data_9DXB
# 
_entry.id   9DXB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9DXB         pdb_00009dxb 10.2210/pdb9dxb/pdb 
WWPDB D_1000289032 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DXB 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mark.white@sydney.edu.au 
_pdbx_contact_author.name_first         Mark 
_pdbx_contact_author.name_last          White 
_pdbx_contact_author.name_mi            D 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1431-0339 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Jiramongkol, Y.' 1 ? 
'Patel, K.'       2 ? 
'White, M.D.'     3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                4761 
_citation.page_last                 4761 
_citation.title                     
'An mRNA-display derived cyclic peptide scaffold reveals the substrate binding interactions of an N-terminal cysteine oxidase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59960-3 
_citation.pdbx_database_id_PubMed   40404614 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jiramongkol, Y.'    1  0000-0003-1824-4313 
primary 'Patel, K.'          2  0000-0003-3034-3840 
primary 'Johansen-Leete, J.' 3  ?                   
primary 'Maxwell, J.W.C.'    4  ?                   
primary 'Chang, Y.'          5  ?                   
primary 'Du, J.J.'           6  0000-0002-7750-4413 
primary 'Passioura, T.'      7  ?                   
primary 'Cook, K.M.'         8  0000-0002-0503-7166 
primary 'Payne, R.J.'        9  0000-0002-3618-9226 
primary 'White, M.D.'        10 0000-0002-1431-0339 
# 
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 '2-aminoethanethiol dioxygenase' 29841.811 1   1.13.11.19 ? ? ? 
2 polymer     syn CP6-L8d-Gly-Ser                  1882.153  1   ?          ? ? ? 
3 non-polymer syn 'COBALT (II) ION'                58.933    1   ?          ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                   35.453    2   ?          ? ? ? 
5 non-polymer syn GLYCEROL                         92.094    5   ?          ? ? ? 
6 water       nat water                            18.015    200 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cysteamine dioxygenase' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;SMPRDNMASLIQRIARQASLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQLRAEDLNIAPRKATLQPLP
PNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGMLKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQP
REREAVRPGVLRSRAEYTEASGPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSAS
DLPREVWLLETPQADDFWCEGEPYPGPKVFP
;
;SMPRDNMASLIQRIARQASLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQLRAEDLNIAPRKATLQPLP
PNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGMLKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQP
REREAVRPGVLRSRAEYTEASGPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSAS
DLPREVWLLETPQADDFWCEGEPYPGPKVFP
;
A ? 
2 'polypeptide(L)' no yes '(ACE)YIVKTFW(A1BC5)GSHRQC(NH2)' XYIVKTFWSGSHRQCX B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'COBALT (II) ION' CO  
4 'CHLORIDE ION'    CL  
5 GLYCEROL          GOL 
6 water             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER   n 
1 2   MET   n 
1 3   PRO   n 
1 4   ARG   n 
1 5   ASP   n 
1 6   ASN   n 
1 7   MET   n 
1 8   ALA   n 
1 9   SER   n 
1 10  LEU   n 
1 11  ILE   n 
1 12  GLN   n 
1 13  ARG   n 
1 14  ILE   n 
1 15  ALA   n 
1 16  ARG   n 
1 17  GLN   n 
1 18  ALA   n 
1 19  SER   n 
1 20  LEU   n 
1 21  THR   n 
1 22  PHE   n 
1 23  ARG   n 
1 24  GLY   n 
1 25  SER   n 
1 26  GLY   n 
1 27  GLY   n 
1 28  GLY   n 
1 29  ARG   n 
1 30  GLY   n 
1 31  ALA   n 
1 32  SER   n 
1 33  ASP   n 
1 34  ARG   n 
1 35  ASP   n 
1 36  ALA   n 
1 37  ALA   n 
1 38  SER   n 
1 39  GLY   n 
1 40  PRO   n 
1 41  GLU   n 
1 42  ALA   n 
1 43  PRO   n 
1 44  MET   n 
1 45  GLN   n 
1 46  PRO   n 
1 47  GLY   n 
1 48  PHE   n 
1 49  PRO   n 
1 50  GLU   n 
1 51  ASN   n 
1 52  LEU   n 
1 53  SER   n 
1 54  LYS   n 
1 55  LEU   n 
1 56  LYS   n 
1 57  SER   n 
1 58  LEU   n 
1 59  LEU   n 
1 60  THR   n 
1 61  GLN   n 
1 62  LEU   n 
1 63  ARG   n 
1 64  ALA   n 
1 65  GLU   n 
1 66  ASP   n 
1 67  LEU   n 
1 68  ASN   n 
1 69  ILE   n 
1 70  ALA   n 
1 71  PRO   n 
1 72  ARG   n 
1 73  LYS   n 
1 74  ALA   n 
1 75  THR   n 
1 76  LEU   n 
1 77  GLN   n 
1 78  PRO   n 
1 79  LEU   n 
1 80  PRO   n 
1 81  PRO   n 
1 82  ASN   n 
1 83  LEU   n 
1 84  PRO   n 
1 85  PRO   n 
1 86  VAL   n 
1 87  THR   n 
1 88  TYR   n 
1 89  MET   n 
1 90  HIS   n 
1 91  ILE   n 
1 92  TYR   n 
1 93  GLU   n 
1 94  THR   n 
1 95  ASP   n 
1 96  GLY   n 
1 97  PHE   n 
1 98  SER   n 
1 99  LEU   n 
1 100 GLY   n 
1 101 VAL   n 
1 102 PHE   n 
1 103 LEU   n 
1 104 LEU   n 
1 105 LYS   n 
1 106 SER   n 
1 107 GLY   n 
1 108 THR   n 
1 109 SER   n 
1 110 ILE   n 
1 111 PRO   n 
1 112 LEU   n 
1 113 HIS   n 
1 114 ASP   n 
1 115 HIS   n 
1 116 PRO   n 
1 117 GLY   n 
1 118 MET   n 
1 119 HIS   n 
1 120 GLY   n 
1 121 MET   n 
1 122 LEU   n 
1 123 LYS   n 
1 124 VAL   n 
1 125 LEU   n 
1 126 TYR   n 
1 127 GLY   n 
1 128 THR   n 
1 129 VAL   n 
1 130 ARG   n 
1 131 ILE   n 
1 132 SER   n 
1 133 CYS   n 
1 134 MET   n 
1 135 ASP   n 
1 136 LYS   n 
1 137 LEU   n 
1 138 ASP   n 
1 139 ALA   n 
1 140 GLY   n 
1 141 GLY   n 
1 142 GLY   n 
1 143 GLN   n 
1 144 ARG   n 
1 145 PRO   n 
1 146 ARG   n 
1 147 ALA   n 
1 148 LEU   n 
1 149 PRO   n 
1 150 PRO   n 
1 151 GLU   n 
1 152 GLN   n 
1 153 GLN   n 
1 154 PHE   n 
1 155 GLU   n 
1 156 PRO   n 
1 157 PRO   n 
1 158 LEU   n 
1 159 GLN   n 
1 160 PRO   n 
1 161 ARG   n 
1 162 GLU   n 
1 163 ARG   n 
1 164 GLU   n 
1 165 ALA   n 
1 166 VAL   n 
1 167 ARG   n 
1 168 PRO   n 
1 169 GLY   n 
1 170 VAL   n 
1 171 LEU   n 
1 172 ARG   n 
1 173 SER   n 
1 174 ARG   n 
1 175 ALA   n 
1 176 GLU   n 
1 177 TYR   n 
1 178 THR   n 
1 179 GLU   n 
1 180 ALA   n 
1 181 SER   n 
1 182 GLY   n 
1 183 PRO   n 
1 184 CYS   n 
1 185 ILE   n 
1 186 LEU   n 
1 187 THR   n 
1 188 PRO   n 
1 189 HIS   n 
1 190 ARG   n 
1 191 ASP   n 
1 192 ASN   n 
1 193 LEU   n 
1 194 HIS   n 
1 195 GLN   n 
1 196 ILE   n 
1 197 ASP   n 
1 198 ALA   n 
1 199 VAL   n 
1 200 GLU   n 
1 201 GLY   n 
1 202 PRO   n 
1 203 ALA   n 
1 204 ALA   n 
1 205 PHE   n 
1 206 LEU   n 
1 207 ASP   n 
1 208 ILE   n 
1 209 LEU   n 
1 210 ALA   n 
1 211 PRO   n 
1 212 PRO   n 
1 213 TYR   n 
1 214 ASP   n 
1 215 PRO   n 
1 216 ASP   n 
1 217 ASP   n 
1 218 GLY   n 
1 219 ARG   n 
1 220 ASP   n 
1 221 CYS   n 
1 222 HIS   n 
1 223 TYR   n 
1 224 TYR   n 
1 225 ARG   n 
1 226 VAL   n 
1 227 LEU   n 
1 228 GLU   n 
1 229 PRO   n 
1 230 VAL   n 
1 231 ARG   n 
1 232 PRO   n 
1 233 LYS   n 
1 234 GLU   n 
1 235 ALA   n 
1 236 SER   n 
1 237 SER   n 
1 238 SER   n 
1 239 ALA   n 
1 240 SER   n 
1 241 ASP   n 
1 242 LEU   n 
1 243 PRO   n 
1 244 ARG   n 
1 245 GLU   n 
1 246 VAL   n 
1 247 TRP   n 
1 248 LEU   n 
1 249 LEU   n 
1 250 GLU   n 
1 251 THR   n 
1 252 PRO   n 
1 253 GLN   n 
1 254 ALA   n 
1 255 ASP   n 
1 256 ASP   n 
1 257 PHE   n 
1 258 TRP   n 
1 259 CYS   n 
1 260 GLU   n 
1 261 GLY   n 
1 262 GLU   n 
1 263 PRO   n 
1 264 TYR   n 
1 265 PRO   n 
1 266 GLY   n 
1 267 PRO   n 
1 268 LYS   n 
1 269 VAL   n 
1 270 PHE   n 
1 271 PRO   n 
2 1   ACE   n 
2 2   TYR   n 
2 3   ILE   n 
2 4   VAL   n 
2 5   LYS   n 
2 6   THR   n 
2 7   PHE   n 
2 8   TRP   n 
2 9   A1BC5 n 
2 10  GLY   n 
2 11  SER   n 
2 12  HIS   n 
2 13  ARG   n 
2 14  GLN   n 
2 15  CYS   n 
2 16  NH2   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                   271 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ADO, C10orf22' 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       16 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
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 
A1BC5 'L-peptide linking' n 'L-seryl-N-[(2S)-2-amino-2-carboxyethyl]glycinamide' ?                               'C8 H16 N4 O5'   
248.236 
ACE   non-polymer         . 'ACETYL GROUP'                                       ?                               'C2 H4 O'        
44.053  
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 
CL    non-polymer         . 'CHLORIDE ION'                                       ?                               'Cl -1'          
35.453  
CO    non-polymer         . 'COBALT (II) ION'                                    ?                               'Co 2'           
58.933  
CYS   'L-peptide linking' y CYSTEINE                                             ?                               'C3 H7 N O2 S'   
121.158 
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  
GOL   non-polymer         . GLYCEROL                                             'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       
92.094  
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 
NH2   non-polymer         . 'AMINO GROUP'                                        ?                               'H2 N'           
16.023  
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 
# 
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   SER   1   0   ?   ?     ?   A . n 
A 1 2   MET   2   1   ?   ?     ?   A . n 
A 1 3   PRO   3   2   ?   ?     ?   A . n 
A 1 4   ARG   4   3   ?   ?     ?   A . n 
A 1 5   ASP   5   4   ?   ?     ?   A . n 
A 1 6   ASN   6   5   5   ASN   ASN A . n 
A 1 7   MET   7   6   6   MET   MET A . n 
A 1 8   ALA   8   7   7   ALA   ALA A . n 
A 1 9   SER   9   8   8   SER   SER A . n 
A 1 10  LEU   10  9   9   LEU   LEU A . n 
A 1 11  ILE   11  10  10  ILE   ILE A . n 
A 1 12  GLN   12  11  11  GLN   GLN A . n 
A 1 13  ARG   13  12  12  ARG   ARG A . n 
A 1 14  ILE   14  13  13  ILE   ILE A . n 
A 1 15  ALA   15  14  14  ALA   ALA A . n 
A 1 16  ARG   16  15  15  ARG   ARG A . n 
A 1 17  GLN   17  16  16  GLN   GLN A . n 
A 1 18  ALA   18  17  17  ALA   ALA A . n 
A 1 19  SER   19  18  18  SER   SER A . n 
A 1 20  LEU   20  19  19  LEU   LEU A . n 
A 1 21  THR   21  20  20  THR   THR A . n 
A 1 22  PHE   22  21  21  PHE   PHE A . n 
A 1 23  ARG   23  22  22  ARG   ARG A . n 
A 1 24  GLY   24  23  ?   ?     ?   A . n 
A 1 25  SER   25  24  ?   ?     ?   A . n 
A 1 26  GLY   26  25  ?   ?     ?   A . n 
A 1 27  GLY   27  26  ?   ?     ?   A . n 
A 1 28  GLY   28  27  ?   ?     ?   A . n 
A 1 29  ARG   29  28  ?   ?     ?   A . n 
A 1 30  GLY   30  29  ?   ?     ?   A . n 
A 1 31  ALA   31  30  ?   ?     ?   A . n 
A 1 32  SER   32  31  ?   ?     ?   A . n 
A 1 33  ASP   33  32  ?   ?     ?   A . n 
A 1 34  ARG   34  33  ?   ?     ?   A . n 
A 1 35  ASP   35  34  ?   ?     ?   A . n 
A 1 36  ALA   36  35  ?   ?     ?   A . n 
A 1 37  ALA   37  36  ?   ?     ?   A . n 
A 1 38  SER   38  37  ?   ?     ?   A . n 
A 1 39  GLY   39  38  ?   ?     ?   A . n 
A 1 40  PRO   40  39  ?   ?     ?   A . n 
A 1 41  GLU   41  40  ?   ?     ?   A . n 
A 1 42  ALA   42  41  41  ALA   GLY A . n 
A 1 43  PRO   43  42  42  PRO   PRO A . n 
A 1 44  MET   44  43  43  MET   MET A . n 
A 1 45  GLN   45  44  44  GLN   GLN A . n 
A 1 46  PRO   46  45  45  PRO   PRO A . n 
A 1 47  GLY   47  46  46  GLY   GLY A . n 
A 1 48  PHE   48  47  47  PHE   PHE A . n 
A 1 49  PRO   49  48  48  PRO   PRO A . n 
A 1 50  GLU   50  49  49  GLU   GLU A . n 
A 1 51  ASN   51  50  50  ASN   ASN A . n 
A 1 52  LEU   52  51  51  LEU   LEU A . n 
A 1 53  SER   53  52  52  SER   SER A . n 
A 1 54  LYS   54  53  53  LYS   LYS A . n 
A 1 55  LEU   55  54  54  LEU   LEU A . n 
A 1 56  LYS   56  55  55  LYS   LYS A . n 
A 1 57  SER   57  56  56  SER   SER A . n 
A 1 58  LEU   58  57  57  LEU   LEU A . n 
A 1 59  LEU   59  58  58  LEU   LEU A . n 
A 1 60  THR   60  59  59  THR   THR A . n 
A 1 61  GLN   61  60  60  GLN   GLN A . n 
A 1 62  LEU   62  61  61  LEU   LEU A . n 
A 1 63  ARG   63  62  62  ARG   ARG A . n 
A 1 64  ALA   64  63  63  ALA   ALA A . n 
A 1 65  GLU   65  64  64  GLU   GLU A . n 
A 1 66  ASP   66  65  65  ASP   ASP A . n 
A 1 67  LEU   67  66  66  LEU   LEU A . n 
A 1 68  ASN   68  67  67  ASN   ASN A . n 
A 1 69  ILE   69  68  68  ILE   ILE A . n 
A 1 70  ALA   70  69  69  ALA   ALA A . n 
A 1 71  PRO   71  70  70  PRO   PRO A . n 
A 1 72  ARG   72  71  71  ARG   ARG A . n 
A 1 73  LYS   73  72  72  LYS   LYS A . n 
A 1 74  ALA   74  73  73  ALA   ALA A . n 
A 1 75  THR   75  74  74  THR   THR A . n 
A 1 76  LEU   76  75  75  LEU   LEU A . n 
A 1 77  GLN   77  76  76  GLN   GLN A . n 
A 1 78  PRO   78  77  77  PRO   PRO A . n 
A 1 79  LEU   79  78  78  LEU   LEU A . n 
A 1 80  PRO   80  79  79  PRO   PRO A . n 
A 1 81  PRO   81  80  80  PRO   PRO A . n 
A 1 82  ASN   82  81  81  ASN   ASN A . n 
A 1 83  LEU   83  82  82  LEU   LEU A . n 
A 1 84  PRO   84  83  83  PRO   PRO A . n 
A 1 85  PRO   85  84  84  PRO   PRO A . n 
A 1 86  VAL   86  85  85  VAL   VAL A . n 
A 1 87  THR   87  86  86  THR   THR A . n 
A 1 88  TYR   88  87  87  TYR   TYR A . n 
A 1 89  MET   89  88  88  MET   MET A . n 
A 1 90  HIS   90  89  89  HIS   HIS A . n 
A 1 91  ILE   91  90  90  ILE   ILE A . n 
A 1 92  TYR   92  91  91  TYR   TYR A . n 
A 1 93  GLU   93  92  92  GLU   GLU A . n 
A 1 94  THR   94  93  93  THR   THR A . n 
A 1 95  ASP   95  94  94  ASP   ASP A . n 
A 1 96  GLY   96  95  95  GLY   GLY A . n 
A 1 97  PHE   97  96  96  PHE   PHE A . n 
A 1 98  SER   98  97  97  SER   SER A . n 
A 1 99  LEU   99  98  98  LEU   LEU A . n 
A 1 100 GLY   100 99  99  GLY   GLY A . n 
A 1 101 VAL   101 100 100 VAL   VAL A . n 
A 1 102 PHE   102 101 101 PHE   PHE A . n 
A 1 103 LEU   103 102 102 LEU   LEU A . n 
A 1 104 LEU   104 103 103 LEU   LEU A . n 
A 1 105 LYS   105 104 104 LYS   LYS A . n 
A 1 106 SER   106 105 105 SER   SER A . n 
A 1 107 GLY   107 106 106 GLY   GLY A . n 
A 1 108 THR   108 107 107 THR   THR A . n 
A 1 109 SER   109 108 108 SER   SER A . n 
A 1 110 ILE   110 109 109 ILE   ILE A . n 
A 1 111 PRO   111 110 110 PRO   PRO A . n 
A 1 112 LEU   112 111 111 LEU   LEU A . n 
A 1 113 HIS   113 112 112 HIS   HIS A . n 
A 1 114 ASP   114 113 113 ASP   ASP A . n 
A 1 115 HIS   115 114 114 HIS   HIS A . n 
A 1 116 PRO   116 115 115 PRO   PRO A . n 
A 1 117 GLY   117 116 116 GLY   GLY A . n 
A 1 118 MET   118 117 117 MET   MET A . n 
A 1 119 HIS   119 118 118 HIS   HIS A . n 
A 1 120 GLY   120 119 119 GLY   GLY A . n 
A 1 121 MET   121 120 120 MET   MET A . n 
A 1 122 LEU   122 121 121 LEU   LEU A . n 
A 1 123 LYS   123 122 122 LYS   LYS A . n 
A 1 124 VAL   124 123 123 VAL   VAL A . n 
A 1 125 LEU   125 124 124 LEU   LEU A . n 
A 1 126 TYR   126 125 125 TYR   TYR A . n 
A 1 127 GLY   127 126 126 GLY   GLY A . n 
A 1 128 THR   128 127 127 THR   THR A . n 
A 1 129 VAL   129 128 128 VAL   VAL A . n 
A 1 130 ARG   130 129 129 ARG   ARG A . n 
A 1 131 ILE   131 130 130 ILE   ILE A . n 
A 1 132 SER   132 131 131 SER   SER A . n 
A 1 133 CYS   133 132 132 CYS   CYS A . n 
A 1 134 MET   134 133 133 MET   MET A . n 
A 1 135 ASP   135 134 134 ASP   ASP A . n 
A 1 136 LYS   136 135 135 LYS   LYS A . n 
A 1 137 LEU   137 136 136 LEU   LEU A . n 
A 1 138 ASP   138 137 137 ASP   ASP A . n 
A 1 139 ALA   139 138 ?   ?     ?   A . n 
A 1 140 GLY   140 139 ?   ?     ?   A . n 
A 1 141 GLY   141 140 ?   ?     ?   A . n 
A 1 142 GLY   142 141 ?   ?     ?   A . n 
A 1 143 GLN   143 142 ?   ?     ?   A . n 
A 1 144 ARG   144 143 ?   ?     ?   A . n 
A 1 145 PRO   145 144 ?   ?     ?   A . n 
A 1 146 ARG   146 145 145 ARG   ARG A . n 
A 1 147 ALA   147 146 146 ALA   ALA A . n 
A 1 148 LEU   148 147 147 LEU   LEU A . n 
A 1 149 PRO   149 148 148 PRO   PRO A . n 
A 1 150 PRO   150 149 149 PRO   PRO A . n 
A 1 151 GLU   151 150 150 GLU   GLU A . n 
A 1 152 GLN   152 151 151 GLN   GLN A . n 
A 1 153 GLN   153 152 152 GLN   GLN A . n 
A 1 154 PHE   154 153 153 PHE   PHE A . n 
A 1 155 GLU   155 154 154 GLU   GLU A . n 
A 1 156 PRO   156 155 155 PRO   PRO A . n 
A 1 157 PRO   157 156 156 PRO   PRO A . n 
A 1 158 LEU   158 157 157 LEU   LEU A . n 
A 1 159 GLN   159 158 158 GLN   GLN A . n 
A 1 160 PRO   160 159 159 PRO   PRO A . n 
A 1 161 ARG   161 160 160 ARG   ARG A . n 
A 1 162 GLU   162 161 161 GLU   GLU A . n 
A 1 163 ARG   163 162 162 ARG   ARG A . n 
A 1 164 GLU   164 163 163 GLU   GLU A . n 
A 1 165 ALA   165 164 164 ALA   ALA A . n 
A 1 166 VAL   166 165 165 VAL   VAL A . n 
A 1 167 ARG   167 166 166 ARG   ARG A . n 
A 1 168 PRO   168 167 167 PRO   PRO A . n 
A 1 169 GLY   169 168 168 GLY   GLY A . n 
A 1 170 VAL   170 169 169 VAL   VAL A . n 
A 1 171 LEU   171 170 170 LEU   LEU A . n 
A 1 172 ARG   172 171 171 ARG   ARG A . n 
A 1 173 SER   173 172 172 SER   SER A . n 
A 1 174 ARG   174 173 173 ARG   ARG A . n 
A 1 175 ALA   175 174 174 ALA   ALA A . n 
A 1 176 GLU   176 175 175 GLU   GLU A . n 
A 1 177 TYR   177 176 176 TYR   TYR A . n 
A 1 178 THR   178 177 177 THR   THR A . n 
A 1 179 GLU   179 178 178 GLU   GLU A . n 
A 1 180 ALA   180 179 179 ALA   ALA A . n 
A 1 181 SER   181 180 180 SER   SER A . n 
A 1 182 GLY   182 181 181 GLY   GLY A . n 
A 1 183 PRO   183 182 182 PRO   PRO A . n 
A 1 184 CYS   184 183 183 CYS   CYS A . n 
A 1 185 ILE   185 184 184 ILE   ILE A . n 
A 1 186 LEU   186 185 185 LEU   LEU A . n 
A 1 187 THR   187 186 186 THR   THR A . n 
A 1 188 PRO   188 187 187 PRO   PRO A . n 
A 1 189 HIS   189 188 188 HIS   HIS A . n 
A 1 190 ARG   190 189 189 ARG   ARG A . n 
A 1 191 ASP   191 190 190 ASP   ASP A . n 
A 1 192 ASN   192 191 191 ASN   ASN A . n 
A 1 193 LEU   193 192 192 LEU   LEU A . n 
A 1 194 HIS   194 193 193 HIS   HIS A . n 
A 1 195 GLN   195 194 194 GLN   GLN A . n 
A 1 196 ILE   196 195 195 ILE   ILE A . n 
A 1 197 ASP   197 196 196 ASP   ASP A . n 
A 1 198 ALA   198 197 197 ALA   ALA A . n 
A 1 199 VAL   199 198 198 VAL   VAL A . n 
A 1 200 GLU   200 199 199 GLU   GLU A . n 
A 1 201 GLY   201 200 200 GLY   GLY A . n 
A 1 202 PRO   202 201 201 PRO   PRO A . n 
A 1 203 ALA   203 202 202 ALA   ALA A . n 
A 1 204 ALA   204 203 203 ALA   ALA A . n 
A 1 205 PHE   205 204 204 PHE   PHE A . n 
A 1 206 LEU   206 205 205 LEU   LEU A . n 
A 1 207 ASP   207 206 206 ASP   ASP A . n 
A 1 208 ILE   208 207 207 ILE   ILE A . n 
A 1 209 LEU   209 208 208 LEU   LEU A . n 
A 1 210 ALA   210 209 209 ALA   ALA A . n 
A 1 211 PRO   211 210 210 PRO   PRO A . n 
A 1 212 PRO   212 211 211 PRO   PRO A . n 
A 1 213 TYR   213 212 212 TYR   TYR A . n 
A 1 214 ASP   214 213 213 ASP   ASP A . n 
A 1 215 PRO   215 214 214 PRO   PRO A . n 
A 1 216 ASP   216 215 215 ASP   ASP A . n 
A 1 217 ASP   217 216 216 ASP   ASP A . n 
A 1 218 GLY   218 217 217 GLY   GLY A . n 
A 1 219 ARG   219 218 218 ARG   ARG A . n 
A 1 220 ASP   220 219 219 ASP   ASP A . n 
A 1 221 CYS   221 220 220 CYS   CYS A . n 
A 1 222 HIS   222 221 221 HIS   HIS A . n 
A 1 223 TYR   223 222 222 TYR   TYR A . n 
A 1 224 TYR   224 223 223 TYR   TYR A . n 
A 1 225 ARG   225 224 224 ARG   ARG A . n 
A 1 226 VAL   226 225 225 VAL   VAL A . n 
A 1 227 LEU   227 226 226 LEU   LEU A . n 
A 1 228 GLU   228 227 227 GLU   GLU A . n 
A 1 229 PRO   229 228 228 PRO   PRO A . n 
A 1 230 VAL   230 229 229 VAL   VAL A . n 
A 1 231 ARG   231 230 ?   ?     ?   A . n 
A 1 232 PRO   232 231 ?   ?     ?   A . n 
A 1 233 LYS   233 232 ?   ?     ?   A . n 
A 1 234 GLU   234 233 ?   ?     ?   A . n 
A 1 235 ALA   235 234 ?   ?     ?   A . n 
A 1 236 SER   236 235 ?   ?     ?   A . n 
A 1 237 SER   237 236 ?   ?     ?   A . n 
A 1 238 SER   238 237 ?   ?     ?   A . n 
A 1 239 ALA   239 238 ?   ?     ?   A . n 
A 1 240 SER   240 239 ?   ?     ?   A . n 
A 1 241 ASP   241 240 240 ASP   ASP A . n 
A 1 242 LEU   242 241 241 LEU   LEU A . n 
A 1 243 PRO   243 242 242 PRO   PRO A . n 
A 1 244 ARG   244 243 243 ARG   ARG A . n 
A 1 245 GLU   245 244 244 GLU   GLU A . n 
A 1 246 VAL   246 245 245 VAL   VAL A . n 
A 1 247 TRP   247 246 246 TRP   TRP A . n 
A 1 248 LEU   248 247 247 LEU   LEU A . n 
A 1 249 LEU   249 248 248 LEU   LEU A . n 
A 1 250 GLU   250 249 249 GLU   GLU A . n 
A 1 251 THR   251 250 250 THR   THR A . n 
A 1 252 PRO   252 251 251 PRO   PRO A . n 
A 1 253 GLN   253 252 252 GLN   GLN A . n 
A 1 254 ALA   254 253 253 ALA   ALA A . n 
A 1 255 ASP   255 254 254 ASP   ASP A . n 
A 1 256 ASP   256 255 255 ASP   ASP A . n 
A 1 257 PHE   257 256 256 PHE   PHE A . n 
A 1 258 TRP   258 257 257 TRP   TRP A . n 
A 1 259 CYS   259 258 258 CYS   CYS A . n 
A 1 260 GLU   260 259 259 GLU   GLU A . n 
A 1 261 GLY   261 260 260 GLY   GLY A . n 
A 1 262 GLU   262 261 261 GLU   GLU A . n 
A 1 263 PRO   263 262 262 PRO   PRO A . n 
A 1 264 TYR   264 263 263 TYR   TYR A . n 
A 1 265 PRO   265 264 264 PRO   PRO A . n 
A 1 266 GLY   266 265 265 GLY   GLY A . n 
A 1 267 PRO   267 266 266 PRO   PRO A . n 
A 1 268 LYS   268 267 267 LYS   LYS A . n 
A 1 269 VAL   269 268 268 VAL   VAL A . n 
A 1 270 PHE   270 269 269 PHE   PHE A . n 
A 1 271 PRO   271 270 270 PRO   PRO A . n 
B 2 1   ACE   1   0   0   ACE   ACE B . n 
B 2 2   TYR   2   1   1   TYR   TYR B . n 
B 2 3   ILE   3   2   2   ILE   ILE B . n 
B 2 4   VAL   4   3   3   VAL   VAL B . n 
B 2 5   LYS   5   4   4   LYS   LYS B . n 
B 2 6   THR   6   5   5   THR   THR B . n 
B 2 7   PHE   7   6   6   PHE   PHE B . n 
B 2 8   TRP   8   7   7   TRP   TRP B . n 
B 2 9   A1BC5 9   8   8   A1BC5 LIG B . n 
B 2 10  GLY   10  9   9   GLY   GLY B . n 
B 2 11  SER   11  10  10  SER   SER B . n 
B 2 12  HIS   12  11  11  HIS   HIS B . n 
B 2 13  ARG   13  12  12  ARG   ARG B . n 
B 2 14  GLN   14  13  13  GLN   GLN B . n 
B 2 15  CYS   15  14  14  CYS   CYS B . n 
B 2 16  NH2   16  15  15  NH2   NH2 B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CO 
_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 
C 3 CO  1   301 1   CO  CO  A . 
