1722 0.0132 0.1951 -0.0030 0.0135  -0.0359 203 ASN B CA  
3748 C  C   A ASN B 203 ? 0.1654 0.0159 0.1574 0.0028  -0.0200 -0.0379 203 ASN B C   
3749 C  C   B ASN B 203 ? 0.1532 0.0209 0.1640 0.0000  -0.0216 -0.0474 203 ASN B C   
3750 O  O   A ASN B 203 ? 0.2366 0.0187 0.1641 0.0092  -0.0059 -0.0438 203 ASN B O   
3751 O  O   B ASN B 203 ? 0.2070 0.0175 0.1958 0.0048  -0.0150 -0.0459 203 ASN B O   
3752 C  CB  A ASN B 203 ? 0.2259 0.0580 0.2609 0.0408  0.0013  -0.0017 203 ASN B CB  
3753 C  CB  B ASN B 203 ? 0.1767 0.0340 0.2297 -0.0026 0.0006  -0.0238 203 ASN B CB  
3754 C  CG  A ASN B 203 ? 0.2916 0.0978 0.2897 0.0257  0.0750  0.0293  203 ASN B CG  
3755 C  CG  B ASN B 203 ? 0.1728 0.1057 0.2425 0.0502  0.0110  0.0317  203 ASN B CG  
3756 O  OD1 A ASN B 203 ? 0.4468 0.0772 0.2902 0.0417  -0.0274 0.1347  203 ASN B OD1 
3757 O  OD1 B ASN B 203 ? 0.1076 0.2101 0.3112 0.0501  0.0095  -0.0209 203 ASN B OD1 
3758 N  ND2 A ASN B 203 ? 0.4326 0.2372 0.1546 0.0639  0.0093  -0.0966 203 ASN B ND2 
3759 N  ND2 B ASN B 203 ? 0.2129 0.0430 0.2533 0.0827  0.0233  0.0384  203 ASN B ND2 
3760 N  N   . PRO B 204 ? 0.2062 0.0390 0.1607 -0.0444 -0.0137 -0.0370 204 PRO B N   
3761 C  CA  . PRO B 204 ? 0.1898 0.0608 0.1791 -0.0133 -0.0239 -0.0142 204 PRO B CA  
3762 C  C   . PRO B 204 ? 0.2114 0.0114 0.1851 -0.0004 0.0013  -0.0302 204 PRO B C   
3763 O  O   . PRO B 204 ? 0.2537 0.0926 0.1979 -0.0085 -0.0040 -0.0487 204 PRO B O   
3764 C  CB  . PRO B 204 ? 0.2092 0.0297 0.2336 -0.0405 -0.0436 -0.0372 204 PRO B CB  
3765 C  CG  . PRO B 204 ? 0.2739 0.0419 0.1687 -0.0743 0.0282  -0.0565 204 PRO B CG  
3766 C  CD  . PRO B 204 ? 0.1568 0.1413 0.1683 -0.0651 -0.0286 -0.0945 204 PRO B CD  
3767 N  N   . THR B 205 ? 0.2113 0.0086 0.1905 0.0106  0.0087  -0.0178 205 THR B N   
3768 C  CA  . THR B 205 ? 0.1797 0.0338 0.1889 0.0000  -0.0072 0.0114  205 THR B CA  
3769 C  C   . THR B 205 ? 0.2058 0.0103 0.2657 0.0227  -0.0127 -0.0202 205 THR B C   
3770 O  O   . THR B 205 ? 0.2116 0.0261 0.2666 0.0334  -0.0106 -0.0537 205 THR B O   
3771 C  CB  . THR B 205 ? 0.2740 0.0149 0.1724 0.0160  -0.0343 -0.0371 205 THR B CB  
3772 O  OG1 . THR B 205 ? 0.2687 0.0277 0.1905 0.0301  -0.0245 -0.0042 205 THR B OG1 
3773 C  CG2 . THR B 205 ? 0.2016 0.0866 0.2200 -0.0430 0.0015  -0.0724 205 THR B CG2 
3774 N  N   . VAL B 206 ? 0.1708 0.0207 0.1907 0.0060  0.0092  -0.0449 206 VAL B N   
3775 C  CA  . VAL B 206 ? 0.1935 0.0065 0.1682 -0.0022 -0.0075 -0.0052 206 VAL B CA  
3776 C  C   . VAL B 206 ? 0.1620 0.0066 0.1617 -0.0029 -0.0041 -0.0063 206 VAL B C   
3777 O  O   . VAL B 206 ? 0.1904 0.0250 0.2224 0.0030  -0.0079 0.0144  206 VAL B O   
3778 C  CB  . VAL B 206 ? 0.1734 0.0074 0.1484 -0.0133 0.0007  0.0012  206 VAL B CB  
3779 C  CG1 . VAL B 206 ? 0.1679 0.0277 0.2157 -0.0252 0.0076  -0.0465 206 VAL B CG1 
3780 C  CG2 . VAL B 206 ? 0.1851 0.0113 0.1943 0.0236  0.0156  0.0206  206 VAL B CG2 
3781 N  N   A LEU B 207 ? 0.1777 0.0069 0.2062 0.0090  0.0613  0.0086  207 LEU B N   
3782 N  N   B LEU B 207 ? 0.1843 0.0067 0.1930 0.0040  0.0490  0.0083  207 LEU B N   
3783 C  CA  A LEU B 207 ? 0.1859 0.0080 0.1508 0.0157  0.0205  0.0087  207 LEU B CA  
3784 C  CA  B LEU B 207 ? 0.2070 0.0085 0.1476 0.0122  0.0093  0.0152  207 LEU B CA  
3785 C  C   A LEU B 207 ? 0.1555 0.0069 0.1643 0.0087  0.0280  -0.0011 207 LEU B C   
3786 C  C   B LEU B 207 ? 0.1460 0.0221 0.1546 0.0108  0.0120  0.0012  207 LEU B C   
3787 O  O   A LEU B 207 ? 0.2176 0.0197 0.1640 -0.0009 -0.0103 -0.0171 207 LEU B O   
3788 O  O   B LEU B 207 ? 0.1904 0.0172 0.1482 -0.0026 -0.0146 0.0166  207 LEU B O   
3789 C  CB  A LEU B 207 ? 0.2033 0.0302 0.1877 0.0457  0.0391  0.0148  207 LEU B CB  
3790 C  CB  B LEU B 207 ? 0.2386 0.0805 0.1553 0.0334  0.0335  -0.0078 207 LEU B CB  
3791 C  CG  A LEU B 207 ? 0.2069 0.0141 0.1758 0.0294  0.0078  -0.0230 207 LEU B CG  
3792 C  CG  B LEU B 207 ? 0.3243 0.0320 0.1679 0.0209  -0.0288 -0.0058 207 LEU B CG  
3793 C  CD1 A LEU B 207 ? 0.2769 0.0142 0.1925 0.0368  -0.0128 -0.0246 207 LEU B CD1 
3794 C  CD1 B LEU B 207 ? 0.3629 0.1725 0.1553 0.0641  0.0251  -0.0391 207 LEU B CD1 
3795 C  CD2 A LEU B 207 ? 0.1793 0.0970 0.2052 0.0081  -0.0105 0.0293  207 LEU B CD2 
3796 C  CD2 B LEU B 207 ? 0.2655 0.1374 0.2308 0.0298  -0.0211 -0.0188 207 LEU B CD2 
3797 N  N   . TRP B 208 ? 0.1184 0.0094 0.1615 -0.0066 0.0043  -0.0151 208 TRP B N   
3798 C  CA  . TRP B 208 ? 0.1608 0.0066 0.1373 0.0008  0.0240  0.0060  208 TRP B CA  
3799 C  C   . TRP B 208 ? 0.1792 0.0075 0.1315 -0.0029 0.0216  0.0113  208 TRP B C   
3800 O  O   . TRP B 208 ? 0.2088 0.0078 0.1496 0.0118  -0.0013 0.0108  208 TRP B O   
3801 C  CB  . TRP B 208 ? 0.1482 0.0277 0.1671 0.0243  0.0103  0.0170  208 TRP B CB  
3802 C  CG  . TRP B 208 ? 0.1761 0.0075 0.1359 0.0134  -0.0142 -0.0063 208 TRP B CG  
3803 C  CD1 . TRP B 208 ? 0.1708 0.0153 0.1434 0.0285  -0.0490 -0.0307 208 TRP B CD1 
3804 C  CD2 . TRP B 208 ? 0.1435 0.0178 0.1435 -0.0005 0.0025  -0.0160 208 TRP B CD2 
3805 N  NE1 . TRP B 208 ? 0.1620 0.0156 0.1699 0.0079  -0.0027 -0.0221 208 TRP B NE1 
3806 C  CE2 . TRP B 208 ? 0.1602 0.0089 0.1191 0.0190  -0.0011 0.0045  208 TRP B CE2 
3807 C  CE3 . TRP B 208 ? 0.1345 0.0230 0.1455 0.0215  -0.0069 -0.0206 208 TRP B CE3 
3808 C  CZ2 . TRP B 208 ? 0.1517 0.0191 0.1051 0.0162  0.0064  -0.0320 208 TRP B CZ2 
3809 C  CZ3 . TRP B 208 ? 0.1297 0.0232 0.1538 -0.0248 0.0109  0.0012  208 TRP B CZ3 
3810 C  CH2 . TRP B 208 ? 0.1346 0.0084 0.1361 -0.0083 -0.0158 -0.0130 208 TRP B CH2 
3811 N  N   . THR B 209 ? 0.1254 0.0126 0.1652 -0.0130 -0.0062 0.0284  209 THR B N   
3812 C  CA  . THR B 209 ? 0.1464 0.0139 0.1697 -0.0114 0.0240  0.0308  209 THR B CA  
3813 C  C   . THR B 209 ? 0.1654 0.0348 0.1412 -0.0030 -0.0309 -0.0034 209 THR B C   
3814 O  O   . THR B 209 ? 0.1822 0.0102 0.1508 0.0220  -0.0212 0.0098  209 THR B O   
3815 C  CB  . THR B 209 ? 0.1396 0.0218 0.1654 -0.0200 0.0202  0.0409  209 THR B CB  
3816 O  OG1 . THR B 209 ? 0.1536 0.0314 0.1647 -0.0021 0.0023  0.0284  209 THR B OG1 
3817 C  CG2 . THR B 209 ? 0.2052 0.0099 0.1992 -0.0260 0.0100  0.0039  209 THR B CG2 
3818 N  N   . VAL B 210 ? 0.1300 0.0153 0.1534 -0.0154 0.0108  0.0135  210 VAL B N   
3819 C  CA  . VAL B 210 ? 0.1227 0.0175 0.1398 -0.0193 0.0066  0.0313  210 VAL B CA  
3820 C  C   . VAL B 210 ? 0.1600 0.0192 0.1176 -0.0384 0.0036  0.0183  210 VAL B C   
3821 O  O   . VAL B 210 ? 0.1672 0.0221 0.1367 0.0015  0.0041  0.0264  210 VAL B O   
3822 C  CB  . VAL B 210 ? 0.1155 0.0092 0.1642 -0.0089 0.0236  0.0164  210 VAL B CB  
3823 C  CG1 . VAL B 210 ? 0.1360 0.0176 0.1504 0.0268  0.0110  0.0308  210 VAL B CG1 
3824 C  CG2 . VAL B 210 ? 0.0972 0.0387 0.1816 -0.0406 -0.0148 0.0561  210 VAL B CG2 
3825 N  N   . PHE B 211 ? 0.1477 0.0124 0.1662 -0.0288 -0.0109 0.0084  211 PHE B N   
3826 C  CA  . PHE B 211 ? 0.1455 0.0118 0.1716 -0.0238 -0.0166 0.0177  211 PHE B CA  
3827 C  C   . PHE B 211 ? 0.1471 0.0529 0.1589 -0.0081 -0.0127 0.0410  211 PHE B C   
3828 O  O   . PHE B 211 ? 0.1725 0.0074 0.1841 -0.0068 0.0060  0.0115  211 PHE B O   
3829 C  CB  . PHE B 211 ? 0.1465 0.0088 0.1868 -0.0139 -0.0285 0.0166  211 PHE B CB  
3830 C  CG  . PHE B 211 ? 0.1567 0.0262 0.1433 -0.0017 -0.0084 0.0177  211 PHE B CG  
3831 C  CD1 . PHE B 211 ? 0.1518 0.0519 0.1925 -0.0111 0.0111  0.0157  211 PHE B CD1 
3832 C  CD2 . PHE B 211 ? 0.1602 0.0072 0.1660 -0.0120 -0.0165 0.0016  211 PHE B CD2 
3833 C  CE1 . PHE B 211 ? 0.1636 0.0340 0.2188 -0.0038 -0.0040 0.0064  211 PHE B CE1 
3834 C  CE2 . PHE B 211 ? 0.1523 0.0255 0.1854 -0.0175 0.0092  -0.0046 211 PHE B CE2 
3835 C  CZ  . PHE B 211 ? 0.1561 0.0556 0.1755 -0.0185 -0.0020 0.0050  211 PHE B CZ  
3836 N  N   . ARG B 212 ? 0.1845 0.0073 0.1852 -0.0005 -0.0178 0.0132  212 ARG B N   
3837 C  CA  . ARG B 212 ? 0.1740 0.0296 0.1719 0.0138  0.0201  0.0188  212 ARG B CA  
3838 C  C   . ARG B 212 ? 0.1834 0.0374 0.1445 0.0044  -0.0011 0.0407  212 ARG B C   
3839 O  O   . ARG B 212 ? 0.1991 0.0136 0.2040 -0.0079 0.0250  -0.0188 212 ARG B O   
3840 C  CB  . ARG B 212 ? 0.1732 0.0331 0.1794 0.0288  0.0094  0.0419  212 ARG B CB  
3841 C  CG  . ARG B 212 ? 0.2214 0.0171 0.1425 0.0414  -0.0115 0.0172  212 ARG B CG  
3842 C  CD  . ARG B 212 ? 0.2630 0.0304 0.1943 0.0502  -0.0153 0.0487  212 ARG B CD  
3843 N  NE  . ARG B 212 ? 0.2773 0.0282 0.2268 0.0613  -0.0252 0.0359  212 ARG B NE  
3844 C  CZ  . ARG B 212 ? 0.2909 0.0559 0.1893 0.0883  -0.0138 0.0274  212 ARG B CZ  
3845 N  NH1 . ARG B 212 ? 0.3586 0.0232 0.2697 0.0659  0.0510  0.0063  212 ARG B NH1 
3846 N  NH2 . ARG B 212 ? 0.2931 0.1362 0.2996 0.1244  0.0147  0.0653  212 ARG B NH2 
3847 N  N   . ASN B 213 ? 0.1999 0.0098 0.1485 0.0252  -0.0214 0.0021  213 ASN B N   
3848 C  CA  . ASN B 213 ? 0.1839 0.0104 0.1474 -0.0005 -0.0201 0.0054  213 ASN B CA  
3849 C  C   . ASN B 213 ? 0.1688 0.0245 0.1629 0.0086  -0.0209 0.0160  213 ASN B C   
3850 O  O   . ASN B 213 ? 0.2063 0.0099 0.1576 0.0133  -0.0072 0.0197  213 ASN B O   
3851 C  CB  . ASN B 213 ? 0.2757 0.0211 0.1791 -0.0630 -0.0195 0.0064  213 ASN B CB  
3852 C  CG  . ASN B 213 ? 0.2621 0.0472 0.2517 0.0201  0.0174  0.0737  213 ASN B CG  
3853 O  OD1 . ASN B 213 ? 0.2758 0.0604 0.4077 -0.0088 0.0016  0.1065  213 ASN B OD1 
3854 N  ND2 . ASN B 213 ? 0.2635 0.0617 0.3510 -0.0242 0.0328  0.0801  213 ASN B ND2 
3855 N  N   . PRO B 214 ? 0.1864 0.0340 0.1609 0.0162  -0.0138 0.0047  214 PRO B N   
3856 C  CA  . PRO B 214 ? 0.1420 0.0070 0.1787 0.0027  -0.0238 0.0097  214 PRO B CA  
3857 C  C   . PRO B 214 ? 0.1597 0.0085 0.1499 -0.0053 -0.0350 0.0151  214 PRO B C   
3858 O  O   . PRO B 214 ? 0.1829 0.0066 0.1963 -0.0075 -0.0076 0.0019  214 PRO B O   
3859 C  CB  . PRO B 214 ? 0.1397 0.0247 0.2448 0.0100  -0.0054 0.0134  214 PRO B CB  
3860 C  CG  . PRO B 214 ? 0.2509 0.0309 0.1923 0.0166  -0.0006 0.0176  214 PRO B CG  
3861 C  CD  . PRO B 214 ? 0.2328 0.0239 0.2020 0.0251  0.0027  -0.0022 214 PRO B CD  
3862 N  N   . VAL B 215 ? 0.1604 0.0188 0.1263 0.0004  -0.0143 0.0104  215 VAL B N   
3863 C  CA  . VAL B 215 ? 0.1619 0.0094 0.1322 0.0210  -0.0229 0.0019  215 VAL B CA  
3864 C  C   . VAL B 215 ? 0.1412 0.0079 0.1622 -0.0019 -0.0061 0.0054  215 VAL B C   
3865 O  O   . VAL B 215 ? 0.1458 0.0101 0.1872 0.0075  -0.0389 -0.0260 215 VAL B O   
3866 C  CB  . VAL B 215 ? 0.1337 0.0155 0.2048 0.0041  0.0136  0.0428  215 VAL B CB  
3867 C  CG1 . VAL B 215 ? 0.1578 0.0156 0.1967 0.0000  0.0076  0.0150  215 VAL B CG1 
3868 C  CG2 . VAL B 215 ? 0.1717 0.0119 0.2430 -0.0132 -0.0102 0.0335  215 VAL B CG2 
3869 N  N   . GLN B 216 ? 0.1751 0.0079 0.1636 -0.0121 -0.0258 0.0121  216 GLN B N   
3870 C  CA  . GLN B 216 ? 0.1491 0.0071 0.1463 -0.0006 -0.0341 0.0102  216 GLN B CA  
3871 C  C   . GLN B 216 ? 0.1148 0.0068 0.1476 0.0017  -0.0260 0.0072  216 GLN B C   
3872 O  O   . GLN B 216 ? 0.1146 0.0365 0.1821 0.0023  -0.0167 -0.0022 216 GLN B O   
3873 C  CB  . GLN B 216 ? 0.1553 0.0197 0.1722 0.0146  -0.0443 -0.0208 216 GLN B CB  
3874 C  CG  . GLN B 216 ? 0.2041 0.0180 0.2116 0.0326  -0.0576 -0.0075 216 GLN B CG  
3875 C  CD  . GLN B 216 ? 0.2834 0.0252 0.1764 0.0009  -0.0273 -0.0159 216 GLN B CD  
3876 O  OE1 . GLN B 216 ? 0.2236 0.0445 0.2340 -0.0055 -0.0475 -0.0280 216 GLN B OE1 
3877 N  NE2 . GLN B 216 ? 0.4135 0.1148 0.2417 0.0343  -0.1156 0.0146  216 GLN B NE2 
3878 N  N   . ILE B 217 ? 0.1598 0.0063 0.1310 -0.0013 -0.0082 -0.0022 217 ILE B N   
3879 C  CA  . ILE B 217 ? 0.1776 0.0093 0.1306 0.0205  -0.0142 -0.0097 217 ILE B CA  
3880 C  C   . ILE B 217 ? 0.1572 0.0069 0.1446 -0.0088 0.0053  -0.0029 217 ILE B C   
3881 O  O   . ILE B 217 ? 0.1535 0.0146 0.1697 -0.0189 -0.0242 -0.0064 217 ILE B O   
3882 C  CB  . ILE B 217 ? 0.1004 0.0085 0.1516 0.0086  -0.0276 -0.0165 217 ILE B CB  
3883 C  CG1 . ILE B 217 ? 0.0941 0.0100 0.1819 0.0134  -0.0102 0.0152  217 ILE B CG1 
3884 C  CG2 . ILE B 217 ? 0.1182 0.0559 0.1661 0.0125  -0.0057 -0.0159 217 ILE B CG2 
3885 C  CD1 . ILE B 217 ? 0.1472 0.0064 0.1995 -0.0033 -0.0328 0.0038  217 ILE B CD1 
3886 N  N   . SER B 218 ? 0.1489 0.0068 0.1362 0.0079  0.0035  -0.0031 218 SER B N   
3887 C  CA  . SER B 218 ? 0.1229 0.0376 0.1270 0.0019  -0.0034 -0.0066 218 SER B CA  
3888 C  C   . SER B 218 ? 0.1363 0.0132 0.1126 0.0017  -0.0158 0.0002  218 SER B C   
3889 O  O   . SER B 218 ? 0.1691 0.0161 0.1560 -0.0394 -0.0419 0.0051  218 SER B O   
3890 C  CB  . SER B 218 ? 0.1869 0.0194 0.1579 0.0002  -0.0585 0.0083  218 SER B CB  
3891 O  OG  . SER B 218 ? 0.2027 0.0071 0.1424 0.0054  -0.0302 0.0021  218 SER B OG  
3892 N  N   . GLN B 219 ? 0.1439 0.0126 0.1772 0.0128  0.0106  0.0024  219 GLN B N   
3893 C  CA  . GLN B 219 ? 0.1559 0.0138 0.1622 0.0170  0.0042  0.0201  219 GLN B CA  
3894 C  C   . GLN B 219 ? 0.1578 0.0098 0.1805 0.0107  0.0061  0.0223  219 GLN B C   
3895 O  O   . GLN B 219 ? 0.1967 0.0099 0.1778 -0.0146 -0.0055 0.0070  219 GLN B O   
3896 C  CB  . GLN B 219 ? 0.1937 0.0288 0.2447 0.0468  0.0290  0.0175  219 GLN B CB  
3897 C  CG  . GLN B 219 ? 0.2020 0.1761 0.2883 0.0648  0.0661  0.0486  219 GLN B CG  
3898 C  CD  . GLN B 219 ? 0.3802 0.0787 0.3629 0.0791  0.0012  0.0593  219 GLN B CD  
3899 O  OE1 . GLN B 219 ? 0.5231 0.1589 0.3881 -0.0791 -0.0707 0.0157  219 GLN B OE1 
3900 N  NE2 . GLN B 219 ? 0.3848 0.4822 0.3721 0.0370  -0.0897 0.0482  219 GLN B NE2 
3901 N  N   . GLU B 220 ? 0.1653 0.0189 0.1527 0.0236  -0.0006 -0.0021 220 GLU B N   
3902 C  CA  . GLU B 220 ? 0.1668 0.0416 0.1503 0.0248  -0.0227 -0.0229 220 GLU B CA  
3903 C  C   . GLU B 220 ? 0.1546 0.0198 0.1421 0.0057  0.0019  -0.0082 220 GLU B C   
3904 O  O   . GLU B 220 ? 0.1769 0.0229 0.1916 -0.0160 -0.0136 0.0034  220 GLU B O   
3905 C  CB  . GLU B 220 ? 0.2056 0.0420 0.1439 0.0288  -0.0548 -0.0226 220 GLU B CB  
3906 C  CG  . GLU B 220 ? 0.2049 0.0347 0.1796 0.0128  -0.0044 -0.0188 220 GLU B CG  
3907 C  CD  . GLU B 220 ? 0.2722 0.0538 0.1410 0.0110  -0.0162 -0.0103 220 GLU B CD  
3908 O  OE1 . GLU B 220 ? 0.2802 0.0478 0.1818 -0.0148 0.0013  -0.0160 220 GLU B OE1 
3909 O  OE2 . GLU B 220 ? 0.3947 0.1502 0.2530 0.0741  0.0416  -0.0469 220 GLU B OE2 
3910 N  N   . GLN B 221 ? 0.1476 0.0092 0.1482 0.0169  -0.0004 -0.0108 221 GLN B N   
3911 C  CA  . GLN B 221 ? 0.1362 0.0112 0.1329 0.0239  -0.0151 -0.0103 221 GLN B CA  
3912 C  C   . GLN B 221 ? 0.1606 0.0253 0.1819 -0.0145 -0.0298 0.0574  221 GLN B C   
3913 O  O   . GLN B 221 ? 0.1622 0.0197 0.1758 0.0025  -0.0118 0.0281  221 GLN B O   
3914 C  CB  . GLN B 221 ? 0.1600 0.0095 0.1630 0.0181  -0.0031 -0.0131 221 GLN B CB  
3915 C  CG  . GLN B 221 ? 0.1627 0.0104 0.1894 0.0187  0.0072  -0.0167 221 GLN B CG  
3916 C  CD  . GLN B 221 ? 0.1509 0.0084 0.1814 -0.0068 -0.0141 0.0182  221 GLN B CD  
3917 O  OE1 . GLN B 221 ? 0.1617 0.0065 0.1963 0.0053  -0.0174 0.0026  221 GLN B OE1 
3918 N  NE2 . GLN B 221 ? 0.1761 0.0072 0.2234 0.0024  -0.0078 -0.0139 221 GLN B NE2 
3919 N  N   . LEU B 222 ? 0.1398 0.0101 0.1530 -0.0176 -0.0271 0.0117  222 LEU B N   
3920 C  CA  . LEU B 222 ? 0.1385 0.0350 0.1453 -0.0258 -0.0207 0.0176  222 LEU B CA  
3921 C  C   . LEU B 222 ? 0.1538 0.0164 0.1481 0.0060  0.0095  0.0132  222 LEU B C   
3922 O  O   . LEU B 222 ? 0.1373 0.0167 0.1678 0.0009  -0.0126 0.0406  222 LEU B O   
3923 C  CB  . LEU B 222 ? 0.1566 0.0385 0.1638 0.0055  -0.0275 -0.0026 222 LEU B CB  
3924 C  CG  . LEU B 222 ? 0.1875 0.0067 0.1628 0.0026  -0.0254 -0.0075 222 LEU B CG  
3925 C  CD1 . LEU B 222 ? 0.1789 0.0078 0.2105 0.0156  -0.0204 -0.0053 222 LEU B CD1 
3926 C  CD2 . LEU B 222 ? 0.1715 0.0182 0.1287 -0.0143 -0.0121 -0.0212 222 LEU B CD2 
3927 N  N   . LEU B 223 ? 0.1531 0.0170 0.1445 -0.0099 0.0010  0.0111  223 LEU B N   
3928 C  CA  . LEU B 223 ? 0.1424 0.0305 0.1239 0.0073  0.0181  -0.0082 223 LEU B CA  
3929 C  C   . LEU B 223 ? 0.1496 0.0367 0.1832 -0.0091 0.0320  0.0362  223 LEU B C   
3930 O  O   . LEU B 223 ? 0.1735 0.0211 0.1936 -0.0132 0.0020  0.0403  223 LEU B O   
3931 C  CB  . LEU B 223 ? 0.2015 0.0241 0.1488 0.0201  0.0491  -0.0128 223 LEU B CB  
3932 C  CG  . LEU B 223 ? 0.2196 0.0550 0.1560 0.0150  0.0450  -0.0039 223 LEU B CG  
3933 C  CD1 . LEU B 223 ? 0.2418 0.0277 0.2274 -0.0076 0.0324  0.0113  223 LEU B CD1 
3934 C  CD2 . LEU B 223 ? 0.2536 0.0708 0.1823 0.0233  0.0376  -0.0253 223 LEU B CD2 
3935 N  N   . ALA B 224 ? 0.1531 0.0284 0.1864 -0.0216 -0.0178 0.0407  224 ALA B N   
3936 C  CA  . ALA B 224 ? 0.1703 0.0188 0.2299 0.0054  -0.0170 0.0210  224 ALA B CA  
3937 C  C   . ALA B 224 ? 0.1423 0.0426 0.1658 -0.0289 0.0226  0.0405  224 ALA B C   
3938 O  O   . ALA B 224 ? 0.1467 0.0408 0.2006 -0.0256 -0.0011 0.0499  224 ALA B O   
3939 C  CB  . ALA B 224 ? 0.1665 0.0681 0.2184 0.0189  -0.0271 0.0256  224 ALA B CB  
3940 N  N   . LEU B 225 ? 0.1646 0.0356 0.1629 -0.0085 0.0264  0.0170  225 LEU B N   
3941 C  CA  . LEU B 225 ? 0.1309 0.0608 0.1467 0.0033  0.0207  0.0049  225 LEU B CA  
3942 C  C   . LEU B 225 ? 0.1557 0.0185 0.2142 -0.0031 -0.0099 -0.0021 225 LEU B C   
3943 O  O   . LEU B 225 ? 0.1706 0.0141 0.1888 -0.0316 0.0078  0.0157  225 LEU B O   
3944 C  CB  . LEU B 225 ? 0.1807 0.0410 0.1406 0.0027  0.0173  -0.0052 225 LEU B CB  
3945 C  CG  . LEU B 225 ? 0.1658 0.0626 0.1288 0.0078  -0.0059 0.0013  225 LEU B CG  
3946 C  CD1 . LEU B 225 ? 0.1543 0.0859 0.1647 0.0105  -0.0156 0.0362  225 LEU B CD1 
3947 C  CD2 . LEU B 225 ? 0.2279 0.1049 0.1639 -0.0308 -0.0178 0.0403  225 LEU B CD2 
3948 N  N   . GLU B 226 ? 0.1474 0.0365 0.1599 0.0097  -0.0044 0.0669  226 GLU B N   
3949 C  CA  . GLU B 226 ? 0.1543 0.0714 0.1553 0.0188  0.0221  0.0435  226 GLU B CA  
3950 C  C   . GLU B 226 ? 0.1606 0.0466 0.1638 0.0120  0.0132  0.0451  226 GLU B C   
3951 O  O   . GLU B 226 ? 0.1635 0.1631 0.2028 -0.0367 -0.0021 0.0879  226 GLU B O   
3952 C  CB  . GLU B 226 ? 0.1613 0.1236 0.1103 0.0525  0.0086  0.0340  226 GLU B CB  
3953 C  CG  . GLU B 226 ? 0.1796 0.0428 0.1474 0.0145  -0.0444 0.0496  226 GLU B CG  
3954 C  CD  . GLU B 226 ? 0.1435 0.0699 0.1342 0.0504  -0.0314 0.0231  226 GLU B CD  
3955 O  OE1 . GLU B 226 ? 0.2115 0.1561 0.1369 0.0364  0.0227  0.0328  226 GLU B OE1 
3956 O  OE2 . GLU B 226 ? 0.2078 0.0390 0.1363 0.0299  -0.0041 0.0017  226 GLU B OE2 
3957 N  N   . THR B 227 ? 0.2007 0.0174 0.1474 0.0076  -0.0040 0.0388  227 THR B N   
3958 C  CA  . THR B 227 ? 0.1606 0.0464 0.1395 0.0259  0.0000  0.0476  227 THR B CA  
3959 C  C   . THR B 227 ? 0.1728 0.0116 0.1672 0.0175  -0.0127 0.0219  227 THR B C   
3960 O  O   . THR B 227 ? 0.2791 0.0706 0.1837 0.0207  -0.0305 0.0573  227 THR B O   
3961 C  CB  . THR B 227 ? 0.1660 0.0977 0.1478 -0.0184 -0.0160 0.0230  227 THR B CB  
3962 O  OG1 . THR B 227 ? 0.1772 0.0450 0.1890 -0.0034 0.0081  0.0200  227 THR B OG1 
3963 C  CG2 . THR B 227 ? 0.1740 0.1002 0.1758 0.0036  -0.0015 0.0540  227 THR B CG2 
3964 N  N   . ALA B 228 ? 0.1332 0.0092 0.2191 -0.0041 -0.0020 0.0241  228 ALA B N   
3965 C  CA  . ALA B 228 ? 0.1703 0.0127 0.2483 0.0318  -0.0130 -0.0013 228 ALA B CA  
3966 C  C   . ALA B 228 ? 0.2399 0.0156 0.1387 0.0122  -0.0627 0.0078  228 ALA B C   
3967 O  O   . ALA B 228 ? 0.2615 0.0988 0.2544 0.0052  -0.1306 0.0504  228 ALA B O   
3968 C  CB  . ALA B 228 ? 0.1200 0.1021 0.2935 -0.0071 -0.0326 0.0149  228 ALA B CB  
3969 N  N   . LEU B 229 ? 0.2121 0.0411 0.1575 -0.0153 -0.0209 0.0021  229 LEU B N   
3970 C  CA  . LEU B 229 ? 0.1747 0.0282 0.1302 -0.0049 -0.0313 0.0195  229 LEU B CA  
3971 C  C   . LEU B 229 ? 0.1843 0.0300 0.1539 0.0035  -0.0199 0.0422  229 LEU B C   
3972 O  O   . LEU B 229 ? 0.1729 0.0399 0.1638 0.0026  -0.0186 0.0385  229 LEU B O   
3973 C  CB  . LEU B 229 ? 0.1658 0.0965 0.1476 -0.0175 -0.0142 0.0145  229 LEU B CB  
3974 C  CG  . LEU B 229 ? 0.1604 0.0571 0.1542 -0.0207 -0.0261 0.0514  229 LEU B CG  
3975 C  CD1 . LEU B 229 ? 0.2053 0.0965 0.1591 0.0111  0.0046  0.0381  229 LEU B CD1 
3976 C  CD2 . LEU B 229 ? 0.1834 0.1668 0.1962 0.0396  -0.0496 0.0547  229 LEU B CD2 
3977 N  N   . TYR B 230 ? 0.1593 0.0267 0.1446 0.0080  -0.0305 0.0168  230 TYR B N   
3978 C  CA  . TYR B 230 ? 0.2037 0.0740 0.1101 -0.0378 -0.0294 0.0149  230 TYR B CA  
3979 C  C   . TYR B 230 ? 0.1553 0.0406 0.1182 -0.0222 -0.0027 0.0331  230 TYR B C   
3980 O  O   . TYR B 230 ? 0.1686 0.0406 0.1979 -0.0359 -0.0015 0.0000  230 TYR B O   
3981 C  CB  . TYR B 230 ? 0.2205 0.1011 0.1185 0.0408  -0.0091 0.0295  230 TYR B CB  
3982 C  CG  . TYR B 230 ? 0.1821 0.0498 0.1144 -0.0190 -0.0292 0.0079  230 TYR B CG  
3983 C  CD1 . TYR B 230 ? 0.2224 0.0354 0.1589 -0.0183 -0.0439 0.0001  230 TYR B CD1 
3984 C  CD2 . TYR B 230 ? 0.1859 0.0923 0.1458 0.0221  -0.0032 0.0125  230 TYR B CD2 
3985 C  CE1 . TYR B 230 ? 0.3201 0.0169 0.2030 0.0214  0.0000  0.0423  230 TYR B CE1 
3986 C  CE2 . TYR B 230 ? 0.2549 0.1003 0.1275 0.0515  -0.0185 0.0156  230 TYR B CE2 
3987 C  CZ  . TYR B 230 ? 0.2770 0.0854 0.1852 0.0638  -0.0335 0.0044  230 TYR B CZ  
3988 O  OH  . TYR B 230 ? 0.4214 0.1075 0.1895 0.0882  0.0156  0.0087  230 TYR B OH  
3989 N  N   . CYS B 231 ? 0.1536 0.0599 0.1703 -0.0320 0.0011  0.0066  231 CYS B N   
3990 C  CA  . CYS B 231 ? 0.1474 0.0278 0.2148 -0.0066 0.0190  0.0088  231 CYS B CA  
3991 C  C   . CYS B 231 ? 0.1722 0.0402 0.1412 -0.0572 0.0267  0.0337  231 CYS B C   
3992 O  O   . CYS B 231 ? 0.2059 0.1024 0.1848 0.0082  0.0087  -0.0046 231 CYS B O   
3993 C  CB  . CYS B 231 ? 0.1837 0.0303 0.2256 -0.0532 0.0084  0.0245  231 CYS B CB  
3994 S  SG  . CYS B 231 ? 0.2067 0.0687 0.2119 -0.0162 -0.0362 0.0244  231 CYS B SG  
3995 N  N   . THR B 232 ? 0.1830 0.0668 0.1439 -0.0133 -0.0012 0.0436  232 THR B N   
3996 C  CA  . THR B 232 ? 0.1696 0.0463 0.1830 -0.0074 0.0148  0.0383  232 THR B CA  
3997 C  C   . THR B 232 ? 0.1401 0.0179 0.1711 -0.0146 0.0264  -0.0010 232 THR B C   
3998 O  O   . THR B 232 ? 0.1600 0.0472 0.1913 -0.0321 0.0069  0.0076  232 THR B O   
3999 C  CB  . THR B 232 ? 0.1489 0.0129 0.1780 -0.0206 -0.0089 -0.0044 232 THR B CB  
4000 O  OG1 . THR B 232 ? 0.1855 0.0124 0.1661 0.0093  0.0232  0.0081  232 THR B OG1 
4001 C  CG2 . THR B 232 ? 0.1602 0.0565 0.1972 -0.0230 -0.0170 -0.0238 232 THR B CG2 
4002 N  N   . HIS B 233 ? 0.2167 0.0454 0.1719 0.0242  0.0302  0.0325  233 HIS B N   
4003 C  CA  . HIS B 233 ? 0.2200 0.0206 0.2127 -0.0255 0.0129  -0.0044 233 HIS B CA  
4004 C  C   . HIS B 233 ? 0.1959 0.0095 0.2107 0.0206  0.0148  0.0152  233 HIS B C   
4005 O  O   . HIS B 233 ? 0.1826 0.0411 0.2028 0.0326  0.0041  0.0385  233 HIS B O   
4006 C  CB  . HIS B 233 ? 0.2691 0.0134 0.2686 -0.0377 0.0474  -0.0274 233 HIS B CB  
4007 C  CG  . HIS B 233 ? 0.2657 0.0399 0.2811 0.0334  0.0212  -0.0279 233 HIS B CG  
4008 N  ND1 . HIS B 233 ? 0.3395 0.0508 0.4691 -0.0051 0.0230  -0.0695 233 HIS B ND1 
4009 C  CD2 . HIS B 233 ? 0.3080 0.0661 0.3027 -0.0159 0.0653  -0.0078 233 HIS B CD2 
4010 C  CE1 . HIS B 233 ? 0.4306 0.1822 0.3753 0.0769  -0.0032 -0.0545 233 HIS B CE1 
4011 N  NE2 . HIS B 233 ? 0.4355 0.1313 0.3332 0.1083  0.0279  -0.0659 233 HIS B NE2 
4012 N  N   . MET B 234 ? 0.1919 0.0191 0.1776 0.0083  0.0285  0.0305  234 MET B N   
4013 C  CA  . MET B 234 ? 0.1844 0.0783 0.1755 0.0176  0.0085  0.0290  234 MET B CA  
4014 C  C   . MET B 234 ? 0.2126 0.0309 0.1804 0.0264  0.0312  0.0157  234 MET B C   
4015 O  O   . MET B 234 ? 0.1936 0.0397 0.1894 -0.0043 0.0157  -0.0128 234 MET B O   
4016 C  CB  . MET B 234 ? 0.2037 0.0183 0.2256 -0.0030 -0.0458 0.0115  234 MET B CB  
4017 C  CG  . MET B 234 ? 0.2347 0.1258 0.1984 0.0760  -0.0370 -0.0041 234 MET B CG  
4018 S  SD  . MET B 234 ? 0.2399 0.2340 0.2784 0.0122  -0.0423 -0.0548 234 MET B SD  
4019 C  CE  . MET B 234 ? 0.3023 0.1808 0.2847 0.0343  0.0920  -0.0359 234 MET B CE  
4020 N  N   . ASP B 235 ? 0.2232 0.0276 0.2254 0.0121  0.0064  0.0312  235 ASP B N   
4021 C  CA  . ASP B 235 ? 0.2347 0.0337 0.2861 0.0054  0.0121  0.0637  235 ASP B CA  
4022 C  C   . ASP B 235 ? 0.2159 0.0714 0.2339 0.0222  0.0083  0.0759  235 ASP B C   
4023 O  O   . ASP B 235 ? 0.2689 0.0977 0.2540 -0.0300 0.0042  0.0824  235 ASP B O   
4024 C  CB  . ASP B 235 ? 0.2834 0.0719 0.3477 0.0714  0.0685  0.0784  235 ASP B CB  
4025 C  CG  . ASP B 235 ? 0.3193 0.0414 0.4923 0.1040  0.0794  0.0106  235 ASP B CG  
4026 O  OD1 . ASP B 235 ? 0.4371 0.1409 0.4953 0.0490  0.0184  -0.0177 235 ASP B OD1 
4027 O  OD2 . ASP B 235 ? 0.5492 0.0748 0.7738 0.1574  0.1980  0.1834  235 ASP B OD2 
4028 N  N   . ASP B 236 ? 0.1836 0.0927 0.2202 0.0139  -0.0063 0.0573  236 ASP B N   
4029 C  CA  . ASP B 236 ? 0.1963 0.0663 0.1713 -0.0176 -0.0080 0.0300  236 ASP B CA  
4030 C  C   . ASP B 236 ? 0.2307 0.0464 0.1627 -0.0034 -0.0011 0.0236  236 ASP B C   
4031 O  O   . ASP B 236 ? 0.2071 0.0329 0.2103 -0.0189 -0.0023 0.0410  236 ASP B O   
4032 C  CB  . ASP B 236 ? 0.2195 0.0463 0.1830 -0.0199 -0.0299 0.0353  236 ASP B CB  
4033 C  CG  . ASP B 236 ? 0.2242 0.0437 0.1927 -0.0387 -0.0025 -0.0027 236 ASP B CG  
4034 O  OD1 . ASP B 236 ? 0.2193 0.0782 0.2171 -0.0417 0.0300  -0.0479 236 ASP B OD1 
4035 O  OD2 . ASP B 236 ? 0.2532 0.1507 0.2074 -0.0346 0.0067  -0.0380 236 ASP B OD2 
4036 N  N   . PRO B 237 ? 0.2099 0.0110 0.1767 0.0251  0.0033  -0.0027 237 PRO B N   
4037 C  CA  . PRO B 237 ? 0.2178 0.0167 0.2115 -0.0041 0.0436  0.0242  237 PRO B CA  
4038 C  C   . PRO B 237 ? 0.2026 0.0471 0.1771 -0.0066 0.0116  -0.0166 237 PRO B C   
4039 O  O   . PRO B 237 ? 0.2223 0.0741 0.1609 0.0139  0.0234  0.0100  237 PRO B O   
4040 C  CB  . PRO B 237 ? 0.2383 0.0252 0.1854 -0.0288 0.0531  0.0038  237 PRO B CB  
4041 C  CG  . PRO B 237 ? 0.2480 0.0174 0.2372 -0.0072 0.0620  -0.0209 237 PRO B CG  
4042 C  CD  . PRO B 237 ? 0.2017 0.0232 0.1873 0.0048  0.0258  -0.0325 237 PRO B CD  
4043 N  N   A SER B 238 ? 0.2156 0.0087 0.1882 -0.0119 0.0035  0.0175  238 SER B N   
4044 N  N   B SER B 238 ? 0.2151 0.0068 0.1869 -0.0029 0.0056  0.0090  238 SER B N   
4045 C  CA  A SER B 238 ? 0.1898 0.0294 0.1823 -0.0276 -0.0158 0.0302  238 SER B CA  
4046 C  CA  B SER B 238 ? 0.1858 0.0347 0.1884 -0.0039 -0.0127 0.0153  238 SER B CA  
4047 C  C   A SER B 238 ? 0.2006 0.0194 0.1762 -0.0210 0.0186  0.0011  238 SER B C   
4048 C  C   B SER B 238 ? 0.1974 0.0341 0.1706 -0.0070 0.0139  -0.0163 238 SER B C   
4049 O  O   A SER B 238 ? 0.2491 0.0119 0.1800 -0.0108 0.0235  0.0285  238 SER B O   
4050 O  O   B SER B 238 ? 0.2121 0.0348 0.1715 0.0160  -0.0023 -0.0187 238 SER B O   
4051 C  CB  A SER B 238 ? 0.1747 0.1011 0.2049 -0.0716 -0.0107 0.0247  238 SER B CB  
4052 C  CB  B SER B 238 ? 0.2227 0.1144 0.2166 -0.0106 -0.0227 -0.0337 238 SER B CB  
4053 O  OG  A SER B 238 ? 0.2034 0.1286 0.2224 -0.0696 -0.0170 0.0803  238 SER B OG  
4054 O  OG  B SER B 238 ? 0.2216 0.2458 0.3436 0.0646  -0.0337 -0.0352 238 SER B OG  
4055 N  N   . PRO B 239 ? 0.1994 0.0188 0.1452 -0.0197 -0.0030 0.0214  239 PRO B N   
4056 C  CA  . PRO B 239 ? 0.2191 0.0557 0.1004 -0.0083 0.0252  0.0282  239 PRO B CA  
4057 C  C   . PRO B 239 ? 0.1665 0.0374 0.1399 -0.0168 0.0223  0.0326  239 PRO B C   
4058 O  O   . PRO B 239 ? 0.1733 0.0559 0.2001 0.0199  0.0125  0.0323  239 PRO B O   
4059 C  CB  . PRO B 239 ? 0.2256 0.0877 0.1460 -0.0656 -0.0190 0.0353  239 PRO B CB  
4060 C  CG  . PRO B 239 ? 0.3084 0.0868 0.2026 -0.0978 0.0422  -0.0187 239 PRO B CG  
4061 C  CD  . PRO B 239 ? 0.2001 0.0275 0.1532 -0.0115 0.0111  -0.0147 239 PRO B CD  
4062 N  N   . ARG B 240 ? 0.1834 0.0402 0.1211 0.0037  0.0138  0.0396  240 ARG B N   
4063 C  CA  . ARG B 240 ? 0.1776 0.1130 0.1057 -0.0188 -0.0068 0.0648  240 ARG B CA  
4064 C  C   . ARG B 240 ? 0.1602 0.0403 0.1225 0.0208  0.0087  0.0458  240 ARG B C   
4065 O  O   . ARG B 240 ? 0.1733 0.0600 0.1678 0.0020  0.0325  0.0316  240 ARG B O   
4066 C  CB  . ARG B 240 ? 0.1905 0.0681 0.1747 -0.0140 -0.0223 0.0311  240 ARG B CB  
4067 C  CG  . ARG B 240 ? 0.2514 0.0410 0.1976 -0.0414 -0.0021 0.0160  240 ARG B CG  
4068 C  CD  . ARG B 240 ? 0.1342 0.1552 0.2191 -0.0097 -0.0271 -0.0294 240 ARG B CD  
4069 N  NE  . ARG B 240 ? 0.1552 0.1629 0.2259 0.0079  0.0105  0.0057  240 ARG B NE  
4070 C  CZ  . ARG B 240 ? 0.1743 0.1049 0.2494 0.0081  0.0345  0.0561  240 ARG B CZ  
4071 N  NH1 . ARG B 240 ? 0.2446 0.0701 0.1888 0.0065  -0.0210 0.0128  240 ARG B NH1 
4072 N  NH2 . ARG B 240 ? 0.2370 0.1843 0.2365 0.0743  -0.0060 -0.0162 240 ARG B NH2 
4073 N  N   . GLU B 241 ? 0.1732 0.0331 0.1388 0.0125  -0.0013 0.0529  241 GLU B N   
4074 C  CA  . GLU B 241 ? 0.1640 0.0564 0.1487 -0.0029 0.0126  0.0418  241 GLU B CA  
4075 C  C   . GLU B 241 ? 0.1553 0.0375 0.1456 -0.0279 -0.0060 0.0356  241 GLU B C   
4076 O  O   . GLU B 241 ? 0.1682 0.0569 0.1557 -0.0326 -0.0085 0.0357  241 GLU B O   
4077 C  CB  . GLU B 241 ? 0.2271 0.0589 0.1804 0.0064  0.0247  0.0223  241 GLU B CB  
4078 C  CG  . GLU B 241 ? 0.2382 0.1065 0.1688 0.0386  -0.0039 0.0245  241 GLU B CG  
4079 C  CD  . GLU B 241 ? 0.2343 0.1036 0.2998 0.0151  -0.0033 -0.0283 241 GLU B CD  
4080 O  OE1 . GLU B 241 ? 0.3046 0.3996 0.3222 0.2196  -0.0555 -0.0810 241 GLU B OE1 
4081 O  OE2 . GLU B 241 ? 0.3630 0.2509 0.3891 0.1582  -0.1001 -0.1351 241 GLU B OE2 
4082 N  N   . MET B 242 ? 0.1555 0.0444 0.1406 -0.0185 0.0222  0.0153  242 MET B N   
4083 C  CA  . MET B 242 ? 0.1424 0.0706 0.1399 0.0260  0.0133  0.0208  242 MET B CA  
4084 C  C   . MET B 242 ? 0.1338 0.0663 0.1108 -0.0126 -0.0443 0.0316  242 MET B C   
4085 O  O   . MET B 242 ? 0.1302 0.1017 0.1555 -0.0239 -0.0247 0.0295  242 MET B O   
4086 C  CB  . MET B 242 ? 0.1345 0.0749 0.1394 -0.0016 0.0003  0.0243  242 MET B CB  
4087 C  CG  . MET B 242 ? 0.1712 0.0553 0.1462 0.0442  0.0219  0.0162  242 MET B CG  
4088 S  SD  . MET B 242 ? 0.1624 0.0496 0.1805 0.0010  -0.0116 0.0300  242 MET B SD  
4089 C  CE  . MET B 242 ? 0.1123 0.0388 0.1844 -0.0204 0.0234  -0.0291 242 MET B CE  
4090 N  N   . ILE B 243 ? 0.1323 0.0636 0.1101 0.0330  -0.0201 0.0418  243 ILE B N   
4091 C  CA  . ILE B 243 ? 0.1240 0.0671 0.1495 0.0331  -0.0187 0.0505  243 ILE B CA  
4092 C  C   . ILE B 243 ? 0.1111 0.0645 0.1528 0.0015  -0.0161 0.0389  243 ILE B C   
4093 O  O   . ILE B 243 ? 0.1160 0.0733 0.1320 -0.0116 0.0061  0.0223  243 ILE B O   
4094 C  CB  . ILE B 243 ? 0.1543 0.0717 0.1377 -0.0205 0.0016  0.0152  243 ILE B CB  
4095 C  CG1 . ILE B 243 ? 0.1742 0.0751 0.1514 -0.0194 0.0299  0.0300  243 ILE B CG1 
4096 C  CG2 . ILE B 243 ? 0.1821 0.1298 0.1351 0.0072  -0.0263 0.0359  243 ILE B CG2 
4097 C  CD1 . ILE B 243 ? 0.2296 0.1155 0.1624 0.0052  0.0506  0.0118  243 ILE B CD1 
4098 N  N   . ASN B 244 ? 0.1331 0.0548 0.1238 0.0255  -0.0023 0.0200  244 ASN B N   
4099 C  CA  . ASN B 244 ? 0.1028 0.0597 0.1311 0.0414  0.0165  0.0113  244 ASN B CA  
4100 C  C   . ASN B 244 ? 0.0955 0.0243 0.1216 0.0327  -0.0065 0.0235  244 ASN B C   
4101 O  O   . ASN B 244 ? 0.1153 0.0405 0.1877 -0.0011 -0.0048 -0.0036 244 ASN B O   
4102 C  CB  . ASN B 244 ? 0.1067 0.0606 0.1773 0.0449  0.0352  0.0353  244 ASN B CB  
4103 C  CG  . ASN B 244 ? 0.0763 0.0645 0.1731 0.0076  0.0238  0.0144  244 ASN B CG  
4104 O  OD1 . ASN B 244 ? 0.1324 0.0747 0.2437 -0.0006 0.0292  0.0330  244 ASN B OD1 
4105 N  ND2 . ASN B 244 ? 0.1589 0.1624 0.2225 0.0223  0.0740  0.0523  244 ASN B ND2 
4106 N  N   . ASN B 245 ? 0.0999 0.0369 0.1372 0.0261  0.0105  0.0334  245 ASN B N   
4107 C  CA  . ASN B 245 ? 0.1078 0.0388 0.1202 0.0170  -0.0205 0.0140  245 ASN B CA  
4108 C  C   . ASN B 245 ? 0.1223 0.0076 0.1341 0.0039  -0.0008 0.0122  245 ASN B C   
4109 O  O   . ASN B 245 ? 0.1428 0.0566 0.1179 0.0082  0.0111  0.0280  245 ASN B O   
4110 C  CB  . ASN B 245 ? 0.1031 0.0663 0.1215 0.0141  -0.0187 0.0348  245 ASN B CB  
4111 C  CG  . ASN B 245 ? 0.1017 0.0208 0.1236 0.0347  -0.0152 0.0094  245 ASN B CG  
4112 O  OD1 . ASN B 245 ? 0.1317 0.0114 0.2129 0.0229  -0.0091 0.0117  245 ASN B OD1 
4113 N  ND2 . ASN B 245 ? 0.1011 0.0196 0.2049 0.0200  -0.0153 0.0009  245 ASN B ND2 
4114 N  N   . PHE B 246 ? 0.1280 0.0190 0.1137 -0.0074 -0.0259 0.0133  246 PHE B N   
4115 C  CA  . PHE B 246 ? 0.1011 0.0105 0.1233 -0.0047 -0.0104 0.0218  246 PHE B CA  
4116 C  C   . PHE B 246 ? 0.1078 0.0107 0.1593 -0.0002 -0.0136 0.0075  246 PHE B C   
4117 O  O   . PHE B 246 ? 0.1220 0.0072 0.1641 0.0019  0.0000  0.0116  246 PHE B O   
4118 C  CB  . PHE B 246 ? 0.1203 0.0067 0.1496 0.0008  -0.0009 0.0024  246 PHE B CB  
4119 C  CG  . PHE B 246 ? 0.1316 0.0363 0.1528 0.0140  0.0000  0.0158  246 PHE B CG  
4120 C  CD1 . PHE B 246 ? 0.1346 0.0076 0.1622 -0.0050 0.0105  0.0126  246 PHE B CD1 
4121 C  CD2 . PHE B 246 ? 0.1462 0.0171 0.1724 -0.0069 -0.0130 0.0421  246 PHE B CD2 
4122 C  CE1 . PHE B 246 ? 0.1238 0.0462 0.1478 0.0015  0.0012  0.0128  246 PHE B CE1 
4123 C  CE2 . PHE B 246 ? 0.1601 0.0064 0.1588 -0.0027 -0.0368 -0.0013 246 PHE B CE2 
4124 C  CZ  . PHE B 246 ? 0.1556 0.0328 0.1442 0.0228  -0.0115 0.0212  246 PHE B CZ  
4125 N  N   . ARG B 247 ? 0.1410 0.0075 0.1494 0.0000  -0.0201 0.0131  247 ARG B N   
4126 C  CA  . ARG B 247 ? 0.1164 0.0283 0.1599 0.0281  -0.0201 -0.0041 247 ARG B CA  
4127 C  C   . ARG B 247 ? 0.0997 0.0275 0.1100 -0.0269 -0.0197 0.0414  247 ARG B C   
4128 O  O   . ARG B 247 ? 0.1245 0.0153 0.1498 -0.0227 0.0080  0.0241  247 ARG B O   
4129 C  CB  . ARG B 247 ? 0.1384 0.0078 0.1527 -0.0110 -0.0011 -0.0092 247 ARG B CB  
4130 C  CG  . ARG B 247 ? 0.1474 0.0092 0.1690 -0.0171 -0.0034 -0.0111 247 ARG B CG  
4131 C  CD  . ARG B 247 ? 0.1297 0.0079 0.1605 -0.0140 -0.0115 0.0032  247 ARG B CD  
4132 N  NE  . ARG B 247 ? 0.1604 0.0070 0.1591 -0.0102 -0.0205 0.0023  247 ARG B NE  
4133 C  CZ  . ARG B 247 ? 0.1271 0.0074 0.1758 -0.0116 -0.0162 0.0018  247 ARG B CZ  
4134 N  NH1 . ARG B 247 ? 0.1399 0.0241 0.1731 0.0110  -0.0012 0.0178  247 ARG B NH1 
4135 N  NH2 . ARG B 247 ? 0.1519 0.0081 0.1814 -0.0162 -0.0130 -0.0003 247 ARG B NH2 
4136 N  N   . GLN B 248 ? 0.1058 0.0217 0.1439 0.0117  -0.0074 0.0227  248 GLN B N   
4137 C  CA  . GLN B 248 ? 0.1271 0.0106 0.1154 0.0014  0.0013  0.0216  248 GLN B CA  
4138 C  C   . GLN B 248 ? 0.1241 0.0141 0.1370 -0.0021 0.0368  0.0296  248 GLN B C   
4139 O  O   . GLN B 248 ? 0.1731 0.0072 0.1435 0.0091  -0.0194 -0.0080 248 GLN B O   
4140 C  CB  . GLN B 248 ? 0.1179 0.0190 0.1746 0.0116  0.0082  0.0265  248 GLN B CB  
4141 C  CG  . GLN B 248 ? 0.1137 0.0082 0.1733 -0.0122 0.0034  0.0083  248 GLN B CG  
4142 C  CD  . GLN B 248 ? 0.1672 0.0205 0.1729 -0.0110 0.0012  -0.0122 248 GLN B CD  
4143 O  OE1 . GLN B 248 ? 0.1524 0.0232 0.1571 -0.0085 -0.0040 0.0233  248 GLN B OE1 
4144 N  NE2 . GLN B 248 ? 0.1520 0.0765 0.1852 -0.0089 -0.0044 0.0348  248 GLN B NE2 
4145 N  N   . VAL B 249 ? 0.1464 0.0111 0.1234 -0.0114 -0.0073 0.0217  249 VAL B N   
4146 C  CA  . VAL B 249 ? 0.1318 0.0109 0.1352 0.0040  0.0189  0.0243  249 VAL B CA  
4147 C  C   . VAL B 249 ? 0.1204 0.0523 0.1456 0.0140  0.0021  0.0103  249 VAL B C   
4148 O  O   . VAL B 249 ? 0.1130 0.0189 0.1518 0.0152  -0.0190 0.0134  249 VAL B O   
4149 C  CB  . VAL B 249 ? 0.1459 0.0173 0.1777 -0.0262 -0.0324 0.0374  249 VAL B CB  
4150 C  CG1 . VAL B 249 ? 0.1372 0.0290 0.1588 0.0071  -0.0344 0.0065  249 VAL B CG1 
4151 C  CG2 . VAL B 249 ? 0.1766 0.0125 0.2139 -0.0118 -0.0304 0.0350  249 VAL B CG2 
4152 N  N   . GLN B 250 ? 0.1424 0.0076 0.1287 -0.0131 -0.0220 0.0039  250 GLN B N   
4153 C  CA  . GLN B 250 ? 0.1419 0.0129 0.1341 -0.0063 -0.0194 -0.0093 250 GLN B CA  
4154 C  C   . GLN B 250 ? 0.1251 0.0426 0.1460 -0.0054 -0.0092 0.0410  250 GLN B C   
4155 O  O   . GLN B 250 ? 0.1667 0.0332 0.1850 -0.0189 -0.0203 0.0315  250 GLN B O   
4156 C  CB  . GLN B 250 ? 0.1536 0.0119 0.1751 0.0043  -0.0228 -0.0026 250 GLN B CB  
4157 C  CG  . GLN B 250 ? 0.1638 0.0164 0.1487 -0.0400 -0.0290 0.0069  250 GLN B CG  
4158 C  CD  . GLN B 250 ? 0.1472 0.0144 0.1182 -0.0104 -0.0519 0.0299  250 GLN B CD  
4159 O  OE1 . GLN B 250 ? 0.1864 0.0296 0.1701 -0.0054 -0.0313 -0.0262 250 GLN B OE1 
4160 N  NE2 . GLN B 250 ? 0.1521 0.0283 0.1448 -0.0091 -0.0257 0.0146  250 GLN B NE2 
4161 N  N   . LYS B 251 ? 0.1559 0.0753 0.1283 0.0121  -0.0061 0.0069  251 LYS B N   
4162 C  CA  . LYS B 251 ? 0.1634 0.0992 0.1133 -0.0225 -0.0044 -0.0104 251 LYS B CA  
4163 C  C   . LYS B 251 ? 0.1530 0.1090 0.1348 0.0120  0.0111  0.0414  251 LYS B C   
4164 O  O   . LYS B 251 ? 0.1541 0.0787 0.1732 0.0088  0.0104  0.0252  251 LYS B O   
4165 C  CB  . LYS B 251 ? 0.1476 0.1015 0.1674 -0.0251 0.0167  -0.0384 251 LYS B CB  
4166 C  CG  . LYS B 251 ? 0.1708 0.1126 0.1712 0.0435  0.0287  0.0249  251 LYS B CG  
4167 C  CD  . LYS B 251 ? 0.1564 0.1291 0.1879 0.0411  -0.0050 0.0275  251 LYS B CD  
4168 C  CE  . LYS B 251 ? 0.1482 0.1148 0.1363 0.0170  -0.0190 -0.0010 251 LYS B CE  
4169 N  NZ  . LYS B 251 ? 0.1713 0.0069 0.1408 -0.0096 -0.0312 0.0024  251 LYS B NZ  
4170 N  N   . PHE B 252 ? 0.2392 0.0706 0.1466 -0.0181 0.0219  0.0261  252 PHE B N   
4171 C  CA  . PHE B 252 ? 0.1998 0.0731 0.1690 -0.0052 0.0052  0.0328  252 PHE B CA  
4172 C  C   . PHE B 252 ? 0.6918 0.1370 0.3209 -0.1965 -0.0073 -0.1509 252 PHE B C   
4173 O  O   . PHE B 252 ? 0.4629 0.2378 0.5062 0.0402  -0.1454 0.1676  252 PHE B O   
4174 C  CB  . PHE B 252 ? 0.3092 0.0959 0.3632 -0.0463 0.1243  -0.0254 252 PHE B CB  
4175 C  CG  . PHE B 252 ? 0.2734 0.2245 0.2832 -0.0171 0.0549  0.0105  252 PHE B CG  
4176 C  CD1 . PHE B 252 ? 0.3300 0.1653 0.2730 -0.0217 -0.0059 -0.0763 252 PHE B CD1 
4177 C  CD2 . PHE B 252 ? 0.3066 0.1361 0.2884 -0.0946 0.0052  -0.0563 252 PHE B CD2 
4178 C  CE1 . PHE B 252 ? 0.3356 0.1902 0.2311 -0.0057 -0.0498 0.0919  252 PHE B CE1 
4179 C  CE2 . PHE B 252 ? 0.2737 0.1452 0.2727 0.0001  -0.0048 0.0430  252 PHE B CE2 
4180 C  CZ  . PHE B 252 ? 0.4302 0.1139 0.3800 -0.0282 -0.1085 0.1301  252 PHE B CZ  
4181 N  N   . ASP B 253 ? 0.4688 0.2770 0.3737 -0.2743 0.1142  -0.1256 253 ASP B N   
4182 C  CA  . ASP B 253 ? 0.5047 0.2512 0.4649 -0.1368 0.1336  -0.1523 253 ASP B CA  
4183 C  C   . ASP B 253 ? 0.7623 0.4665 0.2337 -0.1044 -0.0093 -0.0939 253 ASP B C   
4184 O  O   . ASP B 253 ? 0.8545 0.1722 0.3048 -0.0932 -0.0712 -0.0251 253 ASP B O   
4185 C  CB  . ASP B 253 ? 0.7858 0.2604 0.2987 -0.1982 -0.0405 -0.0872 253 ASP B CB  
4186 C  CG  . ASP B 253 ? 0.8487 0.4489 0.5996 -0.2240 0.1976  -0.0467 253 ASP B CG  
4187 O  OD1 . ASP B 253 ? 1.0714 0.4710 0.2264 -0.1953 0.0836  0.0257  253 ASP B OD1 
4188 O  OD2 . ASP B 253 ? 0.9434 0.3631 0.5215 -0.2004 -0.3032 -0.0317 253 ASP B OD2 
4189 N  N   . GLU B 254 ? 0.2904 0.3948 0.4470 -0.2232 0.0634  -0.1632 254 GLU B N   
4190 C  CA  . GLU B 254 ? 0.5176 0.3012 0.4979 -0.2561 -0.0304 -0.0749 254 GLU B CA  
4191 C  C   . GLU B 254 ? 0.4006 0.4385 0.3850 -0.0882 0.0623  -0.0054 254 GLU B C   
4192 O  O   . GLU B 254 ? 0.3832 0.2712 0.3994 -0.0864 0.0279  0.0283  254 GLU B O   
4193 C  CB  . GLU B 254 ? 0.5939 0.3270 0.5082 0.0578  0.0324  -0.1872 254 GLU B CB  
4194 C  CG  . GLU B 254 ? 0.6006 0.5896 0.7690 -0.1273 -0.0601 -0.0817 254 GLU B CG  
4195 C  CD  . GLU B 254 ? 0.7869 0.5975 0.8263 -0.1423 -0.1244 -0.0536 254 GLU B CD  
4196 O  OE1 . GLU B 254 ? 0.4903 0.7695 0.6943 0.0734  -0.1101 0.0588  254 GLU B OE1 
4197 O  OE2 . GLU B 254 ? 1.0582 0.6576 1.0260 -0.0602 -0.2889 -0.2241 254 GLU B OE2 
4198 N  N   . ARG B 255 ? 0.3393 0.1581 0.3531 -0.0660 0.0754  0.0193  255 ARG B N   
4199 C  CA  . ARG B 255 ? 0.3140 0.0880 0.2020 -0.0218 -0.0564 -0.0454 255 ARG B CA  
4200 C  C   . ARG B 255 ? 0.3271 0.0911 0.3058 -0.0091 -0.0074 -0.0708 255 ARG B C   
4201 O  O   . ARG B 255 ? 0.3125 0.1230 0.3244 -0.0285 -0.0164 -0.0428 255 ARG B O   
4202 C  CB  . ARG B 255 ? 0.3992 0.1435 0.2419 0.1160  -0.0146 -0.0210 255 ARG B CB  
4203 C  CG  . ARG B 255 ? 0.4789 0.1724 0.2476 0.1672  0.0461  0.0908  255 ARG B CG  
4204 C  CD  . ARG B 255 ? 0.3547 0.2574 0.3125 0.1342  -0.0386 0.0442  255 ARG B CD  
4205 N  NE  . ARG B 255 ? 0.4576 0.5468 0.3573 0.0365  -0.0025 0.1441  255 ARG B NE  
4206 C  CZ  . ARG B 255 ? 0.2542 0.4075 0.3880 0.0798  -0.0877 0.0665  255 ARG B CZ  
4207 N  NH1 . ARG B 255 ? 0.2277 0.0333 0.3379 -0.0582 -0.0589 0.0762  255 ARG B NH1 
4208 N  NH2 . ARG B 255 ? 0.3592 0.3095 0.2462 0.1675  -0.0952 0.0670  255 ARG B NH2 
4209 N  N   . LEU B 256 ? 0.2878 0.1980 0.2308 -0.0522 -0.0621 -0.0526 256 LEU B N   
4210 C  CA  . LEU B 256 ? 0.2451 0.1859 0.2232 -0.0286 -0.0380 -0.0365 256 LEU B CA  
4211 C  C   . LEU B 256 ? 0.2261 0.1058 0.2097 -0.0449 -0.0331 -0.0283 256 LEU B C   
4212 O  O   . LEU B 256 ? 0.3074 0.0313 0.2740 -0.0384 -0.0366 -0.0002 256 LEU B O   
4213 C  CB  . LEU B 256 ? 0.3578 0.2423 0.2624 -0.0029 -0.0604 0.0272  256 LEU B CB  
4214 C  CG  . LEU B 256 ? 0.3412 0.1514 0.2667 0.0706  -0.0456 0.0230  256 LEU B CG  
4215 C  CD1 . LEU B 256 ? 0.3535 0.2575 0.2889 -0.0378 -0.0462 0.0380  256 LEU B CD1 
4216 C  CD2 . LEU B 256 ? 0.3448 0.3617 0.2877 0.1030  0.0142  0.0275  256 LEU B CD2 
4217 N  N   . VAL B 257 ? 0.2552 0.0453 0.1574 0.0018  -0.0726 0.0250  257 VAL B N   
4218 C  CA  . VAL B 257 ? 0.1854 0.0649 0.1728 -0.0055 -0.0284 0.0573  257 VAL B CA  
4219 C  C   . VAL B 257 ? 0.1679 0.0508 0.1807 0.0268  -0.0148 0.0644  257 VAL B C   
4220 O  O   . VAL B 257 ? 0.1956 0.0571 0.2480 0.0366  -0.0068 0.0864  257 VAL B O   
4221 C  CB  . VAL B 257 ? 0.1986 0.0182 0.1922 -0.0290 -0.0323 0.0337  257 VAL B CB  
4222 C  CG1 . VAL B 257 ? 0.1930 0.0750 0.1873 -0.0318 -0.0345 0.0280  257 VAL B CG1 
4223 C  CG2 . VAL B 257 ? 0.2218 0.0524 0.2119 -0.0294 0.0076  0.0419  257 VAL B CG2 
4224 N  N   . TYR B 258 ? 0.1535 0.0349 0.1846 0.0015  -0.0128 0.0549  258 TYR B N   
4225 C  CA  . TYR B 258 ? 0.1838 0.0104 0.1486 -0.0017 -0.0013 0.0241  258 TYR B CA  
4226 C  C   . TYR B 258 ? 0.1593 0.0331 0.1324 0.0100  -0.0140 0.0245  258 TYR B C   
4227 O  O   . TYR B 258 ? 0.2444 0.0556 0.1518 0.0013  -0.0311 0.0375  258 TYR B O   
4228 C  CB  . TYR B 258 ? 0.1593 0.0753 0.1737 -0.0012 -0.0005 -0.0132 258 TYR B CB  
4229 C  CG  . TYR B 258 ? 0.2593 0.0792 0.1742 -0.0197 -0.0233 -0.0160 258 TYR B CG  
4230 C  CD1 . TYR B 258 ? 0.2878 0.1399 0.1514 -0.0334 -0.0234 -0.0196 258 TYR B CD1 
4231 C  CD2 . TYR B 258 ? 0.2331 0.0569 0.1972 0.0398  -0.0122 -0.0108 258 TYR B CD2 
4232 C  CE1 . TYR B 258 ? 0.3701 0.1236 0.1846 -0.0574 -0.0628 -0.0013 258 TYR B CE1 
4233 C  CE2 . TYR B 258 ? 0.2563 0.1117 0.1954 -0.0053 -0.0295 0.0188  258 TYR B CE2 
4234 C  CZ  . TYR B 258 ? 0.2859 0.1248 0.1938 -0.0346 -0.0572 0.0199  258 TYR B CZ  
4235 O  OH  . TYR B 258 ? 0.3296 0.1992 0.2561 -0.1007 -0.0583 -0.0040 258 TYR B OH  
4236 N  N   . THR B 259 ? 0.1782 0.0313 0.1987 -0.0068 0.0089  0.0258  259 THR B N   
4237 C  CA  . THR B 259 ? 0.1390 0.0434 0.1412 0.0280  -0.0057 0.0412  259 THR B CA  
4238 C  C   . THR B 259 ? 0.1775 0.0426 0.1584 -0.0003 0.0210  0.0185  259 THR B C   
4239 O  O   . THR B 259 ? 0.1952 0.0724 0.1721 0.0182  0.0256  0.0658  259 THR B O   
4240 C  CB  . THR B 259 ? 0.1557 0.0665 0.1649 0.0441  0.0187  0.0430  259 THR B CB  
4241 O  OG1 . THR B 259 ? 0.2055 0.0823 0.2128 0.0493  -0.0027 0.0759  259 THR B OG1 
4242 C  CG2 . THR B 259 ? 0.1895 0.0719 0.1758 0.0348  0.0407  0.0411  259 THR B CG2 
4243 N  N   . SER B 260 ? 0.1557 0.0305 0.1947 -0.0054 0.0098  0.0069  260 SER B N   
4244 C  CA  . SER B 260 ? 0.1574 0.0204 0.2074 -0.0159 -0.0008 0.0500  260 SER B CA  
4245 C  C   . SER B 260 ? 0.1830 0.0172 0.2213 -0.0047 -0.0084 0.0420  260 SER B C   
4246 O  O   . SER B 260 ? 0.1999 0.0751 0.2839 -0.0015 0.0320  0.0655  260 SER B O   
4247 C  CB  . SER B 260 ? 0.1848 0.0821 0.1765 0.0185  -0.0030 0.0284  260 SER B CB  
4248 O  OG  . SER B 260 ? 0.2103 0.0390 0.1707 -0.0074 0.0162  0.0318  260 SER B OG  
4249 N  N   . PHE B 261 ? 0.1628 0.0218 0.2823 0.0007  0.0001  0.0654  261 PHE B N   
4250 C  CA  . PHE B 261 ? 0.1824 0.0192 0.2174 0.0071  0.0012  0.0516  261 PHE B CA  
4251 C  C   . PHE B 261 ? 0.1747 0.0331 0.2121 0.0023  0.0021  0.0455  261 PHE B C   
4252 O  O   . PHE B 261 ? 0.1797 0.0690 0.2293 -0.0168 -0.0069 0.0605  261 PHE B O   
4253 C  CB  . PHE B 261 ? 0.2131 0.0262 0.2209 0.0033  0.0085  0.0181  261 PHE B CB  
4254 C  CG  . PHE B 261 ? 0.2293 0.0244 0.2185 0.0073  -0.0102 0.0545  261 PHE B CG  
4255 C  CD1 . PHE B 261 ? 0.2347 0.0335 0.1615 0.0462  0.0048  0.0335  261 PHE B CD1 
4256 C  CD2 . PHE B 261 ? 0.2382 0.0548 0.2515 0.0314  -0.0348 0.0040  261 PHE B CD2 
4257 C  CE1 . PHE B 261 ? 0.2081 0.1006 0.1751 0.0185  0.0125  -0.0097 261 PHE B CE1 
4258 C  CE2 . PHE B 261 ? 0.2583 0.0477 0.2459 0.0401  -0.0226 0.0021  261 PHE B CE2 
4259 C  CZ  . PHE B 261 ? 0.1870 0.0672 0.2275 0.0009  0.0300  0.0458  261 PHE B CZ  
4260 N  N   . SER B 262 ? 0.2674 0.0167 0.2595 0.0124  -0.0223 0.0480  262 SER B N   
4261 C  CA  . SER B 262 ? 0.2403 0.0528 0.3185 0.0031  -0.0362 0.0683  262 SER B CA  
4262 C  C   . SER B 262 ? 0.3080 0.3264 0.4001 0.0716  -0.0798 -0.1776 262 SER B C   
4263 O  O   . SER B 262 ? 0.3689 0.6071 0.4207 0.2355  -0.1455 -0.1735 262 SER B O   
4264 C  CB  . SER B 262 ? 0.2943 0.2254 0.3508 -0.0599 -0.0270 0.1123  262 SER B CB  
4265 O  OG  . SER B 262 ? 0.4123 0.1179 0.5184 -0.0188 -0.0674 0.0809  262 SER B OG  
4266 N  N   . GLN B 263 ? 0.3486 0.4572 0.3341 0.2089  -0.1303 -0.1514 263 GLN B N   
4267 C  CA  . GLN B 263 ? 0.4021 0.1610 0.3651 0.1331  -0.0252 0.0752  263 GLN B CA  
4268 C  C   . GLN B 263 ? 0.4486 0.3631 0.4134 0.1261  -0.0594 -0.0120 263 GLN B C   
4269 O  O   . GLN B 263 ? 0.4692 0.1938 0.4921 0.1383  0.0454  0.0882  263 GLN B O   
4270 C  CB  . GLN B 263 ? 0.5701 0.0663 0.5950 0.1467  -0.1219 0.0789  263 GLN B CB  
4271 C  CG  . GLN B 263 ? 0.7956 0.2023 0.5457 -0.0684 0.0768  0.1331  263 GLN B CG  
4272 C  CD  . GLN B 263 ? 0.9082 0.3651 0.5733 0.0108  0.0850  0.2889  263 GLN B CD  
4273 O  OE1 . GLN B 263 ? 0.9944 0.1236 1.0556 -0.1615 0.0820  0.1423  263 GLN B OE1 
4274 N  NE2 . GLN B 263 ? 0.6631 0.1148 0.4467 -0.0255 -0.0379 0.0314  263 GLN B NE2 
4275 O  OXT . GLN B 263 ? 0.3932 0.1500 0.2577 0.0326  0.0055  0.0331  263 GLN B OXT 
4276 N  N   . LYS C 3   ? 0.7573 0.5685 0.8113 -0.1953 -0.3829 0.4381  3   LYS C N   
4277 C  CA  . LYS C 3   ? 1.9500 0.0614 1.6091 0.1170  -0.0246 0.2758  3   LYS C CA  
4278 C  C   . LYS C 3   ? 2.0790 0.3495 2.0176 -0.2285 0.0198  0.5327  3   LYS C C   
4279 O  O   . LYS C 3   ? 1.6941 0.9695 1.0578 -0.2567 -0.0147 -0.2802 3   LYS C O   
4280 C  CB  . LYS C 3   ? 1.5024 0.2761 0.6483 -0.0609 -0.2007 0.0998  3   LYS C CB  
4281 C  CG  . LYS C 3   ? 1.1612 0.3642 0.9337 -0.1310 -0.2482 0.1018  3   LYS C CG  
4282 C  CD  . LYS C 3   ? 1.0595 1.0466 1.0128 -0.2507 -0.3045 0.0665  3   LYS C CD  
4283 N  N   . TRP C 4   ? 0.2762 0.1424 0.2548 -0.0585 -0.0102 -0.0399 4   TRP C N   
4284 C  CA  . TRP C 4   ? 0.2569 0.1212 0.2660 -0.0392 -0.0196 -0.0318 4   TRP C CA  
4285 C  C   . TRP C 4   ? 0.2042 0.1282 0.2706 0.0527  0.0133  -0.0154 4   TRP C C   
4286 O  O   . TRP C 4   ? 0.2423 0.1847 0.3041 0.0343  -0.0234 -0.0407 4   TRP C O   
4287 C  CB  . TRP C 4   ? 0.2662 0.0697 0.2372 -0.0290 -0.0217 0.0095  4   TRP C CB  
4288 C  CG  . TRP C 4   ? 0.2588 0.1280 0.2150 -0.0508 -0.0329 -0.0453 4   TRP C CG  
4289 C  CD1 . TRP C 4   ? 0.3213 0.0319 0.2722 -0.0635 -0.0122 -0.0304 4   TRP C CD1 
4290 C  CD2 . TRP C 4   ? 0.2591 0.1220 0.1786 -0.0555 -0.0422 -0.0192 4   TRP C CD2 
4291 N  NE1 . TRP C 4   ? 0.2808 0.1049 0.3035 -0.0551 -0.0065 -0.0097 4   TRP C NE1 
4292 C  CE2 . TRP C 4   ? 0.2518 0.1445 0.1736 -0.0904 -0.0591 0.0008  4   TRP C CE2 
4293 C  CE3 . TRP C 4   ? 0.2076 0.1812 0.1629 -0.0648 -0.0231 0.0050  4   TRP C CE3 
4294 C  CZ2 . TRP C 4   ? 0.2829 0.2169 0.1966 -0.0265 -0.0257 -0.0330 4   TRP C CZ2 
4295 C  CZ3 . TRP C 4   ? 0.2694 0.2171 0.1282 0.0089  -0.0329 -0.0015 4   TRP C CZ3 
4296 C  CH2 . TRP C 4   ? 0.2885 0.2288 0.1356 -0.0379 -0.0294 -0.0467 4   TRP C CH2 
4297 N  N   . THR C 5   ? 0.3175 0.1161 0.1851 -0.0177 -0.0351 -0.0372 5   THR C N   
4298 C  CA  . THR C 5   ? 0.3008 0.1212 0.1852 0.0149  -0.0243 -0.0266 5   THR C CA  
4299 C  C   . THR C 5   ? 0.2692 0.1441 0.1334 -0.0197 0.0303  -0.0193 5   THR C C   
4300 O  O   . THR C 5   ? 0.2403 0.0961 0.1530 0.0060  -0.0057 0.0029  5   THR C O   
4301 C  CB  . THR C 5   ? 0.3054 0.0929 0.2603 0.0264  -0.0100 -0.1001 5   THR C CB  
4302 O  OG1 . THR C 5   ? 0.3273 0.2449 0.2537 -0.0103 -0.0114 -0.0603 5   THR C OG1 
4303 C  CG2 . THR C 5   ? 0.3990 0.1657 0.3295 -0.0051 -0.0345 -0.1635 5   THR C CG2 
4304 N  N   . TYR C 6   ? 0.3423 0.0692 0.1861 0.0200  0.0185  -0.0135 6   TYR C N   
4305 C  CA  . TYR C 6   ? 0.4289 0.0662 0.2546 -0.0255 0.0547  -0.0743 6   TYR C CA  
4306 C  C   . TYR C 6   ? 0.3531 0.0692 0.2745 0.0244  -0.0238 0.0122  6   TYR C C   
4307 O  O   . TYR C 6   ? 0.4057 0.1830 0.2010 -0.0835 -0.0021 -0.0209 6   TYR C O   
4308 C  CB  . TYR C 6   ? 0.3764 0.1581 0.1599 0.0286  0.0458  -0.0023 6   TYR C CB  
4309 C  CG  . TYR C 6   ? 0.2998 0.0323 0.2257 -0.0266 0.0124  -0.0578 6   TYR C CG  
4310 C  CD1 . TYR C 6   ? 0.3221 0.0118 0.2193 -0.0355 0.0119  -0.0190 6   TYR C CD1 
4311 C  CD2 . TYR C 6   ? 0.3417 0.0121 0.2085 -0.0182 0.0249  -0.0322 6   TYR C CD2 
4312 C  CE1 . TYR C 6   ? 0.3331 0.0974 0.1787 -0.0968 0.0609  -0.0275 6   TYR C CE1 
4313 C  CE2 . TYR C 6   ? 0.3098 0.0183 0.2266 -0.0541 0.0188  -0.0257 6   TYR C CE2 
4314 C  CZ  . TYR C 6   ? 0.3001 0.1035 0.1530 -0.0678 0.0308  0.0006  6   TYR C CZ  
4315 O  OH  . TYR C 6   ? 0.3129 0.1915 0.1381 -0.0996 0.0223  -0.0402 6   TYR C OH  
4316 N  N   . PHE C 7   ? 0.4052 0.1257 0.4095 -0.0282 0.1049  -0.0905 7   PHE C N   
4317 C  CA  . PHE C 7   ? 0.4548 0.3120 0.5619 -0.0573 0.1573  -0.1596 7   PHE C CA  
4318 C  C   . PHE C 7   ? 0.6012 0.2178 0.6468 -0.1679 0.3177  -0.0908 7   PHE C C   
4319 O  O   . PHE C 7   ? 0.5561 0.1974 0.4988 -0.1023 0.2573  -0.0475 7   PHE C O   
4320 C  CB  . PHE C 7   ? 0.6057 0.4642 0.5682 -0.1242 0.1128  -0.2529 7   PHE C CB  
4321 C  CG  . PHE C 7   ? 0.6796 0.4759 0.6941 -0.0783 -0.0294 -0.2929 7   PHE C CG  
4322 C  CD1 . PHE C 7   ? 0.6089 0.4503 0.6341 -0.1094 0.2007  -0.2069 7   PHE C CD1 
4323 C  CD2 . PHE C 7   ? 0.7747 0.2548 0.7984 -0.1803 -0.2453 -0.3259 7   PHE C CD2 
4324 C  CE1 . PHE C 7   ? 0.5071 0.6531 0.4708 -0.2015 -0.0107 -0.0173 7   PHE C CE1 
4325 C  CE2 . PHE C 7   ? 1.0146 0.6766 0.3211 -0.2016 -0.2842 -0.3276 7   PHE C CE2 
4326 C  CZ  . PHE C 7   ? 0.8408 0.3886 0.3599 -0.3940 -0.0042 -0.1005 7   PHE C CZ  
4327 N  N   . GLY C 8   ? 0.4241 0.3118 0.7533 -0.0798 0.1437  -0.0403 8   GLY C N   
4328 C  CA  . GLY C 8   ? 0.2418 0.3668 0.4713 -0.0365 0.0751  -0.0100 8   GLY C CA  
4329 C  C   . GLY C 8   ? 0.3909 0.1682 0.4056 -0.0370 0.0878  -0.1316 8   GLY C C   
4330 O  O   . GLY C 8   ? 0.8457 0.1363 0.3464 0.0618  -0.0315 -0.0680 8   GLY C O   
4331 N  N   . PRO C 9   ? 0.4493 0.1632 0.3121 -0.0066 0.0486  -0.1071 9   PRO C N   
4332 C  CA  . PRO C 9   ? 0.4235 0.1875 0.4014 0.0871  0.0579  -0.0650 9   PRO C CA  
4333 C  C   . PRO C 9   ? 0.3404 0.1981 0.3672 0.1038  0.0003  -0.0871 9   PRO C C   
4334 O  O   . PRO C 9   ? 0.4104 0.0783 0.3592 0.0095  -0.0506 -0.1118 9   PRO C O   
4335 C  CB  . PRO C 9   ? 0.5472 0.2548 0.4293 0.1210  0.0134  -0.1679 9   PRO C CB  
4336 C  CG  . PRO C 9   ? 0.6068 0.3392 0.4343 -0.0283 -0.0192 -0.2119 9   PRO C CG  
4337 C  CD  . PRO C 9   ? 0.5492 0.1973 0.3812 0.1456  0.0160  -0.1782 9   PRO C CD  
4338 N  N   . ASP C 10  ? 0.3240 0.1157 0.3485 0.0319  -0.0098 -0.1156 10  ASP C N   
4339 C  CA  . ASP C 10  ? 0.2896 0.1685 0.2933 0.0368  -0.0201 -0.0769 10  ASP C CA  
4340 C  C   . ASP C 10  ? 0.2912 0.1022 0.3028 -0.0216 -0.0048 -0.0406 10  ASP C C   
4341 O  O   . ASP C 10  ? 0.3118 0.1344 0.2688 -0.0242 -0.0128 -0.1015 10  ASP C O   
4342 C  CB  . ASP C 10  ? 0.4376 0.1524 0.2793 0.0395  -0.0904 -0.1175 10  ASP C CB  
4343 C  CG  . ASP C 10  ? 0.4820 0.1670 0.4643 0.0910  -0.0127 -0.1156 10  ASP C CG  
4344 O  OD1 . ASP C 10  ? 0.4376 0.1144 0.5123 -0.0688 -0.0424 -0.0728 10  ASP C OD1 
4345 O  OD2 . ASP C 10  ? 0.7256 0.2933 0.4694 -0.0149 0.0710  -0.2387 10  ASP C OD2 
4346 N  N   . GLY C 11  ? 0.2703 0.0898 0.2855 -0.0109 0.0150  -0.0950 11  GLY C N   
4347 C  CA  . GLY C 11  ? 0.2612 0.0653 0.1941 0.0201  0.0159  -0.0421 11  GLY C CA  
4348 C  C   . GLY C 11  ? 0.2037 0.0249 0.1803 0.0294  -0.0269 -0.0156 11  GLY C C   
4349 O  O   . GLY C 11  ? 0.2461 0.0647 0.2153 -0.0071 -0.0263 0.0097  11  GLY C O   
4350 N  N   . GLU C 12  ? 0.1708 0.0467 0.1699 -0.0225 -0.0299 -0.0489 12  GLU C N   
4351 C  CA  . GLU C 12  ? 0.2044 0.0163 0.1681 -0.0046 -0.0327 -0.0384 12  GLU C CA  
4352 C  C   . GLU C 12  ? 0.1796 0.0164 0.1740 -0.0163 -0.0153 -0.0013 12  GLU C C   
4353 O  O   . GLU C 12  ? 0.1785 0.0099 0.1746 -0.0250 -0.0177 0.0027  12  GLU C O   
4354 C  CB  . GLU C 12  ? 0.1928 0.0065 0.2105 0.0059  -0.0712 -0.0033 12  GLU C CB  
4355 C  CG  . GLU C 12  ? 0.1899 0.0068 0.2135 0.0055  -0.0214 -0.0084 12  GLU C CG  
4356 C  CD  . GLU C 12  ? 0.1943 0.0110 0.1395 0.0218  -0.0025 0.0088  12  GLU C CD  
4357 O  OE1 . GLU C 12  ? 0.1762 0.0234 0.1703 -0.0013 -0.0102 -0.0126 12  GLU C OE1 
4358 O  OE2 . GLU C 12  ? 0.2376 0.0362 0.1492 -0.0298 0.0100  0.0006  12  GLU C OE2 
4359 N  N   . ASN C 13  ? 0.1815 0.0393 0.2078 -0.0103 -0.0064 -0.0140 13  ASN C N   
4360 C  CA  . ASN C 13  ? 0.1460 0.0292 0.2097 -0.0451 0.0002  -0.0150 13  ASN C CA  
4361 C  C   . ASN C 13  ? 0.1706 0.0230 0.2240 -0.0274 0.0051  0.0040  13  ASN C C   
4362 O  O   . ASN C 13  ? 0.1866 0.0362 0.2303 -0.0126 -0.0291 -0.0268 13  ASN C O   
4363 C  CB  . ASN C 13  ? 0.1655 0.0144 0.2019 -0.0338 0.0255  0.0077  13  ASN C CB  
4364 C  CG  . ASN C 13  ? 0.1657 0.0072 0.1725 -0.0105 0.0036  0.0059  13  ASN C CG  
4365 O  OD1 . ASN C 13  ? 0.1683 0.0410 0.2067 -0.0011 0.0155  -0.0147 13  ASN C OD1 
4366 N  ND2 . ASN C 13  ? 0.1559 0.0326 0.2204 0.0037  -0.0038 -0.0078 13  ASN C ND2 
4367 N  N   . SER C 14  ? 0.1522 0.0135 0.2253 -0.0321 0.0181  0.0011  14  SER C N   
4368 C  CA  . SER C 14  ? 0.2038 0.0185 0.2012 -0.0488 0.0320  -0.0123 14  SER C CA  
4369 C  C   . SER C 14  ? 0.1739 0.0205 0.1784 -0.0469 0.0060  0.0113  14  SER C C   
4370 O  O   . SER C 14  ? 0.2311 0.0187 0.2648 -0.0474 0.0285  -0.0305 14  SER C O   
4371 C  CB  . SER C 14  ? 0.2664 0.0184 0.2469 -0.0411 0.0846  -0.0477 14  SER C CB  
4372 O  OG  . SER C 14  ? 0.2990 0.1042 0.3173 -0.0205 0.0593  -0.0343 14  SER C OG  
4373 N  N   . TRP C 15  ? 0.2204 0.0750 0.1685 -0.0135 0.0000  -0.0355 15  TRP C N   
4374 C  CA  . TRP C 15  ? 0.1945 0.0223 0.1913 0.0085  -0.0273 0.0012  15  TRP C CA  
4375 C  C   . TRP C 15  ? 0.1934 0.0118 0.1795 -0.0265 0.0009  -0.0173 15  TRP C C   
4376 O  O   . TRP C 15  ? 0.2007 0.0147 0.2184 -0.0317 -0.0239 -0.0219 15  TRP C O   
4377 C  CB  . TRP C 15  ? 0.2490 0.0121 0.2033 -0.0068 -0.0090 -0.0328 15  TRP C CB  
4378 C  CG  . TRP C 15  ? 0.1956 0.0311 0.1840 -0.0264 0.0000  -0.0238 15  TRP C CG  
4379 C  CD1 . TRP C 15  ? 0.2236 0.0627 0.1613 -0.0468 -0.0301 0.0148  15  TRP C CD1 
4380 C  CD2 . TRP C 15  ? 0.2266 0.0239 0.1695 -0.0375 -0.0220 -0.0386 15  TRP C CD2 
4381 N  NE1 . TRP C 15  ? 0.2134 0.0440 0.1446 -0.0113 0.0047  -0.0022 15  TRP C NE1 
4382 C  CE2 . TRP C 15  ? 0.2232 0.0301 0.1719 -0.0106 -0.0456 -0.0303 15  TRP C CE2 
4383 C  CE3 . TRP C 15  ? 0.1491 0.0234 0.1987 0.0136  -0.0089 -0.0287 15  TRP C CE3 
4384 C  CZ2 . TRP C 15  ? 0.2339 0.0144 0.1639 -0.0313 -0.0046 -0.0237 15  TRP C CZ2 
4385 C  CZ3 . TRP C 15  ? 0.1767 0.0155 0.1586 -0.0106 -0.0257 -0.0218 15  TRP C CZ3 
4386 C  CH2 . TRP C 15  ? 0.1984 0.0450 0.1618 -0.0440 -0.0298 -0.0454 15  TRP C CH2 
4387 N  N   . SER C 16  ? 0.1888 0.0369 0.1920 -0.0089 -0.0135 -0.0062 16  SER C N   
4388 C  CA  . SER C 16  ? 0.1474 0.0416 0.1844 -0.0217 -0.0186 -0.0302 16  SER C CA  
4389 C  C   . SER C 16  ? 0.1517 0.0381 0.2081 -0.0428 0.0257  -0.0024 16  SER C C   
4390 O  O   . SER C 16  ? 0.1873 0.0200 0.1990 -0.0421 -0.0006 -0.0012 16  SER C O   
4391 C  CB  . SER C 16  ? 0.1668 0.0202 0.1982 -0.0444 -0.0182 -0.0121 16  SER C CB  
4392 O  OG  . SER C 16  ? 0.1885 0.0119 0.2149 -0.0318 -0.0074 0.0020  16  SER C OG  
4393 N  N   A LYS C 17  ? 0.1886 0.0320 0.2225 0.0107  0.0008  -0.0240 17  LYS C N   
4394 N  N   B LYS C 17  ? 0.2042 0.0306 0.2094 0.0020  -0.0062 -0.0245 17  LYS C N   
4395 C  CA  A LYS C 17  ? 0.2302 0.0327 0.2505 -0.0229 0.0289  -0.0361 17  LYS C CA  
4396 C  CA  B LYS C 17  ? 0.2494 0.0308 0.2270 -0.0367 0.0193  -0.0409 17  LYS C CA  
4397 C  C   A LYS C 17  ? 0.1963 0.0072 0.2333 -0.0060 0.0130  0.0119  17  LYS C C   
4398 C  C   B LYS C 17  ? 0.2148 0.0138 0.2042 -0.0239 0.0074  0.0146  17  LYS C C   
4399 O  O   A LYS C 17  ? 0.2448 0.0136 0.3009 0.0128  -0.0394 0.0413  17  LYS C O   
4400 O  O   B LYS C 17  ? 0.2722 0.0160 0.2575 -0.0485 -0.0469 0.0225  17  LYS C O   
4401 C  CB  A LYS C 17  ? 0.2225 0.0134 0.2868 -0.0096 0.0474  -0.0445 17  LYS C CB  
4402 C  CB  B LYS C 17  ? 0.2909 0.0227 0.2336 -0.0379 0.0306  -0.0546 17  LYS C CB  
4403 C  CG  A LYS C 17  ? 0.2191 0.1301 0.2965 -0.0149 0.0921  -0.0416 17  LYS C CG  
4404 C  CG  B LYS C 17  ? 0.3050 0.0976 0.2897 -0.0844 0.0509  -0.0778 17  LYS C CG  
4405 C  CD  A LYS C 17  ? 0.2187 0.1008 0.2937 -0.0055 0.0930  -0.0580 17  LYS C CD  
4406 C  CD  B LYS C 17  ? 0.3754 0.0981 0.2679 -0.0763 0.0660  -0.0748 17  LYS C CD  
4407 C  CE  A LYS C 17  ? 0.2664 0.0173 0.2665 -0.0210 0.1018  0.0368  17  LYS C CE  
4408 C  CE  B LYS C 17  ? 0.4234 0.1521 0.3354 -0.0892 0.1035  -0.2181 17  LYS C CE  
4409 N  NZ  A LYS C 17  ? 0.1539 0.0215 0.2441 0.0010  0.0463  -0.0158 17  LYS C NZ  
4410 N  NZ  B LYS C 17  ? 0.4357 0.0897 0.6638 -0.0993 0.0138  -0.2024 17  LYS C NZ  
4411 N  N   . LYS C 18  ? 0.2194 0.0072 0.2712 -0.0141 -0.0051 0.0000  18  LYS C N   
4412 C  CA  . LYS C 18  ? 0.2148 0.0072 0.2599 -0.0136 -0.0266 -0.0007 18  LYS C CA  
4413 C  C   . LYS C 18  ? 0.2317 0.0608 0.1944 -0.0648 0.0154  -0.0176 18  LYS C C   
4414 O  O   . LYS C 18  ? 0.2747 0.0356 0.3037 -0.0770 0.0385  -0.0566 18  LYS C O   
4415 C  CB  . LYS C 18  ? 0.3123 0.0322 0.2514 -0.0021 -0.0463 0.0040  18  LYS C CB  
4416 C  CG  . LYS C 18  ? 0.4284 0.3096 0.3638 0.0929  0.0219  -0.0973 18  LYS C CG  
4417 C  CD  . LYS C 18  ? 0.5286 0.3357 0.4512 0.0564  -0.0009 -0.0412 18  LYS C CD  
4418 C  CE  . LYS C 18  ? 0.7595 0.1708 0.4090 0.0171  -0.0190 0.0122  18  LYS C CE  
4419 N  NZ  . LYS C 18  ? 0.5719 0.6072 0.6556 0.2293  -0.1429 -0.1843 18  LYS C NZ  
4420 N  N   . TYR C 19  ? 0.2472 0.0392 0.2017 0.0006  -0.0183 -0.0460 19  TYR C N   
4421 C  CA  . TYR C 19  ? 0.1998 0.0109 0.2014 -0.0296 -0.0161 0.0058  19  TYR C CA  
4422 C  C   . TYR C 19  ? 0.1758 0.0835 0.1963 -0.0165 -0.0073 -0.0203 19  TYR C C   
4423 O  O   . TYR C 19  ? 0.1428 0.0559 0.1868 0.0011  -0.0182 -0.0463 19  TYR C O   
4424 C  CB  . TYR C 19  ? 0.2430 0.0079 0.1843 -0.0183 -0.0200 -0.0034 19  TYR C CB  
4425 C  CG  . TYR C 19  ? 0.2357 0.0285 0.1988 -0.0373 -0.0277 -0.0022 19  TYR C CG  
4426 C  CD1 . TYR C 19  ? 0.2227 0.0547 0.2139 -0.0066 -0.0625 -0.0318 19  TYR C CD1 
4427 C  CD2 . TYR C 19  ? 0.2697 0.0065 0.2020 0.0022  -0.0031 0.0063  19  TYR C CD2 
4428 C  CE1 . TYR C 19  ? 0.2889 0.0900 0.1994 -0.0088 -0.0556 -0.0518 19  TYR C CE1 
4429 C  CE2 . TYR C 19  ? 0.2681 0.0516 0.2256 -0.0391 -0.0237 0.0083  19  TYR C CE2 
4430 C  CZ  . TYR C 19  ? 0.3094 0.0422 0.2020 -0.0190 -0.0588 -0.0350 19  TYR C CZ  
4431 O  OH  . TYR C 19  ? 0.3586 0.1724 0.2243 -0.0245 -0.0807 -0.0714 19  TYR C OH  
4432 N  N   . PRO C 20  ? 0.1797 0.0238 0.2134 -0.0463 -0.0201 -0.0268 20  PRO C N   
4433 C  CA  . PRO C 20  ? 0.1750 0.0192 0.1872 -0.0146 -0.0314 0.0067  20  PRO C CA  
4434 C  C   . PRO C 20  ? 0.1588 0.0258 0.1773 -0.0162 -0.0170 0.0027  20  PRO C C   
4435 O  O   . PRO C 20  ? 0.1884 0.0304 0.2126 -0.0345 -0.0237 0.0129  20  PRO C O   
4436 C  CB  . PRO C 20  ? 0.2500 0.0121 0.2544 -0.0162 -0.0135 0.0263  20  PRO C CB  
4437 C  CG  . PRO C 20  ? 0.2845 0.1441 0.2651 -0.1013 -0.0661 0.0374  20  PRO C CG  
4438 C  CD  . PRO C 20  ? 0.2055 0.0348 0.2415 -0.0728 -0.0302 -0.0100 20  PRO C CD  
4439 N  N   . SER C 21  ? 0.1696 0.0162 0.1747 -0.0079 0.0190  -0.0036 21  SER C N   
4440 C  CA  . SER C 21  ? 0.1433 0.0183 0.2124 0.0074  -0.0190 -0.0147 21  SER C CA  
4441 C  C   . SER C 21  ? 0.1409 0.0699 0.1309 -0.0109 -0.0405 -0.0153 21  SER C C   
4442 O  O   . SER C 21  ? 0.1467 0.0297 0.1787 0.0027  -0.0153 -0.0140 21  SER C O   
4443 C  CB  . SER C 21  ? 0.1245 0.0902 0.2142 -0.0084 -0.0267 0.0421  21  SER C CB  
4444 O  OG  . SER C 21  ? 0.1891 0.0900 0.2455 -0.0356 0.0201  -0.0008 21  SER C OG  
4445 N  N   . CYS C 22  ? 0.1844 0.0144 0.1402 -0.0316 -0.0085 0.0098  22  CYS C N   
4446 C  CA  . CYS C 22  ? 0.1604 0.0387 0.1636 -0.0321 -0.0082 0.0310  22  CYS C CA  
4447 C  C   . CYS C 22  ? 0.1072 0.0528 0.2195 0.0170  0.0198  0.0277  22  CYS C C   
4448 O  O   . CYS C 22  ? 0.1426 0.0778 0.1714 -0.0329 0.0068  -0.0064 22  CYS C O   
4449 C  CB  . CYS C 22  ? 0.1825 0.0136 0.1676 -0.0253 0.0077  0.0234  22  CYS C CB  
4450 S  SG  . CYS C 22  ? 0.1940 0.0101 0.2046 -0.0170 -0.0022 0.0000  22  CYS C SG  
4451 N  N   . GLY C 23  ? 0.1460 0.0146 0.1992 -0.0022 -0.0119 -0.0040 23  GLY C N   
4452 C  CA  . GLY C 23  ? 0.1596 0.0075 0.2156 0.0086  -0.0335 0.0097  23  GLY C CA  
4453 C  C   . GLY C 23  ? 0.1864 0.0099 0.2372 -0.0049 -0.0088 0.0283  23  GLY C C   
4454 O  O   . GLY C 23  ? 0.2038 0.0081 0.2221 0.0103  -0.0188 0.0154  23  GLY C O   
4455 N  N   . GLY C 24  ? 0.1825 0.0618 0.1744 -0.0042 -0.0161 0.0298  24  GLY C N   
4456 C  CA  . GLY C 24  ? 0.2131 0.0703 0.1711 0.0181  -0.0332 0.0002  24  GLY C CA  
4457 C  C   . GLY C 24  ? 0.1819 0.0612 0.1520 0.0240  -0.0102 0.0200  24  GLY C C   
4458 O  O   . GLY C 24  ? 0.1728 0.1194 0.1872 -0.0111 -0.0077 0.0421  24  GLY C O   
4459 N  N   . LEU C 25  ? 0.2227 0.0654 0.1531 0.0390  -0.0096 -0.0261 25  LEU C N   
4460 C  CA  . LEU C 25  ? 0.2110 0.0855 0.1661 0.0526  -0.0409 -0.0547 25  LEU C CA  
4461 C  C   . LEU C 25  ? 0.2396 0.1240 0.1683 0.0476  -0.0380 -0.0181 25  LEU C C   
4462 O  O   . LEU C 25  ? 0.2209 0.0918 0.1442 0.0146  -0.0157 0.0061  25  LEU C O   
4463 C  CB  . LEU C 25  ? 0.3235 0.1345 0.1670 0.0868  -0.0398 -0.0136 25  LEU C CB  
4464 C  CG  . LEU C 25  ? 0.3856 0.1241 0.2546 0.0890  -0.0996 -0.0029 25  LEU C CG  
4465 C  CD1 . LEU C 25  ? 0.5605 0.2196 0.2121 0.1193  -0.0916 0.0005  25  LEU C CD1 
4466 C  CD2 . LEU C 25  ? 0.3894 0.2944 0.3162 0.0519  -0.1775 -0.0314 25  LEU C CD2 
4467 N  N   . LEU C 26  ? 0.2139 0.1088 0.1245 -0.0012 -0.0392 0.0172  26  LEU C N   
4468 C  CA  . LEU C 26  ? 0.2556 0.0857 0.1196 0.0209  -0.0232 0.0027  26  LEU C CA  
4469 C  C   . LEU C 26  ? 0.1773 0.0296 0.1221 0.0044  -0.0254 -0.0099 26  LEU C C   
4470 O  O   . LEU C 26  ? 0.1841 0.1205 0.1506 0.0580  -0.0095 0.0017  26  LEU C O   
4471 C  CB  . LEU C 26  ? 0.2854 0.1069 0.1798 0.0535  0.0197  0.0201  26  LEU C CB  
4472 C  CG  . LEU C 26  ? 0.3066 0.3553 0.2587 0.0107  0.0637  -0.0834 26  LEU C CG  
4473 C  CD1 . LEU C 26  ? 0.3680 0.2648 0.3630 0.0950  0.1070  -0.0955 26  LEU C CD1 
4474 C  CD2 . LEU C 26  ? 0.5468 0.2222 0.1916 0.0149  0.0062  -0.0949 26  LEU C CD2 
4475 N  N   . GLN C 27  ? 0.1873 0.0249 0.1273 0.0099  -0.0018 -0.0005 27  GLN C N   
4476 C  CA  . GLN C 27  ? 0.1629 0.0153 0.1316 0.0104  -0.0124 0.0000  27  GLN C CA  
4477 C  C   . GLN C 27  ? 0.1280 0.0233 0.1169 -0.0167 -0.0245 0.0114  27  GLN C C   
4478 O  O   . GLN C 27  ? 0.1937 0.0451 0.1584 -0.0288 -0.0678 -0.0041 27  GLN C O   
4479 C  CB  . GLN C 27  ? 0.1445 0.0146 0.1506 0.0031  0.0042  0.0085  27  GLN C CB  
4480 C  CG  . GLN C 27  ? 0.1538 0.0158 0.1692 -0.0140 -0.0106 0.0106  27  GLN C CG  
4481 C  CD  . GLN C 27  ? 0.1510 0.0217 0.1258 0.0022  -0.0040 0.0136  27  GLN C CD  
4482 O  OE1 . GLN C 27  ? 0.1726 0.0408 0.1255 -0.0170 -0.0059 -0.0020 27  GLN C OE1 
4483 N  NE2 . GLN C 27  ? 0.1636 0.0335 0.1681 0.0148  0.0159  -0.0050 27  GLN C NE2 
4484 N  N   . SER C 28  ? 0.1506 0.0070 0.1193 0.0009  -0.0299 0.0084  28  SER C N   
4485 C  CA  . SER C 28  ? 0.1217 0.0117 0.1382 0.0129  0.0101  0.0239  28  SER C CA  
4486 C  C   . SER C 28  ? 0.1262 0.0413 0.1476 0.0099  -0.0029 -0.0262 28  SER C C   
4487 O  O   . SER C 28  ? 0.1536 0.0281 0.1492 0.0024  0.0023  -0.0156 28  SER C O   
4488 C  CB  . SER C 28  ? 0.1139 0.0093 0.1513 -0.0065 0.0010  -0.0051 28  SER C CB  
4489 O  OG  . SER C 28  ? 0.1509 0.0542 0.1452 -0.0135 0.0139  0.0031  28  SER C OG  
4490 N  N   . PRO C 29  ? 0.1204 0.0450 0.1265 0.0030  -0.0163 -0.0167 29  PRO C N   
4491 C  CA  . PRO C 29  ? 0.1288 0.0389 0.1229 0.0278  -0.0289 -0.0058 29  PRO C CA  
4492 C  C   . PRO C 29  ? 0.1478 0.0848 0.1514 0.0138  -0.0256 -0.0255 29  PRO C C   
4493 O  O   . PRO C 29  ? 0.1304 0.0406 0.1564 -0.0096 -0.0221 -0.0203 29  PRO C O   
4494 C  CB  . PRO C 29  ? 0.1699 0.0714 0.1124 -0.0031 -0.0075 -0.0192 29  PRO C CB  
4495 C  CG  . PRO C 29  ? 0.1313 0.0104 0.1470 -0.0226 -0.0025 0.0010  29  PRO C CG  
4496 C  CD  . PRO C 29  ? 0.1636 0.0162 0.1187 -0.0301 0.0004  0.0190  29  PRO C CD  
4497 N  N   . ILE C 30  ? 0.1153 0.0728 0.1291 0.0062  -0.0081 -0.0106 30  ILE C N   
4498 C  CA  . ILE C 30  ? 0.1682 0.0251 0.1434 -0.0301 -0.0075 -0.0098 30  ILE C CA  
4499 C  C   . ILE C 30  ? 0.1248 0.0161 0.1361 -0.0092 -0.0036 -0.0151 30  ILE C C   
4500 O  O   . ILE C 30  ? 0.1539 0.0309 0.1647 -0.0125 -0.0196 -0.0105 30  ILE C O   
4501 C  CB  . ILE C 30  ? 0.1381 0.0119 0.1426 -0.0049 0.0038  -0.0272 30  ILE C CB  
4502 C  CG1 . ILE C 30  ? 0.1330 0.0999 0.1446 0.0233  0.0023  -0.0380 30  ILE C CG1 
4503 C  CG2 . ILE C 30  ? 0.2020 0.0200 0.2038 -0.0126 -0.0093 0.0026  30  ILE C CG2 
4504 C  CD1 . ILE C 30  ? 0.1755 0.0841 0.1556 0.0385  0.0092  -0.0613 30  ILE C CD1 
4505 N  N   . ASP C 31  ? 0.1708 0.0223 0.1816 -0.0439 -0.0247 -0.0065 31  ASP C N   