D 4 CL  1   302 1   CL  CL  A . 
E 4 CL  1   303 2   CL  CL  A . 
F 5 GOL 1   304 3   GOL GOL A . 
G 5 GOL 1   305 4   GOL GOL A . 
H 5 GOL 1   306 5   GOL GOL A . 
I 5 GOL 1   307 6   GOL GOL A . 
J 5 GOL 1   308 7   GOL GOL A . 
K 6 HOH 1   401 166 HOH HOH A . 
K 6 HOH 2   402 118 HOH HOH A . 
K 6 HOH 3   403 150 HOH HOH A . 
K 6 HOH 4   404 186 HOH HOH A . 
K 6 HOH 5   405 188 HOH HOH A . 
K 6 HOH 6   406 156 HOH HOH A . 
K 6 HOH 7   407 132 HOH HOH A . 
K 6 HOH 8   408 31  HOH HOH A . 
K 6 HOH 9   409 170 HOH HOH A . 
K 6 HOH 10  410 17  HOH HOH A . 
K 6 HOH 11  411 25  HOH HOH A . 
K 6 HOH 12  412 115 HOH HOH A . 
K 6 HOH 13  413 57  HOH HOH A . 
K 6 HOH 14  414 110 HOH HOH A . 
K 6 HOH 15  415 111 HOH HOH A . 
K 6 HOH 16  416 184 HOH HOH A . 
K 6 HOH 17  417 51  HOH HOH A . 
K 6 HOH 18  418 101 HOH HOH A . 
K 6 HOH 19  419 117 HOH HOH A . 
K 6 HOH 20  420 94  HOH HOH A . 
K 6 HOH 21  421 12  HOH HOH A . 
K 6 HOH 22  422 38  HOH HOH A . 
K 6 HOH 23  423 127 HOH HOH A . 
K 6 HOH 24  424 11  HOH HOH A . 
K 6 HOH 25  425 42  HOH HOH A . 
K 6 HOH 26  426 45  HOH HOH A . 
K 6 HOH 27  427 120 HOH HOH A . 
K 6 HOH 28  428 125 HOH HOH A . 
K 6 HOH 29  429 29  HOH HOH A . 
K 6 HOH 30  430 53  HOH HOH A . 
K 6 HOH 31  431 52  HOH HOH A . 
K 6 HOH 32  432 48  HOH HOH A . 
K 6 HOH 33  433 40  HOH HOH A . 
K 6 HOH 34  434 91  HOH HOH A . 
K 6 HOH 35  435 4   HOH HOH A . 
K 6 HOH 36  436 102 HOH HOH A . 
K 6 HOH 37  437 100 HOH HOH A . 
K 6 HOH 38  438 54  HOH HOH A . 
K 6 HOH 39  439 46  HOH HOH A . 
K 6 HOH 40  440 106 HOH HOH A . 
K 6 HOH 41  441 140 HOH HOH A . 
K 6 HOH 42  442 131 HOH HOH A . 
K 6 HOH 43  443 33  HOH HOH A . 
K 6 HOH 44  444 64  HOH HOH A . 
K 6 HOH 45  445 36  HOH HOH A . 
K 6 HOH 46  446 62  HOH HOH A . 
K 6 HOH 47  447 153 HOH HOH A . 
K 6 HOH 48  448 72  HOH HOH A . 
K 6 HOH 49  449 5   HOH HOH A . 
K 6 HOH 50  450 103 HOH HOH A . 
K 6 HOH 51  451 59  HOH HOH A . 
K 6 HOH 52  452 27  HOH HOH A . 
K 6 HOH 53  453 26  HOH HOH A . 
K 6 HOH 54  454 96  HOH HOH A . 
K 6 HOH 55  455 65  HOH HOH A . 
K 6 HOH 56  456 99  HOH HOH A . 
K 6 HOH 57  457 87  HOH HOH A . 
K 6 HOH 58  458 149 HOH HOH A . 
K 6 HOH 59  459 97  HOH HOH A . 
K 6 HOH 60  460 78  HOH HOH A . 
K 6 HOH 61  461 162 HOH HOH A . 
K 6 HOH 62  462 28  HOH HOH A . 
K 6 HOH 63  463 32  HOH HOH A . 
K 6 HOH 64  464 135 HOH HOH A . 
K 6 HOH 65  465 88  HOH HOH A . 
K 6 HOH 66  466 30  HOH HOH A . 
K 6 HOH 67  467 123 HOH HOH A . 
K 6 HOH 68  468 34  HOH HOH A . 
K 6 HOH 69  469 1   HOH HOH A . 
K 6 HOH 70  470 3   HOH HOH A . 
K 6 HOH 71  471 39  HOH HOH A . 
K 6 HOH 72  472 47  HOH HOH A . 
K 6 HOH 73  473 81  HOH HOH A . 
K 6 HOH 74  474 68  HOH HOH A . 
K 6 HOH 75  475 119 HOH HOH A . 
K 6 HOH 76  476 55  HOH HOH A . 
K 6 HOH 77  477 134 HOH HOH A . 
K 6 HOH 78  478 43  HOH HOH A . 
K 6 HOH 79  479 104 HOH HOH A . 
K 6 HOH 80  480 63  HOH HOH A . 
K 6 HOH 81  481 16  HOH HOH A . 
K 6 HOH 82  482 129 HOH HOH A . 
K 6 HOH 83  483 60  HOH HOH A . 
K 6 HOH 84  484 121 HOH HOH A . 
K 6 HOH 85  485 49  HOH HOH A . 
K 6 HOH 86  486 6   HOH HOH A . 
K 6 HOH 87  487 155 HOH HOH A . 
K 6 HOH 88  488 176 HOH HOH A . 
K 6 HOH 89  489 56  HOH HOH A . 
K 6 HOH 90  490 105 HOH HOH A . 
K 6 HOH 91  491 93  HOH HOH A . 
K 6 HOH 92  492 83  HOH HOH A . 
K 6 HOH 93  493 108 HOH HOH A . 
K 6 HOH 94  494 142 HOH HOH A . 
K 6 HOH 95  495 71  HOH HOH A . 
K 6 HOH 96  496 92  HOH HOH A . 
K 6 HOH 97  497 58  HOH HOH A . 
K 6 HOH 98  498 37  HOH HOH A . 
K 6 HOH 99  499 20  HOH HOH A . 
K 6 HOH 100 500 148 HOH HOH A . 
K 6 HOH 101 501 44  HOH HOH A . 
K 6 HOH 102 502 61  HOH HOH A . 
K 6 HOH 103 503 22  HOH HOH A . 
K 6 HOH 104 504 173 HOH HOH A . 
K 6 HOH 105 505 69  HOH HOH A . 
K 6 HOH 106 506 165 HOH HOH A . 
K 6 HOH 107 507 98  HOH HOH A . 
K 6 HOH 108 508 122 HOH HOH A . 
K 6 HOH 109 509 21  HOH HOH A . 
K 6 HOH 110 510 8   HOH HOH A . 
K 6 HOH 111 511 13  HOH HOH A . 
K 6 HOH 112 512 15  HOH HOH A . 
K 6 HOH 113 513 141 HOH HOH A . 
K 6 HOH 114 514 114 HOH HOH A . 
K 6 HOH 115 515 35  HOH HOH A . 
K 6 HOH 116 516 74  HOH HOH A . 
K 6 HOH 117 517 50  HOH HOH A . 
K 6 HOH 118 518 66  HOH HOH A . 
K 6 HOH 119 519 23  HOH HOH A . 
K 6 HOH 120 520 10  HOH HOH A . 
K 6 HOH 121 521 79  HOH HOH A . 
K 6 HOH 122 522 2   HOH HOH A . 
K 6 HOH 123 523 76  HOH HOH A . 
K 6 HOH 124 524 161 HOH HOH A . 
K 6 HOH 125 525 130 HOH HOH A . 
K 6 HOH 126 526 177 HOH HOH A . 
K 6 HOH 127 527 179 HOH HOH A . 
K 6 HOH 128 528 195 HOH HOH A . 
K 6 HOH 129 529 124 HOH HOH A . 
K 6 HOH 130 530 168 HOH HOH A . 
K 6 HOH 131 531 113 HOH HOH A . 
K 6 HOH 132 532 14  HOH HOH A . 
K 6 HOH 133 533 90  HOH HOH A . 
K 6 HOH 134 534 197 HOH HOH A . 
K 6 HOH 135 535 151 HOH HOH A . 
K 6 HOH 136 536 144 HOH HOH A . 
K 6 HOH 137 537 146 HOH HOH A . 
K 6 HOH 138 538 198 HOH HOH A . 
K 6 HOH 139 539 67  HOH HOH A . 
K 6 HOH 140 540 77  HOH HOH A . 
K 6 HOH 141 541 189 HOH HOH A . 
K 6 HOH 142 542 164 HOH HOH A . 
K 6 HOH 143 543 133 HOH HOH A . 
K 6 HOH 144 544 143 HOH HOH A . 
K 6 HOH 145 545 180 HOH HOH A . 
K 6 HOH 146 546 194 HOH HOH A . 
K 6 HOH 147 547 89  HOH HOH A . 
K 6 HOH 148 548 147 HOH HOH A . 
K 6 HOH 149 549 183 HOH HOH A . 
K 6 HOH 150 550 157 HOH HOH A . 
K 6 HOH 151 551 84  HOH HOH A . 
K 6 HOH 152 552 163 HOH HOH A . 
K 6 HOH 153 553 191 HOH HOH A . 
K 6 HOH 154 554 18  HOH HOH A . 
K 6 HOH 155 555 171 HOH HOH A . 
K 6 HOH 156 556 112 HOH HOH A . 
K 6 HOH 157 557 107 HOH HOH A . 
K 6 HOH 158 558 174 HOH HOH A . 
K 6 HOH 159 559 158 HOH HOH A . 
K 6 HOH 160 560 139 HOH HOH A . 
K 6 HOH 161 561 187 HOH HOH A . 
K 6 HOH 162 562 126 HOH HOH A . 
K 6 HOH 163 563 152 HOH HOH A . 
K 6 HOH 164 564 116 HOH HOH A . 
K 6 HOH 165 565 82  HOH HOH A . 
K 6 HOH 166 566 73  HOH HOH A . 
K 6 HOH 167 567 185 HOH HOH A . 
K 6 HOH 168 568 138 HOH HOH A . 
K 6 HOH 169 569 190 HOH HOH A . 
K 6 HOH 170 570 95  HOH HOH A . 
K 6 HOH 171 571 175 HOH HOH A . 
K 6 HOH 172 572 172 HOH HOH A . 
K 6 HOH 173 573 200 HOH HOH A . 
K 6 HOH 174 574 80  HOH HOH A . 
K 6 HOH 175 575 70  HOH HOH A . 
K 6 HOH 176 576 169 HOH HOH A . 
K 6 HOH 177 577 136 HOH HOH A . 
K 6 HOH 178 578 128 HOH HOH A . 
K 6 HOH 179 579 199 HOH HOH A . 
K 6 HOH 180 580 24  HOH HOH A . 
K 6 HOH 181 581 41  HOH HOH A . 
K 6 HOH 182 582 192 HOH HOH A . 
K 6 HOH 183 583 160 HOH HOH A . 
K 6 HOH 184 584 196 HOH HOH A . 
K 6 HOH 185 585 167 HOH HOH A . 
K 6 HOH 186 586 193 HOH HOH A . 
K 6 HOH 187 587 159 HOH HOH A . 
L 6 HOH 1   101 145 HOH HOH B . 
L 6 HOH 2   102 7   HOH HOH B . 
L 6 HOH 3   103 109 HOH HOH B . 
L 6 HOH 4   104 9   HOH HOH B . 
L 6 HOH 5   105 85  HOH HOH B . 
L 6 HOH 6   106 75  HOH HOH B . 
L 6 HOH 7   107 137 HOH HOH B . 
L 6 HOH 8   108 19  HOH HOH B . 
L 6 HOH 9   109 181 HOH HOH B . 
L 6 HOH 10  110 86  HOH HOH B . 
L 6 HOH 11  111 178 HOH HOH B . 
L 6 HOH 12  112 154 HOH HOH B . 
L 6 HOH 13  113 182 HOH HOH B . 
# 
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 ASN 5   ? CG  ? A ASN 6   CG  
2  1 Y 1 A ASN 5   ? OD1 ? A ASN 6   OD1 
3  1 Y 1 A ASN 5   ? ND2 ? A ASN 6   ND2 
4  1 Y 0 A ARG 22  ? CD  ? A ARG 23  CD  
5  1 Y 0 A ARG 22  ? NE  ? A ARG 23  NE  
6  1 Y 0 A ARG 22  ? CZ  ? A ARG 23  CZ  
7  1 Y 0 A ARG 22  ? NH1 ? A ARG 23  NH1 
8  1 Y 0 A ARG 22  ? NH2 ? A ARG 23  NH2 
9  1 Y 1 A ALA 41  ? CB  ? A ALA 42  CB  
10 1 Y 0 A PRO 42  ? CB  ? A PRO 43  CB  
11 1 Y 0 A PRO 42  ? CG  ? A PRO 43  CG  
12 1 Y 0 A PRO 42  ? CD  ? A PRO 43  CD  
13 1 Y 1 A MET 43  ? CG  ? A MET 44  CG  
14 1 Y 1 A MET 43  ? SD  ? A MET 44  SD  
15 1 Y 1 A MET 43  ? CE  ? A MET 44  CE  
16 1 Y 0 A MET 43  ? N   ? A MET 44  N   
17 1 Y 0 A ARG 62  ? CZ  ? A ARG 63  CZ  
18 1 Y 0 A ARG 62  ? NH1 ? A ARG 63  NH1 
19 1 Y 1 A GLU 150 ? CG  ? A GLU 151 CG  
20 1 Y 1 A GLU 150 ? CD  ? A GLU 151 CD  
21 1 Y 1 A GLU 150 ? OE1 ? A GLU 151 OE1 
22 1 Y 1 A GLU 150 ? OE2 ? A GLU 151 OE2 
23 1 Y 0 A ARG 160 ? NE  ? A ARG 161 NE  
24 1 Y 0 A ARG 160 ? CZ  ? A ARG 161 CZ  
25 1 Y 0 A GLU 178 ? CD  ? A GLU 179 CD  
26 1 Y 0 A GLU 227 ? CD  ? A GLU 228 CD  
27 1 Y 0 A GLU 227 ? OE1 ? A GLU 228 OE1 
28 1 Y 0 A GLU 227 ? OE2 ? A GLU 228 OE2 
29 1 Y 0 A GLU 244 ? CD  ? A GLU 245 CD  
30 1 Y 0 A PRO 270 ? C   ? A PRO 271 C   
31 1 Y 0 A PRO 270 ? O   ? A PRO 271 O   
32 1 N 0 A GOL 308 ? C3  ? J GOL ?   C3  
33 1 N 0 A GOL 308 ? O3  ? J GOL ?   O3  
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 ? 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           ? 3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           ? 4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           ? 5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DXB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     36.015 
_cell.length_a_esd                 ? 
_cell.length_b                     71.879 
_cell.length_b_esd                 ? 
_cell.length_c                     108.894 
_cell.length_c_esd                 ? 
_cell.volume                       281896.314 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DXB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (z,x,y)' 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_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                   9DXB 
_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             2.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.66 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_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_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M BIS-Tris, pH 5.5,  25% w/v PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_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   0.9537 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          28.69 
_reflns.entry_id                                       9DXB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.74 
_reflns.d_resolution_low                               43.40 
_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                                     ? 
_reflns.number_obs                                     30023 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.4 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.055 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_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                        ? 
# 
_reflns_shell.d_res_high                                    1.74 
_reflns_shell.d_res_low                                     1.77 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1527 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_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                               12.4 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.852 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.800 
_reflns_shell.pdbx_Rsym_value                               ? 
_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               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               35.04 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9DXB 
_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                            1.74 
_refine.ls_d_res_low                             43.40 
_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                     29967 
_refine.ls_number_reflns_R_free                  1500 
_refine.ls_number_reflns_R_work                  28467 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.75 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1782 
_refine.ls_R_factor_R_free                       0.2177 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1761 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 21.1981 
_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                            0.2312 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.74 
_refine_hist.d_res_low                        43.40 
_refine_hist.number_atoms_solvent             200 
_refine_hist.number_atoms_total               2188 
_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       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1955 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0072 ? 2144 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 1.0060 ? 2932 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 0.0634 ? 316  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.0097 ? 384  ? f_plane_restr      ? ? ? 
'X-RAY DIFFRACTION' ? 7.2881 ? 314  ? f_dihedral_angle_d ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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_error 
_refine_ls_shell.R_factor_R_work 
_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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.74 1.79  . . 119 2494 97.54  . . . . 0.3372 . . . . . . . . . . . . . . . 0.3604 
'X-RAY DIFFRACTION' 1.79 1.86  . . 134 2529 99.96  . . . . 0.2428 . . . . . . . . . . . . . . . 0.2958 
'X-RAY DIFFRACTION' 1.86 1.93  . . 125 2547 100.00 . . . . 0.1906 . . . . . . . . . . . . . . . 0.2224 
'X-RAY DIFFRACTION' 1.93 2.02  . . 158 2563 100.00 . . . . 0.1676 . . . . . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 2.02 2.12  . . 137 2573 99.96  . . . . 0.1784 . . . . . . . . . . . . . . . 0.2352 
'X-RAY DIFFRACTION' 2.12 2.26  . . 149 2554 99.93  . . . . 0.1966 . . . . . . . . . . . . . . . 0.2162 
'X-RAY DIFFRACTION' 2.26 2.43  . . 125 2565 100.00 . . . . 0.1845 . . . . . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 2.43 2.68  . . 128 2609 100.00 . . . . 0.1898 . . . . . . . . . . . . . . . 0.2441 
'X-RAY DIFFRACTION' 2.68 3.06  . . 144 2595 100.00 . . . . 0.1846 . . . . . . . . . . . . . . . 0.2465 
'X-RAY DIFFRACTION' 3.06 3.86  . . 150 2633 100.00 . . . . 0.1633 . . . . . . . . . . . . . . . 0.2055 
'X-RAY DIFFRACTION' 3.86 43.40 . . 131 2805 99.83  . . . . 0.1565 . . . . . . . . . . . . . . . 0.1852 
# 
_struct.entry_id                     9DXB 
_struct.title                        
;Crystal structure of cobalt-incorporated human 2-aminoethanethiol (aka cysteamine) dioxygenase (ADO) variant C18S/C239S in complex with CP6-L8d-Gly-Ser
;
_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        9DXB 
_struct_keywords.text            'oxygen-sensor, thiol dioxygenase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP AEDO_HUMAN Q96SZ5 ? 1 
;MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQLRAEDLNIAPRKATLQPLPP
NLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGMLKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPR
EREAVRPGVLRSRAEYTEASGPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACD
LPREVWLLETPQADDFWCEGEPYPGPKVFP
;
1 
2 PDB 9DXB       9DXB   ? 2 ? 1 
# 
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 9DXB A 2 ? 271 ? Q96SZ5 1 ? 270 ? 1 270 
2 2 9DXB B 1 ? 16  ? 9DXB   0 ? 15  ? 0 15  
# 
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 9DXB SER A 1   ? UNP Q96SZ5 ?   ?   'expression tag' 0   1 
1 9DXB SER A 19  ? UNP Q96SZ5 CYS 18  conflict         18  2 
1 9DXB SER A 240 ? UNP Q96SZ5 CYS 239 conflict         239 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3370  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  12600 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 SER A 9   ? PHE A 22  ? SER A 8   PHE A 21  1 ? 14 
HELX_P HELX_P2 AA2 GLY A 47  ? LEU A 62  ? GLY A 46  LEU A 61  1 ? 16 
HELX_P HELX_P3 AA3 ARG A 63  ? ASN A 68  ? ARG A 62  ASN A 67  5 ? 6  
HELX_P HELX_P4 AA4 GLN A 159 ? VAL A 166 ? GLN A 158 VAL A 165 1 ? 8  
HELX_P HELX_P5 AA5 ASP A 214 ? GLY A 218 ? ASP A 213 GLY A 217 5 ? 5  
# 
_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 
covale1 covale both ? B ACE   1   C   ? ? ? 1_555 B TYR   2  N   ? ? B ACE   0   B TYR   1   1_555 ? ? ? ? ? ? ? 1.319 ? ? 
covale2 covale none ? B ACE   1   CH3 ? ? ? 1_555 B CYS   15 SG  ? ? B ACE   0   B CYS   14  1_555 ? ? ? ? ? ? ? 1.766 ? ? 
covale3 covale one  ? B TRP   8   C   ? ? ? 1_555 B A1BC5 9  N   ? ? B TRP   7   B A1BC5 8   1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale4 covale both ? B A1BC5 9   C   ? ? ? 1_555 B GLY   10 N   ? ? B A1BC5 8   B GLY   9   1_555 ? ? ? ? ? ? ? 1.427 ? ? 
covale5 covale both ? B CYS   15  C   ? ? ? 1_555 B NH2   16 N   ? ? B CYS   14  B NH2   15  1_555 ? ? ? ? ? ? ? 1.427 ? ? 
metalc1 metalc ?    ? A HIS   113 NE2 ? ? ? 1_555 C CO    .  CO  ? ? A HIS   112 A CO    301 1_555 ? ? ? ? ? ? ? 2.169 ? ? 
metalc2 metalc ?    ? A HIS   115 NE2 ? ? ? 1_555 C CO    .  CO  ? ? A HIS   114 A CO    301 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
metalc3 metalc ?    ? A HIS   194 NE2 ? ? ? 1_555 C CO    .  CO  ? ? A HIS   193 A CO    301 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc4 metalc ?    ? C CO    .   CO  ? ? ? 1_555 K HOH   .  O   ? ? A CO    301 A HOH   449 1_555 ? ? ? ? ? ? ? 2.286 ? ? 
metalc5 metalc ?    ? C CO    .   CO  ? ? ? 1_555 B A1BC5 9  N15 ? ? A CO    301 B A1BC5 8   1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc6 metalc ?    ? C CO    .   CO  ? ? ? 1_555 B A1BC5 9  O16 ? ? A CO    301 B A1BC5 8   1_555 ? ? ? ? ? ? ? 2.133 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
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   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 NE2 ? A HIS   115 ? A HIS   114 ? 1_555 93.4  ? 
2  NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 NE2 ? A HIS   194 ? A HIS   193 ? 1_555 90.5  ? 
3  NE2 ? A HIS   115 ? A HIS   114 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 NE2 ? A HIS   194 ? A HIS   193 ? 1_555 93.7  ? 
4  NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O   ? K HOH   .   ? A HOH   449 ? 1_555 179.1 ? 
5  NE2 ? A HIS   115 ? A HIS   114 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O   ? K HOH   .   ? A HOH   449 ? 1_555 87.3  ? 
6  NE2 ? A HIS   194 ? A HIS   193 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O   ? K HOH   .   ? A HOH   449 ? 1_555 90.1  ? 
7  NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 N15 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 101.1 ? 
8  NE2 ? A HIS   115 ? A HIS   114 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 N15 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 162.3 ? 
9  NE2 ? A HIS   194 ? A HIS   193 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 N15 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 96.3  ? 
10 O   ? K HOH   .   ? A HOH   449 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 N15 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 78.1  ? 
11 NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O16 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 90.3  ? 
12 NE2 ? A HIS   115 ? A HIS   114 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O16 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 91.5  ? 
13 NE2 ? A HIS   194 ? A HIS   193 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O16 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 174.7 ? 
14 O   ? K HOH   .   ? A HOH   449 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O16 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 89.1  ? 
15 N15 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O16 ? B A1BC5 9   ? B A1BC5 8   ? 1_555 78.4  ? 
# 
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 A1BC5 B 9  ? .   . .  . A1BC5 B 8  ? 1_555 .   . .  . .     .   .  SER 1  A1BC5 None 'Non-standard residue' 
2 ACE   B 1  ? TYR B 2  ? ACE   B 0  ? 1_555 TYR B 1  ? 1_555 .   .  TYR 5  ACE   None 'Terminal acetylation' 
3 NH2   B 16 ? CYS B 15 ? NH2   B 15 ? 1_555 CYS B 14 ? 1_555 .   .  CYS 11 NH2   None 'Terminal amidation'   
4 ACE   B 1  ? CYS B 15 ? ACE   B 0  ? 1_555 CYS B 14 ? 1_555 CH3 SG .   .  .     None 'Non-standard linkage' 
# 
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 GLU 155 A . ? GLU 154 A PRO 156 A ? PRO 155 A 1 -0.85 
2 ALA 210 A . ? ALA 209 A PRO 211 A ? PRO 210 A 1 -7.62 
3 LEU 242 A . ? LEU 241 A PRO 243 A ? PRO 242 A 1 -0.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 6  ? 
AA3 ? 2  ? 
# 
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  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA1 6 7  ? anti-parallel 
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? anti-parallel 
AA2 5 6  ? parallel      
AA3 1 2  ? anti-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  CYS A 184 ? LEU A 186 ? CYS A 183 LEU A 185 
AA1 2  HIS A 119 ? LYS A 136 ? HIS A 118 LYS A 135 
AA1 3  ARG A 167 ? TYR A 177 ? ARG A 166 TYR A 176 
AA1 4  ARG A 244 ? THR A 251 ? ARG A 243 THR A 250 
AA1 5  TYR A 223 ? LEU A 227 ? TYR A 222 LEU A 226 
AA1 6  SER A 109 ? HIS A 113 ? SER A 108 HIS A 112 
AA1 7  LEU A 193 ? ALA A 210 ? LEU A 192 ALA A 209 
AA1 8  SER A 98  ? LEU A 104 ? SER A 97  LEU A 103 
AA1 9  VAL A 86  ? GLU A 93  ? VAL A 85  GLU A 92  
AA1 10 CYS A 259 ? GLY A 261 ? CYS A 258 GLY A 260 
AA2 1  CYS A 184 ? LEU A 186 ? CYS A 183 LEU A 185 
AA2 2  HIS A 119 ? LYS A 136 ? HIS A 118 LYS A 135 
AA2 3  LEU A 193 ? ALA A 210 ? LEU A 192 ALA A 209 
AA2 4  SER A 98  ? LEU A 104 ? SER A 97  LEU A 103 
AA2 5  VAL A 86  ? GLU A 93  ? VAL A 85  GLU A 92  
AA2 6  CYS A 259 ? GLY A 261 ? CYS A 258 GLY A 260 
AA3 1  ILE B 3   ? THR B 6   ? ILE B 2   THR B 5   
AA3 2  GLY B 10  ? ARG B 13  ? GLY B 9   ARG B 12  
# 
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  O CYS A 184 ? O CYS A 183 N LEU A 122 ? N LEU A 121 
AA1 2 3  N VAL A 129 ? N VAL A 128 O TYR A 177 ? O TYR A 176 
AA1 3 4  N ARG A 167 ? N ARG A 166 O LEU A 248 ? O LEU A 247 
AA1 4 5  O LEU A 249 ? O LEU A 248 N ARG A 225 ? N ARG A 224 
AA1 5 6  O TYR A 224 ? O TYR A 223 N LEU A 112 ? N LEU A 111 
AA1 6 7  N ILE A 110 ? N ILE A 109 O ILE A 196 ? O ILE A 195 
AA1 7 8  O ALA A 203 ? O ALA A 202 N LEU A 104 ? N LEU A 103 
AA1 8 9  O VAL A 101 ? O VAL A 100 N MET A 89  ? N MET A 88  
AA1 9 10 N TYR A 88  ? N TYR A 87  O GLU A 260 ? O GLU A 259 
AA2 1 2  O CYS A 184 ? O CYS A 183 N LEU A 122 ? N LEU A 121 
AA2 2 3  N THR A 128 ? N THR A 127 O VAL A 199 ? O VAL A 198 
AA2 3 4  O ALA A 203 ? O ALA A 202 N LEU A 104 ? N LEU A 103 
AA2 4 5  O VAL A 101 ? O VAL A 100 N MET A 89  ? N MET A 88  
AA2 5 6  N TYR A 88  ? N TYR A 87  O GLU A 260 ? O GLU A 259 
AA3 1 2  N VAL B 4   ? N VAL B 3   O HIS B 12  ? O HIS B 11  
# 
_pdbx_entry_details.entry_id                   9DXB 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   ND1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    89 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.08 
# 
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 ARG   A 173 ? ? -160.99 97.17 
2 1 ASP   A 213 ? ? -154.27 83.73 
3 1 A1BC5 B 8   ? ? -152.78 41.60 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             A1BC5 
_pdbx_validate_main_chain_plane.auth_asym_id             B 
_pdbx_validate_main_chain_plane.auth_seq_id              8 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -14.50 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x,-y,-z         
3 -x,y+1/2,-z+1/2 
4 -x,-y+1/2,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         4.7812567863 
_pdbx_refine_tls.origin_y         18.9750758387 
_pdbx_refine_tls.origin_z         15.4176287003 
_pdbx_refine_tls.T[1][1]          0.183250514862 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.00261569276708 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.00565779026378 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.162795908544 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.00485082705398 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.193746675745 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.922000509094 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0250937654406 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0800957942568 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.462821180327 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0486703488105 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.13532353208 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.024585221683 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.045276546434 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0271323681195 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0531552173863 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0114034099662 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.00620821166717 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0274193410145 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0133231369352 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -3.1775716536e-06 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     5 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   A 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     7 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 584 ? 6.12 . 
2 1 O ? A HOH 585 ? 6.19 . 
3 1 O ? A HOH 586 ? 7.19 . 
4 1 O ? A HOH 587 ? 8.20 . 
5 1 O ? B HOH 113 ? 6.23 . 