4506 C  CA  . ASP C 31  ? 0.1067 0.0192 0.1340 -0.0215 -0.0179 0.0053  31  ASP C CA  
4507 C  C   . ASP C 31  ? 0.1251 0.0941 0.1683 0.0183  -0.0429 -0.0271 31  ASP C C   
4508 O  O   . ASP C 31  ? 0.2119 0.0794 0.1654 0.0048  -0.0269 -0.0134 31  ASP C O   
4509 C  CB  . ASP C 31  ? 0.0981 0.0399 0.2225 0.0061  -0.0029 0.0212  31  ASP C CB  
4510 C  CG  . ASP C 31  ? 0.1349 0.0489 0.1557 -0.0107 -0.0098 0.0218  31  ASP C CG  
4511 O  OD1 . ASP C 31  ? 0.1859 0.0477 0.1739 -0.0156 -0.0248 0.0209  31  ASP C OD1 
4512 O  OD2 . ASP C 31  ? 0.2670 0.1288 0.2426 -0.0355 -0.0885 0.0049  31  ASP C OD2 
4513 N  N   . LEU C 32  ? 0.1507 0.0992 0.1542 0.0247  -0.0230 0.0053  32  LEU C N   
4514 C  CA  . LEU C 32  ? 0.1545 0.0692 0.1740 0.0124  -0.0538 -0.0284 32  LEU C CA  
4515 C  C   . LEU C 32  ? 0.1586 0.0618 0.1474 0.0234  -0.0228 -0.0314 32  LEU C C   
4516 O  O   . LEU C 32  ? 0.2074 0.0974 0.2091 -0.0076 -0.0286 0.0227  32  LEU C O   
4517 C  CB  . LEU C 32  ? 0.1374 0.0796 0.1805 0.0096  -0.0261 -0.0154 32  LEU C CB  
4518 C  CG  . LEU C 32  ? 0.1115 0.1027 0.1575 -0.0033 -0.0092 -0.0065 32  LEU C CG  
4519 C  CD1 . LEU C 32  ? 0.1178 0.1499 0.2315 -0.0136 -0.0480 -0.0095 32  LEU C CD1 
4520 C  CD2 . LEU C 32  ? 0.2196 0.1974 0.2097 -0.0060 0.0038  0.0699  32  LEU C CD2 
4521 N  N   . HIS C 33  ? 0.2658 0.1153 0.2182 -0.0345 -0.1107 -0.0155 33  HIS C N   
4522 C  CA  . HIS C 33  ? 0.2506 0.2187 0.3350 -0.0938 -0.1274 0.0033  33  HIS C CA  
4523 C  C   . HIS C 33  ? 0.2207 0.1604 0.3583 -0.0627 -0.1553 -0.0068 33  HIS C C   
4524 O  O   . HIS C 33  ? 0.2385 0.1453 0.3281 -0.0114 -0.0671 -0.0583 33  HIS C O   
4525 C  CB  . HIS C 33  ? 0.3908 0.2694 0.3754 0.1477  -0.0994 -0.0908 33  HIS C CB  
4526 C  CG  . HIS C 33  ? 0.3819 0.3225 0.3374 0.1710  -0.0901 -0.0750 33  HIS C CG  
4527 N  ND1 . HIS C 33  ? 0.3941 0.4932 0.4405 0.1259  -0.1222 -0.1638 33  HIS C ND1 
4528 C  CD2 . HIS C 33  ? 0.2689 0.4095 0.3357 0.0152  -0.0723 -0.0340 33  HIS C CD2 
4529 C  CE1 . HIS C 33  ? 0.5592 0.5326 0.4742 -0.0084 -0.0804 -0.1148 33  HIS C CE1 
4530 N  NE2 . HIS C 33  ? 0.3789 0.4325 0.4647 0.1178  -0.1741 -0.0272 33  HIS C NE2 
4531 N  N   . SER C 34  ? 0.3100 0.1363 0.4868 -0.0787 -0.0906 0.0312  34  SER C N   
4532 C  CA  . SER C 34  ? 0.3177 0.1164 0.6230 0.0095  -0.1053 0.0268  34  SER C CA  
4533 C  C   . SER C 34  ? 0.2581 0.3428 0.4388 -0.0462 -0.0947 -0.1398 34  SER C C   
4534 O  O   . SER C 34  ? 0.4057 0.2381 0.3834 -0.0242 -0.0930 -0.1277 34  SER C O   
4535 C  CB  . SER C 34  ? 0.4785 0.2919 0.8491 -0.1982 -0.1009 0.1464  34  SER C CB  
4536 O  OG  . SER C 34  ? 0.6141 0.6943 1.0271 -0.1037 0.0134  0.2146  34  SER C OG  
4537 N  N   . ASP C 35  ? 0.2157 0.2159 0.5248 -0.1021 -0.0630 -0.1075 35  ASP C N   
4538 C  CA  . ASP C 35  ? 0.2988 0.3883 0.5468 0.0239  -0.1229 -0.1390 35  ASP C CA  
4539 C  C   . ASP C 35  ? 0.2581 0.4563 0.3272 0.0594  -0.0925 -0.1868 35  ASP C C   
4540 O  O   . ASP C 35  ? 0.3492 0.6380 0.3388 0.0522  -0.1081 -0.2149 35  ASP C O   
4541 C  CB  . ASP C 35  ? 0.2529 0.5184 0.5216 0.0140  -0.1502 -0.1241 35  ASP C CB  
4542 C  CG  . ASP C 35  ? 0.2861 0.6085 0.5577 -0.0096 -0.1073 -0.1787 35  ASP C CG  
4543 O  OD1 . ASP C 35  ? 0.5073 0.5495 0.7040 -0.0901 -0.0781 -0.1926 35  ASP C OD1 
4544 O  OD2 . ASP C 35  ? 0.3208 0.8447 0.5037 -0.0795 -0.0157 -0.3180 35  ASP C OD2 
4545 N  N   . ILE C 36  ? 0.1725 0.3256 0.2832 0.0608  -0.0921 -0.0706 36  ILE C N   
4546 C  CA  . ILE C 36  ? 0.2279 0.2060 0.2790 0.0820  -0.1175 -0.0357 36  ILE C CA  
4547 C  C   . ILE C 36  ? 0.2240 0.1877 0.2236 0.0490  -0.0797 -0.0574 36  ILE C C   
4548 O  O   . ILE C 36  ? 0.2331 0.2144 0.2675 0.0675  -0.0568 -0.0244 36  ILE C O   
4549 C  CB  . ILE C 36  ? 0.2457 0.1941 0.2383 0.0908  -0.0332 0.0030  36  ILE C CB  
4550 C  CG1 . ILE C 36  ? 0.3089 0.0851 0.2078 -0.0012 -0.0011 0.0036  36  ILE C CG1 
4551 C  CG2 . ILE C 36  ? 0.2449 0.2432 0.3265 0.1138  -0.0362 -0.0948 36  ILE C CG2 
4552 C  CD1 . ILE C 36  ? 0.2970 0.1258 0.2771 0.0684  -0.0261 -0.0613 36  ILE C CD1 
4553 N  N   . LEU C 37  ? 0.2475 0.1749 0.2556 0.1008  -0.0836 -0.0866 37  LEU C N   
4554 C  CA  . LEU C 37  ? 0.2419 0.2074 0.2587 0.0800  -0.0979 -0.0564 37  LEU C CA  
4555 C  C   . LEU C 37  ? 0.2130 0.1216 0.2629 0.0539  -0.0814 -0.0702 37  LEU C C   
4556 O  O   . LEU C 37  ? 0.2426 0.3340 0.3455 0.0005  -0.0656 -0.2091 37  LEU C O   
4557 C  CB  . LEU C 37  ? 0.1995 0.2444 0.3450 0.0590  -0.0802 -0.0115 37  LEU C CB  
4558 C  CG  . LEU C 37  ? 0.2113 0.1704 0.3714 0.0493  -0.0785 -0.0774 37  LEU C CG  
4559 C  CD1 . LEU C 37  ? 0.2879 0.1534 0.4575 0.0959  -0.0956 -0.0644 37  LEU C CD1 
4560 C  CD2 . LEU C 37  ? 0.2102 0.1649 0.3310 0.0578  -0.0870 -0.0726 37  LEU C CD2 
4561 N  N   . GLN C 38  ? 0.2281 0.2203 0.2242 0.0429  -0.0712 -0.0941 38  GLN C N   
4562 C  CA  . GLN C 38  ? 0.2928 0.2666 0.2388 0.0880  -0.0604 -0.1092 38  GLN C CA  
4563 C  C   . GLN C 38  ? 0.2940 0.1597 0.2051 0.1094  -0.0801 -0.1204 38  GLN C C   
4564 O  O   . GLN C 38  ? 0.2789 0.1823 0.2725 0.1139  -0.1182 -0.1331 38  GLN C O   
4565 C  CB  . GLN C 38  ? 0.3353 0.3132 0.1749 0.1351  -0.0762 -0.1081 38  GLN C CB  
4566 C  CG  . GLN C 38  ? 0.3424 0.4035 0.2108 0.1461  -0.0886 -0.1814 38  GLN C CG  
4567 C  CD  . GLN C 38  ? 0.3856 0.4578 0.2078 -0.0205 0.0140  -0.0850 38  GLN C CD  
4568 O  OE1 . GLN C 38  ? 0.5387 0.5812 0.4181 0.0759  -0.2014 -0.1849 38  GLN C OE1 
4569 N  NE2 . GLN C 38  ? 0.2889 0.3710 0.2962 -0.0159 -0.0087 -0.1658 38  GLN C NE2 
4570 N  N   . TYR C 39  ? 0.3752 0.1613 0.2635 0.1699  -0.1026 -0.0829 39  TYR C N   
4571 C  CA  . TYR C 39  ? 0.3754 0.1699 0.3118 0.1885  -0.1297 -0.1128 39  TYR C CA  
4572 C  C   . TYR C 39  ? 0.3389 0.3264 0.2762 0.1851  -0.0460 -0.1852 39  TYR C C   
4573 O  O   . TYR C 39  ? 0.4781 0.5220 0.2590 0.0948  -0.1026 -0.1893 39  TYR C O   
4574 C  CB  . TYR C 39  ? 0.4533 0.2088 0.2755 0.1884  -0.1582 -0.1680 39  TYR C CB  
4575 C  CG  . TYR C 39  ? 0.3826 0.3063 0.5614 0.1668  -0.2424 -0.2512 39  TYR C CG  
4576 C  CD1 . TYR C 39  ? 0.2618 0.1474 0.6790 0.0529  -0.1713 -0.2291 39  TYR C CD1 
4577 C  CD2 . TYR C 39  ? 0.4125 0.0996 0.5977 -0.0351 -0.0840 -0.1035 39  TYR C CD2 
4578 C  CE1 . TYR C 39  ? 0.3838 0.3005 0.6718 0.2070  -0.1581 -0.2794 39  TYR C CE1 
4579 C  CE2 . TYR C 39  ? 0.3804 0.5559 0.6651 0.1226  -0.0435 -0.1993 39  TYR C CE2 
4580 C  CZ  . TYR C 39  ? 0.4246 0.1046 0.6769 0.0254  -0.0215 -0.1376 39  TYR C CZ  
4581 O  OH  . TYR C 39  ? 0.5108 0.2389 0.6227 0.1173  0.0725  0.0009  39  TYR C OH  
4582 N  N   A ASP C 40  ? 0.3277 0.4683 0.2684 0.1665  -0.0541 -0.1205 40  ASP C N   
4583 N  N   B ASP C 40  ? 0.3324 0.4802 0.2536 0.1657  -0.0572 -0.1341 40  ASP C N   
4584 C  CA  A ASP C 40  ? 0.2999 0.3541 0.2613 0.2027  -0.0710 -0.1201 40  ASP C CA  
4585 C  CA  B ASP C 40  ? 0.2995 0.3814 0.2726 0.1948  -0.0753 -0.1282 40  ASP C CA  
4586 C  C   A ASP C 40  ? 0.2509 0.3848 0.3103 0.1600  -0.0185 -0.2609 40  ASP C C   
4587 C  C   B ASP C 40  ? 0.2442 0.4528 0.4006 0.1799  -0.0622 -0.2334 40  ASP C C   
4588 O  O   A ASP C 40  ? 0.2754 0.3504 0.2812 0.0992  0.0064  -0.1307 40  ASP C O   
4589 O  O   B ASP C 40  ? 0.2834 0.3191 0.3111 0.0855  -0.0157 -0.1277 40  ASP C O   
4590 C  CB  A ASP C 40  ? 0.3820 0.2579 0.2995 0.0465  -0.0086 0.0125  40  ASP C CB  
4591 C  CB  B ASP C 40  ? 0.3701 0.2827 0.3055 0.0345  -0.0159 0.0218  40  ASP C CB  
4592 C  CG  A ASP C 40  ? 0.3972 0.1083 0.3678 0.1323  0.0044  0.0390  40  ASP C CG  
4593 C  CG  B ASP C 40  ? 0.4012 0.1017 0.3665 0.1267  0.0012  0.0329  40  ASP C CG  
4594 O  OD1 A ASP C 40  ? 0.4458 0.0979 0.3031 0.0919  0.0030  0.0495  40  ASP C OD1 
4595 O  OD1 B ASP C 40  ? 0.4338 0.1887 0.3055 0.0867  -0.0006 0.0472  40  ASP C OD1 
4596 O  OD2 A ASP C 40  ? 0.4777 0.1045 0.5133 0.0229  -0.0167 -0.0276 40  ASP C OD2 
4597 O  OD2 B ASP C 40  ? 0.4667 0.1021 0.5157 0.0280  -0.0077 -0.0310 40  ASP C OD2 
4598 N  N   A ALA C 41  ? 0.2171 0.1736 0.2601 -0.0388 0.1037  -0.0867 41  ALA C N   
4599 N  N   B ALA C 41  ? 0.2825 0.3556 0.3570 0.0986  -0.0044 -0.1382 41  ALA C N   
4600 C  CA  A ALA C 41  ? 0.2912 0.0905 0.1560 0.0414  0.1486  0.0209  41  ALA C CA  
4601 C  CA  B ALA C 41  ? 0.3173 0.2473 0.2938 0.0688  0.0872  -0.0145 41  ALA C CA  
4602 C  C   A ALA C 41  ? 0.2041 0.1941 0.2192 0.0942  0.0469  0.0945  41  ALA C C   
4603 C  C   B ALA C 41  ? 0.3106 0.2546 0.3290 0.0487  0.0549  0.0263  41  ALA C C   
4604 O  O   A ALA C 41  ? 0.2006 0.2205 0.2775 0.1169  0.0671  0.1215  41  ALA C O   
4605 O  O   B ALA C 41  ? 0.3335 0.2902 0.3790 0.0772  0.0630  0.0177  41  ALA C O   
4606 C  CB  A ALA C 41  ? 0.3211 0.2064 0.2376 0.0594  0.0894  -0.1011 41  ALA C CB  
4607 C  CB  B ALA C 41  ? 0.4038 0.2940 0.3601 0.0309  0.0629  -0.0550 41  ALA C CB  
4608 N  N   A SER C 42  ? 0.2631 0.1694 0.2227 0.0902  0.0059  0.0034  42  SER C N   
4609 N  N   B SER C 42  ? 0.3524 0.2072 0.2937 0.1120  0.0209  0.0181  42  SER C N   
4610 C  CA  A SER C 42  ? 0.2652 0.2246 0.2002 0.0584  0.0210  0.1095  42  SER C CA  
4611 C  CA  B SER C 42  ? 0.3536 0.2807 0.2906 0.0281  0.0629  0.0969  42  SER C CA  
4612 C  C   A SER C 42  ? 0.2223 0.4975 0.2117 0.0682  -0.0261 0.0008  42  SER C C   
4613 C  C   B SER C 42  ? 0.2556 0.4843 0.2554 0.0395  -0.0111 0.0659  42  SER C C   
4614 O  O   A SER C 42  ? 0.2685 0.2199 0.2004 0.1400  -0.0256 -0.0001 42  SER C O   
4615 O  O   B SER C 42  ? 0.3001 0.4077 0.2780 0.0877  0.0328  0.0054  42  SER C O   
4616 C  CB  A SER C 42  ? 0.2793 0.2009 0.2112 0.0234  0.0337  0.0919  42  SER C CB  
4617 C  CB  B SER C 42  ? 0.4467 0.2242 0.3480 0.0373  0.0442  0.0787  42  SER C CB  
4618 O  OG  A SER C 42  ? 0.3136 0.1300 0.3386 0.0703  0.0938  0.1265  42  SER C OG  
4619 O  OG  B SER C 42  ? 0.3541 0.3897 0.3651 -0.0006 0.1335  0.0634  42  SER C OG  
4620 N  N   A LEU C 43  ? 0.1790 0.4796 0.2119 0.1502  0.0325  -0.0059 43  LEU C N   
4621 N  N   B LEU C 43  ? 0.2483 0.5350 0.2667 0.0894  0.0433  0.0055  43  LEU C N   
4622 C  CA  A LEU C 43  ? 0.1595 0.3915 0.2207 0.1052  0.0055  0.0434  43  LEU C CA  
4623 C  CA  B LEU C 43  ? 0.1596 0.4119 0.2623 0.0970  0.0128  0.0515  43  LEU C CA  
4624 C  C   A LEU C 43  ? 0.1550 0.2744 0.2789 0.0900  -0.0049 -0.0279 43  LEU C C   
4625 C  C   B LEU C 43  ? 0.1531 0.2746 0.2786 0.0856  -0.0100 -0.0351 43  LEU C C   
4626 O  O   A LEU C 43  ? 0.1983 0.3725 0.3552 0.0516  0.0425  0.0462  43  LEU C O   
4627 O  O   B LEU C 43  ? 0.1991 0.3715 0.3586 0.0506  0.0418  0.0478  43  LEU C O   
4628 C  CB  A LEU C 43  ? 0.1500 0.3021 0.2558 0.0812  0.0091  0.0052  43  LEU C CB  
4629 C  CB  B LEU C 43  ? 0.1507 0.3063 0.2620 0.0784  0.0091  0.0093  43  LEU C CB  
4630 C  CG  A LEU C 43  ? 0.1362 0.2302 0.2485 0.0420  -0.0126 -0.0215 43  LEU C CG  
4631 C  CG  B LEU C 43  ? 0.1398 0.2344 0.2490 0.0424  -0.0103 -0.0203 43  LEU C CG  
4632 C  CD1 A LEU C 43  ? 0.1453 0.2533 0.2919 0.0783  0.0086  0.0247  43  LEU C CD1 
4633 C  CD1 B LEU C 43  ? 0.1489 0.2504 0.2926 0.0713  0.0099  0.0233  43  LEU C CD1 
4634 C  CD2 A LEU C 43  ? 0.1866 0.2635 0.2873 0.0002  0.0083  0.0206  43  LEU C CD2 
4635 C  CD2 B LEU C 43  ? 0.1855 0.2716 0.2897 0.0006  0.0087  0.0243  43  LEU C CD2 
4636 N  N   . THR C 44  ? 0.1765 0.3452 0.2383 0.0425  0.0217  0.0140  44  THR C N   
4637 C  CA  . THR C 44  ? 0.2444 0.2926 0.2153 0.1262  0.0673  -0.0220 44  THR C CA  
4638 C  C   . THR C 44  ? 0.1907 0.3103 0.2101 0.1236  0.0314  -0.0216 44  THR C C   
4639 O  O   . THR C 44  ? 0.2065 0.2610 0.2673 0.1096  0.0353  -0.0042 44  THR C O   
4640 C  CB  . THR C 44  ? 0.2067 0.3560 0.2514 0.0895  0.0475  0.0145  44  THR C CB  
4641 O  OG1 . THR C 44  ? 0.2606 0.3609 0.4057 0.0759  0.0491  0.0290  44  THR C OG1 
4642 C  CG2 . THR C 44  ? 0.2284 0.3560 0.2502 0.1042  0.0564  0.0053  44  THR C CG2 
4643 N  N   . PRO C 45  ? 0.2271 0.2875 0.2583 0.0840  0.0098  0.0058  45  PRO C N   
4644 C  CA  . PRO C 45  ? 0.1983 0.3339 0.2378 0.0974  0.0355  0.0069  45  PRO C CA  
4645 C  C   . PRO C 45  ? 0.2881 0.3132 0.2669 0.0939  0.0272  0.0351  45  PRO C C   
4646 O  O   . PRO C 45  ? 0.3213 0.3970 0.2514 0.0891  0.0595  -0.0249 45  PRO C O   
4647 C  CB  . PRO C 45  ? 0.2846 0.3534 0.2796 0.1680  0.0185  -0.0512 45  PRO C CB  
4648 C  CG  . PRO C 45  ? 0.2139 0.2554 0.2588 0.0800  -0.0136 -0.0069 45  PRO C CG  
4649 C  CD  . PRO C 45  ? 0.2671 0.2962 0.2365 0.1084  0.0158  -0.0174 45  PRO C CD  
4650 N  N   . LEU C 46  ? 0.2304 0.3167 0.2004 0.0594  0.0003  0.0296  46  LEU C N   
4651 C  CA  . LEU C 46  ? 0.2440 0.2108 0.2709 0.0879  0.0109  0.0719  46  LEU C CA  
4652 C  C   . LEU C 46  ? 0.2430 0.3265 0.1995 0.0324  0.0145  0.0932  46  LEU C C   
4653 O  O   . LEU C 46  ? 0.2734 0.2833 0.3080 0.0643  0.0009  0.1198  46  LEU C O   
4654 C  CB  . LEU C 46  ? 0.1916 0.2340 0.2340 0.0271  -0.0197 0.0139  46  LEU C CB  
4655 C  CG  . LEU C 46  ? 0.1913 0.2109 0.3371 0.0772  0.0035  0.0425  46  LEU C CG  
4656 C  CD1 . LEU C 46  ? 0.2134 0.1791 0.3334 0.0302  -0.0583 -0.0692 46  LEU C CD1 
4657 C  CD2 . LEU C 46  ? 0.2590 0.2430 0.3554 0.0432  -0.0281 0.0829  46  LEU C CD2 
4658 N  N   . GLU C 47  ? 0.1852 0.3154 0.2512 0.0672  -0.0010 0.0134  47  GLU C N   
4659 C  CA  . GLU C 47  ? 0.1692 0.3277 0.3476 0.0243  -0.0453 0.0339  47  GLU C CA  
4660 C  C   . GLU C 47  ? 0.1390 0.2186 0.2809 0.0366  -0.0231 0.0910  47  GLU C C   
4661 O  O   . GLU C 47  ? 0.2561 0.2576 0.2865 0.0547  -0.0196 0.1543  47  GLU C O   
4662 C  CB  . GLU C 47  ? 0.2289 0.4822 0.3983 0.0658  -0.0030 -0.0571 47  GLU C CB  
4663 C  CG  . GLU C 47  ? 0.2982 0.5181 0.5827 0.0352  -0.0369 -0.1298 47  GLU C CG  
4664 N  N   . PHE C 48  ? 0.1354 0.3279 0.3134 -0.0403 -0.0507 0.1360  48  PHE C N   
4665 C  CA  . PHE C 48  ? 0.1676 0.2834 0.2896 0.0096  -0.0403 0.1619  48  PHE C CA  
4666 C  C   . PHE C 48  ? 0.1724 0.3319 0.2744 -0.0080 -0.0401 0.1218  48  PHE C C   
4667 O  O   . PHE C 48  ? 0.1683 0.4030 0.4762 0.0401  -0.0752 0.1846  48  PHE C O   
4668 C  CB  . PHE C 48  ? 0.2126 0.2651 0.3024 -0.0807 -0.0650 0.1518  48  PHE C CB  
4669 C  CG  . PHE C 48  ? 0.1708 0.2629 0.3057 -0.0030 -0.0493 0.0828  48  PHE C CG  
4670 C  CD1 . PHE C 48  ? 0.1419 0.3153 0.2803 0.0252  -0.0274 0.0425  48  PHE C CD1 
4671 C  CD2 . PHE C 48  ? 0.2028 0.2521 0.2584 -0.0221 -0.0209 0.1291  48  PHE C CD2 
4672 C  CE1 . PHE C 48  ? 0.1657 0.4159 0.2270 0.0329  -0.0280 0.0298  48  PHE C CE1 
4673 C  CE2 . PHE C 48  ? 0.1819 0.3701 0.2525 -0.0219 0.0086  0.0741  48  PHE C CE2 
4674 C  CZ  . PHE C 48  ? 0.1830 0.3715 0.3046 0.0219  0.0486  0.0422  48  PHE C CZ  
4675 N  N   . GLN C 49  ? 0.1611 0.3086 0.3003 0.0497  -0.0507 0.1486  49  GLN C N   
4676 C  CA  . GLN C 49  ? 0.1654 0.3188 0.3001 0.0525  -0.0186 0.0687  49  GLN C CA  
4677 C  C   . GLN C 49  ? 0.1532 0.3238 0.2063 0.0219  -0.0317 0.1138  49  GLN C C   
4678 O  O   . GLN C 49  ? 0.1277 0.3613 0.2986 0.0148  -0.0359 0.1544  49  GLN C O   
4679 C  CB  . GLN C 49  ? 0.2477 0.4176 0.2408 0.0878  0.0125  0.0597  49  GLN C CB  
4680 C  CG  . GLN C 49  ? 0.3094 0.5177 0.3111 0.0082  0.0542  -0.0166 49  GLN C CG  
4681 C  CD  . GLN C 49  ? 0.5357 0.5452 0.4496 0.1368  -0.1210 0.0092  49  GLN C CD  
4682 O  OE1 . GLN C 49  ? 0.5615 0.8975 0.5184 0.2688  0.0917  -0.0783 49  GLN C OE1 
4683 N  NE2 . GLN C 49  ? 0.6347 0.4275 0.3893 0.2445  -0.0326 0.0872  49  GLN C NE2 
4684 N  N   . GLY C 50  ? 0.1076 0.4707 0.2656 0.0406  -0.0342 0.1273  50  GLY C N   
4685 C  CA  . GLY C 50  ? 0.1397 0.4546 0.2597 0.0005  -0.0678 0.1374  50  GLY C CA  
4686 C  C   . GLY C 50  ? 0.1855 0.5125 0.2539 -0.0065 -0.0476 0.0657  50  GLY C C   
4687 O  O   . GLY C 50  ? 0.1697 0.4533 0.2570 0.0444  -0.0420 0.0626  50  GLY C O   
4688 N  N   . TYR C 51  ? 0.1557 0.4426 0.3213 0.0357  0.0017  0.1923  51  TYR C N   
4689 C  CA  . TYR C 51  ? 0.1607 0.4436 0.2480 -0.0021 -0.0295 0.1306  51  TYR C CA  
4690 C  C   . TYR C 51  ? 0.1805 0.4284 0.2878 -0.0255 -0.0410 0.1631  51  TYR C C   
4691 O  O   . TYR C 51  ? 0.1487 0.5673 0.2791 0.0238  -0.0377 0.1656  51  TYR C O   
4692 C  CB  . TYR C 51  ? 0.1326 0.3632 0.2779 0.0107  -0.0607 0.1507  51  TYR C CB  
4693 C  CG  . TYR C 51  ? 0.1288 0.3535 0.2469 -0.0303 -0.1040 0.1237  51  TYR C CG  
4694 C  CD1 . TYR C 51  ? 0.1934 0.3440 0.2392 0.0147  -0.0634 0.1253  51  TYR C CD1 
4695 C  CD2 . TYR C 51  ? 0.1261 0.3751 0.2227 -0.0026 -0.0635 0.0732  51  TYR C CD2 
4696 C  CE1 . TYR C 51  ? 0.1022 0.2773 0.3109 0.0351  -0.0256 0.0834  51  TYR C CE1 
4697 C  CE2 . TYR C 51  ? 0.1111 0.3345 0.2156 -0.0184 -0.0383 0.0996  51  TYR C CE2 
4698 C  CZ  . TYR C 51  ? 0.1003 0.3486 0.1947 0.0049  -0.0542 0.0958  51  TYR C CZ  
4699 O  OH  . TYR C 51  ? 0.1094 0.3201 0.2478 -0.0091 -0.0516 0.1338  51  TYR C OH  
4700 N  N   . ASN C 52  ? 0.1970 0.4738 0.2920 0.0155  -0.0722 0.1693  52  ASN C N   
4701 C  CA  . ASN C 52  ? 0.2670 0.5677 0.2798 0.0413  -0.0779 0.1632  52  ASN C CA  
4702 C  C   . ASN C 52  ? 0.2364 0.7528 0.2419 0.0089  -0.0751 0.0652  52  ASN C C   
4703 O  O   . ASN C 52  ? 0.2281 0.7425 0.3368 0.0078  -0.0577 0.0927  52  ASN C O   
4704 C  CB  . ASN C 52  ? 0.2658 0.5118 0.2660 0.0107  -0.1060 0.1470  52  ASN C CB  
4705 C  CG  . ASN C 52  ? 0.3782 0.4515 0.3474 0.1169  -0.0040 0.2037  52  ASN C CG  
4706 O  OD1 . ASN C 52  ? 0.2761 0.7182 0.2886 0.0331  -0.0377 0.1903  52  ASN C OD1 
4707 N  ND2 . ASN C 52  ? 0.6023 0.5468 0.4717 0.2524  -0.0363 0.2056  52  ASN C ND2 
4708 N  N   . LEU C 53  ? 0.2637 0.5633 0.2435 0.0538  -0.0741 0.1270  53  LEU C N   
4709 C  CA  . LEU C 53  ? 0.2500 0.6591 0.4102 -0.0242 -0.0949 0.0839  53  LEU C CA  
4710 C  C   . LEU C 53  ? 0.1742 0.5602 0.5051 0.0411  -0.1113 0.0291  53  LEU C C   
4711 O  O   . LEU C 53  ? 0.3393 0.5528 0.3262 0.0753  -0.1753 -0.0290 53  LEU C O   
4712 C  CB  . LEU C 53  ? 0.2390 0.6450 0.2673 -0.0103 -0.0913 0.1123  53  LEU C CB  
4713 C  CG  . LEU C 53  ? 0.2973 0.4746 0.2721 -0.0351 -0.0588 0.1790  53  LEU C CG  
4714 C  CD1 . LEU C 53  ? 0.2231 0.3962 0.3389 -0.0069 -0.1357 0.1083  53  LEU C CD1 
4715 C  CD2 . LEU C 53  ? 0.4013 0.3262 0.3136 -0.0714 -0.0620 0.1641  53  LEU C CD2 
4716 N  N   . SER C 54  ? 0.2288 0.6563 0.4497 -0.0292 -0.0968 -0.1500 54  SER C N   
4717 C  CA  . SER C 54  ? 0.3210 0.5719 0.3253 -0.1083 -0.0943 -0.1236 54  SER C CA  
4718 C  C   . SER C 54  ? 0.4157 0.4704 0.2056 0.0663  -0.1656 0.0350  54  SER C C   
4719 O  O   . SER C 54  ? 0.2017 0.5486 0.7189 0.0162  -0.1487 -0.1474 54  SER C O   
4720 C  CB  . SER C 54  ? 0.1888 0.7785 0.3376 -0.1277 0.0292  -0.1513 54  SER C CB  
4721 O  OG  . SER C 54  ? 0.3177 0.5278 0.5055 0.0664  -0.1278 -0.2078 54  SER C OG  
4722 N  N   . ALA C 55  ? 0.3538 0.2811 0.4306 0.1173  -0.1259 -0.0201 55  ALA C N   
4723 C  CA  . ALA C 55  ? 0.6118 0.4530 0.4757 -0.0958 -0.0616 0.0472  55  ALA C CA  
4724 C  C   . ALA C 55  ? 0.7118 0.2647 0.7183 -0.0359 -0.1131 0.0544  55  ALA C C   
4725 O  O   . ALA C 55  ? 0.5813 0.7093 0.4903 -0.0480 -0.3750 0.1808  55  ALA C O   
4726 C  CB  . ALA C 55  ? 0.5218 0.2952 0.7027 -0.2033 -0.0798 -0.0059 55  ALA C CB  
4727 N  N   . ASN C 56  ? 0.5107 0.2482 0.9160 -0.0136 -0.2635 0.0726  56  ASN C N   
4728 C  CA  . ASN C 56  ? 0.7024 0.3767 0.6885 -0.0541 -0.1461 0.0435  56  ASN C CA  
4729 C  C   . ASN C 56  ? 0.4133 0.4550 0.4028 -0.2130 -0.1414 0.1191  56  ASN C C   
4730 O  O   . ASN C 56  ? 0.3260 0.4091 0.5452 -0.0829 -0.1829 0.0424  56  ASN C O   
4731 C  CB  . ASN C 56  ? 0.6251 0.7991 0.9370 -0.1216 -0.0211 0.1703  56  ASN C CB  
4732 C  CG  . ASN C 56  ? 1.0628 0.9624 0.7695 -0.2864 0.1685  0.0731  56  ASN C CG  
4733 O  OD1 . ASN C 56  ? 0.6812 0.7372 0.7260 -0.3222 -0.0952 0.0673  56  ASN C OD1 
4734 N  ND2 . ASN C 56  ? 0.4332 0.3765 1.3897 0.0985  -0.1047 0.2694  56  ASN C ND2 
4735 N  N   . LYS C 57  ? 0.3782 0.5522 0.3098 0.1050  -0.0827 -0.1197 57  LYS C N   
4736 C  CA  . LYS C 57  ? 0.2634 0.6366 0.3594 0.0771  -0.0715 -0.0339 57  LYS C CA  
4737 C  C   . LYS C 57  ? 0.3604 0.6044 0.4275 -0.0298 0.0621  0.0378  57  LYS C C   
4738 O  O   . LYS C 57  ? 0.1772 0.5945 0.3524 -0.0060 -0.1015 0.0593  57  LYS C O   
4739 C  CB  . LYS C 57  ? 0.1830 0.7334 0.3632 0.1789  -0.0407 -0.0672 57  LYS C CB  
4740 C  CG  . LYS C 57  ? 0.2674 0.8541 0.3667 0.1407  -0.0166 -0.0287 57  LYS C CG  
4741 C  CD  . LYS C 57  ? 0.3305 0.8936 0.3536 0.1442  0.0375  0.0372  57  LYS C CD  
4742 N  N   . GLN C 58  ? 0.2410 0.4994 0.2867 -0.1087 -0.0950 0.0976  58  GLN C N   
4743 C  CA  . GLN C 58  ? 0.3091 0.4942 0.2728 -0.0181 -0.0131 0.2019  58  GLN C CA  
4744 C  C   . GLN C 58  ? 0.2339 0.4113 0.3379 -0.0377 -0.0606 0.1246  58  GLN C C   
4745 O  O   . GLN C 58  ? 0.2859 0.5199 0.3154 -0.1953 -0.1172 0.1091  58  GLN C O   
4746 C  CB  . GLN C 58  ? 0.2382 0.4708 0.2892 -0.0252 -0.0363 0.1738  58  GLN C CB  
4747 C  CG  . GLN C 58  ? 0.2451 0.4623 0.2929 0.0518  0.0253  0.1403  58  GLN C CG  
4748 C  CD  . GLN C 58  ? 0.2092 0.4421 0.2938 0.0637  0.0182  0.1005  58  GLN C CD  
4749 O  OE1 . GLN C 58  ? 0.3059 0.3210 0.4110 0.0491  -0.1015 0.0170  58  GLN C OE1 
4750 N  NE2 . GLN C 58  ? 0.2223 0.3872 0.3019 0.0272  -0.0516 0.0454  58  GLN C NE2 
4751 N  N   . PHE C 59  ? 0.2415 0.5497 0.1733 -0.0568 -0.0753 0.1013  59  PHE C N   
4752 C  CA  . PHE C 59  ? 0.2832 0.4771 0.1233 -0.0109 -0.0407 0.0462  59  PHE C CA  
4753 C  C   . PHE C 59  ? 0.2885 0.4681 0.2284 -0.0525 0.0129  -0.0242 59  PHE C C   
4754 O  O   . PHE C 59  ? 0.2070 0.4990 0.2810 -0.0621 -0.0732 0.0647  59  PHE C O   
4755 C  CB  . PHE C 59  ? 0.2689 0.3371 0.1940 -0.0867 -0.0569 0.0877  59  PHE C CB  
4756 C  CG  . PHE C 59  ? 0.1952 0.4063 0.3229 -0.1202 -0.0262 0.0660  59  PHE C CG  
4757 C  CD1 . PHE C 59  ? 0.2563 0.4137 0.3102 -0.0108 -0.0234 0.1232  59  PHE C CD1 
4758 C  CD2 . PHE C 59  ? 0.2200 0.4903 0.2842 -0.0861 -0.0466 0.0823  59  PHE C CD2 
4759 C  CE1 . PHE C 59  ? 0.2054 0.4873 0.3021 -0.0378 -0.0690 0.0757  59  PHE C CE1 
4760 C  CE2 . PHE C 59  ? 0.1496 0.6219 0.3502 -0.1056 -0.0701 0.1142  59  PHE C CE2 
4761 C  CZ  . PHE C 59  ? 0.2583 0.5661 0.3856 -0.0359 -0.0965 0.2060  59  PHE C CZ  
4762 N  N   . LEU C 60  ? 0.2245 0.4873 0.2210 -0.0938 -0.0543 -0.0581 60  LEU C N   
4763 C  CA  . LEU C 60  ? 0.1912 0.5638 0.1609 -0.0701 -0.0464 -0.0596 60  LEU C CA  
4764 C  C   . LEU C 60  ? 0.1819 0.3475 0.2196 -0.0011 -0.0889 -0.0179 60  LEU C C   
4765 O  O   . LEU C 60  ? 0.2266 0.5807 0.1793 -0.0520 -0.0721 -0.0509 60  LEU C O   
4766 C  CB  . LEU C 60  ? 0.2410 0.6174 0.3098 -0.0970 -0.0171 -0.0223 60  LEU C CB  
4767 C  CG  . LEU C 60  ? 0.2160 0.6138 0.3462 -0.1377 -0.0108 -0.0636 60  LEU C CG  
4768 C  CD1 . LEU C 60  ? 0.3358 0.6123 0.3613 -0.2499 -0.0552 -0.1553 60  LEU C CD1 
4769 C  CD2 . LEU C 60  ? 0.5220 0.6190 0.3333 -0.2971 0.0159  -0.1256 60  LEU C CD2 
4770 N  N   . LEU C 61  ? 0.2489 0.5543 0.2182 -0.0907 -0.0930 0.0054  61  LEU C N   
4771 C  CA  . LEU C 61  ? 0.2654 0.5508 0.1791 -0.1515 -0.0495 -0.0549 61  LEU C CA  
4772 C  C   . LEU C 61  ? 0.3350 0.5870 0.2500 -0.1125 -0.0441 -0.1337 61  LEU C C   
4773 O  O   . LEU C 61  ? 0.4008 0.8327 0.1887 -0.0233 -0.0772 -0.1560 61  LEU C O   
4774 C  CB  . LEU C 61  ? 0.2314 0.6412 0.3228 -0.2345 -0.0375 0.0629  61  LEU C CB  
4775 C  CG  . LEU C 61  ? 0.5356 0.5916 0.1769 -0.2578 -0.1124 0.1005  61  LEU C CG  
4776 C  CD1 . LEU C 61  ? 0.3937 0.6439 0.3200 -0.0729 -0.0074 0.1956  61  LEU C CD1 
4777 C  CD2 . LEU C 61  ? 0.1956 0.5991 0.3709 -0.0463 -0.0989 0.1153  61  LEU C CD2 
4778 N  N   . THR C 62  ? 0.3959 0.6503 0.2064 -0.1113 -0.0506 -0.0325 62  THR C N   
4779 C  CA  . THR C 62  ? 0.2962 0.5949 0.1944 -0.1781 -0.0700 -0.0719 62  THR C CA  
4780 C  C   . THR C 62  ? 0.2428 0.7349 0.2066 0.0011  -0.0617 -0.0725 62  THR C C   
4781 O  O   . THR C 62  ? 0.4236 0.7650 0.1412 -0.1520 -0.0535 -0.0254 62  THR C O   
4782 C  CB  . THR C 62  ? 0.4353 0.6659 0.3955 -0.1018 0.0270  0.0292  62  THR C CB  
4783 O  OG1 . THR C 62  ? 0.4937 0.8875 0.2527 -0.1535 -0.0737 -0.0642 62  THR C OG1 
4784 C  CG2 . THR C 62  ? 0.5668 0.5317 0.4250 -0.1849 -0.0077 0.2158  62  THR C CG2 
4785 N  N   . ASN C 63  ? 0.2808 0.5151 0.2676 -0.0480 -0.0586 -0.1307 63  ASN C N   
4786 C  CA  . ASN C 63  ? 0.2830 0.5651 0.1974 0.0602  0.0321  -0.0892 63  ASN C CA  
4787 C  C   . ASN C 63  ? 0.4542 0.3854 0.3001 -0.2304 -0.0336 -0.1662 63  ASN C C   
4788 O  O   . ASN C 63  ? 0.4673 0.4204 0.4024 -0.2696 0.0344  -0.2208 63  ASN C O   
4789 C  CB  . ASN C 63  ? 0.3085 0.4699 0.1755 -0.1182 -0.0060 -0.0806 63  ASN C CB  
4790 C  CG  . ASN C 63  ? 0.3674 0.2769 0.2144 -0.0397 -0.0053 -0.0963 63  ASN C CG  
4791 O  OD1 . ASN C 63  ? 0.4642 0.3730 0.2336 -0.1379 -0.0362 0.0334  63  ASN C OD1 
4792 N  ND2 . ASN C 63  ? 0.4166 0.5044 0.2145 -0.1844 -0.0432 -0.0838 63  ASN C ND2 
4793 N  N   . ASN C 64  ? 0.4600 0.4151 0.2241 -0.1790 0.0309  -0.0709 64  ASN C N   
4794 C  CA  . ASN C 64  ? 0.4556 0.5602 0.2879 -0.0352 0.0392  0.0285  64  ASN C CA  
4795 C  C   . ASN C 64  ? 0.4120 0.4914 0.3227 -0.0863 0.0325  -0.0747 64  ASN C C   
4796 O  O   . ASN C 64  ? 0.6751 0.3092 0.4815 -0.2111 -0.1383 -0.0784 64  ASN C O   
4797 C  CB  . ASN C 64  ? 0.5055 0.2507 0.2726 -0.1537 0.0736  -0.0901 64  ASN C CB  
4798 C  CG  . ASN C 64  ? 0.3898 0.3931 0.2830 -0.1615 -0.0342 -0.0557 64  ASN C CG  
4799 O  OD1 . ASN C 64  ? 0.4026 0.4032 0.2177 -0.1392 0.0144  -0.0258 64  ASN C OD1 
4800 N  ND2 . ASN C 64  ? 0.4521 0.4347 0.2821 -0.0982 -0.0190 -0.0286 64  ASN C ND2 
4801 N  N   . GLY C 65  ? 0.4987 0.4461 0.2265 -0.1795 -0.0881 -0.0337 65  GLY C N   
4802 C  CA  . GLY C 65  ? 0.5642 0.3053 0.2249 -0.1015 -0.0311 -0.0680 65  GLY C CA  
4803 C  C   . GLY C 65  ? 0.3996 0.4728 0.2430 -0.1082 -0.0304 -0.0223 65  GLY C C   
4804 O  O   . GLY C 65  ? 0.3812 0.5796 0.2842 -0.0136 -0.0328 -0.1216 65  GLY C O   
4805 N  N   . HIS C 66  ? 0.4041 0.3326 0.3118 -0.1502 -0.0240 -0.0873 66  HIS C N   
4806 C  CA  . HIS C 66  ? 0.4640 0.2432 0.3093 -0.0585 -0.1035 -0.0452 66  HIS C CA  
4807 C  C   . HIS C 66  ? 0.2752 0.2078 0.2849 -0.0861 -0.0152 0.0372  66  HIS C C   
4808 O  O   . HIS C 66  ? 0.2879 0.2951 0.3322 -0.1069 -0.0725 0.0447  66  HIS C O   
4809 C  CB  . HIS C 66  ? 0.5485 0.2349 0.2913 -0.0917 -0.0293 -0.1091 66  HIS C CB  
4810 C  CG  . HIS C 66  ? 0.4425 0.2394 0.2403 -0.1129 -0.0141 -0.0779 66  HIS C CG  
4811 N  ND1 . HIS C 66  ? 0.4727 0.2489 0.3696 -0.1663 -0.1680 0.0427  66  HIS C ND1 
4812 C  CD2 . HIS C 66  ? 0.4457 0.3984 0.2442 -0.0140 -0.1234 0.0332  66  HIS C CD2 
4813 C  CE1 . HIS C 66  ? 0.4145 0.4092 0.4014 -0.0441 -0.0502 0.0265  66  HIS C CE1 
4814 N  NE2 . HIS C 66  ? 0.3796 0.4106 0.2449 -0.0558 -0.0770 0.0425  66  HIS C NE2 
4815 N  N   . SER C 67  ? 0.2881 0.3437 0.2764 -0.0954 -0.0418 -0.0458 67  SER C N   
4816 C  CA  . SER C 67  ? 0.2912 0.3173 0.1955 -0.0881 -0.0424 -0.0914 67  SER C CA  
4817 C  C   . SER C 67  ? 0.2913 0.2896 0.1969 -0.1014 -0.0290 -0.0524 67  SER C C   
4818 O  O   . SER C 67  ? 0.4583 0.3222 0.3098 -0.1949 -0.1548 -0.0443 67  SER C O   
4819 C  CB  . SER C 67  ? 0.3868 0.3675 0.2156 0.0190  -0.0747 -0.1324 67  SER C CB  
4820 O  OG  . SER C 67  ? 0.3220 0.3443 0.2517 -0.0234 -0.0768 -0.0561 67  SER C OG  
4821 N  N   . VAL C 68  ? 0.2627 0.3995 0.2249 -0.0211 -0.1130 0.0282  68  VAL C N   
4822 C  CA  . VAL C 68  ? 0.2112 0.5193 0.2076 -0.0195 -0.0563 0.0214  68  VAL C CA  
4823 C  C   . VAL C 68  ? 0.3166 0.4332 0.1848 -0.0787 -0.0125 0.0166  68  VAL C C   
4824 O  O   . VAL C 68  ? 0.1976 0.4317 0.2325 -0.1205 -0.0542 0.0072  68  VAL C O   
4825 C  CB  . VAL C 68  ? 0.3517 0.4911 0.1909 -0.1305 -0.0961 0.0034  68  VAL C CB  
4826 C  CG1 . VAL C 68  ? 0.2182 0.4408 0.3153 -0.0244 -0.0629 -0.1298 68  VAL C CG1 
4827 C  CG2 . VAL C 68  ? 0.3188 0.6623 0.2694 -0.1595 -0.0924 -0.0790 68  VAL C CG2 
4828 N  N   . LYS C 69  ? 0.2279 0.5809 0.1692 -0.0753 -0.0627 -0.0094 69  LYS C N   
4829 C  CA  . LYS C 69  ? 0.1897 0.4377 0.2013 -0.0664 -0.0483 0.0098  69  LYS C CA  
4830 C  C   . LYS C 69  ? 0.1631 0.3642 0.1883 -0.0983 -0.0158 -0.0346 69  LYS C C   
4831 O  O   . LYS C 69  ? 0.3269 0.5898 0.1694 -0.1591 -0.1237 0.0043  69  LYS C O   
4832 C  CB  . LYS C 69  ? 0.4039 0.4204 0.2074 -0.0955 -0.0738 -0.0359 69  LYS C CB  
4833 C  CG  . LYS C 69  ? 0.3897 0.4745 0.3364 -0.1247 -0.1905 0.0016  69  LYS C CG  
4834 C  CD  . LYS C 69  ? 0.6090 0.5140 0.2954 -0.0225 -0.1208 0.0125  69  LYS C CD  
4835 C  CE  . LYS C 69  ? 0.5662 0.5448 0.3976 -0.0611 -0.0774 -0.0791 69  LYS C CE  
4836 N  NZ  . LYS C 69  ? 0.8180 0.6129 0.4434 -0.3249 -0.2314 -0.0595 69  LYS C NZ  
4837 N  N   . LEU C 70  ? 0.1851 0.4571 0.1595 -0.0651 -0.0277 -0.0198 70  LEU C N   
4838 C  CA  . LEU C 70  ? 0.1754 0.4755 0.1408 -0.0825 -0.0741 -0.0296 70  LEU C CA  
4839 C  C   . LEU C 70  ? 0.2696 0.4166 0.2103 -0.1553 -0.0097 -0.0263 70  LEU C C   
4840 O  O   . LEU C 70  ? 0.1671 0.4881 0.1839 -0.1351 -0.0504 0.0390  70  LEU C O   
4841 C  CB  . LEU C 70  ? 0.1951 0.4858 0.1909 -0.0111 -0.0488 0.0303  70  LEU C CB  
4842 C  CG  . LEU C 70  ? 0.1961 0.4670 0.1955 -0.0006 -0.0754 -0.0431 70  LEU C CG  
4843 C  CD1 . LEU C 70  ? 0.2605 0.5841 0.1545 -0.0493 -0.1000 0.0252  70  LEU C CD1 
4844 C  CD2 . LEU C 70  ? 0.2361 0.4906 0.2368 -0.0117 -0.0541 0.0368  70  LEU C CD2 
4845 N  N   . ASN C 71  ? 0.2367 0.4509 0.1949 -0.1302 -0.0675 0.0047  71  ASN C N   
4846 C  CA  . ASN C 71  ? 0.1919 0.3733 0.2353 -0.1479 -0.0768 -0.0257 71  ASN C CA  
4847 C  C   . ASN C 71  ? 0.2038 0.4327 0.2173 -0.1015 -0.0787 0.0211  71  ASN C C   
4848 O  O   . ASN C 71  ? 0.2322 0.4394 0.1832 -0.0054 -0.0487 -0.0013 71  ASN C O   
4849 C  CB  . ASN C 71  ? 0.3054 0.3182 0.2264 -0.1751 -0.1105 0.0562  71  ASN C CB  
4850 C  CG  . ASN C 71  ? 0.3146 0.3866 0.3037 -0.1775 -0.0979 0.0253  71  ASN C CG  
4851 O  OD1 . ASN C 71  ? 0.3471 0.6755 0.3137 -0.2207 -0.1008 0.0879  71  ASN C OD1 
4852 N  ND2 . ASN C 71  ? 0.5804 0.4781 0.3846 -0.3441 -0.0868 0.0378  71  ASN C ND2 
4853 N  N   . LEU C 72  ? 0.1708 0.3323 0.2038 -0.0885 -0.0675 -0.0067 72  LEU C N   
4854 C  CA  . LEU C 72  ? 0.1920 0.3862 0.2139 -0.0675 -0.0595 0.0458  72  LEU C CA  
4855 C  C   . LEU C 72  ? 0.1954 0.3310 0.2017 -0.0891 -0.1122 0.0960  72  LEU C C   
4856 O  O   . LEU C 72  ? 0.2293 0.3270 0.2406 -0.0965 -0.0701 0.0854  72  LEU C O   
4857 C  CB  . LEU C 72  ? 0.1525 0.2361 0.2378 -0.0457 -0.0538 0.0615  72  LEU C CB  
4858 C  CG  . LEU C 72  ? 0.1733 0.3160 0.1620 -0.0706 -0.0760 0.0669  72  LEU C CG  
4859 C  CD1 . LEU C 72  ? 0.1115 0.3190 0.2112 -0.0345 -0.0752 0.0257  72  LEU C CD1 
4860 C  CD2 . LEU C 72  ? 0.1548 0.3262 0.2109 -0.0109 -0.0380 0.0771  72  LEU C CD2 
4861 N  N   . PRO C 73  ? 0.2103 0.3820 0.2864 -0.1101 -0.0575 0.0897  73  PRO C N   
4862 C  CA  . PRO C 73  ? 0.1833 0.4101 0.3018 -0.0833 -0.0523 0.1117  73  PRO C CA  
4863 C  C   . PRO C 73  ? 0.1703 0.4279 0.3001 -0.0917 -0.1015 0.1206  73  PRO C C   
4864 O  O   . PRO C 73  ? 0.1538 0.4690 0.2508 -0.0461 -0.0469 0.0504  73  PRO C O   
4865 C  CB  . PRO C 73  ? 0.1873 0.3804 0.3368 -0.1026 -0.0770 0.1259  73  PRO C CB  
4866 C  CG  . PRO C 73  ? 0.1635 0.3867 0.3190 -0.1312 -0.0996 0.1478  73  PRO C CG  
4867 C  CD  . PRO C 73  ? 0.2310 0.3833 0.2860 -0.0337 -0.0373 0.0561  73  PRO C CD  
4868 N  N   . SER C 74  ? 0.2065 0.4723 0.3190 -0.0884 -0.0421 0.1143  74  SER C N   
4869 C  CA  . SER C 74  ? 0.2217 0.4676 0.3147 -0.1270 -0.0222 0.1313  74  SER C CA  
4870 C  C   . SER C 74  ? 0.1744 0.6027 0.2867 -0.0603 -0.0278 0.1470  74  SER C C   
4871 O  O   . SER C 74  ? 0.2110 0.6948 0.2949 -0.0710 -0.0752 0.1311  74  SER C O   
4872 C  CB  . SER C 74  ? 0.3184 0.5475 0.2934 -0.1843 -0.0189 0.1620  74  SER C CB  
4873 O  OG  . SER C 74  ? 0.2676 0.6423 0.3743 -0.1442 -0.0285 0.1215  74  SER C OG  
4874 N  N   . ASP C 75  ? 0.2041 0.5686 0.3109 -0.0629 -0.0846 0.1400  75  ASP C N   
4875 C  CA  . ASP C 75  ? 0.1995 0.5813 0.2902 -0.0373 -0.1133 0.0787  75  ASP C CA  
4876 C  C   . ASP C 75  ? 0.1938 0.4217 0.2495 0.0113  -0.0320 0.1685  75  ASP C C   
4877 O  O   . ASP C 75  ? 0.1349 0.6646 0.2557 -0.0134 -0.0449 0.0157  75  ASP C O   
4878 C  CB  . ASP C 75  ? 0.2566 0.6239 0.4379 0.0869  -0.1307 0.0982  75  ASP C CB  
4879 C  CG  . ASP C 75  ? 0.3219 0.6639 0.4299 0.0396  -0.1361 0.0728  75  ASP C CG  
4880 O  OD1 . ASP C 75  ? 0.3401 0.4824 0.4317 -0.1202 -0.0725 0.1072  75  ASP C OD1 
4881 O  OD2 . ASP C 75  ? 0.3131 0.6231 0.3374 -0.1362 0.0160  0.0370  75  ASP C OD2 
4882 N  N   . MET C 76  ? 0.1538 0.4808 0.2236 -0.0283 -0.0834 0.1015  76  MET C N   
4883 C  CA  . MET C 76  ? 0.1406 0.4686 0.1800 -0.0423 -0.0425 0.1342  76  MET C CA  
4884 C  C   . MET C 76  ? 0.1248 0.3882 0.1908 0.0163  -0.0436 0.0986  76  MET C C   
4885 O  O   . MET C 76  ? 0.1466 0.3762 0.2458 -0.0059 -0.0418 0.1355  76  MET C O   
4886 C  CB  . MET C 76  ? 0.1143 0.4436 0.2552 -0.0008 -0.0232 0.1138  76  MET C CB  
4887 C  CG  . MET C 76  ? 0.1101 0.4875 0.2750 -0.0329 -0.0291 0.0760  76  MET C CG  
4888 S  SD  . MET C 76  ? 0.1904 0.4276 0.2870 -0.0109 0.0204  0.1017  76  MET C SD  
4889 C  CE  . MET C 76  ? 0.2523 0.4010 0.2856 -0.1222 0.1141  0.0737  76  MET C CE  
4890 N  N   . HIS C 77  ? 0.1011 0.3623 0.1965 -0.0554 -0.0425 0.0845  77  HIS C N   
4891 C  CA  . HIS C 77  ? 0.1361 0.3097 0.1970 -0.0553 -0.0439 0.0982  77  HIS C CA  
4892 C  C   . HIS C 77  ? 0.1200 0.3177 0.2336 -0.0480 -0.0655 0.0957  77  HIS C C   
4893 O  O   . HIS C 77  ? 0.1017 0.3731 0.2315 0.0659  -0.0020 0.1351  77  HIS C O   
4894 C  CB  . HIS C 77  ? 0.1245 0.3445 0.2293 -0.0455 -0.0281 0.1144  77  HIS C CB  
4895 C  CG  . HIS C 77  ? 0.2044 0.3412 0.1812 0.0147  -0.0168 0.1355  77  HIS C CG  
4896 N  ND1 . HIS C 77  ? 0.2096 0.3926 0.2150 0.0278  -0.0301 0.1272  77  HIS C ND1 
4897 C  CD2 . HIS C 77  ? 0.1703 0.3068 0.2849 0.0071  -0.0392 0.0769  77  HIS C CD2 
4898 C  CE1 . HIS C 77  ? 0.1872 0.4254 0.2764 -0.0013 -0.0303 0.1276  77  HIS C CE1 
4899 N  NE2 . HIS C 77  ? 0.1848 0.3426 0.2956 0.0331  -0.0160 0.1041  77  HIS C NE2 
4900 N  N   . ILE C 78  ? 0.1090 0.3072 0.2274 -0.0151 -0.0520 0.0952  78  ILE C N   
4901 C  CA  . ILE C 78  ? 0.1074 0.3294 0.2067 -0.0099 -0.0194 0.0653  78  ILE C CA  
4902 C  C   . ILE C 78  ? 0.0800 0.3113 0.2549 0.0230  0.0130  0.1064  78  ILE C C   
4903 O  O   . ILE C 78  ? 0.1984 0.2910 0.2099 -0.0153 -0.0154 0.0842  78  ILE C O   
4904 C  CB  . ILE C 78  ? 0.1011 0.3256 0.1902 -0.0153 -0.0078 0.0268  78  ILE C CB  
4905 C  CG1 . ILE C 78  ? 0.1543 0.3771 0.2159 0.0301  0.0115  -0.0073 78  ILE C CG1 
4906 C  CG2 . ILE C 78  ? 0.2157 0.3653 0.2333 -0.0636 -0.0368 0.0197  78  ILE C CG2 
4907 C  CD1 . ILE C 78  ? 0.1949 0.2156 0.2465 0.0309  0.0201  0.0589  78  ILE C CD1 
4908 N  N   . GLN C 79  ? 0.1949 0.3795 0.2371 0.0776  0.0162  0.0644  79  GLN C N   
4909 C  CA  . GLN C 79  ? 0.1898 0.5127 0.2731 0.0555  -0.0098 -0.0057 79  GLN C CA  
4910 C  C   . GLN C 79  ? 0.1819 0.4397 0.2709 0.0602  0.0006  0.0315  79  GLN C C   
4911 O  O   . GLN C 79  ? 0.2931 0.3616 0.3182 0.1433  0.0399  0.1067  79  GLN C O   
4912 C  CB  . GLN C 79  ? 0.2339 0.6318 0.4800 0.1346  0.0142  0.0389  79  GLN C CB  
4913 C  CG  . GLN C 79  ? 0.2638 0.8212 0.5502 0.1668  0.0285  -0.0316 79  GLN C CG  
4914 C  CD  . GLN C 79  ? 0.3191 0.8692 0.8162 0.2100  0.0611  -0.0505 79  GLN C CD  
4915 O  OE1 . GLN C 79  ? 0.2811 1.2919 0.9541 -0.0201 -0.2067 -0.1327 79  GLN C OE1 
4916 N  NE2 . GLN C 79  ? 0.5500 0.8454 0.6972 0.4267  0.0788  -0.0003 79  GLN C NE2 
4917 N  N   . GLY C 80  ? 0.2261 0.3175 0.2727 0.0493  0.0410  0.0577  80  GLY C N   
4918 C  CA  . GLY C 80  ? 0.2067 0.4112 0.2886 -0.0212 0.0320  0.0661  80  GLY C CA  
4919 C  C   . GLY C 80  ? 0.2777 0.2969 0.1740 -0.0058 0.0441  0.0173  80  GLY C C   
4920 O  O   . GLY C 80  ? 0.2949 0.3203 0.2881 -0.0475 0.0013  -0.0290 80  GLY C O   
4921 N  N   . LEU C 81  ? 0.2081 0.2685 0.2570 -0.0556 0.0034  -0.0077 81  LEU C N   
4922 C  CA  . LEU C 81  ? 0.2754 0.2894 0.2421 -0.0182 0.0194  0.0281  81  LEU C CA  
4923 C  C   . LEU C 81  ? 0.2789 0.3412 0.2254 -0.0017 0.0316  0.0488  81  LEU C C   
4924 O  O   . LEU C 81  ? 0.2656 0.4249 0.2609 -0.0473 0.0523  0.0447  81  LEU C O   
4925 C  CB  . LEU C 81  ? 0.3089 0.2643 0.2142 0.0120  0.0201  0.0436  81  LEU C CB  
4926 C  CG  . LEU C 81  ? 0.2207 0.2342 0.3145 0.0188  0.0208  0.0542  81  LEU C CG  
4927 C  CD1 . LEU C 81  ? 0.2123 0.1987 0.2896 -0.0294 0.0341  0.0646  81  LEU C CD1 
4928 C  CD2 . LEU C 81  ? 0.2400 0.1913 0.2857 0.0196  0.0048  0.0187  81  LEU C CD2 
4929 N  N   . GLN C 82  ? 0.2272 0.3829 0.2346 -0.0269 -0.0172 0.0563  82  GLN C N   
4930 C  CA  . GLN C 82  ? 0.3744 0.4277 0.2096 -0.0238 0.0120  0.0531  82  GLN C CA  
4931 C  C   . GLN C 82  ? 0.3350 0.4433 0.2292 -0.0242 0.0196  0.0710  82  GLN C C   
4932 O  O   . GLN C 82  ? 0.3970 0.2979 0.2876 -0.1338 0.0037  0.0468  82  GLN C O   
4933 C  CB  . GLN C 82  ? 0.4875 0.3661 0.1884 -0.0157 -0.0389 0.0534  82  GLN C CB  
4934 C  CG  . GLN C 82  ? 0.5872 0.2651 0.3160 0.0553  -0.1071 0.0362  82  GLN C CG  
4935 C  CD  . GLN C 82  ? 0.8072 0.4352 0.3814 -0.0256 -0.0518 -0.0222 82  GLN C CD  
4936 O  OE1 . GLN C 82  ? 0.8666 0.5058 0.2569 -0.0675 -0.0717 0.0281  82  GLN C OE1 
4937 N  NE2 . GLN C 82  ? 0.9813 0.2030 0.4714 0.0440  -0.1998 0.1645  82  GLN C NE2 
4938 N  N   . SER C 83  ? 0.1859 0.2654 0.2400 0.0410  -0.0133 0.0361  83  SER C N   
4939 C  CA  . SER C 83  ? 0.1670 0.3169 0.2468 -0.0134 -0.0219 0.0848  83  SER C CA  
4940 C  C   . SER C 83  ? 0.1496 0.3429 0.1819 -0.0249 -0.0013 0.0107  83  SER C C   
4941 O  O   . SER C 83  ? 0.1480 0.3030 0.1947 -0.0197 -0.0214 0.0566  83  SER C O   
4942 C  CB  . SER C 83  ? 0.1764 0.2949 0.2056 -0.0312 -0.0350 0.0596  83  SER C CB  
4943 O  OG  . SER C 83  ? 0.3064 0.3905 0.2307 0.1045  -0.0145 0.0906  83  SER C OG  
4944 N  N   . ARG C 84  ? 0.1614 0.2804 0.1726 -0.0178 -0.0270 0.0324  84  ARG C N   
4945 C  CA  . ARG C 84  ? 0.1273 0.2931 0.1618 -0.0431 -0.0384 0.0165  84  ARG C CA  
4946 C  C   . ARG C 84  ? 0.1405 0.2164 0.1209 -0.0413 -0.0436 0.0613  84  ARG C C   
4947 O  O   . ARG C 84  ? 0.1280 0.2206 0.2744 -0.0333 0.0081  0.0904  84  ARG C O   
4948 C  CB  . ARG C 84  ? 0.1085 0.2926 0.2109 -0.0270 -0.0342 0.0928  84  ARG C CB  
4949 C  CG  . ARG C 84  ? 0.0951 0.3171 0.2106 -0.0119 -0.0134 0.0911  84  ARG C CG  
4950 C  CD  . ARG C 84  ? 0.0969 0.2858 0.2319 -0.0089 -0.0238 0.1188  84  ARG C CD  
4951 N  NE  . ARG C 84  ? 0.0918 0.3744 0.2520 0.0326  0.0074  0.1272  84  ARG C NE  
4952 C  CZ  . ARG C 84  ? 0.0854 0.2952 0.3575 -0.0260 -0.0185 0.1393  84  ARG C CZ  
4953 N  NH1 . ARG C 84  ? 0.1444 0.3248 0.3482 -0.0318 -0.0420 0.1806  84  ARG C NH1 
4954 N  NH2 . ARG C 84  ? 0.1330 0.3773 0.4324 0.0763  0.0005  0.1553  84  ARG C NH2 
4955 N  N   . TYR C 85  ? 0.1151 0.1837 0.2035 -0.0130 -0.0195 0.0963  85  TYR C N   
4956 C  CA  . TYR C 85  ? 0.1031 0.2170 0.1927 -0.0337 -0.0065 0.0892  85  TYR C CA  
4957 C  C   . TYR C 85  ? 0.1069 0.2071 0.1895 -0.0535 -0.0234 0.0445  85  TYR C C   
4958 O  O   . TYR C 85  ? 0.1482 0.2279 0.1913 -0.0378 -0.0296 0.0870  85  TYR C O   
4959 C  CB  . TYR C 85  ? 0.1065 0.1708 0.2049 -0.0229 -0.0409 0.0794  85  TYR C CB  
4960 C  CG  . TYR C 85  ? 0.1121 0.2259 0.1563 0.0119  -0.0190 0.0516  85  TYR C CG  
4961 C  CD1 . TYR C 85  ? 0.1106 0.2500 0.1701 -0.0281 -0.0192 0.0491  85  TYR C CD1 
4962 C  CD2 . TYR C 85  ? 0.1257 0.1808 0.1936 -0.0183 0.0041  0.0615  85  TYR C CD2 
4963 C  CE1 . TYR C 85  ? 0.1415 0.2320 0.1898 0.0281  -0.0340 0.0255  85  TYR C CE1 
4964 C  CE2 . TYR C 85  ? 0.1535 0.1561 0.1675 -0.0323 -0.0217 0.0231  85  TYR C CE2 
4965 C  CZ  . TYR C 85  ? 0.1270 0.1868 0.1772 -0.0190 -0.0383 0.0094  85  TYR C CZ  
4966 O  OH  . TYR C 85  ? 0.2117 0.1841 0.1823 0.0179  -0.0664 0.0066  85  TYR C OH  
4967 N  N   . SER C 86  ? 0.1294 0.2502 0.1668 -0.0373 -0.0457 0.0212  86  SER C N   
4968 C  CA  . SER C 86  ? 0.1291 0.2852 0.1491 -0.0853 -0.0297 0.0511  86  SER C CA  
4969 C  C   . SER C 86  ? 0.1417 0.3157 0.1543 -0.0417 -0.0337 0.0820  86  SER C C   
4970 O  O   . SER C 86  ? 0.1780 0.2171 0.2239 -0.0512 -0.0598 0.0829  86  SER C O   
4971 C  CB  . SER C 86  ? 0.0990 0.3740 0.2422 -0.1138 -0.0302 0.0471  86  SER C CB  
4972 O  OG  . SER C 86  ? 0.1209 0.4121 0.2353 -0.0756 -0.0417 0.0829  86  SER C OG  
4973 N  N   . ALA C 87  ? 0.1543 0.3023 0.1708 -0.0287 -0.0264 0.0955  87  ALA C N   
4974 C  CA  . ALA C 87  ? 0.1837 0.2977 0.1320 -0.0143 -0.0410 0.0423  87  ALA C CA  
4975 C  C   . ALA C 87  ? 0.1489 0.2981 0.1675 -0.0666 -0.0223 0.0526  87  ALA C C   
4976 O  O   . ALA C 87  ? 0.1413 0.3389 0.2362 -0.0700 -0.0579 0.0408  87  ALA C O   
4977 C  CB  . ALA C 87  ? 0.1847 0.4160 0.1496 -0.0598 -0.0352 0.1265  87  ALA C CB  
4978 N  N   . THR C 88  ? 0.1222 0.3292 0.1722 -0.0690 -0.0226 0.0325  88  THR C N   
4979 C  CA  . THR C 88  ? 0.1952 0.3668 0.1275 -0.0886 -0.0489 0.0105  88  THR C CA  
4980 C  C   . THR C 88  ? 0.1718 0.3854 0.1441 -0.1154 -0.0529 0.0150  88  THR C C   
4981 O  O   . THR C 88  ? 0.2096 0.3048 0.1484 -0.1560 -0.0447 0.0255  88  THR C O   
4982 C  CB  . THR C 88  ? 0.2275 0.2676 0.2903 -0.0894 -0.0787 -0.0211 88  THR C CB  
4983 O  OG1 . THR C 88  ? 0.4267 0.2640 0.2211 -0.1094 -0.0695 0.0227  88  THR C OG1 
4984 C  CG2 . THR C 88  ? 0.2162 0.3052 0.2187 -0.0875 -0.0479 -0.0104 88  THR C CG2 
4985 N  N   . GLN C 89  ? 0.1834 0.3204 0.1498 -0.1011 -0.0249 0.0507  89  GLN C N   
4986 C  CA  . GLN C 89  ? 0.1324 0.3274 0.1701 -0.1351 -0.0120 -0.0013 89  GLN C CA  
4987 C  C   . GLN C 89  ? 0.1796 0.2110 0.1305 -0.0820 -0.0457 -0.0110 89  GLN C C   
4988 O  O   . GLN C 89  ? 0.1596 0.2940 0.1415 -0.1021 -0.0604 -0.0010 89  GLN C O   
4989 C  CB  . GLN C 89  ? 0.1653 0.3554 0.1344 -0.1055 0.0063  -0.0240 89  GLN C CB  
4990 C  CG  . GLN C 89  ? 0.3150 0.2737 0.2390 -0.1403 -0.0763 0.0280  89  GLN C CG  
4991 C  CD  . GLN C 89  ? 0.3257 0.3968 0.1606 -0.0814 -0.0870 0.0227  89  GLN C CD  
4992 O  OE1 . GLN C 89  ? 0.2148 0.3759 0.2035 -0.1058 -0.0267 0.0087  89  GLN C OE1 
4993 N  NE2 . GLN C 89  ? 0.3919 0.1640 0.2979 -0.1365 -0.0722 0.0066  89  GLN C NE2 
4994 N  N   . LEU C 90  ? 0.1416 0.3098 0.1689 -0.0518 -0.0518 0.0632  90  LEU C N   
4995 C  CA  . LEU C 90  ? 0.1703 0.2524 0.1624 -0.0557 -0.0583 0.0227  90  LEU C CA  
4996 C  C   . LEU C 90  ? 0.1509 0.2802 0.1579 -0.0731 -0.0446 0.0421  90  LEU C C   
4997 O  O   . LEU C 90  ? 0.1913 0.3383 0.1632 -0.0930 -0.0292 0.0170  90  LEU C O   
4998 C  CB  . LEU C 90  ? 0.2248 0.2804 0.1112 0.0071  -0.0480 0.0685  90  LEU C CB  
4999 C  CG  . LEU C 90  ? 0.2153 0.3229 0.1516 -0.0731 -0.0750 0.1272  90  LEU C CG  
5000 C  CD1 . LEU C 90  ? 0.1898 0.4482 0.1722 -0.0465 -0.0621 0.1247  90  LEU C CD1 
5001 C  CD2 . LEU C 90  ? 0.2805 0.3737 0.2676 0.0142  -0.1491 0.1337  90  LEU C CD2 
5002 N  N   . HIS C 91  ? 0.1563 0.2416 0.1390 -0.0876 -0.0250 0.0414  91  HIS C N   
5003 C  CA  . HIS C 91  ? 0.1701 0.2369 0.1090 -0.0580 -0.0282 0.0153  91  HIS C CA  
5004 C  C   . HIS C 91  ? 0.1934 0.2563 0.0816 -0.0731 -0.0109 0.0314  91  HIS C C   
5005 O  O   . HIS C 91  ? 0.1401 0.2554 0.1298 -0.0342 -0.0284 0.0158  91  HIS C O   
5006 C  CB  . HIS C 91  ? 0.2062 0.2570 0.1487 -0.0892 -0.0633 0.0046  91  HIS C CB  
5007 C  CG  . HIS C 91  ? 0.2056 0.2550 0.1494 -0.0508 -0.0579 0.0502  91  HIS C CG  
5008 N  ND1 . HIS C 91  ? 0.1726 0.2473 0.1403 -0.0577 -0.0408 0.0081  91  HIS C ND1 
5009 C  CD2 . HIS C 91  ? 0.2130 0.2411 0.1178 -0.0757 -0.0262 -0.0278 91  HIS C CD2 
5010 C  CE1 . HIS C 91  ? 0.1388 0.1485 0.1758 -0.0138 -0.0544 -0.0179 91  HIS C CE1 
5011 N  NE2 . HIS C 91  ? 0.1876 0.2245 0.1265 -0.0609 -0.0346 0.0033  91  HIS C NE2 
5012 N  N   . LEU C 92  ? 0.1172 0.2709 0.1854 -0.0615 -0.0131 0.0151  92  LEU C N   
5013 C  CA  . LEU C 92  ? 0.1902 0.2020 0.1399 -0.0820 -0.0111 0.0122  92  LEU C CA  
5014 C  C   . LEU C 92  ? 0.1423 0.2178 0.1013 -0.0630 -0.0089 0.0240  92  LEU C C   
5015 O  O   . LEU C 92  ? 0.1647 0.2437 0.1826 -0.0589 -0.0444 0.0171  92  LEU C O   
5016 C  CB  . LEU C 92  ? 0.2085 0.3031 0.2155 0.0127  -0.0513 0.0936  92  LEU C CB  
5017 C  CG  . LEU C 92  ? 0.2293 0.3288 0.1859 0.0522  -0.0701 0.1032  92  LEU C CG  
5018 C  CD1 . LEU C 92  ? 0.2169 0.4223 0.2278 0.0826  -0.0604 -0.0147 92  LEU C CD1 
5019 C  CD2 . LEU C 92  ? 0.2831 0.3486 0.1703 -0.0463 -0.0405 0.0227  92  LEU C CD2 
5020 N  N   . HIS C 93  ? 0.1610 0.1859 0.1873 -0.0652 -0.0051 0.0275  93  HIS C N   
5021 C  CA  . HIS C 93  ? 0.1556 0.1959 0.1308 -0.0591 -0.0226 0.0331  93  HIS C CA  
5022 C  C   . HIS C 93  ? 0.1604 0.1683 0.1297 -0.0462 -0.0212 0.0226  93  HIS C C   
5023 O  O   . HIS C 93  ? 0.1829 0.1811 0.1151 0.0030  -0.0346 -0.0084 93  HIS C O   
5024 C  CB  . HIS C 93  ? 0.1455 0.1894 0.1469 -0.0550 -0.0409 0.0401  93  HIS C CB  
5025 C  CG  . HIS C 93  ? 0.1614 0.1075 0.1056 -0.0302 -0.0144 -0.0097 93  HIS C CG  
5026 N  ND1 . HIS C 93  ? 0.1708 0.1236 0.1227 -0.0436 -0.0041 -0.0118 93  HIS C ND1 
5027 C  CD2 . HIS C 93  ? 0.1390 0.1107 0.1099 -0.0528 -0.0208 0.0102  93  HIS C CD2 
5028 C  CE1 . HIS C 93  ? 0.1403 0.1574 0.1022 -0.0275 0.0251  -0.0348 93  HIS C CE1 
5029 N  NE2 . HIS C 93  ? 0.1646 0.0884 0.1234 -0.0254 -0.0076 -0.0214 93  HIS C NE2 
5030 N  N   . TRP C 94  ? 0.1191 0.1661 0.1652 -0.0526 -0.0042 0.0581  94  TRP C N   
5031 C  CA  . TRP C 94  ? 0.1208 0.1811 0.1746 -0.0819 -0.0183 0.0495  94  TRP C CA  
5032 C  C   . TRP C 94  ? 0.1582 0.1945 0.1421 -0.0345 0.0296  0.0215  94  TRP C C   
5033 O  O   . TRP C 94  ? 0.1901 0.1934 0.1293 -0.0469 -0.0189 -0.0104 94  TRP C O   
5034 C  CB  . TRP C 94  ? 0.1785 0.2091 0.1305 -0.0635 -0.0289 0.0078  94  TRP C CB  
5035 C  CG  . TRP C 94  ? 0.2525 0.2078 0.1241 -0.0816 0.0346  0.0209  94  TRP C CG  
5036 C  CD1 . TRP C 94  ? 0.2433 0.1803 0.1057 -0.0461 -0.0033 0.0021  94  TRP C CD1 
5037 C  CD2 . TRP C 94  ? 0.2051 0.2090 0.1444 -0.0493 -0.0147 0.0434  94  TRP C CD2 
5038 N  NE1 . TRP C 94  ? 0.2707 0.2762 0.1255 -0.1172 0.0044  -0.0082 94  TRP C NE1 
5039 C  CE2 . TRP C 94  ? 0.2458 0.2915 0.1065 -0.0854 -0.0089 0.0254  94  TRP C CE2 
5040 C  CE3 . TRP C 94  ? 0.2291 0.2651 0.0809 -0.1055 -0.0183 -0.0085 94  TRP C CE3 
5041 C  CZ2 . TRP C 94  ? 0.2273 0.2649 0.1362 -0.0524 -0.0476 0.0153  94  TRP C CZ2 
5042 C  CZ3 . TRP C 94  ? 0.1277 0.3411 0.1830 -0.0904 -0.0652 0.0133  94  TRP C CZ3 
5043 C  CH2 . TRP C 94  ? 0.2516 0.3353 0.1740 -0.0718 -0.0187 0.0421  94  TRP C CH2 
5044 N  N   . GLY C 95  ? 0.1212 0.2091 0.1582 -0.0820 -0.0035 -0.0293 95  GLY C N   
5045 C  CA  . GLY C 95  ? 0.1707 0.1855 0.1417 -0.0249 0.0263  -0.0025 95  GLY C CA  
5046 C  C   . GLY C 95  ? 0.2229 0.1614 0.1535 -0.0610 0.0430  -0.0403 95  GLY C C   
5047 O  O   . GLY C 95  ? 0.2374 0.1798 0.1830 -0.0722 0.0019  -0.0203 95  GLY C O   
5048 N  N   . ASN C 96  ? 0.2516 0.2972 0.1338 -0.0872 0.0297  0.0254  96  ASN C N   
5049 C  CA  . ASN C 96  ? 0.2523 0.2966 0.1428 -0.0807 0.0217  0.0001  96  ASN C CA  
5050 C  C   . ASN C 96  ? 0.2752 0.2974 0.1051 -0.0866 0.0251  -0.0067 96  ASN C C   
5051 O  O   . ASN C 96  ? 0.2433 0.2820 0.1215 -0.0713 0.0188  -0.0205 96  ASN C O   
5052 C  CB  . ASN C 96  ? 0.2331 0.3560 0.2105 -0.0569 0.0688  -0.0187 96  ASN C CB  
5053 C  CG  . ASN C 96  ? 0.2059 0.4278 0.2279 -0.0108 0.0992  -0.0126 96  ASN C CG  
5054 O  OD1 . ASN C 96  ? 0.2592 0.3718 0.3539 -0.0357 0.1386  0.0414  96  ASN C OD1 
5055 N  ND2 . ASN C 96  ? 0.2615 0.4896 0.2518 -0.0881 0.0073  -0.0508 96  ASN C ND2 
5056 N  N   . PRO C 97  ? 0.2893 0.3238 0.1098 -0.0816 0.0252  -0.0176 97  PRO C N   
5057 C  CA  . PRO C 97  ? 0.2819 0.3668 0.1258 -0.0917 0.0220  0.0646  97  PRO C CA  
5058 C  C   . PRO C 97  ? 0.2777 0.3819 0.2211 -0.0536 -0.0250 -0.0289 97  PRO C C   
5059 O  O   . PRO C 97  ? 0.3233 0.4032 0.1927 -0.1490 0.0121  -0.0127 97  PRO C O   
5060 C  CB  . PRO C 97  ? 0.3689 0.4437 0.1542 -0.1803 -0.0168 0.0100  97  PRO C CB  
5061 C  CG  . PRO C 97  ? 0.3592 0.3531 0.1761 -0.1315 -0.0096 -0.0011 97  PRO C CG  
5062 C  CD  . PRO C 97  ? 0.2805 0.3882 0.1315 -0.1310 0.0015  -0.0195 97  PRO C CD  
5063 N  N   . ASN C 98  ? 0.2466 0.3353 0.1751 -0.0965 0.0034  -0.0534 98  ASN C N   
5064 C  CA  . ASN C 98  ? 0.2542 0.4210 0.1967 -0.1055 -0.0097 -0.0586 98  ASN C CA  
5065 C  C   . ASN C 98  ? 0.1963 0.4174 0.1671 -0.0736 -0.0128 -0.0024 98  ASN C C   
5066 O  O   . ASN C 98  ? 0.1869 0.5577 0.2408 -0.1165 0.0125  -0.0523 98  ASN C O   
5067 C  CB  . ASN C 98  ? 0.3267 0.4918 0.2462 -0.0724 0.0412  -0.0551 98  ASN C CB  
5068 C  CG  . ASN C 98  ? 0.5015 0.5422 0.2750 -0.1018 0.0027  -0.1857 98  ASN C CG  
5069 O  OD1 . ASN C 98  ? 0.5343 0.7869 0.2917 -0.0601 0.1231  -0.0093 98  ASN C OD1 
5070 N  ND2 . ASN C 98  ? 0.6273 0.6188 0.3858 0.1151  0.0377  -0.1443 98  ASN C ND2 
5071 N  N   . ASP C 99  ? 0.2581 0.3441 0.1726 -0.0352 0.0429  -0.0219 99  ASP C N   
5072 C  CA  . ASP C 99  ? 0.2433 0.2658 0.1574 -0.0423 0.0456  0.0256  99  ASP C CA  
5073 C  C   . ASP C 99  ? 0.2084 0.3222 0.1889 -0.0463 -0.0118 0.0767  99  ASP C C   
5074 O  O   . ASP C 99  ? 0.2242 0.2126 0.1864 -0.0449 -0.0046 -0.0038 99  ASP C O   
5075 C  CB  . ASP C 99  ? 0.2753 0.2491 0.1518 -0.0627 -0.0044 -0.0062 99  ASP C CB  
5076 C  CG  . ASP C 99  ? 0.3624 0.1503 0.1588 -0.0108 -0.0044 -0.0350 99  ASP C CG  
5077 O  OD1 . ASP C 99  ? 0.4424 0.1060 0.2271 -0.0557 -0.0077 -0.0182 99  ASP C OD1 
5078 O  OD2 . ASP C 99  ? 0.3083 0.2742 0.3412 0.0630  -0.0636 -0.0245 99  ASP C OD2 
5079 N  N   . PRO C 100 ? 0.2073 0.2332 0.1760 -0.0732 0.0472  0.0416  100 PRO C N   
5080 C  CA  . PRO C 100 ? 0.1981 0.2396 0.1338 -0.0319 0.0017  0.0682  100 PRO C CA  
5081 C  C   . PRO C 100 ? 0.1855 0.2191 0.1336 -0.0606 0.0100  0.0511  100 PRO C C   
5082 O  O   . PRO C 100 ? 0.2103 0.2223 0.1898 -0.0197 0.0153  0.0598  100 PRO C O   
5083 C  CB  . PRO C 100 ? 0.2115 0.2071 0.1908 -0.0381 0.0207  0.0885  100 PRO C CB  
5084 C  CG  . PRO C 100 ? 0.2544 0.2841 0.2256 -0.0855 0.0351  0.0829  100 PRO C CG  
5085 C  CD  . PRO C 100 ? 0.1938 0.2031 0.3234 -0.1260 -0.0314 0.0753  100 PRO C CD  
5086 N  N   . HIS C 101 ? 0.2010 0.1360 0.1413 -0.0751 -0.0082 0.0241  101 HIS C N   
5087 C  CA  . HIS C 101 ? 0.2081 0.1844 0.1225 -0.0805 -0.0389 0.0620  101 HIS C CA  
5088 C  C   . HIS C 101 ? 0.2261 0.1503 0.2128 -0.0674 -0.0162 0.0569  101 HIS C C   
5089 O  O   . HIS C 101 ? 0.2688 0.1514 0.2579 -0.0582 -0.0632 -0.0108 101 HIS C O   
5090 C  CB  . HIS C 101 ? 0.1857 0.1938 0.1836 -0.0596 -0.0284 0.0387  101 HIS C CB  
5091 C  CG  . HIS C 101 ? 0.1861 0.1365 0.2437 -0.0551 -0.0074 0.0151  101 HIS C CG  
5092 N  ND1 . HIS C 101 ? 0.2400 0.1582 0.1920 -0.0204 0.0143  -0.0194 101 HIS C ND1 
5093 C  CD2 . HIS C 101 ? 0.2640 0.1458 0.2087 -0.0763 0.0218  0.0747  101 HIS C CD2 
5094 C  CE1 . HIS C 101 ? 0.2600 0.1994 0.2270 -0.0539 0.0142  -0.0253 101 HIS C CE1 
5095 N  NE2 . HIS C 101 ? 0.2627 0.1013 0.2347 -0.0635 0.0273  0.0341  101 HIS C NE2 
5096 N  N   . GLY C 102 ? 0.1847 0.0496 0.1750 -0.0314 -0.0095 0.0480  102 GLY C N   
5097 C  CA  . GLY C 102 ? 0.2107 0.0602 0.1340 -0.0411 0.0334  0.0419  102 GLY C CA  
5098 C  C   . GLY C 102 ? 0.1790 0.0593 0.0927 -0.0311 -0.0006 0.0641  102 GLY C C   
5099 O  O   . GLY C 102 ? 0.1931 0.0398 0.1864 -0.0359 -0.0108 0.0374  102 GLY C O   
5100 N  N   . SER C 103 ? 0.1478 0.0889 0.1402 0.0161  0.0153  0.0215  103 SER C N   
5101 C  CA  . SER C 103 ? 0.1726 0.0566 0.1505 -0.0005 0.0225  0.0203  103 SER C CA  
5102 C  C   . SER C 103 ? 0.1234 0.1385 0.1295 -0.0368 -0.0370 0.0453  103 SER C C   
5103 O  O   . SER C 103 ? 0.1280 0.1262 0.1761 -0.0292 -0.0118 0.0432  103 SER C O   
5104 C  CB  . SER C 103 ? 0.1613 0.0708 0.1618 -0.0098 -0.0205 -0.0031 103 SER C CB  
5105 O  OG  . SER C 103 ? 0.1460 0.0908 0.1381 -0.0111 -0.0157 0.0274  103 SER C OG  
5106 N  N   . GLU C 104 ? 0.1543 0.0503 0.1395 -0.0097 -0.0002 0.0064  104 GLU C N   
5107 C  CA  . GLU C 104 ? 0.1318 0.0872 0.1115 -0.0485 -0.0363 0.0142  104 GLU C CA  
5108 C  C   . GLU C 104 ? 0.1013 0.0269 0.1772 -0.0400 -0.0052 -0.0233 104 GLU C C   
5109 O  O   . GLU C 104 ? 0.1265 0.0442 0.1701 0.0036  -0.0122 -0.0091 104 GLU C O   
5110 C  CB  . GLU C 104 ? 0.1258 0.0929 0.1262 -0.0531 -0.0203 -0.0287 104 GLU C CB  
5111 C  CG  . GLU C 104 ? 0.1417 0.0696 0.1251 -0.0550 -0.0410 -0.0134 104 GLU C CG  
5112 C  CD  . GLU C 104 ? 0.1736 0.0571 0.1539 -0.0197 -0.0150 0.0040  104 GLU C CD  
5113 O  OE1 . GLU C 104 ? 0.1568 0.0538 0.1941 -0.0030 -0.0127 -0.0024 104 GLU C OE1 
5114 O  OE2 . GLU C 104 ? 0.1361 0.1093 0.1945 -0.0164 0.0152  -0.0092 104 GLU C OE2 
5115 N  N   . HIS C 105 ? 0.1347 0.0340 0.1438 -0.0088 -0.0141 -0.0348 105 HIS C N   
5116 C  CA  . HIS C 105 ? 0.1288 0.0227 0.1708 -0.0300 0.0023  -0.0392 105 HIS C CA  
5117 C  C   . HIS C 105 ? 0.1377 0.0076 0.1542 -0.0125 -0.0301 0.0057  105 HIS C C   
5118 O  O   . HIS C 105 ? 0.1951 0.0103 0.1660 -0.0168 -0.0178 0.0215  105 HIS C O   
5119 C  CB  . HIS C 105 ? 0.1223 0.0811 0.1340 -0.0160 0.0050  0.0136  105 HIS C CB  
5120 C  CG  . HIS C 105 ? 0.1189 0.0863 0.1049 -0.0195 0.0091  -0.0035 105 HIS C CG  
5121 N  ND1 . HIS C 105 ? 0.0970 0.1168 0.1439 -0.0015 -0.0100 -0.0046 105 HIS C ND1 
5122 C  CD2 . HIS C 105 ? 0.1676 0.0063 0.1175 -0.0023 0.0101  0.0001  105 HIS C CD2 
5123 C  CE1 . HIS C 105 ? 0.1365 0.0827 0.1236 -0.0020 -0.0091 -0.0245 105 HIS C CE1 
5124 N  NE2 . HIS C 105 ? 0.1333 0.0268 0.1460 0.0019  -0.0168 0.0216  105 HIS C NE2 
5125 N  N   . THR C 106 ? 0.1035 0.0140 0.2088 -0.0265 -0.0332 0.0178  106 THR C N   
5126 C  CA  . THR C 106 ? 0.1103 0.0214 0.1846 -0.0380 -0.0334 -0.0019 106 THR C CA  
5127 C  C   . THR C 106 ? 0.1305 0.0425 0.1855 -0.0013 -0.0067 0.0080  106 THR C C   
5128 O  O   . THR C 106 ? 0.1342 0.0485 0.1772 -0.0109 -0.0128 -0.0103 106 THR C O   
5129 C  CB  . THR C 106 ? 0.1259 0.0457 0.1707 0.0025  -0.0171 0.0032  106 THR C CB  
5130 O  OG1 . THR C 106 ? 0.1401 0.0241 0.1951 0.0103  -0.0143 0.0264  106 THR C OG1 
5131 C  CG2 . THR C 106 ? 0.1585 0.0597 0.1744 -0.0006 0.0142  0.0092  106 THR C CG2 
5132 N  N   . VAL C 107 ? 0.1223 0.0331 0.1791 -0.0082 -0.0146 -0.0060 107 VAL C N   
5133 C  CA  . VAL C 107 ? 0.1060 0.1018 0.1875 0.0201  -0.0425 -0.0472 107 VAL C CA  
5134 C  C   . VAL C 107 ? 0.1602 0.0086 0.2008 -0.0035 -0.0261 -0.0198 107 VAL C C   
5135 O  O   . VAL C 107 ? 0.1586 0.0491 0.2009 -0.0058 -0.0111 0.0071  107 VAL C O   
5136 C  CB  . VAL C 107 ? 0.1546 0.0458 0.2444 -0.0022 -0.0258 -0.0046 107 VAL C CB  
5137 C  CG1 . VAL C 107 ? 0.1786 0.0703 0.3229 -0.0159 -0.0474 -0.0485 107 VAL C CG1 
5138 C  CG2 . VAL C 107 ? 0.1370 0.0541 0.2808 0.0052  0.0027  0.0260  107 VAL C CG2 
5139 N  N   . SER C 108 ? 0.1638 0.0347 0.1938 0.0100  -0.0341 -0.0241 108 SER C N   
5140 C  CA  . SER C 108 ? 0.1632 0.0546 0.2728 -0.0022 -0.0239 -0.0128 108 SER C CA  
5141 C  C   . SER C 108 ? 0.1495 0.0350 0.2046 0.0334  -0.0541 0.0032  108 SER C C   
5142 O  O   . SER C 108 ? 0.1672 0.1096 0.2644 -0.0142 -0.0354 -0.0233 108 SER C O   
5143 C  CB  . SER C 108 ? 0.1634 0.0544 0.2654 -0.0153 -0.0067 -0.0363 108 SER C CB  
5144 O  OG  . SER C 108 ? 0.2270 0.1500 0.3436 -0.0468 0.0059  -0.1260 108 SER C OG  
5145 N  N   . GLY C 109 ? 0.1532 0.0438 0.2163 0.0357  -0.0247 -0.0229 109 GLY C N   
5146 C  CA  . GLY C 109 ? 0.1466 0.1054 0.1933 0.0223  -0.0072 -0.0277 109 GLY C CA  
5147 C  C   . GLY C 109 ? 0.1164 0.1495 0.2046 -0.0144 -0.0231 -0.0365 109 GLY C C   
5148 O  O   . GLY C 109 ? 0.1850 0.1683 0.2124 0.0091  -0.0049 -0.0370 109 GLY C O   
5149 N  N   . GLN C 110 ? 0.1467 0.1377 0.1724 -0.0164 -0.0266 0.0151  110 GLN C N   
5150 C  CA  . GLN C 110 ? 0.1617 0.0305 0.2020 -0.0408 -0.0422 0.0286  110 GLN C CA  
5151 C  C   . GLN C 110 ? 0.1318 0.0127 0.2135 -0.0223 0.0070  -0.0235 110 GLN C C   
5152 O  O   . GLN C 110 ? 0.1313 0.0207 0.1882 0.0064  -0.0036 0.0197  110 GLN C O   
5153 C  CB  . GLN C 110 ? 0.2074 0.0206 0.2196 -0.0319 -0.0081 0.0026  110 GLN C CB  
5154 C  CG  . GLN C 110 ? 0.1923 0.1222 0.2939 -0.0588 -0.0105 -0.0262 110 GLN C CG  
5155 C  CD  . GLN C 110 ? 0.1897 0.0830 0.2889 -0.0599 -0.0296 -0.0399 110 GLN C CD  
5156 O  OE1 . GLN C 110 ? 0.2517 0.2320 0.3124 -0.0001 -0.0494 -0.0660 110 GLN C OE1 
5157 N  NE2 . GLN C 110 ? 0.2066 0.0513 0.3225 0.0137  0.0573  0.0171  110 GLN C NE2 
5158 N  N   . HIS C 111 ? 0.1990 0.0902 0.1597 -0.0178 -0.0075 -0.0089 111 HIS C N   
5159 C  CA  . HIS C 111 ? 0.1775 0.0686 0.1977 -0.0106 -0.0089 -0.0174 111 HIS C CA  
5160 C  C   . HIS C 111 ? 0.2049 0.1222 0.2268 -0.0352 -0.0120 0.0612  111 HIS C C   
5161 O  O   . HIS C 111 ? 0.2024 0.2058 0.3468 -0.0873 -0.0650 0.1551  111 HIS C O   
5162 C  CB  . HIS C 111 ? 0.1936 0.0832 0.2267 0.0223  0.0074  -0.0226 111 HIS C CB  
5163 C  CG  . HIS C 111 ? 0.1991 0.0390 0.2503 -0.0315 -0.0003 -0.0208 111 HIS C CG  
5164 N  ND1 . HIS C 111 ? 0.1652 0.1491 0.2999 -0.0801 0.0483  -0.0093 111 HIS C ND1 
5165 C  CD2 . HIS C 111 ? 0.1661 0.0392 0.3227 0.0036  0.0130  -0.0232 111 HIS C CD2 
5166 C  CE1 . HIS C 111 ? 0.2697 0.0429 0.3531 -0.0346 0.0412  -0.0629 111 HIS C CE1 
5167 N  NE2 . HIS C 111 ? 0.2606 0.0723 0.3697 -0.0124 0.0693  0.0251  111 HIS C NE2 
5168 N  N   . PHE C 112 ? 0.1980 0.1121 0.1615 -0.0216 -0.0377 0.0227  112 PHE C N   
5169 C  CA  . PHE C 112 ? 0.1595 0.1295 0.1768 -0.0357 -0.0336 0.0340  112 PHE C CA  
5170 C  C   . PHE C 112 ? 0.1725 0.0805 0.1509 -0.0314 -0.0115 0.0533  112 PHE C C   
5171 O  O   . PHE C 112 ? 0.2013 0.1004 0.1872 -0.0032 0.0118  0.0457  112 PHE C O   
5172 C  CB  . PHE C 112 ? 0.1793 0.1040 0.1877 -0.0525 -0.0171 0.0283  112 PHE C CB  
5173 C  CG  . PHE C 112 ? 0.1958 0.0542 0.2778 -0.0757 -0.0117 0.0116  112 PHE C CG  
5174 C  CD1 . PHE C 112 ? 0.2421 0.1635 0.2701 -0.0771 -0.0158 -0.0107 112 PHE C CD1 
5175 C  CD2 . PHE C 112 ? 0.2525 0.0814 0.2818 -0.0609 0.0044  0.0496  112 PHE C CD2 
5176 C  CE1 . PHE C 112 ? 0.3063 0.0979 0.3039 -0.0603 0.0122  0.0131  112 PHE C CE1 
5177 C  CE2 . PHE C 112 ? 0.2156 0.1496 0.3959 -0.0886 -0.0039 -0.0410 112 PHE C CE2 
5178 C  CZ  . PHE C 112 ? 0.2724 0.1245 0.3596 -0.0340 0.0488  0.0271  112 PHE C CZ  
5179 N  N   . ALA C 113 ? 0.1735 0.1234 0.1805 -0.0457 -0.0229 0.0696  113 ALA C N   
5180 C  CA  . ALA C 113 ? 0.1761 0.1708 0.1435 -0.0451 -0.0064 0.0678  113 ALA C CA  
5181 C  C   . ALA C 113 ? 0.1550 0.1848 0.1909 -0.0444 -0.0003 0.0323  113 ALA C C   
5182 O  O   . ALA C 113 ? 0.2128 0.1719 0.1688 -0.0519 -0.0099 0.0359  113 ALA C O   
5183 C  CB  . ALA C 113 ? 0.1963 0.1697 0.2214 -0.0325 -0.0384 0.0813  113 ALA C CB  
5184 N  N   . ALA C 114 ? 0.1718 0.1449 0.1413 -0.0687 -0.0040 0.0500  114 ALA C N   
5185 C  CA  . ALA C 114 ? 0.1983 0.1094 0.1476 -0.0530 -0.0211 0.0276  114 ALA C CA  
5186 C  C   . ALA C 114 ? 0.1905 0.1360 0.1038 -0.0267 -0.0436 0.0697  114 ALA C C   
5187 O  O   . ALA C 114 ? 0.1749 0.1460 0.1585 -0.0334 0.0189  0.0394  114 ALA C O   
5188 C  CB  . ALA C 114 ? 0.1972 0.1291 0.1654 -0.0406 -0.0452 0.0126  114 ALA C CB  
5189 N  N   . GLU C 115 ? 0.1735 0.1162 0.1377 -0.0196 -0.0055 0.0231  115 GLU C N   
5190 C  CA  . GLU C 115 ? 0.1464 0.1466 0.1358 -0.0561 -0.0260 0.0397  115 GLU C CA  
5191 C  C   . GLU C 115 ? 0.1096 0.1352 0.1417 -0.0223 -0.0234 0.0067  115 GLU C C   
5192 O  O   . GLU C 115 ? 0.1571 0.1933 0.1320 -0.0325 -0.0157 -0.0206 115 GLU C O   
5193 C  CB  . GLU C 115 ? 0.1239 0.1363 0.1223 -0.0185 -0.0118 0.0267  115 GLU C CB  
5194 C  CG  . GLU C 115 ? 0.1667 0.1022 0.1173 -0.0147 -0.0132 0.0340  115 GLU C CG  
5195 C  CD  . GLU C 115 ? 0.1124 0.0516 0.1428 0.0249  0.0060  0.0167  115 GLU C CD  
5196 O  OE1 . GLU C 115 ? 0.1331 0.0812 0.1435 -0.0267 -0.0082 0.0148  115 GLU C OE1 
5197 O  OE2 . GLU C 115 ? 0.1262 0.0929 0.1370 -0.0199 -0.0117 0.0215  115 GLU C OE2 
5198 N  N   . LEU C 116 ? 0.1173 0.1531 0.1474 -0.0436 -0.0099 0.0414  116 LEU C N   
5199 C  CA  . LEU C 116 ? 0.1040 0.2236 0.1311 -0.0435 -0.0395 0.0753  116 LEU C CA  
5200 C  C   . LEU C 116 ? 0.1241 0.1701 0.1187 -0.0502 -0.0326 0.0599  116 LEU C C   
5201 O  O   . LEU C 116 ? 0.1448 0.1981 0.1577 -0.0342 -0.0259 0.0309  116 LEU C O   
5202 C  CB  . LEU C 116 ? 0.1469 0.2162 0.1830 -0.0244 -0.0526 0.0754  116 LEU C CB  
5203 C  CG  . LEU C 116 ? 0.1286 0.2790 0.2285 -0.0217 -0.0749 0.0807  116 LEU C CG  
5204 C  CD1 . LEU C 116 ? 0.2536 0.3100 0.2248 0.0344  -0.0364 0.0562  116 LEU C CD1 
5205 C  CD2 . LEU C 116 ? 0.2010 0.2939 0.2921 -0.0049 -0.0376 -0.0109 116 LEU C CD2 
5206 N  N   . HIS C 117 ? 0.1065 0.1733 0.1624 -0.0462 -0.0192 0.0439  117 HIS C N   
5207 C  CA  . HIS C 117 ? 0.0774 0.1911 0.1718 -0.0034 0.0157  0.0369  117 HIS C CA  
5208 C  C   . HIS C 117 ? 0.1101 0.1579 0.1444 -0.0421 -0.0143 0.0099  117 HIS C C   
5209 O  O   . HIS C 117 ? 0.1381 0.1632 0.1654 -0.0510 -0.0408 0.0122  117 HIS C O   
5210 C  CB  . HIS C 117 ? 0.0997 0.1557 0.1665 -0.0242 -0.0551 0.0027  117 HIS C CB  
5211 C  CG  . HIS C 117 ? 0.1263 0.1085 0.1013 -0.0630 -0.0792 0.0336  117 HIS C CG  
5212 N  ND1 . HIS C 117 ? 0.0382 0.0919 0.4199 -0.0522 -0.1148 0.1880  117 HIS C ND1 
5213 C  CD2 . HIS C 117 ? 0.1006 0.0954 0.1083 -0.0599 -0.0455 0.0250  117 HIS C CD2 
5214 C  CE1 . HIS C 117 ? 0.1528 0.0794 0.1341 -0.0562 -0.0165 -0.0209 117 HIS C CE1 
5215 N  NE2 . HIS C 117 ? 0.1029 0.0751 0.1342 -0.0168 -0.0298 0.0107  117 HIS C NE2 
5216 N  N   . ILE C 118 ? 0.0934 0.2125 0.1360 -0.0354 -0.0136 0.0571  118 ILE C N   
5217 C  CA  . ILE C 118 ? 0.0908 0.2535 0.1349 -0.0394 -0.0128 0.0456  118 ILE C CA  
5218 C  C   . ILE C 118 ? 0.0995 0.1334 0.1502 -0.0525 -0.0243 0.0193  118 ILE C C   
5219 O  O   . ILE C 118 ? 0.1474 0.1514 0.1437 -0.0160 -0.0285 0.0261  118 ILE C O   
5220 C  CB  . ILE C 118 ? 0.1280 0.2564 0.1446 -0.0137 -0.0460 0.0655  118 ILE C CB  
5221 C  CG1 . ILE C 118 ? 0.1354 0.2372 0.2185 -0.0111 -0.0348 0.0869  118 ILE C CG1 
5222 C  CG2 . ILE C 118 ? 0.1259 0.3366 0.1819 -0.0187 -0.0664 0.0644  118 ILE C CG2 
5223 C  CD1 . ILE C 118 ? 0.2223 0.2563 0.2344 0.0341  -0.0815 0.0793  118 ILE C CD1 
5224 N  N   . VAL C 119 ? 0.1445 0.1361 0.1816 -0.0399 -0.0159 0.0110  119 VAL C N   
5225 C  CA  . VAL C 119 ? 0.1376 0.1528 0.1439 -0.0538 -0.0125 -0.0006 119 VAL C CA  
5226 C  C   . VAL C 119 ? 0.1094 0.1850 0.1668 0.0185  -0.0328 0.0541  119 VAL C C   
5227 O  O   . VAL C 119 ? 0.1208 0.1973 0.2024 -0.0484 -0.0410 0.0605  119 VAL C O   
5228 C  CB  . VAL C 119 ? 0.1433 0.1376 0.1524 -0.0279 -0.0168 0.0168  119 VAL C CB  
5229 C  CG1 . VAL C 119 ? 0.2034 0.1862 0.1430 -0.0232 -0.0322 0.0368  119 VAL C CG1 
5230 C  CG2 . VAL C 119 ? 0.1293 0.1438 0.1729 -0.0114 -0.0218 -0.0027 119 VAL C CG2 
5231 N  N   . HIS C 120 ? 0.1654 0.1801 0.1683 -0.0141 0.0010  0.0381  120 HIS C N   
5232 C  CA  . HIS C 120 ? 0.1198 0.1316 0.2028 -0.0022 -0.0173 0.0530  120 HIS C CA  
5233 C  C   . HIS C 120 ? 0.1294 0.1227 0.1690 -0.0679 -0.0554 0.0304  120 HIS C C   
5234 O  O   . HIS C 120 ? 0.1257 0.1306 0.1980 -0.0295 -0.0273 0.0365  120 HIS C O   
5235 C  CB  . HIS C 120 ? 0.1686 0.1168 0.1815 -0.0395 -0.0131 0.0380  120 HIS C CB  
5236 C  CG  . HIS C 120 ? 0.1546 0.1323 0.1988 -0.0068 0.0268  0.0542  120 HIS C CG  
5237 N  ND1 . HIS C 120 ? 0.1790 0.1791 0.1566 -0.0623 -0.0299 0.0714  120 HIS C ND1 
5238 C  CD2 . HIS C 120 ? 0.1902 0.2207 0.1807 0.0206  -0.0055 0.0780  120 HIS C CD2 
5239 C  CE1 . HIS C 120 ? 0.1715 0.2125 0.1805 -0.0020 0.0384  0.0768  120 HIS C CE1 
5240 N  NE2 . HIS C 120 ? 0.1566 0.2103 0.1995 -0.0218 -0.0265 0.0631  120 HIS C NE2 
5241 N  N   . TYR C 121 ? 0.1270 0.1668 0.2619 -0.0478 -0.0100 0.0833  121 TYR C N   
5242 C  CA  . TYR C 121 ? 0.1654 0.1688 0.2091 -0.0392 -0.0023 0.0675  121 TYR C CA  
5243 C  C   . TYR C 121 ? 0.1417 0.1923 0.1895 -0.0422 -0.0190 0.0782  121 TYR C C   
5244 O  O   . TYR C 121 ? 0.1342 0.2056 0.2084 -0.0298 -0.0292 0.0750  121 TYR C O   
5245 C  CB  . TYR C 121 ? 0.2141 0.2121 0.2612 -0.0878 -0.0361 0.0494  121 TYR C CB  
5246 C  CG  . TYR C 121 ? 0.2159 0.1796 0.2506 -0.0929 -0.0350 0.0816  121 TYR C CG  
5247 C  CD1 . TYR C 121 ? 0.1891 0.2865 0.2166 0.0018  0.0021  0.0607  121 TYR C CD1 
5248 C  CD2 . TYR C 121 ? 0.2166 0.2933 0.2115 -0.1143 -0.0249 0.0491  121 TYR C CD2 
5249 C  CE1 . TYR C 121 ? 0.1930 0.2948 0.2291 0.0001  0.0154  0.0580  121 TYR C CE1 
5250 C  CE2 . TYR C 121 ? 0.2031 0.3104 0.2098 -0.0487 -0.0055 0.0479  121 TYR C CE2 
5251 C  CZ  . TYR C 121 ? 0.1816 0.3853 0.1782 -0.0484 -0.0111 0.0414  121 TYR C CZ  
5252 O  OH  . TYR C 121 ? 0.1979 0.4167 0.3224 -0.0609 -0.0616 0.0591  121 TYR C OH  
5253 N  N   . ASN C 122 ? 0.1560 0.2113 0.1864 -0.0621 -0.0193 0.0911  122 ASN C N   
5254 C  CA  . ASN C 122 ? 0.1654 0.2318 0.1603 -0.0620 -0.0234 0.0912  122 ASN C CA  
5255 C  C   . ASN C 122 ? 0.1287 0.2433 0.1911 -0.0383 -0.0309 0.0886  122 ASN C C   
5256 O  O   . ASN C 122 ? 0.1581 0.2271 0.2376 -0.0265 -0.0394 0.0501  122 ASN C O   
5257 C  CB  . ASN C 122 ? 0.1489 0.3244 0.2028 -0.0236 -0.0387 0.1105  122 ASN C CB  
5258 C  CG  . ASN C 122 ? 0.1980 0.2130 0.1945 -0.0272 -0.0590 0.0454  122 ASN C CG  
5259 O  OD1 . ASN C 122 ? 0.1812 0.2180 0.1967 -0.0497 -0.0276 0.0751  122 ASN C OD1 
5260 N  ND2 . ASN C 122 ? 0.3415 0.2381 0.2548 0.0165  -0.1480 0.0469  122 ASN C ND2 
5261 N  N   . SER C 123 ? 0.1270 0.2383 0.1986 -0.0433 -0.0328 0.0486  123 SER C N   
5262 C  CA  . SER C 123 ? 0.1262 0.3149 0.1772 -0.0625 -0.0254 0.0425  123 SER C CA  
5263 C  C   . SER C 123 ? 0.1800 0.2214 0.2052 -0.0643 0.0017  0.0644  123 SER C C   
5264 O  O   . SER C 123 ? 0.1683 0.2913 0.2397 -0.0802 -0.0122 0.0638  123 SER C O   