# 
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 SER 0   ? A SER 1   
2  1 Y 1 A MET 1   ? A MET 2   
3  1 Y 1 A PRO 2   ? A PRO 3   
4  1 Y 1 A ARG 3   ? A ARG 4   
5  1 Y 1 A ASP 4   ? A ASP 5   
6  1 Y 1 A GLY 23  ? A GLY 24  
7  1 Y 1 A SER 24  ? A SER 25  
8  1 Y 1 A GLY 25  ? A GLY 26  
9  1 Y 1 A GLY 26  ? A GLY 27  
10 1 Y 1 A GLY 27  ? A GLY 28  
11 1 Y 1 A ARG 28  ? A ARG 29  
12 1 Y 1 A GLY 29  ? A GLY 30  
13 1 Y 1 A ALA 30  ? A ALA 31  
14 1 Y 1 A SER 31  ? A SER 32  
15 1 Y 1 A ASP 32  ? A ASP 33  
16 1 Y 1 A ARG 33  ? A ARG 34  
17 1 Y 1 A ASP 34  ? A ASP 35  
18 1 Y 1 A ALA 35  ? A ALA 36  
19 1 Y 1 A ALA 36  ? A ALA 37  
20 1 Y 1 A SER 37  ? A SER 38  
21 1 Y 1 A GLY 38  ? A GLY 39  
22 1 Y 1 A PRO 39  ? A PRO 40  
23 1 Y 1 A GLU 40  ? A GLU 41  
24 1 Y 1 A ALA 138 ? A ALA 139 
25 1 Y 1 A GLY 139 ? A GLY 140 
26 1 Y 1 A GLY 140 ? A GLY 141 
27 1 Y 1 A GLY 141 ? A GLY 142 
28 1 Y 1 A GLN 142 ? A GLN 143 
29 1 Y 1 A ARG 143 ? A ARG 144 
30 1 Y 1 A PRO 144 ? A PRO 145 
31 1 Y 1 A ARG 230 ? A ARG 231 
32 1 Y 1 A PRO 231 ? A PRO 232 
33 1 Y 1 A LYS 232 ? A LYS 233 
34 1 Y 1 A GLU 233 ? A GLU 234 
35 1 Y 1 A ALA 234 ? A ALA 235 
36 1 Y 1 A SER 235 ? A SER 236 
37 1 Y 1 A SER 236 ? A SER 237 
38 1 Y 1 A SER 237 ? A SER 238 
39 1 Y 1 A ALA 238 ? A ALA 239 
40 1 Y 1 A SER 239 ? A SER 240 
# 
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 
A1BC5 C10  C  N N 1   
A1BC5 C13  C  N N 2   
A1BC5 C02  C  N N 3   
A1BC5 C03  C  N N 4   
A1BC5 CB   C  N N 5   
A1BC5 CA   C  N S 6   
A1BC5 C    C  N N 7   
A1BC5 C12  C  N S 8   
A1BC5 N01  N  N N 9   
A1BC5 N    N  N N 10  
A1BC5 N09  N  N N 11  
A1BC5 N15  N  N N 12  
A1BC5 O    O  N N 13  
A1BC5 O11  O  N N 14  
A1BC5 O14  O  N N 15  
A1BC5 O16  O  N N 16  
A1BC5 H1   H  N N 17  
A1BC5 H19  H  N N 18  
A1BC5 H3   H  N N 19  
A1BC5 H4   H  N N 20  
A1BC5 HB3  H  N N 21  
A1BC5 HB2  H  N N 22  
A1BC5 HA   H  N N 23  
A1BC5 H9   H  N N 24  
A1BC5 H10  H  N N 25  
A1BC5 H    H  N N 26  
A1BC5 H2   H  N N 27  
A1BC5 H14  H  N N 28  
A1BC5 H15  H  N N 29  
A1BC5 H16  H  N N 30  
A1BC5 H18  H  N N 31  
A1BC5 OXT  O  N N 32  
A1BC5 HXT  H  N N 33  
ACE   C    C  N N 34  
ACE   O    O  N N 35  
ACE   CH3  C  N N 36  
ACE   H    H  N N 37  
ACE   H1   H  N N 38  
ACE   H2   H  N N 39  
ACE   H3   H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CL    CL   CL N N 114 
CO    CO   CO N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
GOL   C1   C  N N 179 
GOL   O1   O  N N 180 
GOL   C2   C  N N 181 
GOL   O2   O  N N 182 
GOL   C3   C  N N 183 
GOL   O3   O  N N 184 
GOL   H11  H  N N 185 
GOL   H12  H  N N 186 
GOL   HO1  H  N N 187 
GOL   H2   H  N N 188 
GOL   HO2  H  N N 189 
GOL   H31  H  N N 190 
GOL   H32  H  N N 191 
GOL   HO3  H  N N 192 
HIS   N    N  N N 193 
HIS   CA   C  N S 194 
HIS   C    C  N N 195 
HIS   O    O  N N 196 
HIS   CB   C  N N 197 
HIS   CG   C  Y N 198 
HIS   ND1  N  Y N 199 
HIS   CD2  C  Y N 200 
HIS   CE1  C  Y N 201 
HIS   NE2  N  Y N 202 
HIS   OXT  O  N N 203 
HIS   H    H  N N 204 
HIS   H2   H  N N 205 
HIS   HA   H  N N 206 
HIS   HB2  H  N N 207 
HIS   HB3  H  N N 208 
HIS   HD1  H  N N 209 
HIS   HD2  H  N N 210 
HIS   HE1  H  N N 211 
HIS   HE2  H  N N 212 
HIS   HXT  H  N N 213 
HOH   O    O  N N 214 
HOH   H1   H  N N 215 
HOH   H2   H  N N 216 
ILE   N    N  N N 217 
ILE   CA   C  N S 218 
ILE   C    C  N N 219 
ILE   O    O  N N 220 
ILE   CB   C  N S 221 
ILE   CG1  C  N N 222 
ILE   CG2  C  N N 223 
ILE   CD1  C  N N 224 
ILE   OXT  O  N N 225 
ILE   H    H  N N 226 
ILE   H2   H  N N 227 
ILE   HA   H  N N 228 
ILE   HB   H  N N 229 
ILE   HG12 H  N N 230 
ILE   HG13 H  N N 231 
ILE   HG21 H  N N 232 
ILE   HG22 H  N N 233 
ILE   HG23 H  N N 234 
ILE   HD11 H  N N 235 
ILE   HD12 H  N N 236 
ILE   HD13 H  N N 237 
ILE   HXT  H  N N 238 
LEU   N    N  N N 239 
LEU   CA   C  N S 240 
LEU   C    C  N N 241 
LEU   O    O  N N 242 
LEU   CB   C  N N 243 
LEU   CG   C  N N 244 
LEU   CD1  C  N N 245 
LEU   CD2  C  N N 246 
LEU   OXT  O  N N 247 
LEU   H    H  N N 248 
LEU   H2   H  N N 249 
LEU   HA   H  N N 250 
LEU   HB2  H  N N 251 
LEU   HB3  H  N N 252 
LEU   HG   H  N N 253 
LEU   HD11 H  N N 254 
LEU   HD12 H  N N 255 
LEU   HD13 H  N N 256 
LEU   HD21 H  N N 257 
LEU   HD22 H  N N 258 
LEU   HD23 H  N N 259 
LEU   HXT  H  N N 260 
LYS   N    N  N N 261 
LYS   CA   C  N S 262 
LYS   C    C  N N 263 
LYS   O    O  N N 264 
LYS   CB   C  N N 265 
LYS   CG   C  N N 266 
LYS   CD   C  N N 267 
LYS   CE   C  N N 268 
LYS   NZ   N  N N 269 
LYS   OXT  O  N N 270 
LYS   H    H  N N 271 
LYS   H2   H  N N 272 
LYS   HA   H  N N 273 
LYS   HB2  H  N N 274 
LYS   HB3  H  N N 275 
LYS   HG2  H  N N 276 
LYS   HG3  H  N N 277 
LYS   HD2  H  N N 278 
LYS   HD3  H  N N 279 
LYS   HE2  H  N N 280 
LYS   HE3  H  N N 281 
LYS   HZ1  H  N N 282 
LYS   HZ2  H  N N 283 
LYS   HZ3  H  N N 284 
LYS   HXT  H  N N 285 
MET   N    N  N N 286 
MET   CA   C  N S 287 
MET   C    C  N N 288 
MET   O    O  N N 289 
MET   CB   C  N N 290 
MET   CG   C  N N 291 
MET   SD   S  N N 292 
MET   CE   C  N N 293 
MET   OXT  O  N N 294 
MET   H    H  N N 295 
MET   H2   H  N N 296 
MET   HA   H  N N 297 
MET   HB2  H  N N 298 
MET   HB3  H  N N 299 
MET   HG2  H  N N 300 
MET   HG3  H  N N 301 
MET   HE1  H  N N 302 
MET   HE2  H  N N 303 
MET   HE3  H  N N 304 
MET   HXT  H  N N 305 
NH2   N    N  N N 306 
NH2   HN1  H  N N 307 
NH2   HN2  H  N N 308 
PHE   N    N  N N 309 
PHE   CA   C  N S 310 
PHE   C    C  N N 311 
PHE   O    O  N N 312 
PHE   CB   C  N N 313 
PHE   CG   C  Y N 314 
PHE   CD1  C  Y N 315 
PHE   CD2  C  Y N 316 
PHE   CE1  C  Y N 317 
PHE   CE2  C  Y N 318 
PHE   CZ   C  Y N 319 
PHE   OXT  O  N N 320 
PHE   H    H  N N 321 
PHE   H2   H  N N 322 
PHE   HA   H  N N 323 
PHE   HB2  H  N N 324 
PHE   HB3  H  N N 325 
PHE   HD1  H  N N 326 
PHE   HD2  H  N N 327 
PHE   HE1  H  N N 328 
PHE   HE2  H  N N 329 
PHE   HZ   H  N N 330 
PHE   HXT  H  N N 331 
PRO   N    N  N N 332 
PRO   CA   C  N S 333 
PRO   C    C  N N 334 
PRO   O    O  N N 335 
PRO   CB   C  N N 336 
PRO   CG   C  N N 337 
PRO   CD   C  N N 338 
PRO   OXT  O  N N 339 
PRO   H    H  N N 340 
PRO   HA   H  N N 341 
PRO   HB2  H  N N 342 
PRO   HB3  H  N N 343 
PRO   HG2  H  N N 344 
PRO   HG3  H  N N 345 
PRO   HD2  H  N N 346 
PRO   HD3  H  N N 347 
PRO   HXT  H  N N 348 
SER   N    N  N N 349 
SER   CA   C  N S 350 
SER   C    C  N N 351 
SER   O    O  N N 352 
SER   CB   C  N N 353 
SER   OG   O  N N 354 
SER   OXT  O  N N 355 
SER   H    H  N N 356 
SER   H2   H  N N 357 
SER   HA   H  N N 358 
SER   HB2  H  N N 359 
SER   HB3  H  N N 360 
SER   HG   H  N N 361 
SER   HXT  H  N N 362 
THR   N    N  N N 363 
THR   CA   C  N S 364 
THR   C    C  N N 365 
THR   O    O  N N 366 
THR   CB   C  N R 367 
THR   OG1  O  N N 368 
THR   CG2  C  N N 369 
THR   OXT  O  N N 370 
THR   H    H  N N 371 
THR   H2   H  N N 372 
THR   HA   H  N N 373 
THR   HB   H  N N 374 
THR   HG1  H  N N 375 
THR   HG21 H  N N 376 
THR   HG22 H  N N 377 
THR   HG23 H  N N 378 
THR   HXT  H  N N 379 
TRP   N    N  N N 380 
TRP   CA   C  N S 381 
TRP   C    C  N N 382 
TRP   O    O  N N 383 
TRP   CB   C  N N 384 
TRP   CG   C  Y N 385 
TRP   CD1  C  Y N 386 
TRP   CD2  C  Y N 387 
TRP   NE1  N  Y N 388 
TRP   CE2  C  Y N 389 
TRP   CE3  C  Y N 390 
TRP   CZ2  C  Y N 391 
TRP   CZ3  C  Y N 392 
TRP   CH2  C  Y N 393 
TRP   OXT  O  N N 394 
TRP   H    H  N N 395 
TRP   H2   H  N N 396 
TRP   HA   H  N N 397 
TRP   HB2  H  N N 398 
TRP   HB3  H  N N 399 
TRP   HD1  H  N N 400 
TRP   HE1  H  N N 401 
TRP   HE3  H  N N 402 
TRP   HZ2  H  N N 403 
TRP   HZ3  H  N N 404 
TRP   HH2  H  N N 405 
TRP   HXT  H  N N 406 
TYR   N    N  N N 407 
TYR   CA   C  N S 408 
TYR   C    C  N N 409 
TYR   O    O  N N 410 
TYR   CB   C  N N 411 
TYR   CG   C  Y N 412 
TYR   CD1  C  Y N 413 
TYR   CD2  C  Y N 414 
TYR   CE1  C  Y N 415 
TYR   CE2  C  Y N 416 
TYR   CZ   C  Y N 417 
TYR   OH   O  N N 418 
TYR   OXT  O  N N 419 
TYR   H    H  N N 420 
TYR   H2   H  N N 421 
TYR   HA   H  N N 422 
TYR   HB2  H  N N 423 
TYR   HB3  H  N N 424 
TYR   HD1  H  N N 425 
TYR   HD2  H  N N 426 
TYR   HE1  H  N N 427 
TYR   HE2  H  N N 428 
TYR   HH   H  N N 429 
TYR   HXT  H  N N 430 
VAL   N    N  N N 431 
VAL   CA   C  N S 432 
VAL   C    C  N N 433 
VAL   O    O  N N 434 
VAL   CB   C  N N 435 
VAL   CG1  C  N N 436 
VAL   CG2  C  N N 437 
VAL   OXT  O  N N 438 
VAL   H    H  N N 439 
VAL   H2   H  N N 440 
VAL   HA   H  N N 441 
VAL   HB   H  N N 442 
VAL   HG11 H  N N 443 
VAL   HG12 H  N N 444 
VAL   HG13 H  N N 445 
VAL   HG21 H  N N 446 
VAL   HG22 H  N N 447 
VAL   HG23 H  N N 448 
VAL   HXT  H  N N 449 
# 
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 
A1BC5 O   C    doub N N 1   
A1BC5 C   CA   sing N N 2   
A1BC5 CA  CB   sing N N 3   
A1BC5 CA  N    sing N N 4   
A1BC5 O14 C03  doub N N 5   
A1BC5 CB  N01  sing N N 6   
A1BC5 O16 C13  sing N N 7   
A1BC5 O11 C10  doub N N 8   
A1BC5 C03 N01  sing N N 9   
A1BC5 C03 C02  sing N N 10  
A1BC5 C02 N09  sing N N 11  
A1BC5 C10 N09  sing N N 12  
A1BC5 C10 C12  sing N N 13  
A1BC5 N15 C12  sing N N 14  
A1BC5 C13 C12  sing N N 15  
A1BC5 C13 H1   sing N N 16  
A1BC5 C13 H19  sing N N 17  
A1BC5 C02 H3   sing N N 18  
A1BC5 C02 H4   sing N N 19  
A1BC5 CB  HB3  sing N N 20  
A1BC5 CB  HB2  sing N N 21  
A1BC5 CA  HA   sing N N 22  
A1BC5 C12 H9   sing N N 23  
A1BC5 N01 H10  sing N N 24  
A1BC5 N   H    sing N N 25  
A1BC5 N   H2   sing N N 26  
A1BC5 N09 H14  sing N N 27  
A1BC5 N15 H15  sing N N 28  
A1BC5 N15 H16  sing N N 29  
A1BC5 O16 H18  sing N N 30  
A1BC5 C   OXT  sing N N 31  
A1BC5 OXT HXT  sing N N 32  
ACE   C   O    doub N N 33  
ACE   C   CH3  sing N N 34  
ACE   C   H    sing N N 35  
ACE   CH3 H1   sing N N 36  
ACE   CH3 H2   sing N N 37  
ACE   CH3 H3   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
GOL   C1  O1   sing N N 167 
GOL   C1  C2   sing N N 168 
GOL   C1  H11  sing N N 169 
GOL   C1  H12  sing N N 170 
GOL   O1  HO1  sing N N 171 
GOL   C2  O2   sing N N 172 
GOL   C2  C3   sing N N 173 
GOL   C2  H2   sing N N 174 
GOL   O2  HO2  sing N N 175 
GOL   C3  O3   sing N N 176 
GOL   C3  H31  sing N N 177 
GOL   C3  H32  sing N N 178 
GOL   O3  HO3  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
NH2   N   HN1  sing N N 288 
NH2   N   HN2  sing N N 289 
PHE   N   CA   sing N N 290 
PHE   N   H    sing N N 291 
PHE   N   H2   sing N N 292 
PHE   CA  C    sing N N 293 
PHE   CA  CB   sing N N 294 
PHE   CA  HA   sing N N 295 
PHE   C   O    doub N N 296 
PHE   C   OXT  sing N N 297 
PHE   CB  CG   sing N N 298 
PHE   CB  HB2  sing N N 299 
PHE   CB  HB3  sing N N 300 
PHE   CG  CD1  doub Y N 301 
PHE   CG  CD2  sing Y N 302 
PHE   CD1 CE1  sing Y N 303 
PHE   CD1 HD1  sing N N 304 
PHE   CD2 CE2  doub Y N 305 
PHE   CD2 HD2  sing N N 306 
PHE   CE1 CZ   doub Y N 307 
PHE   CE1 HE1  sing N N 308 
PHE   CE2 CZ   sing Y N 309 
PHE   CE2 HE2  sing N N 310 
PHE   CZ  HZ   sing N N 311 
PHE   OXT HXT  sing N N 312 
PRO   N   CA   sing N N 313 
PRO   N   CD   sing N N 314 
PRO   N   H    sing N N 315 
PRO   CA  C    sing N N 316 
PRO   CA  CB   sing N N 317 
PRO   CA  HA   sing N N 318 
PRO   C   O    doub N N 319 
PRO   C   OXT  sing N N 320 
PRO   CB  CG   sing N N 321 
PRO   CB  HB2  sing N N 322 
PRO   CB  HB3  sing N N 323 
PRO   CG  CD   sing N N 324 
PRO   CG  HG2  sing N N 325 
PRO   CG  HG3  sing N N 326 
PRO   CD  HD2  sing N N 327 
PRO   CD  HD3  sing N N 328 
PRO   OXT HXT  sing N N 329 
SER   N   CA   sing N N 330 
SER   N   H    sing N N 331 
SER   N   H2   sing N N 332 
SER   CA  C    sing N N 333 
SER   CA  CB   sing N N 334 
SER   CA  HA   sing N N 335 
SER   C   O    doub N N 336 
SER   C   OXT  sing N N 337 
SER   CB  OG   sing N N 338 
SER   CB  HB2  sing N N 339 
SER   CB  HB3  sing N N 340 
SER   OG  HG   sing N N 341 
SER   OXT HXT  sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
_pdbx_audit_support.funding_organization   'National Health and Medical Research Council (NHMRC, Australia)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           2008546 
_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   7REI 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 2 21 21' 
_space_group.name_Hall        'P 2 2ab (z,x,y)' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DXB 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.027766 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013912 
_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]   0.009183 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CO ? ? 21.85313 5.04979 ? ? 2.45200  36.11361 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ASN   A 1 6   ? 11.60449  25.35436 47.88785  1.000 78.03451  ? 5   ASN   A N   1 
ATOM   2    C  CA  . ASN   A 1 6   ? 12.68278  26.20658 47.39805  1.000 88.47608  ? 5   ASN   A CA  1 
ATOM   3    C  C   . ASN   A 1 6   ? 12.99576  25.93365 45.92393  1.000 90.03926  ? 5   ASN   A C   1 
ATOM   4    O  O   . ASN   A 1 6   ? 13.65751  26.73342 45.26413  1.000 94.93949  ? 5   ASN   A O   1 
ATOM   5    C  CB  . ASN   A 1 6   ? 13.94539  26.01241 48.24554  1.000 82.71977  ? 5   ASN   A CB  1 
ATOM   6    N  N   . MET   A 1 7   ? 12.50605  24.81133 45.40580  1.000 76.17618  ? 6   MET   A N   1 
ATOM   7    C  CA  . MET   A 1 7   ? 12.85176  24.34613 44.06932  0.752 75.54757  ? 6   MET   A CA  1 
ATOM   8    C  C   . MET   A 1 7   ? 11.59297  24.35905 43.20344  1.000 73.01589  ? 6   MET   A C   1 
ATOM   9    O  O   . MET   A 1 7   ? 10.59707  23.70691 43.53838  1.000 61.44378  ? 6   MET   A O   1 
ATOM   10   C  CB  . MET   A 1 7   ? 13.46304  22.94438 44.13998  1.000 77.56863  ? 6   MET   A CB  1 
ATOM   11   C  CG  . MET   A 1 7   ? 13.92618  22.35902 42.81156  1.000 72.04141  ? 6   MET   A CG  1 
ATOM   12   S  SD  . MET   A 1 7   ? 14.79163  23.55193 41.77206  1.000 79.54105  ? 6   MET   A SD  1 
ATOM   13   C  CE  . MET   A 1 7   ? 15.90966  22.46076 40.89092  1.000 50.97530  ? 6   MET   A CE  1 
ATOM   14   N  N   . ALA   A 1 8   ? 11.63435  25.11119 42.10444  1.000 55.40099  ? 7   ALA   A N   1 
ATOM   15   C  CA  . ALA   A 1 8   ? 10.51428  25.16595 41.17246  1.000 44.60125  ? 7   ALA   A CA  1 
ATOM   16   C  C   . ALA   A 1 8   ? 10.33296  23.82909 40.46366  1.000 42.42100  ? 7   ALA   A C   1 
ATOM   17   O  O   . ALA   A 1 8   ? 11.27290  23.04349 40.32544  1.000 39.32115  ? 7   ALA   A O   1 
ATOM   18   C  CB  . ALA   A 1 8   ? 10.73455  26.27173 40.14109  1.000 39.49472  ? 7   ALA   A CB  1 
ATOM   19   N  N   . SER   A 1 9   ? 9.10493   23.57476 40.00197  1.000 36.81766  ? 8   SER   A N   1 
ATOM   20   C  CA  . SER   A 1 9   ? 8.83671   22.33708 39.27988  1.000 35.97584  ? 8   SER   A CA  1 
ATOM   21   C  C   . SER   A 1 9   ? 9.66664   22.28420 37.99578  1.000 26.23745  ? 8   SER   A C   1 
ATOM   22   O  O   . SER   A 1 9   ? 10.07610  23.30631 37.44543  1.000 29.73651  ? 8   SER   A O   1 
ATOM   23   C  CB  . SER   A 1 9   ? 7.35195   22.21944 38.93046  1.000 32.17698  ? 8   SER   A CB  1 
ATOM   24   O  OG  . SER   A 1 9   ? 6.98319   23.24853 38.01560  1.000 31.15978  ? 8   SER   A OG  1 
ATOM   25   N  N   . LEU   A 1 10  ? 9.90827   21.06762 37.51571  1.000 27.45678  ? 9   LEU   A N   1 
ATOM   26   C  CA  . LEU   A 1 10  ? 10.67207  20.91219 36.27731  1.000 28.10970  ? 9   LEU   A CA  1 
ATOM   27   C  C   . LEU   A 1 10  ? 9.97877   21.60065 35.10454  1.000 27.81676  ? 9   LEU   A C   1 
ATOM   28   O  O   . LEU   A 1 10  ? 10.64044  22.19512 34.24739  1.000 23.99775  ? 9   LEU   A O   1 
ATOM   29   C  CB  . LEU   A 1 10  ? 10.89255  19.42978 35.98121  1.000 23.50694  ? 9   LEU   A CB  1 
ATOM   30   C  CG  . LEU   A 1 10  ? 11.63027  19.09985 34.68662  1.000 29.16849  ? 9   LEU   A CG  1 
ATOM   31   C  CD1 . LEU   A 1 10  ? 12.98913  19.81077 34.64761  1.000 29.23670  ? 9   LEU   A CD1 1 
ATOM   32   C  CD2 . LEU   A 1 10  ? 11.78564  17.58950 34.49085  1.000 28.12742  ? 9   LEU   A CD2 1 
ATOM   33   N  N   . ILE   A 1 11  ? 8.64697   21.56029 35.05089  1.000 25.63903  ? 10  ILE   A N   1 
ATOM   34   C  CA  . ILE   A 1 11  ? 7.98328   22.21802 33.92546  1.000 24.00325  ? 10  ILE   A CA  1 
ATOM   35   C  C   . ILE   A 1 11  ? 8.10172   23.73867 34.03417  1.000 26.43822  ? 10  ILE   A C   1 
ATOM   36   O  O   . ILE   A 1 11  ? 8.27881   24.41884 33.02672  1.000 24.33919  ? 10  ILE   A O   1 
ATOM   37   C  CB  . ILE   A 1 11  ? 6.52229   21.73995 33.78920  1.000 24.39950  ? 10  ILE   A CB  1 
ATOM   38   C  CG1 . ILE   A 1 11  ? 5.92330   22.21974 32.46885  1.000 20.41966  ? 10  ILE   A CG1 1 
ATOM   39   C  CG2 . ILE   A 1 11  ? 5.64927   22.18913 34.96847  1.000 24.33963  ? 10  ILE   A CG2 1 
ATOM   40   C  CD1 . ILE   A 1 11  ? 6.70856   21.72500 31.20678  1.000 21.14295  ? 10  ILE   A CD1 1 
ATOM   41   N  N   . GLN   A 1 12  ? 8.04013   24.29721 35.25529  1.000 24.33154  ? 11  GLN   A N   1 
ATOM   42   C  CA  . GLN   A 1 12  ? 8.37490   25.71291 35.45701  1.000 24.21211  ? 11  GLN   A CA  1 
ATOM   43   C  C   . GLN   A 1 12  ? 9.77531   26.02963 34.95988  1.000 28.41844  ? 11  GLN   A C   1 
ATOM   44   O  O   . GLN   A 1 12  ? 9.99933   27.05997 34.30997  1.000 29.60097  ? 11  GLN   A O   1 
ATOM   45   C  CB  . GLN   A 1 12  ? 8.29719   26.06655 36.95123  1.000 31.78876  ? 11  GLN   A CB  1 
ATOM   46   C  CG  . GLN   A 1 12  ? 8.35834   27.56626 37.37152  1.000 37.54343  ? 11  GLN   A CG  1 
ATOM   47   C  CD  . GLN   A 1 12  ? 7.45242   28.53897 36.62932  1.000 38.50385  ? 11  GLN   A CD  1 
ATOM   48   O  OE1 . GLN   A 1 12  ? 6.24921   28.36389 36.60048  1.000 37.18584  ? 11  GLN   A OE1 1 
ATOM   49   N  NE2 . GLN   A 1 12  ? 8.03602   29.60841 36.08034  1.000 43.14079  ? 11  GLN   A NE2 1 
ATOM   50   N  N   . ARG   A 1 13  ? 10.74269  25.18017 35.30962  1.000 26.18894  ? 12  ARG   A N   1 
ATOM   51   C  CA  A ARG   A 1 13  ? 12.12694  25.42562 34.91942  0.492 26.11688  ? 12  ARG   A CA  1 
ATOM   52   C  CA  B ARG   A 1 13  ? 12.12153  25.44295 34.91856  0.508 26.10719  ? 12  ARG   A CA  1 
ATOM   53   C  C   . ARG   A 1 13  ? 12.30259  25.32617 33.40856  1.000 29.03281  ? 12  ARG   A C   1 
ATOM   54   O  O   . ARG   A 1 13  ? 13.09463  26.06925 32.81829  1.000 28.38836  ? 12  ARG   A O   1 
ATOM   55   C  CB  A ARG   A 1 13  ? 13.04718  24.43966 35.63426  0.492 29.93196  ? 12  ARG   A CB  1 
ATOM   56   C  CB  B ARG   A 1 13  ? 13.05609  24.49169 35.65654  0.508 29.95638  ? 12  ARG   A CB  1 
ATOM   57   C  CG  A ARG   A 1 13  ? 13.02509  24.57678 37.16026  0.492 33.54558  ? 12  ARG   A CG  1 
ATOM   58   C  CG  B ARG   A 1 13  ? 13.22572  24.84898 37.13869  0.508 33.71475  ? 12  ARG   A CG  1 
ATOM   59   C  CD  A ARG   A 1 13  ? 13.72768  23.40519 37.81826  0.492 34.84167  ? 12  ARG   A CD  1 
ATOM   60   C  CD  B ARG   A 1 13  ? 14.23767  23.93588 37.78970  0.508 36.20219  ? 12  ARG   A CD  1 
ATOM   61   N  NE  A ARG   A 1 13  ? 15.09297  23.25413 37.32531  0.492 34.46375  ? 12  ARG   A NE  1 
ATOM   62   N  NE  B ARG   A 1 13  ? 13.62594  22.68882 38.23015  0.508 35.50322  ? 12  ARG   A NE  1 
ATOM   63   C  CZ  A ARG   A 1 13  ? 15.71838  22.09217 37.19402  0.492 39.87256  ? 12  ARG   A CZ  1 
ATOM   64   C  CZ  B ARG   A 1 13  ? 14.14830  21.48973 38.01220  0.508 36.25234  ? 12  ARG   A CZ  1 
ATOM   65   N  NH1 A ARG   A 1 13  ? 15.12648  20.94973 37.50216  0.492 39.82800  ? 12  ARG   A NH1 1 
ATOM   66   N  NH1 B ARG   A 1 13  ? 15.28969  21.34255 37.36023  0.508 39.92969  ? 12  ARG   A NH1 1 
ATOM   67   N  NH2 A ARG   A 1 13  ? 16.97358  22.07647 36.74890  0.492 37.71337  ? 12  ARG   A NH2 1 
ATOM   68   N  NH2 B ARG   A 1 13  ? 13.50986  20.41175 38.45861  0.508 33.82194  ? 12  ARG   A NH2 1 
ATOM   69   N  N   . ILE   A 1 14  ? 11.58127  24.39752 32.76941  1.000 24.09015  ? 13  ILE   A N   1 
ATOM   70   C  CA  . ILE   A 1 14  ? 11.59772  24.30318 31.31038  1.000 25.64165  ? 13  ILE   A CA  1 
ATOM   71   C  C   . ILE   A 1 14  ? 11.04739  25.58051 30.69472  1.000 25.09460  ? 13  ILE   A C   1 
ATOM   72   O  O   . ILE   A 1 14  ? 11.63403  26.14597 29.76766  1.000 25.59183  ? 13  ILE   A O   1 
ATOM   73   C  CB  . ILE   A 1 14  ? 10.80321  23.06740 30.84882  1.000 23.66248  ? 13  ILE   A CB  1 
ATOM   74   C  CG1 . ILE   A 1 14  ? 11.62912  21.80579 31.08497  1.000 23.12818  ? 13  ILE   A CG1 1 
ATOM   75   C  CG2 . ILE   A 1 14  ? 10.41135  23.18909 29.36814  1.000 22.37366  ? 13  ILE   A CG2 1 
ATOM   76   C  CD1 . ILE   A 1 14  ? 10.81044  20.50275 30.98183  1.000 22.96556  ? 13  ILE   A CD1 1 
ATOM   77   N  N   . ALA   A 1 15  ? 9.92070   26.07358 31.22186  1.000 22.96085  ? 14  ALA   A N   1 
ATOM   78   C  CA  . ALA   A 1 15  ? 9.33870   27.29496 30.67802  1.000 26.58654  ? 14  ALA   A CA  1 
ATOM   79   C  C   . ALA   A 1 15  ? 10.28436  28.48056 30.85656  1.000 28.59170  ? 14  ALA   A C   1 
ATOM   80   O  O   . ALA   A 1 15  ? 10.45476  29.29216 29.93889  1.000 27.62551  ? 14  ALA   A O   1 
ATOM   81   C  CB  . ALA   A 1 15  ? 7.99363   27.57349 31.35565  1.000 28.97348  ? 14  ALA   A CB  1 
ATOM   82   N  N   . ARG   A 1 16  ? 10.89581  28.60419 32.04055  1.000 28.22973  ? 15  ARG   A N   1 
ATOM   83   C  CA  A ARG   A 1 16  ? 11.84821  29.68657 32.26910  0.572 34.08449  ? 15  ARG   A CA  1 
ATOM   84   C  CA  B ARG   A 1 16  ? 11.84222  29.69608 32.25838  0.428 34.07228  ? 15  ARG   A CA  1 
ATOM   85   C  C   . ARG   A 1 16  ? 13.02558  29.60427 31.30382  1.000 33.71786  ? 15  ARG   A C   1 
ATOM   86   O  O   . ARG   A 1 16  ? 13.47247  30.62269 30.76077  1.000 32.20256  ? 15  ARG   A O   1 
ATOM   87   C  CB  A ARG   A 1 16  ? 12.35483  29.64042 33.70505  0.572 33.83453  ? 15  ARG   A CB  1 
ATOM   88   C  CB  B ARG   A 1 16  ? 12.33648  29.70260 33.70340  0.428 33.84684  ? 15  ARG   A CB  1 
ATOM   89   C  CG  A ARG   A 1 16  ? 11.51637  30.41744 34.67560  0.572 35.53809  ? 15  ARG   A CG  1 
ATOM   90   C  CG  B ARG   A 1 16  ? 13.21405  30.90463 34.03684  0.428 34.57763  ? 15  ARG   A CG  1 
ATOM   91   C  CD  A ARG   A 1 16  ? 12.16260  30.38943 36.04568  0.572 38.66670  ? 15  ARG   A CD  1 
ATOM   92   C  CD  B ARG   A 1 16  ? 13.19381  31.19569 35.52802  0.428 36.93013  ? 15  ARG   A CD  1 
ATOM   93   N  NE  A ARG   A 1 16  ? 11.19017  30.54528 37.11477  0.572 39.43833  ? 15  ARG   A NE  1 
ATOM   94   N  NE  B ARG   A 1 16  ? 13.42903  29.98514 36.30463  0.428 41.00056  ? 15  ARG   A NE  1 
ATOM   95   C  CZ  A ARG   A 1 16  ? 11.29785  29.98308 38.30952  0.572 35.92871  ? 15  ARG   A CZ  1 
ATOM   96   C  CZ  B ARG   A 1 16  ? 14.62449  29.53183 36.65710  0.428 40.81624  ? 15  ARG   A CZ  1 
ATOM   97   N  NH1 A ARG   A 1 16  ? 12.31611  29.19361 38.61354  0.572 37.33495  ? 15  ARG   A NH1 1 
ATOM   98   N  NH1 B ARG   A 1 16  ? 15.72651  30.22452 36.41662  0.428 41.08952  ? 15  ARG   A NH1 1 
ATOM   99   N  NH2 A ARG   A 1 16  ? 10.36983  30.23244 39.22572  0.572 40.17432  ? 15  ARG   A NH2 1 
ATOM   100  N  NH2 B ARG   A 1 16  ? 14.71435  28.36166 37.28343  0.428 36.86903  ? 15  ARG   A NH2 1 
ATOM   101  N  N   . GLN   A 1 17  ? 13.56641  28.40062 31.10912  1.000 29.82071  ? 16  GLN   A N   1 
ATOM   102  C  CA  . GLN   A 1 17  ? 14.69717  28.24671 30.19692  1.000 26.94478  ? 16  GLN   A CA  1 
ATOM   103  C  C   . GLN   A 1 17  ? 14.28809  28.48652 28.75003  1.000 31.82260  ? 16  GLN   A C   1 
ATOM   104  O  O   . GLN   A 1 17  ? 15.07037  29.04558 27.97153  1.000 29.68242  ? 16  GLN   A O   1 
ATOM   105  C  CB  . GLN   A 1 17  ? 15.32784  26.86356 30.36641  1.000 28.72769  ? 16  GLN   A CB  1 
ATOM   106  C  CG  . GLN   A 1 17  ? 16.58214  26.62822 29.50397  1.000 26.11432  ? 16  GLN   A CG  1 
ATOM   107  C  CD  . GLN   A 1 17  ? 17.72842  27.56649 29.85164  1.000 34.32444  ? 16  GLN   A CD  1 
ATOM   108  O  OE1 . GLN   A 1 17  ? 17.85818  28.02833 30.99431  1.000 35.06761  ? 16  GLN   A OE1 1 
ATOM   109  N  NE2 . GLN   A 1 17  ? 18.57677  27.84191 28.87006  1.000 31.75769  ? 16  GLN   A NE2 1 
ATOM   110  N  N   . ALA   A 1 18  ? 13.07132  28.07280 28.36414  1.000 25.88183  ? 17  ALA   A N   1 
ATOM   111  C  CA  . ALA   A 1 18  ? 12.58981  28.37271 27.02106  1.000 29.31413  ? 17  ALA   A CA  1 
ATOM   112  C  C   . ALA   A 1 18  ? 12.50849  29.87697 26.80096  1.000 31.14392  ? 17  ALA   A C   1 
ATOM   113  O  O   . ALA   A 1 18  ? 12.85040  30.37448 25.72260  1.000 29.10244  ? 17  ALA   A O   1 
ATOM   114  C  CB  . ALA   A 1 18  ? 11.21671  27.72663 26.78049  1.000 25.90081  ? 17  ALA   A CB  1 
ATOM   115  N  N   . SER   A 1 19  ? 12.06625  30.61853 27.81998  1.000 32.89787  ? 18  SER   A N   1 
ATOM   116  C  CA  . SER   A 1 19  ? 11.96217  32.06852 27.68230  1.000 35.10339  ? 18  SER   A CA  1 
ATOM   117  C  C   . SER   A 1 19  ? 13.33165  32.69996 27.46441  1.000 38.26763  ? 18  SER   A C   1 
ATOM   118  O  O   . SER   A 1 19  ? 13.49411  33.57810 26.60875  1.000 44.41237  ? 18  SER   A O   1 
ATOM   119  C  CB  . SER   A 1 19  ? 11.28627  32.66419 28.91359  1.000 40.66814  ? 18  SER   A CB  1 
ATOM   120  O  OG  . SER   A 1 19  ? 10.64879  33.88949 28.58006  1.000 46.12552  ? 18  SER   A OG  1 
ATOM   121  N  N   . LEU   A 1 20  ? 14.32871  32.25789 28.23473  1.000 33.90693  ? 19  LEU   A N   1 
ATOM   122  C  CA  A LEU   A 1 20  ? 15.70113  32.73435 28.05515  0.570 36.77042  ? 19  LEU   A CA  1 
ATOM   123  C  CA  B LEU   A 1 20  ? 15.68574  32.75733 28.04745  0.430 36.78553  ? 19  LEU   A CA  1 
ATOM   124  C  C   . LEU   A 1 20  ? 16.24040  32.37752 26.67734  1.000 38.85713  ? 19  LEU   A C   1 
ATOM   125  O  O   . LEU   A 1 20  ? 16.96142  33.16720 26.05379  1.000 36.96592  ? 19  LEU   A O   1 
ATOM   126  C  CB  A LEU   A 1 20  ? 16.61199  32.12940 29.12398  0.570 37.40288  ? 19  LEU   A CB  1 
ATOM   127  C  CB  B LEU   A 1 20  ? 16.58773  32.22384 29.15793  0.430 37.38916  ? 19  LEU   A CB  1 
ATOM   128  C  CG  A LEU   A 1 20  ? 16.79908  32.74311 30.50737  0.570 40.50723  ? 19  LEU   A CG  1 
ATOM   129  C  CG  B LEU   A 1 20  ? 18.07761  32.52718 29.04451  0.430 37.22296  ? 19  LEU   A CG  1 
ATOM   130  C  CD1 A LEU   A 1 20  ? 17.79894  31.89935 31.27426  0.570 36.13397  ? 19  LEU   A CD1 1 
ATOM   131  C  CD1 B LEU   A 1 20  ? 18.32145  34.03086 29.06248  0.430 40.05375  ? 19  LEU   A CD1 1 
ATOM   132  C  CD2 A LEU   A 1 20  ? 17.29638  34.16572 30.38586  0.570 35.01785  ? 19  LEU   A CD2 1 
ATOM   133  C  CD2 B LEU   A 1 20  ? 18.83332  31.83626 30.16595  0.430 37.61977  ? 19  LEU   A CD2 1 
ATOM   134  N  N   . THR   A 1 21  ? 15.92369  31.17247 26.19625  1.000 31.81352  ? 20  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 21  ? 16.50531  30.69018 24.94863  1.000 31.46613  ? 20  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 21  ? 15.90435  31.40111 23.74748  1.000 34.11128  ? 20  THR   A C   1 
ATOM   137  O  O   . THR   A 1 21  ? 16.61878  31.74885 22.80003  1.000 35.61707  ? 20  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 21  ? 16.29720  29.17808 24.83900  1.000 30.00578  ? 20  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 21  ? 16.91905  28.53309 25.95431  1.000 30.94137  ? 20  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 21  ? 16.87537  28.62492 23.53114  1.000 29.78958  ? 20  THR   A CG2 1 
ATOM   141  N  N   . PHE   A 1 22  ? 14.59694  31.63251 23.77718  1.000 35.65828  ? 21  PHE   A N   1 
ATOM   142  C  CA  . PHE   A 1 22  ? 13.85756  32.21347 22.66292  1.000 40.26786  ? 21  PHE   A CA  1 
ATOM   143  C  C   . PHE   A 1 22  ? 13.26473  33.53430 23.14398  1.000 49.93924  ? 21  PHE   A C   1 
ATOM   144  O  O   . PHE   A 1 22  ? 12.21202  33.55134 23.79346  1.000 55.51550  ? 21  PHE   A O   1 
ATOM   145  C  CB  . PHE   A 1 22  ? 12.76969  31.25974 22.18019  1.000 35.67071  ? 21  PHE   A CB  1 
ATOM   146  C  CG  . PHE   A 1 22  ? 13.27284  29.88990 21.79756  1.000 36.04728  ? 21  PHE   A CG  1 
ATOM   147  C  CD1 . PHE   A 1 22  ? 13.95605  29.69729 20.59851  1.000 30.34427  ? 21  PHE   A CD1 1 
ATOM   148  C  CD2 . PHE   A 1 22  ? 13.00970  28.78938 22.60382  1.000 33.00271  ? 21  PHE   A CD2 1 
ATOM   149  C  CE1 . PHE   A 1 22  ? 14.40385  28.43175 20.22806  1.000 30.83573  ? 21  PHE   A CE1 1 
ATOM   150  C  CE2 . PHE   A 1 22  ? 13.44644  27.51724 22.23934  1.000 33.04610  ? 21  PHE   A CE2 1 
ATOM   151  C  CZ  . PHE   A 1 22  ? 14.14396  27.33729 21.05399  1.000 27.86408  ? 21  PHE   A CZ  1 
ATOM   152  N  N   . ARG   A 1 23  ? 13.93216  34.63758 22.83016  1.000 60.18186  ? 22  ARG   A N   1 
ATOM   153  C  CA  . ARG   A 1 23  ? 13.52307  35.93584 23.35480  1.000 62.48570  ? 22  ARG   A CA  1 
ATOM   154  C  C   . ARG   A 1 23  ? 12.85688  36.78867 22.27788  1.000 71.71830  ? 22  ARG   A C   1 
ATOM   155  O  O   . ARG   A 1 23  ? 11.76159  36.46906 21.80727  1.000 63.36773  ? 22  ARG   A O   1 
ATOM   156  C  CB  . ARG   A 1 23  ? 14.72977  36.67039 23.94694  1.000 65.82912  ? 22  ARG   A CB  1 
ATOM   157  C  CG  . ARG   A 1 23  ? 15.07510  36.26056 25.37401  1.000 58.31973  ? 22  ARG   A CG  1 
ATOM   158  C  CD  . ARG   A 1 23  ? 14.36335  37.12651 26.40614  0.000 60.76701  ? 22  ARG   A CD  1 
ATOM   159  N  NE  . ARG   A 1 23  ? 12.91638  36.94518 26.38606  0.000 61.78470  ? 22  ARG   A NE  1 
ATOM   160  C  CZ  . ARG   A 1 23  ? 12.05549  37.84936 25.93940  0.000 63.35302  ? 22  ARG   A CZ  1 
ATOM   161  N  NH1 . ARG   A 1 23  ? 12.46193  39.01763 25.47022  0.000 66.32643  ? 22  ARG   A NH1 1 
ATOM   162  N  NH2 . ARG   A 1 23  ? 10.75449  37.57462 25.96407  0.000 60.54123  ? 22  ARG   A NH2 1 
ATOM   163  N  N   . ALA   A 1 42  ? 16.51011  32.86042 17.41024  1.000 76.39430  ? 41  ALA   A N   1 
ATOM   164  C  CA  . ALA   A 1 42  ? 17.21561  32.42745 16.21742  1.000 74.60966  ? 41  ALA   A CA  1 
ATOM   165  C  C   . ALA   A 1 42  ? 18.69937  32.19005 16.43176  1.000 79.38108  ? 41  ALA   A C   1 
ATOM   166  O  O   . ALA   A 1 42  ? 19.23393  32.52612 17.49324  1.000 80.49620  ? 41  ALA   A O   1 
ATOM   167  N  N   . PRO   A 1 43  ? 19.36412  31.61540 15.42307  1.000 70.47220  ? 42  PRO   A N   1 
ATOM   168  C  CA  . PRO   A 1 43  ? 20.80243  31.32330 15.55746  1.000 71.65278  ? 42  PRO   A CA  1 
ATOM   169  C  C   . PRO   A 1 43  ? 21.64721  32.54690 15.86329  1.000 78.07792  ? 42  PRO   A C   1 
ATOM   170  O  O   . PRO   A 1 43  ? 22.66793  32.42799 16.55369  1.000 76.40879  ? 42  PRO   A O   1 
ATOM   171  C  CB  . PRO   A 1 43  ? 21.16305  30.74205 14.18406  0.000 67.12482  ? 42  PRO   A CB  1 
ATOM   172  C  CG  . PRO   A 1 43  ? 19.88461  30.19948 13.66125  0.000 64.65363  ? 42  PRO   A CG  1 
ATOM   173  C  CD  . PRO   A 1 43  ? 18.81743  31.12875 14.14555  0.000 70.28604  ? 42  PRO   A CD  1 
ATOM   174  N  N   . MET   A 1 44  ? 21.23401  33.72360 15.37926  0.000 80.45833  ? 43  MET   A N   1 
ATOM   175  C  CA  . MET   A 1 44  ? 22.10339  34.89825 15.38127  1.000 84.81131  ? 43  MET   A CA  1 
ATOM   176  C  C   . MET   A 1 44  ? 22.49463  35.31901 16.79251  1.000 85.94491  ? 43  MET   A C   1 
ATOM   177  O  O   . MET   A 1 44  ? 23.65299  35.67448 17.03905  1.000 91.29401  ? 43  MET   A O   1 
ATOM   178  C  CB  . MET   A 1 44  ? 21.41719  36.05461 14.65259  1.000 79.25851  ? 43  MET   A CB  1 
ATOM   179  N  N   . GLN   A 1 45  ? 21.54901  35.29275 17.72497  1.000 84.19661  ? 44  GLN   A N   1 
ATOM   180  C  CA  . GLN   A 1 45  ? 21.81609  35.78526 19.06835  1.000 81.09303  ? 44  GLN   A CA  1 
ATOM   181  C  C   . GLN   A 1 45  ? 22.97372  35.01470 19.70251  1.000 81.47968  ? 44  GLN   A C   1 
ATOM   182  O  O   . GLN   A 1 45  ? 23.10146  33.80153 19.49505  1.000 71.60178  ? 44  GLN   A O   1 
ATOM   183  C  CB  . GLN   A 1 45  ? 20.56468  35.65773 19.93789  1.000 82.60867  ? 44  GLN   A CB  1 
ATOM   184  C  CG  . GLN   A 1 45  ? 20.67960  36.33524 21.29124  1.000 87.69036  ? 44  GLN   A CG  1 
ATOM   185  C  CD  . GLN   A 1 45  ? 19.39099  37.00737 21.72179  1.000 100.66117 ? 44  GLN   A CD  1 
ATOM   186  O  OE1 . GLN   A 1 45  ? 18.30622  36.43316 21.60422  1.000 98.96515  ? 44  GLN   A OE1 1 
ATOM   187  N  NE2 . GLN   A 1 45  ? 19.50312  38.23259 22.22543  1.000 104.07083 ? 44  GLN   A NE2 1 
ATOM   188  N  N   . PRO   A 1 46  ? 23.84969  35.68388 20.44808  1.000 88.48870  ? 45  PRO   A N   1 
ATOM   189  C  CA  . PRO   A 1 46  ? 24.84923  34.96428 21.24018  1.000 77.87986  ? 45  PRO   A CA  1 
ATOM   190  C  C   . PRO   A 1 46  ? 24.23126  34.39638 22.50821  1.000 72.82371  ? 45  PRO   A C   1 
ATOM   191  O  O   . PRO   A 1 46  ? 23.19795  34.85728 22.99828  1.000 77.31487  ? 45  PRO   A O   1 
ATOM   192  C  CB  . PRO   A 1 46  ? 25.89556  36.03830 21.56920  1.000 81.45019  ? 45  PRO   A CB  1 
ATOM   193  C  CG  . PRO   A 1 46  ? 25.56704  37.19986 20.67368  1.000 86.32601  ? 45  PRO   A CG  1 
ATOM   194  C  CD  . PRO   A 1 46  ? 24.08708  37.13381 20.48236  1.000 91.62552  ? 45  PRO   A CD  1 
ATOM   195  N  N   . GLY   A 1 47  ? 24.89275  33.37221 23.03969  1.000 54.81393  ? 46  GLY   A N   1 
ATOM   196  C  CA  . GLY   A 1 47  ? 24.33109  32.59834 24.12187  1.000 43.92188  ? 46  GLY   A CA  1 
ATOM   197  C  C   . GLY   A 1 47  ? 23.23277  31.64059 23.71897  1.000 40.39517  ? 46  GLY   A C   1 
ATOM   198  O  O   . GLY   A 1 47  ? 22.84852  30.79420 24.53412  1.000 38.10658  ? 46  GLY   A O   1 
ATOM   199  N  N   . PHE   A 1 48  ? 22.71684  31.73560 22.49110  1.000 38.48143  ? 47  PHE   A N   1 
ATOM   200  C  CA  . PHE   A 1 48  ? 21.66663  30.81681 22.05351  1.000 35.64287  ? 47  PHE   A CA  1 
ATOM   201  C  C   . PHE   A 1 48  ? 22.07321  29.34962 22.11677  1.000 36.55458  ? 47  PHE   A C   1 
ATOM   202  O  O   . PHE   A 1 48  ? 21.31763  28.54950 22.69867  1.000 33.43712  ? 47  PHE   A O   1 
ATOM   203  C  CB  . PHE   A 1 48  ? 21.20381  31.18609 20.64160  1.000 41.60685  ? 47  PHE   A CB  1 
ATOM   204  C  CG  . PHE   A 1 48  ? 20.19355  30.23550 20.08262  1.000 37.19338  ? 47  PHE   A CG  1 
ATOM   205  C  CD1 . PHE   A 1 48  ? 18.87380  30.28910 20.48687  1.000 38.63453  ? 47  PHE   A CD1 1 
ATOM   206  C  CD2 . PHE   A 1 48  ? 20.57262  29.27029 19.16253  1.000 37.19156  ? 47  PHE   A CD2 1 
ATOM   207  C  CE1 . PHE   A 1 48  ? 17.94214  29.40240 19.98311  1.000 37.70640  ? 47  PHE   A CE1 1 
ATOM   208  C  CE2 . PHE   A 1 48  ? 19.64315  28.37986 18.64581  1.000 42.57286  ? 47  PHE   A CE2 1 
ATOM   209  C  CZ  . PHE   A 1 48  ? 18.32257  28.44815 19.05965  1.000 37.06244  ? 47  PHE   A CZ  1 
ATOM   210  N  N   . PRO   A 1 49  ? 23.20913  28.91702 21.55158  1.000 35.82546  ? 48  PRO   A N   1 
ATOM   211  C  CA  . PRO   A 1 49  ? 23.50108  27.47228 21.56212  1.000 29.70566  ? 48  PRO   A CA  1 
ATOM   212  C  C   . PRO   A 1 49  ? 23.61426  26.90506 22.96378  1.000 34.46091  ? 48  PRO   A C   1 
ATOM   213  O  O   . PRO   A 1 49  ? 23.13473  25.79461 23.23379  1.000 33.87023  ? 48  PRO   A O   1 
ATOM   214  C  CB  . PRO   A 1 49  ? 24.83401  27.37810 20.80346  1.000 38.37693  ? 48  PRO   A CB  1 
ATOM   215  C  CG  . PRO   A 1 49  ? 24.98013  28.69264 20.09331  1.000 38.04244  ? 48  PRO   A CG  1 
ATOM   216  C  CD  . PRO   A 1 49  ? 24.32894  29.68610 20.97935  1.000 41.12015  ? 48  PRO   A CD  1 
ATOM   217  N  N   . GLU   A 1 50  ? 24.24224  27.64774 23.87114  1.000 31.59242  ? 49  GLU   A N   1 
ATOM   218  C  CA  . GLU   A 1 50  ? 24.34631  27.18568 25.24822  1.000 33.41281  ? 49  GLU   A CA  1 
ATOM   219  C  C   . GLU   A 1 50  ? 22.97528  27.11632 25.90490  1.000 34.18009  ? 49  GLU   A C   1 
ATOM   220  O  O   . GLU   A 1 50  ? 22.68439  26.16949 26.64379  1.000 32.84847  ? 49  GLU   A O   1 
ATOM   221  C  CB  . GLU   A 1 50  ? 25.27727  28.10189 26.04324  1.000 35.86888  ? 49  GLU   A CB  1 
ATOM   222  C  CG  . GLU   A 1 50  ? 26.73481  28.05658 25.60601  1.000 38.19815  ? 49  GLU   A CG  1 
ATOM   223  C  CD  . GLU   A 1 50  ? 27.01744  28.88617 24.35951  1.000 52.41288  ? 49  GLU   A CD  1 
ATOM   224  O  OE1 . GLU   A 1 50  ? 26.10236  29.58739 23.87378  1.000 50.33965  ? 49  GLU   A OE1 1 
ATOM   225  O  OE2 . GLU   A 1 50  ? 28.16294  28.83499 23.86048  1.000 59.40165  ? 49  GLU   A OE2 1 
ATOM   226  N  N   . ASN   A 1 51  ? 22.11473  28.10110 25.63834  1.000 29.50129  ? 50  ASN   A N   1 
ATOM   227  C  CA  . ASN   A 1 51  ? 20.78329  28.07434 26.23820  1.000 30.06327  ? 50  ASN   A CA  1 
ATOM   228  C  C   . ASN   A 1 51  ? 19.94322  26.94686 25.65943  1.000 30.62233  ? 50  ASN   A C   1 
ATOM   229  O  O   . ASN   A 1 51  ? 19.20055  26.27663 26.39359  1.000 31.15734  ? 50  ASN   A O   1 
ATOM   230  C  CB  . ASN   A 1 51  ? 20.09533  29.42096 26.04760  1.000 33.00220  ? 50  ASN   A CB  1 
ATOM   231  C  CG  . ASN   A 1 51  ? 20.52680  30.42746 27.09586  1.000 35.20664  ? 50  ASN   A CG  1 
ATOM   232  O  OD1 . ASN   A 1 51  ? 20.90343  30.04506 28.20106  1.000 39.66080  ? 50  ASN   A OD1 1 
ATOM   233  N  ND2 . ASN   A 1 51  ? 20.52435  31.70359 26.73969  1.000 36.30412  ? 50  ASN   A ND2 1 
ATOM   234  N  N   . LEU   A 1 52  ? 20.06110  26.71813 24.35478  1.000 28.57403  ? 51  LEU   A N   1 
ATOM   235  C  CA  . LEU   A 1 52  ? 19.35101  25.61334 23.71722  1.000 25.98548  ? 51  LEU   A CA  1 
ATOM   236  C  C   . LEU   A 1 52  ? 19.83358  24.27509 24.24736  1.000 29.25323  ? 51  LEU   A C   1 
ATOM   237  O  O   . LEU   A 1 52  ? 19.03348  23.35205 24.44113  1.000 27.79783  ? 51  LEU   A O   1 
ATOM   238  C  CB  . LEU   A 1 52  ? 19.53530  25.68398 22.20408  1.000 28.01780  ? 51  LEU   A CB  1 
ATOM   239  C  CG  . LEU   A 1 52  ? 18.62261  24.74377 21.42267  1.000 31.19827  ? 51  LEU   A CG  1 
ATOM   240  C  CD1 . LEU   A 1 52  ? 17.18808  25.23724 21.48888  1.000 29.33140  ? 51  LEU   A CD1 1 
ATOM   241  C  CD2 . LEU   A 1 52  ? 19.09893  24.63599 19.97892  1.000 35.34221  ? 51  LEU   A CD2 1 
ATOM   242  N  N   . SER   A 1 53  ? 21.14190  24.14717 24.48731  1.000 28.49493  ? 52  SER   A N   1 
ATOM   243  C  CA  A SER   A 1 53  ? 21.66695  22.91219 25.05726  0.685 29.08013  ? 52  SER   A CA  1 
ATOM   244  C  CA  B SER   A 1 53  ? 21.65361  22.90453 25.05213  0.315 29.17720  ? 52  SER   A CA  1 
ATOM   245  C  C   . SER   A 1 53  ? 21.08786  22.66679 26.44350  1.000 26.58786  ? 52  SER   A C   1 
ATOM   246  O  O   . SER   A 1 53  ? 20.70083  21.53932 26.77939  1.000 31.44271  ? 52  SER   A O   1 
ATOM   247  C  CB  A SER   A 1 53  ? 23.19322  22.97935 25.11473  0.685 34.59335  ? 52  SER   A CB  1 
ATOM   248  C  CB  B SER   A 1 53  ? 23.17989  22.92892 25.08594  0.315 34.54832  ? 52  SER   A CB  1 
ATOM   249  O  OG  A SER   A 1 53  ? 23.72728  21.80342 25.68802  0.685 35.68788  ? 52  SER   A OG  1 
ATOM   250  O  OG  B SER   A 1 53  ? 23.70448  22.77380 23.78229  0.315 34.79003  ? 52  SER   A OG  1 
ATOM   251  N  N   . LYS   A 1 54  ? 21.02293  23.71848 27.26195  1.000 26.77467  ? 53  LYS   A N   1 
ATOM   252  C  CA  A LYS   A 1 54  ? 20.45222  23.58630 28.59816  0.425 28.97234  ? 53  LYS   A CA  1 
ATOM   253  C  CA  B LYS   A 1 54  ? 20.45284  23.58481 28.59734  0.575 28.95242  ? 53  LYS   A CA  1 
ATOM   254  C  C   . LYS   A 1 54  ? 18.97858  23.20429 28.53012  1.000 31.29596  ? 53  LYS   A C   1 
ATOM   255  O  O   . LYS   A 1 54  ? 18.51007  22.36922 29.31102  1.000 27.14138  ? 53  LYS   A O   1 
ATOM   256  C  CB  A LYS   A 1 54  ? 20.64349  24.89029 29.37567  0.425 30.54380  ? 53  LYS   A CB  1 
ATOM   257  C  CB  B LYS   A 1 54  ? 20.63523  24.88716 29.37315  0.575 30.52692  ? 53  LYS   A CB  1 
ATOM   258  C  CG  A LYS   A 1 54  ? 20.23119  24.84275 30.84749  0.425 32.09145  ? 53  LYS   A CG  1 
ATOM   259  C  CG  B LYS   A 1 54  ? 22.04691  25.13619 29.85090  0.575 30.70624  ? 53  LYS   A CG  1 
ATOM   260  C  CD  A LYS   A 1 54  ? 20.70448  23.57092 31.53855  0.425 39.80443  ? 53  LYS   A CD  1 
ATOM   261  C  CD  B LYS   A 1 54  ? 22.21478  26.58524 30.29085  0.575 37.11268  ? 53  LYS   A CD  1 
ATOM   262  C  CE  A LYS   A 1 54  ? 20.11837  23.44620 32.93794  0.425 37.86558  ? 53  LYS   A CE  1 
ATOM   263  C  CE  B LYS   A 1 54  ? 23.46436  26.77892 31.14169  0.575 36.54367  ? 53  LYS   A CE  1 
ATOM   264  N  NZ  A LYS   A 1 54  ? 19.75100  24.77771 33.48552  0.425 35.24625  ? 53  LYS   A NZ  1 
ATOM   265  N  NZ  B LYS   A 1 54  ? 24.00200  28.16052 30.99681  0.575 42.78324  ? 53  LYS   A NZ  1 
ATOM   266  N  N   . LEU   A 1 55  ? 18.22910  23.81123 27.60645  1.000 24.84255  ? 54  LEU   A N   1 