5265 C  CB  . SER C 123 ? 0.1532 0.3189 0.2142 -0.0223 -0.0631 0.0115  123 SER C CB  
5266 O  OG  . SER C 123 ? 0.1402 0.2922 0.1919 -0.0241 -0.0302 0.0609  123 SER C OG  
5267 N  N   . ASP C 124 ? 0.1873 0.2994 0.1600 -0.0023 0.0096  0.0628  124 ASP C N   
5268 C  CA  . ASP C 124 ? 0.1751 0.2092 0.1757 0.0055  -0.0004 0.0796  124 ASP C CA  
5269 C  C   . ASP C 124 ? 0.2041 0.1708 0.2529 -0.0726 -0.0276 0.0974  124 ASP C C   
5270 O  O   . ASP C 124 ? 0.2971 0.2638 0.2797 -0.0868 0.0649  0.1005  124 ASP C O   
5271 C  CB  . ASP C 124 ? 0.1834 0.2475 0.1602 0.0111  -0.0446 0.0598  124 ASP C CB  
5272 C  CG  . ASP C 124 ? 0.1744 0.2466 0.1948 0.0272  -0.0189 0.0403  124 ASP C CG  
5273 O  OD1 . ASP C 124 ? 0.1743 0.3427 0.2112 0.0151  -0.0156 0.0883  124 ASP C OD1 
5274 O  OD2 . ASP C 124 ? 0.1646 0.2308 0.2333 -0.0047 0.0189  0.0512  124 ASP C OD2 
5275 N  N   . LEU C 125 ? 0.2181 0.1513 0.2419 -0.0580 -0.0283 0.0095  125 LEU C N   
5276 C  CA  . LEU C 125 ? 0.2610 0.1372 0.2834 -0.0430 0.0010  -0.0199 125 LEU C CA  
5277 C  C   . LEU C 125 ? 0.2900 0.1424 0.2579 -0.0945 -0.0228 -0.0031 125 LEU C C   
5278 O  O   . LEU C 125 ? 0.4436 0.1456 0.2967 -0.0835 0.0770  -0.0033 125 LEU C O   
5279 C  CB  . LEU C 125 ? 0.3074 0.2467 0.2473 -0.0061 -0.0638 0.0059  125 LEU C CB  
5280 C  CG  . LEU C 125 ? 0.3498 0.2929 0.3660 0.0384  -0.1649 -0.1419 125 LEU C CG  
5281 C  CD1 . LEU C 125 ? 0.3520 0.3524 0.5029 -0.0174 -0.1080 -0.2283 125 LEU C CD1 
5282 C  CD2 . LEU C 125 ? 0.3396 0.1758 0.2931 0.0154  -0.0530 -0.0446 125 LEU C CD2 
5283 N  N   . TYR C 126 ? 0.1943 0.2546 0.2516 -0.0343 0.0061  -0.0033 126 TYR C N   
5284 C  CA  . TYR C 126 ? 0.2002 0.2722 0.2297 -0.0331 0.0255  0.0033  126 TYR C CA  
5285 C  C   . TYR C 126 ? 0.2002 0.2390 0.2913 -0.0797 -0.0116 -0.0421 126 TYR C C   
5286 O  O   . TYR C 126 ? 0.1979 0.2715 0.2717 -0.0297 -0.0294 0.0029  126 TYR C O   
5287 C  CB  . TYR C 126 ? 0.1995 0.2385 0.2613 -0.0396 0.0174  0.0089  126 TYR C CB  
5288 C  CG  . TYR C 126 ? 0.2243 0.2303 0.2703 -0.0129 -0.0161 0.0270  126 TYR C CG  
5289 C  CD1 . TYR C 126 ? 0.3012 0.2249 0.2854 -0.0284 -0.0131 0.0115  126 TYR C CD1 
5290 C  CD2 . TYR C 126 ? 0.2054 0.2523 0.3224 -0.0242 -0.0508 0.0605  126 TYR C CD2 
5291 C  CE1 . TYR C 126 ? 0.2922 0.1040 0.2508 -0.0196 -0.0013 0.0065  126 TYR C CE1 
5292 C  CE2 . TYR C 126 ? 0.2152 0.2538 0.2597 0.0199  -0.0048 0.0792  126 TYR C CE2 
5293 C  CZ  . TYR C 126 ? 0.3170 0.2051 0.2600 -0.0924 -0.0543 0.0453  126 TYR C CZ  
5294 O  OH  . TYR C 126 ? 0.3850 0.2372 0.2752 -0.0583 -0.0937 0.0773  126 TYR C OH  
5295 N  N   . PRO C 127 ? 0.3261 0.2037 0.3106 -0.0879 -0.0706 -0.0156 127 PRO C N   
5296 C  CA  . PRO C 127 ? 0.2693 0.2909 0.3380 -0.0634 -0.0805 -0.0806 127 PRO C CA  
5297 C  C   . PRO C 127 ? 0.3234 0.2606 0.3362 -0.0127 -0.0718 -0.0398 127 PRO C C   
5298 O  O   . PRO C 127 ? 0.3811 0.3240 0.3355 0.0547  -0.1098 -0.1208 127 PRO C O   
5299 C  CB  . PRO C 127 ? 0.4311 0.2332 0.4367 -0.0615 -0.1517 0.0291  127 PRO C CB  
5300 C  CG  . PRO C 127 ? 0.3976 0.1159 0.4210 -0.0266 -0.0632 -0.0416 127 PRO C CG  
5301 C  CD  . PRO C 127 ? 0.3370 0.2006 0.3797 -0.0659 -0.0242 -0.0363 127 PRO C CD  
5302 N  N   . ASP C 128 ? 0.3158 0.3854 0.2664 0.0220  -0.0814 -0.0322 128 ASP C N   
5303 C  CA  . ASP C 128 ? 0.3554 0.3362 0.2394 0.1024  -0.0336 -0.0564 128 ASP C CA  
5304 C  C   . ASP C 128 ? 0.3635 0.2581 0.1976 0.0767  0.0334  0.0570  128 ASP C C   
5305 O  O   . ASP C 128 ? 0.3240 0.3025 0.2286 0.0621  -0.0190 0.0314  128 ASP C O   
5306 C  CB  . ASP C 128 ? 0.4458 0.5308 0.2854 0.0819  -0.1073 -0.1297 128 ASP C CB  
5307 C  CG  . ASP C 128 ? 0.4194 0.5547 0.4846 0.0625  -0.1015 -0.0593 128 ASP C CG  
5308 O  OD1 . ASP C 128 ? 0.4523 0.3264 0.3458 0.1005  -0.0370 0.0329  128 ASP C OD1 
5309 O  OD2 . ASP C 128 ? 0.5776 0.6434 0.5464 -0.0299 -0.1889 -0.0453 128 ASP C OD2 
5310 N  N   . ALA C 129 ? 0.4580 0.2059 0.2387 0.0171  0.0897  0.0041  129 ALA C N   
5311 C  CA  . ALA C 129 ? 0.4176 0.2657 0.2397 0.0861  0.0710  0.0099  129 ALA C CA  
5312 C  C   . ALA C 129 ? 0.3256 0.2487 0.2310 0.0240  0.0378  0.0488  129 ALA C C   
5313 O  O   . ALA C 129 ? 0.2768 0.2761 0.3788 0.0397  0.0178  0.1209  129 ALA C O   
5314 C  CB  . ALA C 129 ? 0.4389 0.3045 0.2669 0.0329  -0.0025 0.0616  129 ALA C CB  
5315 N  N   . SER C 130 ? 0.4027 0.2806 0.2541 0.0269  0.0500  -0.0064 130 SER C N   
5316 C  CA  . SER C 130 ? 0.3890 0.3376 0.4264 0.0363  0.0485  -0.0299 130 SER C CA  
5317 C  C   . SER C 130 ? 0.3488 0.3981 0.4264 -0.0495 0.0136  -0.0035 130 SER C C   
5318 O  O   . SER C 130 ? 0.3140 0.1555 0.5000 -0.0377 0.0194  -0.0947 130 SER C O   
5319 C  CB  . SER C 130 ? 0.5708 0.5664 0.4450 0.0021  -0.0413 -0.1034 130 SER C CB  
5320 O  OG  . SER C 130 ? 0.7528 0.6131 0.3617 -0.1559 0.0848  0.0484  130 SER C OG  
5321 N  N   . THR C 131 ? 0.3478 0.3288 0.3664 -0.0083 0.0041  0.0407  131 THR C N   
5322 C  CA  . THR C 131 ? 0.2426 0.3161 0.3246 -0.0209 -0.0145 0.0087  131 THR C CA  
5323 C  C   . THR C 131 ? 0.2715 0.2106 0.3700 -0.0177 -0.0135 0.0458  131 THR C C   
5324 O  O   . THR C 131 ? 0.2186 0.2744 0.4049 -0.0469 -0.0125 0.1052  131 THR C O   
5325 C  CB  . THR C 131 ? 0.3213 0.2314 0.3046 -0.1389 0.0300  0.0494  131 THR C CB  
5326 O  OG1 . THR C 131 ? 0.3369 0.2578 0.4940 -0.1108 -0.1013 0.0296  131 THR C OG1 
5327 C  CG2 . THR C 131 ? 0.3204 0.1800 0.3188 -0.0609 0.0080  0.0609  131 THR C CG2 
5328 N  N   . ALA C 132 ? 0.2484 0.1992 0.3547 -0.0066 0.0432  0.0732  132 ALA C N   
5329 C  CA  . ALA C 132 ? 0.1984 0.1434 0.3853 -0.0122 0.0666  0.0539  132 ALA C CA  
5330 C  C   . ALA C 132 ? 0.1965 0.1492 0.3822 -0.0240 0.0883  0.1276  132 ALA C C   
5331 O  O   . ALA C 132 ? 0.2335 0.1981 0.3854 0.0194  0.0656  0.1219  132 ALA C O   
5332 C  CB  . ALA C 132 ? 0.2332 0.1866 0.2664 0.0139  0.0292  0.0954  132 ALA C CB  
5333 N  N   . SER C 133 ? 0.2315 0.1227 0.4120 -0.0114 0.1076  0.1315  133 SER C N   
5334 C  CA  . SER C 133 ? 0.1923 0.1525 0.4031 0.0167  0.0974  0.0749  133 SER C CA  
5335 C  C   . SER C 133 ? 0.1923 0.0651 0.4160 -0.0479 0.0278  0.0008  133 SER C C   
5336 O  O   . SER C 133 ? 0.1658 0.0864 0.4637 -0.0303 0.0333  -0.0430 133 SER C O   
5337 C  CB  . SER C 133 ? 0.2585 0.1155 0.4361 -0.0218 0.1549  0.0679  133 SER C CB  
5338 O  OG  . SER C 133 ? 0.2582 0.1270 0.4554 -0.0314 0.0412  0.0040  133 SER C OG  
5339 N  N   . ASN C 134 ? 0.2405 0.0963 0.4913 0.0073  0.0275  0.0851  134 ASN C N   
5340 C  CA  . ASN C 134 ? 0.1934 0.1112 0.5820 0.0019  -0.0359 0.0504  134 ASN C CA  
5341 C  C   . ASN C 134 ? 0.2852 0.1306 0.5466 0.0012  -0.0274 0.1092  134 ASN C C   
5342 O  O   . ASN C 134 ? 0.2451 0.2400 0.6257 -0.0145 -0.1118 0.1741  134 ASN C O   
5343 C  CB  . ASN C 134 ? 0.3185 0.1236 0.6132 0.0238  -0.0306 0.0230  134 ASN C CB  
5344 C  CG  . ASN C 134 ? 0.3003 0.0862 0.7378 0.0739  -0.0328 0.1313  134 ASN C CG  
5345 O  OD1 . ASN C 134 ? 0.2877 0.1008 0.7517 -0.0276 0.0029  0.0687  134 ASN C OD1 
5346 N  ND2 . ASN C 134 ? 0.3538 0.0336 0.8184 -0.0309 0.0318  0.0322  134 ASN C ND2 
5347 N  N   . LYS C 135 ? 0.2415 0.1886 0.4824 0.0052  0.0396  0.1421  135 LYS C N   
5348 C  CA  . LYS C 135 ? 0.1965 0.2428 0.4803 0.1018  0.0319  0.1160  135 LYS C CA  
5349 C  C   . LYS C 135 ? 0.2052 0.2719 0.2997 0.0233  0.0345  0.1543  135 LYS C C   
5350 O  O   . LYS C 135 ? 0.2055 0.2690 0.3289 0.0274  0.0485  0.1702  135 LYS C O   
5351 C  CB  . LYS C 135 ? 0.2926 0.3883 0.3330 -0.0533 -0.0070 0.1096  135 LYS C CB  
5352 C  CG  . LYS C 135 ? 0.3149 0.4156 0.5323 -0.1230 -0.0554 0.1069  135 LYS C CG  
5353 C  CD  . LYS C 135 ? 0.2834 0.1232 0.6779 -0.0476 -0.0531 0.1399  135 LYS C CD  
5354 C  CE  . LYS C 135 ? 0.2637 0.2155 0.5909 0.0304  -0.0328 0.1003  135 LYS C CE  
5355 N  NZ  . LYS C 135 ? 0.2768 0.3707 0.6524 -0.1130 0.0158  0.1821  135 LYS C NZ  
5356 N  N   . SER C 136 ? 0.3629 0.2970 0.3086 0.0944  0.0838  0.1372  136 SER C N   
5357 C  CA  . SER C 136 ? 0.3137 0.3125 0.2626 0.1333  0.0798  0.1354  136 SER C CA  
5358 C  C   . SER C 136 ? 0.2690 0.3177 0.3292 0.0818  -0.0320 0.1392  136 SER C C   
5359 O  O   . SER C 136 ? 0.2575 0.2755 0.2809 0.0622  0.0296  0.1145  136 SER C O   
5360 C  CB  . SER C 136 ? 0.6115 0.4500 0.2777 0.1628  0.0712  0.2569  136 SER C CB  
5361 O  OG  . SER C 136 ? 0.5845 0.6052 0.2780 0.2881  0.0187  0.1458  136 SER C OG  
5362 N  N   . GLU C 137 ? 0.4032 0.2412 0.1981 0.0832  0.0042  0.0447  137 GLU C N   
5363 C  CA  . GLU C 137 ? 0.3362 0.2604 0.2461 0.1234  0.0089  -0.0023 137 GLU C CA  
5364 C  C   . GLU C 137 ? 0.2595 0.3254 0.2205 0.1251  0.0397  0.0593  137 GLU C C   
5365 O  O   . GLU C 137 ? 0.3027 0.2888 0.2887 0.1465  0.0582  0.1190  137 GLU C O   
5366 C  CB  . GLU C 137 ? 0.2634 0.2976 0.2846 0.0439  0.0388  0.0066  137 GLU C CB  
5367 C  CG  . GLU C 137 ? 0.4419 0.5165 0.2560 0.2137  -0.0505 -0.0853 137 GLU C CG  
5368 N  N   . GLY C 138 ? 0.1711 0.2073 0.1846 0.0710  0.0176  0.1070  138 GLY C N   
5369 C  CA  . GLY C 138 ? 0.1803 0.1848 0.2247 0.0316  0.0008  0.0932  138 GLY C CA  
5370 C  C   . GLY C 138 ? 0.1035 0.1530 0.2585 -0.0106 -0.0064 0.0998  138 GLY C C   
5371 O  O   . GLY C 138 ? 0.1377 0.1984 0.2723 -0.0369 -0.0359 0.1162  138 GLY C O   
5372 N  N   . LEU C 139 ? 0.1302 0.1265 0.1791 -0.0334 -0.0242 0.0445  139 LEU C N   
5373 C  CA  . LEU C 139 ? 0.1320 0.1245 0.1876 -0.0231 0.0091  0.0508  139 LEU C CA  
5374 C  C   . LEU C 139 ? 0.1076 0.1330 0.1873 -0.0046 -0.0274 0.0304  139 LEU C C   
5375 O  O   . LEU C 139 ? 0.1469 0.1527 0.1755 -0.0157 -0.0219 0.0513  139 LEU C O   
5376 C  CB  . LEU C 139 ? 0.1261 0.1101 0.2125 -0.0238 -0.0077 -0.0055 139 LEU C CB  
5377 C  CG  . LEU C 139 ? 0.1514 0.1126 0.2041 -0.0258 -0.0095 -0.0162 139 LEU C CG  
5378 C  CD1 . LEU C 139 ? 0.1397 0.1182 0.2860 -0.0303 0.0111  -0.0313 139 LEU C CD1 
5379 C  CD2 . LEU C 139 ? 0.1760 0.2252 0.2534 -0.0240 -0.0495 -0.0119 139 LEU C CD2 
5380 N  N   . ALA C 140 ? 0.1185 0.1233 0.1974 -0.0227 0.0013  0.0633  140 ALA C N   
5381 C  CA  . ALA C 140 ? 0.0995 0.1338 0.1250 -0.0285 -0.0211 0.0386  140 ALA C CA  
5382 C  C   . ALA C 140 ? 0.1049 0.1277 0.1349 0.0110  -0.0200 0.0508  140 ALA C C   
5383 O  O   . ALA C 140 ? 0.1385 0.1593 0.1482 -0.0368 -0.0313 0.0411  140 ALA C O   
5384 C  CB  . ALA C 140 ? 0.1176 0.1252 0.1834 -0.0070 -0.0286 0.0249  140 ALA C CB  
5385 N  N   . VAL C 141 ? 0.1082 0.1370 0.1374 0.0032  -0.0121 0.0102  141 VAL C N   
5386 C  CA  . VAL C 141 ? 0.1333 0.0844 0.1489 0.0023  -0.0074 0.0125  141 VAL C CA  
5387 C  C   . VAL C 141 ? 0.0996 0.0821 0.1240 0.0075  -0.0162 -0.0001 141 VAL C C   
5388 O  O   . VAL C 141 ? 0.1275 0.1319 0.1545 -0.0238 -0.0364 -0.0066 141 VAL C O   
5389 C  CB  . VAL C 141 ? 0.1381 0.0338 0.1409 0.0092  -0.0205 0.0099  141 VAL C CB  
5390 C  CG1 . VAL C 141 ? 0.1494 0.2286 0.1293 0.0210  -0.0119 0.0300  141 VAL C CG1 
5391 C  CG2 . VAL C 141 ? 0.1821 0.0326 0.2090 0.0193  -0.0583 -0.0129 141 VAL C CG2 
5392 N  N   . LEU C 142 ? 0.1236 0.0917 0.1812 -0.0135 -0.0173 0.0546  142 LEU C N   
5393 C  CA  . LEU C 142 ? 0.1090 0.0760 0.1625 -0.0053 0.0043  0.0163  142 LEU C CA  
5394 C  C   . LEU C 142 ? 0.1125 0.1555 0.1496 0.0364  -0.0040 0.0245  142 LEU C C   
5395 O  O   . LEU C 142 ? 0.1488 0.1431 0.1474 -0.0366 -0.0262 0.0366  142 LEU C O   
5396 C  CB  . LEU C 142 ? 0.0863 0.2188 0.2008 -0.0052 -0.0187 0.0355  142 LEU C CB  
5397 C  CG  . LEU C 142 ? 0.1011 0.1778 0.1941 0.0329  -0.0055 0.0414  142 LEU C CG  
5398 C  CD1 . LEU C 142 ? 0.1324 0.1850 0.2220 0.0468  -0.0043 0.0791  142 LEU C CD1 
5399 C  CD2 . LEU C 142 ? 0.1309 0.1841 0.1983 -0.0166 -0.0105 0.0401  142 LEU C CD2 
5400 N  N   . ALA C 143 ? 0.1582 0.1216 0.1367 0.0117  -0.0076 0.0146  143 ALA C N   
5401 C  CA  . ALA C 143 ? 0.1527 0.0624 0.1643 -0.0080 -0.0186 0.0495  143 ALA C CA  
5402 C  C   . ALA C 143 ? 0.1171 0.0636 0.1178 0.0141  -0.0200 0.0491  143 ALA C C   
5403 O  O   . ALA C 143 ? 0.1383 0.1593 0.1453 -0.0147 -0.0091 -0.0070 143 ALA C O   
5404 C  CB  . ALA C 143 ? 0.1383 0.1121 0.1826 -0.0019 -0.0187 0.0193  143 ALA C CB  
5405 N  N   . VAL C 144 ? 0.1471 0.1011 0.1390 -0.0054 -0.0034 0.0643  144 VAL C N   
5406 C  CA  . VAL C 144 ? 0.1243 0.0965 0.1442 0.0069  -0.0256 0.0702  144 VAL C CA  
5407 C  C   . VAL C 144 ? 0.0970 0.1433 0.2285 0.0391  -0.0342 0.0040  144 VAL C C   
5408 O  O   . VAL C 144 ? 0.1744 0.0821 0.1848 -0.0201 -0.0025 0.0497  144 VAL C O   
5409 C  CB  . VAL C 144 ? 0.1428 0.1293 0.1818 0.0211  -0.0388 0.0899  144 VAL C CB  
5410 C  CG1 . VAL C 144 ? 0.2046 0.1137 0.2142 0.0158  -0.0783 0.0913  144 VAL C CG1 
5411 C  CG2 . VAL C 144 ? 0.1189 0.2171 0.1898 0.0185  -0.0366 0.0423  144 VAL C CG2 
5412 N  N   . LEU C 145 ? 0.1388 0.1234 0.1927 -0.0161 -0.0044 0.0515  145 LEU C N   
5413 C  CA  . LEU C 145 ? 0.1458 0.1405 0.1905 -0.0048 0.0064  0.0543  145 LEU C CA  
5414 C  C   . LEU C 145 ? 0.1737 0.1541 0.2102 -0.0623 0.0184  0.0876  145 LEU C C   
5415 O  O   . LEU C 145 ? 0.2180 0.2113 0.1654 0.0181  -0.0197 0.0624  145 LEU C O   
5416 C  CB  . LEU C 145 ? 0.1661 0.1764 0.1819 -0.0188 -0.0220 0.0804  145 LEU C CB  
5417 C  CG  . LEU C 145 ? 0.2071 0.1162 0.1840 0.0086  -0.0454 0.0579  145 LEU C CG  
5418 C  CD1 . LEU C 145 ? 0.1724 0.2757 0.2109 -0.0584 -0.0034 -0.0039 145 LEU C CD1 
5419 C  CD2 . LEU C 145 ? 0.2210 0.1430 0.2585 0.0411  -0.0486 0.0927  145 LEU C CD2 
5420 N  N   . ILE C 146 ? 0.1789 0.1487 0.1665 -0.0668 -0.0201 0.0421  146 ILE C N   
5421 C  CA  . ILE C 146 ? 0.2160 0.1755 0.1729 -0.0279 0.0118  0.0557  146 ILE C CA  
5422 C  C   . ILE C 146 ? 0.2114 0.1251 0.1757 -0.0070 -0.0190 0.0927  146 ILE C C   
5423 O  O   . ILE C 146 ? 0.2017 0.1773 0.1987 -0.0220 -0.0326 0.0716  146 ILE C O   
5424 C  CB  . ILE C 146 ? 0.1963 0.1893 0.1586 -0.0242 -0.0236 0.0719  146 ILE C CB  
5425 C  CG1 . ILE C 146 ? 0.1904 0.1775 0.2004 -0.0185 0.0035  0.0247  146 ILE C CG1 
5426 C  CG2 . ILE C 146 ? 0.1815 0.2264 0.1665 -0.0469 -0.0546 0.0881  146 ILE C CG2 
5427 C  CD1 . ILE C 146 ? 0.2267 0.2042 0.1686 -0.0650 -0.0003 0.0316  146 ILE C CD1 
5428 N  N   . GLU C 147 ? 0.1798 0.1166 0.2223 -0.0137 -0.0128 0.0980  147 GLU C N   
5429 C  CA  . GLU C 147 ? 0.2087 0.1907 0.2430 -0.0389 -0.0223 0.1324  147 GLU C CA  
5430 C  C   . GLU C 147 ? 0.2400 0.0927 0.2740 -0.0107 -0.0037 0.1376  147 GLU C C   
5431 O  O   . GLU C 147 ? 0.2404 0.2565 0.2569 0.0447  -0.0064 0.1602  147 GLU C O   
5432 C  CB  . GLU C 147 ? 0.2339 0.1992 0.2893 -0.0098 -0.0144 0.0713  147 GLU C CB  
5433 C  CG  . GLU C 147 ? 0.3100 0.0762 0.3687 -0.0310 -0.0539 0.1017  147 GLU C CG  
5434 C  CD  . GLU C 147 ? 0.2444 0.1615 0.4708 -0.0798 -0.0215 0.0512  147 GLU C CD  
5435 O  OE1 . GLU C 147 ? 0.3368 0.1907 0.3617 -0.0814 -0.0502 0.1097  147 GLU C OE1 
5436 O  OE2 . GLU C 147 ? 0.3896 0.1564 0.4937 -0.0151 0.0006  0.0628  147 GLU C OE2 
5437 N  N   . MET C 148 ? 0.2498 0.2214 0.2381 -0.0701 -0.0026 0.1356  148 MET C N   
5438 C  CA  . MET C 148 ? 0.2460 0.2340 0.2679 -0.0379 -0.0036 0.1668  148 MET C CA  
5439 C  C   . MET C 148 ? 0.2951 0.1966 0.3529 -0.0627 -0.0122 0.1505  148 MET C C   
5440 O  O   . MET C 148 ? 0.3416 0.2564 0.3653 -0.0353 -0.0536 0.1037  148 MET C O   
5441 C  CB  . MET C 148 ? 0.2374 0.4819 0.2609 -0.0341 0.0210  0.2295  148 MET C CB  
5442 C  CG  . MET C 148 ? 0.4176 0.4478 0.2891 -0.0965 -0.0339 0.2364  148 MET C CG  
5443 S  SD  . MET C 148 ? 0.4194 0.4642 0.4066 -0.0428 -0.0037 0.2052  148 MET C SD  
5444 N  N   . GLY C 149 ? 0.2778 0.1791 0.3826 -0.0069 0.0348  0.1517  149 GLY C N   
5445 C  CA  . GLY C 149 ? 0.2432 0.1833 0.2770 -0.0081 0.0249  0.1723  149 GLY C CA  
5446 C  C   . GLY C 149 ? 0.2737 0.2912 0.3434 -0.0166 -0.0070 0.1688  149 GLY C C   
5447 O  O   . GLY C 149 ? 0.3274 0.1879 0.3755 -0.0344 -0.0128 0.1436  149 GLY C O   
5448 N  N   . SER C 150 ? 0.2672 0.3163 0.3801 -0.0088 0.0040  0.1225  150 SER C N   
5449 C  CA  . SER C 150 ? 0.2259 0.3074 0.4500 -0.0157 -0.0164 0.0623  150 SER C CA  
5450 C  C   . SER C 150 ? 0.2365 0.2777 0.3133 -0.0102 -0.0576 0.1319  150 SER C C   
5451 O  O   . SER C 150 ? 0.2786 0.2900 0.2692 -0.0289 -0.0119 0.1282  150 SER C O   
5452 C  CB  . SER C 150 ? 0.2447 0.2286 0.7040 0.0423  -0.0571 -0.0621 150 SER C CB  
5453 O  OG  . SER C 150 ? 0.6636 0.2991 0.6729 -0.0606 -0.1667 0.0750  150 SER C OG  
5454 N  N   . PHE C 151 ? 0.2335 0.4953 0.2931 -0.0438 -0.0348 0.1582  151 PHE C N   
5455 C  CA  . PHE C 151 ? 0.2196 0.4313 0.2324 0.0142  -0.0272 0.1135  151 PHE C CA  
5456 C  C   . PHE C 151 ? 0.2655 0.3747 0.2582 -0.0110 -0.0049 0.2163  151 PHE C C   
5457 O  O   . PHE C 151 ? 0.2397 0.4633 0.3034 0.0502  -0.0634 0.1305  151 PHE C O   
5458 C  CB  . PHE C 151 ? 0.2816 0.3262 0.2569 -0.0065 -0.0296 0.1628  151 PHE C CB  
5459 C  CG  . PHE C 151 ? 0.3216 0.3644 0.2469 -0.0063 -0.0802 0.1541  151 PHE C CG  
5460 C  CD1 . PHE C 151 ? 0.3683 0.4109 0.2422 0.0221  -0.0254 0.1318  151 PHE C CD1 
5461 C  CD2 . PHE C 151 ? 0.3264 0.4067 0.2795 -0.0253 -0.0485 0.0370  151 PHE C CD2 
5462 C  CE1 . PHE C 151 ? 0.3199 0.5391 0.2347 -0.0334 -0.0274 0.1726  151 PHE C CE1 
5463 C  CE2 . PHE C 151 ? 0.3073 0.4778 0.3268 -0.0840 -0.0803 0.0967  151 PHE C CE2 
5464 C  CZ  . PHE C 151 ? 0.3565 0.5715 0.2308 0.0741  -0.0423 0.1998  151 PHE C CZ  
5465 N  N   . ASN C 152 ? 0.2886 0.3317 0.2572 0.0331  0.0001  0.1317  152 ASN C N   
5466 C  CA  . ASN C 152 ? 0.2509 0.3657 0.2909 0.0185  -0.0255 0.2136  152 ASN C CA  
5467 C  C   . ASN C 152 ? 0.2866 0.4623 0.2834 0.0029  -0.0072 0.1671  152 ASN C C   
5468 O  O   . ASN C 152 ? 0.2599 0.4453 0.2444 -0.0164 -0.0744 0.1606  152 ASN C O   
5469 C  CB  . ASN C 152 ? 0.2515 0.4525 0.1841 0.0108  -0.0465 0.1872  152 ASN C CB  
5470 C  CG  . ASN C 152 ? 0.1791 0.4873 0.2285 0.0238  -0.0584 0.2349  152 ASN C CG  
5471 O  OD1 . ASN C 152 ? 0.1841 0.4795 0.2707 0.0178  -0.0422 0.1787  152 ASN C OD1 
5472 N  ND2 . ASN C 152 ? 0.2143 0.3524 0.2072 -0.0027 -0.0099 0.1329  152 ASN C ND2 
5473 N  N   . PRO C 153 ? 0.2601 0.5750 0.2744 0.0229  0.0206  0.1447  153 PRO C N   
5474 C  CA  . PRO C 153 ? 0.2546 0.5996 0.2428 0.0162  -0.0333 0.2121  153 PRO C CA  
5475 C  C   . PRO C 153 ? 0.3118 0.6111 0.2250 -0.0707 0.0267  0.1158  153 PRO C C   
5476 O  O   . PRO C 153 ? 0.3186 0.5255 0.2971 -0.0175 -0.0851 0.1883  153 PRO C O   
5477 C  CB  . PRO C 153 ? 0.3068 0.5216 0.3085 -0.0075 -0.0851 0.1260  153 PRO C CB  
5478 C  CG  . PRO C 153 ? 0.2988 0.4329 0.3940 0.0710  -0.0471 0.1985  153 PRO C CG  
5479 C  CD  . PRO C 153 ? 0.2389 0.5908 0.2746 0.0752  0.0268  0.1614  153 PRO C CD  
5480 N  N   . SER C 154 ? 0.2173 0.4579 0.2161 -0.0241 -0.0320 0.1619  154 SER C N   
5481 C  CA  . SER C 154 ? 0.2393 0.4674 0.1830 -0.0136 -0.0030 0.1458  154 SER C CA  
5482 C  C   . SER C 154 ? 0.1801 0.4642 0.2112 -0.0471 0.0042  0.0584  154 SER C C   
5483 O  O   . SER C 154 ? 0.2346 0.5572 0.2397 -0.1075 -0.0816 0.1339  154 SER C O   
5484 C  CB  . SER C 154 ? 0.3652 0.3994 0.2109 -0.0140 0.0788  0.0851  154 SER C CB  
5485 O  OG  . SER C 154 ? 0.3034 0.4808 0.3557 0.0245  0.0104  0.1793  154 SER C OG  
5486 N  N   . TYR C 155 ? 0.1791 0.4997 0.1884 -0.0092 -0.0380 0.1074  155 TYR C N   
5487 C  CA  . TYR C 155 ? 0.1688 0.4442 0.2174 -0.0416 -0.0585 0.1227  155 TYR C CA  
5488 C  C   . TYR C 155 ? 0.2098 0.5126 0.2041 -0.0732 -0.0673 0.1294  155 TYR C C   
5489 O  O   . TYR C 155 ? 0.2801 0.4920 0.2318 -0.0594 -0.0746 0.1802  155 TYR C O   
5490 C  CB  . TYR C 155 ? 0.1919 0.3956 0.1671 -0.0861 -0.0650 0.1011  155 TYR C CB  
5491 C  CG  . TYR C 155 ? 0.2372 0.3630 0.1543 -0.0835 -0.0358 0.1142  155 TYR C CG  
5492 C  CD1 . TYR C 155 ? 0.1938 0.3768 0.1821 -0.0521 -0.0570 0.0945  155 TYR C CD1 
5493 C  CD2 . TYR C 155 ? 0.2374 0.3495 0.2336 -0.1150 -0.0536 0.1416  155 TYR C CD2 
5494 C  CE1 . TYR C 155 ? 0.2311 0.2091 0.1840 -0.0621 -0.0571 0.1180  155 TYR C CE1 
5495 C  CE2 . TYR C 155 ? 0.2084 0.1986 0.2547 -0.0392 -0.0683 0.1317  155 TYR C CE2 
5496 C  CZ  . TYR C 155 ? 0.1884 0.2728 0.2033 -0.0260 -0.0930 0.1057  155 TYR C CZ  
5497 O  OH  . TYR C 155 ? 0.2268 0.2687 0.2051 -0.0726 -0.0811 0.1174  155 TYR C OH  
5498 N  N   . ASP C 156 ? 0.2439 0.5587 0.1880 -0.0754 -0.0513 0.1310  156 ASP C N   
5499 C  CA  . ASP C 156 ? 0.2564 0.5612 0.1782 -0.1386 -0.0232 0.1266  156 ASP C CA  
5500 C  C   . ASP C 156 ? 0.1714 0.6231 0.3225 -0.0957 -0.0564 0.1284  156 ASP C C   
5501 O  O   . ASP C 156 ? 0.3506 0.6348 0.2653 -0.1696 -0.0480 0.1868  156 ASP C O   
5502 C  CB  . ASP C 156 ? 0.2672 0.6113 0.2175 -0.0947 -0.0368 0.1787  156 ASP C CB  
5503 C  CG  . ASP C 156 ? 0.3296 0.6293 0.2037 -0.0243 -0.0480 0.1710  156 ASP C CG  
5504 O  OD1 . ASP C 156 ? 0.2966 0.4792 0.2544 -0.0878 -0.0609 0.1960  156 ASP C OD1 
5505 O  OD2 . ASP C 156 ? 0.4677 0.5455 0.2191 -0.0738 -0.1013 0.1587  156 ASP C OD2 
5506 N  N   . LYS C 157 ? 0.1755 0.4376 0.2376 -0.0769 -0.1072 0.1461  157 LYS C N   
5507 C  CA  . LYS C 157 ? 0.2053 0.5709 0.2636 -0.1342 -0.0565 0.1293  157 LYS C CA  
5508 C  C   . LYS C 157 ? 0.2523 0.5705 0.2834 -0.1450 -0.0996 0.1304  157 LYS C C   
5509 O  O   . LYS C 157 ? 0.2881 0.5909 0.3077 -0.1212 -0.1262 0.1705  157 LYS C O   
5510 C  CB  . LYS C 157 ? 0.2574 0.5586 0.2514 -0.1201 -0.0688 0.1326  157 LYS C CB  
5511 C  CG  . LYS C 157 ? 0.3087 0.5902 0.2128 -0.0081 -0.0396 0.1051  157 LYS C CG  
5512 C  CD  . LYS C 157 ? 0.3510 0.4144 0.2635 -0.0017 -0.0153 0.1025  157 LYS C CD  
5513 C  CE  . LYS C 157 ? 0.2949 0.4863 0.3444 0.1313  0.0263  0.1207  157 LYS C CE  
5514 N  NZ  . LYS C 157 ? 0.2696 0.6272 0.2940 0.0573  -0.0223 0.0381  157 LYS C NZ  
5515 N  N   . ILE C 158 ? 0.2549 0.5511 0.2015 -0.0502 -0.0392 0.1738  158 ILE C N   
5516 C  CA  . ILE C 158 ? 0.2685 0.4742 0.1941 -0.0741 -0.0622 0.1590  158 ILE C CA  
5517 C  C   . ILE C 158 ? 0.2815 0.4853 0.1870 -0.0754 -0.1008 0.0978  158 ILE C C   
5518 O  O   . ILE C 158 ? 0.3349 0.4586 0.1823 -0.0961 -0.0540 0.0758  158 ILE C O   
5519 C  CB  . ILE C 158 ? 0.3805 0.5321 0.1735 0.0373  -0.0525 0.1460  158 ILE C CB  
5520 C  CG1 . ILE C 158 ? 0.4014 0.6084 0.2236 0.0354  -0.0111 0.0825  158 ILE C CG1 
5521 C  CG2 . ILE C 158 ? 0.2527 0.4399 0.2020 -0.0547 -0.0233 0.0639  158 ILE C CG2 
5522 C  CD1 . ILE C 158 ? 0.3999 0.5392 0.1915 0.1188  0.0238  0.0701  158 ILE C CD1 
5523 N  N   . PHE C 159 ? 0.3028 0.5701 0.2185 -0.1344 -0.0634 0.1737  159 PHE C N   
5524 C  CA  . PHE C 159 ? 0.2995 0.6081 0.1918 -0.1448 -0.0655 0.0466  159 PHE C CA  
5525 C  C   . PHE C 159 ? 0.3425 0.6071 0.1949 -0.1847 -0.0895 0.1149  159 PHE C C   
5526 O  O   . PHE C 159 ? 0.3491 0.6637 0.1821 -0.1796 -0.0926 0.1182  159 PHE C O   
5527 C  CB  . PHE C 159 ? 0.3621 0.4738 0.2064 -0.1398 -0.1280 0.1074  159 PHE C CB  
5528 C  CG  . PHE C 159 ? 0.2966 0.4813 0.1787 -0.0972 -0.0882 0.1074  159 PHE C CG  
5529 C  CD1 . PHE C 159 ? 0.2550 0.4031 0.1911 -0.1453 -0.0811 0.0847  159 PHE C CD1 
5530 C  CD2 . PHE C 159 ? 0.1999 0.4148 0.2236 -0.0480 -0.0822 0.0877  159 PHE C CD2 
5531 C  CE1 . PHE C 159 ? 0.3224 0.4566 0.1821 -0.0619 -0.1087 0.0736  159 PHE C CE1 
5532 C  CE2 . PHE C 159 ? 0.2240 0.5079 0.2108 -0.0332 -0.0848 0.1050  159 PHE C CE2 
5533 C  CZ  . PHE C 159 ? 0.2332 0.4398 0.1961 -0.0243 -0.0653 0.0752  159 PHE C CZ  
5534 N  N   . SER C 160 ? 0.3009 0.7027 0.2102 -0.1925 -0.0809 0.2168  160 SER C N   
5535 C  CA  . SER C 160 ? 0.3085 0.6704 0.1951 -0.1373 -0.0570 -0.0010 160 SER C CA  
5536 C  C   . SER C 160 ? 0.4285 0.6894 0.2060 -0.0647 -0.1333 0.0701  160 SER C C   
5537 O  O   . SER C 160 ? 0.3305 0.7349 0.1851 -0.0311 -0.1031 0.0835  160 SER C O   
5538 C  CB  . SER C 160 ? 0.3283 0.7554 0.1952 -0.1124 -0.0690 0.1403  160 SER C CB  
5539 O  OG  . SER C 160 ? 0.2767 0.7036 0.2886 0.0518  -0.0295 0.2591  160 SER C OG  
5540 N  N   . HIS C 161 ? 0.2483 0.7023 0.2764 -0.0709 -0.1266 0.1163  161 HIS C N   
5541 C  CA  . HIS C 161 ? 0.2800 0.6190 0.2340 -0.0691 -0.0688 0.1220  161 HIS C CA  
5542 C  C   . HIS C 161 ? 0.2116 0.6971 0.2970 -0.0804 -0.0380 0.1283  161 HIS C C   
5543 O  O   . HIS C 161 ? 0.3831 0.7113 0.3019 -0.1834 -0.2093 0.1191  161 HIS C O   
5544 C  CB  . HIS C 161 ? 0.2796 0.6890 0.2893 -0.0463 -0.0379 0.0943  161 HIS C CB  
5545 C  CG  . HIS C 161 ? 0.2042 0.5340 0.3209 -0.1342 -0.0291 0.0377  161 HIS C CG  
5546 N  ND1 . HIS C 161 ? 0.1625 0.5447 0.3489 -0.0522 -0.0833 0.1137  161 HIS C ND1 
5547 C  CD2 . HIS C 161 ? 0.3949 0.5574 0.2411 -0.0283 -0.1243 0.0441  161 HIS C CD2 
5548 C  CE1 . HIS C 161 ? 0.2994 0.4421 0.3374 -0.0794 -0.0894 0.0546  161 HIS C CE1 
5549 N  NE2 . HIS C 161 ? 0.3515 0.6237 0.3023 -0.1158 -0.1289 -0.0098 161 HIS C NE2 
5550 N  N   . LEU C 162 ? 0.3340 0.7390 0.2415 -0.2122 -0.0724 0.1368  162 LEU C N   
5551 C  CA  . LEU C 162 ? 0.3549 0.7400 0.4867 -0.1478 -0.2154 0.0115  162 LEU C CA  
5552 C  C   . LEU C 162 ? 0.4427 0.8341 0.4413 -0.1515 -0.1101 0.0509  162 LEU C C   
5553 O  O   . LEU C 162 ? 0.5705 0.7493 0.3360 -0.2689 -0.1667 0.2308  162 LEU C O   
5554 C  CB  . LEU C 162 ? 0.3585 0.6761 0.5202 -0.2367 -0.0489 -0.0055 162 LEU C CB  
5555 C  CG  . LEU C 162 ? 0.3571 0.7971 0.5174 -0.0904 -0.1280 -0.0222 162 LEU C CG  
5556 C  CD1 . LEU C 162 ? 0.3119 0.7144 0.4420 -0.0768 -0.0107 -0.0425 162 LEU C CD1 
5557 C  CD2 . LEU C 162 ? 0.6233 0.6458 0.3888 0.0109  -0.3012 -0.0455 162 LEU C CD2 
5558 N  N   . GLN C 163 ? 0.3352 0.8339 0.5223 -0.3001 -0.0837 0.1523  163 GLN C N   
5559 C  CA  . GLN C 163 ? 0.4625 0.6552 0.4957 -0.2270 0.0347  0.2372  163 GLN C CA  
5560 C  C   . GLN C 163 ? 0.4041 0.7889 0.3538 -0.1967 -0.1151 -0.0096 163 GLN C C   
5561 O  O   . GLN C 163 ? 0.2933 0.4859 0.6900 -0.1446 -0.2333 0.1042  163 GLN C O   
5562 C  CB  . GLN C 163 ? 0.7921 0.8176 0.3748 -0.1327 -0.1685 0.1487  163 GLN C CB  
5563 C  CG  . GLN C 163 ? 1.0621 0.1733 0.6474 -0.2716 -0.0446 0.2033  163 GLN C CG  
5564 C  CD  . GLN C 163 ? 0.9995 0.3888 0.6207 -0.3134 -0.2159 0.2248  163 GLN C CD  
5565 O  OE1 . GLN C 163 ? 1.0465 0.3865 0.7646 -0.3185 -0.0781 0.1061  163 GLN C OE1 
5566 N  NE2 . GLN C 163 ? 0.6152 0.6488 0.5777 -0.2004 -0.1071 0.1480  163 GLN C NE2 
5567 N  N   . HIS C 164 ? 0.3980 0.8403 0.1348 -0.1953 -0.1311 0.0987  164 HIS C N   
5568 C  CA  . HIS C 164 ? 0.3501 0.8166 0.2187 -0.1069 0.0344  0.0482  164 HIS C CA  
5569 C  C   . HIS C 164 ? 0.3539 0.7419 0.2717 -0.1417 -0.0776 -0.0160 164 HIS C C   
5570 O  O   . HIS C 164 ? 0.4666 0.8123 0.2790 -0.2631 -0.1715 -0.0501 164 HIS C O   
5571 C  CB  . HIS C 164 ? 0.2825 0.7266 0.2669 -0.1340 -0.0708 0.1379  164 HIS C CB  
5572 C  CG  . HIS C 164 ? 0.1859 0.7292 0.3348 -0.1829 -0.0756 0.1767  164 HIS C CG  
5573 N  ND1 . HIS C 164 ? 0.2311 0.9907 0.3708 -0.2314 -0.0537 0.0751  164 HIS C ND1 
5574 C  CD2 . HIS C 164 ? 0.2748 0.7619 0.4930 -0.0548 -0.2591 0.2233  164 HIS C CD2 
5575 C  CE1 . HIS C 164 ? 0.3860 1.0928 0.3608 -0.2489 -0.0629 0.2634  164 HIS C CE1 
5576 N  NE2 . HIS C 164 ? 0.2964 0.9823 0.4392 -0.2451 -0.0828 0.3027  164 HIS C NE2 
5577 N  N   . VAL C 165 ? 0.2967 0.9705 0.3203 -0.0033 -0.1017 -0.1050 165 VAL C N   
5578 C  CA  . VAL C 165 ? 0.2597 0.7105 0.3737 -0.0153 -0.0209 -0.1093 165 VAL C CA  
5579 C  C   . VAL C 165 ? 0.3197 0.5583 0.3052 0.2121  0.0587  -0.0239 165 VAL C C   
5580 O  O   . VAL C 165 ? 0.5118 0.4785 0.2250 -0.3019 -0.0844 0.0829  165 VAL C O   
5581 C  CB  . VAL C 165 ? 0.3055 0.5705 0.3394 0.0396  -0.0891 -0.0920 165 VAL C CB  
5582 C  CG1 . VAL C 165 ? 0.2884 0.7169 0.2658 0.0479  -0.0267 -0.0671 165 VAL C CG1 
5583 C  CG2 . VAL C 165 ? 0.2775 0.5700 0.3276 -0.0076 -0.1370 -0.0468 165 VAL C CG2 
5584 N  N   . LYS C 166 ? 0.3517 0.7720 0.2534 -0.0249 0.0201  -0.1383 166 LYS C N   
5585 C  CA  . LYS C 166 ? 0.3001 0.8802 0.2576 0.1208  0.0050  -0.0467 166 LYS C CA  
5586 C  C   . LYS C 166 ? 0.2542 0.6373 0.2372 -0.0296 -0.0222 -0.0876 166 LYS C C   
5587 O  O   . LYS C 166 ? 0.2958 0.8169 0.2585 0.1095  -0.0793 -0.1524 166 LYS C O   
5588 C  CB  . LYS C 166 ? 0.3847 0.9751 0.2632 0.0250  -0.1011 0.0022  166 LYS C CB  
5589 C  CG  . LYS C 166 ? 0.4583 1.1650 0.3745 -0.1351 -0.1764 -0.0269 166 LYS C CG  
5590 C  CD  . LYS C 166 ? 0.6763 1.2264 0.4063 -0.0662 0.0539  -0.2105 166 LYS C CD  
5591 C  CE  . LYS C 166 ? 0.6995 1.5882 0.6149 0.1033  0.2795  0.2277  166 LYS C CE  
5592 N  NZ  . LYS C 166 ? 0.9326 1.2565 0.3197 -0.0728 -0.0095 -0.2204 166 LYS C NZ  
5593 N  N   . TYR C 167 ? 0.3028 0.5778 0.2518 0.0283  0.0100  -0.0703 167 TYR C N   
5594 C  CA  . TYR C 167 ? 0.3607 0.4509 0.1753 -0.0158 -0.1837 -0.0352 167 TYR C CA  
5595 C  C   . TYR C 167 ? 0.3394 0.4249 0.2649 0.1208  -0.0486 -0.1567 167 TYR C C   
5596 O  O   . TYR C 167 ? 0.3672 0.5153 0.2490 0.1979  -0.0316 -0.0765 167 TYR C O   
5597 C  CB  . TYR C 167 ? 0.2811 0.7128 0.2326 -0.0133 -0.1246 -0.1280 167 TYR C CB  
5598 C  CG  . TYR C 167 ? 0.3365 0.8913 0.2340 0.0317  -0.0214 -0.1058 167 TYR C CG  
5599 C  CD1 . TYR C 167 ? 0.3475 1.0072 0.3040 0.0354  -0.1260 -0.0055 167 TYR C CD1 
5600 C  CD2 . TYR C 167 ? 0.4355 0.7411 0.2545 0.0281  -0.0463 -0.1650 167 TYR C CD2 
5601 C  CE1 . TYR C 167 ? 0.3461 1.1177 0.4392 -0.0486 -0.0520 0.0178  167 TYR C CE1 
5602 C  CE2 . TYR C 167 ? 0.3939 1.0704 0.2113 0.0092  -0.0688 -0.0886 167 TYR C CE2 
5603 C  CZ  . TYR C 167 ? 0.3788 1.1302 0.2901 -0.0414 -0.0072 -0.0462 167 TYR C CZ  
5604 O  OH  . TYR C 167 ? 0.4734 1.2227 0.2380 -0.0294 -0.0139 0.0234  167 TYR C OH  
5605 N  N   . LYS C 168 ? 0.4759 0.1736 0.2530 -0.0734 -0.0429 -0.0484 168 LYS C N   
5606 C  CA  . LYS C 168 ? 0.3440 0.3171 0.3446 0.1149  0.0817  -0.0507 168 LYS C CA  
5607 C  C   . LYS C 168 ? 0.4669 0.6082 0.4778 -0.0602 0.0844  -0.0658 168 LYS C C   
5608 O  O   . LYS C 168 ? 0.4519 0.6987 0.4372 0.2139  -0.0214 -0.0353 168 LYS C O   
5609 C  CB  . LYS C 168 ? 0.3730 0.2314 0.3741 0.1575  0.0150  -0.1198 168 LYS C CB  
5610 C  CG  . LYS C 168 ? 0.8029 0.2127 0.5156 0.1304  0.1596  -0.0790 168 LYS C CG  
5611 C  CD  . LYS C 168 ? 0.6323 0.0719 0.4972 -0.0080 0.2152  0.0027  168 LYS C CD  
5612 C  CE  . LYS C 168 ? 0.5889 0.3739 0.5607 0.0571  0.2485  0.1397  168 LYS C CE  
5613 N  NZ  . LYS C 168 ? 0.6757 0.5166 0.9085 0.0675  0.0495  0.1630  168 LYS C NZ  
5614 N  N   . GLY C 169 ? 0.5782 0.4980 0.5527 -0.0945 0.2035  -0.2240 169 GLY C N   
5615 C  CA  . GLY C 169 ? 0.6203 0.5053 0.5583 -0.0797 0.0859  -0.1500 169 GLY C CA  
5616 C  C   . GLY C 169 ? 0.7154 0.3893 0.5479 -0.2401 0.0240  -0.1151 169 GLY C C   
5617 O  O   . GLY C 169 ? 0.7498 0.6263 0.8865 -0.4075 0.0480  -0.0450 169 GLY C O   
5618 N  N   . GLN C 170 ? 0.4860 0.5560 0.4476 -0.3221 0.0198  0.0793  170 GLN C N   
5619 C  CA  . GLN C 170 ? 0.5287 0.5835 0.3759 -0.0328 -0.0824 -0.2988 170 GLN C CA  
5620 C  C   . GLN C 170 ? 0.3905 0.7008 0.1855 0.0996  -0.1202 -0.1244 170 GLN C C   
5621 O  O   . GLN C 170 ? 0.3105 0.5707 0.2127 0.0674  -0.0737 -0.1446 170 GLN C O   
5622 C  CB  . GLN C 170 ? 0.4934 0.9435 0.6917 -0.2084 -0.0611 -0.1113 170 GLN C CB  
5623 C  CG  . GLN C 170 ? 0.3063 0.9669 0.5789 -0.3667 -0.0606 -0.0905 170 GLN C CG  
5624 C  CD  . GLN C 170 ? 0.6284 1.1952 0.5179 -0.3143 -0.0421 -0.0961 170 GLN C CD  
5625 O  OE1 . GLN C 170 ? 0.5223 1.1235 0.2717 -0.1582 -0.0688 -0.1566 170 GLN C OE1 
5626 N  NE2 . GLN C 170 ? 0.5868 1.0802 0.5478 -0.4133 0.2034  -0.0860 170 GLN C NE2 
5627 N  N   . GLU C 171 ? 0.3247 0.6448 0.3747 0.0972  -0.0787 -0.2807 171 GLU C N   
5628 C  CA  . GLU C 171 ? 0.1812 0.6019 0.2606 0.0125  -0.0659 -0.1330 171 GLU C CA  
5629 C  C   . GLU C 171 ? 0.2565 0.5224 0.2498 -0.0637 0.0165  -0.0992 171 GLU C C   
5630 O  O   . GLU C 171 ? 0.4577 0.7277 0.2649 0.2074  -0.1288 -0.0893 171 GLU C O   
5631 C  CB  . GLU C 171 ? 0.3481 0.5604 0.4288 0.0675  0.0305  -0.1069 171 GLU C CB  
5632 C  CG  . GLU C 171 ? 0.5324 0.3646 0.4896 -0.1586 -0.0122 -0.0214 171 GLU C CG  
5633 C  CD  . GLU C 171 ? 0.5291 0.5276 0.5737 -0.0569 0.3238  -0.0565 171 GLU C CD  
5634 O  OE1 . GLU C 171 ? 0.4597 0.4163 0.7343 -0.0944 0.1280  -0.3339 171 GLU C OE1 
5635 O  OE2 . GLU C 171 ? 0.8493 0.1679 0.7655 -0.2521 0.2965  -0.1234 171 GLU C OE2 
5636 N  N   . ALA C 172 ? 0.2896 0.3960 0.3428 0.0297  -0.1200 -0.0794 172 ALA C N   
5637 C  CA  . ALA C 172 ? 0.3338 0.5396 0.1986 0.0778  -0.1033 -0.0933 172 ALA C CA  
5638 C  C   . ALA C 172 ? 0.3421 0.5184 0.1322 0.1319  -0.0402 0.0561  172 ALA C C   
5639 O  O   . ALA C 172 ? 0.3377 0.5944 0.1832 0.1280  -0.1055 -0.0549 172 ALA C O   
5640 C  CB  . ALA C 172 ? 0.2837 0.6107 0.2433 0.1617  0.0036  0.0021  172 ALA C CB  
5641 N  N   . PHE C 173 ? 0.2652 0.6476 0.2590 0.1526  -0.1153 -0.0983 173 PHE C N   
5642 C  CA  . PHE C 173 ? 0.3000 0.4279 0.2806 0.0611  -0.0817 -0.0871 173 PHE C CA  
5643 C  C   . PHE C 173 ? 0.3199 0.4128 0.2654 -0.0345 -0.0859 -0.0003 173 PHE C C   
5644 O  O   . PHE C 173 ? 0.2956 0.4913 0.2820 0.0206  -0.0434 0.0260  173 PHE C O   
5645 C  CB  . PHE C 173 ? 0.2733 0.4231 0.2863 0.0737  -0.1344 -0.1312 173 PHE C CB  
5646 C  CG  . PHE C 173 ? 0.4281 0.4832 0.2310 0.0739  -0.1002 -0.0413 173 PHE C CG  
5647 C  CD1 . PHE C 173 ? 0.2282 0.4939 0.2631 0.0457  -0.0839 0.0088  173 PHE C CD1 
5648 C  CD2 . PHE C 173 ? 0.2890 0.4270 0.4347 0.0983  -0.0550 -0.1205 173 PHE C CD2 
5649 C  CE1 . PHE C 173 ? 0.3841 0.4824 0.4119 0.0389  -0.1700 0.0357  173 PHE C CE1 
5650 C  CE2 . PHE C 173 ? 0.5409 0.5177 0.4062 0.0569  -0.0506 -0.0292 173 PHE C CE2 
5651 C  CZ  . PHE C 173 ? 0.2715 0.5639 0.4225 -0.0794 -0.0664 -0.0126 173 PHE C CZ  
5652 N  N   . VAL C 174 ? 0.2555 0.2440 0.3092 0.0527  -0.1410 0.0179  174 VAL C N   
5653 C  CA  . VAL C 174 ? 0.2067 0.2735 0.2911 0.0052  -0.0528 0.0111  174 VAL C CA  
5654 C  C   . VAL C 174 ? 0.1864 0.4254 0.3386 0.0337  -0.0569 0.0423  174 VAL C C   
5655 O  O   . VAL C 174 ? 0.3229 0.6654 0.2538 -0.0373 -0.1156 0.0186  174 VAL C O   
5656 C  CB  . VAL C 174 ? 0.2430 0.4917 0.2694 -0.0706 -0.0469 -0.0410 174 VAL C CB  
5657 C  CG1 . VAL C 174 ? 0.3330 0.5176 0.2579 -0.1441 -0.1327 0.0443  174 VAL C CG1 
5658 C  CG2 . VAL C 174 ? 0.2617 0.4262 0.2275 -0.0463 -0.0775 -0.0873 174 VAL C CG2 
5659 N  N   . PRO C 175 ? 0.2290 0.4153 0.2737 0.0253  -0.0544 0.0274  175 PRO C N   
5660 C  CA  . PRO C 175 ? 0.1894 0.4651 0.2787 0.0424  -0.0632 0.0644  175 PRO C CA  
5661 C  C   . PRO C 175 ? 0.1652 0.5929 0.3092 0.0299  -0.0630 0.0241  175 PRO C C   
5662 O  O   . PRO C 175 ? 0.3768 0.5763 0.2156 -0.1729 -0.1221 0.1015  175 PRO C O   
5663 C  CB  . PRO C 175 ? 0.1782 0.4141 0.2852 -0.0047 -0.0436 0.0651  175 PRO C CB  
5664 C  CG  . PRO C 175 ? 0.2707 0.4356 0.3317 0.1133  -0.0177 0.0311  175 PRO C CG  
5665 C  CD  . PRO C 175 ? 0.3573 0.3356 0.2828 0.1829  0.0233  0.0278  175 PRO C CD  
5666 N  N   . GLY C 176 ? 0.2994 0.4354 0.3377 0.0052  -0.0047 0.0305  176 GLY C N   
5667 C  CA  . GLY C 176 ? 0.2189 0.2658 0.3409 0.0582  -0.0345 0.0509  176 GLY C CA  
5668 C  C   . GLY C 176 ? 0.2304 0.3546 0.2078 -0.0649 -0.0234 0.0606  176 GLY C C   
5669 O  O   . GLY C 176 ? 0.2830 0.4419 0.2459 0.0341  -0.0814 0.0409  176 GLY C O   
5670 N  N   . PHE C 177 ? 0.2544 0.4408 0.2989 0.0058  -0.1130 0.0292  177 PHE C N   
5671 C  CA  . PHE C 177 ? 0.2070 0.4576 0.2381 -0.0609 -0.0665 0.0632  177 PHE C CA  
5672 C  C   . PHE C 177 ? 0.1972 0.4422 0.2301 -0.0425 -0.0736 0.1224  177 PHE C C   
5673 O  O   . PHE C 177 ? 0.1715 0.5418 0.3204 -0.0578 -0.0823 0.2048  177 PHE C O   
5674 C  CB  . PHE C 177 ? 0.1776 0.4806 0.2372 -0.0167 -0.0775 0.1236  177 PHE C CB  
5675 C  CG  . PHE C 177 ? 0.1546 0.5360 0.2260 -0.0076 -0.0660 0.0859  177 PHE C CG  
5676 C  CD1 . PHE C 177 ? 0.2128 0.5019 0.1556 -0.0763 0.0006  0.0469  177 PHE C CD1 
5677 C  CD2 . PHE C 177 ? 0.2056 0.4651 0.2733 -0.0772 -0.0943 0.1745  177 PHE C CD2 
5678 C  CE1 . PHE C 177 ? 0.1913 0.7106 0.2644 -0.0980 -0.0208 0.0510  177 PHE C CE1 
5679 C  CE2 . PHE C 177 ? 0.1787 0.5992 0.2846 -0.0651 -0.0826 0.0913  177 PHE C CE2 
5680 C  CZ  . PHE C 177 ? 0.2667 0.5791 0.2042 -0.0979 -0.0688 0.1230  177 PHE C CZ  
5681 N  N   . ASN C 178 ? 0.1854 0.4498 0.2825 -0.0514 -0.0661 0.1345  178 ASN C N   
5682 C  CA  . ASN C 178 ? 0.1507 0.4310 0.2791 0.0033  -0.0605 0.0961  178 ASN C CA  
5683 C  C   . ASN C 178 ? 0.1776 0.4397 0.2846 0.0046  -0.1130 0.1283  178 ASN C C   
5684 O  O   . ASN C 178 ? 0.2097 0.4293 0.2625 -0.0011 -0.0842 0.1193  178 ASN C O   
5685 C  CB  . ASN C 178 ? 0.2069 0.4662 0.2895 0.0469  -0.0629 0.0978  178 ASN C CB  
5686 C  CG  . ASN C 178 ? 0.1574 0.2889 0.3045 0.0040  -0.0138 0.0401  178 ASN C CG  
5687 O  OD1 . ASN C 178 ? 0.1553 0.5586 0.3603 0.0388  -0.0507 0.1956  178 ASN C OD1 
5688 N  ND2 . ASN C 178 ? 0.3226 0.3104 0.3089 0.0363  -0.0588 0.0593  178 ASN C ND2 
5689 N  N   . ILE C 179 ? 0.1701 0.4322 0.2798 0.0178  -0.0723 0.0868  179 ILE C N   
5690 C  CA  . ILE C 179 ? 0.1721 0.4037 0.2886 -0.0152 -0.0847 0.2035  179 ILE C CA  
5691 C  C   . ILE C 179 ? 0.1559 0.3862 0.1909 0.0320  -0.0107 0.1747  179 ILE C C   
5692 O  O   . ILE C 179 ? 0.1564 0.3061 0.2566 -0.0451 -0.0519 0.1338  179 ILE C O   
5693 C  CB  . ILE C 179 ? 0.1117 0.3937 0.2935 -0.0526 -0.0882 0.1885  179 ILE C CB  
5694 C  CG1 . ILE C 179 ? 0.1575 0.4953 0.2606 -0.0773 -0.0583 0.1429  179 ILE C CG1 
5695 C  CG2 . ILE C 179 ? 0.1442 0.3786 0.2771 0.0160  -0.0646 0.1719  179 ILE C CG2 
5696 C  CD1 . ILE C 179 ? 0.2214 0.5447 0.2579 0.0400  -0.0757 0.1395  179 ILE C CD1 
5697 N  N   . GLU C 180 ? 0.1700 0.4134 0.2342 0.0027  -0.0074 0.1257  180 GLU C N   
5698 C  CA  . GLU C 180 ? 0.2041 0.4390 0.2317 -0.0147 0.0034  0.1683  180 GLU C CA  
5699 C  C   . GLU C 180 ? 0.1933 0.3577 0.2890 0.0022  -0.0482 0.2128  180 GLU C C   
5700 O  O   . GLU C 180 ? 0.1664 0.3829 0.2863 0.0387  -0.0304 0.1177  180 GLU C O   
5701 C  CB  . GLU C 180 ? 0.1988 0.5639 0.2292 0.0604  -0.0276 0.1230  180 GLU C CB  
5702 C  CG  . GLU C 180 ? 0.2847 0.4911 0.2500 0.1315  -0.0271 0.1204  180 GLU C CG  
5703 C  CD  . GLU C 180 ? 0.2696 0.4643 0.2552 0.0829  0.0273  0.1850  180 GLU C CD  
5704 O  OE1 . GLU C 180 ? 0.2674 0.4817 0.3687 0.0779  0.0480  0.0704  180 GLU C OE1 
5705 O  OE2 . GLU C 180 ? 0.3809 0.4573 0.3525 0.1762  0.0694  0.0576  180 GLU C OE2 
5706 N  N   . GLU C 181 ? 0.1543 0.4135 0.2943 0.0046  -0.0023 0.1750  181 GLU C N   
5707 C  CA  . GLU C 181 ? 0.1439 0.3953 0.3274 -0.0096 -0.0323 0.1910  181 GLU C CA  
5708 C  C   . GLU C 181 ? 0.1517 0.3572 0.2631 0.0024  0.0100  0.1428  181 GLU C C   
5709 O  O   . GLU C 181 ? 0.1421 0.3637 0.3378 -0.0103 -0.0114 0.1452  181 GLU C O   
5710 C  CB  . GLU C 181 ? 0.1909 0.4238 0.3102 0.0222  -0.0491 0.1715  181 GLU C CB  
5711 C  CG  . GLU C 181 ? 0.2019 0.4807 0.4177 0.0484  -0.0598 0.2005  181 GLU C CG  
5712 C  CD  . GLU C 181 ? 0.3303 0.6772 0.4210 0.0819  -0.0670 0.1482  181 GLU C CD  
5713 O  OE1 . GLU C 181 ? 0.2081 0.7871 0.3364 0.0231  -0.0634 0.1812  181 GLU C OE1 
5714 O  OE2 . GLU C 181 ? 0.3152 0.4787 0.5268 -0.0809 -0.1865 0.2496  181 GLU C OE2 
5715 N  N   . LEU C 182 ? 0.1703 0.3754 0.2031 -0.0080 -0.0423 0.1333  182 LEU C N   
5716 C  CA  . LEU C 182 ? 0.1804 0.2433 0.2266 -0.0122 -0.0179 0.1190  182 LEU C CA  
5717 C  C   . LEU C 182 ? 0.1629 0.2861 0.2326 -0.0204 -0.0079 0.1248  182 LEU C C   
5718 O  O   . LEU C 182 ? 0.1729 0.2300 0.2606 -0.0066 -0.0363 0.1198  182 LEU C O   
5719 C  CB  . LEU C 182 ? 0.2094 0.2781 0.1901 -0.0145 -0.0203 0.1153  182 LEU C CB  
5720 C  CG  . LEU C 182 ? 0.2107 0.2656 0.2056 -0.0323 -0.0596 0.1312  182 LEU C CG  
5721 C  CD1 . LEU C 182 ? 0.2487 0.2828 0.2966 -0.0245 -0.0686 0.1297  182 LEU C CD1 
5722 C  CD2 . LEU C 182 ? 0.1647 0.3701 0.1884 -0.0601 -0.0369 0.0965  182 LEU C CD2 
5723 N  N   . LEU C 183 ? 0.1553 0.3392 0.1941 0.0107  -0.0308 0.1240  183 LEU C N   
5724 C  CA  . LEU C 183 ? 0.1967 0.1967 0.2114 0.0464  -0.0209 0.1158  183 LEU C CA  
5725 C  C   . LEU C 183 ? 0.1951 0.2448 0.1715 -0.0025 -0.0310 0.1149  183 LEU C C   
5726 O  O   . LEU C 183 ? 0.2232 0.2843 0.2854 0.0490  -0.0522 0.1558  183 LEU C O   
5727 C  CB  . LEU C 183 ? 0.2273 0.2428 0.2218 -0.0048 -0.0147 0.0895  183 LEU C CB  
5728 C  CG  . LEU C 183 ? 0.1907 0.2436 0.2653 0.0012  -0.0027 0.0469  183 LEU C CG  
5729 C  CD1 . LEU C 183 ? 0.3204 0.1667 0.2882 -0.0116 0.0592  0.0355  183 LEU C CD1 
5730 C  CD2 . LEU C 183 ? 0.2148 0.2241 0.2286 0.0256  -0.0228 0.0629  183 LEU C CD2 
5731 N  N   . PRO C 184 ? 0.1679 0.1614 0.2808 0.0005  -0.0179 0.1238  184 PRO C N   
5732 C  CA  . PRO C 184 ? 0.1923 0.1880 0.2910 -0.0418 -0.0574 0.0792  184 PRO C CA  
5733 C  C   . PRO C 184 ? 0.2404 0.2539 0.2839 0.0348  -0.0336 0.1571  184 PRO C C   
5734 O  O   . PRO C 184 ? 0.2123 0.2176 0.3441 0.0128  -0.0107 0.0780  184 PRO C O   
5735 C  CB  . PRO C 184 ? 0.1961 0.2630 0.2894 0.0044  -0.0520 0.1118  184 PRO C CB  
5736 C  CG  . PRO C 184 ? 0.2623 0.2207 0.2146 -0.0117 -0.0142 0.0485  184 PRO C CG  
5737 C  CD  . PRO C 184 ? 0.1793 0.2254 0.2176 0.0006  -0.0271 0.1306  184 PRO C CD  
5738 N  N   . GLU C 185 ? 0.3312 0.2414 0.3257 0.0136  -0.0649 0.1986  185 GLU C N   
5739 C  CA  . GLU C 185 ? 0.3260 0.2031 0.3844 -0.0111 0.0008  0.1573  185 GLU C CA  
5740 C  C   . GLU C 185 ? 0.3118 0.1381 0.3896 0.0952  -0.0129 0.1245  185 GLU C C   
5741 O  O   . GLU C 185 ? 0.2417 0.3295 0.3321 0.1078  -0.0093 0.1113  185 GLU C O   
5742 C  CB  . GLU C 185 ? 0.3832 0.1406 0.4056 0.0032  -0.0027 0.1533  185 GLU C CB  
5743 C  CG  . GLU C 185 ? 0.5795 0.1700 0.3603 0.0485  0.1112  0.1380  185 GLU C CG  
5744 C  CD  . GLU C 185 ? 0.5661 0.5091 0.5414 0.1532  0.1259  0.2104  185 GLU C CD  
5745 O  OE1 . GLU C 185 ? 0.8980 0.7156 0.6026 0.0659  0.0431  0.3228  185 GLU C OE1 
5746 O  OE2 . GLU C 185 ? 0.4289 0.5378 0.5517 0.0648  0.0801  0.2474  185 GLU C OE2 
5747 N  N   . ARG C 186 ? 0.3340 0.1877 0.3352 0.0628  -0.0064 0.0886  186 ARG C N   
5748 C  CA  . ARG C 186 ? 0.3216 0.2072 0.3607 0.1320  -0.0158 0.0860  186 ARG C CA  
5749 C  C   . ARG C 186 ? 0.2852 0.1764 0.3646 0.0055  -0.0557 0.0936  186 ARG C C   
5750 O  O   . ARG C 186 ? 0.2523 0.1341 0.3183 0.0485  -0.0188 0.0406  186 ARG C O   
5751 C  CB  . ARG C 186 ? 0.3583 0.1952 0.4356 0.0917  0.0214  0.0608  186 ARG C CB  
5752 C  CG  . ARG C 186 ? 0.4056 0.2279 0.4358 0.1620  0.1065  0.0876  186 ARG C CG  
5753 C  CD  . ARG C 186 ? 0.6262 0.2878 0.6038 -0.0189 0.0132  0.1189  186 ARG C CD  
5754 N  NE  . ARG C 186 ? 0.6735 0.3080 0.7363 -0.0758 0.1153  -0.0661 186 ARG C NE  
5755 C  CZ  . ARG C 186 ? 0.6919 0.6047 0.8970 0.0399  0.0019  0.0582  186 ARG C CZ  
5756 N  NH1 . ARG C 186 ? 0.9000 0.0282 0.7866 0.1018  -0.0547 -0.0463 186 ARG C NH1 
5757 N  NH2 . ARG C 186 ? 1.1831 0.4886 0.9762 -0.0716 0.2187  -0.1142 186 ARG C NH2 
5758 N  N   . THR C 187 ? 0.2103 0.1342 0.2791 0.0768  -0.0003 0.0072  187 THR C N   
5759 C  CA  . THR C 187 ? 0.2469 0.1798 0.2006 0.0515  0.0683  0.0502  187 THR C CA  
5760 C  C   . THR C 187 ? 0.2107 0.2009 0.2307 0.0861  0.0044  0.0653  187 THR C C   
5761 O  O   . THR C 187 ? 0.2042 0.2115 0.2554 0.0866  -0.0153 0.0834  187 THR C O   
5762 C  CB  . THR C 187 ? 0.1821 0.3079 0.2799 0.0507  0.0135  0.0254  187 THR C CB  
5763 O  OG1 . THR C 187 ? 0.2083 0.3718 0.2834 0.0930  -0.0254 0.0567  187 THR C OG1 
5764 C  CG2 . THR C 187 ? 0.3060 0.0844 0.2920 0.0092  0.0059  0.0316  187 THR C CG2 
5765 N  N   . ALA C 188 ? 0.1679 0.2340 0.2521 0.0740  0.0035  0.0012  188 ALA C N   
5766 C  CA  . ALA C 188 ? 0.2148 0.2423 0.2673 0.1416  -0.0225 0.0008  188 ALA C CA  
5767 C  C   . ALA C 188 ? 0.1828 0.1768 0.2585 0.0999  -0.0084 0.0305  188 ALA C C   
5768 O  O   . ALA C 188 ? 0.2124 0.1388 0.2563 0.0644  -0.0471 0.0100  188 ALA C O   
5769 C  CB  . ALA C 188 ? 0.2436 0.2203 0.2987 0.1514  -0.0108 0.0072  188 ALA C CB  
5770 N  N   . GLU C 189 ? 0.1995 0.1021 0.2644 0.0544  -0.0168 -0.0075 189 GLU C N   
5771 C  CA  . GLU C 189 ? 0.2040 0.0832 0.2352 0.0447  -0.0163 0.0272  189 GLU C CA  
5772 C  C   . GLU C 189 ? 0.2046 0.0944 0.2649 0.0322  -0.0194 0.0117  189 GLU C C   
5773 O  O   . GLU C 189 ? 0.1923 0.1419 0.2225 0.0373  -0.0032 0.0484  189 GLU C O   
5774 C  CB  . GLU C 189 ? 0.2354 0.0992 0.2964 0.0587  0.0000  0.0597  189 GLU C CB  
5775 C  CG  . GLU C 189 ? 0.2787 0.1428 0.3847 0.0873  0.0186  0.0130  189 GLU C CG  
5776 C  CD  . GLU C 189 ? 0.3531 0.2103 0.5305 0.0876  0.0441  0.1096  189 GLU C CD  
5777 O  OE1 . GLU C 189 ? 0.3357 0.1051 0.6650 0.0401  0.0928  0.0901  189 GLU C OE1 
5778 O  OE2 . GLU C 189 ? 0.5011 0.1577 0.6018 0.0609  -0.0210 0.0669  189 GLU C OE2 
5779 N  N   . TYR C 190 ? 0.1685 0.1039 0.1765 0.0443  0.0001  -0.0107 190 TYR C N   
5780 C  CA  . TYR C 190 ? 0.1413 0.0939 0.1954 0.0449  -0.0064 0.0040  190 TYR C CA  
5781 C  C   . TYR C 190 ? 0.1690 0.0864 0.1823 0.0576  -0.0030 0.0201  190 TYR C C   
5782 O  O   . TYR C 190 ? 0.1780 0.1189 0.2290 0.0355  0.0006  -0.0272 190 TYR C O   
5783 C  CB  . TYR C 190 ? 0.1282 0.1247 0.1728 0.0436  0.0080  0.0088  190 TYR C CB  
5784 C  CG  . TYR C 190 ? 0.1311 0.0451 0.2350 0.0326  0.0365  0.0544  190 TYR C CG  
5785 C  CD1 . TYR C 190 ? 0.1762 0.1046 0.1837 0.0345  0.0106  0.0453  190 TYR C CD1 
5786 C  CD2 . TYR C 190 ? 0.1635 0.1674 0.2120 0.0928  0.0148  -0.0053 190 TYR C CD2 
5787 C  CE1 . TYR C 190 ? 0.1823 0.1221 0.1832 0.0579  0.0137  0.0094  190 TYR C CE1 
5788 C  CE2 . TYR C 190 ? 0.1639 0.1196 0.2701 0.0446  0.0351  0.0098  190 TYR C CE2 
5789 C  CZ  . TYR C 190 ? 0.1815 0.2198 0.1961 0.0857  0.0300  0.0032  190 TYR C CZ  
5790 O  OH  . TYR C 190 ? 0.2110 0.2211 0.2209 0.0986  0.0450  0.0215  190 TYR C OH  
5791 N  N   . TYR C 191 ? 0.1215 0.0687 0.2268 0.0251  -0.0098 0.0009  191 TYR C N   
5792 C  CA  . TYR C 191 ? 0.1496 0.1029 0.1645 0.0257  -0.0167 -0.0013 191 TYR C CA  
5793 C  C   . TYR C 191 ? 0.1234 0.1532 0.1415 0.0066  -0.0044 0.0131  191 TYR C C   
5794 O  O   . TYR C 191 ? 0.1787 0.1001 0.1579 0.0322  -0.0292 0.0033  191 TYR C O   
5795 C  CB  . TYR C 191 ? 0.1453 0.0665 0.2065 0.0010  0.0000  -0.0128 191 TYR C CB  
5796 C  CG  . TYR C 191 ? 0.1693 0.0292 0.2139 0.0109  -0.0381 -0.0022 191 TYR C CG  
5797 C  CD1 . TYR C 191 ? 0.1557 0.1124 0.1990 -0.0166 0.0064  -0.0381 191 TYR C CD1 
5798 C  CD2 . TYR C 191 ? 0.2131 0.0457 0.2033 0.0362  0.0061  0.0078  191 TYR C CD2 
5799 C  CE1 . TYR C 191 ? 0.2073 0.0812 0.2196 -0.0145 -0.0329 0.0089  191 TYR C CE1 
5800 C  CE2 . TYR C 191 ? 0.2159 0.0227 0.1999 0.0223  -0.0231 -0.0008 191 TYR C CE2 
5801 C  CZ  . TYR C 191 ? 0.1694 0.1067 0.2078 0.0013  -0.0099 0.0032  191 TYR C CZ  
5802 O  OH  . TYR C 191 ? 0.1962 0.0929 0.2790 -0.0206 0.0026  -0.0052 191 TYR C OH  
5803 N  N   . ARG C 192 ? 0.1731 0.0753 0.1417 0.0424  -0.0091 -0.0035 192 ARG C N   
5804 C  CA  . ARG C 192 ? 0.1592 0.0952 0.1460 0.0411  0.0024  -0.0002 192 ARG C CA  
5805 C  C   . ARG C 192 ? 0.1388 0.1392 0.0979 0.0286  -0.0174 -0.0041 192 ARG C C   
5806 O  O   . ARG C 192 ? 0.1537 0.1045 0.1485 0.0212  -0.0300 -0.0242 192 ARG C O   
5807 C  CB  . ARG C 192 ? 0.1694 0.1887 0.1821 0.0598  0.0159  0.0035  192 ARG C CB  
5808 C  CG  . ARG C 192 ? 0.1647 0.2083 0.1634 -0.0024 0.0155  -0.0271 192 ARG C CG  
5809 C  CD  . ARG C 192 ? 0.1735 0.1983 0.1603 0.0205  -0.0103 -0.0201 192 ARG C CD  
5810 N  NE  . ARG C 192 ? 0.1726 0.2433 0.1920 0.0457  0.0076  -0.0100 192 ARG C NE  
5811 C  CZ  . ARG C 192 ? 0.1794 0.2083 0.1851 0.0218  0.0212  -0.0356 192 ARG C CZ  
5812 N  NH1 . ARG C 192 ? 0.1927 0.3375 0.1961 0.0192  0.0575  0.0057  192 ARG C NH1 
5813 N  NH2 . ARG C 192 ? 0.1577 0.2178 0.2295 0.0130  0.0064  -0.0329 192 ARG C NH2 
5814 N  N   . TYR C 193 ? 0.1399 0.1374 0.1456 0.0263  -0.0117 -0.0157 193 TYR C N   
5815 C  CA  . TYR C 193 ? 0.1198 0.1523 0.1282 0.0159  -0.0272 -0.0283 193 TYR C CA  
5816 C  C   . TYR C 193 ? 0.1399 0.1272 0.1171 0.0294  -0.0279 0.0221  193 TYR C C   
5817 O  O   . TYR C 193 ? 0.1613 0.1197 0.1259 0.0378  -0.0414 0.0081  193 TYR C O   
5818 C  CB  . TYR C 193 ? 0.1309 0.1326 0.1471 0.0061  -0.0050 -0.0421 193 TYR C CB  
5819 C  CG  . TYR C 193 ? 0.1622 0.1258 0.1266 0.0151  -0.0052 -0.0251 193 TYR C CG  
5820 C  CD1 . TYR C 193 ? 0.1516 0.1481 0.1223 -0.0134 -0.0002 -0.0212 193 TYR C CD1 
5821 C  CD2 . TYR C 193 ? 0.1525 0.1331 0.1356 0.0219  -0.0195 -0.0369 193 TYR C CD2 
5822 C  CE1 . TYR C 193 ? 0.1248 0.0699 0.1243 0.0168  -0.0121 -0.0089 193 TYR C CE1 
5823 C  CE2 . TYR C 193 ? 0.1320 0.1320 0.1031 0.0212  -0.0092 0.0052  193 TYR C CE2 
5824 C  CZ  . TYR C 193 ? 0.1287 0.0677 0.1236 0.0122  -0.0031 0.0069  193 TYR C CZ  
5825 O  OH  . TYR C 193 ? 0.1254 0.0771 0.1284 0.0190  -0.0034 -0.0006 193 TYR C OH  
5826 N  N   . ARG C 194 ? 0.1525 0.0939 0.0979 0.0104  -0.0232 0.0107  194 ARG C N   
5827 C  CA  . ARG C 194 ? 0.1804 0.1044 0.1336 -0.0152 -0.0011 -0.0047 194 ARG C CA  
5828 C  C   . ARG C 194 ? 0.1582 0.1098 0.1288 0.0071  -0.0114 0.0252  194 ARG C C   
5829 O  O   . ARG C 194 ? 0.1567 0.0893 0.1670 0.0331  -0.0362 0.0052  194 ARG C O   
5830 C  CB  . ARG C 194 ? 0.1897 0.1643 0.1405 0.0195  0.0353  0.0293  194 ARG C CB  
5831 C  CG  . ARG C 194 ? 0.2419 0.2337 0.1778 0.0875  0.0435  0.0148  194 ARG C CG  
5832 C  CD  . ARG C 194 ? 0.4453 0.4264 0.2143 0.0603  0.1701  0.0328  194 ARG C CD  
5833 N  NE  . ARG C 194 ? 0.4712 0.5686 0.4501 0.1671  0.1190  -0.0042 194 ARG C NE  
5834 C  CZ  . ARG C 194 ? 0.4993 0.8070 0.3206 0.1219  0.0994  -0.0668 194 ARG C CZ  
5835 N  NH1 . ARG C 194 ? 0.7458 0.8784 0.1746 0.2146  -0.0619 -0.0326 194 ARG C NH1 
5836 N  NH2 . ARG C 194 ? 0.5070 0.7579 0.4931 0.0722  0.2717  -0.0118 194 ARG C NH2 
5837 N  N   . GLY C 195 ? 0.1679 0.0785 0.1345 0.0329  -0.0022 0.0093  195 GLY C N   
5838 C  CA  . GLY C 195 ? 0.1513 0.0631 0.1546 0.0094  0.0061  -0.0172 195 GLY C CA  
5839 C  C   . GLY C 195 ? 0.1560 0.0647 0.0924 -0.0104 -0.0290 0.0316  195 GLY C C   
5840 O  O   . GLY C 195 ? 0.1541 0.0660 0.1287 0.0104  0.0212  -0.0010 195 GLY C O   
5841 N  N   . SER C 196 ? 0.1539 0.0365 0.1338 -0.0019 -0.0054 -0.0135 196 SER C N   
5842 C  CA  . SER C 196 ? 0.1563 0.0525 0.1198 0.0000  -0.0015 -0.0273 196 SER C CA  
5843 C  C   . SER C 196 ? 0.1484 0.1038 0.1198 -0.0324 0.0238  -0.0006 196 SER C C   
5844 O  O   . SER C 196 ? 0.1356 0.1103 0.1172 -0.0150 -0.0005 0.0245  196 SER C O   
5845 C  CB  . SER C 196 ? 0.1420 0.0602 0.1528 0.0024  -0.0096 0.0240  196 SER C CB  
5846 O  OG  . SER C 196 ? 0.1200 0.0886 0.1478 -0.0170 -0.0179 0.0050  196 SER C OG  
5847 N  N   . LEU C 197 ? 0.1578 0.0533 0.1557 -0.0019 -0.0059 0.0055  197 LEU C N   
5848 C  CA  . LEU C 197 ? 0.1688 0.0563 0.1430 -0.0251 0.0280  0.0109  197 LEU C CA  
5849 C  C   . LEU C 197 ? 0.1549 0.0844 0.1270 0.0005  0.0132  0.0039  197 LEU C C   
5850 O  O   . LEU C 197 ? 0.1699 0.0152 0.1675 -0.0219 -0.0189 -0.0055 197 LEU C O   
5851 C  CB  . LEU C 197 ? 0.1930 0.0985 0.2084 -0.0223 -0.0037 -0.0424 197 LEU C CB  
5852 C  CG  . LEU C 197 ? 0.1898 0.0207 0.2623 -0.0095 -0.0438 0.0335  197 LEU C CG  
5853 C  CD1 . LEU C 197 ? 0.2631 0.1280 0.2343 -0.0656 -0.0057 -0.0163 197 LEU C CD1 
5854 C  CD2 . LEU C 197 ? 0.2530 0.1746 0.2419 -0.0815 -0.0444 -0.0001 197 LEU C CD2 
5855 N  N   . THR C 198 ? 0.1600 0.0389 0.1334 -0.0217 0.0219  -0.0034 198 THR C N   
5856 C  CA  . THR C 198 ? 0.1571 0.0626 0.1390 -0.0212 0.0140  0.0089  198 THR C CA  
5857 C  C   . THR C 198 ? 0.1751 0.0945 0.1416 -0.0456 0.0061  -0.0154 198 THR C C   
5858 O  O   . THR C 198 ? 0.1690 0.0485 0.1890 -0.0462 -0.0018 -0.0136 198 THR C O   
5859 C  CB  . THR C 198 ? 0.1282 0.0467 0.1197 -0.0136 -0.0148 -0.0030 198 THR C CB  
5860 O  OG1 . THR C 198 ? 0.1525 0.0868 0.1266 -0.0380 -0.0167 -0.0212 198 THR C OG1 
5861 C  CG2 . THR C 198 ? 0.1243 0.0830 0.1428 0.0148  -0.0176 -0.0256 198 THR C CG2 
5862 N  N   . THR C 199 ? 0.1372 0.1047 0.1830 -0.0156 -0.0522 -0.0516 199 THR C N   
5863 C  CA  . THR C 199 ? 0.1848 0.1072 0.1227 -0.0409 -0.0215 -0.0278 199 THR C CA  
5864 C  C   . THR C 199 ? 0.1439 0.1139 0.1640 -0.0351 -0.0245 -0.0170 199 THR C C   
5865 O  O   . THR C 199 ? 0.1717 0.0939 0.1620 -0.0292 -0.0087 0.0008  199 THR C O   
5866 C  CB  . THR C 199 ? 0.1794 0.0514 0.1884 -0.0455 -0.0397 -0.0026 199 THR C CB  
5867 O  OG1 . THR C 199 ? 0.1735 0.0615 0.2217 -0.0500 -0.0247 0.0080  199 THR C OG1 
5868 C  CG2 . THR C 199 ? 0.1848 0.0611 0.1909 -0.0121 -0.0739 0.0080  199 THR C CG2 
5869 N  N   . PRO C 200 ? 0.1408 0.0597 0.1654 -0.0499 -0.0194 0.0164  200 PRO C N   
5870 C  CA  . PRO C 200 ? 0.1696 0.0353 0.1973 -0.0474 0.0222  -0.0100 200 PRO C CA  
5871 C  C   . PRO C 200 ? 0.1682 0.0358 0.2204 -0.0280 -0.0314 -0.0348 200 PRO C C   
5872 O  O   . PRO C 200 ? 0.2001 0.0754 0.2159 -0.0597 -0.0303 0.0008  200 PRO C O   
5873 C  CB  . PRO C 200 ? 0.1801 0.0794 0.1938 -0.0330 0.0015  -0.0369 200 PRO C CB  
5874 C  CG  . PRO C 200 ? 0.2128 0.0379 0.1858 -0.0308 0.0111  -0.0241 200 PRO C CG  
5875 C  CD  . PRO C 200 ? 0.2285 0.0478 0.1686 -0.0196 -0.0078 0.0020  200 PRO C CD  
5876 N  N   . PRO C 201 ? 0.1926 0.0742 0.2261 0.0044  -0.0158 -0.0133 201 PRO C N   
5877 C  CA  . PRO C 201 ? 0.2024 0.0482 0.2035 -0.0568 -0.0348 0.0194  201 PRO C CA  
5878 C  C   . PRO C 201 ? 0.2288 0.0401 0.2064 -0.0447 -0.0225 0.0087  201 PRO C C   
5879 O  O   . PRO C 201 ? 0.2078 0.0258 0.2117 -0.0178 0.0005  0.0068  201 PRO C O   
5880 C  CB  . PRO C 201 ? 0.1670 0.0523 0.2694 -0.0413 -0.0159 0.0131  201 PRO C CB  
5881 C  CG  . PRO C 201 ? 0.2078 0.1473 0.3292 -0.0826 -0.0608 0.1179  201 PRO C CG  
5882 C  CD  . PRO C 201 ? 0.1825 0.0935 0.2626 -0.0472 -0.0802 0.0266  201 PRO C CD  
5883 N  N   . CYS C 202 ? 0.1600 0.0381 0.1865 -0.0585 0.0011  0.0070  202 CYS C N   
5884 C  CA  . CYS C 202 ? 0.1463 0.0680 0.2103 -0.0583 0.0066  -0.0093 202 CYS C CA  
5885 C  C   . CYS C 202 ? 0.1223 0.0744 0.2060 -0.0001 -0.0006 -0.0311 202 CYS C C   
5886 O  O   . CYS C 202 ? 0.1272 0.0563 0.2022 -0.0108 -0.0078 -0.0037 202 CYS C O   
5887 C  CB  . CYS C 202 ? 0.1516 0.0854 0.1725 -0.0457 -0.0184 0.0200  202 CYS C CB  
5888 S  SG  . CYS C 202 ? 0.2297 0.0163 0.1762 -0.0397 -0.0048 -0.0030 202 CYS C SG  
5889 N  N   . ASN C 203 ? 0.1126 0.0893 0.1967 0.0215  0.0156  -0.0016 203 ASN C N   
5890 C  CA  . ASN C 203 ? 0.1754 0.0496 0.2175 -0.0588 0.0323  -0.0047 203 ASN C CA  
5891 C  C   . ASN C 203 ? 0.1586 0.0601 0.1848 -0.0172 -0.0065 -0.0013 203 ASN C C   
5892 O  O   . ASN C 203 ? 0.1643 0.1032 0.1923 0.0046  0.0107  0.0423  203 ASN C O   
5893 C  CB  . ASN C 203 ? 0.1582 0.0917 0.2831 -0.0564 0.0400  0.0035  203 ASN C CB  
5894 C  CG  . ASN C 203 ? 0.1822 0.0970 0.2676 -0.0305 -0.0069 -0.0003 203 ASN C CG  
5895 O  OD1 . ASN C 203 ? 0.2105 0.0850 0.3180 -0.0433 0.0142  -0.0341 203 ASN C OD1 
5896 N  ND2 . ASN C 203 ? 0.2428 0.1347 0.4132 -0.0577 0.0394  0.0628  203 ASN C ND2 
5897 N  N   . PRO C 204 ? 0.1936 0.0459 0.1837 0.0066  0.0072  0.0324  204 PRO C N   
5898 C  CA  . PRO C 204 ? 0.1568 0.0929 0.1905 0.0330  -0.0105 -0.0019 204 PRO C CA  
5899 C  C   . PRO C 204 ? 0.1385 0.0776 0.1814 -0.0006 0.0009  0.0353  204 PRO C C   
5900 O  O   . PRO C 204 ? 0.1823 0.1719 0.1758 0.0332  -0.0038 0.0091  204 PRO C O   
5901 C  CB  . PRO C 204 ? 0.1384 0.0835 0.2196 0.0205  -0.0158 0.0334  204 PRO C CB  
5902 C  CG  . PRO C 204 ? 0.2181 0.0855 0.2164 0.0107  -0.0052 0.0537  204 PRO C CG  
5903 C  CD  . PRO C 204 ? 0.2214 0.1033 0.1999 0.0163  -0.0162 0.0758  204 PRO C CD  
5904 N  N   . THR C 205 ? 0.1180 0.1063 0.2090 -0.0086 -0.0044 0.0249  205 THR C N   
5905 C  CA  . THR C 205 ? 0.1322 0.0703 0.2152 0.0052  0.0172  0.0295  205 THR C CA  
5906 C  C   . THR C 205 ? 0.1485 0.0902 0.2342 0.0418  0.0317  0.0260  205 THR C C   
5907 O  O   . THR C 205 ? 0.1577 0.0739 0.2514 0.0254  0.0176  0.0518  205 THR C O   
5908 C  CB  . THR C 205 ? 0.1920 0.0780 0.2390 -0.0554 0.0476  0.0731  205 THR C CB  
5909 O  OG1 . THR C 205 ? 0.1816 0.0769 0.2512 -0.0198 0.0157  0.0512  205 THR C OG1 
5910 C  CG2 . THR C 205 ? 0.2234 0.1087 0.2529 -0.0086 -0.0080 0.0688  205 THR C CG2 
5911 N  N   . VAL C 206 ? 0.1525 0.0942 0.1918 0.0292  0.0047  0.0379  206 VAL C N   
5912 C  CA  . VAL C 206 ? 0.1617 0.0650 0.1503 0.0193  0.0069  0.0111  206 VAL C CA  
5913 C  C   . VAL C 206 ? 0.1229 0.0525 0.1945 -0.0170 0.0042  0.0252  206 VAL C C   
5914 O  O   . VAL C 206 ? 0.1342 0.1033 0.1877 -0.0111 -0.0128 0.0097  206 VAL C O   
5915 C  CB  . VAL C 206 ? 0.1349 0.0832 0.1503 -0.0152 -0.0130 0.0257  206 VAL C CB  
5916 C  CG1 . VAL C 206 ? 0.1448 0.1056 0.1621 0.0223  -0.0020 0.0400  206 VAL C CG1 
5917 C  CG2 . VAL C 206 ? 0.1492 0.0793 0.1909 -0.0225 -0.0025 0.0118  206 VAL C CG2 
5918 N  N   . LEU C 207 ? 0.1556 0.1160 0.1582 0.0170  -0.0001 -0.0044 207 LEU C N   
5919 C  CA  . LEU C 207 ? 0.1268 0.0830 0.1782 0.0036  -0.0060 0.0168  207 LEU C CA  
5920 C  C   . LEU C 207 ? 0.1189 0.0794 0.1560 0.0173  -0.0143 0.0047  207 LEU C C   
5921 O  O   . LEU C 207 ? 0.1348 0.1108 0.1391 0.0097  -0.0141 0.0167  207 LEU C O   
5922 C  CB  . LEU C 207 ? 0.1823 0.1280 0.2010 0.0469  0.0255  0.0136  207 LEU C CB  
5923 C  CG  . LEU C 207 ? 0.2148 0.1517 0.2380 0.0585  -0.0413 -0.0137 207 LEU C CG  
5924 C  CD1 . LEU C 207 ? 0.3581 0.1826 0.2534 0.0517  -0.1100 0.0447  207 LEU C CD1 
5925 C  CD2 . LEU C 207 ? 0.2834 0.2487 0.4011 0.1086  0.0446  -0.0669 207 LEU C CD2 
5926 N  N   . TRP C 208 ? 0.1327 0.0789 0.1442 0.0010  0.0016  0.0153  208 TRP C N   
5927 C  CA  . TRP C 208 ? 0.0968 0.0384 0.1761 0.0162  -0.0149 0.0323  208 TRP C CA  
5928 C  C   . TRP C 208 ? 0.1352 0.0410 0.1480 0.0088  -0.0227 0.0089  208 TRP C C   
5929 O  O   . TRP C 208 ? 0.1561 0.1359 0.1446 0.0159  -0.0091 -0.0140 208 TRP C O   
5930 C  CB  . TRP C 208 ? 0.0997 0.1179 0.1302 0.0272  -0.0049 -0.0003 208 TRP C CB  
5931 C  CG  . TRP C 208 ? 0.1270 0.1130 0.1078 0.0095  0.0100  0.0054  208 TRP C CG  
5932 C  CD1 . TRP C 208 ? 0.1293 0.0924 0.1496 0.0020  -0.0207 -0.0247 208 TRP C CD1 
5933 C  CD2 . TRP C 208 ? 0.1117 0.0830 0.1078 0.0127  -0.0121 -0.0124 208 TRP C CD2 
5934 N  NE1 . TRP C 208 ? 0.1423 0.1076 0.1036 0.0044  -0.0087 -0.0027 208 TRP C NE1 
5935 C  CE2 . TRP C 208 ? 0.1306 0.0769 0.1265 0.0089  -0.0089 0.0084  208 TRP C CE2 
5936 C  CE3 . TRP C 208 ? 0.1348 0.1011 0.1157 -0.0391 -0.0010 0.0234  208 TRP C CE3 
5937 C  CZ2 . TRP C 208 ? 0.1426 0.0604 0.1234 -0.0144 0.0002  0.0275  208 TRP C CZ2 
5938 C  CZ3 . TRP C 208 ? 0.1410 0.0475 0.1349 -0.0088 -0.0179 -0.0018 208 TRP C CZ3 
5939 C  CH2 . TRP C 208 ? 0.1733 0.0348 0.1363 -0.0134 0.0033  0.0277  208 TRP C CH2 
5940 N  N   . THR C 209 ? 0.1654 0.0844 0.1667 0.0312  -0.0185 0.0171  209 THR C N   
5941 C  CA  . THR C 209 ? 0.1248 0.0723 0.1528 0.0100  0.0055  -0.0006 209 THR C CA  
5942 C  C   . THR C 209 ? 0.0897 0.2020 0.1444 0.0307  -0.0287 0.0256  209 THR C C   
5943 O  O   . THR C 209 ? 0.1288 0.0820 0.1609 -0.0201 -0.0290 0.0103  209 THR C O   
5944 C  CB  . THR C 209 ? 0.1301 0.0848 0.1826 -0.0012 0.0119  0.0081  209 THR C CB  
5945 O  OG1 . THR C 209 ? 0.1268 0.1187 0.1638 0.0192  0.0097  0.0119  209 THR C OG1 
5946 C  CG2 . THR C 209 ? 0.1531 0.0879 0.1970 0.0087  -0.0026 0.0097  209 THR C CG2 
5947 N  N   . VAL C 210 ? 0.1024 0.1487 0.1439 0.0219  0.0021  0.0155  210 VAL C N   
5948 C  CA  . VAL C 210 ? 0.0909 0.0902 0.1638 -0.0015 -0.0008 0.0013  210 VAL C CA  
5949 C  C   . VAL C 210 ? 0.1078 0.0927 0.1614 0.0120  -0.0199 0.0057  210 VAL C C   
5950 O  O   . VAL C 210 ? 0.1401 0.1252 0.1965 0.0126  -0.0337 -0.0158 210 VAL C O   
5951 C  CB  . VAL C 210 ? 0.0949 0.0542 0.1646 0.0156  -0.0078 0.0130  210 VAL C CB  
5952 C  CG1 . VAL C 210 ? 0.1259 0.1334 0.1552 -0.0025 -0.0053 0.0120  210 VAL C CG1 
5953 C  CG2 . VAL C 210 ? 0.1653 0.0642 0.1941 0.0518  -0.0264 -0.0005 210 VAL C CG2 
5954 N  N   . PHE C 211 ? 0.1334 0.0697 0.1987 0.0017  -0.0293 0.0226  211 PHE C N   
5955 C  CA  . PHE C 211 ? 0.0963 0.0763 0.1668 0.0187  -0.0111 0.0201  211 PHE C CA  
5956 C  C   . PHE C 211 ? 0.1614 0.1010 0.1830 -0.0318 -0.0266 -0.0192 211 PHE C C   
5957 O  O   . PHE C 211 ? 0.1826 0.0771 0.1998 -0.0185 -0.0037 0.0324  211 PHE C O   
5958 C  CB  . PHE C 211 ? 0.1045 0.1058 0.2228 -0.0127 -0.0410 0.0596  211 PHE C CB  
5959 C  CG  . PHE C 211 ? 0.1029 0.1229 0.2193 -0.0015 -0.0177 0.0515  211 PHE C CG  
5960 C  CD1 . PHE C 211 ? 0.1571 0.2128 0.2157 0.0376  -0.0041 0.1007  211 PHE C CD1 
5961 C  CD2 . PHE C 211 ? 0.1525 0.1532 0.1724 -0.0091 -0.0430 0.0577  211 PHE C CD2 
5962 C  CE1 . PHE C 211 ? 0.1333 0.2210 0.2013 0.0342  -0.0190 0.0743  211 PHE C CE1 
5963 C  CE2 . PHE C 211 ? 0.1377 0.1810 0.2247 0.0160  -0.0168 0.0663  211 PHE C CE2 
5964 C  CZ  . PHE C 211 ? 0.1430 0.2214 0.2357 0.0281  -0.0094 0.0527  211 PHE C CZ  
5965 N  N   . ARG C 212 ? 0.1537 0.0234 0.2256 0.0096  -0.0420 0.0165  212 ARG C N   
5966 C  CA  . ARG C 212 ? 0.1833 0.0278 0.2358 -0.0206 0.0190  0.0229  212 ARG C CA  
5967 C  C   . ARG C 212 ? 0.1936 0.0115 0.2627 0.0074  0.0345  0.0362  212 ARG C C   
5968 O  O   . ARG C 212 ? 0.1877 0.0847 0.2678 -0.0211 0.0320  0.0305  212 ARG C O   
5969 C  CB  . ARG C 212 ? 0.1571 0.0258 0.3243 0.0291  -0.0025 -0.0126 212 ARG C CB  
5970 C  CG  . ARG C 212 ? 0.2643 0.0419 0.3489 -0.0450 -0.0216 -0.0026 212 ARG C CG  
5971 C  CD  . ARG C 212 ? 0.3055 0.0814 0.4307 0.0043  -0.0244 -0.0318 212 ARG C CD  
5972 N  NE  . ARG C 212 ? 0.4116 0.1334 0.4979 -0.1137 -0.0033 -0.0625 212 ARG C NE  
5973 C  CZ  . ARG C 212 ? 0.4417 0.3244 0.6591 -0.1233 -0.0062 -0.2303 212 ARG C CZ  
5974 N  NH1 . ARG C 212 ? 0.4092 0.3245 0.7451 -0.1221 0.0093  -0.0776 212 ARG C NH1 
5975 N  NH2 . ARG C 212 ? 0.5938 0.5414 0.9033 -0.3630 -0.0058 -0.1969 212 ARG C NH2 
5976 N  N   . ASN C 213 ? 0.2128 0.0608 0.2450 0.0195  0.0055  0.0369  213 ASN C N   
5977 C  CA  . ASN C 213 ? 0.2408 0.1074 0.2422 0.0412  0.0157  0.0507  213 ASN C CA  
5978 C  C   . ASN C 213 ? 0.2019 0.1449 0.2288 0.0009  -0.0003 0.0469  213 ASN C C   
5979 O  O   . ASN C 213 ? 0.1963 0.1225 0.2669 0.0364  0.0255  0.0418  213 ASN C O   
5980 C  CB  . ASN C 213 ? 0.2952 0.1038 0.3323 0.0445  -0.0461 0.0947  213 ASN C CB  
5981 C  CG  . ASN C 213 ? 0.2922 0.1439 0.4113 0.0136  0.0143  0.0299  213 ASN C CG  
5982 O  OD1 . ASN C 213 ? 0.3201 0.1894 0.4651 0.0292  0.0472  0.0907  213 ASN C OD1 
5983 N  ND2 . ASN C 213 ? 0.3262 0.1264 0.3360 -0.0395 0.0348  -0.0109 213 ASN C ND2 
5984 N  N   . PRO C 214 ? 0.1600 0.1269 0.2808 0.0068  0.0092  0.0234  214 PRO C N   
5985 C  CA  . PRO C 214 ? 0.2374 0.1291 0.2411 -0.0020 -0.0001 0.0772  214 PRO C CA  
5986 C  C   . PRO C 214 ? 0.2074 0.1794 0.2810 0.0423  -0.0006 0.0545  214 PRO C C   
5987 O  O   . PRO C 214 ? 0.2205 0.1782 0.2883 0.0715  -0.0126 0.0842  214 PRO C O   
5988 C  CB  . PRO C 214 ? 0.2013 0.1342 0.3051 0.0087  -0.0245 0.0237  214 PRO C CB  
5989 C  CG  . PRO C 214 ? 0.2664 0.1197 0.2588 -0.0220 0.0614  0.0440  214 PRO C CG  
5990 C  CD  . PRO C 214 ? 0.2753 0.1694 0.2361 -0.0987 0.0236  0.0142  214 PRO C CD  
5991 N  N   . VAL C 215 ? 0.2367 0.1672 0.1927 0.0354  -0.0077 0.1018  215 VAL C N   
5992 C  CA  . VAL C 215 ? 0.2254 0.2236 0.1891 0.0140  -0.0088 0.1126  215 VAL C CA  
5993 C  C   . VAL C 215 ? 0.2228 0.2500 0.1725 0.0646  -0.0091 0.0501  215 VAL C C   
5994 O  O   . VAL C 215 ? 0.1983 0.1548 0.2750 0.0114  -0.0053 0.1111  215 VAL C O   
5995 C  CB  . VAL C 215 ? 0.2275 0.2483 0.1945 0.0198  -0.0511 0.0938  215 VAL C CB  
5996 C  CG1 . VAL C 215 ? 0.2401 0.1081 0.2274 -0.0097 -0.0184 0.0636  215 VAL C CG1 
5997 C  CG2 . VAL C 215 ? 0.2600 0.2447 0.2743 0.0109  -0.0342 0.1193  215 VAL C CG2 
5998 N  N   . GLN C 216 ? 0.2098 0.2185 0.2146 0.0030  0.0037  0.1066  216 GLN C N   
5999 C  CA  . GLN C 216 ? 0.2026 0.3005 0.2390 -0.0078 0.0022  0.1339  216 GLN C CA  
6000 C  C   . GLN C 216 ? 0.2773 0.2859 0.2847 -0.0009 -0.0332 0.1234  216 GLN C C   
6001 O  O   . GLN C 216 ? 0.2582 0.3215 0.2667 -0.0215 0.0048  0.1430  216 GLN C O   
6002 C  CB  . GLN C 216 ? 0.2422 0.3050 0.3824 -0.0099 -0.0135 0.2010  216 GLN C CB  
6003 C  CG  . GLN C 216 ? 0.3109 0.2369 0.4623 -0.0120 -0.0326 0.1359  216 GLN C CG  
6004 C  CD  . GLN C 216 ? 0.6616 0.1279 0.5424 -0.0513 -0.0447 0.0284  216 GLN C CD  
6005 O  OE1 . GLN C 216 ? 0.3149 0.3754 0.6571 -0.0356 -0.0270 0.1445  216 GLN C OE1 
6006 N  NE2 . GLN C 216 ? 0.7195 0.3719 0.4674 -0.1592 -0.0293 0.1580  216 GLN C NE2 
6007 N  N   . ILE C 217 ? 0.3089 0.1539 0.2512 -0.0423 -0.0031 0.1518  217 ILE C N   
6008 C  CA  . ILE C 217 ? 0.2904 0.2286 0.1625 0.0152  0.0391  0.1201  217 ILE C CA  
6009 C  C   . ILE C 217 ? 0.2449 0.3258 0.1822 -0.0200 0.0111  0.1179  217 ILE C C   
6010 O  O   . ILE C 217 ? 0.2362 0.2731 0.2576 -0.0409 -0.0159 0.1360  217 ILE C O   
6011 C  CB  . ILE C 217 ? 0.2289 0.2573 0.2338 -0.0072 -0.0142 0.1149  217 ILE C CB  
6012 C  CG1 . ILE C 217 ? 0.1731 0.2408 0.1913 -0.0329 0.0115  0.0930  217 ILE C CG1 
6013 C  CG2 . ILE C 217 ? 0.2518 0.2214 0.2139 -0.0362 -0.0219 0.1052  217 ILE C CG2 
6014 C  CD1 . ILE C 217 ? 0.2455 0.2517 0.2283 -0.0615 0.0311  0.1109  217 ILE C CD1 
6015 N  N   . SER C 218 ? 0.2709 0.3524 0.1767 -0.0013 0.0184  0.1641  218 SER C N   
6016 C  CA  . SER C 218 ? 0.2415 0.4011 0.1999 -0.0854 -0.0244 0.1397  218 SER C CA  
6017 C  C   . SER C 218 ? 0.2516 0.3130 0.1769 -0.0251 -0.0341 0.1886  218 SER C C   
6018 O  O   . SER C 218 ? 0.2224 0.3118 0.1628 -0.0126 0.0140  0.1285  218 SER C O   
6019 C  CB  . SER C 218 ? 0.2473 0.4503 0.2224 -0.0244 -0.0402 0.1326  218 SER C CB  
6020 O  OG  . SER C 218 ? 0.3345 0.4385 0.1676 -0.0513 -0.0385 0.1585  218 SER C OG  
6021 N  N   . GLN C 219 ? 0.2480 0.4693 0.2806 -0.0425 0.0040  0.1555  219 GLN C N   
6022 C  CA  . GLN C 219 ? 0.2529 0.3292 0.2789 -0.0606 0.0046  0.1614  219 GLN C CA  
6023 C  C   . GLN C 219 ? 0.2388 0.3217 0.2549 -0.0623 0.0026  0.1984  219 GLN C C   