ATOM   267  C  CA  . LEU   A 1 55  ? 16.82460  23.45177 27.45550  1.000 24.42711  ? 54  LEU   A CA  1 
ATOM   268  C  C   . LEU   A 1 55  ? 16.67893  21.98392 27.08166  1.000 23.53056  ? 54  LEU   A C   1 
ATOM   269  O  O   . LEU   A 1 55  ? 15.80756  21.28301 27.61068  1.000 24.07806  ? 54  LEU   A O   1 
ATOM   270  C  CB  . LEU   A 1 55  ? 16.17492  24.35327 26.40349  1.000 24.42779  ? 54  LEU   A CB  1 
ATOM   271  C  CG  . LEU   A 1 55  ? 14.70206  24.14891 26.09288  1.000 21.59404  ? 54  LEU   A CG  1 
ATOM   272  C  CD1 . LEU   A 1 55  ? 13.83869  24.24685 27.33981  1.000 21.86655  ? 54  LEU   A CD1 1 
ATOM   273  C  CD2 . LEU   A 1 55  ? 14.27776  25.18977 25.06154  1.000 24.25016  ? 54  LEU   A CD2 1 
ATOM   274  N  N   . LYS   A 1 56  ? 17.52782  21.50103 26.16905  1.000 23.39542  ? 55  LYS   A N   1 
ATOM   275  C  CA  . LYS   A 1 56  ? 17.47055  20.10557 25.74807  1.000 23.51955  ? 55  LYS   A CA  1 
ATOM   276  C  C   . LYS   A 1 56  ? 17.72731  19.17874 26.92339  1.000 26.65226  ? 55  LYS   A C   1 
ATOM   277  O  O   . LYS   A 1 56  ? 17.10085  18.12354 27.04494  1.000 26.30932  ? 55  LYS   A O   1 
ATOM   278  C  CB  . LYS   A 1 56  ? 18.51993  19.83967 24.67079  1.000 27.79312  ? 55  LYS   A CB  1 
ATOM   279  C  CG  . LYS   A 1 56  ? 18.25588  20.39597 23.28902  1.000 32.15907  ? 55  LYS   A CG  1 
ATOM   280  C  CD  . LYS   A 1 56  ? 19.39648  19.95322 22.36555  1.000 36.23417  ? 55  LYS   A CD  1 
ATOM   281  C  CE  . LYS   A 1 56  ? 19.56887  20.89764 21.17270  1.000 48.40408  ? 55  LYS   A CE  1 
ATOM   282  N  NZ  . LYS   A 1 56  ? 20.36340  20.31027 20.04629  1.000 50.18970  ? 55  LYS   A NZ  1 
ATOM   283  N  N   . SER   A 1 57  ? 18.68426  19.53708 27.77803  1.000 26.80740  ? 56  SER   A N   1 
ATOM   284  C  CA  . SER   A 1 57  ? 18.98474  18.69583 28.92865  1.000 25.51208  ? 56  SER   A CA  1 
ATOM   285  C  C   . SER   A 1 57  ? 17.81330  18.66472 29.91362  1.000 29.38125  ? 56  SER   A C   1 
ATOM   286  O  O   . SER   A 1 57  ? 17.53794  17.62259 30.51902  1.000 30.38697  ? 56  SER   A O   1 
ATOM   287  C  CB  . SER   A 1 57  ? 20.26457  19.18907 29.60748  1.000 33.64451  ? 56  SER   A CB  1 
ATOM   288  O  OG  . SER   A 1 57  ? 20.20123  18.97875 30.99596  1.000 44.75560  ? 56  SER   A OG  1 
ATOM   289  N  N   . LEU   A 1 58  ? 17.09880  19.78691 30.07393  1.000 25.52361  ? 57  LEU   A N   1 
ATOM   290  C  CA  . LEU   A 1 58  ? 15.88860  19.76900 30.89669  1.000 27.66738  ? 57  LEU   A CA  1 
ATOM   291  C  C   . LEU   A 1 58  ? 14.82570  18.86139 30.28988  1.000 26.25848  ? 57  LEU   A C   1 
ATOM   292  O  O   . LEU   A 1 58  ? 14.19221  18.07207 31.00010  1.000 26.36373  ? 57  LEU   A O   1 
ATOM   293  C  CB  . LEU   A 1 58  ? 15.33909  21.18589 31.07565  1.000 28.35568  ? 57  LEU   A CB  1 
ATOM   294  C  CG  . LEU   A 1 58  ? 16.22929  22.12659 31.89637  1.000 28.82832  ? 57  LEU   A CG  1 
ATOM   295  C  CD1 . LEU   A 1 58  ? 15.70051  23.55584 31.82103  1.000 33.04935  ? 57  LEU   A CD1 1 
ATOM   296  C  CD2 . LEU   A 1 58  ? 16.31595  21.64567 33.34091  1.000 33.66317  ? 57  LEU   A CD2 1 
ATOM   297  N  N   . LEU   A 1 59  ? 14.58433  18.98876 28.97841  1.000 23.94236  ? 58  LEU   A N   1 
ATOM   298  C  CA  A LEU   A 1 59  ? 13.58035  18.14453 28.33386  0.570 23.34192  ? 58  LEU   A CA  1 
ATOM   299  C  CA  B LEU   A 1 59  ? 13.58955  18.14623 28.31892  0.430 23.40503  ? 58  LEU   A CA  1 
ATOM   300  C  C   . LEU   A 1 59  ? 13.95623  16.67566 28.41817  1.000 26.04579  ? 58  LEU   A C   1 
ATOM   301  O  O   . LEU   A 1 59  ? 13.07588  15.81717 28.53439  1.000 26.28164  ? 58  LEU   A O   1 
ATOM   302  C  CB  A LEU   A 1 59  ? 13.39427  18.53825 26.86878  0.570 25.08325  ? 58  LEU   A CB  1 
ATOM   303  C  CB  B LEU   A 1 59  ? 13.45044  18.54238 26.84860  0.430 25.08951  ? 58  LEU   A CB  1 
ATOM   304  C  CG  A LEU   A 1 59  ? 12.08171  19.23967 26.56070  0.570 27.57200  ? 58  LEU   A CG  1 
ATOM   305  C  CG  B LEU   A 1 59  ? 12.88195  19.92895 26.58091  0.430 23.92876  ? 58  LEU   A CG  1 
ATOM   306  C  CD1 A LEU   A 1 59  ? 12.15494  20.63801 27.14902  0.570 29.21027  ? 58  LEU   A CD1 1 
ATOM   307  C  CD1 B LEU   A 1 59  ? 12.88745  20.22548 25.07379  0.430 23.03691  ? 58  LEU   A CD1 1 
ATOM   308  C  CD2 A LEU   A 1 59  ? 11.84392  19.29275 25.06008  0.570 19.80168  ? 58  LEU   A CD2 1 
ATOM   309  C  CD2 B LEU   A 1 59  ? 11.48066  19.99828 27.15205  0.430 27.00696  ? 58  LEU   A CD2 1 
ATOM   310  N  N   . THR   A 1 60  ? 15.25278  16.36760 28.36699  1.000 25.57488  ? 59  THR   A N   1 
ATOM   311  C  CA  . THR   A 1 60  ? 15.68296  14.97866 28.44904  1.000 26.94188  ? 59  THR   A CA  1 
ATOM   312  C  C   . THR   A 1 60  ? 15.23155  14.34817 29.75773  1.000 28.62042  ? 59  THR   A C   1 
ATOM   313  O  O   . THR   A 1 60  ? 14.85374  13.17328 29.78922  1.000 33.05290  ? 59  THR   A O   1 
ATOM   314  C  CB  . THR   A 1 60  ? 17.20392  14.90902 28.29333  1.000 30.87180  ? 59  THR   A CB  1 
ATOM   315  O  OG1 . THR   A 1 60  ? 17.55138  15.29794 26.95802  1.000 33.74938  ? 59  THR   A OG1 1 
ATOM   316  C  CG2 . THR   A 1 60  ? 17.71722  13.50655 28.54830  1.000 33.33609  ? 59  THR   A CG2 1 
ATOM   317  N  N   . GLN   A 1 61  ? 15.23316  15.13228 30.84029  1.000 28.76559  ? 60  GLN   A N   1 
ATOM   318  C  CA  . GLN   A 1 61  ? 14.83189  14.67108 32.16628  1.000 30.95851  ? 60  GLN   A CA  1 
ATOM   319  C  C   . GLN   A 1 61  ? 13.32727  14.54508 32.35299  1.000 32.50434  ? 60  GLN   A C   1 
ATOM   320  O  O   . GLN   A 1 61  ? 12.89108  13.85530 33.28073  1.000 33.98545  ? 60  GLN   A O   1 
ATOM   321  C  CB  . GLN   A 1 61  ? 15.35601  15.62776 33.22958  1.000 32.20669  ? 60  GLN   A CB  1 
ATOM   322  C  CG  . GLN   A 1 61  ? 16.84103  15.88251 33.18143  1.000 37.14597  ? 60  GLN   A CG  1 
ATOM   323  C  CD  . GLN   A 1 61  ? 17.23385  17.00393 34.11524  1.000 47.66247  ? 60  GLN   A CD  1 
ATOM   324  O  OE1 . GLN   A 1 61  ? 16.77721  17.05946 35.26171  1.000 53.63493  ? 60  GLN   A OE1 1 
ATOM   325  N  NE2 . GLN   A 1 61  ? 18.11684  17.88369 33.64763  1.000 42.99260  ? 60  GLN   A NE2 1 
ATOM   326  N  N   . LEU   A 1 62  ? 12.52991  15.21421 31.52693  1.000 26.91086  ? 61  LEU   A N   1 
ATOM   327  C  CA  . LEU   A 1 62  ? 11.09008  15.26596 31.74840  1.000 28.83722  ? 61  LEU   A CA  1 
ATOM   328  C  C   . LEU   A 1 62  ? 10.45227  13.89943 31.54407  1.000 30.04381  ? 61  LEU   A C   1 
ATOM   329  O  O   . LEU   A 1 62  ? 10.76385  13.19227 30.58562  1.000 36.97228  ? 61  LEU   A O   1 
ATOM   330  C  CB  . LEU   A 1 62  ? 10.45461  16.27418 30.79240  1.000 26.33782  ? 61  LEU   A CB  1 
ATOM   331  C  CG  . LEU   A 1 62  ? 8.95838   16.53463 30.91786  1.000 29.23677  ? 61  LEU   A CG  1 
ATOM   332  C  CD1 . LEU   A 1 62  ? 8.68243   17.26043 32.21228  1.000 26.49066  ? 61  LEU   A CD1 1 
ATOM   333  C  CD2 . LEU   A 1 62  ? 8.51570   17.36641 29.71389  1.000 27.88166  ? 61  LEU   A CD2 1 
ATOM   334  N  N   . ARG   A 1 63  ? 9.54083   13.52958 32.44715  1.000 28.43234  ? 62  ARG   A N   1 
ATOM   335  C  CA  . ARG   A 1 63  ? 8.72916   12.33275 32.26927  1.000 30.12875  ? 62  ARG   A CA  1 
ATOM   336  C  C   . ARG   A 1 63  ? 7.25183   12.68656 32.39707  1.000 25.50332  ? 62  ARG   A C   1 
ATOM   337  O  O   . ARG   A 1 63  ? 6.89008   13.74942 32.90389  1.000 25.76022  ? 62  ARG   A O   1 
ATOM   338  C  CB  . ARG   A 1 63  ? 9.10937   11.22629 33.27871  1.000 36.28063  ? 62  ARG   A CB  1 
ATOM   339  C  CG  . ARG   A 1 63  ? 10.54873  11.29192 33.78761  1.000 38.64879  ? 62  ARG   A CG  1 
ATOM   340  C  CD  . ARG   A 1 63  ? 10.69487  10.75625 35.22413  1.000 49.37407  ? 62  ARG   A CD  1 
ATOM   341  N  NE  . ARG   A 1 63  ? 10.28212  11.72917 36.23081  1.000 55.75459  ? 62  ARG   A NE  1 
ATOM   342  C  CZ  . ARG   A 1 63  ? 10.40648  11.55939 37.53964  0.000 51.19445  ? 62  ARG   A CZ  1 
ATOM   343  N  NH1 . ARG   A 1 63  ? 10.93223  10.45704 38.04797  0.000 52.89881  ? 62  ARG   A NH1 1 
ATOM   344  N  NH2 . ARG   A 1 63  ? 9.99205   12.52032 38.35924  1.000 53.96170  ? 62  ARG   A NH2 1 
ATOM   345  N  N   . ALA   A 1 64  ? 6.39714   11.76881 31.94554  1.000 24.82006  ? 63  ALA   A N   1 
ATOM   346  C  CA  . ALA   A 1 64  ? 4.95460   12.00484 32.00782  1.000 24.34258  ? 63  ALA   A CA  1 
ATOM   347  C  C   . ALA   A 1 64  ? 4.49750   12.33374 33.42522  1.000 28.51071  ? 63  ALA   A C   1 
ATOM   348  O  O   . ALA   A 1 64  ? 3.63657   13.20037 33.61561  1.000 23.30202  ? 63  ALA   A O   1 
ATOM   349  C  CB  . ALA   A 1 64  ? 4.18794   10.79372 31.48262  1.000 27.88477  ? 63  ALA   A CB  1 
ATOM   350  N  N   . GLU   A 1 65  ? 5.07551   11.67078 34.43920  1.000 28.19958  ? 64  GLU   A N   1 
ATOM   351  C  CA  . GLU   A 1 65  ? 4.59977   11.89322 35.80673  1.000 28.19363  ? 64  GLU   A CA  1 
ATOM   352  C  C   . GLU   A 1 65  ? 4.87553   13.31503 36.27263  1.000 26.28779  ? 64  GLU   A C   1 
ATOM   353  O  O   . GLU   A 1 65  ? 4.18710   13.81643 37.17044  1.000 26.72843  ? 64  GLU   A O   1 
ATOM   354  C  CB  . GLU   A 1 65  ? 5.26214   10.92455 36.78605  1.000 32.44314  ? 64  GLU   A CB  1 
ATOM   355  C  CG  . GLU   A 1 65  ? 6.74750   10.75736 36.56407  1.000 38.64946  ? 64  GLU   A CG  1 
ATOM   356  C  CD  . GLU   A 1 65  ? 7.39210   9.76583  37.51460  1.000 57.71454  ? 64  GLU   A CD  1 
ATOM   357  O  OE1 . GLU   A 1 65  ? 7.30711   9.96639  38.75020  1.000 55.37737  ? 64  GLU   A OE1 1 
ATOM   358  O  OE2 . GLU   A 1 65  ? 7.99142   8.78713  37.01636  1.000 58.55605  ? 64  GLU   A OE2 1 
ATOM   359  N  N   . ASP   A 1 66  ? 5.88948   13.96878 35.70603  1.000 26.81711  ? 65  ASP   A N   1 
ATOM   360  C  CA  . ASP   A 1 66  ? 6.18925   15.34520 36.08377  1.000 23.53272  ? 65  ASP   A CA  1 
ATOM   361  C  C   . ASP   A 1 66  ? 5.10833   16.30685 35.62065  1.000 24.03243  ? 65  ASP   A C   1 
ATOM   362  O  O   . ASP   A 1 66  ? 5.10678   17.46367 36.05678  1.000 24.48905  ? 65  ASP   A O   1 
ATOM   363  C  CB  . ASP   A 1 66  ? 7.54036   15.79257 35.50582  1.000 26.50956  ? 65  ASP   A CB  1 
ATOM   364  C  CG  . ASP   A 1 66  ? 8.70543   14.90162 35.93727  1.000 35.70811  ? 65  ASP   A CG  1 
ATOM   365  O  OD1 . ASP   A 1 66  ? 8.81452   14.59333 37.14324  1.000 39.34246  ? 65  ASP   A OD1 1 
ATOM   366  O  OD2 . ASP   A 1 66  ? 9.54645   14.55718 35.07579  1.000 35.52086  ? 65  ASP   A OD2 1 
ATOM   367  N  N   . LEU   A 1 67  ? 4.22630   15.86704 34.72093  1.000 21.62565  ? 66  LEU   A N   1 
ATOM   368  C  CA  . LEU   A 1 67  ? 3.10612   16.65907 34.23556  1.000 22.30710  ? 66  LEU   A CA  1 
ATOM   369  C  C   . LEU   A 1 67  ? 1.76517   16.13414 34.73163  1.000 21.98978  ? 66  LEU   A C   1 
ATOM   370  O  O   . LEU   A 1 67  ? 0.71020   16.58997 34.25894  1.000 19.53544  ? 66  LEU   A O   1 
ATOM   371  C  CB  . LEU   A 1 67  ? 3.11765   16.69408 32.70157  1.000 19.53456  ? 66  LEU   A CB  1 
ATOM   372  C  CG  . LEU   A 1 67  ? 4.43478   17.16468 32.09533  1.000 20.43736  ? 66  LEU   A CG  1 
ATOM   373  C  CD1 . LEU   A 1 67  ? 4.31293   17.20434 30.56166  1.000 21.72915  ? 66  LEU   A CD1 1 
ATOM   374  C  CD2 . LEU   A 1 67  ? 4.82994   18.55094 32.62329  1.000 23.93317  ? 66  LEU   A CD2 1 
ATOM   375  N  N   . ASN   A 1 68  ? 1.78799   15.16969 35.65085  1.000 22.97718  ? 67  ASN   A N   1 
ATOM   376  C  CA  . ASN   A 1 68  ? 0.58822   14.49762 36.15449  1.000 25.57239  ? 67  ASN   A CA  1 
ATOM   377  C  C   . ASN   A 1 68  ? -0.23169  13.86293 35.02961  1.000 26.07477  ? 67  ASN   A C   1 
ATOM   378  O  O   . ASN   A 1 68  ? -1.46181  13.79256 35.10490  1.000 23.30434  ? 67  ASN   A O   1 
ATOM   379  C  CB  . ASN   A 1 68  ? -0.26647  15.45866 36.96939  1.000 24.18798  ? 67  ASN   A CB  1 
ATOM   380  C  CG  . ASN   A 1 68  ? 0.41569   15.86591 38.26410  1.000 29.65378  ? 67  ASN   A CG  1 
ATOM   381  O  OD1 . ASN   A 1 68  ? 0.82856   17.00882 38.42568  1.000 27.07577  ? 67  ASN   A OD1 1 
ATOM   382  N  ND2 . ASN   A 1 68  ? 0.54933   14.92024 39.18296  1.000 28.16988  ? 67  ASN   A ND2 1 
ATOM   383  N  N   . ILE   A 1 69  ? 0.44268   13.36406 34.00143  1.000 23.30386  ? 68  ILE   A N   1 
ATOM   384  C  CA  . ILE   A 1 69  ? -0.22006  12.71468 32.87617  1.000 22.96210  ? 68  ILE   A CA  1 
ATOM   385  C  C   . ILE   A 1 69  ? 0.03117   11.21879 32.97038  1.000 26.22309  ? 68  ILE   A C   1 
ATOM   386  O  O   . ILE   A 1 69  ? 1.17522   10.76443 32.85061  1.000 28.73351  ? 68  ILE   A O   1 
ATOM   387  C  CB  . ILE   A 1 69  ? 0.27988   13.25685 31.53104  1.000 23.18260  ? 68  ILE   A CB  1 
ATOM   388  C  CG1 . ILE   A 1 69  ? -0.02039  14.75574 31.42540  1.000 21.78198  ? 68  ILE   A CG1 1 
ATOM   389  C  CG2 . ILE   A 1 69  ? -0.40299  12.49422 30.41208  1.000 27.25739  ? 68  ILE   A CG2 1 
ATOM   390  C  CD1 . ILE   A 1 69  ? 0.59338   15.44252 30.18286  1.000 23.51476  ? 68  ILE   A CD1 1 
ATOM   391  N  N   . ALA   A 1 70  ? -1.03277  10.45590 33.17942  1.000 27.66765  ? 69  ALA   A N   1 
ATOM   392  C  CA  . ALA   A 1 70  ? -0.84025  9.01570  33.18522  1.000 31.49770  ? 69  ALA   A CA  1 
ATOM   393  C  C   . ALA   A 1 70  ? -0.76066  8.50544  31.75078  1.000 28.99693  ? 69  ALA   A C   1 
ATOM   394  O  O   . ALA   A 1 70  ? -1.50439  8.97438  30.88818  1.000 26.46473  ? 69  ALA   A O   1 
ATOM   395  C  CB  . ALA   A 1 70  ? -1.99171  8.32075  33.91109  1.000 31.07933  ? 69  ALA   A CB  1 
ATOM   396  N  N   . PRO   A 1 71  ? 0.10586   7.53820  31.47218  1.000 29.01633  ? 70  PRO   A N   1 
ATOM   397  C  CA  . PRO   A 1 71  ? 0.16704   6.99837  30.11357  1.000 30.71410  ? 70  PRO   A CA  1 
ATOM   398  C  C   . PRO   A 1 71  ? -1.17865  6.42245  29.72021  1.000 30.65485  ? 70  PRO   A C   1 
ATOM   399  O  O   . PRO   A 1 71  ? -1.86051  5.78907  30.52568  1.000 29.99334  ? 70  PRO   A O   1 
ATOM   400  C  CB  . PRO   A 1 71  ? 1.25259   5.92699  30.20587  1.000 31.24751  ? 70  PRO   A CB  1 
ATOM   401  C  CG  . PRO   A 1 71  ? 2.12403   6.41030  31.33352  1.000 34.66911  ? 70  PRO   A CG  1 
ATOM   402  C  CD  . PRO   A 1 71  ? 1.15575   6.97577  32.33683  1.000 32.84794  ? 70  PRO   A CD  1 
ATOM   403  N  N   . ARG   A 1 72  ? -1.59025  6.70823  28.48819  1.000 27.45539  ? 71  ARG   A N   1 
ATOM   404  C  CA  . ARG   A 1 72  ? -2.86361  6.23211  27.97521  1.000 28.52714  ? 71  ARG   A CA  1 
ATOM   405  C  C   . ARG   A 1 72  ? -2.64476  4.99936  27.11685  1.000 28.96432  ? 71  ARG   A C   1 
ATOM   406  O  O   . ARG   A 1 72  ? -1.69369  4.93428  26.33955  1.000 30.52283  ? 71  ARG   A O   1 
ATOM   407  C  CB  . ARG   A 1 72  ? -3.56880  7.32580  27.17509  1.000 24.64427  ? 71  ARG   A CB  1 
ATOM   408  C  CG  . ARG   A 1 72  ? -3.88156  8.51153  28.08480  1.000 26.48195  ? 71  ARG   A CG  1 
ATOM   409  C  CD  . ARG   A 1 72  ? -4.66164  9.58719  27.39894  1.000 28.43447  ? 71  ARG   A CD  1 
ATOM   410  N  NE  . ARG   A 1 72  ? -4.89946  10.67979 28.33837  1.000 26.89770  ? 71  ARG   A NE  1 
ATOM   411  C  CZ  . ARG   A 1 72  ? -5.48586  11.82450 28.02176  1.000 27.05392  ? 71  ARG   A CZ  1 
ATOM   412  N  NH1 . ARG   A 1 72  ? -5.94274  12.05027 26.79663  1.000 26.27446  ? 71  ARG   A NH1 1 
ATOM   413  N  NH2 . ARG   A 1 72  ? -5.61485  12.76681 28.95560  1.000 27.84853  ? 71  ARG   A NH2 1 
ATOM   414  N  N   . LYS   A 1 73  ? -3.51151  4.01042  27.28836  1.000 28.88923  ? 72  LYS   A N   1 
ATOM   415  C  CA  . LYS   A 1 73  ? -3.40164  2.76453  26.55338  1.000 31.12685  ? 72  LYS   A CA  1 
ATOM   416  C  C   . LYS   A 1 73  ? -4.60803  2.60101  25.64917  1.000 28.58047  ? 72  LYS   A C   1 
ATOM   417  O  O   . LYS   A 1 73  ? -5.63781  3.25681  25.82399  1.000 30.82240  ? 72  LYS   A O   1 
ATOM   418  C  CB  . LYS   A 1 73  ? -3.27936  1.57430  27.51410  1.000 30.02142  ? 72  LYS   A CB  1 
ATOM   419  C  CG  . LYS   A 1 73  ? -2.18903  1.80523  28.55372  1.000 33.94977  ? 72  LYS   A CG  1 
ATOM   420  C  CD  . LYS   A 1 73  ? -1.61496  0.50637  29.06503  1.000 41.89492  ? 72  LYS   A CD  1 
ATOM   421  C  CE  . LYS   A 1 73  ? -0.55067  0.76410  30.11793  1.000 52.17996  ? 72  LYS   A CE  1 
ATOM   422  N  NZ  . LYS   A 1 73  ? -0.43141  -0.37476 31.07412  1.000 50.15608  ? 72  LYS   A NZ  1 
ATOM   423  N  N   . ALA   A 1 74  ? -4.46361  1.71327  24.67368  1.000 29.66552  ? 73  ALA   A N   1 
ATOM   424  C  CA  . ALA   A 1 74  ? -5.46149  1.58530  23.62489  1.000 35.01322  ? 73  ALA   A CA  1 
ATOM   425  C  C   . ALA   A 1 74  ? -6.78807  1.09600  24.18645  1.000 35.16062  ? 73  ALA   A C   1 
ATOM   426  O  O   . ALA   A 1 74  ? -6.84107  0.33337  25.15349  1.000 36.41752  ? 73  ALA   A O   1 
ATOM   427  C  CB  . ALA   A 1 74  ? -4.97584  0.62696  22.54037  1.000 36.05450  ? 73  ALA   A CB  1 
ATOM   428  N  N   . THR   A 1 75  ? -7.87080  1.54594  23.56459  1.000 33.26615  ? 74  THR   A N   1 
ATOM   429  C  CA  . THR   A 1 75  ? -9.19646  1.08562  23.94315  1.000 39.19902  ? 74  THR   A CA  1 
ATOM   430  C  C   . THR   A 1 75  ? -9.63151  -0.16161 23.18809  1.000 34.73463  ? 74  THR   A C   1 
ATOM   431  O  O   . THR   A 1 75  ? -10.55956 -0.84670 23.63669  1.000 34.08908  ? 74  THR   A O   1 
ATOM   432  C  CB  . THR   A 1 75  ? -10.21782 2.18866  23.68860  1.000 40.96468  ? 74  THR   A CB  1 
ATOM   433  O  OG1 . THR   A 1 75  ? -10.37687 2.35026  22.27143  1.000 38.87058  ? 74  THR   A OG1 1 
ATOM   434  C  CG2 . THR   A 1 75  ? -9.74316  3.50063  24.30696  1.000 44.35801  ? 74  THR   A CG2 1 
ATOM   435  N  N   . LEU   A 1 76  ? -9.00342  -0.44696 22.05066  1.000 32.52898  ? 75  LEU   A N   1 
ATOM   436  C  CA  . LEU   A 1 76  ? -9.38814  -1.50859 21.12573  1.000 37.39582  ? 75  LEU   A CA  1 
ATOM   437  C  C   . LEU   A 1 76  ? -10.77170 -1.28353 20.52741  1.000 39.65314  ? 75  LEU   A C   1 
ATOM   438  O  O   . LEU   A 1 76  ? -11.29268 -2.16246 19.83906  1.000 36.30963  ? 75  LEU   A O   1 
ATOM   439  C  CB  . LEU   A 1 76  ? -9.30683  -2.89203 21.78745  1.000 32.23311  ? 75  LEU   A CB  1 
ATOM   440  C  CG  . LEU   A 1 76  ? -7.95268  -3.15440 22.45740  1.000 33.04535  ? 75  LEU   A CG  1 
ATOM   441  C  CD1 . LEU   A 1 76  ? -7.86226  -4.58094 23.01114  1.000 35.42692  ? 75  LEU   A CD1 1 
ATOM   442  C  CD2 . LEU   A 1 76  ? -6.81821  -2.88136 21.49538  1.000 34.67695  ? 75  LEU   A CD2 1 
ATOM   443  N  N   . GLN   A 1 77  ? -11.37556 -0.09767 20.74337  1.000 37.47129  ? 76  GLN   A N   1 
ATOM   444  C  CA  . GLN   A 1 77  ? -12.64526 0.24194  20.11148  1.000 38.94795  ? 76  GLN   A CA  1 
ATOM   445  C  C   . GLN   A 1 77  ? -12.43439 1.24366  18.97852  1.000 41.88980  ? 76  GLN   A C   1 
ATOM   446  O  O   . GLN   A 1 77  ? -11.50015 2.05224  19.01776  1.000 37.33778  ? 76  GLN   A O   1 
ATOM   447  C  CB  . GLN   A 1 77  ? -13.61664 0.83477  21.13547  1.000 38.55422  ? 76  GLN   A CB  1 
ATOM   448  C  CG  . GLN   A 1 77  ? -13.74262 0.04568  22.42996  1.000 39.91250  ? 76  GLN   A CG  1 
ATOM   449  C  CD  . GLN   A 1 77  ? -14.10635 -1.41047 22.19366  1.000 45.44121  ? 76  GLN   A CD  1 
ATOM   450  O  OE1 . GLN   A 1 77  ? -13.53985 -2.31110 22.81094  1.000 49.72019  ? 76  GLN   A OE1 1 
ATOM   451  N  NE2 . GLN   A 1 77  ? -15.06611 -1.64521 21.30433  1.000 47.14063  ? 76  GLN   A NE2 1 
ATOM   452  N  N   . PRO   A 1 78  ? -13.27357 1.23974  17.94668  1.000 39.85258  ? 77  PRO   A N   1 
ATOM   453  C  CA  . PRO   A 1 78  ? -13.13769 2.26097  16.90377  1.000 35.17657  ? 77  PRO   A CA  1 
ATOM   454  C  C   . PRO   A 1 78  ? -13.39491 3.64919  17.47803  1.000 42.17167  ? 77  PRO   A C   1 
ATOM   455  O  O   . PRO   A 1 78  ? -14.08257 3.82269  18.48746  1.000 42.34757  ? 77  PRO   A O   1 
ATOM   456  C  CB  . PRO   A 1 78  ? -14.19103 1.87750  15.85670  1.000 44.32948  ? 77  PRO   A CB  1 
ATOM   457  C  CG  . PRO   A 1 78  ? -15.04450 0.83697  16.46660  1.000 45.84473  ? 77  PRO   A CG  1 
ATOM   458  C  CD  . PRO   A 1 78  ? -14.48313 0.41281  17.79058  1.000 46.09834  ? 77  PRO   A CD  1 
ATOM   459  N  N   . LEU   A 1 79  ? -12.80811 4.64861  16.82743  1.000 36.19151  ? 78  LEU   A N   1 
ATOM   460  C  CA  . LEU   A 1 79  ? -12.95449 6.02170  17.28792  1.000 37.25448  ? 78  LEU   A CA  1 
ATOM   461  C  C   . LEU   A 1 79  ? -14.18467 6.64254  16.62547  1.000 32.32307  ? 78  LEU   A C   1 
ATOM   462  O  O   . LEU   A 1 79  ? -14.24543 6.70471  15.39068  1.000 35.55081  ? 78  LEU   A O   1 
ATOM   463  C  CB  . LEU   A 1 79  ? -11.69732 6.82327  16.97740  1.000 37.91742  ? 78  LEU   A CB  1 
ATOM   464  C  CG  . LEU   A 1 79  ? -11.76917 8.34103  17.08508  1.000 40.64222  ? 78  LEU   A CG  1 
ATOM   465  C  CD1 . LEU   A 1 79  ? -11.57418 8.68841  18.54150  1.000 36.82499  ? 78  LEU   A CD1 1 
ATOM   466  C  CD2 . LEU   A 1 79  ? -10.69945 9.00965  16.23325  1.000 40.96833  ? 78  LEU   A CD2 1 
ATOM   467  N  N   . PRO   A 1 80  ? -15.17264 7.09042  17.39030  1.000 36.11117  ? 79  PRO   A N   1 
ATOM   468  C  CA  . PRO   A 1 80  ? -16.43174 7.60263  16.79923  1.000 38.89770  ? 79  PRO   A CA  1 
ATOM   469  C  C   . PRO   A 1 80  ? -16.20301 8.91184  16.06992  1.000 33.00538  ? 79  PRO   A C   1 
ATOM   470  O  O   . PRO   A 1 80  ? -15.27453 9.66178  16.41339  1.000 34.89337  ? 79  PRO   A O   1 
ATOM   471  C  CB  . PRO   A 1 80  ? -17.33584 7.81264  18.02566  1.000 40.99671  ? 79  PRO   A CB  1 
ATOM   472  C  CG  . PRO   A 1 80  ? -16.59445 7.19235  19.19356  1.000 42.80666  ? 79  PRO   A CG  1 
ATOM   473  C  CD  . PRO   A 1 80  ? -15.15323 7.23270  18.85189  1.000 36.10727  ? 79  PRO   A CD  1 
ATOM   474  N  N   . PRO   A 1 81  ? -17.05747 9.24521  15.09633  1.000 32.32608  ? 80  PRO   A N   1 
ATOM   475  C  CA  . PRO   A 1 81  ? -16.78655 10.40853 14.23584  1.000 36.05785  ? 80  PRO   A CA  1 
ATOM   476  C  C   . PRO   A 1 81  ? -16.75075 11.73850 14.96827  1.000 32.16282  ? 80  PRO   A C   1 
ATOM   477  O  O   . PRO   A 1 81  ? -16.19051 12.70494 14.43170  1.000 31.81088  ? 80  PRO   A O   1 
ATOM   478  C  CB  . PRO   A 1 81  ? -17.94686 10.38053 13.22933  1.000 41.10216  ? 80  PRO   A CB  1 
ATOM   479  C  CG  . PRO   A 1 81  ? -18.50537 9.00344  13.29867  1.000 40.12931  ? 80  PRO   A CG  1 
ATOM   480  C  CD  . PRO   A 1 81  ? -18.28179 8.52696  14.69591  1.000 39.26411  ? 80  PRO   A CD  1 
ATOM   481  N  N   . ASN   A 1 82  ? -17.35997 11.84005 16.14405  1.000 28.13592  ? 81  ASN   A N   1 
ATOM   482  C  CA  . ASN   A 1 82  ? -17.45017 13.12277 16.82653  1.000 29.48365  ? 81  ASN   A CA  1 
ATOM   483  C  C   . ASN   A 1 82  ? -16.26715 13.38283 17.75254  1.000 32.53688  ? 81  ASN   A C   1 
ATOM   484  O  O   . ASN   A 1 82  ? -16.18407 14.47299 18.33292  1.000 39.07483  ? 81  ASN   A O   1 
ATOM   485  C  CB  . ASN   A 1 82  ? -18.77110 13.21728 17.61417  1.000 31.32192  ? 81  ASN   A CB  1 
ATOM   486  C  CG  . ASN   A 1 82  ? -18.88117 12.17391 18.70091  1.000 36.10933  ? 81  ASN   A CG  1 
ATOM   487  O  OD1 . ASN   A 1 82  ? -18.51100 11.02010 18.50576  1.000 33.62837  ? 81  ASN   A OD1 1 
ATOM   488  N  ND2 . ASN   A 1 82  ? -19.41129 12.57259 19.85800  1.000 34.90177  ? 81  ASN   A ND2 1 
ATOM   489  N  N   . LEU   A 1 83  ? -15.32523 12.42037 17.89067  1.000 28.63848  ? 82  LEU   A N   1 
ATOM   490  C  CA  . LEU   A 1 83  ? -14.20524 12.73383 18.77829  1.000 28.14305  ? 82  LEU   A CA  1 
ATOM   491  C  C   . LEU   A 1 83  ? -12.92555 12.96475 17.98239  1.000 29.18375  ? 82  LEU   A C   1 
ATOM   492  O  O   . LEU   A 1 83  ? -12.67657 12.27199 16.99243  1.000 25.70374  ? 82  LEU   A O   1 
ATOM   493  C  CB  . LEU   A 1 83  ? -13.94680 11.62095 19.79379  1.000 34.88534  ? 82  LEU   A CB  1 
ATOM   494  C  CG  . LEU   A 1 83  ? -15.19796 11.19894 20.56476  1.000 43.40394  ? 82  LEU   A CG  1 
ATOM   495  C  CD1 . LEU   A 1 83  ? -14.96099 9.87715  21.30805  1.000 44.78520  ? 82  LEU   A CD1 1 
ATOM   496  C  CD2 . LEU   A 1 83  ? -15.69641 12.31627 21.46134  1.000 39.07015  ? 82  LEU   A CD2 1 
ATOM   497  N  N   . PRO   A 1 84  ? -12.07993 13.90284 18.40957  1.000 28.55287  ? 83  PRO   A N   1 
ATOM   498  C  CA  . PRO   A 1 84  ? -10.88266 14.20642 17.63308  1.000 26.02341  ? 83  PRO   A CA  1 
ATOM   499  C  C   . PRO   A 1 84  ? -9.85952  13.09353 17.75727  1.000 24.10641  ? 83  PRO   A C   1 
ATOM   500  O  O   . PRO   A 1 84  ? -9.80146  12.39626 18.78204  1.000 27.36964  ? 83  PRO   A O   1 
ATOM   501  C  CB  . PRO   A 1 84  ? -10.36559 15.50518 18.27739  1.000 26.74603  ? 83  PRO   A CB  1 
ATOM   502  C  CG  . PRO   A 1 84  ? -10.82875 15.40798 19.69195  1.000 28.43677  ? 83  PRO   A CG  1 
ATOM   503  C  CD  . PRO   A 1 84  ? -12.16355 14.69839 19.64928  1.000 31.45666  ? 83  PRO   A CD  1 
ATOM   504  N  N   . PRO   A 1 85  ? -9.00256  12.91452 16.74838  1.000 22.87994  ? 84  PRO   A N   1 
ATOM   505  C  CA  . PRO   A 1 85  ? -7.91672  11.93677 16.87629  1.000 24.26431  ? 84  PRO   A CA  1 
ATOM   506  C  C   . PRO   A 1 85  ? -6.80999  12.39830 17.80484  1.000 21.78096  ? 84  PRO   A C   1 
ATOM   507  O  O   . PRO   A 1 85  ? -6.06694  11.56113 18.32878  1.000 22.67033  ? 84  PRO   A O   1 
ATOM   508  C  CB  . PRO   A 1 85  ? -7.40324  11.79845 15.43727  1.000 22.84487  ? 84  PRO   A CB  1 
ATOM   509  C  CG  . PRO   A 1 85  ? -7.74245  13.12457 14.79547  1.000 23.54259  ? 84  PRO   A CG  1 
ATOM   510  C  CD  . PRO   A 1 85  ? -9.05133  13.54032 15.41886  1.000 24.66416  ? 84  PRO   A CD  1 
ATOM   511  N  N   . VAL   A 1 86  ? -6.67389  13.70223 18.01683  1.000 22.94094  ? 85  VAL   A N   1 
ATOM   512  C  CA  . VAL   A 1 86  ? -5.55721  14.27903 18.76083  1.000 19.52577  ? 85  VAL   A CA  1 
ATOM   513  C  C   . VAL   A 1 86  ? -6.11451  15.36055 19.66643  1.000 18.66468  ? 85  VAL   A C   1 
ATOM   514  O  O   . VAL   A 1 86  ? -7.07340  16.04326 19.30139  1.000 19.81678  ? 85  VAL   A O   1 
ATOM   515  C  CB  . VAL   A 1 86  ? -4.49654  14.86756 17.79720  1.000 22.12740  ? 85  VAL   A CB  1 
ATOM   516  C  CG1 . VAL   A 1 86  ? -3.31185  15.45454 18.56956  1.000 21.60574  ? 85  VAL   A CG1 1 
ATOM   517  C  CG2 . VAL   A 1 86  ? -4.01958  13.79495 16.83400  1.000 21.74194  ? 85  VAL   A CG2 1 
ATOM   518  N  N   . THR   A 1 87  ? -5.53727  15.50919 20.86247  1.000 19.11985  ? 86  THR   A N   1 
ATOM   519  C  CA  . THR   A 1 87  ? -5.91622  16.60651 21.74299  1.000 20.00944  ? 86  THR   A CA  1 
ATOM   520  C  C   . THR   A 1 87  ? -4.65671  17.33661 22.18507  1.000 19.96570  ? 86  THR   A C   1 
ATOM   521  O  O   . THR   A 1 87  ? -3.53430  16.85414 22.01077  1.000 18.94157  ? 86  THR   A O   1 
ATOM   522  C  CB  . THR   A 1 87  ? -6.71599  16.11724 22.95424  1.000 23.70847  ? 86  THR   A CB  1 
ATOM   523  O  OG1 . THR   A 1 87  ? -5.99467  15.05945 23.60428  1.000 22.31581  ? 86  THR   A OG1 1 
ATOM   524  C  CG2 . THR   A 1 87  ? -8.09343  15.59857 22.50751  1.000 24.64910  ? 86  THR   A CG2 1 
ATOM   525  N  N   . TYR   A 1 88  ? -4.85937  18.53336 22.71818  1.000 20.66730  ? 87  TYR   A N   1 
ATOM   526  C  CA  . TYR   A 1 88  ? -3.77802  19.42954 23.10370  1.000 18.91591  ? 87  TYR   A CA  1 
ATOM   527  C  C   . TYR   A 1 88  ? -4.00648  19.95231 24.51115  1.000 19.59193  ? 87  TYR   A C   1 
ATOM   528  O  O   . TYR   A 1 88  ? -5.07472  20.49479 24.80870  1.000 20.23211  ? 87  TYR   A O   1 
ATOM   529  C  CB  . TYR   A 1 88  ? -3.66731  20.61836 22.13221  1.000 19.30873  ? 87  TYR   A CB  1 
ATOM   530  C  CG  . TYR   A 1 88  ? -2.57822  21.60903 22.48380  1.000 21.13955  ? 87  TYR   A CG  1 
ATOM   531  C  CD1 . TYR   A 1 88  ? -1.23981  21.24244 22.41305  1.000 20.07999  ? 87  TYR   A CD1 1 
ATOM   532  C  CD2 . TYR   A 1 88  ? -2.88204  22.90959 22.88514  1.000 23.07955  ? 87  TYR   A CD2 1 
ATOM   533  C  CE1 . TYR   A 1 88  ? -0.23406  22.13112 22.72146  1.000 21.81801  ? 87  TYR   A CE1 1 
ATOM   534  C  CE2 . TYR   A 1 88  ? -1.86571  23.81299 23.20376  1.000 20.32887  ? 87  TYR   A CE2 1 
ATOM   535  C  CZ  . TYR   A 1 88  ? -0.55550  23.41065 23.11251  1.000 21.57865  ? 87  TYR   A CZ  1 
ATOM   536  O  OH  . TYR   A 1 88  ? 0.47840   24.27179 23.41611  1.000 25.13428  ? 87  TYR   A OH  1 
ATOM   537  N  N   . MET   A 1 89  ? -2.99718  19.81630 25.36889  1.000 18.52220  ? 88  MET   A N   1 
ATOM   538  C  CA  . MET   A 1 89  ? -2.98532  20.49821 26.66500  1.000 17.26606  ? 88  MET   A CA  1 
ATOM   539  C  C   . MET   A 1 89  ? -2.04585  21.68994 26.64150  1.000 23.94166  ? 88  MET   A C   1 
ATOM   540  O  O   . MET   A 1 89  ? -0.84095  21.54322 26.43570  1.000 21.25839  ? 88  MET   A O   1 
ATOM   541  C  CB  . MET   A 1 89  ? -2.66229  19.58355 27.85328  1.000 22.81846  ? 88  MET   A CB  1 
ATOM   542  C  CG  . MET   A 1 89  ? -3.20725  18.16780 27.80574  1.000 22.39189  ? 88  MET   A CG  1 
ATOM   543  S  SD  . MET   A 1 89  ? -2.43319  17.13310 29.04502  1.000 21.41732  ? 88  MET   A SD  1 
ATOM   544  C  CE  . MET   A 1 89  ? -3.74445  15.97447 29.36646  1.000 26.60532  ? 88  MET   A CE  1 
ATOM   545  N  N   . HIS   A 1 90  ? -2.61868  22.86857 26.82550  1.000 19.90583  ? 89  HIS   A N   1 
ATOM   546  C  CA  . HIS   A 1 90  ? -1.85151  24.10149 26.85237  1.000 22.67756  ? 89  HIS   A CA  1 
ATOM   547  C  C   . HIS   A 1 90  ? -1.18449  24.28002 28.20775  1.000 23.29961  ? 89  HIS   A C   1 
ATOM   548  O  O   . HIS   A 1 90  ? -1.84236  24.17751 29.25580  1.000 22.79310  ? 89  HIS   A O   1 
ATOM   549  C  CB  . HIS   A 1 90  ? -2.77835  25.27135 26.55028  1.000 25.01909  ? 89  HIS   A CB  1 
ATOM   550  C  CG  . HIS   A 1 90  ? -2.15119  26.61216 26.75762  1.000 32.00665  ? 89  HIS   A CG  1 
ATOM   551  N  ND1 . HIS   A 1 90  ? -1.18236  27.12391 25.92565  1.000 38.99891  ? 89  HIS   A ND1 1 
ATOM   552  C  CD2 . HIS   A 1 90  ? -2.35331  27.54362 27.71827  1.000 41.26322  ? 89  HIS   A CD2 1 
ATOM   553  C  CE1 . HIS   A 1 90  ? -0.82131  28.31946 26.36177  1.000 30.09687  ? 89  HIS   A CE1 1 
ATOM   554  N  NE2 . HIS   A 1 90  ? -1.51558  28.59568 27.44745  1.000 43.19744  ? 89  HIS   A NE2 1 
ATOM   555  N  N   . ILE   A 1 91  ? 0.12260   24.54218 28.19801  1.000 20.56412  ? 90  ILE   A N   1 
ATOM   556  C  CA  . ILE   A 1 91  ? 0.87589   24.80250 29.42419  1.000 19.68918  ? 90  ILE   A CA  1 
ATOM   557  C  C   . ILE   A 1 91  ? 1.24875   26.27627 29.55493  1.000 21.17544  ? 90  ILE   A C   1 
ATOM   558  O  O   . ILE   A 1 91  ? 0.95500   26.90506 30.57597  1.000 23.49260  ? 90  ILE   A O   1 
ATOM   559  C  CB  . ILE   A 1 91  ? 2.12257   23.89350 29.51697  1.000 18.69458  ? 90  ILE   A CB  1 
ATOM   560  C  CG1 . ILE   A 1 91  ? 1.65916   22.42588 29.57088  1.000 22.72587  ? 90  ILE   A CG1 1 
ATOM   561  C  CG2 . ILE   A 1 91  ? 2.96109   24.26699 30.74580  1.000 21.45141  ? 90  ILE   A CG2 1 
ATOM   562  C  CD1 . ILE   A 1 91  ? 2.79744   21.40341 29.66846  1.000 20.96028  ? 90  ILE   A CD1 1 
ATOM   563  N  N   . TYR   A 1 92  ? 1.91389   26.84431 28.54801  1.000 20.42051  ? 91  TYR   A N   1 
ATOM   564  C  CA  . TYR   A 1 92  ? 2.21767   28.27383 28.60592  1.000 20.45621  ? 91  TYR   A CA  1 
ATOM   565  C  C   . TYR   A 1 92  ? 2.52429   28.78988 27.20779  1.000 24.69290  ? 91  TYR   A C   1 
ATOM   566  O  O   . TYR   A 1 92  ? 2.96928   28.04287 26.34118  1.000 24.06648  ? 91  TYR   A O   1 
ATOM   567  C  CB  . TYR   A 1 92  ? 3.40569   28.57021 29.52850  1.000 21.34759  ? 91  TYR   A CB  1 
ATOM   568  C  CG  . TYR   A 1 92  ? 3.27527   29.94373 30.14192  1.000 25.97057  ? 91  TYR   A CG  1 
ATOM   569  C  CD1 . TYR   A 1 92  ? 2.36061   30.16430 31.15151  1.000 27.56459  ? 91  TYR   A CD1 1 
ATOM   570  C  CD2 . TYR   A 1 92  ? 4.02169   31.01924 29.67733  1.000 33.56092  ? 91  TYR   A CD2 1 
ATOM   571  C  CE1 . TYR   A 1 92  ? 2.19867   31.41511 31.71835  1.000 34.25802  ? 91  TYR   A CE1 1 
ATOM   572  C  CE2 . TYR   A 1 92  ? 3.86957   32.28900 30.24327  1.000 33.32308  ? 91  TYR   A CE2 1 
ATOM   573  C  CZ  . TYR   A 1 92  ? 2.95349   32.46973 31.25739  1.000 31.30846  ? 91  TYR   A CZ  1 
ATOM   574  O  OH  . TYR   A 1 92  ? 2.77015   33.71529 31.82657  1.000 37.22388  ? 91  TYR   A OH  1 
ATOM   575  N  N   . GLU   A 1 93  ? 2.31254   30.09088 27.00581  1.000 22.60442  ? 92  GLU   A N   1 
ATOM   576  C  CA  . GLU   A 1 93  ? 2.72045   30.71391 25.75433  1.000 24.72152  ? 92  GLU   A CA  1 
ATOM   577  C  C   . GLU   A 1 93  ? 3.11728   32.15899 26.00329  1.000 30.93459  ? 92  GLU   A C   1 
ATOM   578  O  O   . GLU   A 1 93  ? 2.46358   32.85678 26.78321  1.000 30.12731  ? 92  GLU   A O   1 
ATOM   579  C  CB  . GLU   A 1 93  ? 1.59656   30.64466 24.71551  1.000 29.95948  ? 92  GLU   A CB  1 
ATOM   580  C  CG  . GLU   A 1 93  ? 1.94663   31.24817 23.36199  1.000 34.41908  ? 92  GLU   A CG  1 
ATOM   581  C  CD  . GLU   A 1 93  ? 1.04926   32.41895 23.00674  1.000 48.96870  ? 92  GLU   A CD  1 
ATOM   582  O  OE1 . GLU   A 1 93  ? 0.18064   32.76944 23.83952  1.000 57.52528  ? 92  GLU   A OE1 1 
ATOM   583  O  OE2 . GLU   A 1 93  ? 1.20570   32.97949 21.89374  1.000 51.71374  ? 92  GLU   A OE2 1 
ATOM   584  N  N   . THR   A 1 94  ? 4.20345   32.58473 25.36096  1.000 30.35183  ? 93  THR   A N   1 
ATOM   585  C  CA  . THR   A 1 94  ? 4.61583   33.98639 25.27921  1.000 31.12918  ? 93  THR   A CA  1 
ATOM   586  C  C   . THR   A 1 94  ? 4.70927   34.37840 23.80188  1.000 36.09490  ? 93  THR   A C   1 
ATOM   587  O  O   . THR   A 1 94  ? 4.34383   33.61031 22.90888  1.000 34.88089  ? 93  THR   A O   1 
ATOM   588  C  CB  . THR   A 1 94  ? 5.94465   34.22675 26.00188  1.000 34.97933  ? 93  THR   A CB  1 
ATOM   589  O  OG1 . THR   A 1 94  ? 7.02506   33.64341 25.25429  1.000 34.00123  ? 93  THR   A OG1 1 
ATOM   590  C  CG2 . THR   A 1 94  ? 5.93101   33.65885 27.40163  1.000 34.98254  ? 93  THR   A CG2 1 
ATOM   591  N  N   . ASP   A 1 95  ? 5.18018   35.59963 23.53696  1.000 38.67036  ? 94  ASP   A N   1 
ATOM   592  C  CA  . ASP   A 1 95  ? 5.49694   35.94355 22.15627  1.000 35.07524  ? 94  ASP   A CA  1 
ATOM   593  C  C   . ASP   A 1 95  ? 6.70591   35.16553 21.65206  1.000 34.15288  ? 94  ASP   A C   1 
ATOM   594  O  O   . ASP   A 1 95  ? 6.87253   35.02054 20.43926  1.000 36.41123  ? 94  ASP   A O   1 
ATOM   595  C  CB  . ASP   A 1 95  ? 5.75265   37.44936 22.01983  1.000 42.86567  ? 94  ASP   A CB  1 
ATOM   596  C  CG  . ASP   A 1 95  ? 4.47183   38.26859 22.07113  0.594 37.29443  ? 94  ASP   A CG  1 
ATOM   597  O  OD1 . ASP   A 1 95  ? 3.37081   37.67874 22.07775  0.430 38.69670  ? 94  ASP   A OD1 1 
ATOM   598  O  OD2 . ASP   A 1 95  ? 4.57181   39.51263 22.10842  0.271 40.78660  ? 94  ASP   A OD2 1 
ATOM   599  N  N   . GLY   A 1 96  ? 7.53672   34.64844 22.55619  1.000 33.37880  ? 95  GLY   A N   1 
ATOM   600  C  CA  . GLY   A 1 96  ? 8.74797   33.95770 22.16358  1.000 28.22224  ? 95  GLY   A CA  1 
ATOM   601  C  C   . GLY   A 1 96  ? 8.57162   32.46747 21.93263  1.000 26.77599  ? 95  GLY   A C   1 
ATOM   602  O  O   . GLY   A 1 96  ? 9.27141   31.89297 21.09854  1.000 27.04335  ? 95  GLY   A O   1 
ATOM   603  N  N   . PHE   A 1 97  ? 7.66770   31.82142 22.66735  1.000 25.28079  ? 96  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 97  ? 7.53931   30.37196 22.53640  1.000 22.93362  ? 96  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 97  ? 6.17034   29.91365 23.02209  1.000 25.42088  ? 96  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 97  ? 5.47619   30.60937 23.76834  1.000 26.11382  ? 96  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 97  ? 8.64195   29.64948 23.31810  1.000 22.77263  ? 96  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 97  ? 8.41728   29.66808 24.80286  1.000 23.57982  ? 96  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 97  ? 8.78800   30.78043 25.53727  1.000 30.57759  ? 96  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 97  ? 7.79672   28.61008 25.45463  1.000 24.23350  ? 96  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 97  ? 8.57724   30.83756 26.88574  1.000 30.85124  ? 96  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 97  ? 7.57092   28.66608 26.82112  1.000 27.41521  ? 96  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 97  ? 7.96035   29.78500 27.53435  1.000 34.17599  ? 96  PHE   A CZ  1 
ATOM   614  N  N   . SER   A 1 98  ? 5.78692   28.72382 22.57849  1.000 22.29085  ? 97  SER   A N   1 
ATOM   615  C  CA  A SER   A 1 98  ? 4.59841   28.04394 23.07440  0.595 22.18028  ? 97  SER   A CA  1 
ATOM   616  C  CA  B SER   A 1 98  ? 4.60319   28.04824 23.08045  0.405 22.21744  ? 97  SER   A CA  1 
ATOM   617  C  C   . SER   A 1 98  ? 5.01473   26.70099 23.65382  1.000 22.84013  ? 97  SER   A C   1 
ATOM   618  O  O   . SER   A 1 98  ? 5.95877   26.08352 23.17779  1.000 23.73909  ? 97  SER   A O   1 
ATOM   619  C  CB  A SER   A 1 98  ? 3.56700   27.83577 21.95879  0.595 25.88785  ? 97  SER   A CB  1 
ATOM   620  C  CB  B SER   A 1 98  ? 3.56943   27.85951 21.97528  0.405 25.87492  ? 97  SER   A CB  1 
ATOM   621  O  OG  A SER   A 1 98  ? 3.99836   26.82220 21.06363  0.595 24.55540  ? 97  SER   A OG  1 
ATOM   622  O  OG  B SER   A 1 98  ? 2.43442   27.20810 22.48629  0.405 26.85924  ? 97  SER   A OG  1 
ATOM   623  N  N   . LEU   A 1 99  ? 4.29290   26.25272 24.68229  1.000 21.94246  ? 98  LEU   A N   1 
ATOM   624  C  CA  . LEU   A 1 99  ? 4.63772   25.04007 25.41980  1.000 20.85288  ? 98  LEU   A CA  1 
ATOM   625  C  C   . LEU   A 1 99  ? 3.36530   24.24622 25.69291  1.000 21.52138  ? 98  LEU   A C   1 
ATOM   626  O  O   . LEU   A 1 99  ? 2.43634   24.76733 26.31992  1.000 20.13787  ? 98  LEU   A O   1 
ATOM   627  C  CB  . LEU   A 1 99  ? 5.33099   25.42745 26.74391  1.000 20.30012  ? 98  LEU   A CB  1 
ATOM   628  C  CG  . LEU   A 1 99  ? 5.67311   24.37118 27.78320  1.000 20.57136  ? 98  LEU   A CG  1 
ATOM   629  C  CD1 . LEU   A 1 99  ? 6.75074   23.46260 27.23757  1.000 24.87933  ? 98  LEU   A CD1 1 
ATOM   630  C  CD2 . LEU   A 1 99  ? 6.18787   25.05752 29.05650  1.000 23.13773  ? 98  LEU   A CD2 1 
ATOM   631  N  N   . GLY   A 1 100 ? 3.31720   22.99333 25.24963  1.000 18.19198  ? 99  GLY   A N   1 
ATOM   632  C  CA  . GLY   A 1 100 ? 2.13316   22.19583 25.54277  1.000 18.63429  ? 99  GLY   A CA  1 
ATOM   633  C  C   . GLY   A 1 100 ? 2.36577   20.73766 25.21009  1.000 19.20764  ? 99  GLY   A C   1 
ATOM   634  O  O   . GLY   A 1 100 ? 3.46865   20.33758 24.83622  1.000 19.78812  ? 99  GLY   A O   1 
ATOM   635  N  N   . VAL   A 1 101 ? 1.30138   19.94153 25.33736  1.000 16.96609  ? 100 VAL   A N   1 
ATOM   636  C  CA  . VAL   A 1 101 ? 1.37625   18.49861 25.11151  1.000 16.80164  ? 100 VAL   A CA  1 
ATOM   637  C  C   . VAL   A 1 101 ? 0.35187   18.11826 24.06240  1.000 17.70473  ? 100 VAL   A C   1 
ATOM   638  O  O   . VAL   A 1 101 ? -0.81612  18.50553 24.17534  1.000 17.30360  ? 100 VAL   A O   1 
ATOM   639  C  CB  . VAL   A 1 101 ? 1.11469   17.71186 26.40822  1.000 17.72488  ? 100 VAL   A CB  1 
ATOM   640  C  CG1 . VAL   A 1 101 ? 1.12318   16.18921 26.10622  1.000 18.49037  ? 100 VAL   A CG1 1 
ATOM   641  C  CG2 . VAL   A 1 101 ? 2.15829   18.07070 27.43746  1.000 20.52388  ? 100 VAL   A CG2 1 
ATOM   642  N  N   . PHE   A 1 102 ? 0.77728   17.34174 23.05815  1.000 16.51991  ? 101 PHE   A N   1 
ATOM   643  C  CA  . PHE   A 1 102 ? -0.15764  16.73432 22.11469  1.000 16.43418  ? 101 PHE   A CA  1 
ATOM   644  C  C   . PHE   A 1 102 ? -0.34505  15.26709 22.46920  1.000 17.80424  ? 101 PHE   A C   1 
ATOM   645  O  O   . PHE   A 1 102 ? 0.62579   14.55442 22.74916  1.000 17.97960  ? 101 PHE   A O   1 
ATOM   646  C  CB  . PHE   A 1 102 ? 0.33115   16.89110 20.66364  1.000 14.80633  ? 101 PHE   A CB  1 
ATOM   647  C  CG  . PHE   A 1 102 ? 0.22545   18.28673 20.17627  1.000 16.30392  ? 101 PHE   A CG  1 
ATOM   648  C  CD1 . PHE   A 1 102 ? -0.97229  18.75766 19.64876  1.000 20.74380  ? 101 PHE   A CD1 1 
ATOM   649  C  CD2 . PHE   A 1 102 ? 1.30102   19.14916 20.28647  1.000 17.47477  ? 101 PHE   A CD2 1 
ATOM   650  C  CE1 . PHE   A 1 102 ? -1.08897  20.06890 19.23150  1.000 20.82884  ? 101 PHE   A CE1 1 
ATOM   651  C  CE2 . PHE   A 1 102 ? 1.18427   20.48474 19.88267  1.000 22.04445  ? 101 PHE   A CE2 1 
ATOM   652  C  CZ  . PHE   A 1 102 ? -0.00890  20.93104 19.34612  1.000 21.12735  ? 101 PHE   A CZ  1 
ATOM   653  N  N   . LEU   A 1 103 ? -1.59605  14.82134 22.47697  1.000 18.85742  ? 102 LEU   A N   1 
ATOM   654  C  CA  . LEU   A 1 103 ? -1.93534  13.45879 22.86713  1.000 18.26179  ? 102 LEU   A CA  1 
ATOM   655  C  C   . LEU   A 1 103 ? -2.63078  12.76258 21.70435  1.000 20.22351  ? 102 LEU   A C   1 