6024 O  O   . GLN C 219 ? 0.2615 0.3970 0.2142 -0.0001 0.0160  0.0907  219 GLN C O   
6025 C  CB  . GLN C 219 ? 0.4572 0.4379 0.3078 -0.2317 0.0297  0.1468  219 GLN C CB  
6026 C  CG  . GLN C 219 ? 0.3910 0.5345 0.4175 -0.1639 0.0737  0.2309  219 GLN C CG  
6027 C  CD  . GLN C 219 ? 0.6991 0.2832 0.3575 -0.1340 -0.1004 0.1015  219 GLN C CD  
6028 O  OE1 . GLN C 219 ? 0.6269 0.4006 0.4977 -0.2249 -0.0380 0.0729  219 GLN C OE1 
6029 N  NE2 . GLN C 219 ? 0.5198 0.4530 0.4171 0.0331  0.0581  0.2060  219 GLN C NE2 
6030 N  N   . GLU C 220 ? 0.2918 0.5042 0.2268 -0.0430 -0.0184 0.1985  220 GLU C N   
6031 C  CA  . GLU C 220 ? 0.3156 0.4281 0.1782 0.0359  0.0319  0.1473  220 GLU C CA  
6032 C  C   . GLU C 220 ? 0.1744 0.3903 0.1712 0.0372  0.0057  0.0694  220 GLU C C   
6033 O  O   . GLU C 220 ? 0.3054 0.3310 0.1488 -0.0146 -0.0142 0.0860  220 GLU C O   
6034 C  CB  . GLU C 220 ? 0.4191 0.3837 0.2743 0.0824  0.0636  0.2243  220 GLU C CB  
6035 C  CG  . GLU C 220 ? 0.4067 0.3927 0.3014 0.0420  0.0533  0.2169  220 GLU C CG  
6036 C  CD  . GLU C 220 ? 0.3854 0.4841 0.3656 0.0282  0.0985  0.1447  220 GLU C CD  
6037 O  OE1 . GLU C 220 ? 0.3450 0.4353 0.3151 0.0337  0.0727  0.1682  220 GLU C OE1 
6038 O  OE2 . GLU C 220 ? 0.4132 0.4020 0.3204 -0.0025 0.0879  0.0644  220 GLU C OE2 
6039 N  N   . GLN C 221 ? 0.2182 0.3346 0.1660 0.0027  0.0134  0.0819  221 GLN C N   
6040 C  CA  . GLN C 221 ? 0.2667 0.3317 0.1629 -0.0060 0.0055  0.1081  221 GLN C CA  
6041 C  C   . GLN C 221 ? 0.2210 0.3836 0.1453 -0.0219 -0.0245 0.1120  221 GLN C C   
6042 O  O   . GLN C 221 ? 0.2125 0.3965 0.1568 -0.0795 -0.0258 0.0820  221 GLN C O   
6043 C  CB  . GLN C 221 ? 0.2385 0.3248 0.2211 -0.0089 0.0295  0.1534  221 GLN C CB  
6044 C  CG  . GLN C 221 ? 0.3076 0.3632 0.2369 -0.0093 -0.0041 0.1845  221 GLN C CG  
6045 C  CD  . GLN C 221 ? 0.2850 0.2257 0.1877 -0.0773 -0.0345 0.1471  221 GLN C CD  
6046 O  OE1 . GLN C 221 ? 0.2476 0.3102 0.2319 -0.1266 -0.0190 0.0825  221 GLN C OE1 
6047 N  NE2 . GLN C 221 ? 0.2798 0.3389 0.1979 -0.0899 -0.0400 0.1571  221 GLN C NE2 
6048 N  N   . LEU C 222 ? 0.2329 0.4319 0.1488 -0.0303 -0.0217 0.0956  222 LEU C N   
6049 C  CA  . LEU C 222 ? 0.1913 0.4400 0.1474 -0.0692 -0.0631 0.0651  222 LEU C CA  
6050 C  C   . LEU C 222 ? 0.1944 0.4542 0.1179 -0.0333 0.0062  0.1295  222 LEU C C   
6051 O  O   . LEU C 222 ? 0.2002 0.4591 0.1597 -0.0734 -0.0548 0.1200  222 LEU C O   
6052 C  CB  . LEU C 222 ? 0.1938 0.3945 0.1877 -0.1122 -0.0483 0.0951  222 LEU C CB  
6053 C  CG  . LEU C 222 ? 0.2238 0.4084 0.1889 -0.0906 -0.0513 0.1072  222 LEU C CG  
6054 C  CD1 . LEU C 222 ? 0.2518 0.3448 0.1692 -0.0936 -0.0126 0.0467  222 LEU C CD1 
6055 C  CD2 . LEU C 222 ? 0.2399 0.3819 0.2046 -0.1046 -0.0205 0.1085  222 LEU C CD2 
6056 N  N   . LEU C 223 ? 0.2685 0.5097 0.1288 -0.0729 0.0185  0.1408  223 LEU C N   
6057 C  CA  . LEU C 223 ? 0.2399 0.4120 0.2132 -0.0562 0.0336  0.1122  223 LEU C CA  
6058 C  C   . LEU C 223 ? 0.2076 0.4460 0.1252 -0.0241 0.0113  0.1012  223 LEU C C   
6059 O  O   . LEU C 223 ? 0.2982 0.4441 0.1273 -0.0833 0.0030  0.0217  223 LEU C O   
6060 C  CB  . LEU C 223 ? 0.2191 0.4562 0.2308 -0.0061 0.0499  0.1494  223 LEU C CB  
6061 C  CG  . LEU C 223 ? 0.3176 0.5167 0.2566 -0.0075 0.0952  0.1407  223 LEU C CG  
6062 C  CD1 . LEU C 223 ? 0.3439 0.4421 0.2392 -0.0030 0.0759  0.1697  223 LEU C CD1 
6063 C  CD2 . LEU C 223 ? 0.3224 0.4460 0.1930 -0.0025 0.0363  0.1026  223 LEU C CD2 
6064 N  N   . ALA C 224 ? 0.2028 0.4214 0.1852 -0.0275 0.0195  0.0803  224 ALA C N   
6065 C  CA  . ALA C 224 ? 0.2059 0.4367 0.1963 -0.0244 -0.0005 0.0838  224 ALA C CA  
6066 C  C   . ALA C 224 ? 0.1696 0.3972 0.1338 -0.1029 -0.0334 0.0330  224 ALA C C   
6067 O  O   . ALA C 224 ? 0.3479 0.4415 0.1778 -0.1050 -0.0835 -0.0009 224 ALA C O   
6068 C  CB  . ALA C 224 ? 0.2006 0.5489 0.1793 -0.0043 -0.0219 0.0370  224 ALA C CB  
6069 N  N   . LEU C 225 ? 0.2084 0.4357 0.1209 -0.0885 -0.0259 0.0854  225 LEU C N   
6070 C  CA  . LEU C 225 ? 0.2207 0.3352 0.1473 -0.0298 -0.0190 0.0640  225 LEU C CA  
6071 C  C   . LEU C 225 ? 0.1991 0.1958 0.1166 -0.0737 -0.0399 -0.0060 225 LEU C C   
6072 O  O   . LEU C 225 ? 0.3432 0.2440 0.2414 -0.1585 -0.0751 0.0444  225 LEU C O   
6073 C  CB  . LEU C 225 ? 0.2358 0.3094 0.1664 -0.0403 -0.0460 0.0500  225 LEU C CB  
6074 C  CG  . LEU C 225 ? 0.2454 0.3282 0.1336 -0.0927 -0.0885 0.0359  225 LEU C CG  
6075 C  CD1 . LEU C 225 ? 0.2267 0.2259 0.1703 -0.0446 -0.0604 0.0047  225 LEU C CD1 
6076 C  CD2 . LEU C 225 ? 0.1869 0.3610 0.1503 -0.0626 -0.0801 0.0160  225 LEU C CD2 
6077 N  N   . GLU C 226 ? 0.1801 0.4548 0.1428 -0.0959 -0.0308 0.0135  226 GLU C N   
6078 C  CA  . GLU C 226 ? 0.2127 0.3204 0.1645 -0.0818 -0.0570 -0.0078 226 GLU C CA  
6079 C  C   . GLU C 226 ? 0.2882 0.4397 0.1909 -0.0168 -0.0267 -0.0236 226 GLU C C   
6080 O  O   . GLU C 226 ? 0.3109 0.3273 0.1876 -0.0627 -0.0316 -0.0294 226 GLU C O   
6081 C  CB  . GLU C 226 ? 0.2254 0.3955 0.1653 -0.1170 0.0075  -0.0290 226 GLU C CB  
6082 C  CG  . GLU C 226 ? 0.2372 0.2234 0.1550 -0.0648 0.0292  0.0030  226 GLU C CG  
6083 C  CD  . GLU C 226 ? 0.3107 0.2874 0.1460 -0.1280 0.0378  0.0377  226 GLU C CD  
6084 O  OE1 . GLU C 226 ? 0.3130 0.4077 0.1275 -0.0621 -0.0100 0.0882  226 GLU C OE1 
6085 O  OE2 . GLU C 226 ? 0.2222 0.4296 0.1323 -0.0512 -0.0003 0.0684  226 GLU C OE2 
6086 N  N   . THR C 227 ? 0.2715 0.3441 0.1653 -0.0993 -0.0357 -0.0336 227 THR C N   
6087 C  CA  . THR C 227 ? 0.2964 0.4415 0.1733 -0.1348 0.0258  -0.0408 227 THR C CA  
6088 C  C   . THR C 227 ? 0.2599 0.5183 0.2410 -0.0847 -0.0683 -0.0634 227 THR C C   
6089 O  O   . THR C 227 ? 0.4289 0.4714 0.1876 -0.1619 -0.0280 -0.0097 227 THR C O   
6090 C  CB  . THR C 227 ? 0.2751 0.3654 0.1980 -0.1185 0.0234  -0.0440 227 THR C CB  
6091 O  OG1 . THR C 227 ? 0.3733 0.4240 0.1787 -0.0876 -0.0151 0.0337  227 THR C OG1 
6092 C  CG2 . THR C 227 ? 0.3019 0.4032 0.2441 -0.1746 0.0592  -0.0249 227 THR C CG2 
6093 N  N   . ALA C 228 ? 0.2319 0.5837 0.2053 -0.0665 -0.0765 -0.0197 228 ALA C N   
6094 C  CA  . ALA C 228 ? 0.3153 0.4657 0.2901 -0.1421 -0.1035 0.0671  228 ALA C CA  
6095 C  C   . ALA C 228 ? 0.5082 0.3970 0.2593 -0.1426 -0.1527 -0.0702 228 ALA C C   
6096 O  O   . ALA C 228 ? 0.6066 0.4842 0.2487 -0.3195 -0.2268 0.0793  228 ALA C O   
6097 C  CB  . ALA C 228 ? 0.2627 0.6134 0.4300 -0.1296 -0.0864 0.1234  228 ALA C CB  
6098 N  N   . LEU C 229 ? 0.2976 0.3752 0.1801 -0.1632 -0.0469 0.0064  229 LEU C N   
6099 C  CA  . LEU C 229 ? 0.3718 0.3935 0.1973 -0.1218 -0.1068 0.0457  229 LEU C CA  
6100 C  C   . LEU C 229 ? 0.3689 0.3600 0.2101 -0.0977 -0.0592 -0.0425 229 LEU C C   
6101 O  O   . LEU C 229 ? 0.3510 0.6445 0.1733 -0.1079 -0.0279 0.0152  229 LEU C O   
6102 C  CB  . LEU C 229 ? 0.3145 0.4740 0.2218 -0.1738 -0.0822 0.0775  229 LEU C CB  
6103 C  CG  . LEU C 229 ? 0.2372 0.7268 0.2322 -0.1313 -0.0772 -0.0357 229 LEU C CG  
6104 C  CD1 . LEU C 229 ? 0.3052 0.8312 0.1923 -0.0042 -0.0849 0.0473  229 LEU C CD1 
6105 C  CD2 . LEU C 229 ? 0.3961 0.6390 0.3529 -0.1687 -0.2524 0.0299  229 LEU C CD2 
6106 N  N   . TYR C 230 ? 0.4803 0.3773 0.2688 -0.1206 -0.0998 0.0586  230 TYR C N   
6107 C  CA  . TYR C 230 ? 0.3661 0.3988 0.2651 -0.1665 -0.0974 -0.0262 230 TYR C CA  
6108 C  C   . TYR C 230 ? 0.4659 0.4078 0.1936 -0.1036 -0.0613 -0.0508 230 TYR C C   
6109 O  O   . TYR C 230 ? 0.4830 0.1740 0.2451 -0.0351 0.0084  -0.0149 230 TYR C O   
6110 C  CB  . TYR C 230 ? 0.3898 0.4686 0.1976 -0.0594 -0.0312 0.0073  230 TYR C CB  
6111 C  CG  . TYR C 230 ? 0.4730 0.4504 0.2370 -0.0122 -0.0030 0.0790  230 TYR C CG  
6112 C  CD1 . TYR C 230 ? 0.5992 0.3238 0.3270 0.0114  0.1038  -0.0716 230 TYR C CD1 
6113 C  CD2 . TYR C 230 ? 0.6161 0.2004 0.2624 0.0171  0.0597  -0.0067 230 TYR C CD2 
6114 C  CE1 . TYR C 230 ? 0.7177 0.3454 0.4293 -0.0553 0.1107  0.0097  230 TYR C CE1 
6115 C  CE2 . TYR C 230 ? 0.5938 0.3580 0.4738 -0.0480 0.0916  0.1253  230 TYR C CE2 
6116 C  CZ  . TYR C 230 ? 0.8206 0.1453 0.4677 -0.0210 0.1226  -0.1246 230 TYR C CZ  
6117 O  OH  . TYR C 230 ? 0.9693 0.7504 0.6905 -0.1786 0.1879  0.0832  230 TYR C OH  
6118 N  N   . CYS C 231 ? 0.5065 0.4149 0.2421 -0.0884 -0.1111 -0.0428 231 CYS C N   
6119 C  CA  . CYS C 231 ? 0.5568 0.3359 0.1987 0.0337  -0.0251 -0.1012 231 CYS C CA  
6120 C  C   . CYS C 231 ? 0.5502 0.4134 0.2550 -0.0725 -0.0781 -0.0767 231 CYS C C   
6121 O  O   . CYS C 231 ? 0.8404 0.2442 0.2447 0.0405  -0.0076 -0.0888 231 CYS C O   
6122 C  CB  . CYS C 231 ? 0.6373 0.3826 0.1891 0.0499  -0.0627 -0.0301 231 CYS C CB  
6123 S  SG  . CYS C 231 ? 0.4061 0.4648 0.2951 0.0714  -0.0305 -0.0682 231 CYS C SG  
6124 N  N   . THR C 232 ? 0.4966 0.3808 0.3001 -0.0895 0.0185  -0.1724 232 THR C N   
6125 C  CA  . THR C 232 ? 0.5782 0.3067 0.2717 -0.1312 0.0690  -0.0911 232 THR C CA  
6126 C  C   . THR C 232 ? 0.5777 0.3550 0.2468 -0.1711 0.0594  -0.1535 232 THR C C   
6127 O  O   . THR C 232 ? 0.4112 0.5684 0.2076 -0.1668 0.0139  -0.0784 232 THR C O   
6128 C  CB  . THR C 232 ? 0.6335 0.3258 0.2060 -0.0538 0.0652  -0.0509 232 THR C CB  
6129 O  OG1 . THR C 232 ? 0.4634 0.3838 0.2502 -0.1824 0.0206  -0.0673 232 THR C OG1 
6130 C  CG2 . THR C 232 ? 0.6792 0.2610 0.2550 -0.1099 0.0198  0.0478  232 THR C CG2 
6131 N  N   . HIS C 233 ? 0.7636 0.4398 0.2608 -0.2277 0.1109  -0.2461 233 HIS C N   
6132 C  CA  . HIS C 233 ? 0.6074 0.6643 0.3726 -0.1162 0.0708  -0.1078 233 HIS C CA  
6133 C  C   . HIS C 233 ? 0.4657 0.7269 0.2545 -0.0987 0.0053  -0.2113 233 HIS C C   
6134 O  O   . HIS C 233 ? 0.5085 0.6876 0.2651 -0.0981 0.0440  -0.1483 233 HIS C O   
6135 C  CB  . HIS C 233 ? 0.8831 0.7130 0.3492 -0.0761 0.0824  -0.2981 233 HIS C CB  
6136 C  CG  . HIS C 233 ? 1.0311 1.1174 0.6317 -0.1544 0.1502  -0.0359 233 HIS C CG  
6137 N  ND1 . HIS C 233 ? 1.0723 1.1108 0.9718 -0.0855 -0.1268 -0.1612 233 HIS C ND1 
6138 C  CD2 . HIS C 233 ? 0.9445 1.1871 0.9600 -0.0337 0.1321  -0.0122 233 HIS C CD2 
6139 C  CE1 . HIS C 233 ? 1.4082 0.5991 0.9592 -0.3328 0.3440  -0.0190 233 HIS C CE1 
6140 N  NE2 . HIS C 233 ? 1.0006 1.0964 1.0271 -0.1540 0.4310  0.0728  233 HIS C NE2 
6141 N  N   . MET C 234 ? 0.5448 0.6266 0.3582 -0.0932 -0.0315 -0.1467 234 MET C N   
6142 C  CA  . MET C 234 ? 0.6097 0.7350 0.2031 -0.0412 -0.1135 -0.2438 234 MET C CA  
6143 C  C   . MET C 234 ? 0.5283 0.6560 0.5338 0.0219  -0.1004 -0.2680 234 MET C C   
6144 O  O   . MET C 234 ? 0.4529 0.7447 0.3925 0.2006  -0.1610 -0.1516 234 MET C O   
6145 C  CB  . MET C 234 ? 0.5417 0.8404 0.4785 0.0344  -0.0147 -0.1094 234 MET C CB  
6146 C  CG  . MET C 234 ? 0.5310 1.0178 0.3504 0.2244  0.0418  -0.2612 234 MET C CG  
6147 S  SD  . MET C 234 ? 0.6391 1.0176 0.6171 0.2165  -0.1615 -0.2928 234 MET C SD  
6148 C  CE  . MET C 234 ? 0.3216 0.9208 0.5443 -0.0234 -0.2896 -0.1111 234 MET C CE  
6149 N  N   . ASP C 235 ? 0.7641 0.6294 0.2631 0.0682  -0.0897 -0.2056 235 ASP C N   
6150 C  CA  . ASP C 235 ? 0.5005 0.6610 0.6840 0.2320  -0.0505 -0.2276 235 ASP C CA  
6151 C  C   . ASP C 235 ? 0.5564 0.6105 0.4378 0.1358  -0.1638 -0.2062 235 ASP C C   
6152 O  O   . ASP C 235 ? 0.6508 0.4712 0.6299 -0.0301 -0.0731 -0.3169 235 ASP C O   
6153 C  CB  . ASP C 235 ? 0.5603 0.7819 0.9462 0.1599  -0.2053 -0.2305 235 ASP C CB  
6154 C  CG  . ASP C 235 ? 0.6020 0.7028 0.8696 0.2258  -0.1272 -0.2258 235 ASP C CG  
6155 O  OD1 . ASP C 235 ? 0.5827 0.8493 0.9098 0.2751  -0.1083 -0.1201 235 ASP C OD1 
6156 O  OD2 . ASP C 235 ? 0.8951 0.6330 0.5992 0.4405  -0.3811 -0.4857 235 ASP C OD2 
6157 N  N   . ASP C 236 ? 0.7422 0.6569 0.3927 -0.0403 0.0413  -0.3151 236 ASP C N   
6158 C  CA  . ASP C 236 ? 0.6796 0.6584 0.3689 -0.0988 0.0422  -0.1758 236 ASP C CA  
6159 C  C   . ASP C 236 ? 0.7570 0.4805 0.4492 -0.1447 0.0546  -0.1280 236 ASP C C   
6160 O  O   . ASP C 236 ? 0.5234 0.4597 0.3441 -0.1978 0.1028  -0.1049 236 ASP C O   
6161 C  CB  . ASP C 236 ? 0.9397 0.3007 0.3125 -0.1986 -0.0114 0.0030  236 ASP C CB  
6162 C  CG  . ASP C 236 ? 1.0204 0.3953 0.5713 0.1121  -0.0178 -0.0495 236 ASP C CG  
6163 O  OD1 . ASP C 236 ? 0.8586 0.4090 0.6870 -0.0076 -0.1320 -0.2766 236 ASP C OD1 
6164 O  OD2 . ASP C 236 ? 1.2478 0.3441 0.5184 0.1596  -0.1771 -0.1294 236 ASP C OD2 
6165 N  N   . PRO C 237 ? 0.6799 0.5486 0.5182 -0.1573 0.0106  -0.2178 237 PRO C N   
6166 C  CA  . PRO C 237 ? 0.7922 0.6330 0.5209 -0.1018 0.1298  -0.2303 237 PRO C CA  
6167 C  C   . PRO C 237 ? 0.7640 0.3201 0.7032 -0.1091 0.0928  -0.1146 237 PRO C C   
6168 O  O   . PRO C 237 ? 0.8652 0.5942 0.8239 -0.1360 0.1530  -0.0388 237 PRO C O   
6169 C  CB  . PRO C 237 ? 0.9611 0.4635 0.7436 -0.1768 0.0196  -0.1893 237 PRO C CB  
6170 C  CG  . PRO C 237 ? 0.9916 0.2875 0.8243 -0.0612 0.0921  -0.2009 237 PRO C CG  
6171 C  CD  . PRO C 237 ? 0.9554 0.6006 0.6874 -0.0542 0.0684  -0.1621 237 PRO C CD  
6172 N  N   . SER C 238 ? 0.5637 0.6078 0.7605 0.1780  0.0158  -0.2793 238 SER C N   
6173 C  CA  . SER C 238 ? 0.4954 0.7372 0.7119 0.0916  -0.0084 -0.1801 238 SER C CA  
6174 C  C   . SER C 238 ? 0.5778 0.4884 0.4929 0.0306  -0.1697 -0.1067 238 SER C C   
6175 O  O   . SER C 238 ? 0.7302 0.4672 0.5181 -0.1322 -0.0908 -0.1716 238 SER C O   
6176 C  CB  . SER C 238 ? 0.3041 1.1141 0.9089 -0.0267 -0.1864 0.0228  238 SER C CB  
6177 O  OG  . SER C 238 ? 0.6775 1.0317 1.0411 -0.3089 -0.1960 -0.0067 238 SER C OG  
6178 N  N   . PRO C 239 ? 0.4571 0.4105 0.2999 -0.1372 -0.0601 -0.0272 239 PRO C N   
6179 C  CA  . PRO C 239 ? 0.6249 0.5247 0.1955 -0.0967 -0.0528 -0.1412 239 PRO C CA  
6180 C  C   . PRO C 239 ? 0.5152 0.5143 0.3319 -0.1251 -0.0785 -0.1251 239 PRO C C   
6181 O  O   . PRO C 239 ? 0.4693 0.4940 0.4134 0.0139  0.0022  -0.1498 239 PRO C O   
6182 C  CB  . PRO C 239 ? 0.5026 0.5118 0.2354 -0.1300 0.0771  -0.0780 239 PRO C CB  
6183 C  CG  . PRO C 239 ? 0.5163 0.6833 0.3679 0.0452  0.1429  -0.0309 239 PRO C CG  
6184 C  CD  . PRO C 239 ? 0.5157 0.6594 0.2930 0.0409  -0.0179 -0.0351 239 PRO C CD  
6185 N  N   . ARG C 240 ? 0.5244 0.5796 0.2830 -0.1321 -0.0955 -0.0981 240 ARG C N   
6186 C  CA  . ARG C 240 ? 0.5342 0.5328 0.4442 -0.1778 -0.0671 -0.1852 240 ARG C CA  
6187 C  C   . ARG C 240 ? 0.4521 0.5410 0.4655 -0.1380 -0.1211 -0.0049 240 ARG C C   
6188 O  O   . ARG C 240 ? 0.4720 0.2231 0.3149 -0.0826 -0.0425 -0.0932 240 ARG C O   
6189 C  CB  . ARG C 240 ? 0.4630 0.6365 0.5734 -0.0278 -0.0831 -0.0527 240 ARG C CB  
6190 C  CG  . ARG C 240 ? 0.4911 0.5845 0.5409 -0.0232 -0.1098 -0.3345 240 ARG C CG  
6191 N  N   . GLU C 241 ? 0.4408 0.4401 0.2270 -0.0506 -0.1008 -0.0118 241 GLU C N   
6192 C  CA  . GLU C 241 ? 0.4278 0.4640 0.2209 -0.0398 -0.0994 -0.0696 241 GLU C CA  
6193 C  C   . GLU C 241 ? 0.4195 0.3055 0.2863 -0.1040 0.0131  -0.1183 241 GLU C C   
6194 O  O   . GLU C 241 ? 0.4399 0.3184 0.3204 -0.1131 0.0183  -0.1316 241 GLU C O   
6195 C  CB  . GLU C 241 ? 0.3116 0.5331 0.1636 -0.0271 0.0033  -0.0122 241 GLU C CB  
6196 C  CG  . GLU C 241 ? 0.4486 0.6118 0.1782 -0.0549 -0.0151 0.0133  241 GLU C CG  
6197 C  CD  . GLU C 241 ? 0.6332 0.7620 0.2103 -0.1972 0.1344  0.0302  241 GLU C CD  
6198 O  OE1 . GLU C 241 ? 0.5809 0.8414 0.4843 -0.0748 -0.0187 0.0693  241 GLU C OE1 
6199 O  OE2 . GLU C 241 ? 0.7165 0.7546 0.2345 -0.1489 -0.0310 -0.0587 241 GLU C OE2 
6200 N  N   . MET C 242 ? 0.3823 0.4429 0.1841 -0.0660 -0.0633 -0.1267 242 MET C N   
6201 C  CA  . MET C 242 ? 0.3513 0.3485 0.1884 -0.1366 -0.0296 -0.1066 242 MET C CA  
6202 C  C   . MET C 242 ? 0.2144 0.2829 0.1324 -0.0741 -0.0212 -0.0540 242 MET C C   
6203 O  O   . MET C 242 ? 0.2752 0.4327 0.1559 0.0055  -0.0583 0.0144  242 MET C O   
6204 C  CB  . MET C 242 ? 0.3657 0.3060 0.1444 -0.1091 0.0049  -0.0558 242 MET C CB  
6205 C  CG  . MET C 242 ? 0.3775 0.2763 0.1500 -0.1169 0.0016  0.0174  242 MET C CG  
6206 S  SD  . MET C 242 ? 0.3538 0.2446 0.1994 -0.0902 -0.0372 -0.0237 242 MET C SD  
6207 C  CE  . MET C 242 ? 0.3625 0.2010 0.2145 -0.0429 -0.0814 -0.0339 242 MET C CE  
6208 N  N   . ILE C 243 ? 0.2139 0.2516 0.1564 -0.0403 -0.0315 -0.0066 243 ILE C N   
6209 C  CA  . ILE C 243 ? 0.2361 0.3221 0.1029 -0.0958 -0.0259 -0.0270 243 ILE C CA  
6210 C  C   . ILE C 243 ? 0.1936 0.1900 0.1309 -0.0531 -0.0162 0.0035  243 ILE C C   
6211 O  O   . ILE C 243 ? 0.2689 0.1566 0.1600 -0.0630 -0.0245 -0.0172 243 ILE C O   
6212 C  CB  . ILE C 243 ? 0.2656 0.3116 0.1173 -0.0432 0.0026  0.0000  243 ILE C CB  
6213 C  CG1 . ILE C 243 ? 0.2326 0.2841 0.2119 -0.1134 0.0333  -0.0751 243 ILE C CG1 
6214 C  CG2 . ILE C 243 ? 0.3072 0.4020 0.0882 -0.0497 0.0143  0.0330  243 ILE C CG2 
6215 C  CD1 . ILE C 243 ? 0.2415 0.3042 0.1877 -0.0603 0.0319  0.0227  243 ILE C CD1 
6216 N  N   . ASN C 244 ? 0.1649 0.2270 0.1106 -0.0681 -0.0015 -0.0230 244 ASN C N   
6217 C  CA  . ASN C 244 ? 0.1584 0.2336 0.1555 -0.0587 -0.0225 0.0243  244 ASN C CA  
6218 C  C   . ASN C 244 ? 0.1722 0.1858 0.1571 0.0087  0.0318  0.0128  244 ASN C C   
6219 O  O   . ASN C 244 ? 0.1776 0.1338 0.1711 -0.0157 0.0043  -0.0285 244 ASN C O   
6220 C  CB  . ASN C 244 ? 0.1713 0.3143 0.1502 -0.0807 0.0364  -0.0272 244 ASN C CB  
6221 C  CG  . ASN C 244 ? 0.2521 0.3245 0.2126 -0.0995 0.0561  0.0097  244 ASN C CG  
6222 O  OD1 . ASN C 244 ? 0.2321 0.3072 0.2189 -0.0681 0.0060  -0.0248 244 ASN C OD1 
6223 N  ND2 . ASN C 244 ? 0.2130 0.4391 0.1912 -0.0818 0.0248  0.0200  244 ASN C ND2 
6224 N  N   . ASN C 245 ? 0.1654 0.1768 0.1006 -0.0328 0.0074  0.0294  245 ASN C N   
6225 C  CA  . ASN C 245 ? 0.1549 0.1196 0.1409 -0.0454 0.0260  -0.0217 245 ASN C CA  
6226 C  C   . ASN C 245 ? 0.1679 0.0800 0.1423 -0.0286 -0.0001 -0.0175 245 ASN C C   
6227 O  O   . ASN C 245 ? 0.1668 0.1261 0.1374 -0.0226 -0.0026 -0.0453 245 ASN C O   
6228 C  CB  . ASN C 245 ? 0.2192 0.1597 0.1509 -0.1216 0.0063  -0.0250 245 ASN C CB  
6229 C  CG  . ASN C 245 ? 0.2561 0.2031 0.1844 -0.1057 -0.0346 -0.0058 245 ASN C CG  
6230 O  OD1 . ASN C 245 ? 0.2083 0.1645 0.1742 -0.0745 -0.0200 0.0029  245 ASN C OD1 
6231 N  ND2 . ASN C 245 ? 0.2532 0.2035 0.1814 -0.1051 -0.0657 0.0295  245 ASN C ND2 
6232 N  N   . PHE C 246 ? 0.1855 0.0609 0.1279 -0.0331 -0.0234 0.0110  246 PHE C N   
6233 C  CA  . PHE C 246 ? 0.1753 0.0895 0.1351 -0.0677 -0.0518 -0.0057 246 PHE C CA  
6234 C  C   . PHE C 246 ? 0.1700 0.0811 0.1520 -0.0329 -0.0107 -0.0107 246 PHE C C   
6235 O  O   . PHE C 246 ? 0.2035 0.0610 0.1500 -0.0249 0.0210  0.0078  246 PHE C O   
6236 C  CB  . PHE C 246 ? 0.1600 0.0757 0.1225 -0.0370 -0.0144 0.0271  246 PHE C CB  
6237 C  CG  . PHE C 246 ? 0.1516 0.0359 0.1632 -0.0231 -0.0004 0.0166  246 PHE C CG  
6238 C  CD1 . PHE C 246 ? 0.2218 0.0383 0.1833 -0.0688 0.0285  0.0011  246 PHE C CD1 
6239 C  CD2 . PHE C 246 ? 0.1686 0.0156 0.2411 -0.0345 -0.0220 -0.0164 246 PHE C CD2 
6240 C  CE1 . PHE C 246 ? 0.2275 0.1067 0.1937 -0.0974 0.0000  0.0450  246 PHE C CE1 
6241 C  CE2 . PHE C 246 ? 0.2035 0.0119 0.2002 -0.0329 0.0064  0.0025  246 PHE C CE2 
6242 C  CZ  . PHE C 246 ? 0.2352 0.0093 0.1922 -0.0251 -0.0055 -0.0056 246 PHE C CZ  
6243 N  N   . ARG C 247 ? 0.2064 0.0110 0.1252 -0.0212 -0.0277 -0.0070 247 ARG C N   
6244 C  CA  . ARG C 247 ? 0.1661 0.0505 0.1173 -0.0403 -0.0102 0.0201  247 ARG C CA  
6245 C  C   . ARG C 247 ? 0.1309 0.0553 0.1225 -0.0222 0.0344  -0.0187 247 ARG C C   
6246 O  O   . ARG C 247 ? 0.1636 0.0545 0.1311 0.0190  -0.0100 -0.0089 247 ARG C O   
6247 C  CB  . ARG C 247 ? 0.1925 0.0735 0.0900 -0.0098 0.0024  0.0242  247 ARG C CB  
6248 C  CG  . ARG C 247 ? 0.1877 0.0471 0.0997 -0.0135 -0.0059 0.0032  247 ARG C CG  
6249 C  CD  . ARG C 247 ? 0.2312 0.0106 0.1252 0.0250  0.0375  0.0170  247 ARG C CD  
6250 N  NE  . ARG C 247 ? 0.1552 0.0117 0.1641 -0.0162 -0.0259 0.0264  247 ARG C NE  
6251 C  CZ  . ARG C 247 ? 0.1627 0.0069 0.1343 0.0052  0.0107  -0.0068 247 ARG C CZ  
6252 N  NH1 . ARG C 247 ? 0.1155 0.0581 0.1453 -0.0243 0.0099  0.0069  247 ARG C NH1 
6253 N  NH2 . ARG C 247 ? 0.1919 0.0064 0.1622 -0.0033 -0.0114 -0.0017 247 ARG C NH2 
6254 N  N   . GLN C 248 ? 0.1377 0.0212 0.1543 -0.0276 -0.0036 -0.0025 248 GLN C N   
6255 C  CA  . GLN C 248 ? 0.1352 0.0142 0.1756 -0.0287 0.0201  -0.0200 248 GLN C CA  
6256 C  C   . GLN C 248 ? 0.1546 0.0355 0.1144 -0.0153 -0.0362 0.0325  248 GLN C C   
6257 O  O   . GLN C 248 ? 0.2080 0.0124 0.1302 -0.0082 0.0095  0.0089  248 GLN C O   
6258 C  CB  . GLN C 248 ? 0.1397 0.0403 0.1664 -0.0127 0.0107  -0.0019 248 GLN C CB  
6259 C  CG  . GLN C 248 ? 0.1444 0.0073 0.1618 0.0103  0.0091  0.0062  248 GLN C CG  
6260 C  CD  . GLN C 248 ? 0.1320 0.0308 0.1773 0.0060  -0.0283 0.0417  248 GLN C CD  
6261 O  OE1 . GLN C 248 ? 0.1661 0.0746 0.1830 -0.0297 -0.0558 0.0449  248 GLN C OE1 
6262 N  NE2 . GLN C 248 ? 0.1826 0.1108 0.2037 -0.0354 -0.0196 -0.0175 248 GLN C NE2 
6263 N  N   . VAL C 249 ? 0.1733 0.0336 0.1241 0.0261  -0.0152 -0.0132 249 VAL C N   
6264 C  CA  . VAL C 249 ? 0.1779 0.0160 0.1337 -0.0037 -0.0155 0.0000  249 VAL C CA  
6265 C  C   . VAL C 249 ? 0.1803 0.0654 0.1390 0.0351  -0.0287 -0.0093 249 VAL C C   
6266 O  O   . VAL C 249 ? 0.1714 0.0085 0.1820 0.0145  -0.0245 -0.0146 249 VAL C O   
6267 C  CB  . VAL C 249 ? 0.1782 0.0112 0.2117 0.0019  -0.0476 0.0023  249 VAL C CB  
6268 C  CG1 . VAL C 249 ? 0.2156 0.0096 0.2353 0.0253  -0.0539 -0.0132 249 VAL C CG1 
6269 C  CG2 . VAL C 249 ? 0.2194 0.0489 0.2984 -0.0286 -0.0431 0.0262  249 VAL C CG2 
6270 N  N   . GLN C 250 ? 0.1698 0.0068 0.1597 0.0079  -0.0086 -0.0044 250 GLN C N   
6271 C  CA  . GLN C 250 ? 0.1451 0.0668 0.1288 0.0046  -0.0175 0.0042  250 GLN C CA  
6272 C  C   . GLN C 250 ? 0.1498 0.0742 0.1645 0.0323  -0.0234 -0.0302 250 GLN C C   
6273 O  O   . GLN C 250 ? 0.1714 0.0550 0.1672 0.0173  -0.0239 -0.0248 250 GLN C O   
6274 C  CB  . GLN C 250 ? 0.1173 0.0444 0.1474 0.0098  -0.0146 -0.0401 250 GLN C CB  
6275 C  CG  . GLN C 250 ? 0.1243 0.1051 0.1550 0.0379  -0.0455 -0.0384 250 GLN C CG  
6276 C  CD  . GLN C 250 ? 0.1361 0.0405 0.1530 0.0097  0.0273  0.0311  250 GLN C CD  
6277 O  OE1 . GLN C 250 ? 0.1897 0.0082 0.1618 -0.0003 -0.0041 0.0039  250 GLN C OE1 
6278 N  NE2 . GLN C 250 ? 0.1356 0.0880 0.1430 -0.0222 -0.0089 0.0167  250 GLN C NE2 
6279 N  N   . LYS C 251 ? 0.1291 0.1273 0.1185 0.0328  -0.0091 -0.0205 251 LYS C N   
6280 C  CA  . LYS C 251 ? 0.1474 0.1480 0.1112 0.0348  -0.0080 -0.0218 251 LYS C CA  
6281 C  C   . LYS C 251 ? 0.1345 0.1319 0.1017 -0.0012 -0.0126 -0.0302 251 LYS C C   
6282 O  O   . LYS C 251 ? 0.1313 0.1355 0.1603 0.0031  -0.0190 -0.0170 251 LYS C O   
6283 C  CB  . LYS C 251 ? 0.1311 0.1805 0.1283 0.0318  -0.0196 -0.0243 251 LYS C CB  
6284 C  CG  . LYS C 251 ? 0.1453 0.1162 0.1388 0.0435  0.0064  -0.0172 251 LYS C CG  
6285 C  CD  . LYS C 251 ? 0.1481 0.2015 0.1530 0.0623  0.0020  0.0145  251 LYS C CD  
6286 C  CE  . LYS C 251 ? 0.1354 0.1049 0.1275 0.0340  -0.0005 0.0166  251 LYS C CE  
6287 N  NZ  . LYS C 251 ? 0.1595 0.0604 0.1318 0.0088  0.0060  0.0004  251 LYS C NZ  
6288 N  N   . PHE C 252 ? 0.1826 0.0929 0.1618 0.0610  -0.0025 -0.0324 252 PHE C N   
6289 C  CA  . PHE C 252 ? 0.2081 0.1660 0.1631 0.0876  -0.0038 -0.0306 252 PHE C CA  
6290 C  C   . PHE C 252 ? 0.2874 0.2922 0.2793 0.0410  -0.0414 -0.1203 252 PHE C C   
6291 O  O   . PHE C 252 ? 0.3700 0.2573 0.3567 0.1022  -0.1073 -0.0623 252 PHE C O   
6292 C  CB  . PHE C 252 ? 0.1987 0.1265 0.2250 0.0491  0.0016  0.0008  252 PHE C CB  
6293 C  CG  . PHE C 252 ? 0.2031 0.1395 0.1995 0.0631  -0.0051 0.0106  252 PHE C CG  
6294 C  CD1 . PHE C 252 ? 0.1963 0.1787 0.1690 0.0419  -0.0122 0.0506  252 PHE C CD1 
6295 C  CD2 . PHE C 252 ? 0.2443 0.1234 0.2206 0.0545  0.0107  0.0083  252 PHE C CD2 
6296 C  CE1 . PHE C 252 ? 0.2078 0.2398 0.1728 0.0922  -0.0458 0.0210  252 PHE C CE1 
6297 C  CE2 . PHE C 252 ? 0.2480 0.1682 0.2020 0.0625  0.0105  0.0433  252 PHE C CE2 
6298 C  CZ  . PHE C 252 ? 0.2071 0.2214 0.1995 0.0515  0.0084  0.0387  252 PHE C CZ  
6299 N  N   . ASP C 253 ? 0.3269 0.5317 0.1791 0.0407  -0.0398 -0.0768 253 ASP C N   
6300 C  CA  . ASP C 253 ? 0.3190 0.6585 0.1764 0.1258  -0.0886 -0.0559 253 ASP C CA  
6301 C  C   . ASP C 253 ? 0.2542 0.4178 0.2002 0.0939  -0.0831 -0.0263 253 ASP C C   
6302 O  O   . ASP C 253 ? 0.2700 0.4147 0.3254 0.0528  -0.0319 -0.0209 253 ASP C O   
6303 C  CB  . ASP C 253 ? 0.3866 0.6133 0.2664 0.2011  -0.1037 0.0256  253 ASP C CB  
6304 C  CG  . ASP C 253 ? 0.4278 0.7172 0.4119 0.0119  -0.0932 0.0574  253 ASP C CG  
6305 O  OD1 . ASP C 253 ? 0.4034 0.6587 0.5777 0.1595  -0.0314 0.2083  253 ASP C OD1 
6306 O  OD2 . ASP C 253 ? 0.4989 0.9291 0.3427 0.0464  -0.0204 0.1365  253 ASP C OD2 
6307 N  N   A GLU C 254 ? 0.2632 0.4031 0.2509 0.0392  -0.0717 0.0145  254 GLU C N   
6308 N  N   B GLU C 254 ? 0.2647 0.4028 0.2527 0.0385  -0.0716 0.0135  254 GLU C N   
6309 C  CA  A GLU C 254 ? 0.2618 0.3083 0.3222 0.0629  0.0065  0.0253  254 GLU C CA  
6310 C  CA  B GLU C 254 ? 0.2660 0.3106 0.3268 0.0607  0.0099  0.0209  254 GLU C CA  
6311 C  C   A GLU C 254 ? 0.2593 0.2684 0.2514 0.0731  -0.0132 0.0239  254 GLU C C   
6312 C  C   B GLU C 254 ? 0.2649 0.2715 0.2526 0.0673  -0.0161 0.0280  254 GLU C C   
6313 O  O   A GLU C 254 ? 0.2732 0.3968 0.2684 0.0125  -0.0104 0.0201  254 GLU C O   
6314 O  O   B GLU C 254 ? 0.2743 0.3966 0.2702 0.0104  -0.0102 0.0207  254 GLU C O   
6315 C  CB  A GLU C 254 ? 0.2831 0.4600 0.2153 0.1555  -0.0158 0.0295  254 GLU C CB  
6316 C  CB  B GLU C 254 ? 0.3131 0.4501 0.2186 0.1615  -0.0036 0.0315  254 GLU C CB  
6317 C  CG  A GLU C 254 ? 0.2983 0.4873 0.3877 0.1480  -0.0496 0.0688  254 GLU C CG  
6318 C  CG  B GLU C 254 ? 0.3227 0.5159 0.4295 0.1472  -0.0289 0.0168  254 GLU C CG  
6319 C  CD  A GLU C 254 ? 0.2868 0.5162 0.4816 0.2077  -0.1542 0.1171  254 GLU C CD  
6320 C  CD  B GLU C 254 ? 0.4575 0.4934 0.5302 0.1775  -0.1088 0.0310  254 GLU C CD  
6321 O  OE1 A GLU C 254 ? 0.7438 0.5316 0.5005 0.1178  -0.1289 0.0719  254 GLU C OE1 
6322 O  OE1 B GLU C 254 ? 0.7750 0.6431 0.6409 0.2112  0.0285  -0.0664 254 GLU C OE1 
6323 O  OE2 A GLU C 254 ? 0.5025 0.4288 0.5505 0.0055  0.0405  -0.0618 254 GLU C OE2 
6324 O  OE2 B GLU C 254 ? 0.4902 0.3012 0.7330 0.1980  0.0088  -0.1200 254 GLU C OE2 
6325 N  N   . ARG C 255 ? 0.2767 0.3007 0.2597 0.0263  -0.0445 0.0355  255 ARG C N   
6326 C  CA  . ARG C 255 ? 0.2885 0.2143 0.3558 0.0487  -0.0364 -0.0672 255 ARG C CA  
6327 C  C   . ARG C 255 ? 0.2572 0.2394 0.3744 0.0577  0.0074  -0.0320 255 ARG C C   
6328 O  O   . ARG C 255 ? 0.2455 0.1997 0.3407 0.0217  -0.0348 -0.0325 255 ARG C O   
6329 C  CB  . ARG C 255 ? 0.2891 0.1902 0.2793 0.0263  -0.0522 -0.0116 255 ARG C CB  
6330 C  CG  . ARG C 255 ? 0.3601 0.2078 0.2588 0.0402  -0.1177 0.0151  255 ARG C CG  
6331 C  CD  . ARG C 255 ? 0.3238 0.2552 0.2892 -0.0279 -0.1257 0.0245  255 ARG C CD  
6332 N  NE  . ARG C 255 ? 0.2791 0.3060 0.3495 -0.0886 -0.1045 -0.0181 255 ARG C NE  
6333 C  CZ  . ARG C 255 ? 0.2252 0.3028 0.3098 0.0092  -0.0832 -0.0173 255 ARG C CZ  
6334 N  NH1 . ARG C 255 ? 0.3123 0.1658 0.2977 -0.0201 -0.0594 -0.0151 255 ARG C NH1 
6335 N  NH2 . ARG C 255 ? 0.2182 0.1062 0.2349 -0.0131 -0.0747 0.0036  255 ARG C NH2 
6336 N  N   . LEU C 256 ? 0.2627 0.2814 0.2521 0.0824  0.0150  -0.0309 256 LEU C N   
6337 C  CA  . LEU C 256 ? 0.2779 0.2757 0.2157 0.1090  -0.0314 -0.0674 256 LEU C CA  
6338 C  C   . LEU C 256 ? 0.2954 0.2211 0.2064 0.0969  -0.0341 -0.0551 256 LEU C C   
6339 O  O   . LEU C 256 ? 0.3945 0.2232 0.2335 0.1131  -0.1121 -0.0660 256 LEU C O   
6340 C  CB  . LEU C 256 ? 0.2966 0.2225 0.2634 0.0715  -0.0275 -0.0930 256 LEU C CB  
6341 C  CG  . LEU C 256 ? 0.3642 0.4248 0.2913 0.1033  -0.0856 -0.1014 256 LEU C CG  
6342 C  CD1 . LEU C 256 ? 0.4190 0.5294 0.2301 0.1439  -0.1419 -0.0965 256 LEU C CD1 
6343 C  CD2 . LEU C 256 ? 0.4760 0.5105 0.2254 0.0556  -0.0345 -0.0596 256 LEU C CD2 
6344 N  N   . VAL C 257 ? 0.2620 0.2132 0.2035 0.1252  -0.0368 -0.0604 257 VAL C N   
6345 C  CA  . VAL C 257 ? 0.2375 0.1356 0.1805 0.0780  -0.0256 -0.0534 257 VAL C CA  
6346 C  C   . VAL C 257 ? 0.2031 0.1793 0.2148 0.0883  -0.0274 -0.0736 257 VAL C C   
6347 O  O   . VAL C 257 ? 0.2286 0.1880 0.2121 0.0607  -0.0498 -0.0732 257 VAL C O   
6348 C  CB  . VAL C 257 ? 0.2458 0.1395 0.1707 0.1033  -0.0251 -0.0513 257 VAL C CB  
6349 C  CG1 . VAL C 257 ? 0.2308 0.2085 0.1726 0.0561  -0.0364 -0.0108 257 VAL C CG1 
6350 C  CG2 . VAL C 257 ? 0.2597 0.1915 0.2472 0.1193  0.0215  -0.0757 257 VAL C CG2 
6351 N  N   . TYR C 258 ? 0.1967 0.1606 0.1805 0.0754  -0.0124 -0.0531 258 TYR C N   
6352 C  CA  . TYR C 258 ? 0.2067 0.1811 0.2049 0.1045  -0.0418 -0.0648 258 TYR C CA  
6353 C  C   . TYR C 258 ? 0.2293 0.1767 0.2177 0.0982  -0.0229 -0.0774 258 TYR C C   
6354 O  O   . TYR C 258 ? 0.3318 0.1462 0.2119 0.0743  -0.0458 -0.0736 258 TYR C O   
6355 C  CB  . TYR C 258 ? 0.2286 0.2331 0.1973 0.0789  -0.0100 -0.0906 258 TYR C CB  
6356 C  CG  . TYR C 258 ? 0.2401 0.3221 0.1645 0.0250  -0.0367 -0.0485 258 TYR C CG  
6357 C  CD1 . TYR C 258 ? 0.2419 0.4002 0.1868 0.0656  -0.0796 -0.0662 258 TYR C CD1 
6358 C  CD2 . TYR C 258 ? 0.2665 0.3316 0.2186 0.0430  -0.0678 -0.0392 258 TYR C CD2 
6359 C  CE1 . TYR C 258 ? 0.3520 0.3919 0.2077 0.0806  -0.0335 -0.0297 258 TYR C CE1 
6360 C  CE2 . TYR C 258 ? 0.3308 0.4159 0.2139 -0.0493 -0.1064 0.0268  258 TYR C CE2 
6361 C  CZ  . TYR C 258 ? 0.3303 0.3810 0.1708 0.0424  -0.0746 0.0003  258 TYR C CZ  
6362 O  OH  . TYR C 258 ? 0.4882 0.6104 0.2723 0.0119  -0.1599 0.1385  258 TYR C OH  
6363 N  N   . THR C 259 ? 0.2167 0.1539 0.2203 0.0917  -0.0469 -0.0757 259 THR C N   
6364 C  CA  . THR C 259 ? 0.2319 0.1652 0.2137 0.0904  -0.0262 -0.0628 259 THR C CA  
6365 C  C   . THR C 259 ? 0.2464 0.0604 0.1912 0.0996  -0.0684 -0.0682 259 THR C C   
6366 O  O   . THR C 259 ? 0.2527 0.2110 0.1949 0.1085  -0.0447 -0.0863 259 THR C O   
6367 C  CB  . THR C 259 ? 0.2735 0.1133 0.2397 0.0665  -0.0379 -0.0484 259 THR C CB  
6368 O  OG1 . THR C 259 ? 0.2674 0.2067 0.2636 0.0575  -0.0320 -0.0995 259 THR C OG1 
6369 C  CG2 . THR C 259 ? 0.2622 0.1369 0.2171 0.0408  -0.0253 -0.0597 259 THR C CG2 
6370 N  N   . SER C 260 ? 0.2052 0.1171 0.2019 0.0842  -0.0610 -0.0555 260 SER C N   
6371 C  CA  . SER C 260 ? 0.1999 0.1259 0.2263 0.0672  -0.0054 -0.0342 260 SER C CA  
6372 C  C   . SER C 260 ? 0.2042 0.1233 0.2877 0.0595  0.0066  -0.0779 260 SER C C   
6373 O  O   . SER C 260 ? 0.2421 0.1632 0.3587 0.0862  0.0081  -0.1040 260 SER C O   
6374 C  CB  . SER C 260 ? 0.2171 0.1877 0.2149 0.0521  -0.0085 -0.0451 260 SER C CB  
6375 O  OG  . SER C 260 ? 0.1694 0.1487 0.2192 0.0620  -0.0078 -0.0159 260 SER C OG  
6376 N  N   . PHE C 261 ? 0.2293 0.0762 0.3667 0.0265  -0.0116 -0.0835 261 PHE C N   
6377 C  CA  . PHE C 261 ? 0.2387 0.0663 0.3452 0.0287  -0.0620 -0.0849 261 PHE C CA  
6378 C  C   . PHE C 261 ? 0.2163 0.0990 0.3661 0.0122  -0.0403 -0.0264 261 PHE C C   
6379 O  O   . PHE C 261 ? 0.2761 0.1067 0.4147 0.0529  -0.1143 -0.1148 261 PHE C O   
6380 C  CB  . PHE C 261 ? 0.2630 0.1003 0.3617 0.0457  -0.0250 -0.0835 261 PHE C CB  
6381 C  CG  . PHE C 261 ? 0.2221 0.0620 0.3614 0.0073  -0.0005 -0.0595 261 PHE C CG  
6382 C  CD1 . PHE C 261 ? 0.2746 0.0771 0.3069 0.0546  -0.0597 -0.0756 261 PHE C CD1 
6383 C  CD2 . PHE C 261 ? 0.2345 0.0503 0.4552 0.0027  0.0259  -0.0920 261 PHE C CD2 
6384 C  CE1 . PHE C 261 ? 0.2798 0.0832 0.3586 0.0428  -0.0148 -0.0424 261 PHE C CE1 
6385 C  CE2 . PHE C 261 ? 0.3064 0.0635 0.4527 -0.0130 0.0861  -0.1070 261 PHE C CE2 
6386 C  CZ  . PHE C 261 ? 0.2944 0.1058 0.3757 0.0683  -0.0260 -0.1340 261 PHE C CZ  
6387 N  N   . SER C 262 ? 0.3391 0.1830 0.2679 -0.1277 -0.0234 -0.0651 262 SER C N   
6388 C  CA  . SER C 262 ? 0.3858 0.2013 0.4163 -0.1750 -0.0146 -0.1489 262 SER C CA  
6389 C  C   . SER C 262 ? 0.2868 0.4652 0.6319 -0.3146 -0.0195 0.0268  262 SER C C   
6390 O  O   . SER C 262 ? 0.5984 0.5872 0.5534 -0.1955 0.1427  -0.3436 262 SER C O   
6391 C  CB  . SER C 262 ? 0.4793 0.4468 0.5373 -0.0210 -0.0881 -0.3746 262 SER C CB  
6392 O  OG  . SER C 262 ? 0.7337 0.4119 0.5950 -0.2111 -0.0414 0.0680  262 SER C OG  
6393 N  N   . LYS D 3   ? 0.8566 0.2992 0.7111 0.0845  -0.0793 -0.0446 3   LYS D N   
6394 C  CA  . LYS D 3   ? 0.6994 0.3394 0.5403 0.1523  -0.0354 0.1516  3   LYS D CA  
6395 C  C   . LYS D 3   ? 0.5567 0.0742 0.2803 0.0421  0.0447  0.0195  3   LYS D C   
6396 O  O   . LYS D 3   ? 0.4644 0.1909 0.2953 -0.0041 0.0080  -0.0447 3   LYS D O   
6397 C  CB  . LYS D 3   ? 0.7302 0.1898 0.5335 -0.0772 -0.0954 0.0145  3   LYS D CB  
6398 C  CG  . LYS D 3   ? 0.6176 0.2909 0.7491 -0.2246 0.0838  0.0057  3   LYS D CG  
6399 C  CD  . LYS D 3   ? 0.6283 0.5289 0.6968 -0.1053 -0.0025 0.1918  3   LYS D CD  
6400 C  CE  . LYS D 3   ? 0.5307 0.4367 0.8151 -0.1375 -0.0577 0.1247  3   LYS D CE  
6401 N  NZ  . LYS D 3   ? 0.6355 0.0678 0.5325 0.0723  0.0006  0.0218  3   LYS D NZ  
6402 N  N   . TRP D 4   ? 0.3338 0.0565 0.2996 0.0099  0.0266  0.0493  4   TRP D N   
6403 C  CA  . TRP D 4   ? 0.2419 0.0512 0.2189 0.0036  0.0011  0.0097  4   TRP D CA  
6404 C  C   . TRP D 4   ? 0.1164 0.0812 0.2406 -0.0297 0.0237  -0.0179 4   TRP D C   
6405 O  O   . TRP D 4   ? 0.1731 0.1021 0.2351 -0.0206 0.0098  0.0165  4   TRP D O   
6406 C  CB  . TRP D 4   ? 0.2257 0.0638 0.2347 0.0019  0.0026  0.0107  4   TRP D CB  
6407 C  CG  . TRP D 4   ? 0.2080 0.0643 0.1985 0.0126  -0.0170 -0.0096 4   TRP D CG  
6408 C  CD1 . TRP D 4   ? 0.2132 0.0294 0.1703 0.0042  0.0025  0.0119  4   TRP D CD1 
6409 C  CD2 . TRP D 4   ? 0.1814 0.0486 0.1442 0.0295  -0.0261 -0.0108 4   TRP D CD2 
6410 N  NE1 . TRP D 4   ? 0.2248 0.0557 0.2078 0.0016  -0.0145 0.0013  4   TRP D NE1 
6411 C  CE2 . TRP D 4   ? 0.1941 0.0589 0.1568 0.0323  -0.0281 0.0165  4   TRP D CE2 
6412 C  CE3 . TRP D 4   ? 0.1656 0.0433 0.1372 0.0163  -0.0346 -0.0166 4   TRP D CE3 
6413 C  CZ2 . TRP D 4   ? 0.1922 0.1280 0.1521 -0.0074 -0.0151 -0.0120 4   TRP D CZ2 
6414 C  CZ3 . TRP D 4   ? 0.1778 0.0999 0.1337 -0.0236 -0.0126 -0.0158 4   TRP D CZ3 
6415 C  CH2 . TRP D 4   ? 0.1783 0.1606 0.0954 0.0368  -0.0401 -0.0286 4   TRP D CH2 
6416 N  N   . THR D 5   ? 0.2163 0.0773 0.1719 0.0089  0.0313  0.0008  5   THR D N   
6417 C  CA  . THR D 5   ? 0.1983 0.0466 0.2150 -0.0680 0.0076  0.0154  5   THR D CA  
6418 C  C   . THR D 5   ? 0.2347 0.0701 0.1273 -0.0547 0.0523  0.0062  5   THR D C   
6419 O  O   . THR D 5   ? 0.2221 0.0152 0.1620 -0.0401 0.0026  -0.0151 5   THR D O   
6420 C  CB  . THR D 5   ? 0.2062 0.0139 0.2231 -0.0109 0.0278  0.0372  5   THR D CB  
6421 O  OG1 . THR D 5   ? 0.2091 0.0380 0.2331 -0.0177 0.0330  0.0053  5   THR D OG1 
6422 C  CG2 . THR D 5   ? 0.2609 0.0252 0.1870 -0.0408 -0.0197 0.0379  5   THR D CG2 
6423 N  N   . TYR D 6   ? 0.1801 0.0726 0.1550 -0.0531 -0.0265 -0.0125 6   TYR D N   
6424 C  CA  . TYR D 6   ? 0.1694 0.0760 0.1717 -0.0595 0.0146  0.0335  6   TYR D CA  
6425 C  C   . TYR D 6   ? 0.1486 0.0372 0.2147 -0.0649 -0.0130 0.0215  6   TYR D C   
6426 O  O   . TYR D 6   ? 0.2034 0.0478 0.2049 -0.0321 -0.0058 0.0306  6   TYR D O   
6427 C  CB  . TYR D 6   ? 0.1667 0.0595 0.1642 -0.0407 0.0218  -0.0069 6   TYR D CB  
6428 C  CG  . TYR D 6   ? 0.1855 0.0214 0.1331 -0.0237 0.0250  -0.0064 6   TYR D CG  
6429 C  CD1 . TYR D 6   ? 0.2058 0.0109 0.1661 -0.0175 0.0155  -0.0234 6   TYR D CD1 
6430 C  CD2 . TYR D 6   ? 0.2072 0.0086 0.1276 -0.0189 0.0248  -0.0102 6   TYR D CD2 
6431 C  CE1 . TYR D 6   ? 0.2166 0.0088 0.1594 -0.0021 0.0199  -0.0196 6   TYR D CE1 
6432 C  CE2 . TYR D 6   ? 0.1809 0.0093 0.1444 0.0085  0.0119  -0.0182 6   TYR D CE2 
6433 C  CZ  . TYR D 6   ? 0.1850 0.0139 0.1499 0.0142  -0.0035 -0.0307 6   TYR D CZ  
6434 O  OH  . TYR D 6   ? 0.2189 0.0070 0.1652 0.0123  0.0112  -0.0011 6   TYR D OH  
6435 N  N   . PHE D 7   ? 0.1877 0.0604 0.1758 -0.0714 0.0269  -0.0041 7   PHE D N   
6436 C  CA  . PHE D 7   ? 0.1986 0.0690 0.2508 -0.0254 0.0463  -0.0094 7   PHE D CA  
6437 C  C   . PHE D 7   ? 0.1922 0.1359 0.2714 -0.0144 0.0784  0.0743  7   PHE D C   
6438 O  O   . PHE D 7   ? 0.2137 0.1264 0.2518 -0.0055 0.0119  0.0277  7   PHE D O   
6439 C  CB  . PHE D 7   ? 0.3438 0.1130 0.2629 -0.0561 0.1056  -0.0332 7   PHE D CB  
6440 C  CG  . PHE D 7   ? 0.4630 0.1956 0.3761 -0.0555 0.2123  0.0034  7   PHE D CG  
6441 C  CD1 . PHE D 7   ? 0.5272 0.3141 0.3371 0.0261  0.1896  0.0208  7   PHE D CD1 
6442 C  CD2 . PHE D 7   ? 0.6700 0.1588 0.3856 0.0200  0.2631  0.0111  7   PHE D CD2 
6443 C  CE1 . PHE D 7   ? 0.5567 0.4523 0.4784 -0.0295 0.2978  -0.0137 7   PHE D CE1 
6444 C  CE2 . PHE D 7   ? 0.6998 0.4508 0.4188 0.0199  0.3504  0.0910  7   PHE D CE2 
6445 C  CZ  . PHE D 7   ? 0.8543 0.4307 0.6238 0.0091  0.2411  0.1495  7   PHE D CZ  
6446 N  N   . GLY D 8   ? 0.2249 0.1225 0.2300 -0.0516 0.0055  0.0283  8   GLY D N   
6447 C  CA  . GLY D 8   ? 0.2302 0.1241 0.3063 -0.0629 0.0148  0.0303  8   GLY D CA  
6448 C  C   . GLY D 8   ? 0.2005 0.1241 0.2177 -0.0206 -0.0002 0.0721  8   GLY D C   
6449 O  O   . GLY D 8   ? 0.2066 0.1694 0.2106 -0.0095 -0.0200 0.0480  8   GLY D O   
6450 N  N   . PRO D 9   ? 0.2295 0.1098 0.2500 -0.0373 0.0203  0.0484  9   PRO D N   
6451 C  CA  . PRO D 9   ? 0.2799 0.1409 0.2561 -0.1079 0.0227  0.0665  9   PRO D CA  
6452 C  C   . PRO D 9   ? 0.2340 0.1180 0.2178 -0.0605 -0.0178 0.0776  9   PRO D C   
6453 O  O   . PRO D 9   ? 0.2626 0.1973 0.2639 -0.0380 -0.0747 0.0325  9   PRO D O   
6454 C  CB  . PRO D 9   ? 0.4005 0.1139 0.3125 -0.1291 0.0453  0.0665  9   PRO D CB  
6455 C  CG  . PRO D 9   ? 0.5845 0.0566 0.3784 -0.0876 0.0265  0.0746  9   PRO D CG  
6456 C  CD  . PRO D 9   ? 0.3206 0.0669 0.2428 -0.0249 0.0118  0.0403  9   PRO D CD  
6457 N  N   . ASP D 10  ? 0.2053 0.0710 0.2407 -0.0458 0.0072  0.0600  10  ASP D N   
6458 C  CA  . ASP D 10  ? 0.2254 0.0900 0.1922 -0.0480 -0.0077 0.0511  10  ASP D CA  
6459 C  C   . ASP D 10  ? 0.1861 0.0369 0.1880 -0.0317 -0.0120 0.0161  10  ASP D C   
6460 O  O   . ASP D 10  ? 0.2071 0.0389 0.1877 -0.0431 -0.0102 0.0141  10  ASP D O   
6461 C  CB  . ASP D 10  ? 0.2851 0.0817 0.1970 0.0073  -0.0263 0.0314  10  ASP D CB  
6462 C  CG  . ASP D 10  ? 0.4012 0.1876 0.3274 -0.1160 0.0080  0.0538  10  ASP D CG  
6463 O  OD1 . ASP D 10  ? 0.4088 0.1074 0.3462 -0.0625 -0.0810 0.1025  10  ASP D OD1 
6464 O  OD2 . ASP D 10  ? 0.4608 0.0825 0.3420 -0.0185 0.0559  0.0445  10  ASP D OD2 
6465 N  N   . GLY D 11  ? 0.2005 0.0181 0.1877 -0.0478 0.0021  -0.0009 11  GLY D N   
6466 C  CA  . GLY D 11  ? 0.1535 0.0303 0.1403 -0.0468 -0.0201 0.0089  11  GLY D CA  
6467 C  C   . GLY D 11  ? 0.1456 0.0320 0.1431 -0.0436 -0.0095 0.0004  11  GLY D C   
6468 O  O   . GLY D 11  ? 0.1593 0.0396 0.1793 -0.0395 -0.0316 -0.0136 11  GLY D O   
6469 N  N   . GLU D 12  ? 0.1157 0.0608 0.1247 -0.0089 -0.0190 0.0394  12  GLU D N   
6470 C  CA  . GLU D 12  ? 0.1330 0.0207 0.1347 -0.0220 -0.0073 -0.0001 12  GLU D CA  
6471 C  C   . GLU D 12  ? 0.1273 0.0189 0.1100 -0.0223 0.0009  0.0257  12  GLU D C   
6472 O  O   . GLU D 12  ? 0.1412 0.0122 0.1379 0.0048  0.0219  0.0134  12  GLU D O   
6473 C  CB  . GLU D 12  ? 0.1276 0.0071 0.1446 -0.0044 -0.0404 -0.0075 12  GLU D CB  
6474 C  CG  . GLU D 12  ? 0.1169 0.0080 0.1673 -0.0110 -0.0189 0.0114  12  GLU D CG  
6475 C  CD  . GLU D 12  ? 0.1347 0.0075 0.1403 -0.0110 -0.0124 0.0065  12  GLU D CD  
6476 O  OE1 . GLU D 12  ? 0.1470 0.0200 0.1810 -0.0017 0.0126  0.0133  12  GLU D OE1 
6477 O  OE2 . GLU D 12  ? 0.1927 0.0240 0.1363 -0.0156 -0.0148 0.0077  12  GLU D OE2 
6478 N  N   . ASN D 13  ? 0.1130 0.0514 0.1764 0.0074  -0.0164 0.0187  13  ASN D N   
6479 C  CA  . ASN D 13  ? 0.1151 0.0345 0.1909 0.0168  -0.0176 0.0158  13  ASN D CA  
6480 C  C   . ASN D 13  ? 0.1424 0.0392 0.2529 -0.0095 -0.0212 -0.0420 13  ASN D C   
6481 O  O   . ASN D 13  ? 0.1964 0.0068 0.1980 -0.0052 -0.0129 -0.0076 13  ASN D O   
6482 C  CB  . ASN D 13  ? 0.1459 0.0119 0.2213 0.0189  0.0189  -0.0226 13  ASN D CB  
6483 C  CG  . ASN D 13  ? 0.1271 0.0096 0.1724 -0.0004 -0.0104 -0.0233 13  ASN D CG  
6484 O  OD1 . ASN D 13  ? 0.1439 0.0726 0.1773 -0.0048 -0.0166 0.0239  13  ASN D OD1 
6485 N  ND2 . ASN D 13  ? 0.1191 0.0186 0.2242 -0.0098 0.0108  0.0062  13  ASN D ND2 
6486 N  N   . SER D 14  ? 0.1387 0.0071 0.2076 -0.0081 0.0240  -0.0089 14  SER D N   
6487 C  CA  . SER D 14  ? 0.1366 0.0147 0.2231 -0.0144 0.0410  0.0329  14  SER D CA  
6488 C  C   . SER D 14  ? 0.1375 0.0092 0.2058 0.0041  0.0044  0.0236  14  SER D C   
6489 O  O   . SER D 14  ? 0.1965 0.0068 0.2129 0.0023  0.0098  0.0102  14  SER D O   
6490 C  CB  . SER D 14  ? 0.2036 0.0155 0.2371 0.0191  0.0407  0.0442  14  SER D CB  
6491 O  OG  . SER D 14  ? 0.1865 0.0112 0.2448 -0.0154 0.0168  0.0275  14  SER D OG  
6492 N  N   . TRP D 15  ? 0.1162 0.0256 0.1442 -0.0044 -0.0012 0.0184  15  TRP D N   
6493 C  CA  . TRP D 15  ? 0.1361 0.0075 0.1773 -0.0119 0.0156  -0.0050 15  TRP D CA  
6494 C  C   . TRP D 15  ? 0.1837 0.0537 0.1791 0.0162  -0.0047 -0.0289 15  TRP D C   
6495 O  O   . TRP D 15  ? 0.2055 0.0094 0.2293 -0.0251 0.0450  -0.0059 15  TRP D O   
6496 C  CB  . TRP D 15  ? 0.1717 0.0075 0.1740 -0.0127 0.0443  -0.0094 15  TRP D CB  
6497 C  CG  . TRP D 15  ? 0.1516 0.0069 0.1789 -0.0052 0.0133  -0.0084 15  TRP D CG  
6498 C  CD1 . TRP D 15  ? 0.2002 0.0100 0.1758 -0.0044 0.0140  -0.0161 15  TRP D CD1 
6499 C  CD2 . TRP D 15  ? 0.1610 0.0083 0.1399 0.0010  -0.0094 0.0160  15  TRP D CD2 
6500 N  NE1 . TRP D 15  ? 0.1938 0.0201 0.1518 -0.0086 0.0150  -0.0046 15  TRP D NE1 
6501 C  CE2 . TRP D 15  ? 0.1676 0.0129 0.1444 -0.0027 -0.0228 0.0301  15  TRP D CE2 
6502 C  CE3 . TRP D 15  ? 0.1618 0.0143 0.1512 -0.0348 -0.0073 -0.0033 15  TRP D CE3 
6503 C  CZ2 . TRP D 15  ? 0.1943 0.0102 0.1349 0.0185  -0.0230 -0.0182 15  TRP D CZ2 
6504 C  CZ3 . TRP D 15  ? 0.1744 0.0094 0.1584 -0.0193 -0.0352 -0.0068 15  TRP D CZ3 
6505 C  CH2 . TRP D 15  ? 0.1991 0.0194 0.1309 0.0312  -0.0210 0.0001  15  TRP D CH2 
6506 N  N   . SER D 16  ? 0.1547 0.0092 0.1806 -0.0189 0.0056  -0.0100 16  SER D N   
6507 C  CA  . SER D 16  ? 0.1524 0.0146 0.1858 -0.0308 -0.0240 -0.0124 16  SER D CA  
6508 C  C   . SER D 16  ? 0.1826 0.0122 0.2408 -0.0143 0.0296  0.0105  16  SER D C   
6509 O  O   . SER D 16  ? 0.2006 0.0203 0.1949 -0.0175 0.0082  0.0064  16  SER D O   
6510 C  CB  . SER D 16  ? 0.1894 0.0398 0.2063 -0.0212 -0.0289 0.0011  16  SER D CB  
6511 O  OG  . SER D 16  ? 0.2066 0.0436 0.2743 -0.0010 0.0079  -0.0204 16  SER D OG  
6512 N  N   . LYS D 17  ? 0.1671 0.0157 0.1964 -0.0387 0.0064  -0.0024 17  LYS D N   
6513 C  CA  . LYS D 17  ? 0.1498 0.0160 0.2389 -0.0372 0.0423  -0.0096 17  LYS D CA  
6514 C  C   . LYS D 17  ? 0.1718 0.0086 0.2415 -0.0001 0.0183  -0.0234 17  LYS D C   
6515 O  O   . LYS D 17  ? 0.2343 0.0081 0.3271 -0.0153 0.0043  -0.0161 17  LYS D O   
6516 C  CB  . LYS D 17  ? 0.1634 0.0136 0.2343 -0.0126 0.0317  -0.0248 17  LYS D CB  
6517 C  CG  . LYS D 17  ? 0.1492 0.0436 0.2579 -0.0065 0.0523  0.0255  17  LYS D CG  
6518 C  CD  . LYS D 17  ? 0.1578 0.0150 0.2765 -0.0352 0.0779  -0.0073 17  LYS D CD  
6519 C  CE  . LYS D 17  ? 0.1859 0.0174 0.2579 -0.0106 0.0097  -0.0192 17  LYS D CE  
6520 N  NZ  . LYS D 17  ? 0.1949 0.0267 0.2688 -0.0234 0.0229  -0.0425 17  LYS D NZ  
6521 N  N   . LYS D 18  ? 0.2146 0.0113 0.2718 -0.0264 0.0345  0.0161  18  LYS D N   
6522 C  CA  . LYS D 18  ? 0.2028 0.0407 0.2084 -0.0281 0.0247  0.0227  18  LYS D CA  
6523 C  C   . LYS D 18  ? 0.2210 0.0463 0.2131 -0.0216 0.0140  0.0552  18  LYS D C   
6524 O  O   . LYS D 18  ? 0.2847 0.0150 0.3274 -0.0167 0.0415  0.0465  18  LYS D O   
6525 C  CB  . LYS D 18  ? 0.2365 0.0909 0.1979 -0.0528 -0.0063 0.0392  18  LYS D CB  
6526 C  CG  . LYS D 18  ? 0.2700 0.2211 0.2033 -0.1030 0.0080  0.0262  18  LYS D CG  
6527 C  CD  . LYS D 18  ? 0.2885 0.3470 0.2070 -0.0979 -0.0288 0.0489  18  LYS D CD  
6528 C  CE  . LYS D 18  ? 0.4444 0.3822 0.1683 -0.1023 0.0089  0.0124  18  LYS D CE  
6529 N  NZ  . LYS D 18  ? 0.4381 0.6161 0.2299 -0.2674 -0.0299 -0.0011 18  LYS D NZ  
6530 N  N   . TYR D 19  ? 0.2348 0.0066 0.2170 -0.0074 0.0214  -0.0030 19  TYR D N   
6531 C  CA  . TYR D 19  ? 0.2013 0.0182 0.1821 -0.0062 -0.0184 -0.0073 19  TYR D CA  
6532 C  C   . TYR D 19  ? 0.2182 0.0147 0.1776 0.0032  -0.0145 -0.0029 19  TYR D C   
6533 O  O   . TYR D 19  ? 0.2279 0.0071 0.1730 -0.0052 -0.0064 0.0109  19  TYR D O   
6534 C  CB  . TYR D 19  ? 0.2413 0.0081 0.1682 -0.0039 -0.0027 -0.0167 19  TYR D CB  
6535 C  CG  . TYR D 19  ? 0.2067 0.0074 0.2019 0.0005  0.0040  0.0144  19  TYR D CG  
6536 C  CD1 . TYR D 19  ? 0.1919 0.0311 0.2001 -0.0025 0.0120  0.0097  19  TYR D CD1 
6537 C  CD2 . TYR D 19  ? 0.2285 0.0084 0.2054 -0.0161 0.0059  -0.0141 19  TYR D CD2 
6538 C  CE1 . TYR D 19  ? 0.2777 0.0104 0.2404 0.0242  -0.0150 0.0196  19  TYR D CE1 
6539 C  CE2 . TYR D 19  ? 0.2017 0.0138 0.2198 -0.0376 0.0019  -0.0073 19  TYR D CE2 
6540 C  CZ  . TYR D 19  ? 0.2381 0.0206 0.2184 -0.0047 -0.0377 0.0061  19  TYR D CZ  
6541 O  OH  . TYR D 19  ? 0.2970 0.0965 0.2091 -0.0005 -0.0542 0.0154  19  TYR D OH  
6542 N  N   . PRO D 20  ? 0.2667 0.0071 0.1987 -0.0145 -0.0005 -0.0006 20  PRO D N   
6543 C  CA  . PRO D 20  ? 0.2460 0.0253 0.2272 -0.0612 -0.0266 -0.0204 20  PRO D CA  
6544 C  C   . PRO D 20  ? 0.2138 0.0086 0.1495 -0.0103 -0.0207 -0.0146 20  PRO D C   
6545 O  O   . PRO D 20  ? 0.2276 0.0082 0.2012 -0.0004 -0.0255 -0.0188 20  PRO D O   
6546 C  CB  . PRO D 20  ? 0.3376 0.0089 0.2794 -0.0199 -0.0484 -0.0164 20  PRO D CB  
6547 C  CG  . PRO D 20  ? 0.3358 0.0378 0.3001 0.0583  -0.0556 -0.0690 20  PRO D CG  
6548 C  CD  . PRO D 20  ? 0.2833 0.0068 0.2370 0.0064  0.0139  -0.0087 20  PRO D CD  
6549 N  N   . SER D 21  ? 0.2544 0.0094 0.1629 -0.0165 0.0196  -0.0192 21  SER D N   
6550 C  CA  . SER D 21  ? 0.2064 0.0198 0.1733 -0.0197 0.0086  0.0072  21  SER D CA  
6551 C  C   . SER D 21  ? 0.2424 0.0208 0.1203 -0.0233 -0.0158 0.0055  21  SER D C   
6552 O  O   . SER D 21  ? 0.2827 0.0162 0.1604 -0.0507 0.0238  0.0047  21  SER D O   
6553 C  CB  . SER D 21  ? 0.2146 0.0286 0.1958 -0.0167 -0.0086 -0.0291 21  SER D CB  
6554 O  OG  . SER D 21  ? 0.2343 0.0232 0.2127 -0.0333 0.0185  -0.0346 21  SER D OG  
6555 N  N   . CYS D 22  ? 0.1647 0.0165 0.1388 0.0030  0.0006  -0.0337 22  CYS D N   
6556 C  CA  . CYS D 22  ? 0.1822 0.0092 0.1539 0.0047  -0.0167 -0.0206 22  CYS D CA  
6557 C  C   . CYS D 22  ? 0.1658 0.0155 0.2109 0.0029  -0.0313 -0.0330 22  CYS D C   
6558 O  O   . CYS D 22  ? 0.2200 0.0208 0.2171 0.0251  -0.0283 -0.0201 22  CYS D O   
6559 C  CB  . CYS D 22  ? 0.2147 0.0128 0.1719 -0.0269 -0.0007 -0.0220 22  CYS D CB  
6560 S  SG  . CYS D 22  ? 0.2019 0.0068 0.1806 -0.0084 0.0054  0.0040  22  CYS D SG  
6561 N  N   . GLY D 23  ? 0.1965 0.0110 0.2037 -0.0301 -0.0290 0.0053  23  GLY D N   
6562 C  CA  . GLY D 23  ? 0.1895 0.0607 0.2275 -0.0488 -0.0179 0.0069  23  GLY D CA  
6563 C  C   . GLY D 23  ? 0.2435 0.0088 0.2315 -0.0217 -0.0176 -0.0087 23  GLY D C   
6564 O  O   . GLY D 23  ? 0.3101 0.0489 0.2772 -0.0199 -0.0758 -0.0288 23  GLY D O   
6565 N  N   . GLY D 24  ? 0.2433 0.0226 0.2037 -0.0187 0.0063  -0.0065 24  GLY D N   
6566 C  CA  . GLY D 24  ? 0.3004 0.0401 0.1833 -0.0653 -0.0245 0.0260  24  GLY D CA  
6567 C  C   . GLY D 24  ? 0.3086 0.0325 0.1766 -0.0877 -0.0111 -0.0075 24  GLY D C   
6568 O  O   . GLY D 24  ? 0.3844 0.0632 0.2283 -0.0610 -0.0119 -0.0410 24  GLY D O   
6569 N  N   . LEU D 25  ? 0.2745 0.0571 0.2249 -0.1057 -0.0002 0.0183  25  LEU D N   
6570 C  CA  . LEU D 25  ? 0.2994 0.0536 0.1861 -0.0801 -0.0425 0.0220  25  LEU D CA  
6571 C  C   . LEU D 25  ? 0.2979 0.0593 0.1471 -0.0890 -0.0425 0.0210  25  LEU D C   
6572 O  O   . LEU D 25  ? 0.2696 0.0656 0.1611 -0.0491 -0.0138 -0.0174 25  LEU D O   
6573 C  CB  . LEU D 25  ? 0.4196 0.2058 0.1979 -0.1489 -0.0416 -0.0679 25  LEU D CB  
6574 C  CG  . LEU D 25  ? 0.3413 0.2020 0.2698 -0.1129 -0.0370 -0.0172 25  LEU D CG  
6575 C  CD1 . LEU D 25  ? 0.6596 0.3441 0.2495 -0.2121 -0.0521 -0.0332 25  LEU D CD1 
6576 C  CD2 . LEU D 25  ? 0.3926 0.3249 0.2593 -0.0630 -0.0669 -0.0283 25  LEU D CD2 
6577 N  N   . LEU D 26  ? 0.3343 0.0643 0.1654 -0.1030 -0.0159 0.0295  26  LEU D N   
6578 C  CA  . LEU D 26  ? 0.2472 0.0983 0.1205 -0.0719 0.0200  -0.0179 26  LEU D CA  
6579 C  C   . LEU D 26  ? 0.2275 0.0146 0.1437 -0.0345 -0.0069 0.0140  26  LEU D C   
6580 O  O   . LEU D 26  ? 0.2160 0.0435 0.1615 -0.0003 -0.0116 -0.0111 26  LEU D O   
6581 C  CB  . LEU D 26  ? 0.3484 0.0944 0.1288 -0.0154 0.0469  0.0271  26  LEU D CB  
6582 C  CG  . LEU D 26  ? 0.4985 0.2518 0.1162 -0.0040 0.0413  0.0186  26  LEU D CG  
6583 C  CD1 . LEU D 26  ? 0.5709 0.3301 0.2196 -0.0238 0.1747  0.0788  26  LEU D CD1 
6584 C  CD2 . LEU D 26  ? 0.5793 0.3085 0.1941 -0.0094 -0.0566 0.0350  26  LEU D CD2 
6585 N  N   . GLN D 27  ? 0.2186 0.0394 0.1464 -0.0250 -0.0044 0.0074  27  GLN D N   
6586 C  CA  . GLN D 27  ? 0.2174 0.0101 0.1404 -0.0281 0.0140  -0.0043 27  GLN D CA  
6587 C  C   . GLN D 27  ? 0.1700 0.0071 0.1126 -0.0060 -0.0337 0.0086  27  GLN D C   
6588 O  O   . GLN D 27  ? 0.1942 0.0155 0.1574 0.0224  -0.0066 0.0304  27  GLN D O   
6589 C  CB  . GLN D 27  ? 0.1656 0.0107 0.1428 -0.0255 -0.0100 0.0076  27  GLN D CB  
6590 C  CG  . GLN D 27  ? 0.2242 0.0136 0.1926 -0.0385 -0.0381 -0.0033 27  GLN D CG  
6591 C  CD  . GLN D 27  ? 0.1962 0.0165 0.1576 -0.0337 -0.0176 -0.0218 27  GLN D CD  
6592 O  OE1 . GLN D 27  ? 0.2376 0.0171 0.1568 -0.0331 -0.0001 -0.0300 27  GLN D OE1 
6593 N  NE2 . GLN D 27  ? 0.2269 0.0099 0.1646 -0.0282 0.0093  -0.0014 27  GLN D NE2 
6594 N  N   . SER D 28  ? 0.1675 0.0084 0.0938 -0.0073 -0.0104 -0.0119 28  SER D N   
6595 C  CA  . SER D 28  ? 0.1392 0.0103 0.1291 -0.0097 0.0100  -0.0209 28  SER D CA  
6596 C  C   . SER D 28  ? 0.1377 0.0162 0.1309 0.0337  0.0127  0.0154  28  SER D C   
6597 O  O   . SER D 28  ? 0.1762 0.0267 0.1387 0.0057  0.0047  0.0190  28  SER D O   
6598 C  CB  . SER D 28  ? 0.1551 0.0063 0.1768 -0.0028 0.0079  0.0004  28  SER D CB  
6599 O  OG  . SER D 28  ? 0.1984 0.0075 0.1796 0.0154  0.0228  0.0011  28  SER D OG  
6600 N  N   . PRO D 29  ? 0.1060 0.0120 0.1189 0.0115  -0.0012 0.0222  29  PRO D N   
6601 C  CA  . PRO D 29  ? 0.1131 0.0091 0.1215 -0.0048 -0.0109 0.0175  29  PRO D CA  
6602 C  C   . PRO D 29  ? 0.1511 0.0085 0.1142 0.0054  -0.0249 0.0134  29  PRO D C   
6603 O  O   . PRO D 29  ? 0.1737 0.0063 0.1800 -0.0028 -0.0228 -0.0001 29  PRO D O   
6604 C  CB  . PRO D 29  ? 0.1633 0.0081 0.1372 0.0163  0.0172  0.0052  29  PRO D CB  
6605 C  CG  . PRO D 29  ? 0.1375 0.0071 0.1303 -0.0098 0.0017  -0.0022 29  PRO D CG  
6606 C  CD  . PRO D 29  ? 0.1677 0.0096 0.1310 -0.0001 0.0167  -0.0202 29  PRO D CD  
6607 N  N   . ILE D 30  ? 0.1742 0.0134 0.1198 0.0194  -0.0134 0.0217  30  ILE D N   
6608 C  CA  . ILE D 30  ? 0.1702 0.0084 0.1236 0.0052  -0.0239 0.0139  30  ILE D CA  
6609 C  C   . ILE D 30  ? 0.1366 0.0078 0.1360 0.0106  -0.0125 0.0076  30  ILE D C   
6610 O  O   . ILE D 30  ? 0.1717 0.0082 0.1525 -0.0022 -0.0084 0.0166  30  ILE D O   
6611 C  CB  . ILE D 30  ? 0.1697 0.0071 0.1336 0.0113  0.0005  -0.0014 30  ILE D CB  
6612 C  CG1 . ILE D 30  ? 0.1995 0.0197 0.1923 0.0073  0.0236  -0.0031 30  ILE D CG1 
6613 C  CG2 . ILE D 30  ? 0.2916 0.0064 0.1683 -0.0019 -0.0275 -0.0027 30  ILE D CG2 
6614 C  CD1 . ILE D 30  ? 0.2429 0.0677 0.1719 0.0226  0.0247  -0.0480 30  ILE D CD1 
6615 N  N   . ASP D 31  ? 0.1541 0.0118 0.1597 0.0285  -0.0020 -0.0002 31  ASP D N   
6616 C  CA  . ASP D 31  ? 0.1334 0.0084 0.1230 0.0160  0.0212  -0.0002 31  ASP D CA  
6617 C  C   . ASP D 31  ? 0.1345 0.0437 0.1507 -0.0051 0.0077  0.0136  31  ASP D C   
6618 O  O   . ASP D 31  ? 0.1958 0.0678 0.1506 -0.0093 -0.0066 0.0420  31  ASP D O   
6619 C  CB  . ASP D 31  ? 0.1439 0.0089 0.1873 0.0170  0.0215  0.0081  31  ASP D CB  
6620 C  CG  . ASP D 31  ? 0.1438 0.0068 0.2001 0.0044  -0.0113 0.0074  31  ASP D CG  
6621 O  OD1 . ASP D 31  ? 0.1681 0.0629 0.1980 0.0046  -0.0109 0.0052  31  ASP D OD1 
6622 O  OD2 . ASP D 31  ? 0.2480 0.0441 0.2046 0.0590  -0.0122 0.0111  31  ASP D OD2 
6623 N  N   . LEU D 32  ? 0.1833 0.0088 0.2062 -0.0174 0.0179  0.0106  32  LEU D N   
6624 C  CA  . LEU D 32  ? 0.1686 0.0610 0.2164 -0.0149 -0.0019 0.0694  32  LEU D CA  
6625 C  C   . LEU D 32  ? 0.2218 0.0385 0.1550 -0.0222 0.0152  0.0647  32  LEU D C   
6626 O  O   . LEU D 32  ? 0.2587 0.0508 0.1888 0.0031  -0.0300 0.0265  32  LEU D O   
6627 C  CB  . LEU D 32  ? 0.1769 0.1205 0.1976 -0.0142 -0.0035 0.0491  32  LEU D CB  
6628 C  CG  . LEU D 32  ? 0.1786 0.1139 0.1808 -0.0011 -0.0013 0.0108  32  LEU D CG  
6629 C  CD1 . LEU D 32  ? 0.2092 0.1348 0.2174 -0.0234 -0.0303 0.0154  32  LEU D CD1 
6630 C  CD2 . LEU D 32  ? 0.1905 0.2521 0.2130 0.0611  0.0216  -0.0305 32  LEU D CD2 
6631 N  N   . HIS D 33  ? 0.2037 0.0267 0.1653 0.0353  0.0055  0.0446  33  HIS D N   
6632 C  CA  . HIS D 33  ? 0.2108 0.0365 0.1815 0.0375  -0.0161 0.0580  33  HIS D CA  
6633 C  C   . HIS D 33  ? 0.1707 0.0884 0.1751 0.0159  -0.0116 0.0379  33  HIS D C   
6634 O  O   . HIS D 33  ? 0.1901 0.0893 0.1681 0.0040  0.0168  0.0432  33  HIS D O   
6635 C  CB  . HIS D 33  ? 0.2064 0.1586 0.1883 0.0029  -0.0070 0.0138  33  HIS D CB  
6636 C  CG  . HIS D 33  ? 0.1898 0.1205 0.1506 0.0039  0.0121  0.0591  33  HIS D CG  
6637 N  ND1 . HIS D 33  ? 0.3281 0.1401 0.2273 -0.0487 -0.0655 0.1126  33  HIS D ND1 
6638 C  CD2 . HIS D 33  ? 0.1549 0.2031 0.1531 0.0104  0.0126  0.0297  33  HIS D CD2 
6639 C  CE1 . HIS D 33  ? 0.2736 0.2246 0.1722 -0.0458 -0.0509 0.0905  33  HIS D CE1 
6640 N  NE2 . HIS D 33  ? 0.1668 0.2462 0.1415 -0.0170 -0.0193 0.0490  33  HIS D NE2 
6641 N  N   . SER D 34  ? 0.2199 0.0934 0.1890 -0.0041 -0.0078 0.0806  34  SER D N   
6642 C  CA  . SER D 34  ? 0.2666 0.0645 0.1930 0.0268  0.0015  0.0652  34  SER D CA  
6643 C  C   . SER D 34  ? 0.1832 0.0855 0.1915 0.0044  0.0075  0.0693  34  SER D C   
6644 O  O   . SER D 34  ? 0.1840 0.1462 0.1956 0.0468  0.0029  0.0803  34  SER D O   
6645 C  CB  . SER D 34  ? 0.2292 0.0645 0.2528 0.0312  0.0543  0.0558  34  SER D CB  
6646 O  OG  . SER D 34  ? 0.2663 0.1625 0.3766 -0.0129 -0.0088 0.0432  34  SER D OG  
6647 N  N   . ASP D 35  ? 0.1805 0.0645 0.1904 0.0047  -0.0228 0.0340  35  ASP D N   
6648 C  CA  . ASP D 35  ? 0.1762 0.0357 0.2005 0.0079  -0.0254 0.0410  35  ASP D CA  
6649 C  C   . ASP D 35  ? 0.1509 0.1290 0.2008 0.0380  0.0077  0.0340  35  ASP D C   
6650 O  O   . ASP D 35  ? 0.2451 0.1728 0.2107 0.0519  0.0012  0.0298  35  ASP D O   
6651 C  CB  . ASP D 35  ? 0.1627 0.1327 0.2583 0.0066  -0.0036 0.0372  35  ASP D CB  
6652 C  CG  . ASP D 35  ? 0.2008 0.1363 0.2806 0.0451  -0.0306 0.0445  35  ASP D CG  
6653 O  OD1 . ASP D 35  ? 0.2178 0.2557 0.2429 0.0418  0.0089  0.0389  35  ASP D OD1 
6654 O  OD2 . ASP D 35  ? 0.1708 0.2088 0.2279 0.0325  -0.0034 0.0740  35  ASP D OD2 
6655 N  N   . ILE D 36  ? 0.1902 0.0851 0.2055 0.0330  -0.0184 0.0201  36  ILE D N   
6656 C  CA  . ILE D 36  ? 0.1650 0.0694 0.2788 0.0252  0.0255  0.0425  36  ILE D CA  
6657 C  C   . ILE D 36  ? 0.1861 0.0615 0.1999 0.0033  -0.0120 0.0036  36  ILE D C   
6658 O  O   . ILE D 36  ? 0.2108 0.1187 0.2671 0.0557  -0.0064 0.0061  36  ILE D O   
6659 C  CB  . ILE D 36  ? 0.2439 0.1101 0.2367 -0.0005 -0.0236 0.0678  36  ILE D CB  
6660 C  CG1 . ILE D 36  ? 0.3061 0.1245 0.2381 0.0278  -0.0069 0.0496  36  ILE D CG1 
6661 C  CG2 . ILE D 36  ? 0.2685 0.1159 0.3904 -0.0201 -0.0013 0.0128  36  ILE D CG2 
6662 C  CD1 . ILE D 36  ? 0.2875 0.1744 0.2652 0.0741  -0.0263 0.0188  36  ILE D CD1 
6663 N  N   . LEU D 37  ? 0.1834 0.0462 0.1480 0.0057  -0.0108 0.0274  37  LEU D N   
6664 C  CA  . LEU D 37  ? 0.1941 0.0868 0.1634 0.0474  0.0185  0.0027  37  LEU D CA  
6665 C  C   . LEU D 37  ? 0.1449 0.1209 0.1815 0.0254  0.0196  0.0424  37  LEU D C   
6666 O  O   . LEU D 37  ? 0.1861 0.1546 0.2344 0.0608  0.0130  0.0748  37  LEU D O   
6667 C  CB  . LEU D 37  ? 0.2026 0.1060 0.1829 0.0174  0.0215  -0.0189 37  LEU D CB  
6668 C  CG  . LEU D 37  ? 0.2206 0.1047 0.1735 0.0471  0.0036  -0.0124 37  LEU D CG  
6669 C  CD1 . LEU D 37  ? 0.2707 0.1678 0.1936 0.0136  0.0095  -0.0710 37  LEU D CD1 
6670 C  CD2 . LEU D 37  ? 0.1965 0.1351 0.1916 0.0122  0.0204  0.0590  37  LEU D CD2 
6671 N  N   . GLN D 38  ? 0.1549 0.1318 0.1746 0.0147  0.0462  0.0122  38  GLN D N   
6672 C  CA  . GLN D 38  ? 0.1658 0.0746 0.1848 0.0388  0.0471  0.0255  38  GLN D CA  
6673 C  C   . GLN D 38  ? 0.1627 0.0830 0.1977 0.0489  0.0610  0.0607  38  GLN D C   
6674 O  O   . GLN D 38  ? 0.1852 0.0832 0.1930 0.0388  0.0063  0.0636  38  GLN D O   
6675 C  CB  . GLN D 38  ? 0.2588 0.1295 0.1751 0.0552  0.0263  -0.0114 38  GLN D CB  
6676 C  CG  . GLN D 38  ? 0.2350 0.2342 0.2031 0.0444  0.0306  0.0210  38  GLN D CG  
6677 C  CD  . GLN D 38  ? 0.3416 0.3134 0.2092 0.0763  -0.0585 0.0183  38  GLN D CD  
6678 O  OE1 . GLN D 38  ? 0.3350 0.4659 0.3470 0.1312  -0.0539 0.0285  38  GLN D OE1 
6679 N  NE2 . GLN D 38  ? 0.4275 0.1779 0.2295 -0.0341 0.0179  -0.0172 38  GLN D NE2 
6680 N  N   . TYR D 39  ? 0.1927 0.0611 0.2139 0.0230  0.0473  0.0337  39  TYR D N   
6681 C  CA  . TYR D 39  ? 0.1816 0.0258 0.2117 0.0557  0.0318  0.0285  39  TYR D CA  
6682 C  C   . TYR D 39  ? 0.1726 0.0162 0.1624 0.0295  0.0182  0.0237  39  TYR D C   
6683 O  O   . TYR D 39  ? 0.2223 0.1065 0.1640 0.0237  0.0006  0.0245  39  TYR D O   
6684 C  CB  . TYR D 39  ? 0.1787 0.0453 0.2913 0.0348  -0.0027 0.0806  39  TYR D CB  
6685 C  CG  . TYR D 39  ? 0.1952 0.0671 0.2346 0.0457  0.0454  0.0300  39  TYR D CG  
6686 C  CD1 . TYR D 39  ? 0.2331 0.0927 0.2135 0.0190  0.0425  0.0529  39  TYR D CD1 
6687 C  CD2 . TYR D 39  ? 0.2295 0.0378 0.2062 0.0212  0.0457  -0.0071 39  TYR D CD2 
6688 C  CE1 . TYR D 39  ? 0.2135 0.1017 0.1997 0.0134  0.0439  0.0352  39  TYR D CE1 
6689 C  CE2 . TYR D 39  ? 0.2498 0.0556 0.1949 -0.0181 0.0708  0.0181  39  TYR D CE2 
6690 C  CZ  . TYR D 39  ? 0.2288 0.0520 0.1999 -0.0148 0.0436  0.0325  39  TYR D CZ  
6691 O  OH  . TYR D 39  ? 0.2426 0.0835 0.2485 0.0140  0.0770  0.0113  39  TYR D OH  
6692 N  N   . ASP D 40  ? 0.1951 0.0462 0.1693 0.0460  0.0291  0.0449  40  ASP D N   
6693 C  CA  . ASP D 40  ? 0.2024 0.0440 0.1952 0.0407  0.0397  0.0394  40  ASP D CA  
6694 C  C   . ASP D 40  ? 0.2091 0.0226 0.1553 0.0222  0.0301  0.0164  40  ASP D C   
6695 O  O   . ASP D 40  ? 0.1916 0.1123 0.1909 0.0571  0.0142  0.0591  40  ASP D O   
6696 C  CB  . ASP D 40  ? 0.2899 0.0540 0.1864 0.0765  0.0543  0.0710  40  ASP D CB  
6697 C  CG  . ASP D 40  ? 0.2846 0.0615 0.2393 0.0766  0.0761  0.0669  40  ASP D CG  
6698 O  OD1 . ASP D 40  ? 0.2648 0.0502 0.2153 0.0363  0.0430  0.0433  40  ASP D OD1 
6699 O  OD2 . ASP D 40  ? 0.4112 0.0864 0.3524 0.0705  0.0687  0.1227  40  ASP D OD2 
6700 N  N   . ALA D 41  ? 0.1775 0.0198 0.1850 0.0480  0.0698  0.0176  41  ALA D N   
6701 C  CA  . ALA D 41  ? 0.1822 0.0723 0.1841 0.0317  0.0683  0.0515  41  ALA D CA  
6702 C  C   . ALA D 41  ? 0.1837 0.0495 0.2337 0.0203  0.0442  0.0383  41  ALA D C   
6703 O  O   . ALA D 41  ? 0.1726 0.0871 0.2449 0.0358  0.0538  0.0193  41  ALA D O   
6704 C  CB  . ALA D 41  ? 0.2441 0.0801 0.2081 -0.0114 0.0421  0.0813  41  ALA D CB  
6705 N  N   . SER D 42  ? 0.1913 0.0393 0.1761 0.0362  0.0474  0.0345  42  SER D N   
6706 C  CA  . SER D 42  ? 0.2487 0.0238 0.2200 0.0631  0.0509  -0.0012 42  SER D CA  
6707 C  C   . SER D 42  ? 0.2209 0.0891 0.2064 0.0587  0.0347  0.0313  42  SER D C   
6708 O  O   . SER D 42  ? 0.2309 0.1417 0.2728 0.0776  0.0117  0.0469  42  SER D O   
6709 C  CB  . SER D 42  ? 0.3199 0.0207 0.3547 0.0364  0.1015  -0.0312 42  SER D CB  
6710 O  OG  . SER D 42  ? 0.3296 0.0938 0.3879 0.0422  0.0905  0.0359  42  SER D OG  
6711 N  N   . LEU D 43  ? 0.2401 0.1108 0.2001 0.0565  0.0527  0.0368  43  LEU D N   
6712 C  CA  . LEU D 43  ? 0.1712 0.1482 0.2107 0.0411  0.0486  0.0725  43  LEU D CA  
6713 C  C   . LEU D 43  ? 0.1879 0.1585 0.2185 0.0482  0.0068  0.0792  43  LEU D C   
6714 O  O   . LEU D 43  ? 0.1904 0.1474 0.2716 0.0093  0.0540  0.0526  43  LEU D O   
6715 C  CB  . LEU D 43  ? 0.1324 0.1363 0.2016 0.0242  0.0238  0.0540  43  LEU D CB  
6716 C  CG  . LEU D 43  ? 0.1841 0.0846 0.2436 0.0671  0.0354  0.0502  43  LEU D CG  
6717 C  CD1 . LEU D 43  ? 0.1747 0.0613 0.2498 0.0523  0.0314  0.0111  43  LEU D CD1 
6718 C  CD2 . LEU D 43  ? 0.2150 0.0767 0.3328 0.0544  0.0545  0.0760  43  LEU D CD2 
6719 N  N   . THR D 44  ? 0.1855 0.2090 0.2517 0.0467  0.0440  0.0895  44  THR D N   
6720 C  CA  . THR D 44  ? 0.1873 0.2509 0.2002 0.0358  0.0504  0.0573  44  THR D CA  
6721 C  C   . THR D 44  ? 0.1926 0.1385 0.2002 0.0491  0.0675  0.0756  44  THR D C   
6722 O  O   . THR D 44  ? 0.1714 0.1069 0.2618 0.0469  0.0414  0.0848  44  THR D O   
6723 C  CB  . THR D 44  ? 0.1765 0.3317 0.2755 0.1147  0.0782  0.1232  44  THR D CB  
6724 O  OG1 . THR D 44  ? 0.2561 0.3260 0.3134 0.1295  0.0294  0.0233  44  THR D OG1 
6725 C  CG2 . THR D 44  ? 0.3644 0.3815 0.2372 0.0120  0.0857  0.1037  44  THR D CG2 
6726 N  N   . PRO D 45  ? 0.2372 0.1861 0.2480 -0.0046 0.0593  0.1154  45  PRO D N   
6727 C  CA  . PRO D 45  ? 0.1891 0.0918 0.2526 -0.0039 0.0147  0.1103  45  PRO D CA  
6728 C  C   . PRO D 45  ? 0.2157 0.0807 0.2930 0.0347  0.0342  0.0522  45  PRO D C   
6729 O  O   . PRO D 45  ? 0.2390 0.1834 0.3157 0.0864  0.0598  0.0943  45  PRO D O   
6730 C  CB  . PRO D 45  ? 0.2552 0.1202 0.2759 -0.0570 0.0217  0.0845  45  PRO D CB  
6731 C  CG  . PRO D 45  ? 0.2304 0.1913 0.2942 -0.0903 -0.0247 0.1238  45  PRO D CG  
6732 C  CD  . PRO D 45  ? 0.2575 0.1721 0.2507 -0.0128 0.0190  0.1419  45  PRO D CD  
6733 N  N   . LEU D 46  ? 0.1961 0.0683 0.2234 0.0211  -0.0294 0.0453  46  LEU D N   
6734 C  CA  . LEU D 46  ? 0.1416 0.0882 0.2415 0.0326  -0.0084 0.0552  46  LEU D CA  
6735 C  C   . LEU D 46  ? 0.1665 0.1446 0.2315 0.0328  -0.0231 0.0424  46  LEU D C   
6736 O  O   . LEU D 46  ? 0.2940 0.1269 0.2365 0.0270  0.0381  0.0350  46  LEU D O   
6737 C  CB  . LEU D 46  ? 0.1787 0.1367 0.2527 0.0252  0.0019  0.0666  46  LEU D CB  
6738 C  CG  . LEU D 46  ? 0.1736 0.0983 0.2522 0.0834  -0.0069 -0.0208 46  LEU D CG  
6739 C  CD1 . LEU D 46  ? 0.1967 0.1428 0.3039 0.0060  0.0397  -0.0682 46  LEU D CD1 
6740 C  CD2 . LEU D 46  ? 0.2597 0.1293 0.3560 0.0134  0.0561  -0.0901 46  LEU D CD2 
6741 N  N   . GLU D 47  ? 0.1591 0.1370 0.2918 0.0319  -0.0400 0.0552  47  GLU D N   
6742 C  CA  . GLU D 47  ? 0.1855 0.1356 0.1701 -0.0211 -0.0062 0.0675  47  GLU D CA  
6743 C  C   . GLU D 47  ? 0.1787 0.0399 0.1830 -0.0201 -0.0307 0.0388  47  GLU D C   
6744 O  O   . GLU D 47  ? 0.2467 0.0366 0.2670 -0.0022 -0.0357 -0.0030 47  GLU D O   
6745 C  CB  . GLU D 47  ? 0.2303 0.2412 0.2646 0.0337  0.0533  0.1404  47  GLU D CB  
6746 C  CG  . GLU D 47  ? 0.3565 0.3988 0.3536 0.1280  0.1039  0.2723  47  GLU D CG  
6747 C  CD  . GLU D 47  ? 0.4271 0.5225 0.5132 0.1427  0.2119  0.3629  47  GLU D CD  
6748 O  OE1 . GLU D 47  ? 0.4625 0.8808 0.7914 0.3870  0.1408  0.2068  47  GLU D OE1 
6749 O  OE2 . GLU D 47  ? 0.5883 0.6357 0.7476 -0.0027 0.4495  0.1723  47  GLU D OE2 
6750 N  N   . PHE D 48  ? 0.1778 0.1471 0.1478 -0.0022 -0.0009 0.0137  48  PHE D N   
6751 C  CA  . PHE D 48  ? 0.2578 0.0678 0.1628 0.0197  0.0046  0.0074  48  PHE D CA  
6752 C  C   . PHE D 48  ? 0.2642 0.0674 0.2290 0.0015  0.0035  0.0544  48  PHE D C   
6753 O  O   . PHE D 48  ? 0.2090 0.1348 0.3708 -0.0201 -0.0687 0.0628  48  PHE D O   
6754 C  CB  . PHE D 48  ? 0.2584 0.0656 0.1936 0.0364  0.0051  0.0161  48  PHE D CB  
6755 C  CG  . PHE D 48  ? 0.2661 0.0568 0.2550 0.0173  -0.0117 0.0642  48  PHE D CG  
6756 C  CD1 . PHE D 48  ? 0.2770 0.0574 0.2157 0.0269  0.0386  0.0259  48  PHE D CD1 
6757 C  CD2 . PHE D 48  ? 0.2837 0.0542 0.2627 0.0242  -0.0052 0.0602  48  PHE D CD2 
6758 C  CE1 . PHE D 48  ? 0.2405 0.0999 0.2078 0.0445  0.0643  0.0363  48  PHE D CE1 
6759 C  CE2 . PHE D 48  ? 0.2766 0.1369 0.3076 0.0130  -0.0154 0.0467  48  PHE D CE2 
6760 C  CZ  . PHE D 48  ? 0.2292 0.1051 0.2354 0.0498  0.0458  0.0604  48  PHE D CZ  
6761 N  N   . GLN D 49  ? 0.3064 0.0686 0.2177 0.0374  0.0079  0.0801  49  GLN D N   
6762 C  CA  . GLN D 49  ? 0.2915 0.1453 0.1862 0.0398  -0.0102 -0.0104 49  GLN D CA  
6763 C  C   . GLN D 49  ? 0.1441 0.0866 0.2311 0.0414  -0.0114 0.0058  49  GLN D C   
6764 O  O   . GLN D 49  ? 0.2171 0.0656 0.1958 0.0057  0.0070  0.0144  49  GLN D O   
6765 C  CB  . GLN D 49  ? 0.3181 0.2204 0.1697 0.0152  0.0525  -0.0159 49  GLN D CB  
6766 C  CG  . GLN D 49  ? 0.3824 0.3494 0.1549 0.0210  0.1046  0.0018  49  GLN D CG  
6767 C  CD  . GLN D 49  ? 0.3471 0.2498 0.4137 0.1140  0.0598  0.1782  49  GLN D CD  
6768 O  OE1 . GLN D 49  ? 0.5182 0.1902 0.9114 0.0369  0.0139  0.2507  49  GLN D OE1 
6769 N  NE2 . GLN D 49  ? 0.2537 0.5704 0.8389 -0.0299 -0.0137 0.1722  49  GLN D NE2 
6770 N  N   . GLY D 50  ? 0.1678 0.1117 0.1861 0.0263  -0.0044 -0.0070 50  GLY D N   
6771 C  CA  . GLY D 50  ? 0.1647 0.1318 0.1834 0.0352  0.0067  0.0066  50  GLY D CA  
6772 C  C   . GLY D 50  ? 0.1489 0.0311 0.1987 0.0120  0.0106  0.0116  50  GLY D C   
6773 O  O   . GLY D 50  ? 0.1665 0.0310 0.2261 0.0317  0.0066  0.0307  50  GLY D O   
6774 N  N   . TYR D 51  ? 0.1610 0.0393 0.2223 0.0257  0.0251  0.0147  51  TYR D N   
6775 C  CA  . TYR D 51  ? 0.1266 0.0710 0.1866 0.0326  -0.0163 0.0075  51  TYR D CA  
6776 C  C   . TYR D 51  ? 0.1347 0.0216 0.1922 -0.0168 -0.0115 0.0505  51  TYR D C   
6777 O  O   . TYR D 51  ? 0.1442 0.0406 0.2306 0.0098  0.0219  0.0366  51  TYR D O   
6778 C  CB  . TYR D 51  ? 0.1203 0.0110 0.2178 0.0121  -0.0093 -0.0087 51  TYR D CB  
6779 C  CG  . TYR D 51  ? 0.1187 0.0259 0.2058 -0.0138 0.0106  -0.0210 51  TYR D CG  
6780 C  CD1 . TYR D 51  ? 0.1771 0.0399 0.1556 0.0011  0.0126  0.0053  51  TYR D CD1 
6781 C  CD2 . TYR D 51  ? 0.1303 0.0105 0.2794 -0.0125 0.0336  0.0243  51  TYR D CD2 
6782 C  CE1 . TYR D 51  ? 0.1441 0.0802 0.1718 0.0074  0.0074  0.0331  51  TYR D CE1 