ATOM   656  O  O   . LEU   A 1 103 ? -3.71117  13.18838 21.28207  1.000 19.66974  ? 102 LEU   A O   1 
ATOM   657  C  CB  . LEU   A 1 103 ? -2.82579  13.45424 24.10333  1.000 18.94826  ? 102 LEU   A CB  1 
ATOM   658  C  CG  . LEU   A 1 103 ? -2.13121  14.17957 25.26968  1.000 18.12694  ? 102 LEU   A CG  1 
ATOM   659  C  CD1 . LEU   A 1 103 ? -2.66911  15.60652 25.41207  1.000 18.90721  ? 102 LEU   A CD1 1 
ATOM   660  C  CD2 . LEU   A 1 103 ? -2.29208  13.38947 26.58349  1.000 23.96728  ? 102 LEU   A CD2 1 
ATOM   661  N  N   . LEU   A 1 104 ? -1.99499  11.70834 21.18531  1.000 21.46520  ? 103 LEU   A N   1 
ATOM   662  C  CA  . LEU   A 1 104 ? -2.44336  11.00785 19.97944  1.000 20.86038  ? 103 LEU   A CA  1 
ATOM   663  C  C   . LEU   A 1 104 ? -3.14470  9.71875  20.37554  1.000 19.30827  ? 103 LEU   A C   1 
ATOM   664  O  O   . LEU   A 1 104 ? -2.59793  8.93440  21.15282  1.000 21.94601  ? 103 LEU   A O   1 
ATOM   665  C  CB  . LEU   A 1 104 ? -1.25602  10.66785 19.07168  1.000 18.81285  ? 103 LEU   A CB  1 
ATOM   666  C  CG  . LEU   A 1 104 ? -0.72064  11.80004 18.18954  1.000 22.62473  ? 103 LEU   A CG  1 
ATOM   667  C  CD1 . LEU   A 1 104 ? -0.05529  12.83685 19.09835  1.000 25.63396  ? 103 LEU   A CD1 1 
ATOM   668  C  CD2 . LEU   A 1 104 ? 0.30362   11.24821 17.20204  1.000 24.00363  ? 103 LEU   A CD2 1 
ATOM   669  N  N   . LYS   A 1 105 ? -4.34560  9.49643  19.84052  1.000 19.85247  ? 104 LYS   A N   1 
ATOM   670  C  CA  . LYS   A 1 105 ? -5.01062  8.23616  20.12363  1.000 25.39375  ? 104 LYS   A CA  1 
ATOM   671  C  C   . LYS   A 1 105 ? -4.42130  7.12588  19.25911  1.000 27.68115  ? 104 LYS   A C   1 
ATOM   672  O  O   . LYS   A 1 105 ? -3.61579  7.36964  18.35540  1.000 24.63754  ? 104 LYS   A O   1 
ATOM   673  C  CB  . LYS   A 1 105 ? -6.52275  8.37880  19.91931  1.000 25.47323  ? 104 LYS   A CB  1 
ATOM   674  C  CG  . LYS   A 1 105 ? -7.15528  9.40800  20.85534  1.000 26.84704  ? 104 LYS   A CG  1 
ATOM   675  C  CD  . LYS   A 1 105 ? -8.63729  9.60300  20.57665  1.000 26.44715  ? 104 LYS   A CD  1 
ATOM   676  C  CE  . LYS   A 1 105 ? -9.28290  10.49497 21.60477  1.000 27.31282  ? 104 LYS   A CE  1 
ATOM   677  N  NZ  . LYS   A 1 105 ? -8.89960  11.93131 21.45895  1.000 29.82163  ? 104 LYS   A NZ  1 
ATOM   678  N  N   . SER   A 1 106 ? -4.79377  5.87488  19.57507  1.000 27.48213  ? 105 SER   A N   1 
ATOM   679  C  CA  . SER   A 1 106 ? -4.28248  4.73869  18.80827  1.000 26.92355  ? 105 SER   A CA  1 
ATOM   680  C  C   . SER   A 1 106 ? -4.56593  4.89814  17.32242  1.000 25.06308  ? 105 SER   A C   1 
ATOM   681  O  O   . SER   A 1 106 ? -5.65699  5.30508  16.92296  1.000 28.49975  ? 105 SER   A O   1 
ATOM   682  C  CB  . SER   A 1 106 ? -4.90852  3.42136  19.28831  1.000 30.42491  ? 105 SER   A CB  1 
ATOM   683  O  OG  . SER   A 1 106 ? -4.63464  3.19678  20.64229  1.000 38.61368  ? 105 SER   A OG  1 
ATOM   684  N  N   . GLY   A 1 107 ? -3.57120  4.56449  16.50143  1.000 29.30390  ? 106 GLY   A N   1 
ATOM   685  C  CA  . GLY   A 1 107 ? -3.74823  4.54860  15.06686  1.000 29.54008  ? 106 GLY   A CA  1 
ATOM   686  C  C   . GLY   A 1 107 ? -3.83660  5.90352  14.41507  1.000 30.29288  ? 106 GLY   A C   1 
ATOM   687  O  O   . GLY   A 1 107 ? -4.16390  5.98052  13.22808  1.000 34.13937  ? 106 GLY   A O   1 
ATOM   688  N  N   . THR   A 1 108 ? -3.55845  6.97923  15.14183  1.000 25.33846  ? 107 THR   A N   1 
ATOM   689  C  CA  . THR   A 1 108 ? -3.71139  8.30448  14.57004  1.000 23.44384  ? 107 THR   A CA  1 
ATOM   690  C  C   . THR   A 1 108 ? -2.35701  8.85459  14.15486  1.000 25.14744  ? 107 THR   A C   1 
ATOM   691  O  O   . THR   A 1 108 ? -1.29631  8.37804  14.56342  1.000 24.97501  ? 107 THR   A O   1 
ATOM   692  C  CB  . THR   A 1 108 ? -4.38046  9.27866  15.54667  1.000 25.33973  ? 107 THR   A CB  1 
ATOM   693  O  OG1 . THR   A 1 108 ? -3.54576  9.46890  16.70095  1.000 24.87117  ? 107 THR   A OG1 1 
ATOM   694  C  CG2 . THR   A 1 108 ? -5.73641  8.73291  16.00290  1.000 28.57276  ? 107 THR   A CG2 1 
ATOM   695  N  N   . SER   A 1 109 ? -2.42087  9.88314  13.33397  1.000 28.76168  ? 108 SER   A N   1 
ATOM   696  C  CA  A SER   A 1 109 ? -1.24365  10.57641 12.84958  0.509 25.02976  ? 108 SER   A CA  1 
ATOM   697  C  CA  B SER   A 1 109 ? -1.23927  10.58062 12.86203  0.491 25.03544  ? 108 SER   A CA  1 
ATOM   698  C  C   . SER   A 1 109 ? -1.54901  12.06303 12.84175  1.000 27.71995  ? 108 SER   A C   1 
ATOM   699  O  O   . SER   A 1 109 ? -2.68706  12.46600 12.60120  1.000 25.31561  ? 108 SER   A O   1 
ATOM   700  C  CB  A SER   A 1 109 ? -0.86929  10.07350 11.44446  0.509 27.88959  ? 108 SER   A CB  1 
ATOM   701  C  CB  B SER   A 1 109 ? -0.82262  10.12814 11.45335  0.491 27.88174  ? 108 SER   A CB  1 
ATOM   702  O  OG  A SER   A 1 109 ? -0.16126  11.04014 10.69735  0.509 33.58941  ? 108 SER   A OG  1 
ATOM   703  O  OG  B SER   A 1 109 ? -0.45017  8.76125  11.42080  0.491 28.29721  ? 108 SER   A OG  1 
ATOM   704  N  N   . ILE   A 1 110 ? -0.53739  12.87695 13.11536  1.000 20.84451  ? 109 ILE   A N   1 
ATOM   705  C  CA  . ILE   A 1 110 ? -0.57150  14.28840 12.75533  1.000 18.99939  ? 109 ILE   A CA  1 
ATOM   706  C  C   . ILE   A 1 110 ? 0.04738   14.39807 11.36385  1.000 19.94363  ? 109 ILE   A C   1 
ATOM   707  O  O   . ILE   A 1 110 ? 1.22394   14.05716 11.20166  1.000 20.73267  ? 109 ILE   A O   1 
ATOM   708  C  CB  . ILE   A 1 110 ? 0.18093   15.17249 13.75282  1.000 19.48765  ? 109 ILE   A CB  1 
ATOM   709  C  CG1 . ILE   A 1 110 ? -0.43995  15.05854 15.15164  1.000 19.36834  ? 109 ILE   A CG1 1 
ATOM   710  C  CG2 . ILE   A 1 110 ? 0.11848   16.63004 13.28617  1.000 21.51838  ? 109 ILE   A CG2 1 
ATOM   711  C  CD1 . ILE   A 1 110 ? 0.42555   15.76261 16.20449  1.000 20.54929  ? 109 ILE   A CD1 1 
ATOM   712  N  N   . PRO   A 1 111 ? -0.70827  14.81241 10.35124  1.000 20.95088  ? 110 PRO   A N   1 
ATOM   713  C  CA  . PRO   A 1 111 ? -0.18312  14.84567 8.98043   1.000 25.40294  ? 110 PRO   A CA  1 
ATOM   714  C  C   . PRO   A 1 111 ? 0.99332   15.79254 8.80975   1.000 24.61275  ? 110 PRO   A C   1 
ATOM   715  O  O   . PRO   A 1 111 ? 1.16331   16.76901 9.52967   1.000 21.53657  ? 110 PRO   A O   1 
ATOM   716  C  CB  . PRO   A 1 111 ? -1.38335  15.32751 8.15161   1.000 23.77365  ? 110 PRO   A CB  1 
ATOM   717  C  CG  . PRO   A 1 111 ? -2.57912  14.95972 8.98100   1.000 27.09022  ? 110 PRO   A CG  1 
ATOM   718  C  CD  . PRO   A 1 111 ? -2.12934  15.15860 10.41466  1.000 23.21911  ? 110 PRO   A CD  1 
ATOM   719  N  N   . LEU   A 1 112 ? 1.77718   15.50691 7.77174   1.000 22.92886  ? 111 LEU   A N   1 
ATOM   720  C  CA  . LEU   A 1 112 ? 2.95424   16.28139 7.40622   1.000 21.90741  ? 111 LEU   A CA  1 
ATOM   721  C  C   . LEU   A 1 112 ? 2.66156   17.77716 7.34653   1.000 20.29213  ? 111 LEU   A C   1 
ATOM   722  O  O   . LEU   A 1 112 ? 1.74490   18.21238 6.64021   1.000 21.06611  ? 111 LEU   A O   1 
ATOM   723  C  CB  . LEU   A 1 112 ? 3.42546   15.78057 6.02850   1.000 21.54303  ? 111 LEU   A CB  1 
ATOM   724  C  CG  . LEU   A 1 112 ? 4.71981   16.35637 5.49286   1.000 22.69893  ? 111 LEU   A CG  1 
ATOM   725  C  CD1 . LEU   A 1 112 ? 5.84628   16.07920 6.45202   1.000 25.17586  ? 111 LEU   A CD1 1 
ATOM   726  C  CD2 . LEU   A 1 112 ? 4.97620   15.74048 4.08461   1.000 24.05677  ? 111 LEU   A CD2 1 
ATOM   727  N  N   . HIS   A 1 113 ? 3.45666   18.57342 8.07303   1.000 19.95894  ? 112 HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 113 ? 3.22946   20.01505 8.13653   1.000 22.11598  ? 112 HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 113 ? 4.54816   20.73201 8.36201   1.000 22.06712  ? 112 HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 113 ? 5.51496   20.14238 8.84874   1.000 22.05364  ? 112 HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 113 ? 2.23968   20.38367 9.25607   1.000 18.50298  ? 112 HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 113 ? 2.68979   19.95211 10.63026  1.000 18.72892  ? 112 HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 113 ? 2.45498   18.68972 11.12446  1.000 17.92376  ? 112 HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 113 ? 3.35903   20.61521 11.60266  1.000 20.51458  ? 112 HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 113 ? 2.95255   18.59078 12.34934  1.000 18.80280  ? 112 HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 113 ? 3.50984   19.74642 12.66396  1.000 18.16030  ? 112 HIS   A NE2 1 
ATOM   737  N  N   . ASP   A 1 114 ? 4.56805   22.02809 8.03960   1.000 21.33654  ? 113 ASP   A N   1 
ATOM   738  C  CA  . ASP   A 1 114 ? 5.75235   22.85468 8.20283   1.000 21.72334  ? 113 ASP   A CA  1 
ATOM   739  C  C   . ASP   A 1 114 ? 5.58556   23.82114 9.37580   1.000 20.72276  ? 113 ASP   A C   1 
ATOM   740  O  O   . ASP   A 1 114 ? 4.54443   23.86399 10.04844  1.000 23.86300  ? 113 ASP   A O   1 
ATOM   741  C  CB  . ASP   A 1 114 ? 6.10567   23.59189 6.90033   1.000 21.68844  ? 113 ASP   A CB  1 
ATOM   742  C  CG  . ASP   A 1 114 ? 5.06324   24.62415 6.46710   1.000 29.85567  ? 113 ASP   A CG  1 
ATOM   743  O  OD1 . ASP   A 1 114 ? 4.08013   24.87616 7.18729   1.000 27.06187  ? 113 ASP   A OD1 1 
ATOM   744  O  OD2 . ASP   A 1 114 ? 5.23555   25.18935 5.35426   1.000 35.30669  ? 113 ASP   A OD2 1 
ATOM   745  N  N   . HIS   A 1 115 ? 6.66422   24.54947 9.65662   1.000 20.92284  ? 114 HIS   A N   1 
ATOM   746  C  CA  . HIS   A 1 115 ? 6.74168   25.48189 10.78620  1.000 20.29836  ? 114 HIS   A CA  1 
ATOM   747  C  C   . HIS   A 1 115 ? 7.53551   26.69611 10.33420  1.000 21.83141  ? 114 HIS   A C   1 
ATOM   748  O  O   . HIS   A 1 115 ? 8.70198   26.87569 10.70048  1.000 23.52184  ? 114 HIS   A O   1 
ATOM   749  C  CB  . HIS   A 1 115 ? 7.39907   24.82541 12.00801  1.000 19.37997  ? 114 HIS   A CB  1 
ATOM   750  C  CG  . HIS   A 1 115 ? 6.89582   23.44573 12.31540  1.000 19.13957  ? 114 HIS   A CG  1 
ATOM   751  N  ND1 . HIS   A 1 115 ? 7.28153   22.32922 11.59996  1.000 18.30215  ? 114 HIS   A ND1 1 
ATOM   752  C  CD2 . HIS   A 1 115 ? 6.05766   23.00251 13.28404  1.000 20.11853  ? 114 HIS   A CD2 1 
ATOM   753  C  CE1 . HIS   A 1 115 ? 6.68504   21.26014 12.10778  1.000 21.04812  ? 114 HIS   A CE1 1 
ATOM   754  N  NE2 . HIS   A 1 115 ? 5.94358   21.64272 13.13866  1.000 17.65075  ? 114 HIS   A NE2 1 
ATOM   755  N  N   . PRO   A 1 116 ? 6.92826   27.55683 9.52242   1.000 22.73352  ? 115 PRO   A N   1 
ATOM   756  C  CA  . PRO   A 1 116 ? 7.71714   28.54147 8.76229   1.000 26.25198  ? 115 PRO   A CA  1 
ATOM   757  C  C   . PRO   A 1 116 ? 8.46153   29.51412 9.66278   1.000 24.75665  ? 115 PRO   A C   1 
ATOM   758  O  O   . PRO   A 1 116 ? 7.86583   30.22336 10.47761  1.000 28.21512  ? 115 PRO   A O   1 
ATOM   759  C  CB  . PRO   A 1 116 ? 6.65664   29.25816 7.91695   1.000 27.86447  ? 115 PRO   A CB  1 
ATOM   760  C  CG  . PRO   A 1 116 ? 5.54701   28.26313 7.77623   1.000 27.69718  ? 115 PRO   A CG  1 
ATOM   761  C  CD  . PRO   A 1 116 ? 5.51337   27.53880 9.11262   1.000 22.47857  ? 115 PRO   A CD  1 
ATOM   762  N  N   . GLY   A 1 117 ? 9.77737   29.56449 9.48724   1.000 25.98579  ? 116 GLY   A N   1 
ATOM   763  C  CA  . GLY   A 1 117 ? 10.57310  30.49440 10.25317  1.000 31.93476  ? 116 GLY   A CA  1 
ATOM   764  C  C   . GLY   A 1 117 ? 10.63426  30.17558 11.72189  1.000 30.31131  ? 116 GLY   A C   1 
ATOM   765  O  O   . GLY   A 1 117 ? 10.97560  31.04543 12.52734  1.000 29.17798  ? 116 GLY   A O   1 
ATOM   766  N  N   . MET   A 1 118 ? 10.31684  28.94239 12.09905  1.000 27.32777  ? 117 MET   A N   1 
ATOM   767  C  CA  . MET   A 1 118 ? 10.24218  28.57791 13.50547  1.000 24.91895  ? 117 MET   A CA  1 
ATOM   768  C  C   . MET   A 1 118 ? 11.22269  27.47271 13.86563  1.000 23.97003  ? 117 MET   A C   1 
ATOM   769  O  O   . MET   A 1 118 ? 11.61413  26.65614 13.02363  1.000 24.74191  ? 117 MET   A O   1 
ATOM   770  C  CB  . MET   A 1 118 ? 8.82151   28.13702 13.91170  1.000 24.47851  ? 117 MET   A CB  1 
ATOM   771  C  CG  . MET   A 1 118 ? 7.72713   29.15896 13.62898  1.000 25.74710  ? 117 MET   A CG  1 
ATOM   772  S  SD  . MET   A 1 118 ? 6.15139   28.41005 13.18358  1.000 26.47367  ? 117 MET   A SD  1 
ATOM   773  C  CE  . MET   A 1 118 ? 5.69172   27.58872 14.72931  1.000 25.11007  ? 117 MET   A CE  1 
ATOM   774  N  N   . HIS   A 1 119 ? 11.60685  27.47396 15.14384  1.000 24.41791  ? 118 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 119 ? 12.26907  26.36276 15.80839  1.000 23.34150  ? 118 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 119 ? 11.22416  25.53195 16.54062  1.000 23.04910  ? 118 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 119 ? 10.17886  26.04042 16.94708  1.000 24.29140  ? 118 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 119 ? 13.30855  26.86870 16.81347  1.000 24.82381  ? 118 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 119 ? 14.45184  27.59386 16.18343  1.000 31.62435  ? 118 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 119 ? 15.71308  27.04930 16.09064  1.000 35.22873  ? 118 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 119 ? 14.52941  28.82498 15.62604  1.000 32.40183  ? 118 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 119 ? 16.51788  27.90615 15.48850  1.000 36.50523  ? 118 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 119 ? 15.82517  28.99392 15.20063  1.000 39.17751  ? 118 HIS   A NE2 1 
ATOM   784  N  N   . GLY   A 1 120 ? 11.51317  24.25412 16.73220  1.000 21.70637  ? 119 GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 120 ? 10.61144  23.40443 17.49722  1.000 19.53967  ? 119 GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 120 ? 11.42152  22.38075 18.25766  1.000 23.77164  ? 119 GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 120 ? 12.51081  21.98785 17.82904  1.000 23.62888  ? 119 GLY   A O   1 
ATOM   788  N  N   . MET   A 1 121 ? 10.90361  21.96726 19.41679  1.000 21.29763  ? 120 MET   A N   1 
ATOM   789  C  CA  A MET   A 1 121 ? 11.53086  20.91715 20.21295  0.626 21.12553  ? 120 MET   A CA  1 
ATOM   790  C  CA  B MET   A 1 121 ? 11.52426  20.89481 20.17958  0.374 21.25815  ? 120 MET   A CA  1 
ATOM   791  C  C   . MET   A 1 121 ? 10.43231  19.99701 20.72035  1.000 26.91713  ? 120 MET   A C   1 
ATOM   792  O  O   . MET   A 1 121 ? 9.42595   20.47705 21.24235  1.000 31.50468  ? 120 MET   A O   1 
ATOM   793  C  CB  A MET   A 1 121 ? 12.32754  21.50279 21.38934  0.626 26.41396  ? 120 MET   A CB  1 
ATOM   794  C  CB  B MET   A 1 121 ? 12.36046  21.43543 21.33243  0.374 26.35904  ? 120 MET   A CB  1 
ATOM   795  C  CG  A MET   A 1 121 ? 13.34658  20.53247 21.97499  0.626 23.42168  ? 120 MET   A CG  1 
ATOM   796  C  CG  B MET   A 1 121 ? 13.35195  22.46716 20.92339  0.374 22.26471  ? 120 MET   A CG  1 
ATOM   797  S  SD  A MET   A 1 121 ? 14.34680  21.18898 23.34275  0.626 29.68624  ? 120 MET   A SD  1 
ATOM   798  S  SD  B MET   A 1 121 ? 13.87441  23.28179 22.41288  0.374 29.65282  ? 120 MET   A SD  1 
ATOM   799  C  CE  A MET   A 1 121 ? 15.34883  22.41129 22.50586  0.626 29.36186  ? 120 MET   A CE  1 
ATOM   800  C  CE  B MET   A 1 121 ? 15.17870  22.18623 22.94994  0.374 29.48972  ? 120 MET   A CE  1 
ATOM   801  N  N   . LEU   A 1 122 ? 10.61901  18.69573 20.58446  1.000 18.41626  ? 121 LEU   A N   1 
ATOM   802  C  CA  A LEU   A 1 122 ? 9.61588   17.69661 20.92850  0.589 21.32863  ? 121 LEU   A CA  1 
ATOM   803  C  CA  B LEU   A 1 122 ? 9.60011   17.78122 21.05815  0.411 21.32194  ? 121 LEU   A CA  1 
ATOM   804  C  C   . LEU   A 1 122 ? 10.22765  16.68095 21.88976  1.000 22.46136  ? 121 LEU   A C   1 
ATOM   805  O  O   . LEU   A 1 122 ? 11.37628  16.29435 21.69990  1.000 25.45034  ? 121 LEU   A O   1 
ATOM   806  C  CB  A LEU   A 1 122 ? 9.15629   17.02534 19.63276  0.589 23.50207  ? 121 LEU   A CB  1 
ATOM   807  C  CB  B LEU   A 1 122 ? 8.77789   17.20714 19.91210  0.411 24.14095  ? 121 LEU   A CB  1 
ATOM   808  C  CG  A LEU   A 1 122 ? 8.00131   16.04935 19.52418  0.589 26.50746  ? 121 LEU   A CG  1 
ATOM   809  C  CG  B LEU   A 1 122 ? 9.39476   16.15443 19.00940  0.411 21.29503  ? 121 LEU   A CG  1 
ATOM   810  C  CD1 A LEU   A 1 122 ? 7.52545   16.06920 18.05965  0.589 18.88433  ? 121 LEU   A CD1 1 
ATOM   811  C  CD1 B LEU   A 1 122 ? 9.13906   14.75564 19.50659  0.411 21.25727  ? 121 LEU   A CD1 1 
ATOM   812  C  CD2 A LEU   A 1 122 ? 8.39384   14.64565 19.97350  0.589 23.24378  ? 121 LEU   A CD2 1 
ATOM   813  C  CD2 B LEU   A 1 122 ? 8.75755   16.34404 17.64076  0.411 25.37239  ? 121 LEU   A CD2 1 
ATOM   814  N  N   . LYS   A 1 123 ? 9.46415   16.22042 22.88000  1.000 18.55812  ? 122 LYS   A N   1 
ATOM   815  C  CA  A LYS   A 1 123 ? 9.93107   15.17224 23.78386  0.343 17.67214  ? 122 LYS   A CA  1 
ATOM   816  C  CA  B LYS   A 1 123 ? 9.93366   15.16772 23.77681  0.657 17.47515  ? 122 LYS   A CA  1 
ATOM   817  C  C   . LYS   A 1 123 ? 8.79335   14.18810 23.99772  1.000 21.56245  ? 122 LYS   A C   1 
ATOM   818  O  O   . LYS   A 1 123 ? 7.72666   14.57493 24.48710  1.000 19.80488  ? 122 LYS   A O   1 
ATOM   819  C  CB  A LYS   A 1 123 ? 10.40033  15.75527 25.12404  0.343 21.35984  ? 122 LYS   A CB  1 
ATOM   820  C  CB  B LYS   A 1 123 ? 10.41734  15.75000 25.11386  0.657 21.29076  ? 122 LYS   A CB  1 
ATOM   821  C  CG  A LYS   A 1 123 ? 10.68047  14.70435 26.19419  0.343 24.94790  ? 122 LYS   A CG  1 
ATOM   822  C  CG  B LYS   A 1 123 ? 10.69988  14.70256 26.18829  0.657 24.99303  ? 122 LYS   A CG  1 
ATOM   823  C  CD  A LYS   A 1 123 ? 12.02293  14.03475 25.95348  0.343 26.84751  ? 122 LYS   A CD  1 
ATOM   824  C  CD  B LYS   A 1 123 ? 11.97691  13.94764 25.87265  0.657 26.86642  ? 122 LYS   A CD  1 
ATOM   825  C  CE  A LYS   A 1 123 ? 12.31186  12.99200 27.02667  0.343 29.82694  ? 122 LYS   A CE  1 
ATOM   826  C  CE  B LYS   A 1 123 ? 12.06573  12.68405 26.72364  0.657 30.53095  ? 122 LYS   A CE  1 
ATOM   827  N  NZ  A LYS   A 1 123 ? 11.32782  11.87149 26.99166  0.343 27.86450  ? 122 LYS   A NZ  1 
ATOM   828  N  NZ  B LYS   A 1 123 ? 12.17975  13.01236 28.17055  0.657 27.77819  ? 122 LYS   A NZ  1 
ATOM   829  N  N   . VAL   A 1 124 ? 9.01292   12.92382 23.63463  1.000 19.93005  ? 123 VAL   A N   1 
ATOM   830  C  CA  . VAL   A 1 124 ? 7.96963   11.91753 23.81799  1.000 21.00417  ? 123 VAL   A CA  1 
ATOM   831  C  C   . VAL   A 1 124 ? 7.77574   11.65177 25.30186  1.000 24.53620  ? 123 VAL   A C   1 
ATOM   832  O  O   . VAL   A 1 124 ? 8.75015   11.48379 26.05052  1.000 24.64259  ? 123 VAL   A O   1 
ATOM   833  C  CB  . VAL   A 1 124 ? 8.33066   10.62844 23.06624  1.000 22.30120  ? 123 VAL   A CB  1 
ATOM   834  C  CG1 . VAL   A 1 124 ? 7.26668   9.53558  23.32416  1.000 21.81767  ? 123 VAL   A CG1 1 
ATOM   835  C  CG2 . VAL   A 1 124 ? 8.49095   10.92371 21.57679  1.000 20.63946  ? 123 VAL   A CG2 1 
ATOM   836  N  N   . LEU   A 1 125 ? 6.51139   11.60886 25.73721  1.000 18.85864  ? 124 LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 125 ? 6.16290   11.38568 27.13728  1.000 21.99888  ? 124 LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 125 ? 5.74925   9.95126  27.43361  1.000 26.29430  ? 124 LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 125 ? 6.12670   9.41056  28.47770  1.000 25.62896  ? 124 LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 125 ? 5.03255   12.32250 27.56616  1.000 24.94373  ? 124 LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 125 ? 5.37098   13.80697 27.45381  1.000 23.42862  ? 124 LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 125 ? 4.13558   14.64019 27.78334  1.000 23.89854  ? 124 LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 125 ? 6.48381   14.13192 28.42358  1.000 24.26976  ? 124 LEU   A CD2 1 
ATOM   844  N  N   . TYR   A 1 126 ? 4.95044   9.33848  26.56172  1.000 22.68170  ? 125 TYR   A N   1 
ATOM   845  C  CA  . TYR   A 1 126 ? 4.66328   7.91598  26.64423  1.000 24.14437  ? 125 TYR   A CA  1 
ATOM   846  C  C   . TYR   A 1 126 ? 4.36146   7.41610  25.24707  1.000 26.20637  ? 125 TYR   A C   1 
ATOM   847  O  O   . TYR   A 1 126 ? 4.05084   8.19350  24.33771  1.000 21.63814  ? 125 TYR   A O   1 