6783 C  CE2 . TYR D 51  ? 0.1342 0.0092 0.2401 -0.0062 0.0430  0.0012  51  TYR D CE2 
6784 C  CZ  . TYR D 51  ? 0.1413 0.0086 0.2038 0.0018  -0.0009 0.0210  51  TYR D CZ  
6785 O  OH  . TYR D 51  ? 0.1137 0.0715 0.2115 0.0212  -0.0064 -0.0080 51  TYR D OH  
6786 N  N   . ASN D 52  ? 0.1035 0.0935 0.2577 0.0064  -0.0304 0.0423  52  ASN D N   
6787 C  CA  . ASN D 52  ? 0.1661 0.0359 0.2114 -0.0063 -0.0158 0.0372  52  ASN D CA  
6788 C  C   . ASN D 52  ? 0.1543 0.0758 0.2389 0.0108  -0.0062 0.0672  52  ASN D C   
6789 O  O   . ASN D 52  ? 0.1535 0.1033 0.2936 0.0086  0.0110  0.0712  52  ASN D O   
6790 C  CB  . ASN D 52  ? 0.1807 0.0285 0.2451 -0.0137 -0.0075 0.0187  52  ASN D CB  
6791 C  CG  . ASN D 52  ? 0.2031 0.1118 0.2655 -0.0548 -0.0167 0.0012  52  ASN D CG  
6792 O  OD1 . ASN D 52  ? 0.2491 0.2346 0.2491 -0.0643 -0.0027 0.0027  52  ASN D OD1 
6793 N  ND2 . ASN D 52  ? 0.3213 0.0771 0.3898 -0.0917 -0.0205 -0.0259 52  ASN D ND2 
6794 N  N   . LEU D 53  ? 0.1537 0.0626 0.2327 0.0171  -0.0040 0.0424  53  LEU D N   
6795 C  CA  . LEU D 53  ? 0.1243 0.0539 0.2134 0.0094  -0.0295 0.0258  53  LEU D CA  
6796 C  C   . LEU D 53  ? 0.1354 0.1060 0.1852 0.0281  -0.0086 0.0158  53  LEU D C   
6797 O  O   . LEU D 53  ? 0.2094 0.1126 0.2981 0.0954  0.0197  -0.0272 53  LEU D O   
6798 C  CB  . LEU D 53  ? 0.1352 0.0547 0.2381 0.0178  -0.0168 0.0178  53  LEU D CB  
6799 C  CG  . LEU D 53  ? 0.1124 0.1026 0.2285 0.0255  -0.0163 0.0352  53  LEU D CG  
6800 C  CD1 . LEU D 53  ? 0.1556 0.0532 0.3228 -0.0308 -0.0006 0.0178  53  LEU D CD1 
6801 C  CD2 . LEU D 53  ? 0.2031 0.1449 0.2307 -0.0141 0.0035  -0.0125 53  LEU D CD2 
6802 N  N   . SER D 54  ? 0.1175 0.1512 0.2368 0.0049  -0.0495 0.0818  54  SER D N   
6803 C  CA  . SER D 54  ? 0.1380 0.1751 0.1821 0.0295  -0.0226 0.0316  54  SER D CA  
6804 C  C   . SER D 54  ? 0.1405 0.1466 0.1929 0.0225  -0.0017 0.0254  54  SER D C   
6805 O  O   . SER D 54  ? 0.1708 0.1437 0.2596 0.0148  0.0178  0.0183  54  SER D O   
6806 C  CB  . SER D 54  ? 0.1380 0.1814 0.2309 0.0405  -0.0398 0.0356  54  SER D CB  
6807 O  OG  . SER D 54  ? 0.1556 0.3630 0.2035 0.0118  -0.0367 0.0650  54  SER D OG  
6808 N  N   . ALA D 55  ? 0.2455 0.1331 0.1819 0.0417  -0.0263 0.0122  55  ALA D N   
6809 C  CA  . ALA D 55  ? 0.2441 0.1719 0.2107 0.0200  0.0097  0.0441  55  ALA D CA  
6810 C  C   . ALA D 55  ? 0.1564 0.3668 0.1861 0.0814  -0.0420 0.0413  55  ALA D C   
6811 O  O   . ALA D 55  ? 0.3188 0.4238 0.1925 0.0253  -0.0063 0.0548  55  ALA D O   
6812 C  CB  . ALA D 55  ? 0.3510 0.2281 0.2459 0.0366  -0.0232 -0.0398 55  ALA D CB  
6813 N  N   . ASN D 56  ? 0.1765 0.4348 0.2425 0.1099  0.0034  0.0655  56  ASN D N   
6814 C  CA  . ASN D 56  ? 0.1535 0.3609 0.2540 -0.0477 -0.0359 0.0961  56  ASN D CA  
6815 C  C   . ASN D 56  ? 0.1582 0.3003 0.3718 0.0651  0.0057  0.1232  56  ASN D C   
6816 O  O   . ASN D 56  ? 0.2250 0.2967 0.5253 0.0351  -0.0337 0.2057  56  ASN D O   
6817 C  CB  . ASN D 56  ? 0.1566 0.3740 0.3195 -0.0542 -0.0397 0.1010  56  ASN D CB  
6818 C  CG  . ASN D 56  ? 0.1445 0.5123 0.4180 -0.1163 -0.0856 -0.0166 56  ASN D CG  
6819 O  OD1 . ASN D 56  ? 0.4451 0.7849 0.4958 -0.0782 -0.0831 -0.2401 56  ASN D OD1 
6820 N  ND2 . ASN D 56  ? 0.3096 0.7137 0.5653 -0.2040 0.1036  0.0092  56  ASN D ND2 
6821 N  N   . LYS D 57  ? 0.1352 0.2324 0.2875 -0.0212 0.0401  0.0802  57  LYS D N   
6822 C  CA  . LYS D 57  ? 0.1342 0.2081 0.3405 0.0085  0.0455  0.0945  57  LYS D CA  
6823 C  C   . LYS D 57  ? 0.0929 0.1895 0.2971 0.0119  -0.0040 0.0840  57  LYS D C   
6824 O  O   . LYS D 57  ? 0.1428 0.2297 0.2699 0.0721  0.0146  0.0892  57  LYS D O   
6825 C  CB  . LYS D 57  ? 0.1586 0.1646 0.3224 0.0409  0.0483  0.1141  57  LYS D CB  
6826 C  CG  . LYS D 57  ? 0.2222 0.2900 0.3371 0.0921  0.0973  0.1646  57  LYS D CG  
6827 C  CD  . LYS D 57  ? 0.2653 0.4979 0.3362 0.0161  0.1613  0.0340  57  LYS D CD  
6828 C  CE  . LYS D 57  ? 0.2794 0.5564 0.4853 0.0036  0.1743  -0.0745 57  LYS D CE  
6829 N  NZ  . LYS D 57  ? 0.2688 0.4060 0.5686 -0.0326 0.1538  -0.1371 57  LYS D NZ  
6830 N  N   . GLN D 58  ? 0.1259 0.1724 0.2570 0.0149  0.0303  0.0326  58  GLN D N   
6831 C  CA  . GLN D 58  ? 0.1356 0.2239 0.2922 -0.0231 0.0497  0.0252  58  GLN D CA  
6832 C  C   . GLN D 58  ? 0.1719 0.0826 0.2353 0.0451  0.0196  0.0526  58  GLN D C   
6833 O  O   . GLN D 58  ? 0.2282 0.1205 0.2640 0.0888  0.0407  0.0421  58  GLN D O   
6834 C  CB  . GLN D 58  ? 0.2444 0.3667 0.3059 0.0566  0.0976  0.0897  58  GLN D CB  
6835 C  CG  . GLN D 58  ? 0.2921 0.3531 0.4236 0.0053  0.1106  0.1768  58  GLN D CG  
6836 C  CD  . GLN D 58  ? 0.5371 0.2307 0.4393 -0.0069 0.0422  0.1781  58  GLN D CD  
6837 O  OE1 . GLN D 58  ? 0.2471 0.4296 0.4774 0.0282  -0.0859 0.0432  58  GLN D OE1 
6838 N  NE2 . GLN D 58  ? 0.2957 0.1981 0.7027 0.0023  -0.0584 0.1007  58  GLN D NE2 
6839 N  N   . PHE D 59  ? 0.1520 0.0904 0.2308 0.0218  0.0017  0.0562  59  PHE D N   
6840 C  CA  . PHE D 59  ? 0.1762 0.0767 0.2055 0.0335  -0.0027 0.0326  59  PHE D CA  
6841 C  C   . PHE D 59  ? 0.1503 0.0828 0.2026 0.0357  -0.0057 0.0398  59  PHE D C   
6842 O  O   . PHE D 59  ? 0.1717 0.1067 0.2303 0.0460  0.0135  0.0199  59  PHE D O   
6843 C  CB  . PHE D 59  ? 0.1870 0.0652 0.1908 0.0239  0.0229  0.0343  59  PHE D CB  
6844 C  CG  . PHE D 59  ? 0.1470 0.0476 0.2034 0.0373  0.0133  0.0012  59  PHE D CG  
6845 C  CD1 . PHE D 59  ? 0.1478 0.0446 0.2746 -0.0040 0.0227  0.0341  59  PHE D CD1 
6846 C  CD2 . PHE D 59  ? 0.1944 0.0356 0.2077 0.0185  0.0195  -0.0025 59  PHE D CD2 
6847 C  CE1 . PHE D 59  ? 0.1561 0.0774 0.2637 0.0647  0.0386  0.0252  59  PHE D CE1 
6848 C  CE2 . PHE D 59  ? 0.1611 0.1108 0.2496 0.0301  0.0184  0.0190  59  PHE D CE2 
6849 C  CZ  . PHE D 59  ? 0.1707 0.0739 0.2588 0.0219  0.0471  0.0335  59  PHE D CZ  
6850 N  N   . LEU D 60  ? 0.1798 0.0995 0.2304 0.0323  -0.0291 0.0341  60  LEU D N   
6851 C  CA  . LEU D 60  ? 0.1668 0.1257 0.2161 0.0416  -0.0137 0.0361  60  LEU D CA  
6852 C  C   . LEU D 60  ? 0.1699 0.0981 0.1492 0.0287  -0.0115 0.0505  60  LEU D C   
6853 O  O   . LEU D 60  ? 0.1726 0.1313 0.1613 0.0376  -0.0307 0.0416  60  LEU D O   
6854 C  CB  . LEU D 60  ? 0.2098 0.1054 0.2203 0.0377  0.0297  0.0477  60  LEU D CB  
6855 C  CG  . LEU D 60  ? 0.2881 0.0927 0.2453 -0.0004 0.0502  0.0401  60  LEU D CG  
6856 C  CD1 . LEU D 60  ? 0.2878 0.2441 0.2799 0.0507  0.0383  0.1310  60  LEU D CD1 
6857 C  CD2 . LEU D 60  ? 0.3603 0.0415 0.4734 0.0058  0.0519  0.0456  60  LEU D CD2 
6858 N  N   . LEU D 61  ? 0.1474 0.2031 0.1819 0.0250  0.0040  -0.0024 61  LEU D N   
6859 C  CA  . LEU D 61  ? 0.1243 0.1938 0.1625 0.0071  -0.0345 0.0130  61  LEU D CA  
6860 C  C   . LEU D 61  ? 0.1205 0.2401 0.2016 0.0240  -0.0321 0.0495  61  LEU D C   
6861 O  O   . LEU D 61  ? 0.1866 0.1823 0.1868 0.0100  -0.0477 0.0422  61  LEU D O   
6862 C  CB  . LEU D 61  ? 0.1645 0.2115 0.2150 0.0096  -0.0504 -0.0041 61  LEU D CB  
6863 C  CG  . LEU D 61  ? 0.1811 0.2815 0.1287 0.0306  -0.0386 0.0055  61  LEU D CG  
6864 C  CD1 . LEU D 61  ? 0.1900 0.3495 0.1579 0.0107  -0.0533 0.0484  61  LEU D CD1 
6865 C  CD2 . LEU D 61  ? 0.2185 0.3101 0.1682 0.0412  -0.0280 -0.0298 61  LEU D CD2 
6866 N  N   . THR D 62  ? 0.1291 0.2223 0.1857 -0.0346 -0.0266 0.0936  62  THR D N   
6867 C  CA  . THR D 62  ? 0.1628 0.2536 0.2074 -0.0737 -0.0055 0.0653  62  THR D CA  
6868 C  C   . THR D 62  ? 0.1500 0.3455 0.1890 -0.0877 -0.0113 0.0562  62  THR D C   
6869 O  O   . THR D 62  ? 0.1841 0.4415 0.1660 -0.0182 0.0046  0.0595  62  THR D O   
6870 C  CB  . THR D 62  ? 0.2547 0.2671 0.2509 -0.0041 0.0038  0.0708  62  THR D CB  
6871 O  OG1 . THR D 62  ? 0.2852 0.1911 0.2865 -0.0039 0.0266  0.0214  62  THR D OG1 
6872 C  CG2 . THR D 62  ? 0.2257 0.2687 0.2600 -0.0233 0.0055  -0.0595 62  THR D CG2 
6873 N  N   . ASN D 63  ? 0.1492 0.4627 0.1959 -0.0579 0.0025  0.0683  63  ASN D N   
6874 C  CA  . ASN D 63  ? 0.1668 0.4232 0.2010 -0.0111 0.0218  0.0533  63  ASN D CA  
6875 C  C   . ASN D 63  ? 0.2615 0.4418 0.2157 0.0048  0.0430  0.0086  63  ASN D C   
6876 O  O   . ASN D 63  ? 0.1830 0.4468 0.2058 0.0015  -0.0176 -0.0486 63  ASN D O   
6877 C  CB  . ASN D 63  ? 0.1703 0.2951 0.1642 -0.0439 0.0042  0.0668  63  ASN D CB  
6878 C  CG  . ASN D 63  ? 0.1825 0.1846 0.1638 -0.0427 -0.0483 0.0763  63  ASN D CG  
6879 O  OD1 . ASN D 63  ? 0.1918 0.2313 0.1850 -0.0518 -0.0300 0.0359  63  ASN D OD1 
6880 N  ND2 . ASN D 63  ? 0.2076 0.2013 0.1577 -0.0271 -0.0203 0.0614  63  ASN D ND2 
6881 N  N   . ASN D 64  ? 0.2785 0.0180 0.2829 0.0108  0.0198  0.0345  64  ASN D N   
6882 C  CA  . ASN D 64  ? 0.3236 0.0119 0.3951 0.0052  0.1555  -0.0392 64  ASN D CA  
6883 C  C   . ASN D 64  ? 0.2211 0.1913 0.5353 0.1093  0.0088  -0.0164 64  ASN D C   
6884 O  O   . ASN D 64  ? 0.3818 0.3817 0.6287 0.0107  0.1536  -0.2789 64  ASN D O   
6885 C  CB  . ASN D 64  ? 0.4672 0.1075 0.3129 0.1264  0.0888  0.0019  64  ASN D CB  
6886 C  CG  . ASN D 64  ? 0.4521 0.2067 0.2869 0.0374  -0.1408 -0.0562 64  ASN D CG  
6887 O  OD1 . ASN D 64  ? 0.4272 0.0577 0.2728 -0.1440 0.0446  -0.0388 64  ASN D OD1 
6888 N  ND2 . ASN D 64  ? 0.5680 0.3197 0.2655 0.1380  -0.1266 -0.0370 64  ASN D ND2 
6889 N  N   . GLY D 65  ? 0.1688 0.3265 0.2788 0.0457  0.0179  0.0476  65  GLY D N   
6890 C  CA  . GLY D 65  ? 0.1757 0.3296 0.2625 0.0356  0.0362  0.0025  65  GLY D CA  
6891 C  C   . GLY D 65  ? 0.1762 0.5651 0.2049 -0.0526 -0.1021 0.0424  65  GLY D C   
6892 O  O   . GLY D 65  ? 0.1981 0.2958 0.1936 -0.0380 -0.0173 0.0219  65  GLY D O   
6893 N  N   . HIS D 66  ? 0.2739 0.2602 0.2848 0.0835  -0.0030 0.0367  66  HIS D N   
6894 C  CA  . HIS D 66  ? 0.3715 0.0475 0.3137 -0.0583 -0.1354 -0.0316 66  HIS D CA  
6895 C  C   . HIS D 66  ? 0.2649 0.0260 0.2200 0.0626  0.0489  0.0425  66  HIS D C   
6896 O  O   . HIS D 66  ? 0.3036 0.0347 0.3200 0.0761  -0.0607 -0.0115 66  HIS D O   
6897 C  CB  . HIS D 66  ? 0.4547 0.0557 0.2493 -0.0425 -0.0536 0.0172  66  HIS D CB  
6898 C  CG  . HIS D 66  ? 0.3603 0.0514 0.2964 -0.0216 -0.0035 0.0027  66  HIS D CG  
6899 N  ND1 . HIS D 66  ? 0.2992 0.1232 0.2701 0.0195  -0.0212 0.0296  66  HIS D ND1 
6900 C  CD2 . HIS D 66  ? 0.2518 0.1291 0.1797 0.0186  -0.0510 -0.0037 66  HIS D CD2 
6901 C  CE1 . HIS D 66  ? 0.2189 0.1270 0.1434 -0.0365 -0.0386 0.0132  66  HIS D CE1 
6902 N  NE2 . HIS D 66  ? 0.1952 0.3389 0.2241 -0.0473 -0.0241 0.0171  66  HIS D NE2 
6903 N  N   . SER D 67  ? 0.3098 0.2773 0.3481 -0.1114 -0.0979 0.1195  67  SER D N   
6904 C  CA  . SER D 67  ? 0.1441 0.2986 0.3557 -0.0490 -0.0206 0.0055  67  SER D CA  
6905 C  C   . SER D 67  ? 0.2924 0.1286 0.3606 -0.0463 -0.1388 0.1327  67  SER D C   
6906 O  O   . SER D 67  ? 0.4087 0.0469 0.6316 0.0691  -0.3127 -0.0102 67  SER D O   
6907 C  CB  . SER D 67  ? 0.2453 0.3112 0.3672 -0.1672 0.2159  -0.1615 67  SER D CB  
6908 O  OG  . SER D 67  ? 0.2703 0.1772 0.2794 -0.0564 -0.0400 0.0532  67  SER D OG  
6909 N  N   . VAL D 68  ? 0.1525 0.1999 0.3014 -0.0431 -0.0661 0.0397  68  VAL D N   
6910 C  CA  . VAL D 68  ? 0.1067 0.3896 0.2771 -0.0003 -0.0355 -0.0535 68  VAL D CA  
6911 C  C   . VAL D 68  ? 0.1184 0.4592 0.2217 -0.0325 -0.0548 0.0585  68  VAL D C   
6912 O  O   . VAL D 68  ? 0.1452 0.4500 0.1703 0.0145  0.0024  0.0168  68  VAL D O   
6913 C  CB  . VAL D 68  ? 0.2240 0.2771 0.2125 0.0630  -0.0428 0.0439  68  VAL D CB  
6914 C  CG1 . VAL D 68  ? 0.2685 0.2066 0.3499 0.0024  0.0345  -0.0006 68  VAL D CG1 
6915 C  CG2 . VAL D 68  ? 0.2460 0.4812 0.2169 0.0656  -0.0859 0.0309  68  VAL D CG2 
6916 N  N   . LYS D 69  ? 0.1451 0.4090 0.1320 -0.0313 -0.0303 0.0735  69  LYS D N   
6917 C  CA  . LYS D 69  ? 0.1488 0.3332 0.1657 0.0283  -0.0358 0.0982  69  LYS D CA  
6918 C  C   . LYS D 69  ? 0.1476 0.2207 0.1446 0.0266  0.0047  0.0744  69  LYS D C   
6919 O  O   . LYS D 69  ? 0.1815 0.2374 0.1652 -0.0295 -0.0489 0.0829  69  LYS D O   
6920 C  CB  . LYS D 69  ? 0.3452 0.2964 0.2020 0.0201  0.0917  0.1013  69  LYS D CB  
6921 C  CG  . LYS D 69  ? 0.2192 0.2114 0.3328 0.0341  -0.0692 -0.0938 69  LYS D CG  
6922 C  CD  . LYS D 69  ? 0.4055 0.1997 0.3731 0.0580  0.0419  -0.1497 69  LYS D CD  
6923 C  CE  . LYS D 69  ? 0.3458 0.5287 0.4360 -0.0366 0.0854  0.0906  69  LYS D CE  
6924 N  NZ  . LYS D 69  ? 0.4777 0.4657 0.4536 0.0854  -0.0027 -0.1452 69  LYS D NZ  
6925 N  N   . LEU D 70  ? 0.1318 0.0784 0.1380 -0.0010 -0.0102 0.0001  70  LEU D N   
6926 C  CA  . LEU D 70  ? 0.1367 0.0104 0.1887 -0.0044 0.0137  0.0046  70  LEU D CA  
6927 C  C   . LEU D 70  ? 0.1489 0.0565 0.1471 0.0270  -0.0083 0.0081  70  LEU D C   
6928 O  O   . LEU D 70  ? 0.1631 0.0117 0.1675 0.0257  -0.0173 0.0063  70  LEU D O   
6929 C  CB  . LEU D 70  ? 0.1393 0.0064 0.1738 0.0037  -0.0328 -0.0010 70  LEU D CB  
6930 C  CG  . LEU D 70  ? 0.1442 0.0067 0.1979 -0.0068 -0.0162 0.0036  70  LEU D CG  
6931 C  CD1 . LEU D 70  ? 0.1913 0.1063 0.2157 0.0469  -0.0436 0.0027  70  LEU D CD1 
6932 C  CD2 . LEU D 70  ? 0.1876 0.0078 0.2178 -0.0162 -0.0385 0.0000  70  LEU D CD2 
6933 N  N   . ASN D 71  ? 0.1525 0.0338 0.1829 0.0259  0.0044  -0.0153 71  ASN D N   
6934 C  CA  . ASN D 71  ? 0.2031 0.0087 0.1843 0.0207  0.0227  -0.0037 71  ASN D CA  
6935 C  C   . ASN D 71  ? 0.1798 0.0563 0.2051 0.0262  0.0023  0.0179  71  ASN D C   
6936 O  O   . ASN D 71  ? 0.1999 0.1421 0.2027 -0.0113 0.0091  -0.0148 71  ASN D O   
6937 C  CB  . ASN D 71  ? 0.1843 0.0401 0.2293 0.0464  -0.0128 0.0126  71  ASN D CB  
6938 C  CG  . ASN D 71  ? 0.2200 0.0891 0.3008 0.0296  0.0652  0.0562  71  ASN D CG  
6939 O  OD1 . ASN D 71  ? 0.2365 0.0882 0.3608 -0.0100 0.0379  0.0538  71  ASN D OD1 
6940 N  ND2 . ASN D 71  ? 0.4202 0.0965 0.3379 0.0534  0.0204  0.0760  71  ASN D ND2 
6941 N  N   . LEU D 72  ? 0.1610 0.0166 0.1921 0.0356  -0.0137 0.0161  72  LEU D N   
6942 C  CA  . LEU D 72  ? 0.1631 0.0208 0.1985 0.0249  -0.0021 0.0079  72  LEU D CA  
6943 C  C   . LEU D 72  ? 0.1758 0.0895 0.1737 0.0222  0.0038  -0.0261 72  LEU D C   
6944 O  O   . LEU D 72  ? 0.2454 0.0541 0.2363 0.0231  0.0058  0.0157  72  LEU D O   
6945 C  CB  . LEU D 72  ? 0.1819 0.0090 0.1805 0.0146  0.0119  0.0170  72  LEU D CB  
6946 C  CG  . LEU D 72  ? 0.1710 0.0121 0.1595 0.0261  -0.0208 0.0121  72  LEU D CG  
6947 C  CD1 . LEU D 72  ? 0.1464 0.0571 0.1474 0.0105  -0.0247 0.0208  72  LEU D CD1 
6948 C  CD2 . LEU D 72  ? 0.1778 0.0225 0.2189 0.0111  -0.0221 -0.0167 72  LEU D CD2 
6949 N  N   . PRO D 73  ? 0.2123 0.0093 0.2180 0.0240  -0.0066 -0.0077 73  PRO D N   
6950 C  CA  . PRO D 73  ? 0.2273 0.0356 0.1988 0.0463  -0.0167 -0.0250 73  PRO D CA  
6951 C  C   . PRO D 73  ? 0.2235 0.0458 0.1841 0.0355  -0.0004 0.0071  73  PRO D C   
6952 O  O   . PRO D 73  ? 0.2352 0.0311 0.2019 0.0377  0.0388  0.0121  73  PRO D O   
6953 C  CB  . PRO D 73  ? 0.2010 0.0547 0.2207 0.0727  -0.0234 0.0170  73  PRO D CB  
6954 C  CG  . PRO D 73  ? 0.2055 0.0521 0.2010 0.0684  0.0423  0.0185  73  PRO D CG  
6955 C  CD  . PRO D 73  ? 0.1776 0.0295 0.1973 -0.0003 0.0138  -0.0245 73  PRO D CD  
6956 N  N   . SER D 74  ? 0.2841 0.0578 0.2127 0.0407  0.0313  -0.0057 74  SER D N   
6957 C  CA  . SER D 74  ? 0.2927 0.0612 0.2074 0.0930  0.0398  0.0153  74  SER D CA  
6958 C  C   . SER D 74  ? 0.2814 0.1202 0.2568 0.0598  0.0231  0.0143  74  SER D C   
6959 O  O   . SER D 74  ? 0.2600 0.2327 0.2556 0.0662  0.0131  0.0216  74  SER D O   
6960 C  CB  . SER D 74  ? 0.3671 0.1031 0.2041 0.0890  -0.0168 -0.0417 74  SER D CB  
6961 O  OG  . SER D 74  ? 0.3723 0.1058 0.3693 0.1007  0.0129  -0.0006 74  SER D OG  
6962 N  N   . ASP D 75  ? 0.2361 0.1295 0.2382 0.0651  0.0445  -0.0012 75  ASP D N   
6963 C  CA  . ASP D 75  ? 0.2156 0.1329 0.3050 0.0935  0.0557  0.0309  75  ASP D CA  
6964 C  C   . ASP D 75  ? 0.2480 0.1067 0.2303 0.0631  0.0465  0.0523  75  ASP D C   
6965 O  O   . ASP D 75  ? 0.2435 0.1586 0.3048 0.0527  0.0605  0.1104  75  ASP D O   
6966 C  CB  . ASP D 75  ? 0.1911 0.2566 0.3910 0.0602  0.0568  0.0778  75  ASP D CB  
6967 C  CG  . ASP D 75  ? 0.4760 0.5195 0.4784 -0.0255 0.1401  -0.0595 75  ASP D CG  
6968 O  OD1 . ASP D 75  ? 0.3582 0.4925 0.7255 0.0311  0.2478  0.1468  75  ASP D OD1 
6969 O  OD2 . ASP D 75  ? 0.3230 0.5777 1.0642 -0.0134 -0.0919 -0.0715 75  ASP D OD2 
6970 N  N   A MET D 76  ? 0.1611 0.0478 0.2313 0.0359  -0.0152 -0.0024 76  MET D N   
6971 N  N   B MET D 76  ? 0.1767 0.0826 0.2307 0.0598  -0.0162 -0.0177 76  MET D N   
6972 C  CA  A MET D 76  ? 0.1646 0.0489 0.2098 0.0344  -0.0039 0.0157  76  MET D CA  
6973 C  CA  B MET D 76  ? 0.1749 0.1123 0.1902 0.0840  0.0068  -0.0139 76  MET D CA  
6974 C  C   A MET D 76  ? 0.1397 0.0714 0.2123 0.0063  0.0089  0.0233  76  MET D C   
6975 C  C   B MET D 76  ? 0.1424 0.0834 0.2031 0.0269  0.0136  0.0206  76  MET D C   
6976 O  O   A MET D 76  ? 0.1575 0.0595 0.2248 0.0044  -0.0035 0.0072  76  MET D O   
6977 O  O   B MET D 76  ? 0.1482 0.0591 0.2547 0.0324  0.0188  0.0263  76  MET D O   
6978 C  CB  A MET D 76  ? 0.1408 0.0106 0.2043 -0.0048 0.0070  0.0283  76  MET D CB  
6979 C  CB  B MET D 76  ? 0.1725 0.0936 0.2053 0.0751  0.0189  -0.0408 76  MET D CB  
6980 C  CG  A MET D 76  ? 0.1495 0.0072 0.1648 -0.0010 -0.0208 0.0117  76  MET D CG  
6981 C  CG  B MET D 76  ? 0.1631 0.0967 0.2113 0.0694  0.0220  -0.0665 76  MET D CG  
6982 S  SD  A MET D 76  ? 0.1441 0.0198 0.1747 0.0068  -0.0186 0.0006  76  MET D SD  
6983 S  SD  B MET D 76  ? 0.1941 0.1284 0.1814 0.0309  0.0102  -0.0237 76  MET D SD  
6984 C  CE  A MET D 76  ? 0.1453 0.0103 0.1254 0.0094  0.0334  -0.0172 76  MET D CE  
6985 C  CE  B MET D 76  ? 0.0446 0.1405 0.0573 0.0259  -0.0158 -0.0458 76  MET D CE  
6986 N  N   . HIS D 77  ? 0.1534 0.0862 0.2096 0.0414  0.0160  0.0272  77  HIS D N   
6987 C  CA  . HIS D 77  ? 0.1923 0.0469 0.2001 0.0485  0.0027  0.0049  77  HIS D CA  
6988 C  C   . HIS D 77  ? 0.1805 0.0650 0.1764 0.0174  0.0008  0.0247  77  HIS D C   
6989 O  O   . HIS D 77  ? 0.1797 0.0441 0.2317 0.0052  0.0291  0.0108  77  HIS D O   
6990 C  CB  . HIS D 77  ? 0.2284 0.0842 0.2112 0.0185  0.0558  -0.0197 77  HIS D CB  
6991 C  CG  . HIS D 77  ? 0.2689 0.0688 0.2066 -0.0115 0.0649  -0.0291 77  HIS D CG  
6992 N  ND1 . HIS D 77  ? 0.2630 0.0726 0.3281 -0.0330 0.0560  0.0419  77  HIS D ND1 
6993 C  CD2 . HIS D 77  ? 0.2861 0.0985 0.2657 0.0219  0.1176  0.0506  77  HIS D CD2 
6994 C  CE1 . HIS D 77  ? 0.3222 0.1573 0.2320 -0.0003 0.0853  0.0066  77  HIS D CE1 
6995 N  NE2 . HIS D 77  ? 0.2745 0.1288 0.2770 0.0330  0.0854  0.0231  77  HIS D NE2 
6996 N  N   . ILE D 78  ? 0.2191 0.0625 0.1566 0.0718  -0.0154 0.0234  78  ILE D N   
6997 C  CA  . ILE D 78  ? 0.2376 0.0461 0.1597 0.0574  -0.0205 0.0185  78  ILE D CA  
6998 C  C   . ILE D 78  ? 0.2329 0.0581 0.1736 0.0147  0.0108  -0.0027 78  ILE D C   
6999 O  O   . ILE D 78  ? 0.2045 0.0616 0.2081 0.0549  -0.0227 -0.0376 78  ILE D O   
7000 C  CB  . ILE D 78  ? 0.2134 0.1668 0.2071 0.0430  -0.0086 0.0562  78  ILE D CB  
7001 C  CG1 . ILE D 78  ? 0.2296 0.1599 0.2358 0.0546  -0.0044 0.0630  78  ILE D CG1 
7002 C  CG2 . ILE D 78  ? 0.2933 0.2227 0.2164 0.0876  0.0199  0.0234  78  ILE D CG2 
7003 C  CD1 . ILE D 78  ? 0.2120 0.0550 0.4523 0.0812  -0.0038 0.0620  78  ILE D CD1 
7004 N  N   . GLN D 79  ? 0.2153 0.1017 0.2421 0.0389  0.0104  0.0623  79  GLN D N   
7005 C  CA  . GLN D 79  ? 0.2708 0.0981 0.2429 0.0351  -0.0055 0.0532  79  GLN D CA  
7006 C  C   . GLN D 79  ? 0.2586 0.1130 0.1755 0.0508  -0.0342 -0.0127 79  GLN D C   
7007 O  O   . GLN D 79  ? 0.2997 0.0914 0.2265 0.0345  -0.0107 -0.0166 79  GLN D O   
7008 C  CB  . GLN D 79  ? 0.2654 0.2173 0.3542 0.0304  -0.0091 0.0762  79  GLN D CB  
7009 C  CG  . GLN D 79  ? 0.3463 0.1830 0.4233 0.0798  0.0187  0.0491  79  GLN D CG  
7010 C  CD  . GLN D 79  ? 0.6166 0.2633 0.4498 0.3402  0.1126  0.0058  79  GLN D CD  
7011 O  OE1 . GLN D 79  ? 0.8823 0.4889 0.5190 0.2262  -0.0752 0.0143  79  GLN D OE1 
7012 N  NE2 . GLN D 79  ? 0.5705 0.2954 0.5321 0.1717  -0.0703 0.1111  79  GLN D NE2 
7013 N  N   . GLY D 80  ? 0.3245 0.1384 0.1707 0.0326  -0.0428 0.0106  80  GLY D N   
7014 C  CA  . GLY D 80  ? 0.2597 0.1115 0.2178 -0.0211 -0.0300 0.0756  80  GLY D CA  
7015 C  C   . GLY D 80  ? 0.3041 0.0967 0.3064 -0.0156 -0.0763 0.0600  80  GLY D C   
7016 O  O   . GLY D 80  ? 0.3947 0.1135 0.2653 -0.0048 -0.0386 0.0328  80  GLY D O   
7017 N  N   . LEU D 81  ? 0.2708 0.0201 0.2302 0.0480  0.0041  -0.0328 81  LEU D N   
7018 C  CA  . LEU D 81  ? 0.2762 0.0541 0.2145 0.0163  0.0174  -0.0080 81  LEU D CA  
7019 C  C   . LEU D 81  ? 0.2428 0.0308 0.1851 0.0439  -0.0100 0.0219  81  LEU D C   
7020 O  O   . LEU D 81  ? 0.2581 0.1280 0.2265 0.0178  0.0214  -0.0326 81  LEU D O   
7021 C  CB  . LEU D 81  ? 0.3131 0.0842 0.1622 0.0576  0.0274  -0.0010 81  LEU D CB  
7022 C  CG  . LEU D 81  ? 0.2778 0.0674 0.1819 0.0719  0.0104  0.0050  81  LEU D CG  
7023 C  CD1 . LEU D 81  ? 0.3547 0.1088 0.1545 0.0804  0.0345  0.0074  81  LEU D CD1 
7024 C  CD2 . LEU D 81  ? 0.2261 0.0150 0.2847 0.0428  0.0134  0.0117  81  LEU D CD2 
7025 N  N   . GLN D 82  ? 0.3160 0.0168 0.1793 0.0051  0.0018  0.0134  82  GLN D N   
7026 C  CA  . GLN D 82  ? 0.2254 0.0609 0.1751 0.0092  -0.0156 -0.0064 82  GLN D CA  
7027 C  C   . GLN D 82  ? 0.2773 0.0713 0.1489 0.0298  -0.0214 0.0055  82  GLN D C   
7028 O  O   . GLN D 82  ? 0.2595 0.0582 0.1850 0.0021  0.0091  0.0208  82  GLN D O   
7029 C  CB  . GLN D 82  ? 0.2363 0.0475 0.2102 -0.0359 0.0093  -0.0107 82  GLN D CB  
7030 C  CG  . GLN D 82  ? 0.2676 0.0820 0.2556 -0.0119 0.0233  0.0469  82  GLN D CG  
7031 C  CD  . GLN D 82  ? 0.2805 0.0533 0.2270 -0.0151 0.0114  0.0160  82  GLN D CD  
7032 O  OE1 . GLN D 82  ? 0.3358 0.0828 0.2723 0.0170  0.0006  -0.0157 82  GLN D OE1 
7033 N  NE2 . GLN D 82  ? 0.3018 0.0557 0.2274 -0.0322 0.0289  0.0026  82  GLN D NE2 
7034 N  N   . SER D 83  ? 0.2329 0.0633 0.1615 0.0197  -0.0285 0.0105  83  SER D N   
7035 C  CA  . SER D 83  ? 0.1952 0.0426 0.1564 0.0163  -0.0281 -0.0073 83  SER D CA  
7036 C  C   . SER D 83  ? 0.1861 0.0871 0.1403 0.0025  -0.0125 -0.0066 83  SER D C   
7037 O  O   . SER D 83  ? 0.2254 0.0647 0.1715 0.0163  0.0255  0.0348  83  SER D O   
7038 C  CB  . SER D 83  ? 0.2045 0.0566 0.2107 -0.0066 -0.0523 0.0048  83  SER D CB  
7039 O  OG  . SER D 83  ? 0.2587 0.0802 0.1941 -0.0069 -0.0394 0.0076  83  SER D OG  
7040 N  N   . ARG D 84  ? 0.1927 0.1047 0.1715 -0.0082 -0.0116 0.0155  84  ARG D N   
7041 C  CA  . ARG D 84  ? 0.2054 0.0551 0.1699 0.0185  -0.0096 0.0134  84  ARG D CA  
7042 C  C   . ARG D 84  ? 0.1959 0.0396 0.1764 0.0168  0.0201  -0.0269 84  ARG D C   
7043 O  O   . ARG D 84  ? 0.2121 0.0296 0.1998 0.0248  0.0055  0.0162  84  ARG D O   
7044 C  CB  . ARG D 84  ? 0.1949 0.0523 0.1737 0.0332  0.0108  -0.0172 84  ARG D CB  
7045 C  CG  . ARG D 84  ? 0.1857 0.0629 0.2051 0.0242  -0.0205 -0.0581 84  ARG D CG  
7046 C  CD  . ARG D 84  ? 0.1581 0.1445 0.2056 -0.0041 -0.0094 -0.0100 84  ARG D CD  
7047 N  NE  . ARG D 84  ? 0.2106 0.0934 0.2288 0.0369  -0.0017 -0.0518 84  ARG D NE  
7048 C  CZ  . ARG D 84  ? 0.2076 0.2132 0.2332 0.0406  -0.0187 -0.0469 84  ARG D CZ  
7049 N  NH1 . ARG D 84  ? 0.2060 0.2346 0.3405 0.0364  0.0210  -0.0697 84  ARG D NH1 
7050 N  NH2 . ARG D 84  ? 0.3017 0.1264 0.2653 0.0263  0.0037  -0.0122 84  ARG D NH2 
7051 N  N   . TYR D 85  ? 0.2107 0.0328 0.1391 0.0190  0.0079  -0.0103 85  TYR D N   
7052 C  CA  . TYR D 85  ? 0.1683 0.0273 0.1588 0.0344  0.0166  0.0049  85  TYR D CA  
7053 C  C   . TYR D 85  ? 0.2164 0.0484 0.1520 0.0362  0.0057  0.0093  85  TYR D C   
7054 O  O   . TYR D 85  ? 0.2133 0.0471 0.1976 0.0081  0.0497  0.0131  85  TYR D O   
7055 C  CB  . TYR D 85  ? 0.1757 0.0176 0.1577 0.0408  -0.0042 -0.0157 85  TYR D CB  
7056 C  CG  . TYR D 85  ? 0.2016 0.0084 0.1394 0.0203  -0.0044 -0.0011 85  TYR D CG  
7057 C  CD1 . TYR D 85  ? 0.2468 0.0434 0.1194 0.0646  -0.0060 -0.0339 85  TYR D CD1 
7058 C  CD2 . TYR D 85  ? 0.1904 0.0141 0.1846 0.0290  -0.0027 -0.0243 85  TYR D CD2 
7059 C  CE1 . TYR D 85  ? 0.2078 0.0272 0.1369 0.0241  0.0198  -0.0113 85  TYR D CE1 
7060 C  CE2 . TYR D 85  ? 0.1956 0.0226 0.1654 0.0524  -0.0106 -0.0201 85  TYR D CE2 
7061 C  CZ  . TYR D 85  ? 0.1532 0.0694 0.1686 0.0307  0.0057  -0.0139 85  TYR D CZ  
7062 O  OH  . TYR D 85  ? 0.2013 0.0784 0.1780 -0.0163 -0.0199 -0.0092 85  TYR D OH  
7063 N  N   . SER D 86  ? 0.2288 0.0496 0.1316 0.0474  0.0183  0.0037  86  SER D N   
7064 C  CA  . SER D 86  ? 0.1611 0.0832 0.1453 0.0619  0.0104  0.0075  86  SER D CA  
7065 C  C   . SER D 86  ? 0.1316 0.0378 0.1462 0.0297  0.0080  0.0198  86  SER D C   
7066 O  O   . SER D 86  ? 0.1360 0.0471 0.1679 0.0126  0.0157  -0.0004 86  SER D O   
7067 C  CB  . SER D 86  ? 0.1693 0.0979 0.1840 0.0761  0.0248  0.0048  86  SER D CB  
7068 O  OG  . SER D 86  ? 0.2067 0.0800 0.2164 0.0538  0.0609  0.0078  86  SER D OG  
7069 N  N   . ALA D 87  ? 0.2033 0.0538 0.1449 0.0177  0.0220  0.0078  87  ALA D N   
7070 C  CA  . ALA D 87  ? 0.1773 0.0270 0.1553 0.0012  0.0220  -0.0046 87  ALA D CA  
7071 C  C   . ALA D 87  ? 0.1664 0.0276 0.1682 0.0155  0.0122  0.0024  87  ALA D C   
7072 O  O   . ALA D 87  ? 0.1761 0.0659 0.2066 0.0277  0.0034  0.0348  87  ALA D O   
7073 C  CB  . ALA D 87  ? 0.1609 0.1022 0.1552 -0.0216 0.0111  -0.0346 87  ALA D CB  
7074 N  N   . THR D 88  ? 0.1645 0.0322 0.1255 0.0322  0.0003  0.0177  88  THR D N   
7075 C  CA  . THR D 88  ? 0.2157 0.0105 0.1307 0.0294  0.0024  0.0016  88  THR D CA  
7076 C  C   . THR D 88  ? 0.1627 0.0415 0.1405 0.0391  0.0154  0.0118  88  THR D C   
7077 O  O   . THR D 88  ? 0.2026 0.0443 0.1476 0.0410  -0.0016 0.0082  88  THR D O   
7078 C  CB  . THR D 88  ? 0.2827 0.0106 0.2721 0.0006  -0.0403 0.0333  88  THR D CB  
7079 O  OG1 . THR D 88  ? 0.4586 0.0696 0.2209 -0.0212 -0.0743 0.0483  88  THR D OG1 
7080 C  CG2 . THR D 88  ? 0.2992 0.0681 0.2660 0.0586  -0.0020 -0.0429 88  THR D CG2 
7081 N  N   . GLN D 89  ? 0.1565 0.0071 0.1467 0.0110  0.0103  -0.0006 89  GLN D N   
7082 C  CA  . GLN D 89  ? 0.1731 0.0181 0.1398 0.0214  0.0319  0.0379  89  GLN D CA  
7083 C  C   . GLN D 89  ? 0.1843 0.0086 0.1448 0.0103  0.0094  0.0156  89  GLN D C   
7084 O  O   . GLN D 89  ? 0.1623 0.0091 0.1500 0.0207  0.0002  0.0002  89  GLN D O   
7085 C  CB  . GLN D 89  ? 0.1796 0.0163 0.1421 -0.0046 0.0133  0.0241  89  GLN D CB  
7086 C  CG  . GLN D 89  ? 0.1889 0.0414 0.2087 -0.0003 -0.0017 -0.0220 89  GLN D CG  
7087 C  CD  . GLN D 89  ? 0.1816 0.0145 0.2213 0.0097  -0.0222 -0.0237 89  GLN D CD  
7088 O  OE1 . GLN D 89  ? 0.1943 0.0159 0.1879 0.0423  0.0097  -0.0001 89  GLN D OE1 
7089 N  NE2 . GLN D 89  ? 0.1941 0.0672 0.2860 -0.0192 -0.0372 0.0431  89  GLN D NE2 
7090 N  N   . LEU D 90  ? 0.1331 0.0247 0.1521 0.0183  -0.0062 0.0077  90  LEU D N   
7091 C  CA  . LEU D 90  ? 0.1376 0.0068 0.1606 0.0034  0.0237  -0.0074 90  LEU D CA  
7092 C  C   . LEU D 90  ? 0.1100 0.0148 0.1409 -0.0024 -0.0008 -0.0122 90  LEU D C   
7093 O  O   . LEU D 90  ? 0.1530 0.0111 0.1647 0.0264  0.0021  0.0044  90  LEU D O   
7094 C  CB  . LEU D 90  ? 0.1284 0.0306 0.1481 -0.0281 -0.0228 0.0036  90  LEU D CB  
7095 C  CG  . LEU D 90  ? 0.0857 0.0490 0.1782 -0.0022 -0.0098 -0.0259 90  LEU D CG  
7096 C  CD1 . LEU D 90  ? 0.1302 0.0304 0.1861 0.0253  0.0027  -0.0309 90  LEU D CD1 
7097 C  CD2 . LEU D 90  ? 0.1259 0.0152 0.2315 -0.0018 -0.0320 -0.0073 90  LEU D CD2 
7098 N  N   . HIS D 91  ? 0.1230 0.0097 0.1388 0.0099  -0.0044 -0.0186 91  HIS D N   
7099 C  CA  . HIS D 91  ? 0.1193 0.0069 0.1340 -0.0073 -0.0004 -0.0033 91  HIS D CA  
7100 C  C   . HIS D 91  ? 0.1283 0.0185 0.0990 0.0193  0.0076  -0.0093 91  HIS D C   
7101 O  O   . HIS D 91  ? 0.1502 0.0311 0.1212 0.0038  -0.0032 0.0160  91  HIS D O   
7102 C  CB  . HIS D 91  ? 0.1241 0.0089 0.1553 -0.0173 -0.0336 0.0065  91  HIS D CB  
7103 C  CG  . HIS D 91  ? 0.1442 0.0065 0.1326 -0.0050 -0.0165 0.0000  91  HIS D CG  
7104 N  ND1 . HIS D 91  ? 0.1689 0.0068 0.1321 0.0051  -0.0277 -0.0070 91  HIS D ND1 
7105 C  CD2 . HIS D 91  ? 0.1546 0.0092 0.1537 -0.0135 -0.0300 0.0184  91  HIS D CD2 
7106 C  CE1 . HIS D 91  ? 0.1250 0.0085 0.1427 -0.0009 -0.0127 -0.0012 91  HIS D CE1 
7107 N  NE2 . HIS D 91  ? 0.1230 0.0113 0.1458 0.0005  -0.0012 0.0221  91  HIS D NE2 
7108 N  N   . LEU D 92  ? 0.1088 0.0217 0.1279 0.0058  0.0088  0.0027  92  LEU D N   
7109 C  CA  . LEU D 92  ? 0.1310 0.0066 0.1548 0.0052  -0.0004 -0.0032 92  LEU D CA  
7110 C  C   . LEU D 92  ? 0.1071 0.0403 0.1324 -0.0148 -0.0255 0.0247  92  LEU D C   
7111 O  O   . LEU D 92  ? 0.1298 0.0310 0.1311 -0.0057 -0.0030 0.0122  92  LEU D O   
7112 C  CB  . LEU D 92  ? 0.1241 0.0478 0.2187 -0.0234 -0.0334 -0.0468 92  LEU D CB  
7113 C  CG  . LEU D 92  ? 0.1136 0.0340 0.2117 0.0016  -0.0275 -0.0655 92  LEU D CG  
7114 C  CD1 . LEU D 92  ? 0.1273 0.0542 0.2534 -0.0234 -0.0489 -0.0122 92  LEU D CD1 
7115 C  CD2 . LEU D 92  ? 0.1707 0.0090 0.1858 0.0197  -0.0278 0.0039  92  LEU D CD2 
7116 N  N   . HIS D 93  ? 0.1191 0.0458 0.1584 -0.0034 -0.0110 0.0187  93  HIS D N   
7117 C  CA  . HIS D 93  ? 0.1157 0.0337 0.1304 0.0206  -0.0048 -0.0172 93  HIS D CA  
7118 C  C   . HIS D 93  ? 0.0983 0.0165 0.1069 0.0161  0.0088  0.0104  93  HIS D C   
7119 O  O   . HIS D 93  ? 0.1205 0.0569 0.1230 -0.0384 -0.0086 0.0248  93  HIS D O   
7120 C  CB  . HIS D 93  ? 0.1250 0.0649 0.1291 0.0084  -0.0152 -0.0089 93  HIS D CB  
7121 C  CG  . HIS D 93  ? 0.1085 0.0413 0.1078 -0.0047 0.0061  0.0155  93  HIS D CG  
7122 N  ND1 . HIS D 93  ? 0.1388 0.0328 0.1399 -0.0004 0.0163  -0.0059 93  HIS D ND1 
7123 C  CD2 . HIS D 93  ? 0.1332 0.0242 0.0771 0.0396  -0.0004 -0.0197 93  HIS D CD2 
7124 C  CE1 . HIS D 93  ? 0.1071 0.0376 0.1128 0.0113  0.0154  0.0122  93  HIS D CE1 
7125 N  NE2 . HIS D 93  ? 0.1223 0.0143 0.1194 0.0183  0.0414  -0.0158 93  HIS D NE2 
7126 N  N   . TRP D 94  ? 0.1024 0.0284 0.1311 0.0109  0.0260  -0.0253 94  TRP D N   
7127 C  CA  . TRP D 94  ? 0.0821 0.0268 0.1319 0.0375  -0.0010 -0.0155 94  TRP D CA  
7128 C  C   . TRP D 94  ? 0.0936 0.0172 0.1094 0.0187  0.0103  0.0114  94  TRP D C   
7129 O  O   . TRP D 94  ? 0.1146 0.0434 0.1568 -0.0002 0.0051  -0.0168 94  TRP D O   
7130 C  CB  . TRP D 94  ? 0.1324 0.0269 0.1471 0.0403  -0.0255 0.0154  94  TRP D CB  
7131 C  CG  . TRP D 94  ? 0.1771 0.0123 0.1278 0.0297  0.0003  -0.0100 94  TRP D CG  
7132 C  CD1 . TRP D 94  ? 0.1581 0.0079 0.1700 -0.0017 0.0082  -0.0159 94  TRP D CD1 
7133 C  CD2 . TRP D 94  ? 0.1062 0.0150 0.1433 0.0124  0.0006  0.0171  94  TRP D CD2 
7134 N  NE1 . TRP D 94  ? 0.1410 0.0284 0.1545 0.0050  -0.0110 0.0060  94  TRP D NE1 
7135 C  CE2 . TRP D 94  ? 0.1724 0.0077 0.1239 0.0135  0.0196  -0.0039 94  TRP D CE2 
7136 C  CE3 . TRP D 94  ? 0.1398 0.0106 0.1260 0.0234  0.0105  0.0062  94  TRP D CE3 
7137 C  CZ2 . TRP D 94  ? 0.1496 0.0088 0.1737 0.0178  -0.0083 -0.0073 94  TRP D CZ2 
7138 C  CZ3 . TRP D 94  ? 0.1657 0.0117 0.1500 0.0177  -0.0205 0.0196  94  TRP D CZ3 
7139 C  CH2 . TRP D 94  ? 0.1813 0.0104 0.1261 0.0253  0.0038  0.0075  94  TRP D CH2 
7140 N  N   . GLY D 95  ? 0.1024 0.0485 0.1288 0.0513  0.0330  0.0208  95  GLY D N   
7141 C  CA  . GLY D 95  ? 0.1169 0.0137 0.1358 -0.0074 0.0430  -0.0193 95  GLY D CA  
7142 C  C   . GLY D 95  ? 0.1575 0.0187 0.1481 -0.0013 0.0617  0.0295  95  GLY D C   
7143 O  O   . GLY D 95  ? 0.1455 0.0141 0.1552 0.0110  0.0145  -0.0049 95  GLY D O   
7144 N  N   . ASN D 96  ? 0.1718 0.1176 0.1180 0.0020  0.0035  -0.0552 96  ASN D N   
7145 C  CA  . ASN D 96  ? 0.1584 0.0766 0.1412 0.0020  0.0425  -0.0209 96  ASN D CA  
7146 C  C   . ASN D 96  ? 0.1496 0.0802 0.1312 0.0255  -0.0115 -0.0182 96  ASN D C   
7147 O  O   . ASN D 96  ? 0.1884 0.0947 0.1776 0.0114  0.0212  0.0108  96  ASN D O   
7148 C  CB  . ASN D 96  ? 0.1460 0.1370 0.2423 0.0089  0.0932  0.0294  96  ASN D CB  
7149 C  CG  . ASN D 96  ? 0.1223 0.1972 0.2977 0.0207  0.1219  -0.0407 96  ASN D CG  
7150 O  OD1 . ASN D 96  ? 0.1545 0.2060 0.5097 -0.0095 0.1148  -0.1467 96  ASN D OD1 
7151 N  ND2 . ASN D 96  ? 0.2358 0.0838 0.3318 -0.0001 0.0408  0.0556  96  ASN D ND2 
7152 N  N   . PRO D 97  ? 0.1753 0.1284 0.1395 0.0141  0.0159  -0.0151 97  PRO D N   
7153 C  CA  . PRO D 97  ? 0.2151 0.1385 0.1701 0.0114  0.0116  -0.0392 97  PRO D CA  
7154 C  C   . PRO D 97  ? 0.2483 0.1509 0.2383 0.0345  0.0807  0.0023  97  PRO D C   
7155 O  O   . PRO D 97  ? 0.3441 0.1482 0.2855 -0.0201 0.0247  -0.0569 97  PRO D O   
7156 C  CB  . PRO D 97  ? 0.3204 0.1773 0.1671 0.0311  0.0425  -0.0420 97  PRO D CB  
7157 C  CG  . PRO D 97  ? 0.2419 0.2125 0.2245 0.0394  0.0547  -0.0580 97  PRO D CG  
7158 C  CD  . PRO D 97  ? 0.2083 0.1688 0.1724 0.0359  0.0230  0.0288  97  PRO D CD  
7159 N  N   . ASN D 98  ? 0.1990 0.2077 0.1836 0.0697  0.0798  0.0187  98  ASN D N   
7160 C  CA  . ASN D 98  ? 0.2691 0.3140 0.2304 0.1443  0.1089  0.0366  98  ASN D CA  
7161 C  C   . ASN D 98  ? 0.2897 0.2728 0.2193 0.1477  0.0715  0.0210  98  ASN D C   
7162 O  O   . ASN D 98  ? 0.3407 0.4376 0.3231 0.2549  0.0900  0.1100  98  ASN D O   
7163 C  CB  . ASN D 98  ? 0.2016 0.5211 0.3042 0.0858  0.0383  0.1102  98  ASN D CB  
7164 C  CG  . ASN D 98  ? 0.3948 0.4205 0.2846 0.1022  0.1360  -0.0310 98  ASN D CG  
7165 O  OD1 . ASN D 98  ? 0.5206 0.1958 0.4595 0.0916  0.1249  0.1314  98  ASN D OD1 
7166 N  ND2 . ASN D 98  ? 0.4839 0.6767 0.3709 0.1012  0.1964  0.1989  98  ASN D ND2 
7167 N  N   . ASP D 99  ? 0.2278 0.2202 0.1678 0.0721  0.0552  0.0237  99  ASP D N   
7168 C  CA  . ASP D 99  ? 0.1988 0.1225 0.1683 0.0377  0.0306  0.0141  99  ASP D CA  
7169 C  C   . ASP D 99  ? 0.1694 0.0837 0.1090 0.0612  -0.0008 0.0168  99  ASP D C   
7170 O  O   . ASP D 99  ? 0.2089 0.0501 0.1920 -0.0146 0.0425  -0.0009 99  ASP D O   
7171 C  CB  . ASP D 99  ? 0.2272 0.1445 0.2372 -0.0146 0.0203  0.0232  99  ASP D CB  
7172 C  CG  . ASP D 99  ? 0.2630 0.1794 0.2471 -0.0345 -0.0210 0.0207  99  ASP D CG  
7173 O  OD1 . ASP D 99  ? 0.2102 0.1729 0.2362 0.0547  -0.0233 0.0727  99  ASP D OD1 
7174 O  OD2 . ASP D 99  ? 0.2727 0.2620 0.3314 -0.0877 -0.0970 0.0322  99  ASP D OD2 
7175 N  N   . PRO D 100 ? 0.2230 0.0836 0.1409 0.0397  0.0504  -0.0178 100 PRO D N   
7176 C  CA  . PRO D 100 ? 0.1665 0.0584 0.1456 0.0018  -0.0060 -0.0100 100 PRO D CA  
7177 C  C   . PRO D 100 ? 0.1851 0.0751 0.1268 -0.0074 0.0253  -0.0377 100 PRO D C   
7178 O  O   . PRO D 100 ? 0.2085 0.0562 0.2048 -0.0061 0.0000  -0.0132 100 PRO D O   
7179 C  CB  . PRO D 100 ? 0.3001 0.0174 0.1609 -0.0201 0.0354  -0.0405 100 PRO D CB  
7180 C  CG  . PRO D 100 ? 0.2870 0.0491 0.2121 0.0047  0.0533  -0.0513 100 PRO D CG  
7181 C  CD  . PRO D 100 ? 0.1958 0.0924 0.1383 0.0494  0.0292  -0.0298 100 PRO D CD  
7182 N  N   . HIS D 101 ? 0.1668 0.0398 0.1452 0.0365  -0.0162 -0.0190 101 HIS D N   
7183 C  CA  . HIS D 101 ? 0.1423 0.0677 0.1369 0.0293  0.0015  -0.0210 101 HIS D CA  
7184 C  C   . HIS D 101 ? 0.1471 0.0498 0.1837 0.0151  -0.0115 -0.0071 101 HIS D C   
7185 O  O   . HIS D 101 ? 0.1381 0.0985 0.2380 0.0237  -0.0233 -0.0185 101 HIS D O   
7186 C  CB  . HIS D 101 ? 0.2017 0.0893 0.2006 0.0750  0.0109  0.0038  101 HIS D CB  
7187 C  CG  . HIS D 101 ? 0.1710 0.0728 0.2455 0.0403  -0.0094 0.0010  101 HIS D CG  
7188 N  ND1 . HIS D 101 ? 0.2584 0.0911 0.2133 0.0212  -0.0041 -0.0001 101 HIS D ND1 
7189 C  CD2 . HIS D 101 ? 0.1668 0.0839 0.2304 0.0152  -0.0168 -0.0249 101 HIS D CD2 
7190 C  CE1 . HIS D 101 ? 0.2101 0.1006 0.2644 0.1008  0.0111  -0.0010 101 HIS D CE1 
7191 N  NE2 . HIS D 101 ? 0.2629 0.0611 0.3213 0.0446  -0.0097 0.0033  101 HIS D NE2 
7192 N  N   . GLY D 102 ? 0.1248 0.0206 0.1220 -0.0020 -0.0100 0.0029  102 GLY D N   
7193 C  CA  . GLY D 102 ? 0.1767 0.0234 0.1456 -0.0118 0.0154  -0.0089 102 GLY D CA  
7194 C  C   . GLY D 102 ? 0.1685 0.0064 0.1081 0.0031  0.0095  0.0010  102 GLY D C   
7195 O  O   . GLY D 102 ? 0.1403 0.0084 0.1771 0.0083  -0.0051 -0.0024 102 GLY D O   
7196 N  N   . SER D 103 ? 0.1395 0.0153 0.1449 -0.0282 0.0274  0.0086  103 SER D N   
7197 C  CA  . SER D 103 ? 0.1471 0.0174 0.1482 -0.0375 0.0320  0.0033  103 SER D CA  
7198 C  C   . SER D 103 ? 0.1202 0.0230 0.1528 0.0033  -0.0089 -0.0024 103 SER D C   
7199 O  O   . SER D 103 ? 0.1233 0.0297 0.1710 0.0066  0.0024  -0.0146 103 SER D O   
7200 C  CB  . SER D 103 ? 0.1372 0.0153 0.1491 0.0039  -0.0035 0.0342  103 SER D CB  
7201 O  OG  . SER D 103 ? 0.1397 0.0213 0.1743 -0.0083 -0.0278 -0.0064 103 SER D OG  
7202 N  N   . GLU D 104 ? 0.1353 0.0101 0.1412 -0.0199 -0.0022 -0.0094 104 GLU D N   
7203 C  CA  . GLU D 104 ? 0.1592 0.0082 0.1234 0.0049  -0.0234 -0.0148 104 GLU D CA  
7204 C  C   . GLU D 104 ? 0.1591 0.0099 0.1423 0.0153  -0.0182 -0.0184 104 GLU D C   
7205 O  O   . GLU D 104 ? 0.1668 0.0063 0.1789 0.0016  -0.0179 0.0012  104 GLU D O   
7206 C  CB  . GLU D 104 ? 0.1259 0.0541 0.1094 0.0278  -0.0149 -0.0105 104 GLU D CB  
7207 C  CG  . GLU D 104 ? 0.1622 0.0173 0.0975 0.0281  -0.0305 -0.0278 104 GLU D CG  
7208 C  CD  . GLU D 104 ? 0.1374 0.0076 0.1561 -0.0053 -0.0218 -0.0114 104 GLU D CD  
7209 O  OE1 . GLU D 104 ? 0.1330 0.0129 0.1740 -0.0139 -0.0118 0.0236  104 GLU D OE1 
7210 O  OE2 . GLU D 104 ? 0.1384 0.0338 0.1710 0.0122  0.0133  -0.0216 104 GLU D OE2 
7211 N  N   . HIS D 105 ? 0.1500 0.0331 0.1329 0.0197  -0.0105 0.0091  105 HIS D N   
7212 C  CA  . HIS D 105 ? 0.1559 0.0080 0.1295 0.0156  0.0021  0.0019  105 HIS D CA  
7213 C  C   . HIS D 105 ? 0.1691 0.0098 0.1315 0.0231  -0.0097 0.0038  105 HIS D C   
7214 O  O   . HIS D 105 ? 0.1610 0.0095 0.1671 0.0082  -0.0168 -0.0031 105 HIS D O   
7215 C  CB  . HIS D 105 ? 0.1406 0.0119 0.1647 0.0249  0.0000  -0.0009 105 HIS D CB  
7216 C  CG  . HIS D 105 ? 0.1363 0.0188 0.1620 0.0245  0.0046  -0.0040 105 HIS D CG  
7217 N  ND1 . HIS D 105 ? 0.1322 0.0082 0.1559 0.0149  0.0033  -0.0035 105 HIS D ND1 
7218 C  CD2 . HIS D 105 ? 0.2032 0.0134 0.1280 0.0312  0.0028  0.0165  105 HIS D CD2 
7219 C  CE1 . HIS D 105 ? 0.1816 0.0079 0.1324 -0.0119 0.0110  -0.0053 105 HIS D CE1 
7220 N  NE2 . HIS D 105 ? 0.1884 0.0072 0.1414 0.0078  0.0166  -0.0081 105 HIS D NE2 
7221 N  N   . THR D 106 ? 0.1718 0.0113 0.1647 0.0286  -0.0142 -0.0051 106 THR D N   
7222 C  CA  . THR D 106 ? 0.1918 0.0204 0.1286 0.0476  0.0181  -0.0048 106 THR D CA  
7223 C  C   . THR D 106 ? 0.1992 0.0148 0.1708 0.0044  -0.0069 0.0013  106 THR D C   
7224 O  O   . THR D 106 ? 0.2056 0.0079 0.1553 0.0032  -0.0082 0.0148  106 THR D O   
7225 C  CB  . THR D 106 ? 0.2027 0.0267 0.1577 0.0075  0.0406  -0.0334 106 THR D CB  
7226 O  OG1 . THR D 106 ? 0.1787 0.0464 0.2027 0.0351  -0.0065 -0.0190 106 THR D OG1 
7227 C  CG2 . THR D 106 ? 0.1531 0.0527 0.1787 -0.0078 0.0222  -0.0060 106 THR D CG2 
7228 N  N   . VAL D 107 ? 0.1536 0.0074 0.2046 0.0038  -0.0345 0.0130  107 VAL D N   
7229 C  CA  . VAL D 107 ? 0.1322 0.0954 0.2535 0.0079  -0.0326 0.0690  107 VAL D CA  
7230 C  C   . VAL D 107 ? 0.1568 0.0322 0.2078 0.0102  -0.0164 0.0424  107 VAL D C   
7231 O  O   . VAL D 107 ? 0.2253 0.0577 0.2321 0.0385  0.0074  0.0241  107 VAL D O   
7232 C  CB  . VAL D 107 ? 0.1823 0.0350 0.2487 -0.0047 -0.0002 0.0373  107 VAL D CB  
7233 C  CG1 . VAL D 107 ? 0.2480 0.0329 0.2852 -0.0241 -0.0495 0.0597  107 VAL D CG1 
7234 C  CG2 . VAL D 107 ? 0.1949 0.0310 0.2484 0.0062  0.0042  0.0241  107 VAL D CG2 
7235 N  N   . SER D 108 ? 0.1773 0.0365 0.2342 0.0207  -0.0348 0.0546  108 SER D N   
7236 C  CA  . SER D 108 ? 0.1753 0.0102 0.2753 0.0189  -0.0189 0.0194  108 SER D CA  
7237 C  C   . SER D 108 ? 0.1460 0.0537 0.2578 0.0556  -0.0189 0.0270  108 SER D C   
7238 O  O   . SER D 108 ? 0.1660 0.1173 0.2275 0.0520  -0.0133 -0.0177 108 SER D O   
7239 C  CB  . SER D 108 ? 0.2347 0.0268 0.3710 0.0229  -0.0026 0.0811  108 SER D CB  
7240 O  OG  . SER D 108 ? 0.2902 0.0776 0.3043 0.0143  -0.0341 0.0869  108 SER D OG  
7241 N  N   . GLY D 109 ? 0.2092 0.0669 0.2002 0.0168  -0.0396 0.0364  109 GLY D N   
7242 C  CA  . GLY D 109 ? 0.1449 0.0927 0.2069 0.0326  -0.0299 0.0102  109 GLY D CA  
7243 C  C   . GLY D 109 ? 0.1681 0.1388 0.2022 0.0769  -0.0100 -0.0171 109 GLY D C   
7244 O  O   . GLY D 109 ? 0.2349 0.3261 0.1873 0.0469  -0.0160 0.0281  109 GLY D O   
7245 N  N   . GLN D 110 ? 0.1844 0.1262 0.2232 0.0891  -0.0687 -0.0039 110 GLN D N   
7246 C  CA  . GLN D 110 ? 0.2103 0.1417 0.2227 0.0820  -0.0775 0.0216  110 GLN D CA  
7247 C  C   . GLN D 110 ? 0.1712 0.0977 0.1941 0.0472  -0.0502 0.0346  110 GLN D C   
7248 O  O   . GLN D 110 ? 0.1941 0.0063 0.2550 -0.0004 -0.0154 0.0001  110 GLN D O   
7249 C  CB  . GLN D 110 ? 0.3933 0.0986 0.2895 0.1063  -0.0708 -0.0079 110 GLN D CB  
7250 C  CG  . GLN D 110 ? 0.2157 0.3291 0.3844 0.1459  -0.0233 0.0816  110 GLN D CG  
7251 C  CD  . GLN D 110 ? 0.1990 0.2356 0.4501 0.0854  -0.0161 -0.0107 110 GLN D CD  
7252 O  OE1 . GLN D 110 ? 0.4971 0.3661 0.4766 0.0864  0.0227  -0.1662 110 GLN D OE1 
7253 N  NE2 . GLN D 110 ? 0.3427 0.4372 0.3796 0.0212  -0.0532 0.0174  110 GLN D NE2 
7254 N  N   . HIS D 111 ? 0.2117 0.0326 0.1764 0.0288  -0.0343 0.0013  111 HIS D N   
7255 C  CA  . HIS D 111 ? 0.1435 0.0551 0.1694 -0.0190 -0.0237 0.0290  111 HIS D CA  
7256 C  C   . HIS D 111 ? 0.1684 0.0115 0.1833 0.0034  -0.0013 -0.0300 111 HIS D C   
7257 O  O   . HIS D 111 ? 0.1733 0.0600 0.2551 0.0498  -0.0223 -0.0834 111 HIS D O   
7258 C  CB  . HIS D 111 ? 0.1455 0.0560 0.1591 -0.0200 0.0010  0.0047  111 HIS D CB  
7259 C  CG  . HIS D 111 ? 0.1392 0.0223 0.1326 0.0104  0.0100  0.0043  111 HIS D CG  
7260 N  ND1 . HIS D 111 ? 0.1428 0.0322 0.1959 0.0152  0.0084  -0.0107 111 HIS D ND1 
7261 C  CD2 . HIS D 111 ? 0.1485 0.0380 0.1735 -0.0257 0.0114  -0.0369 111 HIS D CD2 
7262 C  CE1 . HIS D 111 ? 0.1636 0.0665 0.2288 -0.0234 -0.0029 0.0194  111 HIS D CE1 
7263 N  NE2 . HIS D 111 ? 0.2234 0.0159 0.2332 0.0062  0.0004  -0.0131 111 HIS D NE2 
7264 N  N   . PHE D 112 ? 0.1360 0.0495 0.1710 0.0009  -0.0284 0.0210  112 PHE D N   
7265 C  CA  . PHE D 112 ? 0.1356 0.0192 0.1715 0.0125  -0.0064 -0.0025 112 PHE D CA  
7266 C  C   . PHE D 112 ? 0.1338 0.0476 0.1708 -0.0097 -0.0472 0.0216  112 PHE D C   
7267 O  O   . PHE D 112 ? 0.1586 0.0080 0.1907 0.0126  -0.0054 -0.0111 112 PHE D O   
7268 C  CB  . PHE D 112 ? 0.1752 0.0077 0.1767 0.0147  0.0339  -0.0013 112 PHE D CB  
7269 C  CG  . PHE D 112 ? 0.1872 0.0165 0.2642 0.0059  0.0054  0.0508  112 PHE D CG  
7270 C  CD1 . PHE D 112 ? 0.1797 0.0996 0.2599 0.0700  0.0030  0.0512  112 PHE D CD1 
7271 C  CD2 . PHE D 112 ? 0.2938 0.0134 0.2227 -0.0267 0.0188  0.0296  112 PHE D CD2 
7272 C  CE1 . PHE D 112 ? 0.2805 0.1381 0.2644 0.0719  -0.0376 0.0761  112 PHE D CE1 
7273 C  CE2 . PHE D 112 ? 0.3054 0.0583 0.3046 0.0532  0.0340  0.1027  112 PHE D CE2 
7274 C  CZ  . PHE D 112 ? 0.2563 0.1586 0.2713 0.0348  0.0531  0.1354  112 PHE D CZ  
7275 N  N   . ALA D 113 ? 0.1087 0.0194 0.1537 0.0355  -0.0265 -0.0193 113 ALA D N   
7276 C  CA  . ALA D 113 ? 0.1679 0.0152 0.1395 0.0102  -0.0134 -0.0308 113 ALA D CA  
7277 C  C   . ALA D 113 ? 0.1049 0.0148 0.1679 0.0009  -0.0122 0.0226  113 ALA D C   
7278 O  O   . ALA D 113 ? 0.1464 0.0153 0.1441 0.0114  0.0156  0.0115  113 ALA D O   
7279 C  CB  . ALA D 113 ? 0.1843 0.0453 0.1498 0.0005  -0.0097 -0.0339 113 ALA D CB  
7280 N  N   . ALA D 114 ? 0.1379 0.0073 0.1385 0.0080  -0.0002 -0.0078 114 ALA D N   
7281 C  CA  . ALA D 114 ? 0.1214 0.0076 0.1430 0.0087  0.0112  0.0099  114 ALA D CA  
7282 C  C   . ALA D 114 ? 0.1474 0.0122 0.0998 0.0181  -0.0092 -0.0192 114 ALA D C   
7283 O  O   . ALA D 114 ? 0.1619 0.0102 0.1505 -0.0244 0.0136  -0.0037 114 ALA D O   
7284 C  CB  . ALA D 114 ? 0.1507 0.0066 0.1489 -0.0059 -0.0016 0.0020  114 ALA D CB  
7285 N  N   . GLU D 115 ? 0.1254 0.0065 0.1509 0.0036  0.0165  -0.0023 115 GLU D N   
7286 C  CA  . GLU D 115 ? 0.1121 0.0093 0.1396 -0.0020 -0.0018 0.0197  115 GLU D CA  
7287 C  C   . GLU D 115 ? 0.1035 0.0275 0.1477 0.0013  0.0004  0.0385  115 GLU D C   
7288 O  O   . GLU D 115 ? 0.1359 0.0102 0.1537 -0.0088 0.0225  0.0204  115 GLU D O   
7289 C  CB  . GLU D 115 ? 0.1284 0.0286 0.1176 -0.0142 -0.0066 0.0272  115 GLU D CB  
7290 C  CG  . GLU D 115 ? 0.1545 0.0405 0.1196 0.0053  -0.0096 0.0324  115 GLU D CG  
7291 C  CD  . GLU D 115 ? 0.1080 0.0121 0.1690 -0.0017 0.0044  -0.0046 115 GLU D CD  
7292 O  OE1 . GLU D 115 ? 0.1040 0.0119 0.1406 0.0047  -0.0168 0.0144  115 GLU D OE1 
7293 O  OE2 . GLU D 115 ? 0.1385 0.0115 0.1726 0.0261  -0.0088 -0.0034 115 GLU D OE2 
7294 N  N   . LEU D 116 ? 0.1116 0.0084 0.1575 0.0120  0.0198  -0.0078 116 LEU D N   
7295 C  CA  . LEU D 116 ? 0.0875 0.0317 0.1640 0.0067  0.0021  -0.0080 116 LEU D CA  
7296 C  C   . LEU D 116 ? 0.1265 0.0072 0.1399 0.0104  0.0253  0.0032  116 LEU D C   
7297 O  O   . LEU D 116 ? 0.1482 0.0104 0.1373 -0.0040 0.0041  -0.0231 116 LEU D O   
7298 C  CB  . LEU D 116 ? 0.1042 0.0286 0.2017 -0.0035 0.0051  -0.0379 116 LEU D CB  
7299 C  CG  . LEU D 116 ? 0.1003 0.0100 0.1782 -0.0047 -0.0089 0.0247  116 LEU D CG  
7300 C  CD1 . LEU D 116 ? 0.1693 0.0268 0.1599 0.0098  -0.0161 0.0190  116 LEU D CD1 
7301 C  CD2 . LEU D 116 ? 0.1622 0.0215 0.2248 -0.0486 -0.0159 0.0049  116 LEU D CD2 
7302 N  N   . HIS D 117 ? 0.1370 0.0125 0.1688 0.0257  0.0171  -0.0101 117 HIS D N   
7303 C  CA  . HIS D 117 ? 0.0978 0.0270 0.1356 -0.0421 0.0011  -0.0136 117 HIS D CA  
7304 C  C   . HIS D 117 ? 0.1477 0.0100 0.1164 0.0179  0.0093  -0.0111 117 HIS D C   
7305 O  O   . HIS D 117 ? 0.1492 0.0110 0.1370 0.0233  0.0047  0.0113  117 HIS D O   
7306 C  CB  . HIS D 117 ? 0.0822 0.0147 0.1691 -0.0188 -0.0028 -0.0238 117 HIS D CB  
7307 C  CG  . HIS D 117 ? 0.0692 0.0135 0.1465 -0.0182 0.0349  0.0048  117 HIS D CG  
7308 N  ND1 . HIS D 117 ? 0.0091 0.0238 0.8751 0.0069  -0.0491 -0.1232 117 HIS D ND1 
7309 C  CD2 . HIS D 117 ? 0.1158 0.0122 0.2194 0.0186  -0.0102 -0.0257 117 HIS D CD2 
7310 C  CE1 . HIS D 117 ? 0.1082 0.0510 0.1372 -0.0601 -0.0388 -0.0097 117 HIS D CE1 
7311 N  NE2 . HIS D 117 ? 0.1116 0.0079 0.1945 -0.0011 -0.0103 -0.0171 117 HIS D NE2 
7312 N  N   . ILE D 118 ? 0.1121 0.0259 0.1449 0.0263  0.0139  0.0019  118 ILE D N   
7313 C  CA  . ILE D 118 ? 0.0814 0.0464 0.1277 0.0100  -0.0144 -0.0053 118 ILE D CA  
7314 C  C   . ILE D 118 ? 0.1185 0.0234 0.1171 0.0397  0.0040  0.0113  118 ILE D C   
7315 O  O   . ILE D 118 ? 0.1507 0.0133 0.1329 0.0283  -0.0055 -0.0044 118 ILE D O   
7316 C  CB  . ILE D 118 ? 0.1514 0.0066 0.1547 0.0061  0.0129  0.0038  118 ILE D CB  
7317 C  CG1 . ILE D 118 ? 0.1638 0.0069 0.1370 -0.0068 0.0156  0.0054  118 ILE D CG1 
7318 C  CG2 . ILE D 118 ? 0.1469 0.0706 0.1536 0.0226  0.0074  0.0313  118 ILE D CG2 
7319 C  CD1 . ILE D 118 ? 0.1938 0.0566 0.1868 -0.0457 0.0359  0.0037  118 ILE D CD1 
7320 N  N   . VAL D 119 ? 0.1452 0.0190 0.1261 0.0405  -0.0091 -0.0124 119 VAL D N   
7321 C  CA  . VAL D 119 ? 0.1543 0.0143 0.1092 0.0308  0.0035  -0.0118 119 VAL D CA  
7322 C  C   . VAL D 119 ? 0.1591 0.0075 0.1194 0.0128  0.0131  0.0043  119 VAL D C   
7323 O  O   . VAL D 119 ? 0.1518 0.0372 0.1449 0.0222  0.0044  -0.0106 119 VAL D O   
7324 C  CB  . VAL D 119 ? 0.1635 0.0128 0.1577 0.0104  0.0177  -0.0282 119 VAL D CB  
7325 C  CG1 . VAL D 119 ? 0.2329 0.0164 0.1636 0.0337  -0.0049 -0.0291 119 VAL D CG1 
7326 C  CG2 . VAL D 119 ? 0.1471 0.0267 0.1499 0.0282  -0.0016 -0.0129 119 VAL D CG2 
7327 N  N   . HIS D 120 ? 0.1535 0.0099 0.1240 0.0109  0.0193  0.0015  120 HIS D N   
7328 C  CA  . HIS D 120 ? 0.1561 0.0490 0.1276 0.0068  0.0223  -0.0204 120 HIS D CA  
7329 C  C   . HIS D 120 ? 0.1686 0.0189 0.1324 0.0423  0.0173  -0.0092 120 HIS D C   
7330 O  O   . HIS D 120 ? 0.1815 0.0098 0.1991 0.0246  0.0132  0.0039  120 HIS D O   
7331 C  CB  . HIS D 120 ? 0.1624 0.0475 0.1385 0.0040  -0.0108 0.0037  120 HIS D CB  
7332 C  CG  . HIS D 120 ? 0.1322 0.0444 0.1401 0.0305  -0.0089 -0.0132 120 HIS D CG  
7333 N  ND1 . HIS D 120 ? 0.1754 0.0390 0.1811 0.0466  -0.0218 -0.0348 120 HIS D ND1 
7334 C  CD2 . HIS D 120 ? 0.1563 0.0238 0.1280 0.0320  0.0308  -0.0089 120 HIS D CD2 
7335 C  CE1 . HIS D 120 ? 0.1420 0.0914 0.1650 -0.0038 -0.0184 -0.0128 120 HIS D CE1 
7336 N  NE2 . HIS D 120 ? 0.1879 0.0344 0.1488 0.0436  0.0247  -0.0229 120 HIS D NE2 
7337 N  N   . TYR D 121 ? 0.1596 0.0274 0.1774 0.0388  -0.0025 -0.0443 121 TYR D N   
7338 C  CA  . TYR D 121 ? 0.2394 0.0067 0.1363 0.0033  0.0118  -0.0068 121 TYR D CA  
7339 C  C   . TYR D 121 ? 0.2058 0.0082 0.1621 0.0145  0.0039  0.0116  121 TYR D C   
7340 O  O   . TYR D 121 ? 0.1802 0.0112 0.1961 0.0275  0.0251  0.0136  121 TYR D O   
7341 C  CB  . TYR D 121 ? 0.2091 0.0080 0.1625 0.0180  0.0116  -0.0023 121 TYR D CB  
7342 C  CG  . TYR D 121 ? 0.2057 0.0084 0.1549 0.0186  0.0108  0.0081  121 TYR D CG  
7343 C  CD1 . TYR D 121 ? 0.2131 0.0399 0.1538 0.0403  -0.0220 0.0102  121 TYR D CD1 
7344 C  CD2 . TYR D 121 ? 0.2057 0.0226 0.1885 0.0516  0.0110  0.0257  121 TYR D CD2 
7345 C  CE1 . TYR D 121 ? 0.2332 0.0286 0.2315 0.0588  -0.0259 0.0326  121 TYR D CE1 
7346 C  CE2 . TYR D 121 ? 0.2037 0.0625 0.1902 0.0409  -0.0008 0.0607  121 TYR D CE2 
7347 C  CZ  . TYR D 121 ? 0.2168 0.0913 0.2091 0.0701  -0.0073 0.0380  121 TYR D CZ  
7348 O  OH  . TYR D 121 ? 0.2325 0.0751 0.3023 0.0324  -0.0458 0.0649  121 TYR D OH  
7349 N  N   . ASN D 122 ? 0.2078 0.0170 0.1715 0.0389  0.0121  -0.0203 122 ASN D N   
7350 C  CA  . ASN D 122 ? 0.1632 0.0329 0.1772 0.0380  0.0072  -0.0203 122 ASN D CA  
7351 C  C   . ASN D 122 ? 0.1618 0.0267 0.1690 0.0247  -0.0252 0.0267  122 ASN D C   
7352 O  O   . ASN D 122 ? 0.1944 0.0233 0.2176 0.0269  0.0165  0.0177  122 ASN D O   
7353 C  CB  . ASN D 122 ? 0.1860 0.0110 0.1641 0.0287  -0.0014 -0.0048 122 ASN D CB  
7354 C  CG  . ASN D 122 ? 0.1866 0.0286 0.1667 0.0378  0.0040  -0.0155 122 ASN D CG  
7355 O  OD1 . ASN D 122 ? 0.1965 0.0347 0.2015 0.0543  0.0236  -0.0229 122 ASN D OD1 
7356 N  ND2 . ASN D 122 ? 0.2356 0.0647 0.1798 0.0252  -0.0238 0.0082  122 ASN D ND2 
7357 N  N   . SER D 123 ? 0.1232 0.1036 0.1277 0.0391  0.0164  -0.0079 123 SER D N   
7358 C  CA  . SER D 123 ? 0.1225 0.0393 0.2211 0.0250  0.0223  -0.0536 123 SER D CA  
7359 C  C   . SER D 123 ? 0.1477 0.0575 0.1949 0.0405  0.0072  -0.0383 123 SER D C   
7360 O  O   . SER D 123 ? 0.1891 0.0443 0.2478 0.0518  0.0204  -0.0040 123 SER D O   
7361 C  CB  . SER D 123 ? 0.1991 0.0392 0.1987 -0.0220 0.0091  -0.0184 123 SER D CB  
7362 O  OG  . SER D 123 ? 0.1726 0.0303 0.2099 -0.0017 0.0092  -0.0135 123 SER D OG  
7363 N  N   . ASP D 124 ? 0.2188 0.0696 0.1880 0.0370  0.0330  -0.0301 124 ASP D N   
7364 C  CA  . ASP D 124 ? 0.2593 0.0253 0.1767 0.0271  0.0273  -0.0241 124 ASP D CA  
7365 C  C   . ASP D 124 ? 0.2451 0.0305 0.1981 0.0102  0.0343  -0.0055 124 ASP D C   
7366 O  O   . ASP D 124 ? 0.2586 0.1039 0.2984 0.0156  0.0782  -0.0615 124 ASP D O   
7367 C  CB  . ASP D 124 ? 0.2577 0.0336 0.2078 0.0097  0.0002  -0.0095 124 ASP D CB  
7368 C  CG  . ASP D 124 ? 0.1636 0.1004 0.1634 0.0062  0.0120  -0.0187 124 ASP D CG  
7369 O  OD1 . ASP D 124 ? 0.1937 0.1186 0.1866 0.0244  -0.0105 0.0035  124 ASP D OD1 
7370 O  OD2 . ASP D 124 ? 0.2382 0.1105 0.1801 0.0223  0.0057  -0.0084 124 ASP D OD2 
7371 N  N   . LEU D 125 ? 0.2694 0.0194 0.1925 0.0089  0.0612  -0.0200 125 LEU D N   
7372 C  CA  . LEU D 125 ? 0.2487 0.0265 0.1909 0.0342  0.0206  -0.0318 125 LEU D CA  
7373 C  C   . LEU D 125 ? 0.1992 0.0401 0.2042 0.0299  0.0212  -0.0178 125 LEU D C   
7374 O  O   . LEU D 125 ? 0.2779 0.0507 0.2676 0.0548  -0.0064 -0.0624 125 LEU D O   
7375 C  CB  . LEU D 125 ? 0.2340 0.0602 0.2304 0.0018  -0.0259 0.0236  125 LEU D CB  
7376 C  CG  . LEU D 125 ? 0.2223 0.1577 0.2315 -0.0269 0.0037  0.0310  125 LEU D CG  
7377 C  CD1 . LEU D 125 ? 0.2802 0.1708 0.2944 -0.0020 0.0833  0.0696  125 LEU D CD1 
7378 C  CD2 . LEU D 125 ? 0.2279 0.1753 0.3300 -0.0130 -0.0029 0.0281  125 LEU D CD2 
7379 N  N   . TYR D 126 ? 0.2163 0.0498 0.1782 0.0485  0.0230  0.0037  126 TYR D N   
7380 C  CA  . TYR D 126 ? 0.2171 0.0450 0.1926 0.0257  0.0004  0.0113  126 TYR D CA  
7381 C  C   . TYR D 126 ? 0.2547 0.0466 0.2293 0.0407  -0.0311 0.0154  126 TYR D C   
7382 O  O   . TYR D 126 ? 0.2390 0.1015 0.2521 0.0013  -0.0243 0.0206  126 TYR D O   
7383 C  CB  . TYR D 126 ? 0.2157 0.0365 0.2002 0.0741  -0.0215 -0.0296 126 TYR D CB  
7384 C  CG  . TYR D 126 ? 0.2137 0.0602 0.2156 0.0316  -0.0221 -0.0109 126 TYR D CG  
7385 C  CD1 . TYR D 126 ? 0.2502 0.0516 0.2200 0.0128  -0.0128 0.0077  126 TYR D CD1 
7386 C  CD2 . TYR D 126 ? 0.2319 0.0643 0.1798 0.0125  -0.0167 0.0244  126 TYR D CD2 
7387 C  CE1 . TYR D 126 ? 0.2451 0.0523 0.1998 0.0254  -0.0052 -0.0009 126 TYR D CE1 
7388 C  CE2 . TYR D 126 ? 0.2252 0.0338 0.1844 -0.0089 -0.0150 -0.0055 126 TYR D CE2 
7389 C  CZ  . TYR D 126 ? 0.1908 0.0408 0.1852 0.0161  -0.0155 -0.0238 126 TYR D CZ  
7390 O  OH  . TYR D 126 ? 0.2132 0.0489 0.1819 0.0151  -0.0162 -0.0211 126 TYR D OH  
7391 N  N   . PRO D 127 ? 0.2684 0.0162 0.2917 0.0145  -0.0241 0.0288  127 PRO D N   
7392 C  CA  . PRO D 127 ? 0.3140 0.0710 0.2987 -0.0077 -0.0675 0.0566  127 PRO D CA  
7393 C  C   . PRO D 127 ? 0.3110 0.0927 0.2846 -0.0293 -0.0537 0.0765  127 PRO D C   
7394 O  O   . PRO D 127 ? 0.3721 0.1638 0.2687 0.0029  -0.0829 0.0743  127 PRO D O   
7395 C  CB  . PRO D 127 ? 0.3559 0.0863 0.3255 0.0628  -0.0474 0.0643  127 PRO D CB  
7396 C  CG  . PRO D 127 ? 0.4458 0.0875 0.2772 0.0218  -0.0880 0.0775  127 PRO D CG  
7397 C  CD  . PRO D 127 ? 0.3558 0.0195 0.2761 0.0044  -0.0359 0.0586  127 PRO D CD  
7398 N  N   . ASP D 128 ? 0.3121 0.0930 0.2070 -0.0585 -0.0716 0.0705  128 ASP D N   
7399 C  CA  . ASP D 128 ? 0.2676 0.1241 0.2102 -0.0961 -0.0392 0.0766  128 ASP D CA  
7400 C  C   . ASP D 128 ? 0.2847 0.0455 0.1859 -0.0688 -0.0301 0.0368  128 ASP D C   
7401 O  O   . ASP D 128 ? 0.3607 0.0802 0.1769 -0.0545 -0.0462 0.0122  128 ASP D O   
7402 C  CB  . ASP D 128 ? 0.3524 0.0905 0.2424 -0.0524 -0.0175 0.0871  128 ASP D CB  
7403 C  CG  . ASP D 128 ? 0.3291 0.1721 0.2656 -0.1153 -0.0805 0.1000  128 ASP D CG  
7404 O  OD1 . ASP D 128 ? 0.3702 0.1046 0.3622 -0.0368 -0.1247 0.0296  128 ASP D OD1 
7405 O  OD2 . ASP D 128 ? 0.5972 0.2249 0.3983 0.0044  -0.0853 0.1500  128 ASP D OD2 
7406 N  N   . ALA D 129 ? 0.3623 0.0549 0.1879 -0.0585 -0.0601 0.0200  129 ALA D N   
7407 C  CA  . ALA D 129 ? 0.3072 0.0632 0.2324 -0.0939 -0.0614 -0.0412 129 ALA D CA  
7408 C  C   . ALA D 129 ? 0.2872 0.0281 0.2354 -0.0590 -0.0595 0.0124  129 ALA D C   
7409 O  O   . ALA D 129 ? 0.3077 0.0369 0.2378 -0.0245 -0.0663 0.0170  129 ALA D O   
7410 C  CB  . ALA D 129 ? 0.3402 0.0417 0.2347 -0.0398 -0.0747 -0.0281 129 ALA D CB  
7411 N  N   . SER D 130 ? 0.3394 0.0640 0.1758 -0.0649 -0.0122 0.0137  130 SER D N   
7412 C  CA  . SER D 130 ? 0.3679 0.0749 0.1747 -0.0875 -0.0161 0.0381  130 SER D CA  
7413 C  C   . SER D 130 ? 0.3319 0.0598 0.2108 -0.0582 -0.0350 0.0234  130 SER D C   
7414 O  O   . SER D 130 ? 0.3260 0.0660 0.2491 -0.0549 -0.0661 -0.0088 130 SER D O   
7415 C  CB  . SER D 130 ? 0.3599 0.1011 0.3757 -0.0768 -0.0076 0.1539  130 SER D CB  
7416 O  OG  . SER D 130 ? 0.4487 0.2038 0.5681 -0.1659 0.0105  0.0664  130 SER D OG  
7417 N  N   . THR D 131 ? 0.3608 0.0152 0.2302 -0.0400 -0.0180 0.0333  131 THR D N   
7418 C  CA  . THR D 131 ? 0.2952 0.0332 0.2137 -0.0184 -0.0273 0.0251  131 THR D CA  
7419 C  C   . THR D 131 ? 0.2885 0.0153 0.2565 0.0298  -0.0450 0.0013  131 THR D C   
7420 O  O   . THR D 131 ? 0.2364 0.0139 0.2404 -0.0061 -0.0120 -0.0051 131 THR D O   
7421 C  CB  . THR D 131 ? 0.2543 0.0647 0.2375 -0.0110 -0.0601 0.0097  131 THR D CB  
7422 O  OG1 . THR D 131 ? 0.2841 0.0895 0.3731 0.0059  -0.0397 0.0969  131 THR D OG1 
7423 C  CG2 . THR D 131 ? 0.2931 0.0253 0.3035 0.0312  -0.0563 -0.0416 131 THR D CG2 
7424 N  N   . ALA D 132 ? 0.3033 0.0297 0.1352 0.0017  -0.0072 0.0040  132 ALA D N   
7425 C  CA  . ALA D 132 ? 0.2089 0.0068 0.1814 -0.0100 -0.0274 0.0025  132 ALA D CA  
7426 C  C   . ALA D 132 ? 0.2284 0.0099 0.1615 0.0111  -0.0037 0.0055  132 ALA D C   
7427 O  O   . ALA D 132 ? 0.2322 0.0282 0.1428 0.0193  -0.0161 -0.0061 132 ALA D O   
7428 C  CB  . ALA D 132 ? 0.2204 0.0408 0.1643 -0.0290 -0.0306 -0.0428 132 ALA D CB  
7429 N  N   . SER D 133 ? 0.2518 0.0262 0.1798 0.0000  0.0146  -0.0146 133 SER D N   
7430 C  CA  . SER D 133 ? 0.2893 0.0066 0.2015 0.0098  0.0623  0.0028  133 SER D CA  
7431 C  C   . SER D 133 ? 0.2854 0.0394 0.1930 0.0591  0.0316  -0.0159 133 SER D C   
7432 O  O   . SER D 133 ? 0.2721 0.0100 0.2202 0.0310  0.0342  0.0071  133 SER D O   
7433 C  CB  . SER D 133 ? 0.3147 0.0175 0.1793 0.0452  0.0296  0.0321  133 SER D CB  
7434 O  OG  . SER D 133 ? 0.3503 0.0238 0.1805 -0.0021 0.0099  0.0386  133 SER D OG  
7435 N  N   . ASN D 134 ? 0.2017 0.0282 0.1822 -0.0067 0.0146  0.0003  134 ASN D N   
7436 C  CA  . ASN D 134 ? 0.2231 0.0504 0.1938 -0.0366 0.0237  0.0266  134 ASN D CA  
7437 C  C   . ASN D 134 ? 0.1986 0.0507 0.1956 -0.0183 0.0331  -0.0001 134 ASN D C   
7438 O  O   . ASN D 134 ? 0.2265 0.0911 0.2394 -0.0120 0.0083  -0.0287 134 ASN D O   
7439 C  CB  . ASN D 134 ? 0.2476 0.0244 0.2345 -0.0249 0.0234  0.0296  134 ASN D CB  
7440 C  CG  . ASN D 134 ? 0.2707 0.0633 0.2889 0.0063  0.0739  0.0444  134 ASN D CG  
7441 O  OD1 . ASN D 134 ? 0.2764 0.0319 0.2881 -0.0195 -0.0039 0.0497  134 ASN D OD1 
7442 N  ND2 . ASN D 134 ? 0.2891 0.0774 0.3338 -0.0070 0.0063  0.0882  134 ASN D ND2 
7443 N  N   . LYS D 135 ? 0.2187 0.0128 0.2027 -0.0104 0.0472  0.0309  135 LYS D N   
7444 C  CA  . LYS D 135 ? 0.2134 0.0414 0.2013 0.0000  0.0252  0.0179  135 LYS D CA  
7445 C  C   . LYS D 135 ? 0.2534 0.0338 0.1437 -0.0341 -0.0264 -0.0088 135 LYS D C   
7446 O  O   . LYS D 135 ? 0.2275 0.0355 0.1877 -0.0136 -0.0135 -0.0269 135 LYS D O   
7447 C  CB  . LYS D 135 ? 0.2394 0.0098 0.2279 -0.0030 0.0118  -0.0061 135 LYS D CB  
7448 C  CG  . LYS D 135 ? 0.2346 0.0073 0.2345 -0.0040 0.0195  -0.0070 135 LYS D CG  
7449 C  CD  . LYS D 135 ? 0.2670 0.0463 0.2586 0.0359  0.0037  0.0052  135 LYS D CD  
7450 C  CE  . LYS D 135 ? 0.2572 0.0101 0.2921 0.0115  0.0120  -0.0300 135 LYS D CE  
7451 N  NZ  . LYS D 135 ? 0.2529 0.0173 0.3166 -0.0102 0.0002  -0.0260 135 LYS D NZ  
7452 N  N   A SER D 136 ? 0.2428 0.0609 0.1448 -0.0268 -0.0058 0.0179  136 SER D N   
7453 N  N   B SER D 136 ? 0.2467 0.0838 0.1482 -0.0309 -0.0027 -0.0047 136 SER D N   
7454 C  CA  A SER D 136 ? 0.2146 0.0159 0.1776 -0.0288 -0.0233 0.0044  136 SER D CA  
7455 C  CA  B SER D 136 ? 0.2282 0.0440 0.1663 -0.0381 -0.0203 -0.0195 136 SER D CA  
7456 C  C   A SER D 136 ? 0.2175 0.0303 0.1988 -0.0243 -0.0325 -0.0414 136 SER D C   
7457 C  C   B SER D 136 ? 0.2145 0.0366 0.1962 -0.0134 -0.0342 -0.0498 136 SER D C   
7458 O  O   A SER D 136 ? 0.2128 0.0250 0.1895 -0.0428 0.0010  0.0097  136 SER D O   
7459 O  O   B SER D 136 ? 0.2189 0.0610 0.1775 -0.0066 -0.0082 0.0042  136 SER D O   
7460 C  CB  A SER D 136 ? 0.2728 0.0120 0.1830 0.0069  -0.0300 0.0015  136 SER D CB  
7461 C  CB  B SER D 136 ? 0.2888 0.0578 0.1678 -0.0197 0.0060  -0.0065 136 SER D CB  
7462 O  OG  A SER D 136 ? 0.2709 0.0105 0.2198 0.0242  -0.0708 0.0130  136 SER D OG  
7463 O  OG  B SER D 136 ? 0.3426 0.0992 0.2203 -0.0062 -0.0583 -0.0684 136 SER D OG  
7464 N  N   . GLU D 137 ? 0.2375 0.0318 0.1823 -0.0144 -0.0048 -0.0197 137 GLU D N   
7465 C  CA  . GLU D 137 ? 0.1970 0.0207 0.1927 0.0027  -0.0212 0.0057  137 GLU D CA  
7466 C  C   . GLU D 137 ? 0.1949 0.0167 0.1708 0.0000  -0.0027 -0.0047 137 GLU D C   
7467 O  O   . GLU D 137 ? 0.2038 0.0167 0.1919 -0.0154 -0.0227 -0.0017 137 GLU D O   
7468 C  CB  . GLU D 137 ? 0.2845 0.0106 0.1456 -0.0068 -0.0263 0.0243  137 GLU D CB  
7469 C  CG  . GLU D 137 ? 0.3287 0.0524 0.1575 0.0330  -0.0348 -0.0040 137 GLU D CG  
7470 C  CD  . GLU D 137 ? 0.3797 0.1837 0.2189 0.1155  -0.0663 0.0610  137 GLU D CD  
7471 O  OE1 . GLU D 137 ? 0.3473 0.0578 0.4774 0.0331  0.0209  0.0380  137 GLU D OE1 
7472 O  OE2 . GLU D 137 ? 0.4563 0.3901 0.3599 0.1879  -0.1910 0.0247  137 GLU D OE2 
7473 N  N   . GLY D 138 ? 0.2189 0.0111 0.1570 -0.0183 0.0009  -0.0219 138 GLY D N   
7474 C  CA  . GLY D 138 ? 0.1869 0.0181 0.1988 0.0280  -0.0313 -0.0347 138 GLY D CA  
7475 C  C   . GLY D 138 ? 0.1777 0.0088 0.1687 0.0133  0.0031  -0.0150 138 GLY D C   
7476 O  O   . GLY D 138 ? 0.2020 0.0110 0.1639 0.0044  -0.0002 0.0083  138 GLY D O   
7477 N  N   . LEU D 139 ? 0.1942 0.0082 0.1218 0.0157  0.0204  -0.0064 139 LEU D N   
7478 C  CA  . LEU D 139 ? 0.2254 0.0070 0.1413 0.0118  -0.0120 -0.0035 139 LEU D CA  
7479 C  C   . LEU D 139 ? 0.2021 0.0093 0.1682 0.0161  0.0012  0.0164  139 LEU D C   
7480 O  O   . LEU D 139 ? 0.1878 0.0149 0.1581 0.0128  0.0218  -0.0322 139 LEU D O   
7481 C  CB  . LEU D 139 ? 0.2367 0.0212 0.1821 0.0552  0.0340  0.0247  139 LEU D CB  
7482 C  CG  . LEU D 139 ? 0.2267 0.0208 0.1334 0.0553  0.0191  0.0131  139 LEU D CG  
7483 C  CD1 . LEU D 139 ? 0.2324 0.0182 0.1729 0.0519  0.0381  0.0084  139 LEU D CD1 
7484 C  CD2 . LEU D 139 ? 0.2390 0.0214 0.1872 0.0166  -0.0100 0.0492  139 LEU D CD2 
7485 N  N   . ALA D 140 ? 0.1653 0.0231 0.1631 0.0515  0.0000  -0.0030 140 ALA D N   
7486 C  CA  . ALA D 140 ? 0.1807 0.0281 0.1124 0.0612  0.0131  0.0099  140 ALA D CA  
7487 C  C   . ALA D 140 ? 0.2077 0.0152 0.1263 0.0399  0.0002  0.0106  140 ALA D C   
7488 O  O   . ALA D 140 ? 0.1987 0.0210 0.1541 0.0531  0.0000  0.0000  140 ALA D O   
7489 C  CB  . ALA D 140 ? 0.1783 0.0227 0.1979 0.0523  0.0144  -0.0046 140 ALA D CB  
7490 N  N   . VAL D 141 ? 0.1624 0.0075 0.1474 0.0135  0.0181  -0.0002 141 VAL D N   
7491 C  CA  . VAL D 141 ? 0.1647 0.0071 0.1341 0.0098  0.0100  0.0060  141 VAL D CA  
7492 C  C   . VAL D 141 ? 0.1356 0.0189 0.1676 0.0231  0.0079  0.0384  141 VAL D C   
7493 O  O   . VAL D 141 ? 0.2012 0.0086 0.1330 0.0213  0.0106  0.0011  141 VAL D O   
7494 C  CB  . VAL D 141 ? 0.1590 0.0102 0.1215 0.0116  0.0100  0.0192  141 VAL D CB  
7495 C  CG1 . VAL D 141 ? 0.2360 0.0652 0.1374 -0.0132 -0.0039 -0.0061 141 VAL D CG1 
7496 C  CG2 . VAL D 141 ? 0.2362 0.0340 0.1473 -0.0183 0.0359  0.0567  141 VAL D CG2 
7497 N  N   . LEU D 142 ? 0.1500 0.0110 0.1444 0.0258  0.0268  0.0070  142 LEU D N   
7498 C  CA  . LEU D 142 ? 0.1370 0.0195 0.1233 0.0390  0.0219  0.0197  142 LEU D CA  
7499 C  C   . LEU D 142 ? 0.1411 0.0067 0.1284 0.0004  0.0144  0.0074  142 LEU D C   
7500 O  O   . LEU D 142 ? 0.1808 0.0201 0.1414 0.0372  0.0160  0.0312  142 LEU D O   
7501 C  CB  . LEU D 142 ? 0.1836 0.0374 0.1306 0.0348  0.0078  -0.0064 142 LEU D CB  
7502 C  CG  . LEU D 142 ? 0.1477 0.0656 0.1646 0.0119  0.0103  -0.0068 142 LEU D CG  
7503 C  CD1 . LEU D 142 ? 0.1625 0.0677 0.2441 -0.0264 0.0194  0.0057  142 LEU D CD1 
7504 C  CD2 . LEU D 142 ? 0.1920 0.0742 0.1563 0.0497  0.0253  -0.0162 142 LEU D CD2 
7505 N  N   . ALA D 143 ? 0.1476 0.0071 0.1892 0.0100  0.0151  0.0058  143 ALA D N   
7506 C  CA  . ALA D 143 ? 0.1390 0.0071 0.1650 -0.0100 -0.0024 -0.0009 143 ALA D CA  
7507 C  C   . ALA D 143 ? 0.1107 0.0090 0.1201 -0.0143 -0.0185 0.0112  143 ALA D C   
7508 O  O   . ALA D 143 ? 0.1851 0.0107 0.1493 -0.0028 0.0054  0.0247  143 ALA D O   
7509 C  CB  . ALA D 143 ? 0.1374 0.0150 0.1629 0.0074  -0.0019 0.0096  143 ALA D CB  
7510 N  N   . VAL D 144 ? 0.1473 0.0063 0.1417 0.0021  0.0029  -0.0009 144 VAL D N   
7511 C  CA  . VAL D 144 ? 0.1244 0.0088 0.1629 0.0169  -0.0028 -0.0036 144 VAL D CA  
7512 C  C   . VAL D 144 ? 0.1748 0.0088 0.1338 0.0085  0.0037  -0.0159 144 VAL D C   
7513 O  O   . VAL D 144 ? 0.1962 0.0104 0.1490 0.0246  0.0139  -0.0093 144 VAL D O   
7514 C  CB  . VAL D 144 ? 0.1462 0.0070 0.1578 -0.0071 0.0129  -0.0081 144 VAL D CB  
7515 C  CG1 . VAL D 144 ? 0.1624 0.0077 0.1779 0.0021  -0.0245 -0.0158 144 VAL D CG1 
7516 C  CG2 . VAL D 144 ? 0.1496 0.0322 0.1681 -0.0055 0.0220  -0.0148 144 VAL D CG2 
7517 N  N   . LEU D 145 ? 0.1332 0.0077 0.1989 0.0132  0.0125  0.0002  145 LEU D N   
7518 C  CA  . LEU D 145 ? 0.1204 0.0160 0.1578 0.0076  -0.0105 -0.0031 145 LEU D CA  
7519 C  C   . LEU D 145 ? 0.1194 0.0083 0.1694 -0.0008 0.0187  -0.0178 145 LEU D C   
7520 O  O   . LEU D 145 ? 0.1423 0.0072 0.2051 -0.0104 0.0192  0.0035  145 LEU D O   
7521 C  CB  . LEU D 145 ? 0.1354 0.0253 0.1703 0.0088  -0.0255 -0.0048 145 LEU D CB  
7522 C  CG  . LEU D 145 ? 0.1893 0.0069 0.1826 -0.0102 -0.0315 0.0058  145 LEU D CG  
7523 C  CD1 . LEU D 145 ? 0.2767 0.0212 0.1821 0.0341  -0.0260 0.0058  145 LEU D CD1 
7524 C  CD2 . LEU D 145 ? 0.2140 0.0117 0.2272 -0.0271 -0.0049 -0.0193 145 LEU D CD2 
7525 N  N   . ILE D 146 ? 0.1585 0.0091 0.1496 0.0173  0.0218  -0.0080 146 ILE D N   
7526 C  CA  . ILE D 146 ? 0.1609 0.0372 0.1517 -0.0126 0.0164  0.0009  146 ILE D CA  
7527 C  C   . ILE D 146 ? 0.1603 0.0116 0.1676 -0.0282 0.0146  -0.0071 146 ILE D C   
7528 O  O   . ILE D 146 ? 0.1397 0.0071 0.1794 0.0043  0.0312  -0.0094 146 ILE D O   
7529 C  CB  . ILE D 146 ? 0.1747 0.0296 0.1502 0.0417  0.0027  -0.0205 146 ILE D CB  
7530 C  CG1 . ILE D 146 ? 0.1612 0.0171 0.2354 0.0375  0.0219  0.0246  146 ILE D CG1 
7531 C  CG2 . ILE D 146 ? 0.1356 0.0518 0.1751 -0.0170 0.0006  -0.0300 146 ILE D CG2 
7532 C  CD1 . ILE D 146 ? 0.1708 0.0084 0.1706 0.0060  -0.0135 0.0173  146 ILE D CD1 
7533 N  N   A GLU D 147 ? 0.1616 0.0070 0.1459 -0.0100 -0.0092 -0.0029 147 GLU D N   
7534 N  N   B GLU D 147 ? 0.1667 0.0069 0.1410 -0.0084 -0.0013 -0.0046 147 GLU D N   
7535 C  CA  A GLU D 147 ? 0.1832 0.0717 0.1428 0.0498  -0.0239 0.0058  147 GLU D CA  
7536 C  CA  B GLU D 147 ? 0.1837 0.0529 0.1489 0.0292  -0.0171 -0.0259 147 GLU D CA  
7537 C  C   A GLU D 147 ? 0.1306 0.0121 0.1689 0.0267  -0.0170 -0.0022 147 GLU D C   
7538 C  C   B GLU D 147 ? 0.1688 0.0113 0.1588 0.0221  -0.0046 -0.0179 147 GLU D C   
7539 O  O   A GLU D 147 ? 0.1313 0.0077 0.1676 0.0116  -0.0292 0.0037  147 GLU D O   
7540 O  O   B GLU D 147 ? 0.1757 0.0130 0.1638 0.0270  -0.0207 -0.0228 147 GLU D O   
7541 C  CB  A GLU D 147 ? 0.1771 0.0451 0.2678 0.0800  -0.0447 -0.0034 147 GLU D CB  
7542 C  CB  B GLU D 147 ? 0.2205 0.0383 0.2101 0.0337  0.0381  -0.0300 147 GLU D CB  
7543 C  CG  A GLU D 147 ? 0.2491 0.0633 0.2516 0.0431  -0.0072 0.0168  147 GLU D CG  
7544 C  CG  B GLU D 147 ? 0.2331 0.0582 0.1776 0.0631  -0.0192 -0.0396 147 GLU D CG  
7545 C  CD  A GLU D 147 ? 0.3300 0.0895 0.3360 0.1250  -0.0333 0.0434  147 GLU D CD  
7546 C  CD  B GLU D 147 ? 0.3074 0.0640 0.2737 0.0614  0.0356  0.0370  147 GLU D CD  
7547 O  OE1 A GLU D 147 ? 0.3438 0.2613 0.2864 0.1462  -0.0171 0.1202  147 GLU D OE1 
7548 O  OE1 B GLU D 147 ? 0.4329 0.0805 0.2735 0.0906  0.0708  0.0367  147 GLU D OE1 
7549 O  OE2 A GLU D 147 ? 0.4063 0.1193 0.3080 0.1011  -0.1197 0.0076  147 GLU D OE2 
7550 O  OE2 B GLU D 147 ? 0.4713 0.0377 0.3837 0.1183  0.0628  0.0375  147 GLU D OE2 
7551 N  N   . MET D 148 ? 0.1764 0.0292 0.1688 0.0298  0.0044  -0.0143 148 MET D N   
7552 C  CA  . MET D 148 ? 0.1639 0.0286 0.1929 -0.0047 0.0052  -0.0370 148 MET D CA  
7553 C  C   . MET D 148 ? 0.1986 0.0123 0.1495 0.0103  -0.0375 -0.0292 148 MET D C   
7554 O  O   . MET D 148 ? 0.1938 0.0147 0.2549 0.0187  -0.0602 -0.0013 148 MET D O   
7555 C  CB  . MET D 148 ? 0.1513 0.0160 0.2081 0.0071  0.0037  -0.0074 148 MET D CB  
7556 C  CG  . MET D 148 ? 0.2709 0.0469 0.1951 0.0105  0.0364  -0.0110 148 MET D CG  
7557 S  SD  . MET D 148 ? 0.2612 0.0327 0.2394 0.0041  0.0400  -0.0269 148 MET D SD  
7558 C  CE  . MET D 148 ? 0.2346 0.0311 0.3008 0.0076  -0.0024 -0.0660 148 MET D CE  
7559 N  N   . GLY D 149 ? 0.1800 0.0144 0.1951 -0.0020 -0.0162 -0.0388 149 GLY D N   
7560 C  CA  . GLY D 149 ? 0.1964 0.0076 0.2142 -0.0008 -0.0360 -0.0157 149 GLY D CA  
7561 C  C   . GLY D 149 ? 0.1472 0.0096 0.2286 0.0164  -0.0071 -0.0182 149 GLY D C   
7562 O  O   . GLY D 149 ? 0.1780 0.0142 0.1997 0.0001  0.0139  -0.0388 149 GLY D O   
7563 N  N   . SER D 150 ? 0.1407 0.0102 0.2187 0.0227  -0.0275 -0.0008 150 SER D N   
7564 C  CA  . SER D 150 ? 0.0851 0.0478 0.2143 0.0532  -0.0035 0.0253  150 SER D CA  
7565 C  C   . SER D 150 ? 0.1542 0.0143 0.1752 0.0331  -0.0085 -0.0115 150 SER D C   
7566 O  O   . SER D 150 ? 0.2109 0.0498 0.1794 0.0089  -0.0478 -0.0262 150 SER D O   
7567 C  CB  . SER D 150 ? 0.1327 0.0203 0.2515 0.0395  0.0174  0.0250  150 SER D CB  
7568 O  OG  . SER D 150 ? 0.1461 0.0156 0.2607 0.0357  -0.0070 0.0045  150 SER D OG  
7569 N  N   . PHE D 151 ? 0.2235 0.0167 0.1940 0.0447  -0.0282 0.0085  151 PHE D N   
7570 C  CA  . PHE D 151 ? 0.1992 0.0329 0.1833 0.0655  -0.0437 0.0118  151 PHE D CA  
7571 C  C   . PHE D 151 ? 0.1777 0.0135 0.1680 0.0211  -0.0447 -0.0317 151 PHE D C   
7572 O  O   . PHE D 151 ? 0.2327 0.0408 0.2351 0.0411  0.0227  -0.0052 151 PHE D O   
7573 C  CB  . PHE D 151 ? 0.1908 0.0080 0.2199 0.0178  -0.0482 -0.0058 151 PHE D CB  
7574 C  CG  . PHE D 151 ? 0.1803 0.0072 0.1861 0.0105  -0.0663 0.0016  151 PHE D CG  
7575 C  CD1 . PHE D 151 ? 0.2503 0.0101 0.2211 -0.0126 -0.0633 0.0166  151 PHE D CD1 
7576 C  CD2 . PHE D 151 ? 0.1807 0.0591 0.2632 0.0029  -0.0443 0.0132  151 PHE D CD2 
7577 C  CE1 . PHE D 151 ? 0.1963 0.0564 0.2302 0.0071  -0.0700 0.0106  151 PHE D CE1 
7578 C  CE2 . PHE D 151 ? 0.2069 0.0729 0.2590 0.0073  -0.0912 -0.0001 151 PHE D CE2 
7579 C  CZ  . PHE D 151 ? 0.2272 0.0223 0.2354 0.0271  -0.0829 -0.0146 151 PHE D CZ  
7580 N  N   . ASN D 152 ? 0.1826 0.0359 0.2119 0.0602  -0.0262 -0.0514 152 ASN D N   
7581 C  CA  . ASN D 152 ? 0.1431 0.0501 0.1855 0.0046  -0.0244 -0.0204 152 ASN D CA  
7582 C  C   . ASN D 152 ? 0.1733 0.0080 0.2525 -0.0129 -0.0675 -0.0070 152 ASN D C   
7583 O  O   . ASN D 152 ? 0.1611 0.0087 0.2337 0.0010  -0.0047 -0.0232 152 ASN D O   
7584 C  CB  . ASN D 152 ? 0.1247 0.0383 0.2013 -0.0060 -0.0218 -0.0243 152 ASN D CB  
7585 C  CG  . ASN D 152 ? 0.1427 0.0261 0.2225 0.0042  -0.0049 -0.0227 152 ASN D CG  
7586 O  OD1 . ASN D 152 ? 0.1562 0.0074 0.2235 0.0130  -0.0206 -0.0012 152 ASN D OD1 
7587 N  ND2 . ASN D 152 ? 0.1814 0.0065 0.2522 -0.0029 -0.0301 -0.0057 152 ASN D ND2 
7588 N  N   . PRO D 153 ? 0.1828 0.0131 0.2425 -0.0316 -0.0601 -0.0047 153 PRO D N   
7589 C  CA  . PRO D 153 ? 0.1280 0.0819 0.2081 -0.0111 -0.0626 -0.0649 153 PRO D CA  
7590 C  C   . PRO D 153 ? 0.1804 0.0272 0.2354 -0.0182 -0.0359 -0.0259 153 PRO D C   
7591 O  O   . PRO D 153 ? 0.2157 0.0495 0.2461 0.0096  -0.0299 -0.0145 153 PRO D O   
7592 C  CB  . PRO D 153 ? 0.1602 0.0311 0.2833 -0.0061 -0.0424 -0.0356 153 PRO D CB  
7593 C  CG  . PRO D 153 ? 0.1672 0.0199 0.4012 -0.0114 -0.0600 0.0003  153 PRO D CG  
7594 C  CD  . PRO D 153 ? 0.1736 0.0179 0.3701 -0.0397 -0.0762 -0.0081 153 PRO D CD  
7595 N  N   . SER D 154 ? 0.1421 0.0401 0.1951 0.0059  -0.0245 -0.0300 154 SER D N   
7596 C  CA  . SER D 154 ? 0.1740 0.0550 0.2303 -0.0082 -0.0183 -0.0512 154 SER D CA  
7597 C  C   . SER D 154 ? 0.1282 0.0206 0.2537 0.0337  -0.0009 -0.0072 154 SER D C   
7598 O  O   . SER D 154 ? 0.1597 0.0156 0.2358 0.0334  -0.0141 -0.0190 154 SER D O   
7599 C  CB  . SER D 154 ? 0.1634 0.0568 0.2243 -0.0160 0.0253  -0.0712 154 SER D CB  
7600 O  OG  . SER D 154 ? 0.1930 0.0545 0.2827 -0.0298 0.0134  -0.0208 154 SER D OG  
7601 N  N   . TYR D 155 ? 0.1305 0.0269 0.2240 -0.0065 -0.0239 -0.0221 155 TYR D N   
7602 C  CA  . TYR D 155 ? 0.1151 0.0340 0.1690 0.0040  -0.0299 -0.0044 155 TYR D CA  
7603 C  C   . TYR D 155 ? 0.1598 0.0070 0.1789 0.0105  -0.0799 -0.0046 155 TYR D C   
7604 O  O   . TYR D 155 ? 0.1623 0.0082 0.2102 0.0155  -0.0187 -0.0097 155 TYR D O   
7605 C  CB  . TYR D 155 ? 0.1330 0.0105 0.1951 0.0224  -0.0433 -0.0131 155 TYR D CB  
7606 C  CG  . TYR D 155 ? 0.1387 0.0232 0.1747 -0.0107 -0.0143 0.0052  155 TYR D CG  
7607 C  CD1 . TYR D 155 ? 0.1468 0.0109 0.1689 0.0253  -0.0029 -0.0006 155 TYR D CD1 
7608 C  CD2 . TYR D 155 ? 0.1658 0.0201 0.2067 0.0057  -0.0401 -0.0259 155 TYR D CD2 
7609 C  CE1 . TYR D 155 ? 0.1615 0.0083 0.1628 -0.0141 -0.0136 0.0118  155 TYR D CE1 
7610 C  CE2 . TYR D 155 ? 0.1474 0.0394 0.1850 0.0104  -0.0054 0.0006  155 TYR D CE2 
7611 C  CZ  . TYR D 155 ? 0.1517 0.0084 0.1953 0.0030  0.0048  -0.0193 155 TYR D CZ  
7612 O  OH  . TYR D 155 ? 0.1782 0.0162 0.2145 -0.0049 -0.0088 -0.0210 155 TYR D OH  
7613 N  N   . ASP D 156 ? 0.2180 0.0188 0.1519 0.0149  -0.0141 -0.0416 156 ASP D N   
7614 C  CA  . ASP D 156 ? 0.2133 0.0331 0.1588 0.0440  -0.0348 -0.0578 156 ASP D CA  
7615 C  C   . ASP D 156 ? 0.1731 0.0370 0.1796 0.0271  -0.0362 -0.0559 156 ASP D C   
7616 O  O   . ASP D 156 ? 0.1830 0.0714 0.1974 0.0196  -0.0493 -0.0132 156 ASP D O   
7617 C  CB  . ASP D 156 ? 0.2408 0.0278 0.1816 0.0331  -0.0217 -0.0571 156 ASP D CB  
7618 C  CG  . ASP D 156 ? 0.2615 0.0653 0.1876 0.0367  -0.0366 -0.0409 156 ASP D CG  
7619 O  OD1 . ASP D 156 ? 0.2382 0.0282 0.2459 0.0442  -0.0334 -0.0100 156 ASP D OD1 
7620 O  OD2 . ASP D 156 ? 0.3153 0.1477 0.2203 -0.0527 -0.0986 0.0278  156 ASP D OD2 
7621 N  N   . LYS D 157 ? 0.1703 0.0407 0.2248 0.0323  -0.0029 -0.0079 157 LYS D N   
7622 C  CA  . LYS D 157 ? 0.1607 0.0216 0.2630 0.0203  -0.0189 -0.0245 157 LYS D CA  
7623 C  C   . LYS D 157 ? 0.1535 0.0117 0.3013 0.0262  -0.0165 0.0111  157 LYS D C   
7624 O  O   . LYS D 157 ? 0.2059 0.0356 0.4312 0.0441  -0.0722 0.0377  157 LYS D O   
7625 C  CB  . LYS D 157 ? 0.1577 0.0125 0.3040 0.0303  -0.0070 -0.0072 157 LYS D CB  
7626 C  CG  . LYS D 157 ? 0.2667 0.0218 0.3062 -0.0353 0.0205  0.0015  157 LYS D CG  
7627 C  CD  . LYS D 157 ? 0.1895 0.0322 0.3502 0.0013  -0.0116 -0.0125 157 LYS D CD  
7628 C  CE  . LYS D 157 ? 0.1868 0.0435 0.3147 -0.0222 -0.0214 0.0249  157 LYS D CE  
7629 N  NZ  . LYS D 157 ? 0.1726 0.1270 0.3709 -0.0079 -0.0058 0.0944  157 LYS D NZ  
7630 N  N   . ILE D 158 ? 0.1773 0.0278 0.2339 -0.0130 -0.0279 0.0108  158 ILE D N   
7631 C  CA  . ILE D 158 ? 0.1584 0.0302 0.1981 -0.0074 -0.0153 0.0332  158 ILE D CA  
7632 C  C   . ILE D 158 ? 0.1177 0.0365 0.2228 0.0193  -0.0033 0.0381  158 ILE D C   
7633 O  O   . ILE D 158 ? 0.2240 0.0338 0.1855 0.0066  -0.0187 0.0222  158 ILE D O   
7634 C  CB  . ILE D 158 ? 0.2066 0.0329 0.1804 -0.0588 -0.0091 -0.0135 158 ILE D CB  
7635 C  CG1 . ILE D 158 ? 0.2555 0.0529 0.2055 -0.0559 0.0298  0.0288  158 ILE D CG1 
7636 C  CG2 . ILE D 158 ? 0.2352 0.0113 0.2537 -0.0335 -0.0211 0.0064  158 ILE D CG2 
7637 C  CD1 . ILE D 158 ? 0.3443 0.1153 0.1758 -0.0635 0.0488  -0.0052 158 ILE D CD1 
7638 N  N   . PHE D 159 ? 0.1610 0.0383 0.1755 0.0186  -0.0074 -0.0203 159 PHE D N   
7639 C  CA  . PHE D 159 ? 0.1514 0.0335 0.1833 0.0407  -0.0138 0.0159  159 PHE D CA  
7640 C  C   . PHE D 159 ? 0.1348 0.0872 0.1805 0.0108  -0.0263 0.0017  159 PHE D C   
7641 O  O   . PHE D 159 ? 0.1729 0.0668 0.2268 0.0080  0.0106  0.0150  159 PHE D O   
7642 C  CB  . PHE D 159 ? 0.1631 0.0130 0.1991 0.0245  -0.0253 -0.0274 159 PHE D CB  
7643 C  CG  . PHE D 159 ? 0.1642 0.0385 0.2066 -0.0074 -0.0255 0.0172  159 PHE D CG  
7644 C  CD1 . PHE D 159 ? 0.1622 0.1004 0.2060 0.0232  -0.0489 -0.0061 159 PHE D CD1 
7645 C  CD2 . PHE D 159 ? 0.1456 0.0542 0.2200 0.0254  0.0055  0.0254  159 PHE D CD2 
7646 C  CE1 . PHE D 159 ? 0.1538 0.0311 0.2175 0.0051  -0.0493 -0.0080 159 PHE D CE1 
7647 C  CE2 . PHE D 159 ? 0.1721 0.0821 0.1610 0.0094  0.0150  -0.0486 159 PHE D CE2 
7648 C  CZ  . PHE D 159 ? 0.1636 0.0192 0.2180 0.0008  -0.0370 -0.0218 159 PHE D CZ  
7649 N  N   . SER D 160 ? 0.1402 0.1424 0.1696 0.0084  -0.0406 -0.0307 160 SER D N   
7650 C  CA  . SER D 160 ? 0.1464 0.1513 0.1733 0.0258  -0.0440 -0.0347 160 SER D CA  
7651 C  C   . SER D 160 ? 0.1426 0.1866 0.1636 0.0370  -0.0446 -0.0087 160 SER D C   
7652 O  O   . SER D 160 ? 0.2279 0.2530 0.1728 0.0291  -0.0851 0.0106  160 SER D O   
7653 C  CB  . SER D 160 ? 0.1797 0.2253 0.1808 -0.0065 -0.0542 -0.0721 160 SER D CB  
7654 O  OG  . SER D 160 ? 0.2095 0.1409 0.2606 -0.0022 -0.0135 -0.0394 160 SER D OG  
7655 N  N   . HIS D 161 ? 0.1557 0.1395 0.1742 0.0440  -0.0233 0.0150  161 HIS D N   
7656 C  CA  . HIS D 161 ? 0.1671 0.1347 0.2364 0.0641  -0.0284 0.0174  161 HIS D CA  
7657 C  C   . HIS D 161 ? 0.1629 0.1466 0.1654 0.0464  -0.0178 0.0556  161 HIS D C   
7658 O  O   . HIS D 161 ? 0.2110 0.1660 0.2372 0.0653  0.0160  0.0882  161 HIS D O   
7659 C  CB  . HIS D 161 ? 0.1507 0.1261 0.2164 0.0322  -0.0262 0.0250  161 HIS D CB  
7660 C  CG  . HIS D 161 ? 0.1606 0.1981 0.2195 0.0137  -0.0319 -0.0409 161 HIS D CG  
7661 N  ND1 . HIS D 161 ? 0.2408 0.2031 0.3064 0.0200  -0.0759 0.0111  161 HIS D ND1 
7662 C  CD2 . HIS D 161 ? 0.1761 0.1286 0.3440 0.0098  -0.0232 -0.0420 161 HIS D CD2 
7663 C  CE1 . HIS D 161 ? 0.2660 0.2733 0.3601 -0.0409 -0.0779 0.0376  161 HIS D CE1 
7664 N  NE2 . HIS D 161 ? 0.2178 0.1729 0.4320 0.0237  -0.0706 -0.0253 161 HIS D NE2 
7665 N  N   . LEU D 162 ? 0.1286 0.2495 0.2637 0.0414  0.0005  0.0678  162 LEU D N   
7666 C  CA  . LEU D 162 ? 0.1439 0.2392 0.2841 0.0252  -0.0495 0.1771  162 LEU D CA  
7667 C  C   . LEU D 162 ? 0.1439 0.0835 0.2559 0.0103  -0.0491 0.1137  162 LEU D C   
7668 O  O   . LEU D 162 ? 0.1714 0.1099 0.3269 -0.0069 -0.0341 0.1095  162 LEU D O   
7669 C  CB  . LEU D 162 ? 0.1595 0.2085 0.2620 0.0299  -0.0955 0.0895  162 LEU D CB  
7670 C  CG  . LEU D 162 ? 0.2520 0.3420 0.3093 -0.0522 -0.1663 0.1850  162 LEU D CG  
7671 C  CD1 . LEU D 162 ? 0.2523 0.4110 0.3996 -0.0267 -0.1367 0.2079  162 LEU D CD1 
7672 C  CD2 . LEU D 162 ? 0.2701 0.3170 0.3564 -0.0735 -0.1373 0.1867  162 LEU D CD2 
7673 N  N   . GLN D 163 ? 0.1828 0.2378 0.2881 0.0411  -0.0003 0.0439  163 GLN D N   
7674 C  CA  . GLN D 163 ? 0.1638 0.2462 0.2390 0.0784  0.0011  0.0283  163 GLN D CA  
7675 C  C   . GLN D 163 ? 0.1280 0.2424 0.2522 0.0603  -0.0270 0.0999  163 GLN D C   
7676 O  O   . GLN D 163 ? 0.2703 0.2306 0.2672 0.0760  0.0706  0.0837  163 GLN D O   
7677 C  CB  . GLN D 163 ? 0.2103 0.2333 0.3416 0.0084  0.0142  -0.0284 163 GLN D CB  
7678 C  CG  . GLN D 163 ? 0.2915 0.5166 0.2954 -0.0262 -0.1383 -0.1267 163 GLN D CG  
7679 C  CD  . GLN D 163 ? 0.3596 0.4117 0.4023 -0.0696 -0.0810 -0.1884 163 GLN D CD  
7680 O  OE1 . GLN D 163 ? 0.6026 0.4810 0.4192 -0.1042 -0.0693 -0.1305 163 GLN D OE1 
7681 N  NE2 . GLN D 163 ? 0.2090 0.4836 0.3935 0.0005  -0.0228 0.0979  163 GLN D NE2 
7682 N  N   . HIS D 164 ? 0.1090 0.2307 0.2351 0.0230  -0.0457 0.0522  164 HIS D N   
7683 C  CA  . HIS D 164 ? 0.1478 0.2218 0.2242 0.0095  -0.0597 0.0695  164 HIS D CA  
7684 C  C   . HIS D 164 ? 0.1550 0.1509 0.1790 0.0500  -0.0212 0.0633  164 HIS D C   
7685 O  O   . HIS D 164 ? 0.1963 0.1518 0.2295 0.0551  -0.0322 0.0449  164 HIS D O   
7686 C  CB  . HIS D 164 ? 0.1324 0.2054 0.2354 0.0366  -0.0705 0.0319  164 HIS D CB  
7687 C  CG  . HIS D 164 ? 0.1502 0.2444 0.2811 -0.0106 -0.0741 0.0146  164 HIS D CG  
7688 N  ND1 . HIS D 164 ? 0.2683 0.2547 0.2684 -0.0054 -0.0892 -0.0163 164 HIS D ND1 
7689 C  CD2 . HIS D 164 ? 0.2260 0.1969 0.2976 0.0430  -0.0851 0.0293  164 HIS D CD2 
7690 C  CE1 . HIS D 164 ? 0.3536 0.2604 0.2972 -0.0036 -0.0717 -0.0517 164 HIS D CE1 
7691 N  NE2 . HIS D 164 ? 0.2490 0.2772 0.3347 0.0234  -0.0719 -0.0368 164 HIS D NE2 
7692 N  N   . VAL D 165 ? 0.1503 0.1873 0.1675 -0.0051 -0.0446 0.0571  165 VAL D N   
7693 C  CA  . VAL D 165 ? 0.1615 0.1737 0.1920 -0.0001 -0.0400 0.0603  165 VAL D CA  
7694 C  C   . VAL D 165 ? 0.1805 0.1645 0.1819 0.0019  -0.0091 0.0571  165 VAL D C   
7695 O  O   . VAL D 165 ? 0.1729 0.1862 0.1753 0.0017  -0.0237 0.0379  165 VAL D O   
7696 C  CB  . VAL D 165 ? 0.2097 0.1891 0.2049 0.0154  -0.0017 0.0625  165 VAL D CB  
7697 C  CG1 . VAL D 165 ? 0.1821 0.3045 0.2406 -0.0118 -0.0293 0.0408  165 VAL D CG1 
7698 C  CG2 . VAL D 165 ? 0.2099 0.1909 0.1994 -0.0211 0.0003  0.0937  165 VAL D CG2 
7699 N  N   . LYS D 166 ? 0.2207 0.1284 0.1776 -0.0062 -0.0138 0.0455  166 LYS D N   
7700 C  CA  . LYS D 166 ? 0.2282 0.0922 0.1485 -0.0236 0.0046  0.0070  166 LYS D CA  
7701 C  C   . LYS D 166 ? 0.1688 0.1042 0.1277 0.0071  -0.0137 0.0065  166 LYS D C   
7702 O  O   . LYS D 166 ? 0.1855 0.1105 0.1848 0.0373  -0.0324 0.0320  166 LYS D O   
7703 C  CB  . LYS D 166 ? 0.2397 0.1410 0.1645 -0.0083 -0.0137 -0.0581 166 LYS D CB  
7704 C  CG  . LYS D 166 ? 0.2822 0.1783 0.1672 0.0245  0.0359  -0.0534 166 LYS D CG  
7705 C  CD  . LYS D 166 ? 0.3800 0.0859 0.1807 0.0289  0.0322  -0.0387 166 LYS D CD  
7706 C  CE  . LYS D 166 ? 0.4549 0.2124 0.2447 0.1312  0.0785  -0.0051 166 LYS D CE  
7707 N  NZ  . LYS D 166 ? 0.5014 0.3853 0.2416 0.1599  0.0536  -0.0732 166 LYS D NZ  
7708 N  N   . TYR D 167 ? 0.2040 0.0947 0.1600 0.0013  -0.0013 0.0184  167 TYR D N   
7709 C  CA  . TYR D 167 ? 0.1981 0.1162 0.1685 -0.0053 0.0108  0.0029  167 TYR D CA  
7710 C  C   . TYR D 167 ? 0.2058 0.0760 0.1825 -0.0376 0.0292  -0.0063 167 TYR D C   
7711 O  O   . TYR D 167 ? 0.1769 0.0927 0.2090 -0.0113 0.0082  -0.0049 167 TYR D O   
7712 C  CB  . TYR D 167 ? 0.2754 0.0381 0.2130 0.0205  0.0249  0.0059  167 TYR D CB  
7713 C  CG  . TYR D 167 ? 0.2989 0.1211 0.1775 0.0752  0.0316  0.0456  167 TYR D CG  
7714 C  CD1 . TYR D 167 ? 0.2893 0.0978 0.2066 0.0286  0.0580  0.0381  167 TYR D CD1 
7715 C  CD2 . TYR D 167 ? 0.3787 0.1681 0.1385 0.0361  0.0396  0.0440  167 TYR D CD2 
7716 C  CE1 . TYR D 167 ? 0.3398 0.0875 0.2307 0.0702  0.0847  0.0688  167 TYR D CE1 
7717 C  CE2 . TYR D 167 ? 0.3708 0.2203 0.1564 0.1324  0.0275  0.0576  167 TYR D CE2 
7718 C  CZ  . TYR D 167 ? 0.3600 0.2504 0.2578 0.0653  0.0602  -0.0077 167 TYR D CZ  
7719 O  OH  . TYR D 167 ? 0.5959 0.2611 0.3000 0.2088  0.1124  0.0524  167 TYR D OH  
7720 N  N   . LYS D 168 ? 0.2163 0.0703 0.2067 -0.0131 -0.0100 0.0145  168 LYS D N   
7721 C  CA  . LYS D 168 ? 0.2515 0.2055 0.2288 -0.0802 -0.0031 -0.0683 168 LYS D CA  
7722 C  C   . LYS D 168 ? 0.2281 0.2981 0.2901 -0.0151 0.0454  -0.0678 168 LYS D C   
7723 O  O   . LYS D 168 ? 0.3005 0.0562 0.3703 0.0124  0.0559  -0.0417 168 LYS D O   
7724 C  CB  . LYS D 168 ? 0.2252 0.1589 0.3095 -0.0578 0.0374  -0.1211 168 LYS D CB  
7725 C  CG  . LYS D 168 ? 0.3434 0.3305 0.3644 -0.1317 0.0266  -0.2339 168 LYS D CG  
7726 C  CD  . LYS D 168 ? 0.3173 0.3172 0.4166 -0.0820 -0.0381 -0.2692 168 LYS D CD  
7727 C  CE  . LYS D 168 ? 0.4142 0.4154 0.5204 -0.1011 0.0447  -0.3864 168 LYS D CE  
7728 N  NZ  . LYS D 168 ? 0.4515 0.7041 0.5814 -0.2412 0.0743  -0.3201 168 LYS D NZ  
7729 N  N   . GLY D 169 ? 0.2484 0.3426 0.3294 -0.0590 0.0804  -0.1759 169 GLY D N   
7730 C  CA  . GLY D 169 ? 0.2437 0.3231 0.4673 -0.0738 0.0539  -0.1680 169 GLY D CA  
7731 C  C   . GLY D 169 ? 0.2128 0.2489 0.3534 0.0055  0.0532  -0.1265 169 GLY D C   
7732 O  O   . GLY D 169 ? 0.2328 0.3481 0.5396 0.0718  0.0111  -0.1429 169 GLY D O   
7733 N  N   . GLN D 170 ? 0.2102 0.2054 0.1941 0.0256  0.0281  -0.0591 170 GLN D N   
7734 C  CA  . GLN D 170 ? 0.1758 0.2688 0.2218 -0.0095 0.0430  0.0105  170 GLN D CA  
7735 C  C   . GLN D 170 ? 0.1733 0.1710 0.2202 0.0362  0.0072  0.0541  170 GLN D C   
7736 O  O   . GLN D 170 ? 0.2543 0.3299 0.1733 0.0228  -0.0182 0.0326  170 GLN D O   
7737 C  CB  . GLN D 170 ? 0.1926 0.1559 0.2178 0.0663  0.0001  0.0604  170 GLN D CB  
7738 C  CG  . GLN D 170 ? 0.2437 0.2691 0.1894 0.0738  0.0485  0.0455  170 GLN D CG  
7739 C  CD  . GLN D 170 ? 0.2040 0.2614 0.1780 0.1025  0.0046  0.0644  170 GLN D CD  
7740 O  OE1 . GLN D 170 ? 0.2376 0.2148 0.1816 0.0717  -0.0346 0.0480  170 GLN D OE1 
7741 N  NE2 . GLN D 170 ? 0.3287 0.2285 0.1884 0.1174  0.0009  0.0842  170 GLN D NE2 
7742 N  N   . GLU D 171 ? 0.1715 0.2479 0.2313 0.0628  0.0160  0.0222  171 GLU D N   
7743 C  CA  . GLU D 171 ? 0.2263 0.1747 0.2144 0.0673  0.0352  0.0414  171 GLU D CA  
7744 C  C   . GLU D 171 ? 0.2020 0.3043 0.1561 -0.0048 0.0540  0.0617  171 GLU D C   
7745 O  O   . GLU D 171 ? 0.2281 0.3078 0.2106 -0.0046 -0.0179 0.1442  171 GLU D O   
7746 C  CB  . GLU D 171 ? 0.2691 0.2671 0.3542 0.0190  0.1582  -0.0536 171 GLU D CB  
7747 C  CG  . GLU D 171 ? 0.3859 0.2753 0.4548 0.0306  0.0146  -0.0013 171 GLU D CG  
7748 C  CD  . GLU D 171 ? 0.4025 0.3222 0.5256 -0.0309 0.0600  -0.0882 171 GLU D CD  
7749 O  OE1 . GLU D 171 ? 0.4714 0.1690 0.4656 0.0299  0.1069  0.0801  171 GLU D OE1 
7750 O  OE2 . GLU D 171 ? 0.5942 0.3037 0.5105 -0.0990 0.0367  -0.0688 171 GLU D OE2 
7751 N  N   . ALA D 172 ? 0.1635 0.2647 0.1719 -0.0193 -0.0110 0.0690  172 ALA D N   
7752 C  CA  . ALA D 172 ? 0.2288 0.3212 0.1456 -0.0314 -0.0104 0.0282  172 ALA D CA  
7753 C  C   . ALA D 172 ? 0.1634 0.2870 0.1999 0.0524  0.0143  0.0402  172 ALA D C   
7754 O  O   . ALA D 172 ? 0.2049 0.3987 0.1862 -0.0394 0.0088  0.0612  172 ALA D O   
7755 C  CB  . ALA D 172 ? 0.2087 0.3392 0.1836 -0.0558 0.0161  -0.0003 172 ALA D CB  
7756 N  N   . PHE D 173 ? 0.1837 0.3060 0.1882 0.0254  -0.0134 0.0776  173 PHE D N   
7757 C  CA  . PHE D 173 ? 0.2168 0.1862 0.2175 0.0145  0.0179  0.0570  173 PHE D CA  
7758 C  C   . PHE D 173 ? 0.1744 0.1823 0.2227 -0.0527 -0.0346 0.0134  173 PHE D C   
7759 O  O   . PHE D 173 ? 0.2806 0.4580 0.2584 -0.0220 0.0124  -0.1031 173 PHE D O   
7760 C  CB  . PHE D 173 ? 0.1690 0.2582 0.2944 -0.0203 -0.0207 0.0478  173 PHE D CB  
7761 C  CG  . PHE D 173 ? 0.1866 0.2333 0.3101 0.0086  0.0454  0.0870  173 PHE D CG  
7762 C  CD1 . PHE D 173 ? 0.2460 0.2509 0.3193 0.0251  -0.0441 0.0458  173 PHE D CD1 
7763 C  CD2 . PHE D 173 ? 0.3459 0.2832 0.3909 0.0010  0.0134  0.1465  173 PHE D CD2 
7764 C  CE1 . PHE D 173 ? 0.3053 0.2740 0.4239 0.1340  0.0641  0.0759  173 PHE D CE1 
7765 C  CE2 . PHE D 173 ? 0.4701 0.3361 0.4257 -0.0089 0.0642  0.0993  173 PHE D CE2 
7766 C  CZ  . PHE D 173 ? 0.3653 0.2078 0.4117 0.0238  -0.0111 0.0522  173 PHE D CZ  
7767 N  N   . VAL D 174 ? 0.1999 0.1640 0.2321 -0.0135 0.0249  0.0255  174 VAL D N   
7768 C  CA  . VAL D 174 ? 0.1692 0.1280 0.2590 -0.0514 -0.0287 -0.0289 174 VAL D CA  
7769 C  C   . VAL D 174 ? 0.1503 0.1772 0.2767 0.0207  -0.0170 -0.0446 174 VAL D C   
7770 O  O   . VAL D 174 ? 0.1812 0.1241 0.2773 0.0166  0.0189  -0.0234 174 VAL D O   
7771 C  CB  . VAL D 174 ? 0.1628 0.0911 0.3421 0.0345  0.0000  -0.0309 174 VAL D CB  
7772 C  CG1 . VAL D 174 ? 0.1683 0.1216 0.2840 0.0204  0.0018  0.0453  174 VAL D CG1 
7773 C  CG2 . VAL D 174 ? 0.1761 0.1679 0.3833 0.0074  -0.0151 -0.0100 174 VAL D CG2 
7774 N  N   . PRO D 175 ? 0.1550 0.0942 0.2833 -0.0075 0.0356  0.0176  175 PRO D N   
7775 C  CA  . PRO D 175 ? 0.1567 0.1126 0.2010 -0.0089 0.0116  0.0005  175 PRO D CA  
7776 C  C   . PRO D 175 ? 0.2010 0.0947 0.2210 0.0151  0.0115  0.0231  175 PRO D C   
7777 O  O   . PRO D 175 ? 0.2216 0.0617 0.2507 0.0244  -0.0062 0.0345  175 PRO D O   
7778 C  CB  . PRO D 175 ? 0.2773 0.1354 0.2295 -0.0251 0.0237  -0.0413 175 PRO D CB  
7779 C  CG  . PRO D 175 ? 0.1821 0.2909 0.2444 -0.0703 -0.0011 0.0108  175 PRO D CG  
7780 C  CD  . PRO D 175 ? 0.1433 0.1786 0.2728 -0.0221 0.0145  -0.0020 175 PRO D CD  
7781 N  N   . GLY D 176 ? 0.1956 0.0838 0.2049 0.0042  0.0208  0.0646  176 GLY D N   
7782 C  CA  . GLY D 176 ? 0.2189 0.0352 0.2127 0.0294  0.0076  0.0505  176 GLY D CA  
7783 C  C   . GLY D 176 ? 0.1762 0.0348 0.2350 0.0216  0.0133  0.0591  176 GLY D C   
7784 O  O   . GLY D 176 ? 0.1963 0.1518 0.2664 0.0129  -0.0397 0.0614  176 GLY D O   
7785 N  N   . PHE D 177 ? 0.1815 0.0088 0.2728 0.0103  -0.0364 0.0177  177 PHE D N   
7786 C  CA  . PHE D 177 ? 0.1543 0.0261 0.2460 0.0182  -0.0048 0.0643  177 PHE D CA  
7787 C  C   . PHE D 177 ? 0.1360 0.0501 0.2289 -0.0245 -0.0334 0.0352  177 PHE D C   
7788 O  O   . PHE D 177 ? 0.1643 0.0621 0.2475 0.0021  -0.0358 0.0081  177 PHE D O   
7789 C  CB  . PHE D 177 ? 0.1898 0.1015 0.2888 -0.0055 0.0098  -0.0330 177 PHE D CB  
7790 C  CG  . PHE D 177 ? 0.1852 0.0274 0.2723 0.0108  -0.0497 0.0118  177 PHE D CG  
7791 C  CD1 . PHE D 177 ? 0.1561 0.0481 0.2342 0.0111  0.0271  -0.0434 177 PHE D CD1 
7792 C  CD2 . PHE D 177 ? 0.1670 0.0672 0.2232 0.0066  -0.0418 0.0003  177 PHE D CD2 
7793 C  CE1 . PHE D 177 ? 0.1471 0.1592 0.2418 0.0179  0.0298  -0.0179 177 PHE D CE1 
7794 C  CE2 . PHE D 177 ? 0.1683 0.1094 0.2541 0.0095  -0.0710 0.0066  177 PHE D CE2 
7795 C  CZ  . PHE D 177 ? 0.1744 0.1272 0.2657 0.0078  0.0140  -0.0080 177 PHE D CZ  
7796 N  N   . ASN D 178 ? 0.1302 0.0318 0.2363 0.0131  -0.0518 0.0230  178 ASN D N   
7797 C  CA  . ASN D 178 ? 0.1316 0.0518 0.2411 -0.0118 -0.0270 0.0343  178 ASN D CA  
7798 C  C   . ASN D 178 ? 0.1151 0.0704 0.1852 0.0033  -0.0027 -0.0388 178 ASN D C   
7799 O  O   . ASN D 178 ? 0.1362 0.0325 0.2350 0.0013  0.0135  -0.0122 178 ASN D O   
7800 C  CB  . ASN D 178 ? 0.1726 0.0346 0.3221 -0.0071 -0.0111 0.0428  178 ASN D CB  
7801 C  CG  . ASN D 178 ? 0.1621 0.0794 0.3243 -0.0536 -0.0311 -0.0010 178 ASN D CG  
7802 O  OD1 . ASN D 178 ? 0.1751 0.0442 0.2889 0.0042  0.0109  0.0131  178 ASN D OD1 
7803 N  ND2 . ASN D 178 ? 0.3440 0.0926 0.3958 -0.0441 -0.0252 0.0394  178 ASN D ND2 
7804 N  N   . ILE D 179 ? 0.1136 0.0514 0.2204 -0.0175 -0.0104 -0.0188 179 ILE D N   
7805 C  CA  . ILE D 179 ? 0.1124 0.0124 0.2114 -0.0206 -0.0124 -0.0181 179 ILE D CA  
7806 C  C   . ILE D 179 ? 0.1348 0.0499 0.2090 -0.0021 0.0027  0.0013  179 ILE D C   
7807 O  O   . ILE D 179 ? 0.1319 0.0318 0.1895 -0.0006 -0.0085 0.0016  179 ILE D O   
7808 C  CB  . ILE D 179 ? 0.1481 0.0084 0.2130 -0.0142 -0.0034 -0.0113 179 ILE D CB  
7809 C  CG1 . ILE D 179 ? 0.1611 0.0641 0.1948 0.0060  0.0001  0.0095  179 ILE D CG1 
7810 C  CG2 . ILE D 179 ? 0.1390 0.0105 0.2638 0.0223  -0.0003 0.0101  179 ILE D CG2 
7811 C  CD1 . ILE D 179 ? 0.1819 0.0602 0.2178 0.0139  0.0206  0.0017  179 ILE D CD1 
7812 N  N   A GLU D 180 ? 0.1483 0.0129 0.2184 0.0240  0.0062  0.0240  180 GLU D N   
7813 N  N   B GLU D 180 ? 0.1441 0.0097 0.2267 0.0209  0.0230  -0.0030 180 GLU D N   
7814 C  CA  A GLU D 180 ? 0.1981 0.0453 0.1907 0.0305  0.0025  0.0447  180 GLU D CA  
7815 C  CA  B GLU D 180 ? 0.1995 0.0399 0.1889 0.0272  0.0244  0.0139  180 GLU D CA  
7816 C  C   A GLU D 180 ? 0.1760 0.0434 0.2236 0.0075  0.0223  0.0254  180 GLU D C   
7817 C  C   B GLU D 180 ? 0.1779 0.0231 0.2162 -0.0020 0.0362  0.0011  180 GLU D C   
7818 O  O   A GLU D 180 ? 0.2293 0.0724 0.2496 0.0321  0.0035  0.0302  180 GLU D O   
7819 O  O   B GLU D 180 ? 0.1611 0.0365 0.2325 -0.0267 0.0345  0.0270  180 GLU D O   
7820 C  CB  A GLU D 180 ? 0.2246 0.0751 0.2615 0.0126  0.0269  0.1022  180 GLU D CB  
7821 C  CB  B GLU D 180 ? 0.2155 0.0758 0.2471 0.0403  0.0897  -0.0086 180 GLU D CB  
7822 C  CG  A GLU D 180 ? 0.1976 0.1524 0.2715 0.0583  0.0140  0.1014  180 GLU D CG  
7823 C  CG  B GLU D 180 ? 0.2170 0.1004 0.2343 0.0176  0.0988  -0.0175 180 GLU D CG  
7824 C  CD  A GLU D 180 ? 0.2274 0.1933 0.2345 0.0965  0.0257  0.0942  180 GLU D CD  
7825 C  CD  B GLU D 180 ? 0.2715 0.0152 0.3040 -0.0273 0.0880  0.0214  180 GLU D CD  
7826 O  OE1 A GLU D 180 ? 0.2331 0.1893 0.3286 0.1054  0.0185  0.1452  180 GLU D OE1 
7827 O  OE1 B GLU D 180 ? 0.3486 0.1164 0.3041 0.0031  0.0507  0.0613  180 GLU D OE1 
7828 O  OE2 A GLU D 180 ? 0.2526 0.2561 0.2531 -0.0013 0.0147  0.1725  180 GLU D OE2 
7829 O  OE2 B GLU D 180 ? 0.1902 0.0773 0.3229 -0.0593 0.0309  0.0244  180 GLU D OE2 
7830 N  N   . GLU D 181 ? 0.1391 0.0411 0.2266 -0.0067 0.0304  -0.0245 181 GLU D N   
7831 C  CA  . GLU D 181 ? 0.1230 0.0380 0.2170 0.0167  -0.0010 -0.0218 181 GLU D CA  
7832 C  C   . GLU D 181 ? 0.1236 0.0063 0.2188 -0.0007 0.0005  0.0030  181 GLU D C   
7833 O  O   . GLU D 181 ? 0.1283 0.0468 0.2358 0.0225  0.0278  -0.0058 181 GLU D O   
7834 C  CB  . GLU D 181 ? 0.1721 0.0433 0.2367 -0.0244 -0.0267 0.0170  181 GLU D CB  
7835 C  CG  . GLU D 181 ? 0.1546 0.0677 0.2573 -0.0024 -0.0370 -0.0280 181 GLU D CG  
7836 C  CD  . GLU D 181 ? 0.1693 0.0848 0.2412 -0.0586 -0.0383 -0.0385 181 GLU D CD  
7837 O  OE1 . GLU D 181 ? 0.1915 0.1166 0.2979 -0.0006 -0.0229 0.0473  181 GLU D OE1 
7838 O  OE2 . GLU D 181 ? 0.1704 0.1362 0.3066 -0.0467 -0.0374 0.0036  181 GLU D OE2 
7839 N  N   . LEU D 182 ? 0.1278 0.0104 0.1957 -0.0191 0.0092  0.0125  182 LEU D N   
7840 C  CA  . LEU D 182 ? 0.1043 0.0075 0.2076 0.0004  -0.0242 0.0149  182 LEU D CA  
7841 C  C   . LEU D 182 ? 0.1509 0.0083 0.1789 0.0135  -0.0051 -0.0115 182 LEU D C   
7842 O  O   . LEU D 182 ? 0.1543 0.0139 0.2178 0.0336  0.0143  0.0060  182 LEU D O   
7843 C  CB  . LEU D 182 ? 0.1670 0.0126 0.2072 -0.0168 -0.0326 0.0276  182 LEU D CB  
7844 C  CG  . LEU D 182 ? 0.1334 0.0102 0.1676 -0.0221 -0.0141 0.0039  182 LEU D CG  
7845 C  CD1 . LEU D 182 ? 0.1934 0.0098 0.2015 -0.0250 0.0074  0.0042  182 LEU D CD1 
7846 C  CD2 . LEU D 182 ? 0.1282 0.0296 0.1861 0.0232  -0.0201 -0.0140 182 LEU D CD2 
7847 N  N   . LEU D 183 ? 0.1816 0.0157 0.1930 0.0320  -0.0015 0.0253  183 LEU D N   
7848 C  CA  . LEU D 183 ? 0.1873 0.0226 0.1843 0.0306  -0.0176 0.0086  183 LEU D CA  
7849 C  C   . LEU D 183 ? 0.1485 0.0199 0.1823 0.0218  -0.0310 0.0210  183 LEU D C   
7850 O  O   . LEU D 183 ? 0.1600 0.0577 0.2260 -0.0154 -0.0186 0.0102  183 LEU D O   
7851 C  CB  . LEU D 183 ? 0.2268 0.0514 0.1979 0.0943  0.0000  0.0304  183 LEU D CB  
7852 C  CG  . LEU D 183 ? 0.2178 0.0206 0.2531 0.0400  0.0333  0.0369  183 LEU D CG  
7853 C  CD1 . LEU D 183 ? 0.3290 0.0871 0.2441 0.0522  0.0592  0.0362  183 LEU D CD1 
7854 C  CD2 . LEU D 183 ? 0.2548 0.1035 0.2615 -0.0319 0.0220  0.0079  183 LEU D CD2 
7855 N  N   . PRO D 184 ? 0.1635 0.0130 0.1812 0.0040  -0.0315 0.0324  184 PRO D N   
7856 C  CA  . PRO D 184 ? 0.1546 0.0259 0.2110 0.0320  -0.0104 0.0445  184 PRO D CA  
7857 C  C   . PRO D 184 ? 0.2117 0.0071 0.2336 -0.0026 0.0238  -0.0131 184 PRO D C   
7858 O  O   . PRO D 184 ? 0.2060 0.0151 0.2567 -0.0034 0.0209  -0.0078 184 PRO D O   
7859 C  CB  . PRO D 184 ? 0.1585 0.0671 0.1902 0.0201  -0.0058 -0.0365 184 PRO D CB  
7860 C  CG  . PRO D 184 ? 0.1925 0.0220 0.2227 0.0534  0.0077  -0.0059 184 PRO D CG  
7861 C  CD  . PRO D 184 ? 0.1329 0.0461 0.2010 -0.0009 -0.0334 0.0194  184 PRO D CD  
7862 N  N   . GLU D 185 ? 0.2386 0.0063 0.2444 -0.0007 0.0201  0.0034  185 GLU D N   
7863 C  CA  . GLU D 185 ? 0.2295 0.0348 0.2737 -0.0117 0.0255  0.0095  185 GLU D CA  
7864 C  C   . GLU D 185 ? 0.1710 0.0374 0.2697 -0.0161 0.0111  0.0281  185 GLU D C   
7865 O  O   . GLU D 185 ? 0.1639 0.0658 0.2609 -0.0059 -0.0081 0.0506  185 GLU D O   
7866 C  CB  . GLU D 185 ? 0.2469 0.0282 0.3817 -0.0083 0.0207  0.0124  185 GLU D CB  
7867 C  CG  . GLU D 185 ? 0.3629 0.0688 0.3603 -0.0106 0.0507  0.0150  185 GLU D CG  
7868 C  CD  . GLU D 185 ? 0.5459 0.0542 0.6439 -0.0110 0.0342  0.0641  185 GLU D CD  
7869 O  OE1 . GLU D 185 ? 0.6614 0.1442 0.7765 -0.0449 0.1543  -0.0137 185 GLU D OE1 
7870 O  OE2 . GLU D 185 ? 0.6496 0.2722 0.8142 -0.2157 -0.0326 0.0212  185 GLU D OE2 
7871 N  N   . ARG D 186 ? 0.2083 0.0217 0.2751 -0.0320 0.0178  0.0318  186 ARG D N   
7872 C  CA  . ARG D 186 ? 0.2038 0.0573 0.2712 -0.0466 0.0063  0.0121  186 ARG D CA  
7873 C  C   . ARG D 186 ? 0.1624 0.0206 0.2954 -0.0234 0.0487  0.0403  186 ARG D C   
7874 O  O   . ARG D 186 ? 0.1962 0.0562 0.2656 -0.0141 0.0203  0.0258  186 ARG D O   
7875 C  CB  . ARG D 186 ? 0.2843 0.0283 0.3177 -0.0206 0.0043  0.0326  186 ARG D CB  
7876 C  CG  . ARG D 186 ? 0.3107 0.0660 0.3983 -0.0693 -0.0585 0.0425  186 ARG D CG  
7877 C  CD  . ARG D 186 ? 0.4104 0.1381 0.3661 -0.0027 -0.0190 0.1333  186 ARG D CD  
7878 N  NE  . ARG D 186 ? 0.4916 0.0999 0.3213 -0.0377 0.0109  0.0322  186 ARG D NE  
7879 C  CZ  . ARG D 186 ? 0.6388 0.1577 0.4388 0.0512  0.0456  -0.0951 186 ARG D CZ  
7880 N  NH1 . ARG D 186 ? 0.6395 0.1930 0.4213 0.1234  -0.0322 0.0058  186 ARG D NH1 
7881 N  NH2 . ARG D 186 ? 0.6908 0.1409 0.4400 0.1226  0.0634  0.0047  186 ARG D NH2 
7882 N  N   . THR D 187 ? 0.2145 0.0402 0.2576 -0.0127 -0.0078 0.0528  187 THR D N   
7883 C  CA  . THR D 187 ? 0.1912 0.0346 0.2295 -0.0052 0.0234  0.0502  187 THR D CA  
7884 C  C   . THR D 187 ? 0.1622 0.1098 0.2261 -0.0775 -0.0136 0.0536  187 THR D C   
7885 O  O   . THR D 187 ? 0.1607 0.0514 0.2139 -0.0144 0.0154  0.0262  187 THR D O   
7886 C  CB  . THR D 187 ? 0.1614 0.1067 0.2250 -0.0057 -0.0119 0.0577  187 THR D CB  
7887 O  OG1 . THR D 187 ? 0.1780 0.0569 0.3317 0.0326  0.0222  0.0592  187 THR D OG1 
7888 C  CG2 . THR D 187 ? 0.2788 0.0839 0.2101 0.0089  -0.0081 0.0300  187 THR D CG2 
7889 N  N   . ALA D 188 ? 0.1883 0.0758 0.2149 -0.0072 0.0396  0.0423  188 ALA D N   
7890 C  CA  . ALA D 188 ? 0.1796 0.0688 0.2322 -0.0044 0.0277  0.0615  188 ALA D CA  
7891 C  C   . ALA D 188 ? 0.1798 0.0392 0.1934 -0.0290 0.0337  0.0410  188 ALA D C   
7892 O  O   . ALA D 188 ? 0.1974 0.0644 0.1938 0.0026  0.0102  0.0285  188 ALA D O   
7893 C  CB  . ALA D 188 ? 0.2242 0.1376 0.2450 -0.0854 0.0069  0.0672  188 ALA D CB  
7894 N  N   . GLU D 189 ? 0.1747 0.0405 0.2173 0.0122  0.0356  0.0558  189 GLU D N   
7895 C  CA  . GLU D 189 ? 0.1918 0.0064 0.2203 0.0003  0.0058  0.0045  189 GLU D CA  
7896 C  C   . GLU D 189 ? 0.1841 0.0294 0.1967 -0.0008 0.0274  0.0104  189 GLU D C   
7897 O  O   . GLU D 189 ? 0.1765 0.0186 0.2211 -0.0111 0.0339  0.0304  189 GLU D O   
7898 C  CB  . GLU D 189 ? 0.1860 0.0066 0.2303 -0.0004 0.0048  -0.0080 189 GLU D CB  
7899 C  CG  . GLU D 189 ? 0.1923 0.0462 0.3737 0.0034  0.0248  0.0749  189 GLU D CG  
7900 C  CD  . GLU D 189 ? 0.2320 0.0914 0.3295 -0.0005 0.0245  0.0207  189 GLU D CD  
7901 O  OE1 . GLU D 189 ? 0.2967 0.0211 0.4257 0.0166  0.0807  -0.0094 189 GLU D OE1 
7902 O  OE2 . GLU D 189 ? 0.2906 0.0747 0.4773 -0.0093 -0.0042 0.0916  189 GLU D OE2 
7903 N  N   . TYR D 190 ? 0.1840 0.0095 0.2172 0.0052  0.0129  0.0257  190 TYR D N   
7904 C  CA  . TYR D 190 ? 0.1775 0.0091 0.1944 0.0103  0.0344  0.0217  190 TYR D CA  
7905 C  C   . TYR D 190 ? 0.1829 0.0112 0.1616 0.0199  0.0292  0.0232  190 TYR D C   
7906 O  O   . TYR D 190 ? 0.2223 0.0139 0.1604 0.0265  0.0315  0.0295  190 TYR D O   
7907 C  CB  . TYR D 190 ? 0.1768 0.0189 0.1848 0.0223  0.0387  0.0381  190 TYR D CB  
7908 C  CG  . TYR D 190 ? 0.1852 0.0444 0.1632 -0.0108 0.0507  0.0462  190 TYR D CG  
7909 C  CD1 . TYR D 190 ? 0.1966 0.0162 0.2078 0.0080  0.0245  0.0445  190 TYR D CD1 
7910 C  CD2 . TYR D 190 ? 0.1775 0.0155 0.2036 0.0222  0.0483  0.0402  190 TYR D CD2 
7911 C  CE1 . TYR D 190 ? 0.2119 0.0251 0.2225 0.0306  0.0481  0.0610  190 TYR D CE1 
7912 C  CE2 . TYR D 190 ? 0.1930 0.0286 0.1517 0.0044  0.0234  0.0362  190 TYR D CE2 
7913 C  CZ  . TYR D 190 ? 0.2001 0.0221 0.1448 0.0252  0.0220  0.0226  190 TYR D CZ  
7914 O  OH  . TYR D 190 ? 0.2257 0.0499 0.1374 0.0243  0.0406  0.0435  190 TYR D OH  
7915 N  N   . TYR D 191 ? 0.1625 0.0496 0.1268 -0.0140 0.0397  -0.0076 191 TYR D N   
7916 C  CA  . TYR D 191 ? 0.1678 0.0119 0.1938 -0.0085 0.0049  0.0310  191 TYR D CA  
7917 C  C   . TYR D 191 ? 0.1758 0.0120 0.1909 0.0046  -0.0021 0.0271  191 TYR D C   
7918 O  O   . TYR D 191 ? 0.2207 0.0313 0.1385 0.0092  0.0060  0.0044  191 TYR D O   
7919 C  CB  . TYR D 191 ? 0.1629 0.0084 0.1609 0.0094  0.0030  -0.0155 191 TYR D CB  
7920 C  CG  . TYR D 191 ? 0.1694 0.0125 0.1241 0.0307  0.0126  0.0087  191 TYR D CG  
7921 C  CD1 . TYR D 191 ? 0.1489 0.0364 0.1294 0.0168  0.0121  0.0122  191 TYR D CD1 
7922 C  CD2 . TYR D 191 ? 0.1980 0.0117 0.1579 0.0301  -0.0109 -0.0114 191 TYR D CD2 
7923 C  CE1 . TYR D 191 ? 0.1984 0.0478 0.1553 0.0307  0.0294  -0.0015 191 TYR D CE1 
7924 C  CE2 . TYR D 191 ? 0.1743 0.0256 0.1768 0.0389  -0.0016 -0.0149 191 TYR D CE2 
7925 C  CZ  . TYR D 191 ? 0.1629 0.0268 0.2074 0.0284  -0.0073 -0.0177 191 TYR D CZ  
7926 O  OH  . TYR D 191 ? 0.2394 0.0311 0.2439 0.0475  0.0013  -0.0280 191 TYR D OH  
7927 N  N   . ARG D 192 ? 0.2212 0.0118 0.1663 0.0249  0.0262  0.0233  192 ARG D N   
7928 C  CA  . ARG D 192 ? 0.1916 0.0071 0.1449 -0.0048 0.0131  0.0095  192 ARG D CA  
7929 C  C   . ARG D 192 ? 0.1855 0.0259 0.0981 -0.0104 0.0044  0.0323  192 ARG D C   
7930 O  O   . ARG D 192 ? 0.2058 0.0100 0.1518 0.0075  -0.0175 0.0213  192 ARG D O   
7931 C  CB  . ARG D 192 ? 0.1843 0.0270 0.1941 0.0446  0.0429  0.0144  192 ARG D CB  
7932 C  CG  . ARG D 192 ? 0.2446 0.0147 0.2386 0.0358  0.0331  0.0310  192 ARG D CG  
7933 C  CD  . ARG D 192 ? 0.2415 0.0297 0.1905 0.0286  -0.0086 0.0178  192 ARG D CD  
7934 N  NE  . ARG D 192 ? 0.2133 0.0523 0.2565 0.0670  0.0089  -0.0059 192 ARG D NE  
7935 C  CZ  . ARG D 192 ? 0.2325 0.0812 0.1925 0.0562  0.0211  0.0625  192 ARG D CZ  
7936 N  NH1 . ARG D 192 ? 0.3413 0.1155 0.1951 0.1404  0.0284  0.0259  192 ARG D NH1 
7937 N  NH2 . ARG D 192 ? 0.2669 0.0783 0.2511 0.0836  -0.0116 0.0373  192 ARG D NH2 
7938 N  N   . TYR D 193 ? 0.1601 0.0115 0.1302 -0.0257 0.0320  0.0046  193 TYR D N   
7939 C  CA  . TYR D 193 ? 0.1431 0.0156 0.1194 0.0025  0.0004  0.0201  193 TYR D CA  
7940 C  C   . TYR D 193 ? 0.1656 0.0145 0.1223 0.0192  -0.0198 0.0030  193 TYR D C   
7941 O  O   . TYR D 193 ? 0.1896 0.0088 0.1525 0.0146  -0.0279 0.0113  193 TYR D O   
7942 C  CB  . TYR D 193 ? 0.1545 0.0868 0.1406 0.0038  0.0205  0.0318  193 TYR D CB  
7943 C  CG  . TYR D 193 ? 0.1311 0.0101 0.1262 0.0026  0.0112  0.0214  193 TYR D CG  
7944 C  CD1 . TYR D 193 ? 0.2237 0.0183 0.1445 0.0501  0.0142  -0.0038 193 TYR D CD1 
7945 C  CD2 . TYR D 193 ? 0.1811 0.0114 0.1475 -0.0294 0.0148  0.0022  193 TYR D CD2 
7946 C  CE1 . TYR D 193 ? 0.1734 0.0109 0.1687 0.0132  0.0311  0.0260  193 TYR D CE1 
7947 C  CE2 . TYR D 193 ? 0.1658 0.0533 0.1161 0.0325  0.0120  -0.0171 193 TYR D CE2 
7948 C  CZ  . TYR D 193 ? 0.1744 0.0067 0.1397 0.0049  0.0193  0.0068  193 TYR D CZ  
7949 O  OH  . TYR D 193 ? 0.1782 0.0172 0.1309 -0.0061 0.0153  -0.0059 193 TYR D OH  
7950 N  N   . ARG D 194 ? 0.2190 0.0104 0.1684 -0.0262 -0.0082 0.0127  194 ARG D N   
7951 C  CA  . ARG D 194 ? 0.2474 0.0119 0.1651 -0.0347 0.0035  0.0091  194 ARG D CA  
7952 C  C   . ARG D 194 ? 0.2202 0.0182 0.1558 -0.0409 -0.0382 0.0312  194 ARG D C   
7953 O  O   . ARG D 194 ? 0.2278 0.0264 0.2015 -0.0097 -0.0113 0.0088  194 ARG D O   
7954 C  CB  . ARG D 194 ? 0.2605 0.0776 0.1879 -0.0619 -0.0263 -0.0144 194 ARG D CB  
7955 C  CG  . ARG D 194 ? 0.3015 0.0959 0.2663 -0.0341 0.0319  0.0117  194 ARG D CG  
7956 C  CD  . ARG D 194 ? 0.2340 0.3427 0.3318 0.0172  -0.0145 0.0317  194 ARG D CD  
7957 N  NE  . ARG D 194 ? 0.4659 0.2168 0.3824 0.0694  0.1366  -0.0602 194 ARG D NE  
7958 C  CZ  . ARG D 194 ? 0.4730 0.2467 0.4362 0.0902  0.1636  -0.0732 194 ARG D CZ  
7959 N  NH1 . ARG D 194 ? 0.4249 0.1333 0.6224 -0.0178 0.1702  -0.0254 194 ARG D NH1 
7960 N  NH2 . ARG D 194 ? 0.5161 0.1908 0.4695 -0.0165 0.1656  -0.0981 194 ARG D NH2 
7961 N  N   . GLY D 195 ? 0.2073 0.0091 0.1155 0.0040  -0.0052 0.0117  195 GLY D N   
7962 C  CA  . GLY D 195 ? 0.2264 0.0110 0.1519 0.0025  0.0194  0.0260  195 GLY D CA  
7963 C  C   . GLY D 195 ? 0.2249 0.0079 0.1390 0.0152  -0.0065 0.0077  195 GLY D C   
7964 O  O   . GLY D 195 ? 0.2027 0.0177 0.1509 0.0273  0.0140  0.0085  195 GLY D O   
7965 N  N   . SER D 196 ? 0.2185 0.0104 0.1236 0.0223  -0.0280 0.0110  196 SER D N   
7966 C  CA  . SER D 196 ? 0.1958 0.0164 0.1255 0.0012  0.0015  0.0348  196 SER D CA  
7967 C  C   . SER D 196 ? 0.2243 0.0075 0.0958 0.0160  0.0243  0.0005  196 SER D C   
7968 O  O   . SER D 196 ? 0.1715 0.0079 0.1135 0.0094  -0.0055 -0.0108 196 SER D O   
7969 C  CB  . SER D 196 ? 0.1993 0.0070 0.1646 -0.0076 0.0202  0.0066  196 SER D CB  
7970 O  OG  . SER D 196 ? 0.1646 0.0081 0.1772 -0.0141 0.0027  -0.0098 196 SER D OG  
7971 N  N   . LEU D 197 ? 0.1790 0.0148 0.1265 -0.0107 0.0114  0.0297  197 LEU D N   
7972 C  CA  . LEU D 197 ? 0.1899 0.0173 0.1099 0.0054  0.0290  0.0335  197 LEU D CA  
7973 C  C   . LEU D 197 ? 0.1656 0.0429 0.1243 -0.0167 0.0140  0.0120  197 LEU D C   
7974 O  O   . LEU D 197 ? 0.1623 0.0067 0.1837 0.0017  0.0062  -0.0078 197 LEU D O   
7975 C  CB  . LEU D 197 ? 0.1912 0.0188 0.1755 0.0142  0.0090  0.0444  197 LEU D CB  
7976 C  CG  . LEU D 197 ? 0.1880 0.0088 0.1979 -0.0043 -0.0124 0.0217  197 LEU D CG  
7977 C  CD1 . LEU D 197 ? 0.3005 0.0651 0.1990 0.0608  0.0076  0.0452  197 LEU D CD1 
7978 C  CD2 . LEU D 197 ? 0.2716 0.0740 0.1958 0.0487  0.0153  0.0604  197 LEU D CD2 
7979 N  N   . THR D 198 ? 0.1304 0.0480 0.1130 0.0136  0.0104  0.0057  198 THR D N   
7980 C  CA  . THR D 198 ? 0.1467 0.0075 0.1428 -0.0125 0.0365  -0.0076 198 THR D CA  
7981 C  C   . THR D 198 ? 0.1502 0.0125 0.1211 -0.0036 0.0131  0.0006  198 THR D C   
7982 O  O   . THR D 198 ? 0.1368 0.0094 0.1791 -0.0168 0.0101  -0.0135 198 THR D O   
7983 C  CB  . THR D 198 ? 0.1276 0.0078 0.1352 -0.0134 -0.0134 0.0000  198 THR D CB  
7984 O  OG1 . THR D 198 ? 0.1420 0.0083 0.1540 -0.0140 -0.0202 0.0108  198 THR D OG1 
7985 C  CG2 . THR D 198 ? 0.1509 0.0086 0.1664 -0.0022 0.0208  0.0185  198 THR D CG2 
7986 N  N   . THR D 199 ? 0.1255 0.0274 0.1553 -0.0096 -0.0161 0.0232  199 THR D N   
7987 C  CA  . THR D 199 ? 0.1492 0.0207 0.1198 0.0046  -0.0054 0.0043  199 THR D CA  
7988 C  C   . THR D 199 ? 0.1534 0.0299 0.1101 0.0066  -0.0196 0.0023  199 THR D C   
7989 O  O   . THR D 199 ? 0.1897 0.0063 0.1425 -0.0010 0.0117  0.0009  199 THR D O   
7990 C  CB  . THR D 199 ? 0.1568 0.0092 0.1737 0.0022  -0.0270 -0.0218 199 THR D CB  
7991 O  OG1 . THR D 199 ? 0.1794 0.0101 0.2080 0.0006  0.0018  0.0062  199 THR D OG1 
7992 C  CG2 . THR D 199 ? 0.1476 0.0115 0.2225 -0.0122 -0.0133 -0.0285 199 THR D CG2 
7993 N  N   . PRO D 200 ? 0.1561 0.0104 0.1241 0.0242  -0.0092 -0.0069 200 PRO D N   
7994 C  CA  . PRO D 200 ? 0.1674 0.0102 0.1441 0.0019  0.0100  -0.0231 200 PRO D CA  
7995 C  C   . PRO D 200 ? 0.1834 0.0094 0.1441 0.0138  -0.0030 0.0096  200 PRO D C   
7996 O  O   . PRO D 200 ? 0.1812 0.0191 0.1527 0.0089  0.0099  0.0076  200 PRO D O   
7997 C  CB  . PRO D 200 ? 0.1735 0.0313 0.1639 -0.0131 0.0201  -0.0108 200 PRO D CB  
7998 C  CG  . PRO D 200 ? 0.1812 0.0106 0.1604 -0.0260 0.0192  -0.0104 200 PRO D CG  
7999 C  CD  . PRO D 200 ? 0.1736 0.0080 0.1444 -0.0160 0.0140  0.0029  200 PRO D CD  
8000 N  N   . PRO D 201 ? 0.1785 0.0148 0.1807 -0.0038 0.0212  -0.0113 201 PRO D N   
8001 C  CA  . PRO D 201 ? 0.2024 0.0253 0.1632 0.0308  0.0059  -0.0342 201 PRO D CA  
8002 C  C   . PRO D 201 ? 0.2159 0.0105 0.1703 -0.0278 0.0187  -0.0110 201 PRO D C   
8003 O  O   . PRO D 201 ? 0.2208 0.0083 0.1802 0.0093  0.0046  -0.0162 201 PRO D O   
8004 C  CB  . PRO D 201 ? 0.2542 0.0074 0.2280 0.0145  0.0423  -0.0050 201 PRO D CB  
8005 C  CG  . PRO D 201 ? 0.2733 0.0408 0.2636 -0.0133 0.0181  -0.0534 201 PRO D CG  
8006 C  CD  . PRO D 201 ? 0.1632 0.0304 0.2576 -0.0111 -0.0033 -0.0245 201 PRO D CD  
8007 N  N   . CYS D 202 ? 0.1693 0.0068 0.1816 0.0035  0.0210  0.0093  202 CYS D N   
8008 C  CA  . CYS D 202 ? 0.1834 0.0260 0.1581 0.0282  0.0100  -0.0036 202 CYS D CA  
8009 C  C   . CYS D 202 ? 0.1689 0.0108 0.1685 -0.0244 0.0232  -0.0147 202 CYS D C   
8010 O  O   . CYS D 202 ? 0.2007 0.0082 0.1798 -0.0028 0.0152  -0.0179 202 CYS D O   
8011 C  CB  . CYS D 202 ? 0.1752 0.0064 0.1708 -0.0022 0.0139  -0.0034 202 CYS D CB  
8012 S  SG  . CYS D 202 ? 0.2052 0.0066 0.1630 0.0038  -0.0105 -0.0063 202 CYS D SG  
8013 N  N   . ASN D 203 ? 0.1547 0.0142 0.1650 -0.0323 0.0427  -0.0203 203 ASN D N   
8014 C  CA  . ASN D 203 ? 0.2117 0.0413 0.1331 0.0058  0.0187  -0.0027 203 ASN D CA  
8015 C  C   . ASN D 203 ? 0.1861 0.0231 0.1294 -0.0142 0.0050  -0.0178 203 ASN D C   
8016 O  O   . ASN D 203 ? 0.1882 0.0157 0.1578 0.0086  0.0170  -0.0358 203 ASN D O   
8017 C  CB  . ASN D 203 ? 0.2300 0.0310 0.1606 0.0348  0.0337  0.0064  203 ASN D CB  
8018 C  CG  . ASN D 203 ? 0.2340 0.0171 0.1780 0.0005  0.0341  -0.0017 203 ASN D CG  
8019 O  OD1 . ASN D 203 ? 0.2508 0.0179 0.1826 0.0019  0.0233  0.0337  203 ASN D OD1 
8020 N  ND2 . ASN D 203 ? 0.2394 0.0336 0.2242 -0.0009 0.0308  -0.0287 203 ASN D ND2 
8021 N  N   . PRO D 204 ? 0.2291 0.0137 0.1431 -0.0284 0.0007  -0.0226 204 PRO D N   
8022 C  CA  . PRO D 204 ? 0.1984 0.0083 0.2020 -0.0196 0.0146  0.0021  204 PRO D CA  
8023 C  C   . PRO D 204 ? 0.2266 0.0065 0.1754 0.0058  0.0216  -0.0007 204 PRO D C   
8024 O  O   . PRO D 204 ? 0.2275 0.0783 0.1701 0.0065  0.0058  0.0006  204 PRO D O   
8025 C  CB  . PRO D 204 ? 0.2892 0.0262 0.1362 -0.0240 -0.0012 -0.0456 204 PRO D CB  
8026 C  CG  . PRO D 204 ? 0.2754 0.0247 0.1600 -0.0458 -0.0236 -0.0279 204 PRO D CG  
8027 C  CD  . PRO D 204 ? 0.2594 0.0236 0.1632 -0.0491 -0.0200 -0.0309 204 PRO D CD  
8028 N  N   . THR D 205 ? 0.1895 0.0115 0.1811 0.0266  0.0158  -0.0125 205 THR D N   
8029 C  CA  . THR D 205 ? 0.1868 0.0232 0.1365 0.0088  0.0049  0.0200  205 THR D CA  
8030 C  C   . THR D 205 ? 0.1743 0.0308 0.1711 0.0163  0.0411  -0.0263 205 THR D C   
8031 O  O   . THR D 205 ? 0.2024 0.0108 0.1667 0.0263  0.0202  -0.0095 205 THR D O   
8032 C  CB  . THR D 205 ? 0.2081 0.0067 0.1384 -0.0093 -0.0243 -0.0009 205 THR D CB  
8033 O  OG1 . THR D 205 ? 0.2456 0.0070 0.1497 0.0116  0.0091  -0.0040 205 THR D OG1 
8034 C  CG2 . THR D 205 ? 0.2489 0.0082 0.2198 -0.0074 -0.0300 -0.0179 205 THR D CG2 
8035 N  N   . VAL D 206 ? 0.2437 0.0070 0.1711 0.0126  0.0000  0.0011  206 VAL D N   
8036 C  CA  . VAL D 206 ? 0.1925 0.0375 0.1209 -0.0252 0.0174  -0.0098 206 VAL D CA  
8037 C  C   . VAL D 206 ? 0.1593 0.0223 0.1437 0.0431  0.0120  -0.0158 206 VAL D C   
8038 O  O   . VAL D 206 ? 0.1574 0.0122 0.2225 0.0116  -0.0089 0.0125  206 VAL D O   
8039 C  CB  . VAL D 206 ? 0.1772 0.0079 0.1180 -0.0131 0.0061  -0.0085 206 VAL D CB  
8040 C  CG1 . VAL D 206 ? 0.1409 0.0450 0.1714 -0.0068 0.0003  -0.0660 206 VAL D CG1 
8041 C  CG2 . VAL D 206 ? 0.2044 0.0213 0.1302 0.0124  0.0171  0.0087  206 VAL D CG2 
8042 N  N   . LEU D 207 ? 0.1980 0.0079 0.1639 0.0160  0.0182  -0.0047 207 LEU D N   
8043 C  CA  . LEU D 207 ? 0.1870 0.0129 0.1819 0.0345  0.0084  0.0047  207 LEU D CA  
8044 C  C   . LEU D 207 ? 0.1546 0.0281 0.1294 0.0127  -0.0102 0.0111  207 LEU D C   
8045 O  O   . LEU D 207 ? 0.1714 0.0094 0.1748 0.0059  -0.0028 0.0219  207 LEU D O   
8046 C  CB  . LEU D 207 ? 0.2238 0.0211 0.1818 0.0206  0.0385  0.0174  207 LEU D CB  
8047 C  CG  . LEU D 207 ? 0.2719 0.0397 0.1864 0.0086  0.0365  0.0271  207 LEU D CG  
8048 C  CD1 . LEU D 207 ? 0.3093 0.0665 0.1857 0.0013  0.0058  0.0173  207 LEU D CD1 
8049 C  CD2 . LEU D 207 ? 0.2721 0.2256 0.2387 -0.0199 0.0407  0.0725  207 LEU D CD2 
8050 N  N   . TRP D 208 ? 0.1508 0.0066 0.1637 -0.0065 0.0202  0.0006  208 TRP D N   
8051 C  CA  . TRP D 208 ? 0.1761 0.0073 0.1487 0.0126  -0.0063 0.0022  208 TRP D CA  
8052 C  C   . TRP D 208 ? 0.1148 0.0267 0.1463 0.0296  -0.0015 0.0279  208 TRP D C   
8053 O  O   . TRP D 208 ? 0.1857 0.0146 0.1410 0.0196  -0.0004 0.0055  208 TRP D O   
8054 C  CB  . TRP D 208 ? 0.1496 0.0128 0.1793 0.0116  -0.0244 0.0285  208 TRP D CB  
8055 C  CG  . TRP D 208 ? 0.1225 0.0069 0.1229 0.0014  -0.0118 -0.0086 208 TRP D CG  
8056 C  CD1 . TRP D 208 ? 0.1904 0.0073 0.1688 0.0097  -0.0191 -0.0095 208 TRP D CD1 
8057 C  CD2 . TRP D 208 ? 0.1381 0.0075 0.1223 0.0067  0.0159  0.0107  208 TRP D CD2 
8058 N  NE1 . TRP D 208 ? 0.1518 0.0096 0.1337 -0.0025 -0.0076 -0.0202 208 TRP D NE1 
8059 C  CE2 . TRP D 208 ? 0.1386 0.0081 0.1326 -0.0139 -0.0032 -0.0063 208 TRP D CE2 
8060 C  CE3 . TRP D 208 ? 0.1919 0.0147 0.1324 0.0231  0.0122  -0.0248 208 TRP D CE3 
8061 C  CZ2 . TRP D 208 ? 0.1607 0.0172 0.1339 0.0392  -0.0067 -0.0122 208 TRP D CZ2 
8062 C  CZ3 . TRP D 208 ? 0.1706 0.0175 0.1464 0.0372  0.0188  0.0237  208 TRP D CZ3 
8063 C  CH2 . TRP D 208 ? 0.1884 0.0091 0.1444 0.0141  0.0104  -0.0143 208 TRP D CH2 
8064 N  N   . THR D 209 ? 0.1712 0.0075 0.1521 -0.0042 0.0141  0.0120  209 THR D N   
8065 C  CA  . THR D 209 ? 0.1446 0.0082 0.1367 -0.0098 -0.0009 0.0124  209 THR D CA  
8066 C  C   . THR D 209 ? 0.1203 0.0084 0.1647 -0.0058 -0.0266 -0.0149 209 THR D C   
8067 O  O   . THR D 209 ? 0.2087 0.0114 0.1616 0.0288  -0.0288 -0.0162 209 THR D O   
8068 C  CB  . THR D 209 ? 0.1587 0.0106 0.1731 -0.0235 0.0131  0.0084  209 THR D CB  
8069 O  OG1 . THR D 209 ? 0.1855 0.0344 0.1434 -0.0079 0.0168  0.0132  209 THR D OG1 
8070 C  CG2 . THR D 209 ? 0.1266 0.0182 0.1810 -0.0219 -0.0223 0.0409  209 THR D CG2 
8071 N  N   . VAL D 210 ? 0.1233 0.0370 0.1513 0.0203  0.0105  0.0053  210 VAL D N   
8072 C  CA  . VAL D 210 ? 0.1356 0.0067 0.1765 0.0041  0.0085  -0.0070 210 VAL D CA  
8073 C  C   . VAL D 210 ? 0.0877 0.0275 0.1708 -0.0005 -0.0225 0.0363  210 VAL D C   
8074 O  O   . VAL D 210 ? 0.1643 0.0367 0.1349 0.0052  -0.0077 0.0001  210 VAL D O   
8075 C  CB  . VAL D 210 ? 0.1298 0.0078 0.1600 -0.0124 0.0135  -0.0069 210 VAL D CB  
8076 C  CG1 . VAL D 210 ? 0.1957 0.0078 0.1940 0.0118  0.0312  -0.0095 210 VAL D CG1 
8077 C  CG2 . VAL D 210 ? 0.1899 0.0081 0.1938 -0.0174 0.0127  0.0032  210 VAL D CG2 
8078 N  N   . PHE D 211 ? 0.1337 0.0140 0.1703 -0.0312 0.0184  -0.0032 211 PHE D N   
8079 C  CA  . PHE D 211 ? 0.1490 0.0163 0.1982 -0.0212 0.0027  0.0357  211 PHE D CA  
8080 C  C   . PHE D 211 ? 0.1776 0.0288 0.1819 -0.0030 0.0507  0.0506  211 PHE D C   
8081 O  O   . PHE D 211 ? 0.1518 0.0068 0.1697 -0.0011 0.0146  0.0088  211 PHE D O   
8082 C  CB  . PHE D 211 ? 0.1628 0.0086 0.1913 0.0088  0.0036  -0.0179 211 PHE D CB  
8083 C  CG  . PHE D 211 ? 0.1596 0.0071 0.1627 0.0102  0.0095  0.0043  211 PHE D CG  
8084 C  CD1 . PHE D 211 ? 0.1923 0.0370 0.1765 0.0347  0.0279  0.0039  211 PHE D CD1 
8085 C  CD2 . PHE D 211 ? 0.1524 0.0104 0.2073 -0.0158 -0.0113 0.0229  211 PHE D CD2 
8086 C  CE1 . PHE D 211 ? 0.1788 0.0128 0.2139 0.0264  0.0131  0.0242  211 PHE D CE1 
8087 C  CE2 . PHE D 211 ? 0.1819 0.0209 0.1970 0.0037  -0.0027 0.0122  211 PHE D CE2 
8088 C  CZ  . PHE D 211 ? 0.2087 0.0223 0.1951 0.0334  0.0131  0.0229  211 PHE D CZ  
8089 N  N   . ARG D 212 ? 0.1796 0.0164 0.2077 -0.0047 0.0074  0.0447  212 ARG D N   
8090 C  CA  . ARG D 212 ? 0.2028 0.0424 0.1647 0.0314  -0.0248 0.0335  212 ARG D CA  
8091 C  C   . ARG D 212 ? 0.1931 0.0268 0.2139 0.0027  0.0082  -0.0033 212 ARG D C   
8092 O  O   . ARG D 212 ? 0.2065 0.0319 0.1866 -0.0027 0.0063  0.0051  212 ARG D O   
8093 C  CB  . ARG D 212 ? 0.1480 0.0480 0.1837 0.0312  -0.0380 0.0451  212 ARG D CB  
8094 C  CG  . ARG D 212 ? 0.2318 0.0281 0.2423 0.0617  0.0253  0.0404  212 ARG D CG  
8095 C  CD  . ARG D 212 ? 0.2433 0.0295 0.2227 0.0707  0.0212  0.0271  212 ARG D CD  
8096 N  NE  . ARG D 212 ? 0.2918 0.0375 0.2451 0.0911  0.0087  0.0248  212 ARG D NE  
8097 C  CZ  . ARG D 212 ? 0.3157 0.1056 0.2846 0.0618  0.0116  0.0912  212 ARG D CZ  
8098 N  NH1 . ARG D 212 ? 0.2785 0.0697 0.2845 0.0451  -0.0061 0.0236  212 ARG D NH1 
8099 N  NH2 . ARG D 212 ? 0.3585 0.1204 0.4070 0.1001  -0.0506 0.0966  212 ARG D NH2 
8100 N  N   . ASN D 213 ? 0.2206 0.0084 0.2097 -0.0097 -0.0175 0.0192  213 ASN D N   
8101 C  CA  . ASN D 213 ? 0.1683 0.0211 0.1729 0.0075  -0.0234 0.0142  213 ASN D CA  
8102 C  C   . ASN D 213 ? 0.1879 0.0098 0.1919 0.0181  0.0028  0.0179  213 ASN D C   
8103 O  O   . ASN D 213 ? 0.1814 0.0094 0.1954 0.0186  -0.0027 0.0147  213 ASN D O   
8104 C  CB  . ASN D 213 ? 0.2418 0.0296 0.2049 -0.0363 0.0306  0.0436  213 ASN D CB  
8105 C  CG  . ASN D 213 ? 0.2225 0.0323 0.2561 -0.0015 0.0444  0.0730  213 ASN D CG  
8106 O  OD1 . ASN D 213 ? 0.3413 0.1467 0.3732 0.1301  0.0609  0.1354  213 ASN D OD1 
8107 N  ND2 . ASN D 213 ? 0.2975 0.1234 0.2775 0.0042  0.1000  0.0775  213 ASN D ND2 
8108 N  N   . PRO D 214 ? 0.1943 0.0168 0.1719 0.0400  -0.0277 0.0118  214 PRO D N   
8109 C  CA  . PRO D 214 ? 0.1611 0.0218 0.1518 0.0108  -0.0004 0.0074  214 PRO D CA  
8110 C  C   . PRO D 214 ? 0.1540 0.0069 0.1592 0.0086  0.0000  -0.0042 214 PRO D C   
8111 O  O   . PRO D 214 ? 0.1812 0.0090 0.2292 -0.0082 -0.0221 0.0234  214 PRO D O   
8112 C  CB  . PRO D 214 ? 0.1847 0.0095 0.2127 0.0208  0.0188  -0.0099 214 PRO D CB  
8113 C  CG  . PRO D 214 ? 0.2637 0.0091 0.2222 0.0209  -0.0037 0.0115  214 PRO D CG  
8114 C  CD  . PRO D 214 ? 0.2625 0.0315 0.1923 0.0589  -0.0147 0.0428  214 PRO D CD  
8115 N  N   . VAL D 215 ? 0.1459 0.0299 0.1591 -0.0022 -0.0118 0.0089  215 VAL D N   
8116 C  CA  . VAL D 215 ? 0.1421 0.0178 0.1682 0.0003  -0.0151 0.0226  215 VAL D CA  
8117 C  C   . VAL D 215 ? 0.1334 0.0091 0.1712 -0.0112 -0.0124 0.0180  215 VAL D C   
8118 O  O   . VAL D 215 ? 0.1325 0.0089 0.1954 0.0077  -0.0153 -0.0210 215 VAL D O   
8119 C  CB  . VAL D 215 ? 0.1698 0.0066 0.1776 0.0003  -0.0167 0.0068  215 VAL D CB  
8120 C  CG1 . VAL D 215 ? 0.1579 0.0566 0.2006 -0.0130 0.0121  0.0037  215 VAL D CG1 
8121 C  CG2 . VAL D 215 ? 0.1615 0.0182 0.2278 -0.0089 -0.0015 0.0355  215 VAL D CG2 
8122 N  N   . GLN D 216 ? 0.1678 0.0165 0.1639 -0.0100 -0.0080 -0.0023 216 GLN D N   
8123 C  CA  . GLN D 216 ? 0.1624 0.0066 0.1650 0.0073  -0.0151 -0.0015 216 GLN D CA  
8124 C  C   . GLN D 216 ? 0.1403 0.0063 0.1857 0.0008  -0.0225 0.0028  216 GLN D C   
8125 O  O   . GLN D 216 ? 0.1469 0.0329 0.2105 0.0196  -0.0276 -0.0256 216 GLN D O   
8126 C  CB  . GLN D 216 ? 0.1597 0.0085 0.2457 0.0179  -0.0385 -0.0083 216 GLN D CB  
8127 C  CG  . GLN D 216 ? 0.2514 0.0096 0.2802 0.0275  -0.0473 0.0026  216 GLN D CG  
8128 C  CD  . GLN D 216 ? 0.2813 0.0232 0.2293 0.0029  -0.0369 -0.0355 216 GLN D CD  
8129 O  OE1 . GLN D 216 ? 0.2549 0.1531 0.1920 0.0390  -0.0120 0.0093  216 GLN D OE1 
8130 N  NE2 . GLN D 216 ? 0.4577 0.3006 0.3481 0.0640  -0.0901 0.1124  216 GLN D NE2 
8131 N  N   . ILE D 217 ? 0.1573 0.0075 0.1455 0.0109  -0.0188 -0.0090 217 ILE D N   
8132 C  CA  . ILE D 217 ? 0.1543 0.0090 0.1423 0.0166  -0.0219 -0.0013 217 ILE D CA  
8133 C  C   . ILE D 217 ? 0.1485 0.0502 0.1424 0.0239  -0.0150 -0.0012 217 ILE D C   
8134 O  O   . ILE D 217 ? 0.1526 0.0096 0.1879 0.0218  -0.0018 -0.0027 217 ILE D O   
8135 C  CB  . ILE D 217 ? 0.1367 0.0112 0.1792 0.0235  -0.0262 -0.0151 217 ILE D CB  
8136 C  CG1 . ILE D 217 ? 0.1230 0.0090 0.1958 0.0171  -0.0562 -0.0031 217 ILE D CG1 
8137 C  CG2 . ILE D 217 ? 0.1326 0.0740 0.1972 -0.0031 0.0044  -0.0287 217 ILE D CG2 
8138 C  CD1 . ILE D 217 ? 0.2180 0.0088 0.2006 0.0192  -0.0148 0.0104  217 ILE D CD1 
8139 N  N   . SER D 218 ? 0.1542 0.0090 0.1451 0.0122  0.0019  -0.0150 218 SER D N   
8140 C  CA  . SER D 218 ? 0.1234 0.0423 0.1758 0.0277  0.0040  -0.0248 218 SER D CA  
8141 C  C   . SER D 218 ? 0.1362 0.0072 0.1467 0.0076  -0.0233 -0.0095 218 SER D C   
8142 O  O   . SER D 218 ? 0.1966 0.0063 0.2166 0.0025  -0.0202 -0.0016 218 SER D O   
8143 C  CB  . SER D 218 ? 0.1890 0.0217 0.2227 0.0288  -0.0661 0.0186  218 SER D CB  
8144 O  OG  . SER D 218 ? 0.2606 0.0101 0.1991 0.0293  -0.0341 -0.0123 218 SER D OG  
8145 N  N   . GLN D 219 ? 0.1374 0.0825 0.1320 0.0206  -0.0098 0.0011  219 GLN D N   
8146 C  CA  . GLN D 219 ? 0.1489 0.0829 0.1628 0.0419  0.0001  0.0215  219 GLN D CA  
8147 C  C   . GLN D 219 ? 0.2041 0.0095 0.1742 -0.0250 -0.0455 0.0043  219 GLN D C   
8148 O  O   . GLN D 219 ? 0.2081 0.0108 0.1789 -0.0297 -0.0019 -0.0047 219 GLN D O   
8149 C  CB  . GLN D 219 ? 0.1740 0.0851 0.2318 0.0457  0.0298  0.0116  219 GLN D CB  
8150 C  CG  . GLN D 219 ? 0.2240 0.1886 0.3061 0.0556  0.0693  0.1220  219 GLN D CG  
8151 C  CD  . GLN D 219 ? 0.3403 0.0785 0.2891 0.0480  0.0738  0.0580  219 GLN D CD  
8152 O  OE1 . GLN D 219 ? 0.3353 0.4269 0.4307 0.1265  0.0023  -0.0842 219 GLN D OE1 
8153 N  NE2 . GLN D 219 ? 0.3111 0.1927 0.3796 0.0120  0.0619  0.0998  219 GLN D NE2 
8154 N  N   . GLU D 220 ? 0.1645 0.0592 0.1613 0.0364  -0.0296 -0.0017 220 GLU D N   
8155 C  CA  . GLU D 220 ? 0.1873 0.0431 0.1507 0.0156  -0.0540 -0.0166 220 GLU D CA  
8156 C  C   . GLU D 220 ? 0.1747 0.0105 0.2009 -0.0246 0.0019  0.0101  220 GLU D C   
8157 O  O   . GLU D 220 ? 0.1978 0.0087 0.1713 -0.0130 -0.0139 0.0167  220 GLU D O   
8158 C  CB  . GLU D 220 ? 0.1945 0.0349 0.1650 0.0256  -0.0428 -0.0323 220 GLU D CB  
8159 C  CG  . GLU D 220 ? 0.2652 0.0269 0.1826 0.0445  -0.0479 -0.0370 220 GLU D CG  
8160 C  CD  . GLU D 220 ? 0.3222 0.0192 0.1825 -0.0208 -0.0330 -0.0425 220 GLU D CD  
8161 O  OE1 . GLU D 220 ? 0.3827 0.0136 0.2157 -0.0117 0.0332  -0.0208 220 GLU D OE1 
8162 O  OE2 . GLU D 220 ? 0.4386 0.0828 0.2803 0.0308  0.0359  -0.0901 220 GLU D OE2 
8163 N  N   . GLN D 221 ? 0.1527 0.0097 0.1624 0.0197  -0.0009 -0.0111 221 GLN D N   
8164 C  CA  . GLN D 221 ? 0.1762 0.0131 0.1781 0.0217  -0.0095 -0.0272 221 GLN D CA  
8165 C  C   . GLN D 221 ? 0.1726 0.0067 0.1769 0.0072  -0.0486 0.0027  221 GLN D C   
8166 O  O   . GLN D 221 ? 0.1897 0.0066 0.1982 0.0066  -0.0137 0.0025  221 GLN D O   
8167 C  CB  . GLN D 221 ? 0.1482 0.0248 0.1755 -0.0017 -0.0085 -0.0383 221 GLN D CB  
8168 C  CG  . GLN D 221 ? 0.1470 0.0065 0.2106 0.0048  -0.0216 -0.0018 221 GLN D CG  
8169 C  CD  . GLN D 221 ? 0.1837 0.0429 0.1768 0.0218  -0.0108 0.0052  221 GLN D CD  
8170 O  OE1 . GLN D 221 ? 0.1800 0.0069 0.2402 0.0060  -0.0128 0.0087  221 GLN D OE1 
8171 N  NE2 . GLN D 221 ? 0.1924 0.0120 0.2518 0.0117  -0.0384 -0.0368 221 GLN D NE2 
8172 N  N   . LEU D 222 ? 0.1789 0.0303 0.1661 0.0131  -0.0384 0.0009  222 LEU D N   
8173 C  CA  . LEU D 222 ? 0.1826 0.0379 0.1726 -0.0096 -0.0295 0.0185  222 LEU D CA  
8174 C  C   . LEU D 222 ? 0.1881 0.0118 0.1573 0.0084  -0.0359 0.0253  222 LEU D C   
8175 O  O   . LEU D 222 ? 0.2084 0.0083 0.1952 -0.0024 -0.0288 0.0194  222 LEU D O   
8176 C  CB  . LEU D 222 ? 0.1961 0.0080 0.1732 0.0108  -0.0122 -0.0139 222 LEU D CB  
8177 C  CG  . LEU D 222 ? 0.2537 0.0099 0.1859 0.0230  0.0207  -0.0139 222 LEU D CG  
8178 C  CD1 . LEU D 222 ? 0.2074 0.0216 0.2552 0.0258  0.0156  0.0381  222 LEU D CD1 
8179 C  CD2 . LEU D 222 ? 0.2106 0.0495 0.1952 0.0326  -0.0154 -0.0635 222 LEU D CD2 
8180 N  N   . LEU D 223 ? 0.1556 0.0768 0.1697 0.0294  0.0087  0.0222  223 LEU D N   
8181 C  CA  . LEU D 223 ? 0.1837 0.0394 0.1294 0.0409  0.0059  -0.0121 223 LEU D CA  
8182 C  C   . LEU D 223 ? 0.1760 0.0172 0.2035 -0.0171 -0.0551 0.0276  223 LEU D C   
8183 O  O   . LEU D 223 ? 0.1960 0.0064 0.2110 0.0045  -0.0280 0.0016  223 LEU D O   
8184 C  CB  . LEU D 223 ? 0.1918 0.0408 0.1421 0.0119  0.0021  -0.0291 223 LEU D CB  
8185 C  CG  . LEU D 223 ? 0.1933 0.0554 0.1725 0.0385  0.0143  -0.0156 223 LEU D CG  
8186 C  CD1 . LEU D 223 ? 0.1947 0.0746 0.3617 0.0186  0.0189  -0.0268 223 LEU D CD1 
8187 C  CD2 . LEU D 223 ? 0.2263 0.0581 0.2069 -0.0044 0.0440  -0.0344 223 LEU D CD2 
8188 N  N   . ALA D 224 ? 0.1729 0.0564 0.1794 0.0066  -0.0257 0.0321  224 ALA D N   
8189 C  CA  . ALA D 224 ? 0.1469 0.1035 0.1825 0.0285  -0.0658 -0.0022 224 ALA D CA  
8190 C  C   . ALA D 224 ? 0.1563 0.0240 0.1889 -0.0232 -0.0364 0.0405  224 ALA D C   
8191 O  O   . ALA D 224 ? 0.1744 0.0313 0.2461 0.0033  -0.0091 0.0690  224 ALA D O   
8192 C  CB  . ALA D 224 ? 0.1640 0.0882 0.2717 0.0030  -0.0469 0.0110  224 ALA D CB  
8193 N  N   . LEU D 225 ? 0.1679 0.0226 0.1639 -0.0074 0.0147  0.0003  225 LEU D N   
8194 C  CA  . LEU D 225 ? 0.1180 0.0588 0.1675 0.0145  0.0176  -0.0172 225 LEU D CA  
8195 C  C   . LEU D 225 ? 0.1250 0.0199 0.1593 -0.0043 -0.0083 0.0320  225 LEU D C   
8196 O  O   . LEU D 225 ? 0.1699 0.0227 0.2700 -0.0176 0.0238  0.0334  225 LEU D O   
8197 C  CB  . LEU D 225 ? 0.1949 0.0217 0.1893 -0.0281 0.0480  -0.0057 225 LEU D CB  
8198 C  CG  . LEU D 225 ? 0.2252 0.0127 0.1821 0.0372  -0.0037 0.0015  225 LEU D CG  
8199 C  CD1 . LEU D 225 ? 0.1909 0.0533 0.2166 0.0451  -0.0295 -0.0048 225 LEU D CD1 
8200 C  CD2 . LEU D 225 ? 0.2175 0.0571 0.1804 -0.0326 -0.0277 0.0132  225 LEU D CD2 
8201 N  N   . GLU D 226 ? 0.1488 0.0666 0.1704 0.0091  0.0097  0.0143  226 GLU D N   
8202 C  CA  . GLU D 226 ? 0.1546 0.0442 0.1916 0.0042  0.0076  0.0307  226 GLU D CA  
8203 C  C   . GLU D 226 ? 0.1706 0.0505 0.1750 -0.0136 -0.0153 0.0214  226 GLU D C   
8204 O  O   . GLU D 226 ? 0.1636 0.1277 0.2354 -0.0370 -0.0300 0.0494  226 GLU D O   
8205 C  CB  . GLU D 226 ? 0.1672 0.0944 0.1288 0.0369  0.0084  0.0231  226 GLU D CB  
8206 C  CG  . GLU D 226 ? 0.1488 0.0467 0.1358 0.0368  0.0003  0.0152  226 GLU D CG  
8207 C  CD  . GLU D 226 ? 0.1765 0.0326 0.1230 0.0179  -0.0219 0.0017  226 GLU D CD  
8208 O  OE1 . GLU D 226 ? 0.2046 0.1787 0.1233 0.0508  -0.0065 0.0012  226 GLU D OE1 
8209 O  OE2 . GLU D 226 ? 0.2723 0.0633 0.1358 0.0322  -0.0232 0.0152  226 GLU D OE2 
8210 N  N   . THR D 227 ? 0.1597 0.0602 0.1523 0.0200  -0.0015 0.0217  227 THR D N   
8211 C  CA  . THR D 227 ? 0.1826 0.0566 0.1597 0.0316  -0.0013 0.0333  227 THR D CA  
8212 C  C   . THR D 227 ? 0.1740 0.0262 0.1825 0.0176  0.0039  0.0343  227 THR D C   
8213 O  O   . THR D 227 ? 0.2591 0.0742 0.1974 0.0267  -0.0111 0.0600  227 THR D O   
8214 C  CB  . THR D 227 ? 0.1481 0.1015 0.2045 0.0331  -0.0239 -0.0086 227 THR D CB  
8215 O  OG1 . THR D 227 ? 0.2176 0.0347 0.1923 0.0147  -0.0060 -0.0041 227 THR D OG1 
8216 C  CG2 . THR D 227 ? 0.1221 0.1347 0.2482 0.0339  0.0077  0.0053  227 THR D CG2 
8217 N  N   . ALA D 228 ? 0.1719 0.0245 0.1945 0.0120  -0.0024 0.0245  228 ALA D N   
8218 C  CA  . ALA D 228 ? 0.1568 0.0577 0.1873 0.0176  -0.0109 0.0030  228 ALA D CA  
8219 C  C   . ALA D 228 ? 0.2380 0.0593 0.1830 0.0144  -0.0299 0.0265  228 ALA D C   
8220 O  O   . ALA D 228 ? 0.2462 0.0900 0.2196 0.0067  -0.0772 0.0486  228 ALA D O   
8221 C  CB  . ALA D 228 ? 0.1564 0.1259 0.2879 -0.0010 -0.0209 0.0701  228 ALA D CB  
8222 N  N   . LEU D 229 ? 0.1654 0.0525 0.1617 0.0177  -0.0126 0.0434  229 LEU D N   
8223 C  CA  . LEU D 229 ? 0.1984 0.0568 0.1839 -0.0198 -0.0019 0.0286  229 LEU D CA  
8224 C  C   . LEU D 229 ? 0.1738 0.0402 0.1596 0.0107  -0.0234 0.0690  229 LEU D C   
8225 O  O   . LEU D 229 ? 0.1787 0.1042 0.1801 0.0318  -0.0150 0.0392  229 LEU D O   
8226 C  CB  . LEU D 229 ? 0.1464 0.0785 0.1647 0.0102  -0.0189 0.0212  229 LEU D CB  
8227 C  CG  . LEU D 229 ? 0.1482 0.1735 0.1639 -0.0099 -0.0138 0.0340  229 LEU D CG  
8228 C  CD1 . LEU D 229 ? 0.1895 0.2484 0.1760 -0.0351 0.0082  0.0545  229 LEU D CD1 
8229 C  CD2 . LEU D 229 ? 0.1492 0.3134 0.2060 -0.0002 -0.0391 0.0825  229 LEU D CD2 
8230 N  N   . TYR D 230 ? 0.2374 0.0310 0.1955 0.0251  0.0005  0.0527  230 TYR D N   
8231 C  CA  . TYR D 230 ? 0.1983 0.1388 0.1814 0.0041  0.0023  0.0505  230 TYR D CA  
8232 C  C   . TYR D 230 ? 0.1816 0.0595 0.1922 -0.0602 0.0320  0.0653  230 TYR D C   
8233 O  O   . TYR D 230 ? 0.1864 0.0695 0.2471 -0.0146 0.0047  0.0439  230 TYR D O   
8234 C  CB  . TYR D 230 ? 0.2212 0.1078 0.1654 -0.0109 -0.0201 0.0435  230 TYR D CB  
8235 C  CG  . TYR D 230 ? 0.2300 0.1658 0.1907 0.0237  -0.0450 0.0223  230 TYR D CG  
8236 C  CD1 . TYR D 230 ? 0.3098 0.1272 0.2365 -0.0040 0.0119  -0.0147 230 TYR D CD1 
8237 C  CD2 . TYR D 230 ? 0.2683 0.1600 0.2024 -0.0317 -0.0176 -0.0012 230 TYR D CD2 
8238 C  CE1 . TYR D 230 ? 0.2872 0.1589 0.3003 0.0948  -0.0538 -0.0368 230 TYR D CE1 
8239 C  CE2 . TYR D 230 ? 0.3085 0.2685 0.1862 0.0848  -0.1023 -0.0351 230 TYR D CE2 
8240 C  CZ  . TYR D 230 ? 0.2991 0.2340 0.2855 -0.0130 -0.0039 0.0320  230 TYR D CZ  
8241 O  OH  . TYR D 230 ? 0.2964 0.3122 0.2754 -0.0550 0.0031  -0.0172 230 TYR D OH  
8242 N  N   . CYS D 231 ? 0.1710 0.1456 0.2010 -0.0217 -0.0044 0.0296  231 CYS D N   
8243 C  CA  . CYS D 231 ? 0.2062 0.1306 0.1722 -0.0607 -0.0064 0.0385  231 CYS D CA  
8244 C  C   . CYS D 231 ? 0.1870 0.1379 0.1807 -0.0012 -0.0299 0.0234  231 CYS D C   
8245 O  O   . CYS D 231 ? 0.2500 0.1912 0.1661 0.0179  -0.0100 0.0120  231 CYS D O   
8246 C  CB  . CYS D 231 ? 0.1909 0.1484 0.2002 -0.0092 -0.0146 0.0577  231 CYS D CB  
8247 S  SG  . CYS D 231 ? 0.2424 0.1205 0.2326 -0.0332 -0.0134 0.0444  231 CYS D SG  
8248 N  N   . THR D 232 ? 0.2148 0.0956 0.2110 -0.0397 0.0257  0.0643  232 THR D N   
8249 C  CA  . THR D 232 ? 0.2430 0.1032 0.1800 -0.0487 0.0097  0.0644  232 THR D CA  
8250 C  C   . THR D 232 ? 0.2189 0.0729 0.2412 -0.0088 0.0358  0.0397  232 THR D C   
8251 O  O   . THR D 232 ? 0.1782 0.1338 0.1841 -0.0167 0.0095  0.0113  232 THR D O   
8252 C  CB  . THR D 232 ? 0.2308 0.0692 0.2175 -0.0217 -0.0114 0.0389  232 THR D CB  
8253 O  OG1 . THR D 232 ? 0.2290 0.0827 0.2103 0.0038  -0.0109 0.0285  232 THR D OG1 
8254 C  CG2 . THR D 232 ? 0.2271 0.0902 0.2563 -0.0159 -0.0269 0.0340  232 THR D CG2 
8255 N  N   A HIS D 233 ? 0.2779 0.0301 0.2910 -0.0163 -0.0069 -0.0451 233 HIS D N   
8256 N  N   B HIS D 233 ? 0.2892 0.0783 0.2512 0.0443  0.0354  0.0271  233 HIS D N   
8257 C  CA  A HIS D 233 ? 0.2726 0.0531 0.2850 -0.0242 0.0126  -0.0111 233 HIS D CA  
8258 C  CA  B HIS D 233 ? 0.3150 0.0678 0.2146 0.0060  0.0250  0.0409  233 HIS D CA  
8259 C  C   A HIS D 233 ? 0.2892 0.0785 0.2613 -0.0168 -0.0050 0.0135  233 HIS D C   
8260 C  C   B HIS D 233 ? 0.3226 0.0839 0.2200 -0.0005 0.0167  0.0332  233 HIS D C   
8261 O  O   A HIS D 233 ? 0.2559 0.0303 0.2890 0.0179  -0.0239 0.0196  233 HIS D O   
8262 O  O   B HIS D 233 ? 0.2787 0.0428 0.2724 0.0262  -0.0096 0.0201  233 HIS D O   
8263 C  CB  A HIS D 233 ? 0.3209 0.0598 0.4506 0.0163  0.0501  0.0038  233 HIS D CB  
8264 C  CB  B HIS D 233 ? 0.3687 0.0706 0.3256 0.0341  0.0757  0.0812  233 HIS D CB  
8265 C  CG  A HIS D 233 ? 0.2865 0.0189 0.5008 -0.0591 0.0738  -0.0250 233 HIS D CG  
8266 C  CG  B HIS D 233 ? 0.3660 0.1101 0.3367 0.0341  0.0724  0.1000  233 HIS D CG  
8267 N  ND1 A HIS D 233 ? 0.3520 0.1518 0.5222 -0.0990 0.0002  -0.1620 233 HIS D ND1 
8268 N  ND1 B HIS D 233 ? 0.4449 0.0149 0.3398 0.0495  0.1536  0.0464  233 HIS D ND1 
8269 C  CD2 A HIS D 233 ? 0.2830 0.0531 0.4602 0.0564  0.0867  -0.0565 233 HIS D CD2 
8270 C  CD2 B HIS D 233 ? 0.4528 0.1476 0.2992 0.1033  0.1156  0.1289  233 HIS D CD2 
8271 C  CE1 A HIS D 233 ? 0.3617 0.1259 0.5769 0.0047  0.0264  -0.1750 233 HIS D CE1 
8272 C  CE1 B HIS D 233 ? 0.4547 0.1121 0.3922 0.0383  0.1223  0.1780  233 HIS D CE1 
8273 N  NE2 A HIS D 233 ? 0.3257 0.1602 0.5519 0.0238  0.0728  -0.1351 233 HIS D NE2 
8274 N  NE2 B HIS D 233 ? 0.5175 0.1234 0.3421 0.0981  0.0791  0.1418  233 HIS D NE2 
8275 N  N   A MET D 234 ? 0.2759 0.0419 0.2466 0.0168  -0.0094 0.0386  234 MET D N   
8276 N  N   B MET D 234 ? 0.3189 0.0461 0.2379 0.0231  0.0000  0.0559  234 MET D N   
8277 C  CA  A MET D 234 ? 0.3107 0.1020 0.2254 0.0058  -0.0578 0.0291  234 MET D CA  
8278 C  CA  B MET D 234 ? 0.3800 0.0661 0.2164 0.0117  -0.0417 0.0633  234 MET D CA  
8279 C  C   A MET D 234 ? 0.3761 0.1388 0.2092 -0.0093 -0.0227 0.0266  234 MET D C   
8280 C  C   B MET D 234 ? 0.3884 0.1287 0.1983 0.0283  0.0075  0.0445  234 MET D C   
8281 O  O   A MET D 234 ? 0.3230 0.0597 0.2314 -0.1130 0.0026  0.0394  234 MET D O   
8282 O  O   B MET D 234 ? 0.4398 0.3370 0.1787 0.1358  -0.0152 0.0380  234 MET D O   
8283 C  CB  A MET D 234 ? 0.2852 0.1647 0.2722 0.0229  -0.0379 0.0293  234 MET D CB  
8284 C  CB  B MET D 234 ? 0.3439 0.0295 0.2968 0.0333  0.0016  0.0761  234 MET D CB  
8285 C  CG  A MET D 234 ? 0.2333 0.2558 0.2755 0.1558  -0.0100 -0.0130 234 MET D CG  
8286 C  CG  B MET D 234 ? 0.4634 0.2564 0.2430 0.0900  -0.0249 0.0132  234 MET D CG  
8287 S  SD  A MET D 234 ? 0.2791 0.4867 0.5108 0.1380  -0.1385 0.0200  234 MET D SD  
8288 S  SD  B MET D 234 ? 0.4406 0.5755 0.2874 0.1074  -0.0105 -0.1888 234 MET D SD  
8289 C  CE  A MET D 234 ? 0.2045 0.4997 0.3847 0.1979  -0.0192 0.0205  234 MET D CE  
8290 C  CE  B MET D 234 ? 0.1427 0.6429 0.3503 0.1350  -0.1894 -0.3891 234 MET D CE  
8291 N  N   . ASP D 235 ? 0.2962 0.1352 0.3250 -0.0120 -0.0376 0.0663  235 ASP D N   
8292 C  CA  . ASP D 235 ? 0.5231 0.1373 0.3113 -0.0262 -0.0307 0.1446  235 ASP D CA  
8293 C  C   . ASP D 235 ? 0.4064 0.0796 0.3667 -0.0251 0.0262  0.1506  235 ASP D C   
8294 O  O   . ASP D 235 ? 0.3687 0.1435 0.3560 -0.0356 -0.0058 0.1581  235 ASP D O   
8295 C  CB  . ASP D 235 ? 0.6235 0.1312 0.4806 0.0666  0.0390  0.0496  235 ASP D CB  
8296 C  CG  . ASP D 235 ? 0.7055 0.1658 0.5572 0.1076  0.2953  0.0890  235 ASP D CG  
8297 O  OD1 . ASP D 235 ? 0.8420 0.2164 0.5842 0.1165  0.1615  0.0066  235 ASP D OD1 
8298 O  OD2 . ASP D 235 ? 0.7709 0.1221 0.9010 0.0929  0.1434  -0.0109 235 ASP D OD2 
8299 N  N   . ASP D 236 ? 0.3418 0.1793 0.3222 0.0311  -0.0037 0.0954  236 ASP D N   
8300 C  CA  . ASP D 236 ? 0.3553 0.1342 0.2517 0.0039  0.0451  0.1145  236 ASP D CA  
8301 C  C   . ASP D 236 ? 0.2772 0.2974 0.3005 -0.0122 0.0410  0.0837  236 ASP D C   
8302 O  O   . ASP D 236 ? 0.3176 0.2913 0.2135 0.0899  0.0214  0.0631  236 ASP D O   
8303 C  CB  . ASP D 236 ? 0.4451 0.0311 0.2205 -0.0837 -0.0947 0.0248  236 ASP D CB  
8304 C  CG  . ASP D 236 ? 0.3845 0.0771 0.3143 -0.0140 -0.0741 -0.0700 236 ASP D CG  
8305 O  OD1 . ASP D 236 ? 0.3951 0.2666 0.3045 0.0946  -0.0229 0.0418  236 ASP D OD1 
8306 O  OD2 . ASP D 236 ? 0.3938 0.2403 0.3269 -0.1163 -0.0171 -0.0173 236 ASP D OD2 
8307 N  N   . PRO D 237 ? 0.3452 0.0970 0.2935 -0.0058 0.0211  0.0679  237 PRO D N   
8308 C  CA  . PRO D 237 ? 0.2763 0.1923 0.3790 0.0263  0.0438  0.1169  237 PRO D CA  
8309 C  C   . PRO D 237 ? 0.3285 0.2528 0.2800 0.0526  0.0858  0.1477  237 PRO D C   
8310 O  O   . PRO D 237 ? 0.3553 0.2660 0.3728 0.0276  0.1344  0.0876  237 PRO D O   
8311 C  CB  . PRO D 237 ? 0.4270 0.3001 0.4473 -0.0813 0.0769  0.1496  237 PRO D CB  
8312 C  CG  . PRO D 237 ? 0.4361 0.1785 0.5035 -0.0660 0.1038  0.1769  237 PRO D CG  
8313 C  CD  . PRO D 237 ? 0.3714 0.0787 0.4626 -0.0328 0.0483  0.0885  237 PRO D CD  
8314 N  N   . SER D 238 ? 0.3456 0.3911 0.2719 0.0463  0.0784  0.1779  238 SER D N   
8315 C  CA  . SER D 238 ? 0.4210 0.1703 0.3319 0.0100  0.0787  0.1617  238 SER D CA  
8316 C  C   . SER D 238 ? 0.2575 0.1909 0.2791 0.0270  -0.0159 0.1728  238 SER D C   
8317 O  O   . SER D 238 ? 0.2343 0.2182 0.2903 -0.0094 -0.0129 0.1222  238 SER D O   
8318 C  CB  . SER D 238 ? 0.4623 0.2737 0.4196 -0.0784 0.0639  0.1474  238 SER D CB  
8319 O  OG  . SER D 238 ? 0.6639 0.5118 0.5807 0.0284  0.0966  0.2832  238 SER D OG  
8320 N  N   . PRO D 239 ? 0.2536 0.2264 0.2623 0.0413  0.0502  0.1061  239 PRO D N   
8321 C  CA  . PRO D 239 ? 0.3364 0.1336 0.2352 0.0280  0.0345  0.1242  239 PRO D CA  
8322 C  C   . PRO D 239 ? 0.2354 0.0942 0.2549 0.0326  0.0562  0.0977  239 PRO D C   
8323 O  O   . PRO D 239 ? 0.2013 0.2198 0.2166 0.0295  0.0072  0.0657  239 PRO D O   
8324 C  CB  . PRO D 239 ? 0.3305 0.3049 0.2502 0.0461  0.0791  0.0429  239 PRO D CB  
8325 C  CG  . PRO D 239 ? 0.4096 0.2116 0.2376 0.0339  0.0998  0.0983  239 PRO D CG  
8326 C  CD  . PRO D 239 ? 0.3331 0.2308 0.2579 0.0462  0.1017  0.0971  239 PRO D CD  
8327 N  N   . ARG D 240 ? 0.2273 0.1363 0.1808 -0.0487 -0.0043 0.0738  240 ARG D N   
8328 C  CA  . ARG D 240 ? 0.1841 0.1105 0.2058 -0.0174 -0.0039 0.0458  240 ARG D CA  
8329 C  C   . ARG D 240 ? 0.1611 0.1324 0.2221 -0.0127 -0.0039 0.0651  240 ARG D C   
8330 O  O   . ARG D 240 ? 0.1870 0.1173 0.2135 -0.0239 0.0228  0.0326  240 ARG D O   
8331 C  CB  . ARG D 240 ? 0.2869 0.0681 0.2351 -0.0613 -0.0099 0.0411  240 ARG D CB  
8332 C  CG  . ARG D 240 ? 0.2567 0.1374 0.2795 -0.0727 0.0006  0.0002  240 ARG D CG  
8333 C  CD  . ARG D 240 ? 0.2967 0.1227 0.2396 -0.0295 0.0168  0.0144  240 ARG D CD  
8334 N  NE  . ARG D 240 ? 0.2784 0.1254 0.2577 -0.0420 -0.0013 -0.0185 240 ARG D NE  
8335 C  CZ  . ARG D 240 ? 0.3263 0.2508 0.2573 0.0666  0.0142  0.0185  240 ARG D CZ  
8336 N  NH1 . ARG D 240 ? 0.2354 0.2372 0.2145 -0.0216 0.0339  0.0138  240 ARG D NH1 
8337 N  NH2 . ARG D 240 ? 0.2762 0.1451 0.3062 0.0138  -0.0210 0.0280  240 ARG D NH2 
8338 N  N   . GLU D 241 ? 0.1952 0.1121 0.1532 -0.0270 -0.0149 0.0706  241 GLU D N   
8339 C  CA  . GLU D 241 ? 0.2356 0.0857 0.1444 -0.0399 -0.0154 0.0487  241 GLU D CA  
8340 C  C   . GLU D 241 ? 0.1855 0.1194 0.1639 0.0212  -0.0205 0.0469  241 GLU D C   
8341 O  O   . GLU D 241 ? 0.1930 0.1039 0.1755 -0.0296 -0.0299 0.0807  241 GLU D O   
8342 C  CB  . GLU D 241 ? 0.2640 0.1524 0.1676 0.0048  -0.0076 -0.0053 241 GLU D CB  
8343 C  CG  . GLU D 241 ? 0.2678 0.2263 0.1647 -0.0140 -0.0201 -0.0060 241 GLU D CG  
8344 C  CD  . GLU D 241 ? 0.3313 0.4066 0.2380 0.1306  -0.0488 0.0021  241 GLU D CD  
8345 O  OE1 . GLU D 241 ? 0.4032 0.6567 0.2922 0.2628  -0.0846 -0.0756 241 GLU D OE1 
8346 O  OE2 . GLU D 241 ? 0.3888 0.3855 0.3416 -0.0138 -0.0436 -0.0315 241 GLU D OE2 
8347 N  N   . MET D 242 ? 0.1922 0.0811 0.1632 0.0176  -0.0080 0.0639  242 MET D N   
8348 C  CA  . MET D 242 ? 0.1664 0.0848 0.1739 0.0133  0.0122  0.0359  242 MET D CA  
8349 C  C   . MET D 242 ? 0.1446 0.0801 0.1365 0.0079  -0.0130 0.0170  242 MET D C   
8350 O  O   . MET D 242 ? 0.1570 0.1324 0.1374 -0.0247 -0.0119 0.0321  242 MET D O   
8351 C  CB  . MET D 242 ? 0.1726 0.1074 0.1742 0.0294  0.0068  0.0494  242 MET D CB  
8352 C  CG  . MET D 242 ? 0.1991 0.0591 0.1773 -0.0118 0.0011  0.0211  242 MET D CG  
8353 S  SD  . MET D 242 ? 0.1911 0.0571 0.1943 -0.0148 -0.0022 0.0355  242 MET D SD  
8354 C  CE  . MET D 242 ? 0.2435 0.0658 0.2806 -0.0288 -0.0337 0.0685  242 MET D CE  
8355 N  N   . ILE D 243 ? 0.1520 0.0520 0.1649 -0.0192 -0.0218 0.0361  243 ILE D N   
8356 C  CA  . ILE D 243 ? 0.1410 0.0540 0.1085 -0.0021 0.0093  0.0200  243 ILE D CA  
8357 C  C   . ILE D 243 ? 0.1261 0.0607 0.1008 -0.0336 0.0093  -0.0006 243 ILE D C   
8358 O  O   . ILE D 243 ? 0.1341 0.0610 0.1517 -0.0354 0.0094  -0.0065 243 ILE D O   
8359 C  CB  . ILE D 243 ? 0.1814 0.1017 0.1160 -0.0286 0.0345  0.0019  243 ILE D CB  
8360 C  CG1 . ILE D 243 ? 0.1282 0.1520 0.1826 -0.0230 0.0436  0.0196  243 ILE D CG1 
8361 C  CG2 . ILE D 243 ? 0.2134 0.0996 0.1377 -0.0024 0.0005  -0.0211 243 ILE D CG2 
8362 C  CD1 . ILE D 243 ? 0.1649 0.1649 0.2455 -0.0530 0.0863  -0.0150 243 ILE D CD1 
8363 N  N   . ASN D 244 ? 0.0986 0.1132 0.1367 -0.0044 0.0217  0.0424  244 ASN D N   
8364 C  CA  . ASN D 244 ? 0.1155 0.0692 0.1563 0.0170  -0.0001 -0.0030 244 ASN D CA  
8365 C  C   . ASN D 244 ? 0.1096 0.0499 0.1462 -0.0222 0.0111  -0.0003 244 ASN D C   
8366 O  O   . ASN D 244 ? 0.1417 0.0452 0.1661 -0.0107 -0.0153 -0.0020 244 ASN D O   
8367 C  CB  . ASN D 244 ? 0.1212 0.1002 0.1907 0.0190  0.0178  0.0147  244 ASN D CB  
8368 C  CG  . ASN D 244 ? 0.1261 0.1318 0.2054 0.0447  0.0209  0.0139  244 ASN D CG  
8369 O  OD1 . ASN D 244 ? 0.1392 0.1410 0.2002 0.0271  0.0127  0.0409  244 ASN D OD1 
8370 N  ND2 . ASN D 244 ? 0.1890 0.1173 0.2163 0.0055  0.0343  -0.0048 244 ASN D ND2 
8371 N  N   . ASN D 245 ? 0.1065 0.0325 0.1365 0.0093  -0.0199 -0.0009 245 ASN D N   
8372 C  CA  . ASN D 245 ? 0.1405 0.0348 0.1399 0.0228  0.0168  0.0184  245 ASN D CA  
8373 C  C   . ASN D 245 ? 0.1176 0.0087 0.1435 0.0033  -0.0026 0.0175  245 ASN D C   
8374 O  O   . ASN D 245 ? 0.1243 0.0341 0.1521 0.0295  -0.0044 0.0044  245 ASN D O   
8375 C  CB  . ASN D 245 ? 0.1340 0.0420 0.1494 0.0010  -0.0078 0.0031  245 ASN D CB  
8376 C  CG  . ASN D 245 ? 0.1430 0.0204 0.1877 0.0114  0.0005  -0.0088 245 ASN D CG  
8377 O  OD1 . ASN D 245 ? 0.1516 0.0236 0.1746 0.0323  -0.0015 0.0042  245 ASN D OD1 
8378 N  ND2 . ASN D 245 ? 0.1502 0.0143 0.2328 0.0338  -0.0156 -0.0036 245 ASN D ND2 
8379 N  N   . PHE D 246 ? 0.1403 0.0064 0.1336 0.0027  -0.0286 0.0020  246 PHE D N   
8380 C  CA  . PHE D 246 ? 0.1351 0.0088 0.1234 0.0128  -0.0109 -0.0030 246 PHE D CA  
8381 C  C   . PHE D 246 ? 0.1229 0.0075 0.1582 0.0116  0.0095  -0.0029 246 PHE D C   
8382 O  O   . PHE D 246 ? 0.1317 0.0073 0.1571 -0.0020 0.0082  0.0117  246 PHE D O   
8383 C  CB  . PHE D 246 ? 0.1424 0.0135 0.1475 0.0060  0.0184  -0.0301 246 PHE D CB  
8384 C  CG  . PHE D 246 ? 0.1279 0.0083 0.1662 -0.0108 0.0102  -0.0135 246 PHE D CG  
8385 C  CD1 . PHE D 246 ? 0.1605 0.0101 0.1638 -0.0185 0.0373  -0.0198 246 PHE D CD1 
8386 C  CD2 . PHE D 246 ? 0.1529 0.0067 0.1688 -0.0027 -0.0057 -0.0074 246 PHE D CD2 
8387 C  CE1 . PHE D 246 ? 0.1230 0.0541 0.1372 -0.0156 0.0052  -0.0088 246 PHE D CE1 
8388 C  CE2 . PHE D 246 ? 0.1584 0.0365 0.1543 0.0055  -0.0205 -0.0323 246 PHE D CE2 
8389 C  CZ  . PHE D 246 ? 0.1439 0.0415 0.1405 -0.0013 -0.0030 -0.0165 246 PHE D CZ  
8390 N  N   . ARG D 247 ? 0.1503 0.0067 0.1335 -0.0041 -0.0077 0.0065  247 ARG D N   
8391 C  CA  . ARG D 247 ? 0.1456 0.0334 0.1207 0.0236  -0.0182 -0.0109 247 ARG D CA  
8392 C  C   . ARG D 247 ? 0.1562 0.0104 0.1631 0.0026  0.0282  0.0252  247 ARG D C   
8393 O  O   . ARG D 247 ? 0.1323 0.0089 0.1518 -0.0092 -0.0075 0.0172  247 ARG D O   
8394 C  CB  . ARG D 247 ? 0.1518 0.0385 0.1376 -0.0227 0.0142  -0.0337 247 ARG D CB  
8395 C  CG  . ARG D 247 ? 0.1397 0.0084 0.1268 -0.0016 0.0047  -0.0159 247 ARG D CG  
8396 C  CD  . ARG D 247 ? 0.1510 0.0183 0.1549 -0.0357 0.0363  -0.0299 247 ARG D CD  
8397 N  NE  . ARG D 247 ? 0.1500 0.0071 0.1619 -0.0078 -0.0243 -0.0059 247 ARG D NE  
8398 C  CZ  . ARG D 247 ? 0.1420 0.0072 0.1586 -0.0094 0.0157  -0.0068 247 ARG D CZ  
8399 N  NH1 . ARG D 247 ? 0.1634 0.0068 0.1481 0.0074  0.0132  0.0054  247 ARG D NH1 
8400 N  NH2 . ARG D 247 ? 0.1478 0.0122 0.1640 -0.0100 -0.0353 0.0304  247 ARG D NH2 
8401 N  N   . GLN D 248 ? 0.1579 0.0189 0.1494 0.0415  0.0112  0.0160  248 GLN D N   
8402 C  CA  . GLN D 248 ? 0.1297 0.0134 0.1541 0.0276  0.0252  0.0168  248 GLN D CA  
8403 C  C   . GLN D 248 ? 0.1611 0.0066 0.1123 -0.0015 -0.0147 -0.0053 248 GLN D C   
8404 O  O   . GLN D 248 ? 0.1625 0.0119 0.1349 -0.0058 0.0143  -0.0168 248 GLN D O   
8405 C  CB  . GLN D 248 ? 0.1227 0.0223 0.1640 0.0432  0.0023  -0.0006 248 GLN D CB  
8406 C  CG  . GLN D 248 ? 0.1359 0.0105 0.1577 -0.0113 0.0090  -0.0226 248 GLN D CG  
8407 C  CD  . GLN D 248 ? 0.1283 0.0161 0.1575 -0.0207 -0.0151 -0.0278 248 GLN D CD  
8408 O  OE1 . GLN D 248 ? 0.1586 0.0075 0.1815 0.0063  -0.0428 -0.0140 248 GLN D OE1 
8409 N  NE2 . GLN D 248 ? 0.1672 0.0796 0.1674 0.0183  -0.0185 -0.0162 248 GLN D NE2 
8410 N  N   . VAL D 249 ? 0.1753 0.0173 0.1252 -0.0133 0.0193  0.0259  249 VAL D N   
8411 C  CA  . VAL D 249 ? 0.1583 0.0065 0.1249 -0.0039 0.0077  0.0038  249 VAL D CA  
8412 C  C   . VAL D 249 ? 0.1708 0.0197 0.1460 -0.0193 0.0009  0.0049  249 VAL D C   
8413 O  O   . VAL D 249 ? 0.1635 0.0071 0.1736 -0.0104 -0.0091 -0.0030 249 VAL D O   
8414 C  CB  . VAL D 249 ? 0.1399 0.0087 0.1657 0.0107  0.0016  0.0155  249 VAL D CB  
8415 C  CG1 . VAL D 249 ? 0.2109 0.0364 0.1399 -0.0347 0.0048  0.0039  249 VAL D CG1 
8416 C  CG2 . VAL D 249 ? 0.1426 0.0068 0.2387 0.0023  -0.0066 0.0104  249 VAL D CG2 
8417 N  N   . GLN D 250 ? 0.1721 0.0124 0.1491 -0.0296 -0.0105 -0.0084 250 GLN D N   
8418 C  CA  . GLN D 250 ? 0.1496 0.0245 0.1306 -0.0088 -0.0115 -0.0282 250 GLN D CA  
8419 C  C   . GLN D 250 ? 0.1500 0.0498 0.1175 -0.0234 0.0233  0.0010  250 GLN D C   
8420 O  O   . GLN D 250 ? 0.1821 0.0541 0.1518 -0.0358 -0.0159 0.0345  250 GLN D O   
8421 C  CB  . GLN D 250 ? 0.1578 0.0453 0.1236 -0.0092 0.0021  -0.0299 250 GLN D CB  
8422 C  CG  . GLN D 250 ? 0.1821 0.0589 0.1180 -0.0236 0.0092  0.0035  250 GLN D CG  
8423 C  CD  . GLN D 250 ? 0.1127 0.0112 0.1699 -0.0008 0.0213  -0.0280 250 GLN D CD  
8424 O  OE1 . GLN D 250 ? 0.2430 0.0127 0.1661 -0.0098 -0.0075 -0.0297 250 GLN D OE1 
8425 N  NE2 . GLN D 250 ? 0.1615 0.0113 0.1578 -0.0271 0.0098  0.0044  250 GLN D NE2 
8426 N  N   . LYS D 251 ? 0.1550 0.0726 0.1421 0.0070  -0.0320 -0.0200 251 LYS D N   
8427 C  CA  . LYS D 251 ? 0.1528 0.1232 0.1155 -0.0365 0.0009  -0.0339 251 LYS D CA  
8428 C  C   . LYS D 251 ? 0.1550 0.0679 0.1251 -0.0109 0.0026  0.0108  251 LYS D C   
8429 O  O   . LYS D 251 ? 0.1645 0.0618 0.1650 -0.0070 -0.0155 0.0222  251 LYS D O   
8430 C  CB  . LYS D 251 ? 0.1668 0.1602 0.1610 -0.0494 -0.0020 -0.0608 251 LYS D CB  
8431 C  CG  . LYS D 251 ? 0.1679 0.1330 0.1674 -0.0193 0.0012  0.0158  251 LYS D CG  
8432 C  CD  . LYS D 251 ? 0.2092 0.1316 0.1719 0.0133  0.0245  0.0267  251 LYS D CD  
8433 C  CE  . LYS D 251 ? 0.2174 0.1557 0.1602 -0.0674 0.0126  -0.0098 251 LYS D CE  
8434 N  NZ  . LYS D 251 ? 0.2217 0.0346 0.1543 -0.0663 -0.0116 0.0157  251 LYS D NZ  
8435 N  N   . PHE D 252 ? 0.2037 0.0864 0.1566 -0.0096 0.0289  0.0450  252 PHE D N   
8436 C  CA  . PHE D 252 ? 0.2074 0.0933 0.1433 -0.0345 0.0173  0.0421  252 PHE D CA  
8437 C  C   . PHE D 252 ? 0.2621 0.1058 0.2156 -0.0471 0.0513  0.0068  252 PHE D C   
8438 O  O   . PHE D 252 ? 0.2801 0.1494 0.2371 0.0551  0.0497  0.0609  252 PHE D O   
8439 C  CB  . PHE D 252 ? 0.2673 0.0615 0.2110 0.0021  0.0403  0.0193  252 PHE D CB  
8440 C  CG  . PHE D 252 ? 0.2708 0.1345 0.2432 -0.0074 -0.0204 0.0013  252 PHE D CG  
8441 C  CD1 . PHE D 252 ? 0.5305 0.0758 0.3057 -0.0201 0.0518  0.0343  252 PHE D CD1 
8442 C  CD2 . PHE D 252 ? 0.3343 0.0886 0.4231 -0.0846 -0.0506 0.1065  252 PHE D CD2 
8443 C  CE1 . PHE D 252 ? 0.4257 0.1841 0.3474 -0.1025 -0.0079 0.0877  252 PHE D CE1 
8444 C  CE2 . PHE D 252 ? 0.3866 0.0879 0.4183 0.0749  -0.0549 -0.0190 252 PHE D CE2 
8445 C  CZ  . PHE D 252 ? 0.3881 0.0126 0.3963 -0.0120 -0.0021 0.0176  252 PHE D CZ  
8446 N  N   . ASP D 253 ? 0.2548 0.0617 0.2637 -0.0025 -0.0328 -0.0306 253 ASP D N   
8447 C  CA  . ASP D 253 ? 0.3164 0.0581 0.2182 0.0288  -0.0044 -0.0043 253 ASP D CA  
8448 C  C   . ASP D 253 ? 0.4117 0.1398 0.3027 -0.0512 0.0314  0.0365  253 ASP D C   
8449 O  O   . ASP D 253 ? 0.3515 0.1984 0.2897 -0.0666 0.0151  0.0026  253 ASP D O   
8450 C  CB  . ASP D 253 ? 0.3407 0.0466 0.3575 -0.0129 -0.0585 0.0438  253 ASP D CB  
8451 C  CG  . ASP D 253 ? 0.3780 0.0926 0.2800 0.0271  -0.0489 0.0055  253 ASP D CG  
8452 O  OD1 . ASP D 253 ? 0.3494 0.2663 0.4766 -0.0317 -0.0176 0.0458  253 ASP D OD1 
8453 O  OD2 . ASP D 253 ? 0.4030 0.0881 0.2356 0.0538  -0.0142 0.0061  253 ASP D OD2 
8454 N  N   . GLU D 254 ? 0.3661 0.1280 0.1861 -0.0795 -0.0347 0.0176  254 GLU D N   
8455 C  CA  . GLU D 254 ? 0.3758 0.1609 0.2370 -0.0811 -0.0133 0.0610  254 GLU D CA  
8456 C  C   . GLU D 254 ? 0.3206 0.2482 0.2335 -0.0326 -0.0351 0.0391  254 GLU D C   
8457 O  O   . GLU D 254 ? 0.3984 0.2131 0.2482 -0.0820 -0.0363 0.0620  254 GLU D O   
8458 C  CB  . GLU D 254 ? 0.4968 0.3721 0.1816 -0.0527 -0.0346 0.0247  254 GLU D CB  
8459 C  CG  . GLU D 254 ? 0.4836 0.5235 0.3434 0.0013  -0.1474 -0.1764 254 GLU D CG  
8460 C  CD  . GLU D 254 ? 0.7388 0.4896 0.8380 -0.1873 -0.0458 -0.1612 254 GLU D CD  
8461 O  OE1 . GLU D 254 ? 0.7892 0.2121 0.8738 0.1760  -0.0100 0.0704  254 GLU D OE1 
8462 O  OE2 . GLU D 254 ? 0.8349 0.5472 1.1373 -0.1112 0.0061  -0.1795 254 GLU D OE2 
8463 N  N   . ARG D 255 ? 0.2813 0.1361 0.2182 -0.0206 -0.0065 0.0328  255 ARG D N   
8464 C  CA  . ARG D 255 ? 0.2535 0.0410 0.2102 -0.0171 0.0044  0.0111  255 ARG D CA  
8465 C  C   . ARG D 255 ? 0.2468 0.0394 0.2207 0.0126  0.0374  -0.0229 255 ARG D C   
8466 O  O   . ARG D 255 ? 0.2389 0.1524 0.3101 0.0334  0.0208  -0.0697 255 ARG D O   
8467 C  CB  . ARG D 255 ? 0.2989 0.0800 0.1951 0.0452  0.0394  0.0403  255 ARG D CB  
8468 C  CG  . ARG D 255 ? 0.3034 0.0769 0.2062 0.0355  -0.0203 0.0006  255 ARG D CG  
8469 C  CD  . ARG D 255 ? 0.2614 0.0954 0.2110 0.0683  0.0122  0.0905  255 ARG D CD  
8470 N  NE  . ARG D 255 ? 0.2769 0.0988 0.1951 -0.0407 0.0011  0.0336  255 ARG D NE  
8471 C  CZ  . ARG D 255 ? 0.2099 0.0972 0.2017 0.0244  0.0064  0.0361  255 ARG D CZ  
8472 N  NH1 . ARG D 255 ? 0.1908 0.0232 0.2633 -0.0048 0.0055  0.0656  255 ARG D NH1 
8473 N  NH2 . ARG D 255 ? 0.1981 0.1363 0.1927 0.0158  0.0015  -0.0004 255 ARG D NH2 
8474 N  N   . LEU D 256 ? 0.2512 0.0972 0.1575 -0.0155 -0.0053 -0.0146 256 LEU D N   
8475 C  CA  . LEU D 256 ? 0.2257 0.0906 0.1586 0.0034  -0.0253 -0.0134 256 LEU D CA  
8476 C  C   . LEU D 256 ? 0.2357 0.0936 0.1740 0.0285  -0.0290 0.0245  256 LEU D C   
8477 O  O   . LEU D 256 ? 0.2314 0.0557 0.2282 0.0067  -0.0402 0.0109  256 LEU D O   
8478 C  CB  . LEU D 256 ? 0.2841 0.1094 0.1966 0.0012  -0.0403 0.0348  256 LEU D CB  
8479 C  CG  . LEU D 256 ? 0.2703 0.2448 0.1843 0.0505  -0.0243 0.0483  256 LEU D CG  
8480 C  CD1 . LEU D 256 ? 0.3443 0.3274 0.2467 -0.0519 -0.0570 0.1039  256 LEU D CD1 
8481 C  CD2 . LEU D 256 ? 0.3067 0.2322 0.2994 0.1124  -0.0834 0.0208  256 LEU D CD2 
8482 N  N   . VAL D 257 ? 0.2526 0.0739 0.1879 -0.0034 -0.0403 0.0280  257 VAL D N   
8483 C  CA  . VAL D 257 ? 0.1916 0.0853 0.1744 0.0306  0.0187  0.0482  257 VAL D CA  
8484 C  C   . VAL D 257 ? 0.1692 0.0741 0.1934 0.0436  0.0004  0.0659  257 VAL D C   
8485 O  O   . VAL D 257 ? 0.2365 0.0541 0.2442 0.0644  0.0027  0.0455  257 VAL D O   
8486 C  CB  . VAL D 257 ? 0.2296 0.0198 0.1823 0.0053  0.0055  0.0441  257 VAL D CB  
8487 C  CG1 . VAL D 257 ? 0.2203 0.1135 0.1875 0.0215  -0.0097 0.0165  257 VAL D CG1 
8488 C  CG2 . VAL D 257 ? 0.2439 0.0956 0.1992 -0.0194 0.0243  0.0628  257 VAL D CG2 
8489 N  N   . TYR D 258 ? 0.1810 0.0363 0.1794 0.0445  0.0219  0.0352  258 TYR D N   
8490 C  CA  . TYR D 258 ? 0.1908 0.0357 0.1782 0.0189  0.0061  0.0271  258 TYR D CA  
8491 C  C   . TYR D 258 ? 0.2460 0.0191 0.1585 0.0165  -0.0020 0.0421  258 TYR D C   
8492 O  O   . TYR D 258 ? 0.2639 0.0220 0.1833 0.0038  -0.0126 0.0523  258 TYR D O   
8493 C  CB  . TYR D 258 ? 0.2261 0.0692 0.1649 0.0161  0.0066  -0.0122 258 TYR D CB  
8494 C  CG  . TYR D 258 ? 0.2235 0.0365 0.1351 0.0190  0.0022  0.0185  258 TYR D CG  
8495 C  CD1 . TYR D 258 ? 0.1829 0.1212 0.1284 0.0127  -0.0051 0.0030  258 TYR D CD1 
8496 C  CD2 . TYR D 258 ? 0.2198 0.0406 0.2552 0.0011  0.0347  0.0085  258 TYR D CD2 
8497 C  CE1 . TYR D 258 ? 0.2101 0.1220 0.2002 -0.0381 -0.0018 0.0183  258 TYR D CE1 
8498 C  CE2 . TYR D 258 ? 0.2392 0.0275 0.2622 -0.0041 -0.0078 0.0185  258 TYR D CE2 
8499 C  CZ  . TYR D 258 ? 0.2333 0.0626 0.2046 0.0091  0.0240  -0.0300 258 TYR D CZ  
8500 O  OH  . TYR D 258 ? 0.2916 0.0983 0.2786 -0.0396 -0.0208 -0.0093 258 TYR D OH  
8501 N  N   . THR D 259 ? 0.1692 0.0318 0.1562 0.0151  -0.0114 0.0587  259 THR D N   
8502 C  CA  . THR D 259 ? 0.1581 0.0675 0.1634 0.0243  0.0306  -0.0171 259 THR D CA  
8503 C  C   . THR D 259 ? 0.1571 0.0422 0.1686 0.0643  0.0232  0.0465  259 THR D C   
8504 O  O   . THR D 259 ? 0.1676 0.0836 0.1696 0.0318  0.0110  0.0398  259 THR D O   
8505 C  CB  . THR D 259 ? 0.1855 0.0803 0.1593 0.0659  0.0219  0.0274  259 THR D CB  
8506 O  OG1 . THR D 259 ? 0.2006 0.0670 0.1751 0.0526  0.0078  0.0136  259 THR D OG1 
8507 C  CG2 . THR D 259 ? 0.2070 0.0974 0.1969 0.0145  0.0485  -0.0115 259 THR D CG2 
8508 N  N   . SER D 260 ? 0.1670 0.0508 0.1923 0.0334  0.0318  0.0498  260 SER D N   
8509 C  CA  . SER D 260 ? 0.1679 0.0529 0.2024 0.0363  0.0366  0.0734  260 SER D CA  
8510 C  C   . SER D 260 ? 0.1994 0.0540 0.2455 0.0144  0.0225  0.0390  260 SER D C   
8511 O  O   . SER D 260 ? 0.2430 0.1096 0.3082 -0.0105 0.0110  0.0803  260 SER D O   
8512 C  CB  . SER D 260 ? 0.2214 0.0900 0.1726 0.0127  -0.0149 0.0311  260 SER D CB  
8513 O  OG  . SER D 260 ? 0.1963 0.0886 0.1877 0.0058  0.0348  0.0270  260 SER D OG  
8514 N  N   . PHE D 261 ? 0.2649 0.0618 0.3018 0.0723  0.0560  0.0398  261 PHE D N   
8515 C  CA  . PHE D 261 ? 0.2400 0.0541 0.2724 0.0480  0.0580  0.0853  261 PHE D CA  
8516 C  C   . PHE D 261 ? 0.2929 0.0917 0.3326 0.0283  -0.0032 0.1638  261 PHE D C   
8517 O  O   . PHE D 261 ? 0.3257 0.0472 0.2482 0.0539  -0.0137 0.0463  261 PHE D O   
8518 C  CB  . PHE D 261 ? 0.2195 0.0363 0.2794 -0.0032 0.0151  0.0719  261 PHE D CB  
8519 C  CG  . PHE D 261 ? 0.2145 0.0457 0.2775 0.0087  0.0232  0.0782  261 PHE D CG  
8520 C  CD1 . PHE D 261 ? 0.1982 0.0097 0.2433 0.0073  0.0321  0.0282  261 PHE D CD1 
8521 C  CD2 . PHE D 261 ? 0.2130 0.0659 0.3118 0.0006  0.0431  0.0341  261 PHE D CD2 
8522 C  CE1 . PHE D 261 ? 0.1916 0.0765 0.2250 -0.0064 0.0365  0.0106  261 PHE D CE1 
8523 C  CE2 . PHE D 261 ? 0.2119 0.0785 0.3314 0.0268  0.0570  0.0584  261 PHE D CE2 
8524 C  CZ  . PHE D 261 ? 0.2024 0.0621 0.2447 0.0029  0.0023  0.0152  261 PHE D CZ  
8525 N  N   . SER D 262 ? 0.3377 0.0572 0.5582 0.0549  -0.0429 0.1409  262 SER D N   
8526 C  CA  . SER D 262 ? 0.3952 0.2449 0.4839 0.1094  -0.0624 0.1923  262 SER D CA  
8527 C  C   . SER D 262 ? 0.4880 0.2417 0.5598 0.0970  -0.0366 0.1403  262 SER D C   
8528 O  O   . SER D 262 ? 0.6345 0.2432 0.6788 0.1194  0.1136  0.0987  262 SER D O   
8529 C  CB  . SER D 262 ? 0.5284 0.3333 0.4130 0.1664  0.0628  0.1102  262 SER D CB  
8530 O  OG  . SER D 262 ? 0.7022 0.7914 0.2507 0.2198  0.0407  -0.0374 262 SER D OG  
8531 N  N   . GLN D 263 ? 0.6822 0.3100 0.9967 -0.1351 0.0305  -0.0781 263 GLN D N   
8532 C  CA  . GLN D 263 ? 0.8219 0.7025 0.8652 0.1496  0.2775  -0.0613 263 GLN D CA  
8533 C  C   . GLN D 263 ? 1.1427 0.4727 0.7596 0.6730  0.4591  0.4680  263 GLN D C   
8534 O  O   . GLN D 263 ? 1.5450 0.1811 1.1688 0.4011  0.5811  0.1652  263 GLN D O   
8535 C  CB  . GLN D 263 ? 1.3651 0.4104 0.2583 0.0525  0.1377  0.3146  263 GLN D CB  
8536 C  CG  . GLN D 263 ? 0.9815 0.6924 0.9375 -0.0162 -0.0116 -0.0378 263 GLN D CG  
8537 C  CD  . GLN D 263 ? 0.6238 0.9540 0.8008 0.1606  -0.1872 0.0260  263 GLN D CD  
8538 O  OE1 . GLN D 263 ? 0.7464 0.2513 0.6420 0.0078  -0.0207 0.1004  263 GLN D OE1 
8539 N  NE2 . GLN D 263 ? 0.2888 0.3632 0.9124 -0.1120 -0.0276 -0.0787 263 GLN D NE2 
8540 ZN ZN  . ZN  E .   ? 0.1320 0.0557 0.1453 0.0089  -0.0164 0.0295  301 ZN  A ZN  
8541 C  C1  . EDO F .   ? 0.2804 0.2465 0.2227 0.0271  0.0819  0.0568  302 EDO A C1  
8542 O  O1  . EDO F .   ? 0.1967 0.1632 0.2240 -0.0068 0.0279  -0.0320 302 EDO A O1  
8543 C  C2  . EDO F .   ? 0.4081 0.3400 0.2088 0.0834  0.0816  0.0903  302 EDO A C2  
8544 O  O2  . EDO F .   ? 0.4673 0.3217 0.4189 0.0541  0.0311  0.1119  302 EDO A O2  
8545 C  C1  . EDO G .   ? 0.5702 0.3316 0.5013 -0.0325 -0.0013 -0.0754 303 EDO A C1  
8546 O  O1  . EDO G .   ? 0.1998 0.2661 0.2254 -0.0201 -0.0183 0.0502  303 EDO A O1  
8547 C  C2  . EDO G .   ? 0.0898 0.3647 0.6433 0.0862  -0.0845 0.1030  303 EDO A C2  
8548 O  O2  . EDO G .   ? 0.3098 0.9093 0.3278 0.0257  0.0702  0.0715  303 EDO A O2  
8549 O  O18 . 84Z H .   ? 0.1764 0.1248 0.2653 -0.0387 -0.0650 0.0256  304 84Z A O18 
8550 S  S16 . 84Z H .   ? 0.1837 0.1571 0.2535 -0.0284 -0.0480 0.0232  304 84Z A S16 
8551 O  O17 . 84Z H .   ? 0.2110 0.1247 0.3702 0.0025  -0.0463 0.0273  304 84Z A O17 
8552 C  C19 . 84Z H .   ? 0.2988 0.0989 0.3207 -0.1598 0.0191  0.0296  304 84Z A C19 
8553 C  C24 . 84Z H .   ? 0.2656 0.1600 0.3838 0.0043  -0.0731 0.0203  304 84Z A C24 
8554 C  C23 . 84Z H .   ? 0.2910 0.2225 0.3728 -0.0150 -0.0670 0.1154  304 84Z A C23 
8555 C  C22 . 84Z H .   ? 0.2166 0.1749 0.3439 0.0531  -0.0788 0.0307  304 84Z A C22 
8556 C  C21 . 84Z H .   ? 0.3148 0.1015 0.4024 -0.0747 -0.0465 0.0024  304 84Z A C21 
8557 C  C20 . 84Z H .   ? 0.3142 0.1212 0.2947 -0.1005 0.0122  0.0231  304 84Z A C20 
8558 C  C3  . 84Z H .   ? 0.1405 0.1397 0.1787 0.0015  -0.0486 0.0144  304 84Z A C3  
8559 C  C2  . 84Z H .   ? 0.1654 0.1197 0.1719 -0.0103 0.0031  0.0308  304 84Z A C2  
8560 C  C4  . 84Z H .   ? 0.1654 0.1117 0.1448 0.0071  -0.0381 0.0113  304 84Z A C4  
8561 C  C12 . 84Z H .   ? 0.1703 0.1038 0.2026 -0.0009 -0.0537 -0.0260 304 84Z A C12 
8562 O  O14 . 84Z H .   ? 0.1819 0.0932 0.3314 -0.0365 -0.0107 -0.0366 304 84Z A O14 
8563 C  C15 . 84Z H .   ? 0.2820 0.1366 0.3941 0.0582  -0.1188 -0.1146 304 84Z A C15 
8564 O  O13 . 84Z H .   ? 0.1927 0.2661 0.1833 0.0065  -0.0198 -0.0370 304 84Z A O13 
8565 C  C5  . 84Z H .   ? 0.1282 0.1297 0.1460 0.0108  -0.0772 0.0013  304 84Z A C5  
8566 C  C6  . 84Z H .   ? 0.1640 0.0366 0.1191 0.0154  0.0228  0.0558  304 84Z A C6  
8567 C  C1  . 84Z H .   ? 0.1154 0.1215 0.1629 0.0162  -0.0085 0.0546  304 84Z A C1  
8568 CL CL1 . 84Z H .   ? 0.1492 0.0829 0.1895 0.0114  -0.0117 0.0258  304 84Z A CL1 
8569 S  S7  . 84Z H .   ? 0.1356 0.0557 0.1804 0.0230  -0.0476 0.0337  304 84Z A S7  
8570 O  O8  . 84Z H .   ? 0.0967 0.0988 0.1500 0.0212  -0.0059 0.0428  304 84Z A O8  
8571 O  O9  . 84Z H .   ? 0.1151 0.0719 0.1559 0.0193  -0.0170 0.0212  304 84Z A O9  
8572 N  N10 . 84Z H .   ? 0.1466 0.0075 0.4991 -0.0104 0.2013  -0.0053 304 84Z A N10 
8573 ZN ZN  . ZN  I .   ? 0.1353 0.0063 0.1636 -0.0025 -0.0092 0.0006  301 ZN  B ZN  
8574 C  C1  . EDO J .   ? 0.5586 0.1439 0.3083 -0.0317 -0.0820 0.1245  302 EDO B C1  
8575 O  O1  . EDO J .   ? 0.3366 0.1624 0.3788 0.0240  0.0179  0.0535  302 EDO B O1  
8576 C  C2  . EDO J .   ? 0.7192 0.2117 0.2549 0.0516  0.0467  0.1620  302 EDO B C2  
8577 O  O2  . EDO J .   ? 0.2362 0.2177 0.2450 -0.0358 0.0137  0.0680  302 EDO B O2  
8578 C  C1  . PEG K .   ? 0.2627 0.0269 0.1979 0.0105  0.0860  0.0343  303 PEG B C1  
8579 O  O1  . PEG K .   ? 0.3488 0.4199 0.4120 0.0194  -0.0776 0.0303  303 PEG B O1  
8580 C  C2  . PEG K .   ? 0.2376 0.2426 0.2894 0.0743  0.1134  0.0062  303 PEG B C2  
8581 O  O2  . PEG K .   ? 0.5207 0.5505 0.3524 -0.0804 0.0862  -0.0864 303 PEG B O2  
8582 C  C3  . PEG K .   ? 0.3273 0.4493 0.4123 0.0758  0.0087  -0.0675 303 PEG B C3  
8583 C  C4  . PEG K .   ? 0.5425 0.3332 0.7282 0.0188  0.1553  0.0467  303 PEG B C4  
8584 O  O4  . PEG K .   ? 0.5962 0.4315 0.4915 -0.0847 -0.0321 0.0812  303 PEG B O4  
8585 O  O18 . 84Z L .   ? 0.2177 0.0392 0.2274 -0.0055 -0.0550 0.0217  304 84Z B O18 
8586 S  S16 . 84Z L .   ? 0.1952 0.0156 0.2530 0.0351  -0.0374 0.0061  304 84Z B S16 
8587 O  O17 . 84Z L .   ? 0.2083 0.0485 0.3148 0.0487  -0.0188 0.0146  304 84Z B O17 
8588 C  C19 . 84Z L .   ? 0.1998 0.0347 0.2944 0.0685  0.0060  -0.0320 304 84Z B C19 
8589 C  C24 . 84Z L .   ? 0.2444 0.1173 0.2259 0.0552  0.0040  -0.0074 304 84Z B C24 
8590 C  C23 . 84Z L .   ? 0.2674 0.1171 0.2918 0.0633  0.0011  -0.0595 304 84Z B C23 
8591 C  C22 . 84Z L .   ? 0.1679 0.0699 0.2789 0.0364  -0.0259 -0.0188 304 84Z B C22 
8592 C  C21 . 84Z L .   ? 0.2985 0.0229 0.3865 0.0536  0.0363  -0.0435 304 84Z B C21 
8593 C  C20 . 84Z L .   ? 0.2291 0.0215 0.2855 0.0501  -0.0082 -0.0247 304 84Z B C20 
8594 C  C3  . 84Z L .   ? 0.1728 0.0088 0.1762 0.0196  -0.0299 -0.0083 304 84Z B C3  
8595 C  C2  . 84Z L .   ? 0.2030 0.0467 0.1642 0.0260  -0.0348 -0.0135 304 84Z B C2  
8596 C  C4  . 84Z L .   ? 0.1937 0.0914 0.1197 0.0399  -0.0233 0.0118  304 84Z B C4  
8597 C  C12 . 84Z L .   ? 0.1351 0.0268 0.2324 0.0488  0.0175  0.0282  304 84Z B C12 
8598 O  O14 . 84Z L .   ? 0.1997 0.0240 0.2340 0.0196  0.0044  0.0288  304 84Z B O14 
8599 C  C15 . 84Z L .   ? 0.1528 0.1430 0.2278 0.0149  -0.0394 0.1286  304 84Z B C15 
8600 O  O13 . 84Z L .   ? 0.1367 0.1646 0.1805 0.0159  0.0015  0.0313  304 84Z B O13 
8601 C  C5  . 84Z L .   ? 0.1372 0.1114 0.1320 0.0155  -0.0751 0.0482  304 84Z B C5  
8602 C  C6  . 84Z L .   ? 0.2516 0.0113 0.1254 0.0345  0.0184  -0.0016 304 84Z B C6  
8603 C  C1  . 84Z L .   ? 0.1658 0.0113 0.1665 -0.0229 -0.0103 -0.0149 304 84Z B C1  
8604 CL CL1 . 84Z L .   ? 0.1793 0.0065 0.1868 0.0031  0.0195  -0.0044 304 84Z B CL1 
8605 S  S7  . 84Z L .   ? 0.1587 0.0085 0.1850 -0.0135 -0.0341 0.0159  304 84Z B S7  
8606 O  O8  . 84Z L .   ? 0.1379 0.0067 0.1873 -0.0024 0.0050  -0.0083 304 84Z B O8  
8607 O  O9  . 84Z L .   ? 0.1505 0.0104 0.1589 0.0180  -0.0058 0.0160  304 84Z B O9  
8608 N  N10 . 84Z L .   ? 0.0505 0.0186 0.4176 -0.0229 0.1289  -0.0704 304 84Z B N10 
8609 ZN ZN  . ZN  M .   ? 0.1611 0.0909 0.1469 -0.0425 -0.0217 0.0013  301 ZN  C ZN  
8610 C  C1  . EDO N .   ? 0.2637 0.5317 0.2175 -0.0003 0.0787  0.1045  302 EDO C C1  
8611 O  O1  . EDO N .   ? 0.2411 0.4156 0.2278 0.1130  0.0491  0.0347  302 EDO C O1  
8612 C  C2  . EDO N .   ? 0.4879 0.7260 0.1858 -0.0025 0.1087  0.1476  302 EDO C C2  
8613 O  O2  . EDO N .   ? 0.8018 0.5564 0.3225 -0.1020 -0.0578 -0.0054 302 EDO C O2  
8614 C  C1  . EDO O .   ? 0.3007 0.0767 0.3917 0.0026  0.0244  0.0620  303 EDO C C1  
8615 O  O1  . EDO O .   ? 0.3444 0.1992 0.5578 0.0472  -0.0541 0.0418  303 EDO C O1  
8616 C  C2  . EDO O .   ? 0.3152 0.0905 0.2508 -0.0122 0.0117  0.0506  303 EDO C C2  
8617 O  O2  . EDO O .   ? 0.3383 0.1625 0.3356 -0.1169 -0.0115 -0.0017 303 EDO C O2  
8618 C  C1  . EDO P .   ? 0.1861 0.5190 0.3433 0.0340  0.0036  0.0196  304 EDO C C1  
8619 O  O1  . EDO P .   ? 0.3507 0.5710 0.5003 -0.0039 0.0592  -0.0212 304 EDO C O1  
8620 C  C2  . EDO P .   ? 0.3859 0.3675 0.6483 0.0766  0.0126  -0.1265 304 EDO C C2  
8621 O  O2  . EDO P .   ? 0.2991 0.3170 0.5619 -0.0230 0.0047  0.0550  304 EDO C O2  
8622 O  O18 . 84Z Q .   ? 0.2089 0.1773 0.2749 -0.0697 -0.0863 0.0299  305 84Z C O18 
8623 S  S16 . 84Z Q .   ? 0.2019 0.1962 0.2537 -0.0970 -0.0463 -0.0037 305 84Z C S16 
8624 O  O17 . 84Z Q .   ? 0.2028 0.3481 0.3168 -0.1033 -0.0242 -0.0451 305 84Z C O17 
8625 C  C19 . 84Z Q .   ? 0.3088 0.1586 0.2639 -0.1948 -0.0618 0.0447  305 84Z C C19 
8626 C  C24 . 84Z Q .   ? 0.3169 0.2808 0.4753 -0.1423 0.0342  -0.0247 305 84Z C C24 
8627 C  C23 . 84Z Q .   ? 0.5156 0.2760 0.3441 -0.2253 -0.0696 -0.0521 305 84Z C C23 
8628 C  C22 . 84Z Q .   ? 0.3482 0.3929 0.3639 -0.2001 -0.1368 0.0216  305 84Z C C22 
8629 C  C21 . 84Z Q .   ? 0.4742 0.2085 0.4273 -0.1728 -0.1600 -0.0098 305 84Z C C21 
8630 C  C20 . 84Z Q .   ? 0.3433 0.2594 0.2933 -0.2257 -0.0573 0.0643  305 84Z C C20 
8631 C  C3  . 84Z Q .   ? 0.2419 0.0766 0.2081 -0.0900 0.0211  0.0031  305 84Z C C3  
8632 C  C2  . 84Z Q .   ? 0.1887 0.0848 0.2009 -0.0469 -0.0526 -0.0113 305 84Z C C2  
8633 C  C4  . 84Z Q .   ? 0.1663 0.1839 0.1523 -0.0785 -0.0466 0.0208  305 84Z C C4  
8634 C  C12 . 84Z Q .   ? 0.1902 0.1204 0.2528 -0.0611 -0.0272 -0.0406 305 84Z C C12 
8635 O  O14 . 84Z Q .   ? 0.2193 0.1444 0.2716 -0.0035 -0.0117 -0.0568 305 84Z C O14 
8636 C  C15 . 84Z Q .   ? 0.2480 0.1589 0.3158 -0.0042 0.0081  -0.0677 305 84Z C C15 
8637 O  O13 . 84Z Q .   ? 0.2205 0.3456 0.2356 -0.0674 0.0001  -0.0578 305 84Z C O13 
8638 C  C5  . 84Z Q .   ? 0.1898 0.1312 0.1819 -0.0450 -0.0454 -0.0144 305 84Z C C5  
8639 C  C6  . 84Z Q .   ? 0.1545 0.1094 0.1528 -0.0467 -0.0539 0.0120  305 84Z C C6  
8640 C  C1  . 84Z Q .   ? 0.1873 0.0807 0.1941 -0.0625 -0.0173 0.0107  305 84Z C C1  
8641 CL CL1 . 84Z Q .   ? 0.1814 0.1185 0.1814 -0.0217 -0.0078 0.0026  305 84Z C CL1 
8642 S  S7  . 84Z Q .   ? 0.1815 0.0715 0.1577 -0.0388 -0.0142 0.0142  305 84Z C S7  
8643 O  O8  . 84Z Q .   ? 0.1775 0.0389 0.1365 -0.0196 -0.0074 0.0153  305 84Z C O8  
8644 O  O9  . 84Z Q .   ? 0.2833 0.0708 0.0938 -0.0013 -0.0211 0.0298  305 84Z C O9  
8645 N  N10 . 84Z Q .   ? 0.2058 0.0942 0.1311 -0.0545 -0.0331 0.0311  305 84Z C N10 
8646 ZN ZN  . ZN  R .   ? 0.1547 0.0064 0.1538 -0.0001 0.0058  0.0043  301 ZN  D ZN  
8647 C  C1  . EDO S .   ? 0.2327 0.1072 0.2943 0.0469  0.0694  0.0075  302 EDO D C1  
8648 O  O1  . EDO S .   ? 0.3459 0.0965 0.3279 0.0697  0.1318  0.0736  302 EDO D O1  
8649 C  C2  . EDO S .   ? 0.2649 0.2283 0.3007 0.0901  0.0076  0.0522  302 EDO D C2  
8650 O  O2  . EDO S .   ? 0.2710 0.2903 0.3357 0.0455  0.0396  0.0388  302 EDO D O2  
8651 O  O18 . 84Z T .   ? 0.2700 0.0088 0.2626 0.0254  -0.0524 -0.0009 303 84Z D O18 
8652 S  S16 . 84Z T .   ? 0.2322 0.0198 0.2613 0.0512  -0.0212 -0.0011 303 84Z D S16 
8653 O  O17 . 84Z T .   ? 0.2640 0.0142 0.2899 0.0448  -0.0033 0.0051  303 84Z D O17 
8654 C  C19 . 84Z T .   ? 0.2358 0.0259 0.2394 0.0665  -0.0244 0.0009  303 84Z D C19 
8655 C  C24 . 84Z T .   ? 0.2839 0.0549 0.3337 0.0079  -0.0087 0.0453  303 84Z D C24 
8656 C  C23 . 84Z T .   ? 0.3110 0.0713 0.3206 -0.0217 -0.0144 0.0517  303 84Z D C23 
8657 C  C22 . 84Z T .   ? 0.2692 0.0672 0.3274 0.0284  0.0136  0.0119  303 84Z D C22 
8658 C  C21 . 84Z T .   ? 0.2804 0.0364 0.3132 0.0396  0.0356  0.0118  303 84Z D C21 
8659 C  C20 . 84Z T .   ? 0.2994 0.0485 0.2755 0.0715  -0.0050 -0.0483 303 84Z D C20 
8660 C  C3  . 84Z T .   ? 0.2157 0.0100 0.1659 0.0225  -0.0085 0.0132  303 84Z D C3  
8661 C  C2  . 84Z T .   ? 0.2178 0.0171 0.1561 0.0078  -0.0490 0.0220  303 84Z D C2  
8662 C  C4  . 84Z T .   ? 0.1790 0.1006 0.1826 0.0398  -0.0192 0.0010  303 84Z D C4  
8663 C  C12 . 84Z T .   ? 0.1631 0.0383 0.2423 0.0605  -0.0216 0.0363  303 84Z D C12 
8664 O  O14 . 84Z T .   ? 0.2555 0.0486 0.2608 -0.0055 -0.0125 0.0798  303 84Z D O14 
8665 C  C15 . 84Z T .   ? 0.2570 0.1245 0.3071 0.0166  -0.0010 0.1478  303 84Z D C15 
8666 O  O13 . 84Z T .   ? 0.2311 0.2570 0.1821 0.0457  0.0172  0.0268  303 84Z D O13 
8667 C  C5  . 84Z T .   ? 0.1552 0.0763 0.1735 0.0223  0.0211  0.0015  303 84Z D C5  
8668 C  C6  . 84Z T .   ? 0.1288 0.0082 0.2025 0.0060  0.0137  0.0182  303 84Z D C6  
8669 C  C1  . 84Z T .   ? 0.2001 0.0090 0.1956 0.0226  0.0233  0.0001  303 84Z D C1  
8670 CL CL1 . 84Z T .   ? 0.1962 0.0089 0.1829 0.0177  0.0109  -0.0117 303 84Z D CL1 
8671 S  S7  . 84Z T .   ? 0.1593 0.0072 0.1620 0.0117  0.0003  -0.0005 303 84Z D S7  
8672 O  O8  . 84Z T .   ? 0.1888 0.0415 0.1297 -0.0387 -0.0013 0.0001  303 84Z D O8  
8673 O  O9  . 84Z T .   ? 0.1874 0.0073 0.1339 0.0121  -0.0124 0.0035  303 84Z D O9  
8674 N  N10 . 84Z T .   ? 0.1940 0.0178 0.1934 -0.0350 0.0243  -0.0346 303 84Z D N10 
8675 O  O   . HOH U .   ? 0.2421 0.4156 0.8018 -0.0412 0.0732  -0.2362 401 HOH A O   
8676 O  O   . HOH U .   ? 0.3464 0.2857 0.2931 -0.0377 0.0104  -0.0664 402 HOH A O   
8677 O  O   . HOH U .   ? 0.4858 0.3226 1.0166 0.0518  -0.1668 0.2827  403 HOH A O   
8678 O  O   . HOH U .   ? 0.2857 0.3365 0.3104 0.0581  0.0936  0.0248  404 HOH A O   
8679 O  O   . HOH U .   ? 0.3642 0.1500 0.3860 0.0139  0.0013  -0.0485 405 HOH A O   
8680 O  O   . HOH U .   ? 0.7590 0.4089 0.6763 -0.2322 -0.2719 0.1067  406 HOH A O   
8681 O  O   . HOH U .   ? 0.3622 0.5152 0.3517 -0.0344 0.0287  0.1439  407 HOH A O   
8682 O  O   . HOH U .   ? 0.4386 0.8577 0.3398 -0.0611 -0.1120 0.0661  408 HOH A O   
8683 O  O   . HOH U .   ? 0.3926 0.3349 0.7426 0.0352  0.0322  0.2694  409 HOH A O   
8684 O  O   . HOH U .   ? 0.4663 0.3326 0.3257 0.0006  0.0383  0.0532  410 HOH A O   
8685 O  O   . HOH U .   ? 0.2489 0.2119 0.2919 -0.0525 0.0254  -0.0076 411 HOH A O   
8686 O  O   . HOH U .   ? 0.4190 0.3836 0.3349 -0.0642 -0.0591 -0.0151 412 HOH A O   
8687 O  O   . HOH U .   ? 0.4154 0.1712 0.4044 -0.0620 0.0740  -0.0270 413 HOH A O   
8688 O  O   . HOH U .   ? 0.6959 0.4206 0.5173 -0.0550 -0.2790 0.1259  414 HOH A O   
8689 O  O   . HOH U .   ? 0.3174 0.5572 0.5197 0.0681  -0.0425 -0.1256 415 HOH A O   
8690 O  O   . HOH U .   ? 0.3889 0.3367 0.3106 0.0941  -0.0344 0.1986  416 HOH A O   
8691 O  O   . HOH U .   ? 0.5328 0.2296 1.0468 0.0280  0.1498  0.0204  417 HOH A O   
8692 O  O   . HOH U .   ? 0.3965 0.3733 0.4160 0.0688  -0.1385 0.0798  418 HOH A O   
8693 O  O   . HOH U .   ? 0.2243 0.2705 0.1974 -0.0147 -0.0032 0.0626  419 HOH A O   
8694 O  O   . HOH U .   ? 0.5659 0.1726 0.4887 0.0684  -0.2860 -0.0278 420 HOH A O   
8695 O  O   . HOH U .   ? 0.2444 0.3764 0.3679 0.0252  0.0003  0.1166  421 HOH A O   
8696 O  O   . HOH U .   ? 0.3192 0.4044 0.3353 0.0256  -0.0538 -0.0205 422 HOH A O   
8697 O  O   . HOH U .   ? 0.6763 0.2433 0.4957 -0.1665 -0.0335 -0.0206 423 HOH A O   
8698 O  O   . HOH U .   ? 0.2132 0.1733 0.1852 -0.0406 -0.0728 -0.0172 424 HOH A O   
8699 O  O   . HOH U .   ? 0.6729 0.2019 0.4684 0.1584  0.1714  0.0826  425 HOH A O   
8700 O  O   . HOH U .   ? 0.1588 0.1107 0.2028 0.0219  -0.0179 0.0185  426 HOH A O   
8701 O  O   . HOH U .   ? 0.2052 0.6855 0.4227 0.1298  -0.0019 0.1062  427 HOH A O   
8702 O  O   . HOH U .   ? 0.6513 0.5029 0.2850 -0.0068 -0.1228 0.1644  428 HOH A O   
8703 O  O   . HOH U .   ? 0.3837 0.1179 0.6219 -0.0186 -0.0204 0.0424  429 HOH A O   
8704 O  O   . HOH U .   ? 0.3265 0.1992 0.5418 0.0982  0.0574  0.0568  430 HOH A O   
8705 O  O   . HOH U .   ? 0.4674 0.3826 0.5478 -0.0082 -0.1723 0.0259  431 HOH A O   
8706 O  O   . HOH U .   ? 0.2992 0.3228 0.2418 -0.0251 -0.0048 -0.0388 432 HOH A O   
8707 O  O   . HOH U .   ? 0.1767 0.2870 0.2365 0.0311  -0.0358 0.0976  433 HOH A O   
8708 O  O   . HOH U .   ? 0.4588 0.3131 0.3290 0.0353  -0.1782 0.0372  434 HOH A O   
8709 O  O   . HOH U .   ? 0.5384 0.3439 0.5261 0.0140  -0.0300 0.2446  435 HOH A O   
8710 O  O   . HOH U .   ? 0.2554 0.3616 0.5048 -0.1016 -0.0102 0.0736  436 HOH A O   
8711 O  O   . HOH U .   ? 0.4642 0.1778 0.5321 0.0693  0.0409  0.1223  437 HOH A O   
8712 O  O   . HOH U .   ? 0.4119 0.1894 0.4102 0.0482  -0.1338 0.0187  438 HOH A O   
8713 O  O   . HOH U .   ? 0.1762 0.2495 0.2904 0.0512  0.0185  0.0908  439 HOH A O   
8714 O  O   . HOH U .   ? 0.3445 0.2451 0.3219 0.0577  -0.0156 0.1036  440 HOH A O   
8715 O  O   . HOH U .   ? 0.4757 0.3148 0.4733 -0.1063 0.0974  -0.0877 441 HOH A O   
8716 O  O   . HOH U .   ? 0.1550 0.2955 0.2845 -0.0063 0.0019  0.1302  442 HOH A O   
8717 O  O   . HOH U .   ? 0.9338 0.3350 0.4585 0.0105  0.0599  -0.1001 443 HOH A O   
8718 O  O   . HOH U .   ? 0.2437 0.0651 0.1732 -0.0068 0.0057  0.0168  444 HOH A O   
8719 O  O   . HOH U .   ? 0.2425 0.0274 0.2379 -0.0259 -0.0403 0.0100  445 HOH A O   
8720 O  O   . HOH U .   ? 0.3923 0.2806 0.4422 -0.0325 -0.1462 -0.0560 446 HOH A O   
8721 O  O   . HOH U .   ? 0.2278 0.2766 0.2200 -0.0536 -0.0856 0.0832  447 HOH A O   
8722 O  O   . HOH U .   ? 1.0045 0.3546 0.4508 -0.1953 -0.2521 0.2251  448 HOH A O   
8723 O  O   . HOH U .   ? 0.1573 0.0800 0.1675 0.0050  -0.0168 0.0183  449 HOH A O   
8724 O  O   . HOH U .   ? 0.7334 0.4095 0.7896 -0.1901 0.2676  0.1047  450 HOH A O   
8725 O  O   . HOH U .   ? 0.3450 0.3058 0.4627 0.1762  -0.0130 0.1668  451 HOH A O   
8726 O  O   . HOH U .   ? 0.3074 0.3087 0.4233 -0.0682 -0.1900 0.0460  452 HOH A O   
8727 O  O   . HOH U .   ? 0.2600 0.3560 0.2625 -0.0324 -0.0316 0.0708  453 HOH A O   
8728 O  O   . HOH U .   ? 0.5902 0.7907 0.5783 0.1542  0.1937  0.3115  454 HOH A O   
8729 O  O   . HOH U .   ? 0.1464 0.2513 0.3009 -0.0079 -0.0128 -0.0158 455 HOH A O   
8730 O  O   . HOH U .   ? 0.1421 0.0884 0.1545 -0.0005 -0.0247 0.0198  456 HOH A O   
8731 O  O   . HOH U .   ? 0.1602 0.1078 0.1729 0.0015  0.0206  0.0222  457 HOH A O   
8732 O  O   . HOH U .   ? 0.2976 0.2328 0.3476 0.0128  -0.0690 0.0483  458 HOH A O   
8733 O  O   . HOH U .   ? 0.1791 0.0728 0.2694 0.0571  -0.0255 0.0037  459 HOH A O   
8734 O  O   . HOH U .   ? 0.2077 0.2059 0.2275 0.0326  -0.0068 -0.0738 460 HOH A O   
8735 O  O   . HOH U .   ? 0.5240 0.1984 0.3667 0.1224  -0.0133 0.0175  461 HOH A O   
8736 O  O   . HOH U .   ? 0.3021 0.5704 0.2414 0.0370  0.0019  0.1147  462 HOH A O   
8737 O  O   . HOH U .   ? 0.2997 0.1689 0.3432 0.0822  0.1126  0.0504  463 HOH A O   
8738 O  O   . HOH U .   ? 0.1703 0.0600 0.1916 0.0143  -0.0194 0.0209  464 HOH A O   
8739 O  O   . HOH U .   ? 0.2496 0.4594 0.3077 0.0285  -0.0359 0.0161  465 HOH A O   
8740 O  O   . HOH U .   ? 0.5215 0.4413 0.8889 0.1319  0.2608  -0.0199 466 HOH A O   
8741 O  O   . HOH U .   ? 0.8950 0.5097 0.3415 -0.2910 -0.2163 0.0804  467 HOH A O   
8742 O  O   . HOH U .   ? 0.2304 0.0487 0.3025 -0.0500 -0.0798 0.0271  468 HOH A O   
8743 O  O   . HOH U .   ? 0.2283 0.1940 0.3558 -0.0236 -0.0029 0.0033  469 HOH A O   
8744 O  O   . HOH U .   ? 0.4297 0.5317 0.4342 0.0030  0.0570  -0.1795 470 HOH A O   
8745 O  O   . HOH U .   ? 0.2606 0.1144 0.8345 0.0091  0.1057  0.1627  471 HOH A O   
8746 O  O   . HOH U .   ? 0.4401 0.2522 0.6301 0.1221  -0.0746 -0.1868 472 HOH A O   
8747 O  O   . HOH U .   ? 0.2335 0.2149 0.2975 0.0124  0.0238  0.0946  473 HOH A O   
8748 O  O   . HOH U .   ? 0.3895 0.4740 0.4399 -0.0593 -0.0518 -0.0350 474 HOH A O   
8749 O  O   . HOH U .   ? 0.2557 0.1564 0.3558 -0.0286 0.0243  0.0378  475 HOH A O   
8750 O  O   . HOH U .   ? 0.2311 0.6226 0.3246 0.0318  -0.0375 0.1749  476 HOH A O   
8751 O  O   . HOH U .   ? 0.2310 0.1869 0.2785 0.0403  0.0277  -0.0563 477 HOH A O   
8752 O  O   . HOH U .   ? 0.4175 0.1582 0.2751 0.0562  -0.0628 0.0456  478 HOH A O   
8753 O  O   . HOH U .   ? 0.3912 0.2833 0.6463 0.0779  0.1020  -0.0703 479 HOH A O   
8754 O  O   . HOH U .   ? 0.2381 0.1240 0.3094 0.0094  -0.0222 0.0196  480 HOH A O   
8755 O  O   . HOH U .   ? 0.4305 0.5787 0.4106 -0.0684 -0.0135 0.1237  481 HOH A O   
8756 O  O   . HOH U .   ? 0.2777 0.2531 0.2199 -0.0772 -0.0811 -0.0084 482 HOH A O   
8757 O  O   . HOH U .   ? 0.3105 0.5105 0.3459 0.0599  -0.0589 -0.0106 483 HOH A O   
8758 O  O   . HOH U .   ? 0.3004 0.2702 0.2629 0.1202  0.0609  0.1170  484 HOH A O   
8759 O  O   . HOH U .   ? 0.3595 0.2860 0.4864 -0.0255 0.0456  0.0174  485 HOH A O   
8760 O  O   . HOH U .   ? 0.2927 0.5521 0.4443 -0.0397 -0.0490 -0.0523 486 HOH A O   
8761 O  O   . HOH U .   ? 0.1415 0.0798 0.2887 -0.0081 -0.0422 0.0148  487 HOH A O   
8762 O  O   . HOH U .   ? 0.1621 0.0507 0.2535 -0.0027 -0.0361 0.0266  488 HOH A O   
8763 O  O   . HOH U .   ? 0.2586 0.3318 0.4457 0.0684  -0.0044 0.1003  489 HOH A O   
8764 O  O   . HOH U .   ? 0.5310 0.5347 0.4429 0.0966  0.2028  0.1015  490 HOH A O   
8765 O  O   . HOH U .   ? 0.2797 0.2460 0.1758 0.0020  -0.0051 0.0146  491 HOH A O   
8766 O  O   . HOH U .   ? 0.4832 0.2998 0.3549 0.0487  -0.0173 -0.0463 492 HOH A O   
8767 O  O   . HOH U .   ? 0.3015 0.6916 0.3319 0.0557  -0.0441 0.2531  493 HOH A O   
8768 O  O   . HOH U .   ? 0.4465 0.7896 0.5069 -0.1147 -0.0411 0.3955  494 HOH A O   
8769 O  O   . HOH U .   ? 0.3139 0.3976 0.4183 0.0553  0.1425  0.1775  495 HOH A O   
8770 O  O   . HOH U .   ? 0.4619 0.2418 0.3637 0.0000  0.1119  0.0859  496 HOH A O   
8771 O  O   . HOH U .   ? 0.2433 0.3397 0.5934 0.0471  -0.0669 0.0211  497 HOH A O   
8772 O  O   . HOH U .   ? 0.4692 0.2451 0.3069 -0.1330 0.0603  0.0425  498 HOH A O   
8773 O  O   . HOH U .   ? 0.2017 0.3346 0.3626 0.0370  -0.0527 -0.0178 499 HOH A O   
8774 O  O   . HOH U .   ? 0.2184 0.0505 0.1902 0.0122  0.0348  0.0239  500 HOH A O   
8775 O  O   . HOH U .   ? 0.3201 0.3855 0.2332 0.0735  -0.0075 0.0692  501 HOH A O   
8776 O  O   . HOH U .   ? 0.3180 0.0918 0.2480 -0.0156 -0.0273 0.0234  502 HOH A O   
8777 O  O   . HOH U .   ? 0.2965 0.2627 0.2601 -0.0922 0.0590  -0.0061 503 HOH A O   
8778 O  O   . HOH U .   ? 0.7655 0.2542 0.6531 0.0710  -0.3283 -0.2160 504 HOH A O   
8779 O  O   . HOH U .   ? 0.2919 0.2439 0.2410 0.0089  -0.0154 -0.0483 505 HOH A O   
8780 O  O   . HOH U .   ? 0.4708 0.5881 0.2642 0.1855  0.0220  0.1421  506 HOH A O   
8781 O  O   . HOH U .   ? 0.1967 0.0087 0.2350 -0.0111 -0.0418 0.0218  507 HOH A O   
8782 O  O   . HOH U .   ? 0.2112 0.3074 0.2543 0.0125  0.0621  0.0495  508 HOH A O   
8783 O  O   . HOH U .   ? 0.1564 0.0223 0.1753 -0.0189 -0.0064 0.0280  509 HOH A O   
8784 O  O   . HOH U .   ? 0.3086 0.2592 0.4125 0.0977  -0.0723 -0.0368 510 HOH A O   
8785 O  O   . HOH U .   ? 0.3863 0.5912 0.2340 0.1101  0.0440  0.0321  511 HOH A O   
8786 O  O   . HOH U .   ? 0.5256 0.4656 0.3680 0.1800  0.1313  0.1532  512 HOH A O   
8787 O  O   . HOH U .   ? 0.2229 0.5633 0.3394 -0.0138 0.0055  0.0657  513 HOH A O   
8788 O  O   . HOH U .   ? 0.3604 0.6358 0.4850 0.0611  -0.1135 0.2424  514 HOH A O   
8789 O  O   . HOH U .   ? 0.1180 0.0371 0.1543 0.0165  -0.0182 0.0064  515 HOH A O   
8790 O  O   . HOH U .   ? 0.3743 0.4396 0.5697 0.0185  -0.0753 -0.1447 516 HOH A O   
8791 O  O   . HOH U .   ? 0.1847 0.0075 0.2198 -0.0147 -0.0455 0.0052  517 HOH A O   
8792 O  O   . HOH U .   ? 0.2117 0.4087 0.2955 -0.0098 0.0092  -0.0850 518 HOH A O   
8793 O  O   . HOH U .   ? 0.4851 0.2520 0.5879 0.1008  -0.1373 0.0659  519 HOH A O   
8794 O  O   . HOH U .   ? 0.3083 0.3869 0.3668 -0.0141 -0.0664 0.0005  520 HOH A O   
8795 O  O   . HOH U .   ? 0.1787 0.1481 0.4255 0.0447  -0.0069 -0.0149 521 HOH A O   
8796 O  O   . HOH U .   ? 0.3231 0.2744 0.5963 -0.0212 0.0279  0.1057  522 HOH A O   
8797 O  O   . HOH U .   ? 0.4516 0.3142 0.2593 -0.1625 -0.1161 0.0037  523 HOH A O   
8798 O  O   . HOH U .   ? 0.2768 0.3042 0.2918 -0.0030 -0.0201 0.1091  524 HOH A O   
8799 O  O   . HOH U .   ? 0.2657 0.5125 0.2645 0.0276  0.0354  0.1658  525 HOH A O   
8800 O  O   . HOH U .   ? 0.6547 0.3027 0.4925 0.0647  -0.1928 -0.0263 526 HOH A O   
8801 O  O   . HOH U .   ? 0.1629 0.0336 0.1961 0.0206  -0.0094 0.0147  527 HOH A O   
8802 O  O   . HOH U .   ? 0.2567 0.4034 0.3747 -0.0379 0.0403  0.0851  528 HOH A O   
8803 O  O   . HOH U .   ? 0.3036 0.2133 0.4185 0.0237  -0.1018 -0.1018 529 HOH A O   
8804 O  O   . HOH U .   ? 0.6533 0.2608 0.2250 -0.0308 -0.1861 0.0114  530 HOH A O   
8805 O  O   . HOH U .   ? 0.4735 0.4774 0.3932 -0.1914 0.0087  -0.0688 531 HOH A O   
8806 O  O   . HOH U .   ? 0.2946 0.2653 0.2635 0.1093  -0.0968 -0.0375 532 HOH A O   
8807 O  O   . HOH U .   ? 0.3457 0.6097 0.4879 -0.0447 0.0013  -0.1364 533 HOH A O   
8808 O  O   . HOH U .   ? 0.4241 0.4579 0.3185 -0.0567 -0.0316 0.0794  534 HOH A O   
8809 O  O   . HOH U .   ? 0.1883 0.0811 0.2133 0.0250  -0.0106 0.0278  535 HOH A O   
8810 O  O   . HOH U .   ? 0.4407 0.2207 0.4362 0.1357  -0.0607 0.0233  536 HOH A O   
8811 O  O   . HOH U .   ? 0.2703 0.1828 0.2261 -0.0229 -0.0416 0.0005  537 HOH A O   
8812 O  O   . HOH U .   ? 0.2670 0.1520 0.3028 0.0273  0.0414  0.0303  538 HOH A O   
8813 O  O   . HOH U .   ? 0.3234 0.1451 0.3716 0.0259  0.0281  0.0964  539 HOH A O   
8814 O  O   . HOH U .   ? 0.3383 0.2803 0.5987 -0.0144 0.0065  -0.1294 540 HOH A O   
8815 O  O   . HOH U .   ? 0.2591 0.2099 0.2058 0.0049  -0.0674 0.0558  541 HOH A O   
8816 O  O   . HOH U .   ? 0.3104 0.2285 0.3357 0.0454  0.0432  0.1237  542 HOH A O   
8817 O  O   . HOH U .   ? 0.2696 0.3161 0.3125 0.1438  0.0630  0.0694  543 HOH A O   
8818 O  O   . HOH U .   ? 0.7803 0.5123 0.5536 -0.0147 0.0146  -0.1806 544 HOH A O   
8819 O  O   . HOH U .   ? 0.3791 0.3475 0.2755 0.1370  0.0586  0.0925  545 HOH A O   
8820 O  O   . HOH U .   ? 0.3898 0.1460 0.2327 -0.0035 -0.0899 0.0297  546 HOH A O   
8821 O  O   . HOH U .   ? 0.5042 0.2015 0.4032 -0.0108 -0.0038 0.0530  547 HOH A O   
8822 O  O   . HOH U .   ? 0.3253 0.1986 0.3142 0.1102  -0.0190 0.0696  548 HOH A O   
8823 O  O   . HOH U .   ? 0.2605 0.2549 0.4319 0.1257  -0.0080 -0.0141 549 HOH A O   
8824 O  O   . HOH U .   ? 0.4095 1.0684 0.6630 -0.2889 0.1719  -0.2370 550 HOH A O   
8825 O  O   . HOH U .   ? 0.2657 0.4305 0.3310 0.0078  -0.0653 0.0908  551 HOH A O   
8826 O  O   . HOH U .   ? 0.3599 0.2408 0.2910 -0.0268 -0.0434 0.0136  552 HOH A O   
8827 O  O   . HOH U .   ? 0.3066 0.4987 0.4183 0.0253  -0.0688 0.1574  553 HOH A O   
8828 O  O   . HOH U .   ? 0.3695 0.4092 0.4146 -0.2465 -0.0471 -0.0532 554 HOH A O   
8829 O  O   . HOH U .   ? 0.3299 0.1797 0.2275 0.0002  0.0651  0.0328  555 HOH A O   
8830 O  O   . HOH U .   ? 0.3996 0.1758 0.4153 0.1100  0.0330  0.0647  556 HOH A O   
8831 O  O   . HOH U .   ? 0.1985 0.1778 0.2524 0.0271  -0.0060 0.0728  557 HOH A O   
8832 O  O   . HOH U .   ? 0.5206 0.4573 0.7350 -0.1393 0.0566  -0.3181 558 HOH A O   
8833 O  O   . HOH U .   ? 0.3340 0.1999 0.3909 0.1089  -0.0032 0.0819  559 HOH A O   
8834 O  O   . HOH U .   ? 0.4621 0.3984 0.3893 -0.1649 0.0727  -0.0741 560 HOH A O   
8835 O  O   . HOH U .   ? 0.6815 0.2888 0.4004 0.1676  -0.1738 -0.0238 561 HOH A O   
8836 O  O   . HOH U .   ? 0.1726 0.0741 0.2477 -0.0199 -0.0544 0.0392  562 HOH A O   
8837 O  O   . HOH U .   ? 0.3765 0.1212 0.2621 -0.0182 -0.0206 0.0013  563 HOH A O   
8838 O  O   . HOH U .   ? 0.2326 0.0884 0.2124 0.0058  0.0124  0.0087  564 HOH A O   
8839 O  O   . HOH U .   ? 0.6828 0.0611 0.2307 -0.0641 0.1072  0.0166  565 HOH A O   
8840 O  O   . HOH U .   ? 0.3174 0.3154 0.2527 -0.0499 -0.0450 0.0133  566 HOH A O   
8841 O  O   . HOH U .   ? 0.3695 0.2700 0.4665 -0.0109 -0.0499 0.0520  567 HOH A O   
8842 O  O   . HOH U .   ? 0.5649 0.3926 0.3504 -0.1267 0.0817  -0.0833 568 HOH A O   
8843 O  O   . HOH U .   ? 0.3110 0.1682 0.2790 0.0114  -0.0314 -0.0105 569 HOH A O   
8844 O  O   . HOH U .   ? 0.2904 0.3931 0.3862 -0.0212 -0.1158 -0.0885 570 HOH A O   
8845 O  O   . HOH U .   ? 0.3773 0.2417 0.3847 0.1820  0.0419  0.0091  571 HOH A O   
8846 O  O   . HOH U .   ? 0.5702 0.2195 0.2833 0.1189  0.0162  0.0074  572 HOH A O   
8847 O  O   . HOH U .   ? 0.2771 0.6776 0.5443 -0.0469 -0.0598 0.0708  573 HOH A O   
8848 O  O   . HOH U .   ? 0.4441 0.2852 0.4060 0.0464  0.0154  0.0418  574 HOH A O   
8849 O  O   . HOH U .   ? 0.2572 0.2124 0.7100 0.0826  0.1247  -0.0046 575 HOH A O   
8850 O  O   . HOH U .   ? 0.2528 0.3133 0.2207 -0.0077 -0.0058 0.0223  576 HOH A O   
8851 O  O   . HOH U .   ? 0.8764 0.2594 0.3994 0.2517  0.0595  -0.0345 577 HOH A O   
8852 O  O   . HOH U .   ? 0.5772 0.2203 0.4822 -0.0378 -0.0435 -0.1057 578 HOH A O   
8853 O  O   . HOH U .   ? 0.2929 0.7207 0.2915 0.0261  -0.0124 0.2498  579 HOH A O   
8854 O  O   . HOH U .   ? 0.1313 0.2734 0.2457 0.0345  0.0036  -0.1158 580 HOH A O   
8855 O  O   . HOH U .   ? 0.4106 0.3341 0.4974 0.0119  0.0633  0.2117  581 HOH A O   
8856 O  O   . HOH U .   ? 0.3265 0.1851 0.5249 0.0403  0.0862  0.0674  582 HOH A O   
8857 O  O   . HOH U .   ? 0.4103 0.2006 0.3834 0.1436  -0.0368 -0.0474 583 HOH A O   
8858 O  O   . HOH U .   ? 0.3545 0.3941 0.4205 -0.0368 -0.0187 0.2700  584 HOH A O   
8859 O  O   . HOH U .   ? 0.4467 0.5431 0.6377 0.1585  -0.2137 -0.1900 585 HOH A O   
8860 O  O   . HOH U .   ? 0.2776 0.3809 0.2969 -0.0147 0.1034  -0.0416 586 HOH A O   
8861 O  O   . HOH U .   ? 0.5224 0.3229 0.3204 -0.1062 0.0483  -0.1601 587 HOH A O   
8862 O  O   . HOH U .   ? 0.3515 0.2400 0.2596 0.0046  -0.0480 0.0454  588 HOH A O   
8863 O  O   . HOH U .   ? 0.4084 0.1374 0.1911 0.0520  -0.0303 -0.0105 589 HOH A O   
8864 O  O   . HOH U .   ? 0.4197 0.3438 0.3290 0.1436  -0.0379 -0.0412 590 HOH A O   
8865 O  O   . HOH U .   ? 0.4609 0.3782 0.4535 -0.0187 0.0375  0.0889  591 HOH A O   
8866 O  O   . HOH U .   ? 0.4651 0.3299 0.6649 -0.1506 -0.1070 0.2377  592 HOH A O   
8867 O  O   . HOH U .   ? 0.4092 0.2163 0.3380 0.0856  -0.0480 -0.0478 593 HOH A O   
8868 O  O   . HOH U .   ? 0.2388 0.1852 0.3083 0.0344  -0.0973 0.0468  594 HOH A O   
8869 O  O   . HOH U .   ? 0.3462 0.3312 0.3130 -0.0076 -0.0800 -0.0556 595 HOH A O   
8870 O  O   . HOH U .   ? 0.3327 0.3538 0.4832 0.0526  -0.0829 0.0173  596 HOH A O   
8871 O  O   . HOH U .   ? 0.3397 0.4904 0.4365 -0.0375 -0.0099 0.1784  597 HOH A O   
8872 O  O   . HOH U .   ? 0.2444 0.0920 0.2592 0.0040  0.0168  0.0739  598 HOH A O   
8873 O  O   . HOH U .   ? 0.4291 0.4073 0.3963 0.0239  -0.0348 0.0958  599 HOH A O   
8874 O  O   . HOH U .   ? 0.2963 0.3360 0.4274 0.0620  -0.0526 0.1746  600 HOH A O   
8875 O  O   . HOH U .   ? 0.3380 0.5558 0.3348 -0.0018 0.0125  -0.0134 601 HOH A O   
8876 O  O   . HOH U .   ? 0.6848 0.2929 0.4059 0.0790  -0.0222 0.0636  602 HOH A O   
8877 O  O   . HOH U .   ? 0.4642 0.2990 0.5536 -0.0337 0.0392  -0.1141 603 HOH A O   
8878 O  O   . HOH U .   ? 0.4045 0.3385 0.4867 0.0097  0.0054  0.0189  604 HOH A O   
8879 O  O   . HOH U .   ? 0.2174 0.3098 0.3378 0.0013  0.0212  0.0198  605 HOH A O   
8880 O  O   . HOH U .   ? 0.4494 0.4824 0.3764 0.0314  -0.0348 -0.0063 606 HOH A O   
8881 O  O   . HOH U .   ? 0.4592 0.2178 0.4405 0.0023  -0.0176 0.0193  607 HOH A O   
8882 O  O   . HOH U .   ? 0.3522 0.1848 0.4642 0.0454  -0.0569 -0.0201 608 HOH A O   
8883 O  O   . HOH U .   ? 0.3327 0.2214 0.4587 -0.0152 -0.1407 -0.0440 609 HOH A O   
8884 O  O   . HOH U .   ? 0.2797 0.5592 0.2983 -0.0494 -0.0193 0.0176  610 HOH A O   
8885 O  O   . HOH U .   ? 0.5892 0.2401 0.4637 -0.0150 -0.1710 0.1316  611 HOH A O   
8886 O  O   . HOH U .   ? 0.3747 0.9014 0.5532 0.0132  0.0240  -0.2723 612 HOH A O   
8887 O  O   . HOH U .   ? 0.4928 0.3209 0.4796 -0.0351 0.0279  0.0669  613 HOH A O   
8888 O  O   . HOH U .   ? 0.7993 0.1967 0.4807 -0.1284 -0.1890 0.0240  614 HOH A O   
8889 O  O   . HOH U .   ? 0.4792 0.2725 0.3746 -0.0672 -0.1224 -0.0497 615 HOH A O   
8890 O  O   . HOH U .   ? 0.6644 0.3248 0.3353 0.0493  0.0493  -0.0346 616 HOH A O   
8891 O  O   . HOH U .   ? 0.4299 0.7842 0.2658 -0.0188 -0.0957 0.0509  617 HOH A O   
8892 O  O   . HOH U .   ? 0.3332 0.2761 0.3434 0.0639  -0.0344 0.0304  618 HOH A O   
8893 O  O   . HOH U .   ? 0.3661 0.5480 0.4799 -0.0507 -0.1429 -0.0141 619 HOH A O   
8894 O  O   . HOH U .   ? 0.3041 0.1861 0.3934 -0.0211 0.0597  -0.0672 620 HOH A O   
8895 O  O   . HOH U .   ? 0.5017 0.4828 0.5891 0.1266  0.1657  -0.1777 621 HOH A O   
8896 O  O   . HOH U .   ? 0.3667 0.2428 0.6447 -0.0253 0.0258  -0.0106 622 HOH A O   
8897 O  O   . HOH U .   ? 0.3063 0.2998 0.6339 0.0399  0.1040  0.1773  623 HOH A O   
8898 O  O   . HOH U .   ? 0.3528 0.4789 0.3218 -0.0097 0.0306  0.0591  624 HOH A O   
8899 O  O   . HOH U .   ? 0.3172 0.3475 0.2689 0.0381  0.0017  0.0451  625 HOH A O   
8900 O  O   . HOH U .   ? 0.4149 0.3882 0.8077 -0.0269 -0.1629 0.2568  626 HOH A O   
8901 O  O   . HOH U .   ? 0.8722 0.4041 0.2812 -0.0134 -0.0122 0.0820  627 HOH A O   
8902 O  O   . HOH U .   ? 0.5827 0.1751 0.4735 0.0269  -0.0297 0.1525  628 HOH A O   
8903 O  O   . HOH U .   ? 0.5700 0.2028 0.4137 0.1254  -0.0688 0.0003  629 HOH A O   
8904 O  O   . HOH U .   ? 0.3394 0.3590 0.3692 0.1136  0.0432  0.1022  630 HOH A O   
8905 O  O   . HOH U .   ? 0.4724 0.3551 0.3887 -0.0034 0.0141  0.0695  631 HOH A O   
8906 O  O   . HOH U .   ? 0.2468 0.4875 0.3200 -0.0569 -0.0534 -0.0463 632 HOH A O   
8907 O  O   . HOH U .   ? 0.5286 0.6522 0.4490 -0.1210 -0.0990 -0.1974 633 HOH A O   
8908 O  O   . HOH U .   ? 0.5041 0.3240 0.5270 -0.0262 0.2065  -0.0346 634 HOH A O   
8909 O  O   . HOH U .   ? 0.7924 1.0910 0.5888 -0.4976 0.2060  -0.3280 635 HOH A O   
8910 O  O   . HOH U .   ? 0.3709 0.3560 0.4453 0.0717  0.1309  0.1622  636 HOH A O   
8911 O  O   . HOH U .   ? 0.5871 0.3810 0.3861 -0.0148 0.0730  0.1101  637 HOH A O   
8912 O  O   . HOH U .   ? 0.4075 0.5037 0.3712 0.0350  -0.0023 0.1181  638 HOH A O   
8913 O  O   . HOH U .   ? 0.5334 0.2343 0.7209 0.1137  -0.2001 0.0171  639 HOH A O   
8914 O  O   . HOH U .   ? 0.7271 0.5182 0.3088 0.2325  -0.0268 0.0636  640 HOH A O   
8915 O  O   . HOH U .   ? 0.5241 0.7084 0.3646 0.0876  0.0454  0.2044  641 HOH A O   
8916 O  O   . HOH U .   ? 0.2687 0.0961 0.2933 -0.0267 -0.0804 -0.0052 642 HOH A O   
8917 O  O   . HOH U .   ? 0.5542 0.6439 0.3045 -0.1045 -0.1138 0.0747  643 HOH A O   
8918 O  O   . HOH U .   ? 0.4939 0.1657 0.5793 0.0463  -0.1637 0.1057  644 HOH A O   
8919 O  O   . HOH U .   ? 0.3084 0.4180 0.3746 0.1234  0.0182  0.0405  645 HOH A O   
8920 O  O   . HOH U .   ? 0.3437 0.2209 0.3001 0.1053  0.0053  0.0868  646 HOH A O   
8921 O  O   . HOH U .   ? 0.4774 0.3938 0.3904 0.0737  0.0278  0.1053  647 HOH A O   
8922 O  O   . HOH U .   ? 0.3058 0.3985 0.2937 0.0370  -0.0277 0.0340  648 HOH A O   
8923 O  O   . HOH U .   ? 0.3494 0.6639 0.3696 -0.1497 -0.0674 0.1375  649 HOH A O   
8924 O  O   . HOH U .   ? 0.3122 1.2404 0.3139 0.0974  0.0599  0.0331  650 HOH A O   
8925 O  O   . HOH U .   ? 0.6019 0.3292 0.4225 -0.1559 -0.1333 0.0495  651 HOH A O   
8926 O  O   . HOH U .   ? 0.5396 0.2107 0.6485 -0.0192 0.0079  -0.0510 652 HOH A O   
8927 O  O   . HOH U .   ? 0.4189 0.2818 0.5826 0.0702  0.0556  -0.1754 653 HOH A O   
8928 O  O   . HOH U .   ? 0.5350 0.4522 0.3843 0.1781  -0.1595 -0.2211 654 HOH A O   
8929 O  O   . HOH U .   ? 0.5228 0.4210 0.6029 0.1230  0.0796  -0.2094 655 HOH A O   
8930 O  O   . HOH U .   ? 0.5370 0.7030 0.3730 -0.1989 -0.0538 0.1615  656 HOH A O   
8931 O  O   . HOH U .   ? 0.5233 0.4259 0.3773 0.1186  0.1303  0.1333  657 HOH A O   
8932 O  O   . HOH U .   ? 0.2649 0.3429 0.3143 0.0006  0.0299  0.0800  658 HOH A O   
8933 O  O   . HOH U .   ? 0.2056 0.3740 0.2854 0.0593  -0.0341 0.1437  659 HOH A O   
8934 O  O   . HOH U .   ? 0.3571 0.6201 0.3149 -0.0534 -0.0160 0.1698  660 HOH A O   
8935 O  O   . HOH U .   ? 0.2376 0.2779 0.3622 -0.0425 0.0552  0.0701  661 HOH A O   
8936 O  O   . HOH U .   ? 0.3740 0.2289 0.5486 0.0389  0.0377  0.0947  662 HOH A O   
8937 O  O   . HOH U .   ? 0.4958 0.5093 0.6460 0.0084  -0.0607 0.1103  663 HOH A O   
8938 O  O   . HOH U .   ? 0.4155 0.1840 0.6589 0.0408  0.0996  0.1282  664 HOH A O   
8939 O  O   . HOH U .   ? 0.3085 0.1031 0.7435 -0.0776 -0.1351 0.0902  665 HOH A O   
8940 O  O   . HOH U .   ? 0.9273 0.4083 0.2370 0.1171  -0.0380 0.0307  666 HOH A O   
8941 O  O   . HOH U .   ? 0.7518 0.1676 0.4542 0.0083  -0.0955 -0.0569 667 HOH A O   
8942 O  O   . HOH U .   ? 0.3008 0.2575 0.3534 0.0282  -0.0004 0.0570  668 HOH A O   
8943 O  O   . HOH U .   ? 0.5305 0.1459 0.5816 -0.0129 -0.1524 0.0337  669 HOH A O   
8944 O  O   . HOH U .   ? 0.4860 0.2074 0.8262 0.0314  -0.0289 0.1331  670 HOH A O   
8945 O  O   . HOH U .   ? 0.4764 0.2582 0.3502 0.0153  -0.0196 0.0000  671 HOH A O   
8946 O  O   . HOH U .   ? 0.6132 0.5238 0.3867 -0.0861 -0.0042 0.1124  672 HOH A O   
8947 O  O   . HOH U .   ? 0.4120 0.2582 0.3491 0.0072  0.1333  0.0920  673 HOH A O   
8948 O  O   . HOH U .   ? 0.3122 0.6179 0.4358 0.1506  -0.0418 0.0289  674 HOH A O   
8949 O  O   . HOH U .   ? 0.6226 0.5723 0.6620 0.1903  0.0566  0.3426  675 HOH A O   
8950 O  O   . HOH U .   ? 0.5133 0.1999 0.3317 -0.0358 0.0239  0.0738  676 HOH A O   
8951 O  O   . HOH U .   ? 0.4544 0.3978 0.4654 -0.0279 0.0184  -0.0120 677 HOH A O   
8952 O  O   . HOH U .   ? 0.5438 0.6078 0.2673 0.0497  0.0351  0.0440  678 HOH A O   
8953 O  O   . HOH U .   ? 0.5525 0.5169 0.3741 0.0993  0.0372  0.0648  679 HOH A O   
8954 O  O   . HOH U .   ? 0.4659 0.3903 0.3579 -0.0263 0.0041  -0.0263 680 HOH A O   
8955 O  O   . HOH V .   ? 0.4706 0.5071 0.7082 -0.1185 0.1489  -0.1865 401 HOH B O   
8956 O  O   . HOH V .   ? 0.4935 0.3170 0.3369 0.1678  0.0970  0.1082  402 HOH B O   
8957 O  O   . HOH V .   ? 0.5024 0.3847 0.4365 0.0284  -0.0017 0.0068  403 HOH B O   
8958 O  O   . HOH V .   ? 0.3380 0.4020 0.2796 -0.0702 -0.0238 -0.0692 404 HOH B O   
8959 O  O   . HOH V .   ? 0.4281 0.3496 0.3268 -0.1047 0.0037  -0.0182 405 HOH B O   
8960 O  O   . HOH V .   ? 0.5594 0.2177 0.8455 0.0781  0.1717  0.1409  406 HOH B O   
8961 O  O   . HOH V .   ? 0.4472 0.0730 0.2803 0.0223  0.0337  0.0174  407 HOH B O   
8962 O  O   . HOH V .   ? 0.5438 0.7070 0.3077 0.0019  -0.1659 -0.1327 408 HOH B O   
8963 O  O   . HOH V .   ? 0.3051 0.2417 0.2392 0.0694  -0.0103 0.0477  409 HOH B O   
8964 O  O   . HOH V .   ? 0.3444 0.4055 0.4020 0.0631  -0.0009 0.0277  410 HOH B O   
8965 O  O   . HOH V .   ? 0.4635 0.3060 0.4650 -0.1282 -0.0978 0.0454  411 HOH B O   
8966 O  O   . HOH V .   ? 0.4008 0.2339 0.3556 -0.0089 -0.0380 0.1039  412 HOH B O   
8967 O  O   . HOH V .   ? 0.6284 0.2726 0.7253 0.0167  0.1718  0.0054  413 HOH B O   
8968 O  O   . HOH V .   ? 0.5737 0.4469 0.5488 -0.2174 -0.2042 0.2672  414 HOH B O   
8969 O  O   . HOH V .   ? 0.2185 0.2671 0.3176 -0.0036 -0.0070 -0.0406 415 HOH B O   
8970 O  O   . HOH V .   ? 0.7692 0.2354 0.6387 -0.1357 0.3869  -0.0220 416 HOH B O   
8971 O  O   . HOH V .   ? 0.4228 0.3317 0.5496 0.0009  0.0429  0.1537  417 HOH B O   
8972 O  O   . HOH V .   ? 0.4683 0.1428 0.2367 0.1432  0.0458  -0.0174 418 HOH B O   
8973 O  O   . HOH V .   ? 0.2973 0.3204 0.5220 -0.0219 -0.1991 0.0487  419 HOH B O   
8974 O  O   . HOH V .   ? 0.1979 0.0250 0.1505 0.0055  0.0244  0.0089  420 HOH B O   
8975 O  O   . HOH V .   ? 0.2825 0.2625 0.6400 -0.0954 0.0525  -0.0245 421 HOH B O   
8976 O  O   . HOH V .   ? 0.4570 0.2426 0.5976 -0.0359 0.1123  -0.0773 422 HOH B O   
8977 O  O   . HOH V .   ? 0.3560 0.4865 0.4379 -0.0474 -0.0195 0.0364  423 HOH B O   
8978 O  O   . HOH V .   ? 0.1888 0.1726 0.1699 0.0414  -0.0198 0.0134  424 HOH B O   
8979 O  O   . HOH V .   ? 0.4155 0.2361 0.6014 -0.0068 -0.1935 0.1113  425 HOH B O   
8980 O  O   . HOH V .   ? 0.6197 0.3564 0.4943 0.0993  -0.0626 0.0615  426 HOH B O   
8981 O  O   . HOH V .   ? 0.2067 0.1606 0.2935 0.0069  0.0130  -0.0664 427 HOH B O   
8982 O  O   . HOH V .   ? 0.2733 0.1690 1.0132 0.0682  0.2339  0.1935  428 HOH B O   
8983 O  O   . HOH V .   ? 0.2625 0.1197 0.2119 0.0502  -0.0429 -0.0203 429 HOH B O   
8984 O  O   . HOH V .   ? 0.2274 0.0469 0.2535 -0.0329 0.0150  -0.0247 430 HOH B O   
8985 O  O   . HOH V .   ? 0.7294 0.2667 0.4048 0.0727  0.0143  -0.0133 431 HOH B O   
8986 O  O   . HOH V .   ? 0.5260 0.3277 0.5935 -0.1518 0.1419  -0.0695 432 HOH B O   
8987 O  O   . HOH V .   ? 0.2759 0.0857 0.3510 0.0147  -0.0480 -0.0117 433 HOH B O   
8988 O  O   . HOH V .   ? 0.3639 0.2533 0.5089 0.0983  -0.1110 -0.0017 434 HOH B O   
8989 O  O   . HOH V .   ? 0.3479 0.1216 0.3441 -0.0342 -0.0364 -0.0813 435 HOH B O   
8990 O  O   . HOH V .   ? 0.3632 0.7871 0.5472 0.2172  0.1038  0.0714  436 HOH B O   
8991 O  O   . HOH V .   ? 0.3887 0.3888 0.4917 0.0685  -0.1606 -0.0043 437 HOH B O   
8992 O  O   . HOH V .   ? 0.3371 0.3403 0.5669 -0.0209 -0.0068 0.2156  438 HOH B O   
8993 O  O   . HOH V .   ? 0.2967 0.2303 0.4623 0.0594  -0.0577 -0.0552 439 HOH B O   
8994 O  O   . HOH V .   ? 0.5062 0.2139 0.4595 -0.1630 -0.0469 0.1541  440 HOH B O   
8995 O  O   . HOH V .   ? 0.1956 0.1247 0.2542 0.0175  0.0232  0.0053  441 HOH B O   
8996 O  O   . HOH V .   ? 0.5443 0.4645 0.6539 0.1983  -0.0930 0.1549  442 HOH B O   
8997 O  O   . HOH V .   ? 0.4177 0.2142 0.3855 0.1628  -0.0486 0.0046  443 HOH B O   
8998 O  O   . HOH V .   ? 0.2635 0.2360 0.3881 -0.0932 0.0464  -0.0789 444 HOH B O   
8999 O  O   . HOH V .   ? 0.3959 0.1857 0.3646 0.0021  -0.0026 0.0032  445 HOH B O   
9000 O  O   . HOH V .   ? 0.1682 0.2037 0.2155 0.0229  -0.0059 0.0461  446 HOH B O   
9001 O  O   . HOH V .   ? 1.0875 0.3269 0.3581 0.2713  0.1784  0.0572  447 HOH B O   
9002 O  O   . HOH V .   ? 0.3847 0.1701 0.2592 -0.0588 0.0824  -0.0284 448 HOH B O   
9003 O  O   . HOH V .   ? 0.3110 0.2150 0.4458 0.0943  0.0820  0.0882  449 HOH B O   
9004 O  O   . HOH V .   ? 0.3273 0.3026 0.4026 -0.0216 -0.0348 0.0631  450 HOH B O   
9005 O  O   . HOH V .   ? 0.5437 0.3022 0.5687 0.2062  0.2192  0.1480  451 HOH B O   
9006 O  O   . HOH V .   ? 0.4591 0.0717 0.4230 -0.0274 -0.0566 0.0164  452 HOH B O   
9007 O  O   . HOH V .   ? 0.2279 0.0750 0.1985 0.0259  -0.0125 0.0311  453 HOH B O   
9008 O  O   . HOH V .   ? 0.2408 0.1383 0.3570 -0.0048 -0.0310 0.0708  454 HOH B O   
9009 O  O   . HOH V .   ? 0.2972 0.1376 0.3113 0.0159  0.0303  0.0613  455 HOH B O   
9010 O  O   . HOH V .   ? 0.3162 0.4602 0.4815 -0.0089 0.0544  0.1205  456 HOH B O   
9011 O  O   . HOH V .   ? 0.2110 0.1769 0.2207 -0.0458 -0.0392 0.0421  457 HOH B O   
9012 O  O   . HOH V .   ? 0.2315 0.2720 0.3053 -0.0982 -0.0684 0.0008  458 HOH B O   
9013 O  O   . HOH V .   ? 0.3538 0.1473 0.2985 0.0856  -0.1012 -0.0665 459 HOH B O   
9014 O  O   . HOH V .   ? 0.1812 0.0325 0.1798 0.0115  -0.0301 0.0144  460 HOH B O   
9015 O  O   . HOH V .   ? 0.5216 0.1191 0.6606 0.0187  0.2470  0.0809  461 HOH B O   
9016 O  O   . HOH V .   ? 0.2343 0.0997 0.2361 -0.0076 -0.0478 0.0037  462 HOH B O   
9017 O  O   . HOH V .   ? 0.1674 0.0155 0.2140 0.0067  -0.0029 0.0428  463 HOH B O   
9018 O  O   . HOH V .   ? 0.2285 0.0365 0.2978 -0.0436 0.0347  -0.0314 464 HOH B O   
9019 O  O   . HOH V .   ? 0.2207 0.1121 0.2446 -0.0303 -0.0407 -0.0554 465 HOH B O   
9020 O  O   . HOH V .   ? 0.4788 0.5349 0.3173 0.2736  -0.1229 -0.1190 466 HOH B O   
9021 O  O   . HOH V .   ? 0.3535 0.2117 0.7869 0.0662  -0.1390 -0.0013 467 HOH B O   
9022 O  O   . HOH V .   ? 0.1464 0.0268 0.2924 -0.0215 -0.0309 -0.0120 468 HOH B O   
9023 O  O   . HOH V .   ? 0.1851 0.0406 0.1622 -0.0027 0.0069  0.0195  469 HOH B O   
9024 O  O   . HOH V .   ? 0.4656 0.5553 0.2821 -0.1129 -0.0706 0.1759  470 HOH B O   
9025 O  O   . HOH V .   ? 0.2699 0.1049 0.2498 -0.0076 0.0161  0.0111  471 HOH B O   
9026 O  O   . HOH V .   ? 0.1776 0.0776 0.2414 0.0122  -0.0365 0.0260  472 HOH B O   
9027 O  O   . HOH V .   ? 0.2707 0.1193 0.2902 -0.0063 -0.0151 -0.0563 473 HOH B O   
9028 O  O   . HOH V .   ? 0.2938 0.0611 0.2055 0.0276  0.0062  0.0194  474 HOH B O   
9029 O  O   . HOH V .   ? 0.3466 0.3142 0.4305 0.0741  -0.0599 -0.0510 475 HOH B O   
9030 O  O   . HOH V .   ? 0.4305 0.1288 0.4954 0.0413  0.1145  -0.0057 476 HOH B O   
9031 O  O   . HOH V .   ? 0.4176 0.4487 0.3338 -0.0837 0.0156  -0.2126 477 HOH B O   
9032 O  O   . HOH V .   ? 0.2132 0.1909 0.2006 -0.0584 -0.0273 0.0410  478 HOH B O   
9033 O  O   . HOH V .   ? 0.2188 0.0950 0.3115 0.0562  -0.0274 0.0092  479 HOH B O   
9034 O  O   . HOH V .   ? 0.2245 0.2681 0.3561 0.0464  -0.0780 -0.0033 480 HOH B O   
9035 O  O   . HOH V .   ? 0.3510 0.2825 0.3139 0.0055  0.0348  0.0176  481 HOH B O   
9036 O  O   . HOH V .   ? 0.3375 0.1521 0.2325 0.0373  -0.0952 -0.0034 482 HOH B O   
9037 O  O   . HOH V .   ? 0.4514 0.1367 0.5783 -0.0738 -0.2455 0.1370  483 HOH B O   
9038 O  O   . HOH V .   ? 0.2260 0.0108 0.1540 0.0306  0.0082  0.0073  484 HOH B O   
9039 O  O   . HOH V .   ? 0.2133 0.0109 0.2381 0.0306  0.0216  0.0071  485 HOH B O   
9040 O  O   . HOH V .   ? 0.2935 0.2453 0.3208 0.0124  -0.0116 -0.0682 486 HOH B O   
9041 O  O   . HOH V .   ? 0.3772 0.1209 0.7656 -0.0328 0.0384  -0.0936 487 HOH B O   
9042 O  O   . HOH V .   ? 0.1678 0.0325 0.2408 0.0077  -0.0552 -0.0124 488 HOH B O   
9043 O  O   . HOH V .   ? 0.1880 0.0261 0.2588 -0.0084 -0.0203 0.0035  489 HOH B O   
9044 O  O   . HOH V .   ? 0.2676 0.1459 0.2667 0.0153  -0.0945 -0.0105 490 HOH B O   
9045 O  O   . HOH V .   ? 0.6458 0.1782 0.3253 -0.0936 -0.1381 0.0309  491 HOH B O   
9046 O  O   . HOH V .   ? 0.2728 0.2408 0.7752 0.1166  0.1027  0.2289  492 HOH B O   
9047 O  O   . HOH V .   ? 0.5657 0.8373 0.2901 -0.0842 -0.1415 0.1307  493 HOH B O   
9048 O  O   . HOH V .   ? 0.3459 0.3700 0.3679 0.0532  -0.0239 -0.1161 494 HOH B O   
9049 O  O   . HOH V .   ? 0.2326 0.3443 0.2406 0.0517  0.0189  0.0967  495 HOH B O   
9050 O  O   . HOH V .   ? 0.1800 0.1424 0.2579 0.0041  0.0226  0.0204  496 HOH B O   
9051 O  O   . HOH V .   ? 0.2858 0.0313 0.2037 -0.0425 -0.0179 -0.0160 497 HOH B O   
9052 O  O   . HOH V .   ? 0.2722 0.1259 0.3273 -0.0518 -0.1008 -0.0131 498 HOH B O   
9053 O  O   . HOH V .   ? 0.1319 0.0341 0.1843 0.0122  -0.0074 -0.0117 499 HOH B O   
9054 O  O   . HOH V .   ? 0.2303 0.2364 0.3220 0.0131  0.0081  0.0593  500 HOH B O   
9055 O  O   . HOH V .   ? 0.2210 0.3873 0.3735 -0.0176 -0.0127 -0.0575 501 HOH B O   
9056 O  O   . HOH V .   ? 0.2261 0.1205 0.3114 0.0026  0.0372  0.0009  502 HOH B O   
9057 O  O   . HOH V .   ? 0.1582 0.0145 0.1891 -0.0234 -0.0111 0.0047  503 HOH B O   
9058 O  O   . HOH V .   ? 0.6052 0.1596 0.2741 0.1454  -0.0519 0.0118  504 HOH B O   
9059 O  O   . HOH V .   ? 0.2795 0.1049 0.2949 0.0724  -0.0167 -0.0049 505 HOH B O   
9060 O  O   . HOH V .   ? 0.5903 0.1435 0.5917 -0.0031 -0.0379 -0.1428 506 HOH B O   
9061 O  O   . HOH V .   ? 0.1879 0.0304 0.1900 -0.0247 -0.0245 0.0369  507 HOH B O   
9062 O  O   . HOH V .   ? 0.2304 0.1564 0.2187 0.0018  -0.0186 -0.0006 508 HOH B O   
9063 O  O   . HOH V .   ? 0.4231 0.1559 0.6781 0.0544  -0.1002 -0.1118 509 HOH B O   
9064 O  O   . HOH V .   ? 0.2983 0.6556 0.2380 0.0463  -0.0451 0.0049  510 HOH B O   
9065 O  O   . HOH V .   ? 0.3851 0.2467 0.3426 -0.0138 0.0442  0.0913  511 HOH B O   
9066 O  O   . HOH V .   ? 0.3344 0.0635 0.3158 -0.0238 -0.0372 0.0012  512 HOH B O   
9067 O  O   . HOH V .   ? 0.3164 0.3231 0.2818 0.0251  -0.0636 0.0660  513 HOH B O   
9068 O  O   . HOH V .   ? 0.2667 0.0826 0.2793 0.0241  -0.0211 0.0006  514 HOH B O   
9069 O  O   . HOH V .   ? 0.4626 0.2647 0.5122 0.0262  0.0414  0.1065  515 HOH B O   
9070 O  O   . HOH V .   ? 0.2913 0.0656 0.2304 -0.0921 -0.0399 0.0004  516 HOH B O   
9071 O  O   . HOH V .   ? 0.4450 0.0706 0.3492 0.0609  -0.0994 0.0023  517 HOH B O   
9072 O  O   . HOH V .   ? 0.3975 0.2451 0.3970 0.1119  -0.0109 -0.1129 518 HOH B O   
9073 O  O   . HOH V .   ? 0.1715 0.0416 0.1693 -0.0066 -0.0287 0.0285  519 HOH B O   
9074 O  O   . HOH V .   ? 0.6503 0.1694 0.2586 -0.1623 0.0873  0.0023  520 HOH B O   
9075 O  O   . HOH V .   ? 0.7201 0.0722 0.4662 0.1584  -0.0605 -0.0414 521 HOH B O   
9076 O  O   . HOH V .   ? 0.7835 0.3840 0.3609 0.3362  -0.0344 0.0924  522 HOH B O   
9077 O  O   . HOH V .   ? 0.4302 0.1805 0.3498 -0.0190 -0.0099 -0.0068 523 HOH B O   
9078 O  O   . HOH V .   ? 0.2718 0.5906 0.3596 0.0732  -0.0319 0.1258  524 HOH B O   
9079 O  O   . HOH V .   ? 0.4491 0.1708 0.4866 0.1259  0.0337  -0.0011 525 HOH B O   
9080 O  O   . HOH V .   ? 0.1958 0.0607 0.2902 -0.0046 -0.0181 -0.0233 526 HOH B O   
9081 O  O   . HOH V .   ? 0.5583 0.2308 0.3280 0.1135  -0.0416 0.0322  527 HOH B O   
9082 O  O   . HOH V .   ? 0.1268 0.0255 0.1685 -0.0073 -0.0273 -0.0005 528 HOH B O   
9083 O  O   . HOH V .   ? 0.1553 0.3817 0.8684 -0.0469 -0.1145 0.3219  529 HOH B O   
9084 O  O   . HOH V .   ? 0.1891 0.0665 0.2319 0.0167  0.0122  -0.0115 530 HOH B O   
9085 O  O   . HOH V .   ? 0.5426 0.1650 0.3703 0.1687  -0.0094 -0.0292 531 HOH B O   
9086 O  O   . HOH V .   ? 1.0757 0.2081 0.2031 0.1989  -0.0223 -0.0095 532 HOH B O   
9087 O  O   . HOH V .   ? 0.4609 0.3542 0.4477 0.0395  -0.0155 0.0325  533 HOH B O   
9088 O  O   . HOH V .   ? 0.5468 0.2760 0.6933 -0.3555 -0.1891 0.1203  534 HOH B O   
9089 O  O   . HOH V .   ? 0.2322 0.0449 0.1916 0.0016  0.0313  0.0190  535 HOH B O   
9090 O  O   . HOH V .   ? 0.4892 0.1245 0.2828 -0.0207 0.0638  -0.0328 536 HOH B O   
9091 O  O   . HOH V .   ? 0.1586 0.2322 0.3527 -0.0668 -0.0431 0.1513  537 HOH B O   
9092 O  O   . HOH V .   ? 0.1470 0.0717 0.2194 0.0212  -0.0326 0.0506  538 HOH B O   
9093 O  O   . HOH V .   ? 0.2713 0.2167 0.6394 0.1044  -0.0026 0.0134  539 HOH B O   
9094 O  O   . HOH V .   ? 0.3327 0.2042 0.3031 0.0257  -0.0115 0.0296  540 HOH B O   
9095 O  O   . HOH V .   ? 0.2672 0.0907 0.2727 -0.0122 -0.0073 0.0096  541 HOH B O   
9096 O  O   . HOH V .   ? 0.2994 0.3431 0.4262 0.1031  -0.1283 -0.1074 542 HOH B O   
9097 O  O   . HOH V .   ? 0.2123 0.1749 0.2940 0.0076  -0.0329 0.0164  543 HOH B O   
9098 O  O   . HOH V .   ? 0.3793 0.2266 0.6012 -0.0234 0.1882  0.1659  544 HOH B O   
9099 O  O   . HOH V .   ? 0.2575 0.4121 0.5714 0.0038  -0.0375 -0.2991 545 HOH B O   
9100 O  O   . HOH V .   ? 0.3437 0.1927 0.3231 0.0494  0.0220  -0.0150 546 HOH B O   
9101 O  O   . HOH V .   ? 0.1776 0.0733 0.3148 -0.0268 0.0271  0.0516  547 HOH B O   
9102 O  O   . HOH V .   ? 0.1922 0.1340 0.3931 -0.0629 -0.0089 -0.0359 548 HOH B O   
9103 O  O   . HOH V .   ? 0.1944 0.1146 0.2175 0.0509  -0.0258 0.0037  549 HOH B O   
9104 O  O   . HOH V .   ? 0.3601 0.2221 0.4166 -0.1170 -0.0181 0.0152  550 HOH B O   
9105 O  O   . HOH V .   ? 0.2854 0.1477 0.2394 -0.1137 -0.0917 0.0680  551 HOH B O   
9106 O  O   . HOH V .   ? 0.3609 0.2368 0.2789 -0.0398 -0.0273 0.0317  552 HOH B O   
9107 O  O   . HOH V .   ? 0.2189 0.1531 0.1778 0.0418  -0.0231 0.0399  553 HOH B O   
9108 O  O   . HOH V .   ? 0.4665 0.4073 0.4960 -0.1486 0.1469  -0.1583 554 HOH B O   
9109 O  O   . HOH V .   ? 0.2400 0.0343 0.2891 0.0044  -0.1057 0.0192  555 HOH B O   
9110 O  O   . HOH V .   ? 0.1999 0.2597 0.3098 0.0480  0.0212  0.0895  556 HOH B O   
9111 O  O   . HOH V .   ? 0.3086 0.1574 0.2678 0.0317  0.0172  0.0178  557 HOH B O   
9112 O  O   . HOH V .   ? 0.6420 0.4081 0.3788 -0.2746 -0.2200 0.1492  558 HOH B O   
9113 O  O   . HOH V .   ? 0.3195 0.5519 0.3804 -0.1403 -0.0034 0.1443  559 HOH B O   
9114 O  O   . HOH V .   ? 0.4893 0.1647 0.7960 -0.0088 0.1530  -0.0357 560 HOH B O   
9115 O  O   . HOH V .   ? 0.3234 0.4108 0.4061 0.0894  0.1476  0.1148  561 HOH B O   
9116 O  O   . HOH V .   ? 0.1719 0.6906 0.4255 0.0010  0.0538  -0.2525 562 HOH B O   
9117 O  O   . HOH V .   ? 0.2816 0.7180 0.4943 0.0710  0.0260  0.4792  563 HOH B O   
9118 O  O   . HOH V .   ? 0.2116 0.2291 0.3946 -0.0203 0.0933  0.0636  564 HOH B O   
9119 O  O   . HOH V .   ? 0.3524 0.3662 0.5745 0.1069  0.0032  -0.0234 565 HOH B O   
9120 O  O   . HOH V .   ? 0.1621 0.0402 0.1927 0.0115  -0.0053 -0.0107 566 HOH B O   
9121 O  O   . HOH V .   ? 1.0515 0.7647 0.4105 -0.2508 0.0302  -0.2936 567 HOH B O   
9122 O  O   . HOH V .   ? 0.3305 0.0159 0.3919 -0.0163 0.0548  -0.0544 568 HOH B O   
9123 O  O   . HOH V .   ? 0.3202 0.1291 0.2565 0.0545  -0.0983 -0.0204 569 HOH B O   
9124 O  O   . HOH V .   ? 0.4322 0.3118 0.4626 0.0413  -0.0651 0.1040  570 HOH B O   
9125 O  O   . HOH V .   ? 0.2070 0.0489 0.3541 -0.0073 0.0005  0.0009  571 HOH B O   
9126 O  O   . HOH V .   ? 0.2333 0.0656 0.1800 -0.0163 -0.0208 0.0335  572 HOH B O   
9127 O  O   . HOH V .   ? 0.4335 0.1420 0.6562 0.1036  0.1912  0.0776  573 HOH B O   
9128 O  O   . HOH V .   ? 0.3599 0.2371 0.2879 0.0818  0.0058  0.1095  574 HOH B O   
9129 O  O   . HOH V .   ? 0.2103 0.0782 0.3477 -0.0185 -0.0077 0.1089  575 HOH B O   
9130 O  O   . HOH V .   ? 0.3852 0.3386 0.4410 0.2399  0.0060  0.0787  576 HOH B O   
9131 O  O   . HOH V .   ? 0.7166 0.6452 0.3333 -0.2661 -0.0042 0.1895  577 HOH B O   
9132 O  O   . HOH V .   ? 0.4746 0.1962 0.4368 0.0666  -0.0354 -0.0765 578 HOH B O   
9133 O  O   . HOH V .   ? 0.3715 0.0534 0.4836 -0.0289 -0.0921 0.0573  579 HOH B O   
9134 O  O   . HOH V .   ? 0.2612 0.2819 0.3793 -0.0700 0.0867  -0.0351 580 HOH B O   
9135 O  O   . HOH V .   ? 0.2998 0.1063 0.3346 0.0317  -0.0444 0.0175  581 HOH B O   
9136 O  O   . HOH V .   ? 0.1439 0.0936 0.2242 0.0185  0.0034  0.0337  582 HOH B O   
9137 O  O   . HOH V .   ? 0.3455 0.2281 0.4068 -0.0454 0.0434  0.0487  583 HOH B O   
9138 O  O   . HOH V .   ? 0.2116 0.1575 0.3422 -0.0263 0.0276  -0.0119 584 HOH B O   
9139 O  O   . HOH V .   ? 0.3776 0.1243 0.3375 -0.0546 -0.0811 0.1158  585 HOH B O   
9140 O  O   . HOH V .   ? 0.2480 0.2724 0.3282 -0.0100 -0.0468 0.0856  586 HOH B O   
9141 O  O   . HOH V .   ? 0.3145 0.4684 0.7106 -0.0928 -0.1130 0.0108  587 HOH B O   
9142 O  O   . HOH V .   ? 0.3137 0.0480 0.2545 -0.0021 0.0425  0.0154  588 HOH B O   
9143 O  O   . HOH V .   ? 0.1718 0.2151 0.2279 0.0178  -0.0073 -0.0299 589 HOH B O   
9144 O  O   . HOH V .   ? 0.4537 0.2996 0.3400 0.0447  -0.0309 0.0615  590 HOH B O   
9145 O  O   . HOH V .   ? 0.4235 0.2717 0.3510 -0.1495 -0.0249 0.0092  591 HOH B O   
9146 O  O   . HOH V .   ? 0.2293 0.1036 0.2437 -0.0113 -0.0086 0.0083  592 HOH B O   
9147 O  O   . HOH V .   ? 0.4525 0.1538 0.2680 -0.0543 -0.0464 0.0217  593 HOH B O   
9148 O  O   . HOH V .   ? 0.3522 0.1099 0.2802 -0.0495 0.0659  -0.0159 594 HOH B O   
9149 O  O   . HOH V .   ? 0.4355 0.2399 0.2939 0.0015  0.0236  0.0357  595 HOH B O   
9150 O  O   . HOH V .   ? 0.2824 0.1663 0.3421 -0.1055 0.0304  0.0198  596 HOH B O   
9151 O  O   . HOH V .   ? 0.6269 0.0927 0.4370 0.1503  0.0985  0.0773  597 HOH B O   
9152 O  O   . HOH V .   ? 0.4485 0.2581 0.5028 0.0847  0.0118  0.1051  598 HOH B O   
9153 O  O   . HOH V .   ? 0.6702 0.1410 0.5467 0.1235  0.0277  -0.0467 599 HOH B O   
9154 O  O   . HOH V .   ? 0.2457 0.2430 0.2902 0.0580  0.0253  0.0639  600 HOH B O   
9155 O  O   . HOH V .   ? 0.2015 0.0911 0.3544 -0.0317 0.0301  0.0409  601 HOH B O   
9156 O  O   . HOH V .   ? 0.2764 0.0514 0.2974 -0.0058 0.0118  -0.0373 602 HOH B O   
9157 O  O   . HOH V .   ? 0.4658 0.1417 0.4966 0.1183  0.1225  0.0547  603 HOH B O   
9158 O  O   . HOH V .   ? 0.3748 0.6819 0.1954 -0.1438 -0.0827 0.0166  604 HOH B O   
9159 O  O   . HOH V .   ? 0.3750 0.1693 0.2203 0.0409  -0.0423 -0.0458 605 HOH B O   
9160 O  O   . HOH V .   ? 0.6970 0.3319 0.5034 0.2379  0.0912  0.1522  606 HOH B O   
9161 O  O   . HOH V .   ? 0.2388 0.1773 0.4300 0.0861  0.0558  0.1390  607 HOH B O   
9162 O  O   . HOH V .   ? 0.5874 0.6412 0.7534 0.3415  -0.2289 -0.2664 608 HOH B O   
9163 O  O   . HOH V .   ? 0.6296 0.1564 0.3536 -0.0889 0.0233  -0.1145 609 HOH B O   
9164 O  O   . HOH V .   ? 0.3123 0.7305 0.4791 0.0502  -0.0225 -0.0864 610 HOH B O   
9165 O  O   . HOH V .   ? 0.3840 0.3222 0.3780 0.0083  -0.0109 -0.0238 611 HOH B O   
9166 O  O   . HOH V .   ? 0.3083 0.1420 0.4096 0.0623  -0.1366 -0.0706 612 HOH B O   
9167 O  O   . HOH V .   ? 0.4559 0.3000 0.2722 0.0504  -0.0583 -0.0396 613 HOH B O   
9168 O  O   . HOH V .   ? 0.2487 0.3628 0.4544 -0.0859 -0.0249 -0.1113 614 HOH B O   
9169 O  O   . HOH V .   ? 0.3318 0.0733 0.2980 0.0763  -0.0942 -0.1029 615 HOH B O   
9170 O  O   . HOH V .   ? 0.3826 0.2737 0.4645 0.0771  -0.0988 -0.1310 616 HOH B O   
9171 O  O   . HOH V .   ? 0.4415 0.1855 0.6886 -0.0539 0.1054  -0.1344 617 HOH B O   
9172 O  O   . HOH V .   ? 0.3995 0.4413 0.4080 -0.0021 -0.0597 0.0482  618 HOH B O   
9173 O  O   . HOH V .   ? 0.5895 0.2097 0.5935 -0.1875 0.2092  -0.0474 619 HOH B O   
9174 O  O   . HOH V .   ? 0.2153 0.3617 0.2987 0.0104  0.0008  0.0241  620 HOH B O   
9175 O  O   . HOH V .   ? 0.4016 0.1166 0.3499 -0.0500 0.0603  0.0250  621 HOH B O   
9176 O  O   . HOH V .   ? 0.2868 0.2308 0.4254 0.0935  0.0572  -0.0027 622 HOH B O   
9177 O  O   . HOH V .   ? 0.4090 0.5819 0.5049 -0.0125 -0.0709 0.1577  623 HOH B O   
9178 O  O   . HOH V .   ? 0.5673 0.8010 0.2786 0.0111  -0.0024 -0.0167 624 HOH B O   
9179 O  O   . HOH V .   ? 0.2794 0.3129 0.4101 -0.0458 -0.0790 0.0288  625 HOH B O   
9180 O  O   . HOH V .   ? 0.6843 0.2230 0.3095 0.1227  -0.1753 0.0046  626 HOH B O   
9181 O  O   . HOH V .   ? 0.4067 0.2961 0.8352 -0.0631 0.0339  -0.0477 627 HOH B O   
9182 O  O   . HOH V .   ? 0.4621 0.0697 0.4242 -0.0122 -0.0076 -0.0219 628 HOH B O   
9183 O  O   . HOH V .   ? 0.5420 0.2640 0.3911 -0.2425 0.1305  -0.0589 629 HOH B O   
9184 O  O   . HOH V .   ? 0.2971 0.1640 0.4799 -0.0696 -0.1674 0.0954  630 HOH B O   
9185 O  O   . HOH V .   ? 0.3735 0.2442 0.4173 -0.0023 -0.0175 0.0450  631 HOH B O   
9186 O  O   . HOH V .   ? 0.4367 0.4623 0.7639 0.0537  0.2132  0.1865  632 HOH B O   
9187 O  O   . HOH V .   ? 0.4735 0.7662 0.3522 0.3701  -0.0680 0.0634  633 HOH B O   
9188 O  O   . HOH V .   ? 0.4264 0.5302 0.2192 -0.0554 -0.0550 0.0891  634 HOH B O   
9189 O  O   . HOH V .   ? 0.5425 0.2401 0.6280 -0.1560 0.1625  -0.1273 635 HOH B O   
9190 O  O   . HOH V .   ? 0.2067 0.5414 0.2869 0.0107  -0.0628 -0.1058 636 HOH B O   
9191 O  O   . HOH V .   ? 0.3636 0.2682 0.5582 0.0353  0.0427  0.0093  637 HOH B O   
9192 O  O   . HOH V .   ? 0.5177 0.2536 0.6803 -0.0844 -0.1322 0.0047  638 HOH B O   
9193 O  O   . HOH V .   ? 0.4859 0.1707 0.3990 0.1219  -0.1105 0.0569  639 HOH B O   
9194 O  O   . HOH V .   ? 0.4119 0.2358 0.2720 -0.0189 -0.0423 0.0483  640 HOH B O   
9195 O  O   . HOH V .   ? 0.5791 0.7432 0.6009 0.1692  -0.3561 -0.1049 641 HOH B O   
9196 O  O   . HOH V .   ? 0.4832 0.8940 0.2764 0.2992  -0.0512 -0.1178 642 HOH B O   
9197 O  O   . HOH V .   ? 0.4748 0.5853 0.6875 0.0550  0.2561  -0.0222 643 HOH B O   
9198 O  O   . HOH V .   ? 0.6718 0.8587 0.3925 -0.3395 0.0326  -0.1782 644 HOH B O   
9199 O  O   . HOH V .   ? 0.5796 0.6510 0.4141 0.2081  0.0790  -0.0584 645 HOH B O   
9200 O  O   . HOH V .   ? 0.3441 0.2372 0.4153 0.0341  0.0089  -0.0297 646 HOH B O   
9201 O  O   . HOH V .   ? 0.9186 0.1596 0.5650 -0.0285 0.2197  -0.0394 647 HOH B O   
9202 O  O   . HOH V .   ? 0.5405 0.3101 0.4331 -0.0447 -0.1547 0.0872  648 HOH B O   
9203 O  O   . HOH V .   ? 0.8305 0.1870 0.3977 -0.0167 -0.0052 0.0536  649 HOH B O   
9204 O  O   . HOH V .   ? 0.4492 0.1776 0.3622 -0.0783 -0.0606 0.1014  650 HOH B O   
9205 O  O   . HOH V .   ? 0.4133 0.2526 0.3177 -0.0067 0.0091  0.0219  651 HOH B O   
9206 O  O   . HOH V .   ? 0.6934 0.4511 0.4736 0.1246  -0.0013 0.0842  652 HOH B O   
9207 O  O   . HOH V .   ? 0.5177 0.1403 0.3048 -0.0990 -0.0307 0.1014  653 HOH B O   
9208 O  O   . HOH V .   ? 0.4633 0.5180 0.3578 0.0210  0.0410  -0.0135 654 HOH B O   
9209 O  O   . HOH V .   ? 0.2146 0.4893 0.6441 0.0297  -0.0634 0.3204  655 HOH B O   
9210 O  O   . HOH V .   ? 0.7414 0.2922 0.5168 0.0372  0.1339  -0.1277 656 HOH B O   
9211 O  O   . HOH V .   ? 0.3100 0.1119 0.3095 0.0083  -0.0042 0.0567  657 HOH B O   
9212 O  O   . HOH V .   ? 0.2408 0.6470 0.3682 -0.1279 -0.1011 0.2286  658 HOH B O   
9213 O  O   . HOH V .   ? 0.5641 0.1787 0.5601 0.1142  0.1752  0.0081  659 HOH B O   
9214 O  O   . HOH V .   ? 0.6926 0.3664 0.6962 -0.0607 -0.0625 0.2583  660 HOH B O   
9215 O  O   . HOH V .   ? 0.4762 0.2430 0.4458 0.1212  -0.0916 0.0771  661 HOH B O   
9216 O  O   . HOH V .   ? 0.4226 0.1455 0.7653 -0.0047 -0.0418 0.0427  662 HOH B O   
9217 O  O   . HOH V .   ? 0.4370 0.2679 0.5804 -0.0708 -0.0094 0.0053  663 HOH B O   
9218 O  O   . HOH V .   ? 0.3563 0.6687 0.2059 0.1600  -0.0100 -0.0383 664 HOH B O   
9219 O  O   . HOH V .   ? 0.3672 0.2407 0.5109 -0.1090 0.0493  0.0754  665 HOH B O   
9220 O  O   . HOH V .   ? 0.2569 0.2113 0.2231 -0.0044 -0.0093 0.0333  666 HOH B O   
9221 O  O   . HOH V .   ? 0.4526 0.1611 0.2715 0.0413  0.1057  0.0201  667 HOH B O   
9222 O  O   . HOH V .   ? 0.2759 0.3346 0.4347 -0.0079 0.0043  0.1073  668 HOH B O   
9223 O  O   . HOH V .   ? 0.3804 0.1509 0.3297 0.0409  0.0417  0.1042  669 HOH B O   
9224 O  O   . HOH V .   ? 0.3827 0.2522 0.6211 0.0869  -0.0570 -0.0292 670 HOH B O   
9225 O  O   . HOH V .   ? 0.6438 0.2940 0.5985 0.0933  0.0737  0.2243  671 HOH B O   
9226 O  O   . HOH V .   ? 0.4328 0.1976 0.8822 -0.0234 -0.0933 0.1001  672 HOH B O   
9227 O  O   . HOH V .   ? 0.2920 0.2139 0.3239 0.0166  -0.0751 0.0443  673 HOH B O   
9228 O  O   . HOH V .   ? 0.3705 0.2752 0.3783 0.0264  -0.1024 0.0128  674 HOH B O   
9229 O  O   . HOH V .   ? 0.4918 0.2837 0.5070 -0.1515 0.1961  -0.1264 675 HOH B O   
9230 O  O   . HOH V .   ? 0.7454 0.2297 0.7376 -0.0399 -0.1706 -0.0705 676 HOH B O   
9231 O  O   . HOH V .   ? 0.3948 0.4092 0.3349 0.1165  -0.0119 -0.0589 677 HOH B O   
9232 O  O   . HOH V .   ? 0.5623 0.2055 0.2815 -0.1338 -0.0212 0.0264  678 HOH B O   
9233 O  O   . HOH V .   ? 0.6853 0.1647 0.3404 -0.0060 -0.1118 0.0259  679 HOH B O   
9234 O  O   . HOH V .   ? 0.3740 0.2852 0.3138 -0.0156 -0.0163 0.0256  680 HOH B O   
9235 O  O   . HOH V .   ? 0.3672 0.4095 0.2860 0.1177  -0.0034 -0.0550 681 HOH B O   
9236 O  O   . HOH V .   ? 0.4260 0.2117 0.7729 -0.1113 0.1283  -0.1971 682 HOH B O   
9237 O  O   . HOH V .   ? 0.3893 0.2773 0.4151 -0.0443 -0.0798 -0.0441 683 HOH B O   
9238 O  O   . HOH V .   ? 0.5473 0.2231 0.3644 -0.1066 0.0357  0.0875  684 HOH B O   
9239 O  O   . HOH V .   ? 0.4952 0.1038 0.5899 0.0943  0.0455  0.0102  685 HOH B O   
9240 O  O   . HOH V .   ? 0.4056 0.3551 0.3283 -0.1057 -0.0534 -0.0529 686 HOH B O   
9241 O  O   . HOH V .   ? 0.4049 0.1449 0.3130 0.0936  -0.1393 -0.0376 687 HOH B O   
9242 O  O   . HOH V .   ? 0.6828 0.2162 0.6116 0.1017  0.1680  -0.0070 688 HOH B O   
9243 O  O   . HOH V .   ? 0.4074 0.3199 0.4671 -0.1092 0.1518  -0.0579 689 HOH B O   
9244 O  O   . HOH V .   ? 0.2656 0.6749 0.5037 0.0211  -0.0218 -0.1673 690 HOH B O   
9245 O  O   . HOH V .   ? 0.6150 0.1349 0.5008 0.1037  0.1920  0.0666  691 HOH B O   
9246 O  O   . HOH V .   ? 0.4101 0.3711 0.3862 0.0040  -0.0062 0.0146  692 HOH B O   
9247 O  O   . HOH V .   ? 0.3145 0.1370 0.3374 0.0533  -0.0618 0.0130  693 HOH B O   
9248 O  O   . HOH V .   ? 0.3981 0.1341 0.6281 0.0697  0.0216  0.0176  694 HOH B O   
9249 O  O   . HOH V .   ? 0.4856 0.3831 0.4113 -0.0156 -0.0039 0.0623  695 HOH B O   
9250 O  O   . HOH V .   ? 0.4234 0.5024 0.4292 0.0443  -0.0026 0.0081  696 HOH B O   
9251 O  O   . HOH V .   ? 0.5140 0.1282 0.3091 0.0719  -0.0709 0.0261  697 HOH B O   
9252 O  O   . HOH V .   ? 0.6364 0.1316 0.4678 -0.1307 -0.0031 0.0348  698 HOH B O   
9253 O  O   . HOH V .   ? 0.4461 0.3897 0.3999 -0.0570 0.0113  0.0305  699 HOH B O   
9254 O  O   . HOH V .   ? 0.2894 0.0961 0.2705 0.0124  0.0268  -0.0042 700 HOH B O   
9255 O  O   . HOH V .   ? 0.4559 0.4877 0.3705 0.1427  -0.0219 0.0653  701 HOH B O   
9256 O  O   . HOH V .   ? 0.5964 0.1890 0.5768 0.0333  0.0578  0.0029  702 HOH B O   
9257 O  O   . HOH V .   ? 0.6746 0.2814 0.3023 -0.1489 -0.1753 0.0490  703 HOH B O   
9258 O  O   . HOH V .   ? 0.4442 0.3123 0.4911 -0.0471 0.0592  -0.0010 704 HOH B O   
9259 O  O   . HOH V .   ? 0.7513 0.1908 0.2491 -0.0384 0.0044  -0.0048 705 HOH B O   
9260 O  O   . HOH V .   ? 0.5984 0.5031 0.6635 0.0664  -0.1078 0.0638  706 HOH B O   
9261 O  O   . HOH V .   ? 0.4157 0.4343 0.4242 0.0187  -0.0039 0.0023  707 HOH B O   
9262 O  O   . HOH V .   ? 0.4960 0.3130 0.7734 -0.0421 -0.1336 -0.1751 708 HOH B O   
9263 O  O   . HOH V .   ? 0.3894 1.0235 0.6161 -0.0425 -0.2168 0.1168  709 HOH B O   
9264 O  O   . HOH V .   ? 0.4160 0.4013 0.4389 -0.0428 -0.0151 0.0118  710 HOH B O   
9265 O  O   . HOH V .   ? 0.3128 0.3246 0.4184 0.0963  0.0074  0.0563  711 HOH B O   
9266 O  O   . HOH V .   ? 0.4185 0.3996 0.4218 0.0001  -0.0121 -0.0217 712 HOH B O   
9267 O  O   . HOH V .   ? 0.4479 0.4090 0.4471 -0.0231 0.0144  -0.0590 713 HOH B O   
9268 O  O   . HOH W .   ? 0.3488 0.2363 0.3416 -0.0152 0.1306  0.0149  401 HOH C O   
9269 O  O   . HOH W .   ? 1.0844 0.3205 1.0011 -0.5637 -0.3039 0.2915  402 HOH C O   
9270 O  O   . HOH W .   ? 0.4842 0.5529 0.2597 -0.2398 -0.0897 0.0337  403 HOH C O   
9271 O  O   . HOH W .   ? 0.2748 0.4405 0.2691 -0.0451 0.0498  -0.0046 404 HOH C O   
9272 O  O   . HOH W .   ? 0.2927 0.2396 1.0084 -0.0314 0.1471  -0.1151 405 HOH C O   
9273 O  O   . HOH W .   ? 0.5881 0.9707 0.7802 0.2620  0.4532  0.2658  406 HOH C O   
9274 O  O   . HOH W .   ? 0.4712 0.5800 0.3925 0.0311  -0.0955 0.1031  407 HOH C O   
9275 O  O   . HOH W .   ? 0.2899 0.6368 0.3037 -0.1214 0.0181  0.1018  408 HOH C O   
9276 O  O   . HOH W .   ? 0.2102 0.2338 0.4411 -0.0162 0.0057  -0.0605 409 HOH C O   
9277 O  O   . HOH W .   ? 0.2864 0.6081 0.4698 0.0043  0.0060  -0.0152 410 HOH C O   
9278 O  O   . HOH W .   ? 0.3514 0.2072 0.9060 0.0482  -0.1153 0.0584  411 HOH C O   
9279 O  O   . HOH W .   ? 0.3797 0.2500 0.3288 0.0552  0.0663  -0.0029 412 HOH C O   
9280 O  O   . HOH W .   ? 0.5095 0.5205 0.3616 -0.1763 -0.0105 0.0267  413 HOH C O   
9281 O  O   . HOH W .   ? 0.6523 0.2709 0.3217 -0.0569 0.0565  0.0694  414 HOH C O   
9282 O  O   . HOH W .   ? 0.2999 0.4923 0.3860 0.0129  -0.0423 -0.0265 415 HOH C O   
9283 O  O   . HOH W .   ? 0.2773 0.3893 0.4415 0.0351  0.0719  -0.0040 416 HOH C O   
9284 O  O   . HOH W .   ? 0.4048 0.4476 0.4305 0.0080  -0.0156 0.0115  417 HOH C O   
9285 O  O   . HOH W .   ? 0.3564 0.4540 0.2679 -0.0444 -0.0650 0.0678  418 HOH C O   
9286 O  O   . HOH W .   ? 0.3899 0.9628 0.2808 -0.2070 0.0068  -0.2794 419 HOH C O   
9287 O  O   . HOH W .   ? 0.2711 0.3136 0.2797 0.0898  -0.0155 -0.0559 420 HOH C O   
9288 O  O   . HOH W .   ? 0.2182 0.1512 0.1568 -0.0330 0.0006  -0.0313 421 HOH C O   
9289 O  O   . HOH W .   ? 0.1625 0.3182 1.3317 -0.1502 0.1208  -0.0623 422 HOH C O   
9290 O  O   . HOH W .   ? 0.1575 0.0620 0.1593 -0.0003 -0.0156 -0.0135 423 HOH C O   
9291 O  O   . HOH W .   ? 0.4638 0.4536 0.4314 -0.2346 -0.0884 0.0523  424 HOH C O   
9292 O  O   . HOH W .   ? 0.2554 0.1927 0.3263 -0.0660 0.0304  -0.0719 425 HOH C O   
9293 O  O   . HOH W .   ? 0.3000 0.4595 0.1818 -0.0712 -0.0403 0.0762  426 HOH C O   
9294 O  O   . HOH W .   ? 0.4232 0.6315 0.3249 0.0880  0.0057  0.2545  427 HOH C O   
9295 O  O   . HOH W .   ? 0.2060 0.3833 0.2042 0.0462  -0.0183 0.1101  428 HOH C O   
9296 O  O   . HOH W .   ? 0.3718 0.4721 0.1866 0.0314  -0.0147 0.0731  429 HOH C O   
9297 O  O   . HOH W .   ? 0.1767 0.2658 0.3297 -0.0015 -0.0175 0.0708  430 HOH C O   
9298 O  O   . HOH W .   ? 0.8308 0.1715 0.4396 0.0553  -0.3015 -0.1728 431 HOH C O   
9299 O  O   . HOH W .   ? 0.3068 0.3855 0.3496 0.0828  0.0119  0.2037  432 HOH C O   
9300 O  O   . HOH W .   ? 0.2173 0.6950 0.3740 0.0038  0.0054  0.0528  433 HOH C O   
9301 O  O   . HOH W .   ? 0.3068 0.2816 0.3444 -0.1348 0.0075  0.0923  434 HOH C O   
9302 O  O   . HOH W .   ? 0.2741 0.2840 0.3033 -0.0136 0.0145  0.0974  435 HOH C O   
9303 O  O   . HOH W .   ? 0.2125 0.1036 0.2472 0.0313  -0.0168 -0.0348 436 HOH C O   
9304 O  O   . HOH W .   ? 0.3521 0.0478 0.2177 -0.0179 -0.0019 -0.0472 437 HOH C O   
9305 O  O   . HOH W .   ? 0.8006 0.4105 0.3089 -0.0277 -0.0780 0.0707  438 HOH C O   
9306 O  O   . HOH W .   ? 0.2405 0.2006 0.1812 -0.0390 0.0043  0.0479  439 HOH C O   
9307 O  O   . HOH W .   ? 0.1830 0.4792 0.4293 -0.0346 -0.0675 0.2498  440 HOH C O   
9308 O  O   . HOH W .   ? 0.2153 0.2225 0.1987 -0.0401 -0.0717 0.0335  441 HOH C O   
9309 O  O   . HOH W .   ? 0.2005 0.0522 0.2595 0.0147  -0.0111 -0.0329 442 HOH C O   
9310 O  O   . HOH W .   ? 0.4290 0.4132 0.4774 -0.0596 -0.0952 -0.0675 443 HOH C O   
9311 O  O   . HOH W .   ? 0.7783 0.2943 0.8644 -0.1776 -0.3065 0.1699  444 HOH C O   
9312 O  O   . HOH W .   ? 0.1864 0.0832 0.1234 0.0413  0.0106  -0.0002 445 HOH C O   
9313 O  O   . HOH W .   ? 0.4568 0.2632 0.2123 0.0022  -0.0388 -0.0455 446 HOH C O   
9314 O  O   . HOH W .   ? 0.4665 0.4055 0.6556 0.1565  0.0373  0.1763  447 HOH C O   
9315 O  O   . HOH W .   ? 0.4745 0.6510 0.4745 -0.1734 0.0409  0.0128  448 HOH C O   
9316 O  O   . HOH W .   ? 0.5446 0.4582 0.4424 0.1031  0.0175  -0.0138 449 HOH C O   
9317 O  O   . HOH W .   ? 0.4271 0.2350 0.5506 -0.1456 0.0599  0.0463  450 HOH C O   
9318 O  O   . HOH W .   ? 0.4242 0.1760 0.3638 0.0144  0.0303  0.0794  451 HOH C O   
9319 O  O   . HOH W .   ? 0.2518 0.5849 0.5332 0.0402  -0.0561 0.1927  452 HOH C O   
9320 O  O   . HOH W .   ? 0.1329 0.1316 0.2204 0.0162  -0.0176 0.0369  453 HOH C O   
9321 O  O   . HOH W .   ? 0.3149 0.1399 0.4017 -0.0915 -0.1703 0.0644  454 HOH C O   
9322 O  O   . HOH W .   ? 0.4994 0.1729 0.2254 -0.1179 0.0306  0.0413  455 HOH C O   
9323 O  O   . HOH W .   ? 0.2461 0.6734 0.5446 0.0875  -0.0388 0.2268  456 HOH C O   
9324 O  O   . HOH W .   ? 0.2676 0.3692 0.3018 -0.0695 -0.0837 0.1192  457 HOH C O   
9325 O  O   . HOH W .   ? 0.4098 0.1994 0.3596 0.0488  -0.0094 -0.0332 458 HOH C O   
9326 O  O   . HOH W .   ? 0.3281 0.0835 0.2535 -0.0930 -0.0547 -0.0279 459 HOH C O   
9327 O  O   . HOH W .   ? 0.5536 0.3829 0.5425 0.1227  0.0685  0.2413  460 HOH C O   
9328 O  O   . HOH W .   ? 0.4228 0.4940 0.4936 0.1460  -0.1241 -0.0070 461 HOH C O   
9329 O  O   . HOH W .   ? 0.1733 0.0411 0.2188 0.0104  -0.0006 -0.0033 462 HOH C O   
9330 O  O   . HOH W .   ? 0.2956 0.7289 0.2468 0.0683  -0.0342 0.1158  463 HOH C O   
9331 O  O   . HOH W .   ? 0.2486 0.2597 0.4891 -0.0141 0.0245  0.0650  464 HOH C O   
9332 O  O   . HOH W .   ? 0.2872 0.6302 0.4763 -0.0595 -0.1613 0.0100  465 HOH C O   
9333 O  O   . HOH W .   ? 0.2121 0.0079 0.1937 -0.0171 -0.0019 0.0053  466 HOH C O   
9334 O  O   . HOH W .   ? 0.2655 0.5762 0.4057 0.1125  0.0403  0.0038  467 HOH C O   
9335 O  O   . HOH W .   ? 0.1518 0.1600 0.2342 0.0348  -0.0612 0.0207  468 HOH C O   
9336 O  O   . HOH W .   ? 0.3274 0.1719 0.7407 0.0652  0.0172  -0.0879 469 HOH C O   
9337 O  O   . HOH W .   ? 0.3162 0.4837 0.3412 0.0049  0.0551  0.0030  470 HOH C O   
9338 O  O   . HOH W .   ? 0.4220 0.2841 0.5619 -0.1328 -0.1038 -0.0274 471 HOH C O   
9339 O  O   . HOH W .   ? 0.4515 0.4788 0.2404 0.1790  0.1098  0.0917  472 HOH C O   
9340 O  O   . HOH W .   ? 0.2732 0.3602 0.1714 -0.0619 -0.0688 -0.0047 473 HOH C O   
9341 O  O   . HOH W .   ? 0.3488 0.4630 0.4090 0.0110  0.1135  0.1292  474 HOH C O   
9342 O  O   . HOH W .   ? 0.2113 0.2254 0.2480 0.0502  -0.0304 0.0093  475 HOH C O   
9343 O  O   . HOH W .   ? 0.2637 0.3319 0.2648 0.1397  0.0074  0.0024  476 HOH C O   
9344 O  O   . HOH W .   ? 0.2001 0.1284 0.2250 -0.0363 -0.0070 0.0027  477 HOH C O   
9345 O  O   . HOH W .   ? 0.3261 0.1365 0.2559 0.0484  -0.0534 0.0185  478 HOH C O   
9346 O  O   . HOH W .   ? 0.6257 0.5651 0.4063 -0.1742 -0.2780 0.2378  479 HOH C O   
9347 O  O   . HOH W .   ? 0.4069 0.5583 0.4138 -0.0031 -0.0899 -0.1041 480 HOH C O   
9348 O  O   . HOH W .   ? 0.4166 0.5727 0.3852 0.0589  -0.0751 0.3148  481 HOH C O   
9349 O  O   . HOH W .   ? 0.2372 0.0929 0.3752 0.0615  -0.0719 -0.0350 482 HOH C O   
9350 O  O   . HOH W .   ? 0.4918 0.1284 0.2220 0.0311  -0.1319 -0.0159 483 HOH C O   
9351 O  O   . HOH W .   ? 0.3364 0.6571 0.3704 -0.0359 -0.1241 0.2142  484 HOH C O   
9352 O  O   . HOH W .   ? 0.4494 0.2555 0.2315 -0.0758 -0.0367 0.0179  485 HOH C O   
9353 O  O   . HOH W .   ? 0.5360 0.2543 0.5654 0.1533  -0.0346 -0.0549 486 HOH C O   
9354 O  O   . HOH W .   ? 0.2314 0.4163 0.5691 -0.0027 -0.0653 -0.2296 487 HOH C O   
9355 O  O   . HOH W .   ? 0.3086 0.0814 0.5197 -0.0612 0.0097  0.0206  488 HOH C O   
9356 O  O   . HOH W .   ? 0.1531 0.0364 0.1333 0.0182  -0.0027 0.0070  489 HOH C O   
9357 O  O   . HOH W .   ? 0.4613 0.5069 0.2403 0.0305  -0.0140 -0.0861 490 HOH C O   
9358 O  O   . HOH W .   ? 0.2294 0.0086 0.2488 0.0186  0.0036  0.0136  491 HOH C O   
9359 O  O   . HOH W .   ? 0.2741 0.1943 0.4135 -0.0306 0.0436  0.1027  492 HOH C O   
9360 O  O   . HOH W .   ? 0.2987 0.1464 0.2307 0.0095  0.0089  0.0003  493 HOH C O   
9361 O  O   . HOH W .   ? 0.1610 0.1045 0.4320 -0.0069 -0.0373 -0.0620 494 HOH C O   
9362 O  O   . HOH W .   ? 0.5371 0.6438 0.3755 0.0142  -0.0094 -0.1753 495 HOH C O   
9363 O  O   . HOH W .   ? 0.2121 0.0457 0.2579 -0.0260 -0.0026 -0.0096 496 HOH C O   
9364 O  O   . HOH W .   ? 0.3669 0.4927 0.4872 -0.0247 -0.0504 0.0331  497 HOH C O   
9365 O  O   . HOH W .   ? 0.2965 0.3013 0.2769 0.0131  0.0260  0.0529  498 HOH C O   
9366 O  O   . HOH W .   ? 0.5013 0.5704 0.4396 -0.1269 0.1400  -0.1592 499 HOH C O   
9367 O  O   . HOH W .   ? 0.5191 0.2067 0.5640 -0.1538 -0.1634 0.1819  500 HOH C O   
9368 O  O   . HOH W .   ? 0.3213 0.4492 0.4534 0.0259  -0.0557 0.0488  501 HOH C O   
9369 O  O   . HOH W .   ? 0.1941 0.0780 0.1690 0.0311  -0.0093 0.0157  502 HOH C O   
9370 O  O   . HOH W .   ? 0.4875 0.3465 0.2564 -0.0653 0.0080  0.0392  503 HOH C O   
9371 O  O   . HOH W .   ? 0.2518 0.4503 0.2801 -0.0703 0.0558  0.1123  504 HOH C O   
9372 O  O   . HOH W .   ? 0.3300 0.1613 0.4873 0.1078  0.0309  0.1553  505 HOH C O   
9373 O  O   . HOH W .   ? 0.2008 0.0870 0.1640 0.0122  -0.0097 0.0004  506 HOH C O   
9374 O  O   . HOH W .   ? 0.3589 0.3830 0.2987 -0.0450 -0.0173 0.1024  507 HOH C O   
9375 O  O   . HOH W .   ? 0.3394 0.4913 0.2851 -0.1467 -0.0737 0.0805  508 HOH C O   
9376 O  O   . HOH W .   ? 0.3504 0.1456 0.1862 -0.0308 0.0445  0.0115  509 HOH C O   
9377 O  O   . HOH W .   ? 0.2841 0.7632 0.4819 -0.1929 -0.0762 0.0633  510 HOH C O   
9378 O  O   . HOH W .   ? 0.3145 0.6079 0.3638 0.0110  0.0435  0.1760  511 HOH C O   
9379 O  O   . HOH W .   ? 0.2133 0.3560 0.4212 -0.1219 -0.0970 0.0814  512 HOH C O   
9380 O  O   . HOH W .   ? 0.2590 0.2267 0.2857 0.0372  -0.0546 -0.0591 513 HOH C O   
9381 O  O   . HOH W .   ? 0.3832 0.2133 0.2037 -0.0783 -0.0820 0.0065  514 HOH C O   
9382 O  O   . HOH W .   ? 0.4570 0.0588 0.2042 -0.0592 0.0474  0.0098  515 HOH C O   
9383 O  O   . HOH W .   ? 0.2992 0.0886 0.3927 0.0458  0.0623  0.0751  516 HOH C O   
9384 O  O   . HOH W .   ? 0.3951 0.2623 0.5340 0.1269  -0.1448 0.0835  517 HOH C O   
9385 O  O   . HOH W .   ? 0.3154 0.5202 0.3093 -0.1840 -0.0990 0.1355  518 HOH C O   
9386 O  O   . HOH W .   ? 0.3224 0.3965 0.6345 -0.1995 -0.1938 0.1527  519 HOH C O   
9387 O  O   . HOH W .   ? 0.2060 0.0510 0.1963 -0.0249 -0.0264 0.0079  520 HOH C O   
9388 O  O   . HOH W .   ? 0.4710 0.9881 0.4217 0.0908  -0.1175 0.0614  521 HOH C O   
9389 O  O   . HOH W .   ? 0.3783 0.3414 0.3026 -0.1830 -0.0646 0.0055  522 HOH C O   
9390 O  O   . HOH W .   ? 0.2460 0.5747 0.4694 0.0787  0.0254  0.2661  523 HOH C O   
9391 O  O   . HOH W .   ? 0.4692 0.2900 0.3688 0.2504  0.0577  0.1134  524 HOH C O   
9392 O  O   . HOH W .   ? 0.7790 0.1103 0.3890 -0.0095 -0.1047 0.0600  525 HOH C O   
9393 O  O   . HOH W .   ? 0.2174 0.2084 0.2834 0.0133  0.0127  0.0782  526 HOH C O   
9394 O  O   . HOH W .   ? 0.6355 0.1840 0.4191 0.0009  0.0705  -0.1284 527 HOH C O   
9395 O  O   . HOH W .   ? 0.5386 0.4039 0.3696 -0.0901 0.0237  -0.2023 528 HOH C O   
9396 O  O   . HOH W .   ? 0.4875 0.3791 0.5294 -0.0579 0.1240  -0.0098 529 HOH C O   
9397 O  O   . HOH W .   ? 0.4915 0.2250 0.3234 0.1463  0.0582  -0.0167 530 HOH C O   
9398 O  O   . HOH W .   ? 0.2120 0.1959 0.2390 -0.0275 -0.0339 0.0452  531 HOH C O   
9399 O  O   . HOH W .   ? 0.5313 0.4895 0.5863 -0.0893 -0.0586 0.4206  532 HOH C O   
9400 O  O   . HOH W .   ? 0.2933 0.2525 0.2175 -0.0190 -0.0316 0.0027  533 HOH C O   
9401 O  O   . HOH W .   ? 0.2582 0.4558 0.3270 0.0330  -0.0637 0.1599  534 HOH C O   
9402 O  O   . HOH W .   ? 0.1216 0.1909 0.2224 0.0085  0.0174  -0.1273 535 HOH C O   
9403 O  O   . HOH W .   ? 0.3996 0.3783 0.4075 -0.1340 0.1057  -0.1115 536 HOH C O   
9404 O  O   . HOH W .   ? 0.3170 0.1776 0.3127 -0.1028 0.0271  0.0207  537 HOH C O   
9405 O  O   . HOH W .   ? 0.4602 0.4598 0.3753 -0.0148 -0.1465 -0.1323 538 HOH C O   
9406 O  O   . HOH W .   ? 0.3305 0.2687 0.3776 0.0136  0.0531  0.0660  539 HOH C O   
9407 O  O   . HOH W .   ? 0.5154 0.1227 0.6741 0.0785  -0.0295 0.0297  540 HOH C O   
9408 O  O   . HOH W .   ? 0.3220 0.4927 0.2638 0.0107  -0.0374 -0.0785 541 HOH C O   
9409 O  O   . HOH W .   ? 0.2196 0.1067 0.2845 0.0351  0.0006  0.0629  542 HOH C O   
9410 O  O   . HOH W .   ? 0.3005 0.4401 0.4947 0.1239  -0.0170 0.1076  543 HOH C O   
9411 O  O   . HOH W .   ? 0.5256 0.2830 0.3544 0.1165  -0.0656 -0.1273 544 HOH C O   
9412 O  O   . HOH W .   ? 0.4683 0.3016 0.2314 0.0440  -0.0040 -0.0347 545 HOH C O   
9413 O  O   . HOH W .   ? 0.3733 0.1089 0.5157 -0.0673 0.0157  0.0336  546 HOH C O   
9414 O  O   . HOH W .   ? 0.2737 0.5535 0.3786 -0.0259 0.1056  -0.0457 547 HOH C O   
9415 O  O   . HOH W .   ? 0.8531 0.7537 0.2279 0.0286  0.1624  -0.0066 548 HOH C O   
9416 O  O   . HOH W .   ? 0.3541 0.1778 0.4918 0.0156  0.0771  0.1436  549 HOH C O   
9417 O  O   . HOH W .   ? 0.4350 0.4809 0.4593 0.1439  -0.0971 0.1531  550 HOH C O   
9418 O  O   . HOH W .   ? 0.4989 0.4568 0.3637 -0.0168 0.0730  0.0658  551 HOH C O   
9419 O  O   . HOH W .   ? 0.3201 0.3513 0.2849 0.0023  -0.0561 -0.0012 552 HOH C O   
9420 O  O   . HOH W .   ? 0.4644 0.2325 0.6350 0.0065  -0.0729 0.1077  553 HOH C O   
9421 O  O   . HOH W .   ? 0.5750 0.2213 0.4693 0.0163  0.0710  -0.0900 554 HOH C O   
9422 O  O   . HOH W .   ? 0.5172 0.4030 0.2789 0.0473  0.0593  -0.0033 555 HOH C O   
9423 O  O   . HOH W .   ? 0.3592 0.4422 0.2872 0.1470  -0.0295 0.0930  556 HOH C O   
9424 O  O   . HOH W .   ? 0.4151 0.3781 0.4191 -0.0237 0.0214  0.0587  557 HOH C O   
9425 O  O   . HOH W .   ? 0.8873 0.2771 0.3784 0.0095  -0.1355 0.0076  558 HOH C O   
9426 O  O   . HOH W .   ? 0.3650 0.2789 0.2671 0.1144  0.0392  0.0546  559 HOH C O   
9427 O  O   . HOH W .   ? 0.2602 0.1578 0.2720 0.0272  -0.0965 -0.0128 560 HOH C O   
9428 O  O   . HOH W .   ? 0.5323 0.3174 0.3495 -0.0002 -0.1958 0.0260  561 HOH C O   
9429 O  O   . HOH W .   ? 0.5159 0.6294 0.5326 -0.0942 -0.2740 0.0644  562 HOH C O   
9430 O  O   . HOH W .   ? 0.3717 0.2715 0.3940 -0.0254 -0.0200 0.0109  563 HOH C O   
9431 O  O   . HOH W .   ? 0.3712 0.3437 0.6345 -0.0060 0.0510  -0.2706 564 HOH C O   
9432 O  O   . HOH W .   ? 0.2275 0.1700 0.3260 -0.0464 -0.0157 0.1031  565 HOH C O   
9433 O  O   . HOH W .   ? 0.5953 0.4895 0.8349 -0.0298 0.0916  0.0658  566 HOH C O   
9434 O  O   . HOH W .   ? 0.3700 0.7447 0.4209 -0.0617 0.0027  0.3580  567 HOH C O   
9435 O  O   . HOH W .   ? 0.3580 0.3545 0.3981 -0.0072 -0.0809 0.1207  568 HOH C O   
9436 O  O   . HOH W .   ? 0.5194 0.1615 0.5005 -0.0408 0.1406  0.0298  569 HOH C O   
9437 O  O   . HOH W .   ? 0.3940 0.8511 0.9047 0.0392  -0.0678 0.1474  570 HOH C O   
9438 O  O   . HOH W .   ? 0.9575 0.7643 0.4046 0.3345  0.0558  -0.1691 571 HOH C O   
9439 O  O   . HOH W .   ? 0.3067 0.4098 0.5531 -0.0647 -0.0716 0.0163  572 HOH C O   
9440 O  O   . HOH W .   ? 0.2110 0.4921 0.2730 0.1215  0.0022  0.0118  573 HOH C O   
9441 O  O   . HOH W .   ? 0.4674 0.2253 0.4156 0.0040  0.0133  -0.0330 574 HOH C O   
9442 O  O   . HOH W .   ? 0.4995 0.2117 0.4585 0.1212  -0.0548 0.0145  575 HOH C O   
9443 O  O   . HOH W .   ? 0.4315 0.5482 0.7641 -0.1322 0.1637  0.0008  576 HOH C O   
9444 O  O   . HOH W .   ? 0.6151 0.8677 0.3705 -0.0498 0.0712  0.1580  577 HOH C O   
9445 O  O   . HOH W .   ? 0.4625 0.4247 0.3879 -0.1406 -0.1949 0.0336  578 HOH C O   
9446 O  O   . HOH W .   ? 0.5632 0.1746 0.6667 -0.0640 -0.2545 0.0616  579 HOH C O   
9447 O  O   . HOH W .   ? 0.3609 0.5662 0.2552 -0.0994 -0.0155 0.0414  580 HOH C O   
9448 O  O   . HOH W .   ? 0.3735 0.7286 0.3154 0.1733  -0.1091 0.0316  581 HOH C O   
9449 O  O   . HOH W .   ? 0.4906 0.2055 0.3418 0.0992  0.0403  0.0027  582 HOH C O   
9450 O  O   . HOH W .   ? 0.3934 0.1901 0.3981 -0.0184 -0.0052 0.0318  583 HOH C O   
9451 O  O   . HOH W .   ? 0.4020 0.3985 0.4345 0.0396  0.0266  0.0498  584 HOH C O   
9452 O  O   . HOH W .   ? 0.2972 0.2755 0.8510 -0.0995 -0.0853 0.2263  585 HOH C O   
9453 O  O   . HOH W .   ? 0.3219 0.6569 0.4672 0.0059  0.0611  0.1920  586 HOH C O   
9454 O  O   . HOH W .   ? 0.3860 0.3711 0.4735 -0.0310 -0.0832 0.0212  587 HOH C O   
9455 O  O   . HOH W .   ? 0.3574 0.0812 0.2916 -0.0163 -0.0741 -0.0270 588 HOH C O   
9456 O  O   . HOH W .   ? 0.4670 1.0103 0.2876 -0.1932 -0.0851 0.0791  589 HOH C O   
9457 O  O   . HOH W .   ? 0.3659 0.2109 0.5324 0.0732  -0.0124 -0.1550 590 HOH C O   
9458 O  O   . HOH W .   ? 0.2866 0.6182 0.4202 -0.0098 -0.0429 -0.0881 591 HOH C O   
9459 O  O   . HOH W .   ? 0.3247 0.8678 0.5343 -0.1993 -0.1107 0.1031  592 HOH C O   
9460 O  O   . HOH W .   ? 0.4723 0.4412 0.4404 0.0456  -0.0392 0.0648  593 HOH C O   
9461 O  O   . HOH W .   ? 0.4390 0.3606 0.4550 0.0400  0.0091  0.1066  594 HOH C O   
9462 O  O   . HOH W .   ? 0.4644 0.3070 0.4106 0.0027  0.0011  -0.0008 595 HOH C O   
9463 O  O   . HOH W .   ? 0.4615 0.4846 0.4760 0.0461  0.1127  -0.0189 596 HOH C O   
9464 O  O   . HOH W .   ? 0.3025 0.4606 0.3926 0.0136  -0.0497 0.0462  597 HOH C O   
9465 O  O   . HOH W .   ? 0.6041 0.6500 0.3104 -0.2292 -0.0908 0.0653  598 HOH C O   
9466 O  O   . HOH W .   ? 0.8151 0.3066 0.3945 0.2258  0.0630  -0.0079 599 HOH C O   
9467 O  O   . HOH W .   ? 0.4626 0.8154 0.5140 0.2151  -0.1932 -0.4189 600 HOH C O   
9468 O  O   . HOH W .   ? 0.4238 0.2809 0.2900 0.0272  0.0641  0.0136  601 HOH C O   
9469 O  O   . HOH W .   ? 0.6573 0.1847 0.9633 -0.0215 0.0435  0.0190  602 HOH C O   
9470 O  O   . HOH W .   ? 0.3995 0.2845 0.5373 0.0572  0.1609  0.0895  603 HOH C O   
9471 O  O   . HOH W .   ? 0.2547 0.4257 0.5177 -0.0143 0.0231  0.1837  604 HOH C O   
9472 O  O   . HOH W .   ? 0.4375 0.5103 0.5711 -0.0328 -0.0471 0.0182  605 HOH C O   
9473 O  O   . HOH W .   ? 0.3712 0.5047 0.4622 -0.0774 -0.0675 0.0350  606 HOH C O   
9474 O  O   . HOH W .   ? 0.4943 0.4145 0.5916 -0.0397 -0.1960 0.0257  607 HOH C O   
9475 O  O   . HOH W .   ? 0.3098 0.0832 0.8150 -0.1105 -0.0389 0.0992  608 HOH C O   
9476 O  O   . HOH W .   ? 0.3285 1.0712 0.3459 -0.0871 -0.0491 0.1161  609 HOH C O   
9477 O  O   . HOH W .   ? 0.3538 0.2825 0.4644 -0.0291 -0.0044 -0.1260 610 HOH C O   
9478 O  O   . HOH W .   ? 0.5806 0.4903 0.2454 0.3027  0.0313  0.0702  611 HOH C O   
9479 O  O   . HOH W .   ? 0.9769 0.3754 0.2370 0.1446  0.0131  -0.0206 612 HOH C O   
9480 O  O   . HOH W .   ? 0.4408 0.3844 0.4346 -0.0105 0.0030  0.0553  613 HOH C O   
9481 O  O   . HOH W .   ? 0.3254 0.3632 0.4268 0.1152  0.0952  0.0883  614 HOH C O   
9482 O  O   . HOH W .   ? 0.4099 0.1444 0.7422 -0.0381 -0.2322 0.0502  615 HOH C O   
9483 O  O   . HOH W .   ? 0.4982 0.3194 0.4627 -0.0568 -0.0519 -0.0410 616 HOH C O   
9484 O  O   . HOH W .   ? 0.3757 0.5829 0.5564 0.1837  -0.0425 0.0229  617 HOH C O   
9485 O  O   . HOH W .   ? 0.6258 0.2549 0.5522 -0.0566 0.1778  -0.0803 618 HOH C O   
9486 O  O   . HOH W .   ? 0.4096 0.5684 0.3642 0.1515  -0.0310 0.0697  619 HOH C O   
9487 O  O   . HOH W .   ? 0.7219 0.3301 0.2980 0.2077  0.1256  0.1203  620 HOH C O   
9488 O  O   . HOH W .   ? 0.4336 0.3609 0.4407 -0.0159 0.0513  -0.0042 621 HOH C O   
9489 O  O   . HOH X .   ? 0.3883 0.6439 0.3181 0.1974  -0.0366 -0.0206 401 HOH D O   
9490 O  O   . HOH X .   ? 0.3186 0.1958 0.2315 0.0741  0.0284  0.0596  402 HOH D O   
9491 O  O   . HOH X .   ? 0.3961 0.0870 0.6452 0.0286  -0.0391 -0.0410 403 HOH D O   
9492 O  O   . HOH X .   ? 0.2702 0.1082 0.3398 0.0644  0.0201  0.0326  404 HOH D O   
9493 O  O   . HOH X .   ? 0.6403 0.2548 0.5770 -0.1751 0.0917  0.0343  405 HOH D O   
9494 O  O   . HOH X .   ? 0.4304 0.4353 0.3872 0.0069  -0.0217 -0.0036 406 HOH D O   
9495 O  O   . HOH X .   ? 0.4062 0.3850 0.7555 -0.1845 -0.2640 0.2524  407 HOH D O   
9496 O  O   . HOH X .   ? 0.5147 0.3690 0.3240 0.1336  -0.0021 -0.0895 408 HOH D O   
9497 O  O   . HOH X .   ? 0.3021 0.2028 0.3981 -0.0664 -0.0480 -0.0696 409 HOH D O   
9498 O  O   . HOH X .   ? 0.6675 0.1639 0.5059 -0.0131 -0.1920 0.0055  410 HOH D O   
9499 O  O   . HOH X .   ? 0.3672 0.2900 0.8794 -0.0407 -0.1330 0.2415  411 HOH D O   
9500 O  O   . HOH X .   ? 0.6190 0.9847 0.2814 0.1951  0.0582  0.1706  412 HOH D O   
9501 O  O   . HOH X .   ? 0.2315 0.1185 0.2286 -0.0166 -0.0403 -0.0140 413 HOH D O   
9502 O  O   . HOH X .   ? 0.3376 0.3423 0.4592 0.1328  -0.2002 -0.0237 414 HOH D O   
9503 O  O   . HOH X .   ? 0.2502 0.1311 0.4313 -0.0175 -0.0801 -0.0105 415 HOH D O   
9504 O  O   . HOH X .   ? 0.2495 0.1609 0.3441 0.0677  0.0163  -0.0033 416 HOH D O   
9505 O  O   . HOH X .   ? 0.5250 0.3652 0.4758 -0.0019 0.2693  0.0581  417 HOH D O   
9506 O  O   . HOH X .   ? 0.3481 0.2192 0.3740 0.1470  -0.0576 -0.1179 418 HOH D O   
9507 O  O   . HOH X .   ? 0.2764 0.2368 0.4859 0.0751  -0.0364 -0.0502 419 HOH D O   
9508 O  O   . HOH X .   ? 0.4970 0.1581 0.1999 0.1468  -0.0385 -0.0323 420 HOH D O   
9509 O  O   . HOH X .   ? 0.7224 0.2473 0.5043 0.1656  -0.2584 -0.0098 421 HOH D O   
9510 O  O   . HOH X .   ? 0.3940 0.2790 0.5732 -0.0921 -0.0816 -0.0961 422 HOH D O   
9511 O  O   . HOH X .   ? 0.4135 0.2634 0.6233 0.0451  -0.1531 0.0596  423 HOH D O   
9512 O  O   . HOH X .   ? 0.4931 0.1671 0.5924 -0.0734 -0.2829 0.1529  424 HOH D O   
9513 O  O   . HOH X .   ? 0.5649 0.1664 0.3475 0.0105  0.0132  0.0111  425 HOH D O   
9514 O  O   . HOH X .   ? 0.2749 0.0771 0.2715 -0.0311 0.0464  0.0369  426 HOH D O   
9515 O  O   . HOH X .   ? 0.2064 0.0074 0.1718 0.0021  0.0239  -0.0103 427 HOH D O   
9516 O  O   . HOH X .   ? 0.4825 0.2807 0.3940 0.0402  0.1309  -0.1162 428 HOH D O   
9517 O  O   . HOH X .   ? 0.4607 0.7217 0.4643 -0.3309 -0.1575 0.2922  429 HOH D O   
9518 O  O   . HOH X .   ? 0.6052 0.1069 0.7585 0.0407  0.1650  0.0190  430 HOH D O   
9519 O  O   . HOH X .   ? 0.4163 0.3532 0.3664 0.0590  0.0605  -0.0198 431 HOH D O   
9520 O  O   . HOH X .   ? 0.4774 0.4394 0.6991 0.0326  0.2365  0.1855  432 HOH D O   
9521 O  O   . HOH X .   ? 0.4498 0.6483 0.7025 -0.3459 0.1576  -0.1652 433 HOH D O   
9522 O  O   . HOH X .   ? 0.3356 0.2872 0.7817 0.1246  -0.1636 -0.1593 434 HOH D O   
9523 O  O   . HOH X .   ? 0.4263 0.1360 0.7866 -0.0558 0.0044  0.0074  435 HOH D O   
9524 O  O   . HOH X .   ? 0.5274 0.1775 0.2822 -0.0005 0.0970  0.0164  436 HOH D O   
9525 O  O   . HOH X .   ? 0.2907 0.0819 0.2517 0.0502  -0.0188 0.0044  437 HOH D O   
9526 O  O   . HOH X .   ? 0.3915 0.4260 0.3407 0.1094  0.0089  0.1190  438 HOH D O   
9527 O  O   . HOH X .   ? 0.4123 0.0560 0.3371 -0.0089 -0.0763 -0.0317 439 HOH D O   
9528 O  O   . HOH X .   ? 0.3290 0.1622 0.2500 -0.0179 -0.0643 -0.0194 440 HOH D O   
9529 O  O   . HOH X .   ? 0.2308 0.1478 0.2924 0.0657  -0.0449 -0.0357 441 HOH D O   
9530 O  O   . HOH X .   ? 0.5426 0.5102 0.3032 -0.0084 -0.0119 0.1631  442 HOH D O   
9531 O  O   . HOH X .   ? 0.4099 0.1254 0.3830 0.0366  0.0653  0.1036  443 HOH D O   
9532 O  O   . HOH X .   ? 0.4382 0.2225 0.5116 -0.0124 0.0732  0.0078  444 HOH D O   
9533 O  O   . HOH X .   ? 0.5347 0.0811 0.4731 0.0357  0.1773  -0.0280 445 HOH D O   
9534 O  O   . HOH X .   ? 0.6070 0.2121 0.4652 -0.0811 -0.0934 0.0646  446 HOH D O   
9535 O  O   . HOH X .   ? 0.4801 0.2462 0.5033 0.0254  0.1040  -0.0059 447 HOH D O   
9536 O  O   . HOH X .   ? 0.2855 0.0565 0.2290 0.0231  -0.0359 0.0392  448 HOH D O   
9537 O  O   . HOH X .   ? 0.2915 1.0506 0.3025 -0.0621 0.1067  -0.0339 449 HOH D O   
9538 O  O   . HOH X .   ? 0.3240 0.1056 0.5671 -0.0405 0.0644  -0.1318 450 HOH D O   
9539 O  O   . HOH X .   ? 0.4314 0.2634 0.4221 0.0262  -0.2172 0.0745  451 HOH D O   
9540 O  O   . HOH X .   ? 0.4357 0.1876 0.3004 -0.0022 -0.0252 0.0060  452 HOH D O   
9541 O  O   . HOH X .   ? 0.3017 0.1374 0.9318 -0.0027 -0.0379 0.0341  453 HOH D O   
9542 O  O   . HOH X .   ? 0.3934 0.3063 0.7264 0.0386  0.1609  0.2128  454 HOH D O   
9543 O  O   . HOH X .   ? 0.2216 0.5519 0.3877 -0.0047 0.0105  0.0321  455 HOH D O   
9544 O  O   . HOH X .   ? 0.3164 0.1379 0.3317 -0.0064 -0.0230 -0.0133 456 HOH D O   
9545 O  O   . HOH X .   ? 0.2533 0.1083 0.3873 -0.0002 -0.0530 0.0019  457 HOH D O   
9546 O  O   . HOH X .   ? 0.6451 0.3134 0.4613 -0.1172 -0.2259 0.1468  458 HOH D O   
9547 O  O   . HOH X .   ? 0.1909 0.0369 0.2135 0.0072  -0.0401 -0.0175 459 HOH D O   
9548 O  O   . HOH X .   ? 0.2948 0.1223 0.4995 0.0036  -0.1180 0.0615  460 HOH D O   
9549 O  O   . HOH X .   ? 0.3400 0.0712 0.4264 -0.0409 -0.0142 -0.0600 461 HOH D O   
9550 O  O   . HOH X .   ? 0.2212 0.0601 0.1639 -0.0085 0.0117  -0.0005 462 HOH D O   
9551 O  O   . HOH X .   ? 0.4613 0.3171 0.3984 0.0740  0.0052  0.0596  463 HOH D O   
9552 O  O   . HOH X .   ? 0.9263 0.3827 0.3075 -0.2344 -0.1649 0.1372  464 HOH D O   
9553 O  O   . HOH X .   ? 0.2590 0.0565 0.5314 0.0027  -0.0175 0.0385  465 HOH D O   
9554 O  O   . HOH X .   ? 0.2442 0.1254 0.2083 0.0695  -0.0424 -0.0074 466 HOH D O   
9555 O  O   . HOH X .   ? 0.1857 0.0979 0.2121 -0.0144 0.0370  0.0078  467 HOH D O   
9556 O  O   . HOH X .   ? 0.2286 0.3517 0.2425 0.0983  -0.0193 0.0186  468 HOH D O   
9557 O  O   . HOH X .   ? 0.5118 0.6208 0.3022 -0.2042 0.0350  -0.0968 469 HOH D O   
9558 O  O   . HOH X .   ? 0.3413 0.1187 0.3100 0.0674  -0.0957 -0.0226 470 HOH D O   
9559 O  O   . HOH X .   ? 0.2128 0.0663 0.4005 0.0043  0.0271  0.1146  471 HOH D O   
9560 O  O   . HOH X .   ? 0.7469 0.4745 0.2241 0.2637  0.0461  0.0036  472 HOH D O   
9561 O  O   . HOH X .   ? 0.2721 0.0976 0.2200 -0.0055 0.0117  0.0049  473 HOH D O   
9562 O  O   . HOH X .   ? 0.1785 0.0656 0.3181 -0.0231 0.0110  -0.0290 474 HOH D O   
9563 O  O   . HOH X .   ? 0.2224 0.1909 0.2423 -0.0411 0.0141  0.0469  475 HOH D O   
9564 O  O   . HOH X .   ? 0.2236 0.2367 0.2375 -0.0319 -0.0490 0.0375  476 HOH D O   
9565 O  O   . HOH X .   ? 0.8373 0.1087 0.2741 -0.0096 -0.0933 -0.0403 477 HOH D O   
9566 O  O   . HOH X .   ? 0.3125 0.2978 0.5267 -0.0754 0.1241  -0.0033 478 HOH D O   
9567 O  O   . HOH X .   ? 0.1740 0.0250 0.1762 0.0039  0.0116  -0.0158 479 HOH D O   
9568 O  O   . HOH X .   ? 0.3151 0.4626 0.7953 -0.0092 -0.0265 -0.3556 480 HOH D O   
9569 O  O   . HOH X .   ? 0.4916 0.1185 0.3990 -0.0225 0.0019  0.0208  481 HOH D O   
9570 O  O   . HOH X .   ? 0.1922 0.0072 0.1998 0.0109  0.0299  0.0083  482 HOH D O   
9571 O  O   . HOH X .   ? 0.2088 0.1467 0.2361 0.0155  -0.0362 -0.0055 483 HOH D O   
9572 O  O   . HOH X .   ? 0.4080 0.2008 0.4090 0.0925  -0.1145 0.0195  484 HOH D O   
9573 O  O   . HOH X .   ? 0.2982 0.2171 0.3937 0.0273  -0.0548 0.0844  485 HOH D O   
9574 O  O   . HOH X .   ? 0.3335 0.3880 0.3054 0.0337  0.0398  0.1123  486 HOH D O   
9575 O  O   . HOH X .   ? 0.1715 0.0453 0.2113 0.0000  -0.0293 0.0387  487 HOH D O   
9576 O  O   . HOH X .   ? 0.3297 0.1948 0.2929 0.0185  -0.0057 -0.0337 488 HOH D O   
9577 O  O   . HOH X .   ? 0.4530 0.0396 0.4190 -0.0469 0.0835  0.0110  489 HOH D O   
9578 O  O   . HOH X .   ? 0.4160 0.2297 0.7588 0.1312  -0.0391 -0.0212 490 HOH D O   
9579 O  O   . HOH X .   ? 0.6759 0.5522 0.6964 0.0334  -0.0576 0.1411  491 HOH D O   
9580 O  O   . HOH X .   ? 0.2275 0.0549 0.1607 0.0066  0.0102  0.0006  492 HOH D O   
9581 O  O   . HOH X .   ? 0.3502 0.5231 0.3567 0.2143  -0.0543 -0.1092 493 HOH D O   
9582 O  O   . HOH X .   ? 0.3207 0.1218 0.3063 0.0287  0.0641  0.0172  494 HOH D O   
9583 O  O   . HOH X .   ? 0.4898 0.2666 0.3300 0.0743  -0.0780 0.1423  495 HOH D O   
9584 O  O   . HOH X .   ? 0.3052 0.2652 0.3661 -0.1333 0.0430  -0.0580 496 HOH D O   
9585 O  O   . HOH X .   ? 1.0752 0.5985 0.5428 -0.3170 -0.2409 0.1298  497 HOH D O   
9586 O  O   . HOH X .   ? 0.2069 0.2177 0.4027 0.0305  0.0136  0.0178  498 HOH D O   
9587 O  O   . HOH X .   ? 0.3070 0.1488 0.3371 0.0547  0.0416  0.0134  499 HOH D O   
9588 O  O   . HOH X .   ? 0.2466 0.0093 0.3712 -0.0094 -0.0699 -0.0274 500 HOH D O   
9589 O  O   . HOH X .   ? 0.2760 0.2640 0.2837 0.0352  -0.0399 -0.0002 501 HOH D O   
9590 O  O   . HOH X .   ? 0.4817 0.1036 0.4005 0.1018  0.0425  0.0100  502 HOH D O   
9591 O  O   . HOH X .   ? 0.6129 0.0532 0.6014 -0.0339 0.0713  -0.0864 503 HOH D O   
9592 O  O   . HOH X .   ? 0.4242 0.4559 0.2232 0.0906  -0.0480 0.0468  504 HOH D O   
9593 O  O   . HOH X .   ? 0.4390 0.0907 0.4638 0.0472  0.0480  0.0682  505 HOH D O   
9594 O  O   . HOH X .   ? 0.2769 0.0128 0.3335 -0.0417 0.0497  -0.0057 506 HOH D O   
9595 O  O   . HOH X .   ? 0.2837 0.0643 0.2113 -0.0267 -0.0097 0.0365  507 HOH D O   
9596 O  O   . HOH X .   ? 0.1877 0.0217 0.1890 0.0057  0.0067  -0.0019 508 HOH D O   
9597 O  O   . HOH X .   ? 0.1980 0.0469 0.1500 0.0279  0.0222  0.0107  509 HOH D O   
9598 O  O   . HOH X .   ? 0.2601 0.3500 0.4054 -0.0031 0.0143  0.0632  510 HOH D O   
9599 O  O   . HOH X .   ? 0.3958 0.5138 0.5904 -0.0599 0.1892  0.0422  511 HOH D O   
9600 O  O   . HOH X .   ? 0.3963 0.1367 0.3985 0.0109  0.0488  0.0103  512 HOH D O   
9601 O  O   . HOH X .   ? 0.4550 0.4120 0.3740 0.2614  -0.0592 -0.1419 513 HOH D O   
9602 O  O   . HOH X .   ? 0.2027 0.1652 0.2351 0.0392  0.0380  0.0934  514 HOH D O   
9603 O  O   . HOH X .   ? 0.4097 0.4809 0.2487 0.1374  -0.0546 0.0204  515 HOH D O   
9604 O  O   . HOH X .   ? 0.2227 0.0074 0.1694 0.0015  0.0122  0.0131  516 HOH D O   
9605 O  O   . HOH X .   ? 0.5800 0.3966 0.3646 -0.1720 0.1310  -0.1079 517 HOH D O   
9606 O  O   . HOH X .   ? 0.2688 0.1150 0.2520 0.0739  0.0000  0.0017  518 HOH D O   
9607 O  O   . HOH X .   ? 0.3087 0.1029 0.2949 -0.0113 0.0165  -0.0081 519 HOH D O   
9608 O  O   . HOH X .   ? 0.4482 0.2153 0.6786 0.0201  0.0425  0.0196  520 HOH D O   
9609 O  O   . HOH X .   ? 0.5712 0.2639 0.3867 0.1477  -0.1056 -0.0431 521 HOH D O   
9610 O  O   . HOH X .   ? 0.7929 0.1848 0.2773 -0.2381 0.0986  -0.0546 522 HOH D O   
9611 O  O   . HOH X .   ? 0.2663 0.1280 0.2301 0.0170  0.0179  -0.0253 523 HOH D O   
9612 O  O   . HOH X .   ? 0.1654 0.0776 0.2437 -0.0004 -0.0083 0.0369  524 HOH D O   
9613 O  O   . HOH X .   ? 0.2008 0.0097 0.2551 -0.0036 0.0178  -0.0289 525 HOH D O   
9614 O  O   . HOH X .   ? 0.4349 0.2796 0.3766 -0.0316 -0.0592 0.0509  526 HOH D O   
9615 O  O   . HOH X .   ? 0.2606 0.1062 0.2652 -0.0095 0.0604  0.0204  527 HOH D O   
9616 O  O   . HOH X .   ? 0.3180 0.1157 0.3875 0.0735  -0.0209 0.0439  528 HOH D O   
9617 O  O   . HOH X .   ? 0.4069 0.1923 0.3521 -0.0891 -0.1303 0.0820  529 HOH D O   
9618 O  O   . HOH X .   ? 0.3714 0.4039 0.3518 -0.0625 0.0006  0.0750  530 HOH D O   
9619 O  O   . HOH X .   ? 0.2903 0.2225 0.4598 -0.1016 0.0855  0.0832  531 HOH D O   
9620 O  O   . HOH X .   ? 0.6013 0.4708 0.6218 0.2334  -0.0433 -0.1450 532 HOH D O   
9621 O  O   . HOH X .   ? 0.3024 0.1610 0.2574 0.0449  -0.0158 0.0435  533 HOH D O   
9622 O  O   . HOH X .   ? 0.3456 0.2455 0.3405 0.0726  0.0004  -0.0532 534 HOH D O   
9623 O  O   . HOH X .   ? 0.4666 0.4752 0.5246 0.2042  0.1641  0.1700  535 HOH D O   
9624 O  O   . HOH X .   ? 0.7419 0.2451 0.3902 0.0604  0.2109  -0.0461 536 HOH D O   
9625 O  O   . HOH X .   ? 0.3653 0.3143 0.3968 0.1342  -0.0167 0.0192  537 HOH D O   
9626 O  O   . HOH X .   ? 0.6712 0.6351 0.8645 -0.0682 0.1884  0.0820  538 HOH D O   
9627 O  O   . HOH X .   ? 0.3510 0.1338 0.2252 0.0735  0.0285  0.0152  539 HOH D O   
9628 O  O   . HOH X .   ? 0.5713 0.0914 0.4559 -0.0021 0.0590  0.0499  540 HOH D O   
9629 O  O   . HOH X .   ? 0.5600 0.1761 0.4573 0.0100  -0.0919 0.0032  541 HOH D O   
9630 O  O   . HOH X .   ? 0.2267 0.0467 0.3567 -0.0044 0.0232  -0.0201 542 HOH D O   
9631 O  O   . HOH X .   ? 0.1471 0.0093 0.1703 -0.0088 -0.0158 0.0128  543 HOH D O   
9632 O  O   . HOH X .   ? 0.3438 0.0911 0.2723 0.0395  -0.0149 0.0042  544 HOH D O   
9633 O  O   . HOH X .   ? 0.3735 0.0760 0.3424 -0.0707 -0.0441 0.0283  545 HOH D O   
9634 O  O   . HOH X .   ? 0.3590 0.1033 0.3036 -0.0783 0.0366  -0.0737 546 HOH D O   
9635 O  O   . HOH X .   ? 0.2569 0.2256 0.2502 0.0597  -0.0036 0.0261  547 HOH D O   
9636 O  O   . HOH X .   ? 0.2309 0.0859 0.2955 -0.0367 -0.0131 -0.0434 548 HOH D O   
9637 O  O   . HOH X .   ? 0.5414 0.2031 0.3570 -0.1733 -0.0922 0.0414  549 HOH D O   
9638 O  O   . HOH X .   ? 0.2558 0.2074 0.4542 -0.1267 -0.0055 0.0587  550 HOH D O   
9639 O  O   . HOH X .   ? 0.4557 0.5288 0.2757 -0.0026 -0.1025 0.0298  551 HOH D O   
9640 O  O   . HOH X .   ? 0.2802 0.4246 0.4084 0.0603  0.0743  0.2100  552 HOH D O   
9641 O  O   . HOH X .   ? 0.4587 0.2652 0.7993 0.1388  -0.0485 0.0934  553 HOH D O   
9642 O  O   . HOH X .   ? 0.2035 0.0985 0.2279 0.0462  0.0155  -0.0159 554 HOH D O   
9643 O  O   . HOH X .   ? 0.4475 0.2863 0.4151 -0.0566 -0.0381 0.0641  555 HOH D O   
9644 O  O   . HOH X .   ? 0.2141 0.3973 0.5562 0.0054  -0.0514 -0.1240 556 HOH D O   
9645 O  O   . HOH X .   ? 0.4098 0.2024 0.1984 -0.1972 -0.1215 0.0650  557 HOH D O   
9646 O  O   . HOH X .   ? 0.2288 0.1959 0.3001 -0.0818 -0.0009 -0.0173 558 HOH D O   
9647 O  O   . HOH X .   ? 0.6341 0.1750 0.3129 0.1453  0.0084  0.0469  559 HOH D O   
9648 O  O   . HOH X .   ? 0.3376 0.0638 0.3903 -0.0547 -0.0285 -0.0025 560 HOH D O   
9649 O  O   . HOH X .   ? 0.2689 0.1148 0.2570 -0.0302 0.0342  0.0034  561 HOH D O   
9650 O  O   . HOH X .   ? 0.3321 0.1980 0.7676 0.0292  0.2051  0.0491  562 HOH D O   
9651 O  O   . HOH X .   ? 0.2342 0.0161 0.2306 -0.0450 -0.0141 -0.0111 563 HOH D O   
9652 O  O   . HOH X .   ? 0.2508 0.1898 0.4307 0.0321  -0.0853 0.0033  564 HOH D O   
9653 O  O   . HOH X .   ? 0.4714 0.1498 0.5265 0.0129  -0.0278 0.1008  565 HOH D O   
9654 O  O   . HOH X .   ? 0.3621 0.3977 0.4551 -0.0234 -0.0190 0.0376  566 HOH D O   
9655 O  O   . HOH X .   ? 0.4520 0.2098 0.3977 -0.1029 0.1417  -0.0713 567 HOH D O   
9656 O  O   . HOH X .   ? 0.2706 0.1647 0.3058 -0.0027 -0.0110 0.0242  568 HOH D O   
9657 O  O   . HOH X .   ? 0.2990 0.2264 0.2601 0.0029  0.0436  -0.0052 569 HOH D O   
9658 O  O   . HOH X .   ? 0.3185 0.3948 0.3762 -0.0023 -0.0512 0.1846  570 HOH D O   
9659 O  O   . HOH X .   ? 0.1780 0.1855 0.3323 0.0272  -0.0156 0.0425  571 HOH D O   
9660 O  O   . HOH X .   ? 0.2120 0.1381 0.2017 0.0201  -0.0071 -0.0370 572 HOH D O   
9661 O  O   . HOH X .   ? 0.2454 0.3340 0.2949 0.0845  0.0702  0.0257  573 HOH D O   
9662 O  O   . HOH X .   ? 0.3820 0.4163 0.2767 0.1808  -0.0553 -0.0017 574 HOH D O   
9663 O  O   . HOH X .   ? 0.3238 0.0884 0.3534 -0.0306 -0.0626 0.0105  575 HOH D O   
9664 O  O   . HOH X .   ? 0.1882 0.0692 0.2078 -0.0025 0.0002  0.0210  576 HOH D O   
9665 O  O   . HOH X .   ? 0.6030 0.6208 0.3769 0.3902  0.1425  0.1397  577 HOH D O   
9666 O  O   . HOH X .   ? 0.2720 0.1834 0.2110 -0.0331 -0.0155 0.0219  578 HOH D O   
9667 O  O   . HOH X .   ? 0.2963 0.0252 0.1987 -0.0159 -0.0148 -0.0097 579 HOH D O   
9668 O  O   . HOH X .   ? 0.2555 0.2841 0.1735 -0.0245 -0.0475 0.0494  580 HOH D O   
9669 O  O   . HOH X .   ? 0.7340 0.1600 0.3235 -0.1975 -0.2614 0.0505  581 HOH D O   
9670 O  O   . HOH X .   ? 0.4447 0.2071 0.4064 -0.1632 -0.0619 0.1033  582 HOH D O   
9671 O  O   . HOH X .   ? 0.6603 0.2701 0.3097 0.0495  -0.1100 -0.0214 583 HOH D O   
9672 O  O   . HOH X .   ? 0.5443 0.2349 0.3151 -0.0919 -0.0283 -0.0848 584 HOH D O   
9673 O  O   . HOH X .   ? 0.2254 0.3494 0.2561 -0.0596 0.0011  -0.0605 585 HOH D O   
9674 O  O   . HOH X .   ? 0.3153 0.5457 0.4566 -0.0829 -0.0094 0.1223  586 HOH D O   
9675 O  O   . HOH X .   ? 0.3054 0.0574 0.2906 0.0541  -0.0601 0.0192  587 HOH D O   
9676 O  O   . HOH X .   ? 0.3222 0.6954 0.2820 -0.1463 -0.0925 0.1848  588 HOH D O   
9677 O  O   . HOH X .   ? 0.4001 0.2819 0.3353 -0.0441 -0.0439 0.0337  589 HOH D O   
9678 O  O   . HOH X .   ? 0.3840 0.2078 0.3025 0.1582  0.0751  0.0776  590 HOH D O   
9679 O  O   . HOH X .   ? 0.4377 0.1273 0.5613 0.0212  -0.1837 0.0583  591 HOH D O   
9680 O  O   . HOH X .   ? 0.4939 0.3680 0.4621 -0.0227 -0.0067 -0.0326 592 HOH D O   
9681 O  O   . HOH X .   ? 0.2780 0.2827 0.7119 0.0729  0.0141  0.2832  593 HOH D O   
9682 O  O   . HOH X .   ? 0.2060 0.0163 0.1489 -0.0234 0.0065  0.0004  594 HOH D O   
9683 O  O   . HOH X .   ? 0.2153 0.0877 0.4425 -0.0548 0.0135  -0.0261 595 HOH D O   
9684 O  O   . HOH X .   ? 0.2986 0.0390 0.2415 -0.0122 0.0618  -0.0288 596 HOH D O   
9685 O  O   . HOH X .   ? 0.2138 0.4460 0.2845 0.0046  -0.0160 -0.0158 597 HOH D O   
9686 O  O   . HOH X .   ? 0.3375 0.5934 0.4588 0.1137  0.1082  0.2638  598 HOH D O   
9687 O  O   . HOH X .   ? 0.2098 0.1169 0.3565 -0.0436 -0.0107 -0.0504 599 HOH D O   
9688 O  O   . HOH X .   ? 0.4021 0.2921 0.2991 0.1047  0.0177  -0.0902 600 HOH D O   
9689 O  O   . HOH X .   ? 0.1500 0.2837 0.3507 -0.0555 -0.0513 0.1289  601 HOH D O   
9690 O  O   . HOH X .   ? 0.5202 0.4401 0.7752 -0.0142 0.2990  0.1140  602 HOH D O   
9691 O  O   . HOH X .   ? 0.3395 0.2812 0.2887 0.0341  0.0935  0.0227  603 HOH D O   
9692 O  O   . HOH X .   ? 0.4275 0.2200 0.2182 -0.0710 -0.0429 -0.0318 604 HOH D O   
9693 O  O   . HOH X .   ? 0.2748 0.1717 0.2523 0.0222  0.0284  0.0295  605 HOH D O   
9694 O  O   . HOH X .   ? 0.5569 0.1571 0.5281 0.0788  -0.1129 -0.0684 606 HOH D O   
9695 O  O   . HOH X .   ? 0.6998 0.2682 0.3916 -0.2208 0.0482  0.0283  607 HOH D O   
9696 O  O   . HOH X .   ? 0.3491 0.1534 0.4042 -0.1100 0.0758  -0.0373 608 HOH D O   
9697 O  O   . HOH X .   ? 0.2933 0.3215 0.3542 -0.1859 0.0784  -0.0032 609 HOH D O   
9698 O  O   . HOH X .   ? 0.2354 0.1826 0.2665 -0.0340 -0.0207 0.0263  610 HOH D O   
9699 O  O   . HOH X .   ? 0.4766 0.2663 0.5622 -0.0341 0.0329  -0.2628 611 HOH D O   
9700 O  O   . HOH X .   ? 0.2591 0.4899 0.4595 0.0184  -0.0410 0.2956  612 HOH D O   
9701 O  O   . HOH X .   ? 0.1785 0.0586 0.2189 -0.0044 -0.0059 0.0018  613 HOH D O   
9702 O  O   . HOH X .   ? 0.6475 0.1065 0.3425 0.1190  -0.0387 0.0359  614 HOH D O   
9703 O  O   . HOH X .   ? 0.4210 0.3290 0.2199 -0.0170 0.0408  -0.1005 615 HOH D O   
9704 O  O   . HOH X .   ? 0.3767 0.0480 0.2024 0.0634  0.0082  -0.0078 616 HOH D O   
9705 O  O   . HOH X .   ? 0.2884 0.1090 0.2683 0.0172  0.0067  0.0055  617 HOH D O   
9706 O  O   . HOH X .   ? 0.2110 0.1119 0.1884 -0.0311 -0.0129 -0.0145 618 HOH D O   
9707 O  O   . HOH X .   ? 0.3977 0.1045 0.2736 -0.0526 0.0302  -0.0262 619 HOH D O   
9708 O  O   . HOH X .   ? 0.7937 0.0406 0.6371 0.0920  -0.1295 0.1045  620 HOH D O   
9709 O  O   . HOH X .   ? 0.2676 0.1420 0.3183 -0.0009 0.0694  -0.0139 621 HOH D O   
9710 O  O   . HOH X .   ? 0.3790 0.1464 0.4724 -0.0679 -0.1072 0.1077  622 HOH D O   
9711 O  O   . HOH X .   ? 0.8505 0.3855 0.3789 -0.1898 0.0138  0.0343  623 HOH D O   
9712 O  O   . HOH X .   ? 0.5602 0.1658 0.4444 0.0073  -0.0860 -0.0712 624 HOH D O   
9713 O  O   . HOH X .   ? 0.3324 0.0347 0.2698 0.0051  0.0260  -0.0276 625 HOH D O   
9714 O  O   . HOH X .   ? 0.3059 0.1973 0.4959 0.1251  0.0156  -0.0025 626 HOH D O   
9715 O  O   . HOH X .   ? 0.2570 0.0188 0.2994 -0.0044 0.0159  -0.0042 627 HOH D O   
9716 O  O   . HOH X .   ? 0.3682 0.1385 0.4472 0.0103  0.0089  -0.0410 628 HOH D O   
9717 O  O   . HOH X .   ? 0.3492 0.1280 0.3246 0.0663  -0.0939 -0.0114 629 HOH D O   
9718 O  O   . HOH X .   ? 0.2636 0.2441 0.3233 0.0939  -0.0088 -0.0266 630 HOH D O   
9719 O  O   . HOH X .   ? 0.3216 0.4034 0.2052 -0.1200 -0.0652 0.0222  631 HOH D O   
9720 O  O   . HOH X .   ? 0.4213 0.5805 0.4131 0.1806  -0.0675 -0.0664 632 HOH D O   
9721 O  O   . HOH X .   ? 0.9806 0.6370 0.3237 -0.4821 -0.0540 0.0857  633 HOH D O   
9722 O  O   . HOH X .   ? 0.5499 0.2209 0.6231 0.0024  0.0272  -0.1687 634 HOH D O   
9723 O  O   . HOH X .   ? 0.3147 0.1500 0.3744 0.0122  0.0750  -0.0137 635 HOH D O   
9724 O  O   . HOH X .   ? 0.3701 0.0677 0.4262 -0.0168 -0.0036 -0.0172 636 HOH D O   
9725 O  O   . HOH X .   ? 0.3405 0.4713 0.7440 -0.0381 0.1354  0.2885  637 HOH D O   
9726 O  O   . HOH X .   ? 0.4047 0.6172 0.4103 -0.1172 -0.0335 -0.2222 638 HOH D O   
9727 O  O   . HOH X .   ? 0.2825 0.4121 0.3319 0.0135  -0.0022 -0.1080 639 HOH D O   
9728 O  O   . HOH X .   ? 0.8882 0.4025 0.4379 0.1925  0.0502  0.0989  640 HOH D O   
9729 O  O   . HOH X .   ? 0.5335 0.2182 0.3277 0.0304  0.0277  0.0037  641 HOH D O   
9730 O  O   . HOH X .   ? 0.3689 0.6364 0.4238 0.0630  0.1198  0.1806  642 HOH D O   
9731 O  O   . HOH X .   ? 0.5985 0.1471 0.5734 0.0549  0.0622  -0.0467 643 HOH D O   
9732 O  O   . HOH X .   ? 0.3101 0.0359 0.3751 -0.0077 -0.0226 -0.0120 644 HOH D O   
9733 O  O   . HOH X .   ? 0.4440 0.5506 0.4500 -0.1156 0.0834  0.0791  645 HOH D O   
9734 O  O   . HOH X .   ? 0.4250 0.8635 0.3910 0.1631  0.0038  0.1909  646 HOH D O   
9735 O  O   . HOH X .   ? 0.5531 0.1392 0.4638 0.1042  -0.1027 0.0049  647 HOH D O   
9736 O  O   . HOH X .   ? 0.5778 0.3506 0.6010 0.0501  -0.1796 0.0013  648 HOH D O   
9737 O  O   . HOH X .   ? 0.5489 0.4604 0.6069 0.1253  -0.0016 -0.2565 649 HOH D O   
9738 O  O   . HOH X .   ? 0.3853 0.2942 0.5608 0.0902  0.0418  0.0858  650 HOH D O   
9739 O  O   . HOH X .   ? 0.5538 0.2552 0.6145 0.0785  0.2132  0.0856  651 HOH D O   
9740 O  O   . HOH X .   ? 0.3913 0.3940 0.5013 0.0271  -0.0276 0.0142  652 HOH D O   
9741 O  O   . HOH X .   ? 0.3246 0.3776 0.8403 0.1049  -0.0301 -0.1944 653 HOH D O   
9742 O  O   . HOH X .   ? 0.7153 0.2894 0.4875 -0.0055 -0.2782 -0.1153 654 HOH D O   
9743 O  O   . HOH X .   ? 0.4871 0.1430 0.2919 -0.0846 0.0117  0.0051  655 HOH D O   
9744 O  O   . HOH X .   ? 0.5402 0.4300 0.7610 -0.1113 0.2795  -0.0248 656 HOH D O   
9745 O  O   . HOH X .   ? 0.3603 0.1686 0.8158 0.0434  0.1700  0.0512  657 HOH D O   
9746 O  O   . HOH X .   ? 0.3765 0.0929 0.5755 0.0392  0.0715  -0.0707 658 HOH D O   
9747 O  O   . HOH X .   ? 0.5382 0.5699 0.5921 -0.2673 -0.0823 -0.0486 659 HOH D O   
9748 O  O   . HOH X .   ? 0.4128 0.3853 0.4644 -0.0447 0.0469  0.0728  660 HOH D O   
9749 O  O   . HOH X .   ? 0.4676 0.3378 0.5730 0.0594  -0.1793 -0.0233 661 HOH D O   
9750 O  O   . HOH X .   ? 0.4917 0.2108 0.6821 0.0113  0.0241  0.1211  662 HOH D O   
9751 O  O   . HOH X .   ? 0.4614 0.2040 0.3481 0.0284  -0.0949 -0.0077 663 HOH D O   
9752 O  O   . HOH X .   ? 0.3438 0.1290 0.3396 -0.0392 -0.0244 0.0153  664 HOH D O   
9753 O  O   . HOH X .   ? 0.3502 0.2527 0.3960 0.0563  -0.0423 0.0440  665 HOH D O   
9754 O  O   . HOH X .   ? 0.3326 0.5586 0.4390 -0.0639 -0.0988 0.0923  666 HOH D O   
9755 O  O   . HOH X .   ? 0.5845 0.3668 0.3546 0.1788  0.1509  0.0298  667 HOH D O   
9756 O  O   . HOH X .   ? 0.3948 0.2656 0.4062 0.0904  0.0157  -0.0943 668 HOH D O   
9757 O  O   . HOH X .   ? 0.3318 0.1555 0.2870 -0.0204 -0.0760 -0.0467 669 HOH D O   
9758 O  O   . HOH X .   ? 0.3506 0.1599 0.3087 0.0075  -0.0771 0.0611  670 HOH D O   
9759 O  O   . HOH X .   ? 0.4069 0.1403 0.4061 0.0611  0.0039  0.0590  671 HOH D O   
9760 O  O   . HOH X .   ? 0.3786 0.5976 0.3822 -0.0585 -0.0653 0.0643  672 HOH D O   
9761 O  O   . HOH X .   ? 0.2713 0.2908 0.3814 0.0439  0.0143  0.0797  673 HOH D O   
9762 O  O   . HOH X .   ? 0.6297 0.3280 0.4097 -0.0198 0.1091  0.0557  674 HOH D O   
9763 O  O   . HOH X .   ? 0.4372 0.3430 0.9432 -0.2008 -0.1465 -0.0457 675 HOH D O   
9764 O  O   . HOH X .   ? 0.3974 0.2242 0.3736 -0.0757 -0.0270 0.0197  676 HOH D O   
9765 O  O   . HOH X .   ? 0.3924 0.1548 0.5223 0.0504  -0.2010 -0.0477 677 HOH D O   
9766 O  O   . HOH X .   ? 0.3215 0.1706 0.2876 0.0119  -0.0472 0.0162  678 HOH D O   
9767 O  O   . HOH X .   ? 0.1823 0.2983 0.2246 0.0013  -0.0390 0.0458  679 HOH D O   
9768 O  O   . HOH X .   ? 0.5492 0.1067 0.6103 -0.0312 -0.0445 -0.0781 680 HOH D O   
9769 O  O   . HOH X .   ? 0.3069 0.2711 0.8631 0.0026  0.1223  0.2066  681 HOH D O   
9770 O  O   . HOH X .   ? 0.5385 0.3620 0.3722 -0.1424 0.0211  0.0886  682 HOH D O   
9771 O  O   . HOH X .   ? 0.4586 0.3475 0.4134 -0.0087 0.0231  0.0190  683 HOH D O   
9772 O  O   . HOH X .   ? 0.7031 0.1539 0.4049 -0.1303 -0.0921 0.0566  684 HOH D O   
9773 O  O   . HOH X .   ? 0.5730 0.2049 0.7476 -0.0162 0.1380  0.0716  685 HOH D O   
9774 O  O   . HOH X .   ? 0.2380 0.2561 0.3419 0.0032  -0.0154 0.0342  686 HOH D O   
9775 O  O   . HOH X .   ? 0.9932 0.1911 0.2664 -0.1728 -0.0018 0.0200  687 HOH D O   
9776 O  O   . HOH X .   ? 0.4795 0.5674 0.5610 0.0869  -0.2305 -0.1905 688 HOH D O   
9777 O  O   . HOH X .   ? 0.5711 0.0891 0.5264 -0.0603 -0.0378 0.0624  689 HOH D O   
9778 O  O   . HOH X .   ? 0.4085 0.2426 0.3375 -0.0211 0.0490  0.1321  690 HOH D O   
9779 O  O   . HOH X .   ? 0.4174 0.1984 0.3968 0.1254  -0.0694 0.0589  691 HOH D O   
9780 O  O   . HOH X .   ? 0.6670 0.2534 0.3930 -0.1526 0.0401  -0.0240 692 HOH D O   
9781 O  O   . HOH X .   ? 0.3274 0.2169 0.5277 0.0643  -0.1267 -0.1134 693 HOH D O   
9782 O  O   . HOH X .   ? 0.3045 0.1880 0.2766 0.0039  -0.0241 0.0486  694 HOH D O   
9783 O  O   . HOH X .   ? 0.4019 0.3529 0.4293 0.1184  -0.2230 -0.0171 695 HOH D O   
9784 O  O   . HOH X .   ? 0.3328 0.3106 0.3027 0.0458  0.0027  0.0479  696 HOH D O   
9785 O  O   . HOH X .   ? 0.3521 0.2710 0.4908 -0.0214 0.0480  -0.1307 697 HOH D O   
9786 O  O   . HOH X .   ? 0.5493 0.3529 0.5111 -0.0669 0.1455  0.0697  698 HOH D O   
9787 O  O   . HOH X .   ? 0.4741 0.2128 0.4939 0.1032  0.0594  0.1368  699 HOH D O   
9788 O  O   . HOH X .   ? 0.5019 0.4139 0.4774 0.1964  -0.0193 0.0520  700 HOH D O   
9789 O  O   . HOH X .   ? 0.6283 0.1805 0.4167 -0.0573 -0.1779 0.0836  701 HOH D O   
9790 O  O   . HOH X .   ? 0.3912 0.2981 0.5122 -0.0316 -0.0929 0.0635  702 HOH D O   
9791 O  O   . HOH X .   ? 0.4609 0.3018 0.3616 -0.0359 0.0506  -0.0541 703 HOH D O   
9792 O  O   . HOH X .   ? 0.4487 0.4053 0.3439 -0.0515 -0.1205 0.1729  704 HOH D O   
9793 O  O   . HOH X .   ? 0.2336 0.2399 0.2505 0.0741  -0.0458 0.0754  705 HOH D O   
9794 O  O   . HOH X .   ? 0.3017 0.0462 0.4256 0.0221  -0.0287 -0.0495 706 HOH D O   
9795 O  O   . HOH X .   ? 0.4425 0.3459 0.4207 -0.0085 -0.0264 0.1125  707 HOH D O   
9796 O  O   . HOH X .   ? 0.3759 0.2207 0.3875 0.0625  0.0108  0.0385  708 HOH D O   
9797 O  O   . HOH X .   ? 0.5956 0.2099 0.5945 0.0487  -0.1720 0.0253  709 HOH D O   
9798 O  O   . HOH X .   ? 0.4211 0.3811 0.4588 0.0760  0.0361  0.0031  710 HOH D O   
9799 O  O   . HOH X .   ? 0.2847 0.4096 0.3065 -0.0208 -0.0139 0.0527  711 HOH D O   
9800 O  O   . HOH X .   ? 0.4403 0.1259 0.2144 0.0139  -0.0753 -0.0397 712 HOH D O   
9801 O  O   . HOH X .   ? 0.7516 0.2744 0.3375 0.1268  0.0220  0.0444  713 HOH D O   
9802 O  O   . HOH X .   ? 0.4534 0.1552 0.4767 0.0463  -0.0138 -0.1154 714 HOH D O   
9803 O  O   . HOH X .   ? 0.4155 0.4365 0.5448 -0.0273 0.0125  0.0416  715 HOH D O   
9804 O  O   . HOH X .   ? 0.4037 0.4010 0.4518 -0.0248 0.0166  -0.0621 716 HOH D O   
9805 O  O   . HOH X .   ? 0.4731 0.3511 0.3829 -0.0715 0.0375  -0.0266 717 HOH D O   
9806 O  O   . HOH X .   ? 0.5314 0.2074 0.4515 -0.0442 -0.0598 0.0780  718 HOH D O   
9807 O  O   . HOH X .   ? 0.3820 0.3258 0.3371 -0.0307 0.0140  -0.0996 719 HOH D O   
9808 O  O   . HOH X .   ? 0.4461 0.1568 0.3765 -0.0469 0.0892  0.0625  720 HOH D O   
9809 O  O   . HOH X .   ? 0.3644 0.1284 0.3198 -0.0302 0.0205  -0.0356 721 HOH D O   
9810 O  O   . HOH X .   ? 0.3217 0.1696 0.2954 0.0317  0.0239  -0.0974 722 HOH D O   
9811 O  O   . HOH X .   ? 0.3148 0.2288 0.3561 -0.0765 0.0008  0.0747  723 HOH D O   
9812 O  O   . HOH X .   ? 0.4777 0.1977 0.5934 0.0182  0.0683  0.0967  724 HOH D O   
9813 O  O   . HOH X .   ? 0.3883 0.0995 0.3486 0.0015  0.0963  -0.0134 725 HOH D O   
9814 O  O   . HOH X .   ? 0.3846 0.3984 0.4200 -0.0299 -0.0334 -0.0037 726 HOH D O   
9815 O  O   . HOH X .   ? 0.3565 0.4218 0.3046 0.1232  -0.0288 0.0750  727 HOH D O   
9816 O  O   . HOH X .   ? 0.3378 0.1916 0.3998 0.0278  -0.0025 -0.0567 728 HOH D O   
9817 O  O   . HOH X .   ? 0.5930 0.3412 0.4587 -0.1394 -0.0204 -0.0217 729 HOH D O   
# 