ATOM   848  C  CB  . TYR   A 1 126 ? 3.48900   7.59350  27.58866  1.000 22.07151  ? 125 TYR   A CB  1 
ATOM   849  C  CG  . TYR   A 1 126 ? 2.16243   8.24281  27.23335  1.000 21.12502  ? 125 TYR   A CG  1 
ATOM   850  C  CD1 . TYR   A 1 126 ? 1.32962   7.69297  26.26574  1.000 23.23339  ? 125 TYR   A CD1 1 
ATOM   851  C  CD2 . TYR   A 1 126 ? 1.74549   9.39961  27.88136  1.000 21.11298  ? 125 TYR   A CD2 1 
ATOM   852  C  CE1 . TYR   A 1 126 ? 0.13257   8.28481  25.93970  1.000 23.16938  ? 125 TYR   A CE1 1 
ATOM   853  C  CE2 . TYR   A 1 126 ? 0.54947   9.99654  27.57897  1.000 21.51635  ? 125 TYR   A CE2 1 
ATOM   854  C  CZ  . TYR   A 1 126 ? -0.25354  9.43853  26.59829  1.000 21.46448  ? 125 TYR   A CZ  1 
ATOM   855  O  OH  . TYR   A 1 126 ? -1.43039  10.04228 26.27425  1.000 23.04360  ? 125 TYR   A OH  1 
ATOM   856  N  N   . GLY   A 1 127 ? 4.41743   6.10136  25.09053  1.000 25.84253  ? 126 GLY   A N   1 
ATOM   857  C  CA  . GLY   A 1 127 ? 4.15115   5.54847  23.78124  1.000 22.19364  ? 126 GLY   A CA  1 
ATOM   858  C  C   . GLY   A 1 127 ? 5.35075   5.68430  22.86217  1.000 22.75328  ? 126 GLY   A C   1 
ATOM   859  O  O   . GLY   A 1 127 ? 6.46635   6.05586  23.26249  1.000 26.97208  ? 126 GLY   A O   1 
ATOM   860  N  N   . THR   A 1 128 ? 5.09872   5.36524  21.59779  1.000 22.81542  ? 127 THR   A N   1 
ATOM   861  C  CA  . THR   A 1 128 ? 6.08378   5.42700  20.52188  1.000 23.34030  ? 127 THR   A CA  1 
ATOM   862  C  C   . THR   A 1 128 ? 5.50952   6.24318  19.37447  1.000 24.47666  ? 127 THR   A C   1 
ATOM   863  O  O   . THR   A 1 128 ? 4.36408   6.02014  18.96903  1.000 23.95343  ? 127 THR   A O   1 
ATOM   864  C  CB  . THR   A 1 128 ? 6.41795   4.01936  20.00310  1.000 29.89805  ? 127 THR   A CB  1 
ATOM   865  O  OG1 . THR   A 1 128 ? 6.87828   3.21040  21.08620  1.000 32.43572  ? 127 THR   A OG1 1 
ATOM   866  C  CG2 . THR   A 1 128 ? 7.50345   4.07068  18.89772  1.000 29.09100  ? 127 THR   A CG2 1 
ATOM   867  N  N   . VAL   A 1 129 ? 6.30395   7.16015  18.81853  1.000 22.97069  ? 128 VAL   A N   1 
ATOM   868  C  CA  . VAL   A 1 129 ? 5.90109   7.87150  17.60958  1.000 21.02545  ? 128 VAL   A CA  1 
ATOM   869  C  C   . VAL   A 1 129 ? 6.93997   7.64728  16.52549  1.000 24.26073  ? 128 VAL   A C   1 
ATOM   870  O  O   . VAL   A 1 129 ? 8.14293   7.58206  16.80443  1.000 27.36311  ? 128 VAL   A O   1 
ATOM   871  C  CB  . VAL   A 1 129 ? 5.69012   9.38756  17.81744  1.000 22.28511  ? 128 VAL   A CB  1 
ATOM   872  C  CG1 . VAL   A 1 129 ? 4.45926   9.65451  18.73593  1.000 28.28852  ? 128 VAL   A CG1 1 
ATOM   873  C  CG2 . VAL   A 1 129 ? 6.93551   10.03033 18.36654  1.000 23.45782  ? 128 VAL   A CG2 1 
ATOM   874  N  N   . ARG   A 1 130 ? 6.46715   7.54774  15.28766  1.000 23.67023  ? 129 ARG   A N   1 
ATOM   875  C  CA  . ARG   A 1 130 ? 7.33301   7.62094  14.11725  1.000 22.20208  ? 129 ARG   A CA  1 
ATOM   876  C  C   . ARG   A 1 130 ? 7.33679   9.05701  13.62826  1.000 23.87828  ? 129 ARG   A C   1 
ATOM   877  O  O   . ARG   A 1 130 ? 6.27921   9.60191  13.29569  1.000 24.42557  ? 129 ARG   A O   1 
ATOM   878  C  CB  . ARG   A 1 130 ? 6.84625   6.68905  13.00694  1.000 25.64778  ? 129 ARG   A CB  1 
ATOM   879  C  CG  . ARG   A 1 130 ? 7.72651   6.73087  11.76064  1.000 30.33890  ? 129 ARG   A CG  1 
ATOM   880  C  CD  . ARG   A 1 130 ? 7.16958   5.86141  10.64747  1.000 33.52029  ? 129 ARG   A CD  1 
ATOM   881  N  NE  . ARG   A 1 130 ? 6.92709   4.50459  11.11808  1.000 39.46853  ? 129 ARG   A NE  1 
ATOM   882  C  CZ  . ARG   A 1 130 ? 5.72429   3.99166  11.34654  1.000 43.12406  ? 129 ARG   A CZ  1 
ATOM   883  N  NH1 . ARG   A 1 130 ? 4.62108   4.69070  11.12700  1.000 35.95172  ? 129 ARG   A NH1 1 
ATOM   884  N  NH2 . ARG   A 1 130 ? 5.62634   2.75264  11.82791  1.000 41.20586  ? 129 ARG   A NH2 1 
ATOM   885  N  N   . ILE   A 1 131 ? 8.50363   9.68980  13.60115  1.000 21.44478  ? 130 ILE   A N   1 
ATOM   886  C  CA  . ILE   A 1 131 ? 8.59055   11.05247 13.09428  1.000 20.42745  ? 130 ILE   A CA  1 
ATOM   887  C  C   . ILE   A 1 131 ? 9.32910   10.98852 11.76905  1.000 24.64292  ? 130 ILE   A C   1 
ATOM   888  O  O   . ILE   A 1 131 ? 10.47346  10.52818 11.72022  1.000 23.47285  ? 130 ILE   A O   1 
ATOM   889  C  CB  . ILE   A 1 131 ? 9.29858   11.98934 14.07849  1.000 22.01202  ? 130 ILE   A CB  1 
ATOM   890  C  CG1 . ILE   A 1 131 ? 8.55657   11.97400 15.42831  1.000 24.01976  ? 130 ILE   A CG1 1 
ATOM   891  C  CG2 . ILE   A 1 131 ? 9.28951   13.40596 13.51103  1.000 24.02397  ? 130 ILE   A CG2 1 
ATOM   892  C  CD1 . ILE   A 1 131 ? 9.27475   12.74798 16.53174  1.000 22.56963  ? 130 ILE   A CD1 1 
ATOM   893  N  N   . SER   A 1 132 ? 8.67576   11.44802 10.71299  1.000 22.28857  ? 131 SER   A N   1 
ATOM   894  C  CA  . SER   A 1 132 ? 9.28396   11.59749 9.39537   1.000 24.26002  ? 131 SER   A CA  1 
ATOM   895  C  C   . SER   A 1 132 ? 9.65549   13.05920 9.20097   1.000 26.55887  ? 131 SER   A C   1 
ATOM   896  O  O   . SER   A 1 132 ? 8.80178   13.93639 9.34080   1.000 26.48805  ? 131 SER   A O   1 
ATOM   897  C  CB  . SER   A 1 132 ? 8.31642   11.13167 8.30841   1.000 25.11218  ? 131 SER   A CB  1 
ATOM   898  O  OG  . SER   A 1 132 ? 7.93601   9.77007  8.53938   1.000 28.31008  ? 131 SER   A OG  1 
ATOM   899  N  N   . CYS   A 1 133 ? 10.92307  13.31841 8.88050   1.000 26.37891  ? 132 CYS   A N   1 
ATOM   900  C  CA  . CYS   A 1 133 ? 11.48062  14.66726 8.84611   1.000 22.55241  ? 132 CYS   A CA  1 
ATOM   901  C  C   . CYS   A 1 133 ? 11.87029  15.03217 7.42450   1.000 28.09703  ? 132 CYS   A C   1 
ATOM   902  O  O   . CYS   A 1 133 ? 12.56848  14.26130 6.75378   1.000 27.36023  ? 132 CYS   A O   1 
ATOM   903  C  CB  . CYS   A 1 133 ? 12.70335  14.75894 9.75017   1.000 23.20677  ? 132 CYS   A CB  1 
ATOM   904  S  SG  . CYS   A 1 133 ? 12.28584  14.35886 11.48177  1.000 29.39127  ? 132 CYS   A SG  1 
ATOM   905  N  N   . MET   A 1 134 ? 11.45724  16.21893 6.97869   1.000 24.12682  ? 133 MET   A N   1 
ATOM   906  C  CA  . MET   A 1 134 ? 11.61134  16.56570 5.56894   1.000 25.08523  ? 133 MET   A CA  1 
ATOM   907  C  C   . MET   A 1 134 ? 11.86850  18.05480 5.46178   1.000 26.38981  ? 133 MET   A C   1 
ATOM   908  O  O   . MET   A 1 134 ? 11.65856  18.80455 6.41841   1.000 24.29304  ? 133 MET   A O   1 
ATOM   909  C  CB  . MET   A 1 134 ? 10.33689  16.21425 4.79600   1.000 25.17072  ? 133 MET   A CB  1 
ATOM   910  C  CG  . MET   A 1 134 ? 10.00262  14.77743 4.85164   1.000 33.46280  ? 133 MET   A CG  1 
ATOM   911  S  SD  . MET   A 1 134 ? 8.57592   14.42416 3.84716   1.000 32.00761  ? 133 MET   A SD  1 
ATOM   912  C  CE  . MET   A 1 134 ? 7.97826   12.97662 4.72010   1.000 36.58077  ? 133 MET   A CE  1 
ATOM   913  N  N   . ASP   A 1 135 ? 12.31458  18.48505 4.27960   1.000 23.76127  ? 134 ASP   A N   1 
ATOM   914  C  CA  . ASP   A 1 135 ? 12.47042  19.90021 4.00045   1.000 24.96873  ? 134 ASP   A CA  1 
ATOM   915  C  C   . ASP   A 1 135 ? 12.09871  20.17089 2.55460   1.000 24.20997  ? 134 ASP   A C   1 
ATOM   916  O  O   . ASP   A 1 135 ? 12.24985  19.30832 1.68898   1.000 29.04132  ? 134 ASP   A O   1 
ATOM   917  C  CB  . ASP   A 1 135 ? 13.90013  20.38789 4.23426   1.000 29.26884  ? 134 ASP   A CB  1 
ATOM   918  C  CG  . ASP   A 1 135 ? 14.21934  20.56018 5.70061   1.000 27.94677  ? 134 ASP   A CG  1 
ATOM   919  O  OD1 . ASP   A 1 135 ? 13.64394  21.46535 6.35319   1.000 27.62953  ? 134 ASP   A OD1 1 
ATOM   920  O  OD2 . ASP   A 1 135 ? 15.05980  19.77769 6.19275   1.000 27.87931  ? 134 ASP   A OD2 1 
ATOM   921  N  N   . LYS   A 1 136 ? 11.61845  21.38011 2.30913   1.000 27.93011  ? 135 LYS   A N   1 
ATOM   922  C  CA  . LYS   A 1 136 ? 11.39595  21.83129 0.94460   1.000 32.47796  ? 135 LYS   A CA  1 
ATOM   923  C  C   . LYS   A 1 136 ? 12.72944  22.25338 0.34844   1.000 38.13599  ? 135 LYS   A C   1 
ATOM   924  O  O   . LYS   A 1 136 ? 13.57412  22.83158 1.03508   1.000 34.95074  ? 135 LYS   A O   1 
ATOM   925  C  CB  . LYS   A 1 136 ? 10.38342  22.97799 0.94422   1.000 36.27276  ? 135 LYS   A CB  1 
ATOM   926  C  CG  . LYS   A 1 136 ? 8.95671   22.45718 0.91408   1.000 42.66285  ? 135 LYS   A CG  1 
ATOM   927  C  CD  . LYS   A 1 136 ? 7.88035   23.49530 1.24096   1.000 50.46076  ? 135 LYS   A CD  1 
ATOM   928  C  CE  . LYS   A 1 136 ? 8.40762   24.91208 1.30199   1.000 45.46566  ? 135 LYS   A CE  1 
ATOM   929  N  NZ  . LYS   A 1 136 ? 7.32735   25.86926 1.69172   1.000 46.28685  ? 135 LYS   A NZ  1 
ATOM   930  N  N   . LEU   A 1 137 ? 12.94843  21.92264 -0.92126  1.000 33.72301  ? 136 LEU   A N   1 
ATOM   931  C  CA  . LEU   A 1 137 ? 14.18240  22.29849 -1.59721  1.000 44.82462  ? 136 LEU   A CA  1 
ATOM   932  C  C   . LEU   A 1 137 ? 13.93367  23.58239 -2.37918  1.000 54.85359  ? 136 LEU   A C   1 
ATOM   933  O  O   . LEU   A 1 137 ? 13.11252  23.60117 -3.30001  1.000 61.48971  ? 136 LEU   A O   1 
ATOM   934  C  CB  . LEU   A 1 137 ? 14.67336  21.17825 -2.51277  1.000 41.24682  ? 136 LEU   A CB  1 
ATOM   935  C  CG  . LEU   A 1 137 ? 15.04420  19.88066 -1.79289  1.000 39.55542  ? 136 LEU   A CG  1 
ATOM   936  C  CD1 . LEU   A 1 137 ? 15.48879  18.82252 -2.78213  1.000 48.38364  ? 136 LEU   A CD1 1 
ATOM   937  C  CD2 . LEU   A 1 137 ? 16.12361  20.14159 -0.76152  1.000 44.81454  ? 136 LEU   A CD2 1 
ATOM   938  N  N   . ASP   A 1 138 ? 14.62194  24.65419 -2.00047  1.000 65.12950  ? 137 ASP   A N   1 
ATOM   939  C  CA  . ASP   A 1 138 ? 14.44208  25.93246 -2.67965  1.000 75.74358  ? 137 ASP   A CA  1 
ATOM   940  C  C   . ASP   A 1 138 ? 15.73082  26.35283 -3.37517  1.000 80.17279  ? 137 ASP   A C   1 
ATOM   941  O  O   . ASP   A 1 138 ? 15.78519  27.40019 -4.01621  1.000 90.91352  ? 137 ASP   A O   1 
ATOM   942  C  CB  . ASP   A 1 138 ? 13.99130  27.01838 -1.69435  1.000 86.30942  ? 137 ASP   A CB  1 
ATOM   943  C  CG  . ASP   A 1 138 ? 14.78673  27.00625 -0.39770  1.000 87.98927  ? 137 ASP   A CG  1 
ATOM   944  O  OD1 . ASP   A 1 138 ? 14.98405  25.91573 0.18127   1.000 84.04881  ? 137 ASP   A OD1 1 
ATOM   945  O  OD2 . ASP   A 1 138 ? 15.20599  28.09697 0.04772   1.000 89.94785  ? 137 ASP   A OD2 1 
ATOM   946  N  N   . ARG   A 1 146 ? 12.06206  24.23674 -8.30461  1.000 75.59641  ? 145 ARG   A N   1 
ATOM   947  C  CA  . ARG   A 1 146 ? 12.23728  23.40387 -9.48968  1.000 72.78248  ? 145 ARG   A CA  1 
ATOM   948  C  C   . ARG   A 1 146 ? 10.91566  22.82430 -9.98946  1.000 70.35517  ? 145 ARG   A C   1 
ATOM   949  O  O   . ARG   A 1 146 ? 9.96519   22.63386 -9.21819  1.000 53.84870  ? 145 ARG   A O   1 
ATOM   950  C  CB  . ARG   A 1 146 ? 13.22934  22.27178 -9.20993  1.000 74.11977  ? 145 ARG   A CB  1 
ATOM   951  C  CG  . ARG   A 1 146 ? 14.11529  21.94875 -10.39659 1.000 72.67802  ? 145 ARG   A CG  1 
ATOM   952  C  CD  . ARG   A 1 146 ? 15.21019  20.95192 -10.05534 1.000 78.43330  ? 145 ARG   A CD  1 
ATOM   953  N  NE  . ARG   A 1 146 ? 14.83688  19.99397 -9.02158  1.000 64.55479  ? 145 ARG   A NE  1 
ATOM   954  C  CZ  . ARG   A 1 146 ? 14.39224  18.76967 -9.27242  1.000 68.23749  ? 145 ARG   A CZ  1 
ATOM   955  N  NH1 . ARG   A 1 146 ? 14.15032  18.36244 -10.50968 1.000 66.85209  ? 145 ARG   A NH1 1 
ATOM   956  N  NH2 . ARG   A 1 146 ? 14.18508  17.93330 -8.25898  1.000 61.50880  ? 145 ARG   A NH2 1 
ATOM   957  N  N   . ALA   A 1 147 ? 10.87182  22.53818 -11.28908 1.000 65.43816  ? 146 ALA   A N   1 
ATOM   958  C  CA  . ALA   A 1 147 ? 9.66781   22.06672 -11.95634 1.000 50.62613  ? 146 ALA   A CA  1 
ATOM   959  C  C   . ALA   A 1 147 ? 9.64751   20.54469 -12.04297 1.000 46.55899  ? 146 ALA   A C   1 
ATOM   960  O  O   . ALA   A 1 147 ? 10.68606  19.90153 -12.23885 1.000 45.61407  ? 146 ALA   A O   1 
ATOM   961  C  CB  . ALA   A 1 147 ? 9.55798   22.66333 -13.36212 1.000 59.29027  ? 146 ALA   A CB  1 
ATOM   962  N  N   . LEU   A 1 148 ? 8.45586   19.97876 -11.89744 1.000 38.00484  ? 147 LEU   A N   1 
ATOM   963  C  CA  . LEU   A 1 148 ? 8.26835   18.54789 -12.11710 1.000 41.41157  ? 147 LEU   A CA  1 
ATOM   964  C  C   . LEU   A 1 148 ? 8.55793   18.20523 -13.57674 1.000 38.29894  ? 147 LEU   A C   1 
ATOM   965  O  O   . LEU   A 1 148 ? 8.01888   18.86407 -14.47369 1.000 41.84683  ? 147 LEU   A O   1 
ATOM   966  C  CB  . LEU   A 1 148 ? 6.83746   18.16282 -11.77442 1.000 38.25940  ? 147 LEU   A CB  1 
ATOM   967  C  CG  . LEU   A 1 148 ? 6.38160   16.74109 -12.06657 1.000 33.53433  ? 147 LEU   A CG  1 
ATOM   968  C  CD1 . LEU   A 1 148 ? 6.91157   15.82176 -10.96540 1.000 31.90035  ? 147 LEU   A CD1 1 
ATOM   969  C  CD2 . LEU   A 1 148 ? 4.86394   16.70143 -12.09546 1.000 32.33252  ? 147 LEU   A CD2 1 
ATOM   970  N  N   . PRO   A 1 149 ? 9.39123   17.20177 -13.85589 1.000 33.63679  ? 148 PRO   A N   1 
ATOM   971  C  CA  . PRO   A 1 149 ? 9.64159   16.80291 -15.25252 1.000 36.28701  ? 148 PRO   A CA  1 
ATOM   972  C  C   . PRO   A 1 149 ? 8.35330   16.37389 -15.92777 1.000 35.98786  ? 148 PRO   A C   1 
ATOM   973  O  O   . PRO   A 1 149 ? 7.51631   15.69769 -15.30601 1.000 32.92975  ? 148 PRO   A O   1 
ATOM   974  C  CB  . PRO   A 1 149 ? 10.60366  15.61230 -15.13141 1.000 41.03753  ? 148 PRO   A CB  1 
ATOM   975  C  CG  . PRO   A 1 149 ? 10.96011  15.49168 -13.67541 1.000 39.75523  ? 148 PRO   A CG  1 
ATOM   976  C  CD  . PRO   A 1 149 ? 10.36935  16.62914 -12.92095 1.000 41.66035  ? 148 PRO   A CD  1 
ATOM   977  N  N   . PRO   A 1 150 ? 8.18407   16.70651 -17.21186 1.000 35.78012  ? 149 PRO   A N   1 
ATOM   978  C  CA  . PRO   A 1 150 ? 6.89512   16.43561 -17.87867 1.000 34.09107  ? 149 PRO   A CA  1 
ATOM   979  C  C   . PRO   A 1 150 ? 6.43951   14.98656 -17.79997 1.000 36.32700  ? 149 PRO   A C   1 
ATOM   980  O  O   . PRO   A 1 150 ? 5.24075   14.73686 -17.61628 1.000 34.90454  ? 149 PRO   A O   1 
ATOM   981  C  CB  . PRO   A 1 150 ? 7.15437   16.85328 -19.33700 1.000 34.87502  ? 149 PRO   A CB  1 
ATOM   982  C  CG  . PRO   A 1 150 ? 8.32393   17.75859 -19.28542 1.000 43.63251  ? 149 PRO   A CG  1 
ATOM   983  C  CD  . PRO   A 1 150 ? 9.16383   17.33932 -18.10878 1.000 36.24349  ? 149 PRO   A CD  1 
ATOM   984  N  N   . GLU   A 1 151 ? 7.34758   14.01970 -17.96476 1.000 30.62343  ? 150 GLU   A N   1 
ATOM   985  C  CA  . GLU   A 1 151 ? 6.91423   12.62966 -18.05476 1.000 35.46287  ? 150 GLU   A CA  1 
ATOM   986  C  C   . GLU   A 1 151 ? 6.64718   12.00106 -16.69463 1.000 37.98643  ? 150 GLU   A C   1 
ATOM   987  O  O   . GLU   A 1 151 ? 6.08378   10.90070 -16.64559 1.000 42.10994  ? 150 GLU   A O   1 
ATOM   988  C  CB  . GLU   A 1 151 ? 7.95086   11.78933 -18.81110 1.000 41.21626  ? 150 GLU   A CB  1 
ATOM   989  N  N   . GLN   A 1 152 ? 7.01615   12.67481 -15.60797 1.000 37.09589  ? 151 GLN   A N   1 
ATOM   990  C  CA  . GLN   A 1 152 ? 6.84177   12.10024 -14.28023 1.000 41.14820  ? 151 GLN   A CA  1 
ATOM   991  C  C   . GLN   A 1 152 ? 5.37616   11.81161 -13.98658 1.000 45.43501  ? 151 GLN   A C   1 
ATOM   992  O  O   . GLN   A 1 152 ? 4.48507   12.60891 -14.29503 1.000 37.96566  ? 151 GLN   A O   1 
ATOM   993  C  CB  . GLN   A 1 152 ? 7.41916   13.02052 -13.21467 1.000 35.28909  ? 151 GLN   A CB  1 
ATOM   994  C  CG  . GLN   A 1 152 ? 7.59154   12.31897 -11.86541 1.000 49.33004  ? 151 GLN   A CG  1 
ATOM   995  C  CD  . GLN   A 1 152 ? 8.67679   11.26461 -11.89663 1.000 52.49886  ? 151 GLN   A CD  1 
ATOM   996  O  OE1 . GLN   A 1 152 ? 9.86707   11.57954 -11.89969 1.000 63.13325  ? 151 GLN   A OE1 1 
ATOM   997  N  NE2 . GLN   A 1 152 ? 8.26905   10.00011 -11.93876 1.000 60.30510  ? 151 GLN   A NE2 1 
ATOM   998  N  N   . GLN   A 1 153 ? 5.15205   10.64362 -13.39543 1.000 44.01964  ? 152 GLN   A N   1 
ATOM   999  C  CA  . GLN   A 1 153 ? 3.85504   10.07562 -13.07699 1.000 41.51664  ? 152 GLN   A CA  1 
ATOM   1000 C  C   . GLN   A 1 153 ? 3.84037   9.72889  -11.59400 1.000 39.25208  ? 152 GLN   A C   1 
ATOM   1001 O  O   . GLN   A 1 153 ? 4.88251   9.39362  -11.02834 1.000 45.26905  ? 152 GLN   A O   1 
ATOM   1002 C  CB  . GLN   A 1 153 ? 3.64446   8.80825  -13.87416 1.000 43.34837  ? 152 GLN   A CB  1 
ATOM   1003 C  CG  . GLN   A 1 153 ? 2.23683   8.39384  -14.11487 1.000 50.28102  ? 152 GLN   A CG  1 
ATOM   1004 C  CD  . GLN   A 1 153 ? 2.16460   7.50566  -15.33030 1.000 54.73603  ? 152 GLN   A CD  1 
ATOM   1005 O  OE1 . GLN   A 1 153 ? 1.20865   6.75878  -15.51578 1.000 65.28755  ? 152 GLN   A OE1 1 
ATOM   1006 N  NE2 . GLN   A 1 153 ? 3.21320   7.54490  -16.14795 1.000 58.06870  ? 152 GLN   A NE2 1 
ATOM   1007 N  N   . PHE   A 1 154 ? 2.66490   9.79444  -10.96561 1.000 36.51033  ? 153 PHE   A N   1 
ATOM   1008 C  CA  . PHE   A 1 154 ? 2.51601   9.41302  -9.56044  1.000 36.26761  ? 153 PHE   A CA  1 
ATOM   1009 C  C   . PHE   A 1 154 ? 1.34066   8.45762  -9.41217  1.000 45.86448  ? 153 PHE   A C   1 
ATOM   1010 O  O   . PHE   A 1 154 ? 0.50277   8.32207  -10.30950 1.000 45.60727  ? 153 PHE   A O   1 
ATOM   1011 C  CB  . PHE   A 1 154 ? 2.30483   10.63058 -8.64035  1.000 33.79168  ? 153 PHE   A CB  1 
ATOM   1012 C  CG  . PHE   A 1 154 ? 3.46031   11.59145 -8.62365  1.000 36.44162  ? 153 PHE   A CG  1 
ATOM   1013 C  CD1 . PHE   A 1 154 ? 4.58730   11.32843 -7.87260  1.000 33.54917  ? 153 PHE   A CD1 1 
ATOM   1014 C  CD2 . PHE   A 1 154 ? 3.43666   12.74202 -9.40782  1.000 43.43934  ? 153 PHE   A CD2 1 
ATOM   1015 C  CE1 . PHE   A 1 154 ? 5.64974   12.20686 -7.85952  1.000 38.48610  ? 153 PHE   A CE1 1 
ATOM   1016 C  CE2 . PHE   A 1 154 ? 4.50208   13.62504 -9.40275  1.000 38.06020  ? 153 PHE   A CE2 1 
ATOM   1017 C  CZ  . PHE   A 1 154 ? 5.61081   13.35438 -8.63297  1.000 36.52127  ? 153 PHE   A CZ  1 
ATOM   1018 N  N   . GLU   A 1 155 ? 1.27827   7.79001  -8.26094  1.000 44.72766  ? 154 GLU   A N   1 
ATOM   1019 C  CA  . GLU   A 1 155 ? 0.17763   6.88060  -7.96917  1.000 47.11901  ? 154 GLU   A CA  1 
ATOM   1020 C  C   . GLU   A 1 155 ? -0.33388  7.24346  -6.58271  1.000 49.58000  ? 154 GLU   A C   1 
ATOM   1021 O  O   . GLU   A 1 155 ? 0.42678   7.13434  -5.60013  1.000 47.96202  ? 154 GLU   A O   1 
ATOM   1022 C  CB  . GLU   A 1 155 ? 0.62506   5.41894  -8.03193  1.000 60.67158  ? 154 GLU   A CB  1 
ATOM   1023 C  CG  . GLU   A 1 155 ? -0.38415  4.48794  -8.69283  1.000 65.44794  ? 154 GLU   A CG  1 
ATOM   1024 C  CD  . GLU   A 1 155 ? -1.71077  4.43764  -7.96421  1.000 75.46953  ? 154 GLU   A CD  1 
ATOM   1025 O  OE1 . GLU   A 1 155 ? -1.73421  3.97687  -6.80425  1.000 82.40681  ? 154 GLU   A OE1 1 
ATOM   1026 O  OE2 . GLU   A 1 155 ? -2.73430  4.84403  -8.56296  1.000 81.06563  ? 154 GLU   A OE2 1 
ATOM   1027 N  N   . PRO   A 1 156 ? -1.58210  7.71058  -6.44361  1.000 46.95887  ? 155 PRO   A N   1 
ATOM   1028 C  CA  . PRO   A 1 156 ? -2.58783  7.95562  -7.49236  1.000 53.05786  ? 155 PRO   A CA  1 
ATOM   1029 C  C   . PRO   A 1 156 ? -2.19292  9.10406  -8.42000  1.000 50.27441  ? 155 PRO   A C   1 
ATOM   1030 O  O   . PRO   A 1 156 ? -1.37697  9.94996  -8.05224  1.000 45.03800  ? 155 PRO   A O   1 
ATOM   1031 C  CB  . PRO   A 1 156 ? -3.85235  8.28778  -6.68616  1.000 50.77728  ? 155 PRO   A CB  1 
ATOM   1032 C  CG  . PRO   A 1 156 ? -3.33773  8.84922  -5.39928  1.000 49.55740  ? 155 PRO   A CG  1 
ATOM   1033 C  CD  . PRO   A 1 156 ? -2.09780  8.05514  -5.10688  1.000 51.02139  ? 155 PRO   A CD  1 
ATOM   1034 N  N   . PRO   A 1 157 ? -2.74930  9.14257  -9.62839  1.000 47.43895  ? 156 PRO   A N   1 
ATOM   1035 C  CA  . PRO   A 1 157 ? -2.37755  10.20177 -10.57328 1.000 42.75839  ? 156 PRO   A CA  1 
ATOM   1036 C  C   . PRO   A 1 157 ? -2.80370  11.57398 -10.08182 1.000 39.40961  ? 156 PRO   A C   1 
ATOM   1037 O  O   . PRO   A 1 157 ? -3.78981  11.72997 -9.35707  1.000 41.97883  ? 156 PRO   A O   1 
ATOM   1038 C  CB  . PRO   A 1 157 ? -3.11442  9.82663  -11.86485 1.000 41.96898  ? 156 PRO   A CB  1 
ATOM   1039 C  CG  . PRO   A 1 157 ? -3.94237  8.63914  -11.56628 1.000 50.96576  ? 156 PRO   A CG  1 
ATOM   1040 C  CD  . PRO   A 1 157 ? -3.58538  8.09114  -10.23008 1.000 51.77972  ? 156 PRO   A CD  1 
ATOM   1041 N  N   . LEU   A 1 158 ? -2.04021  12.57931 -10.49567 1.000 36.58991  ? 157 LEU   A N   1 
ATOM   1042 C  CA  . LEU   A 1 158 ? -2.30678  13.95847 -10.12550 1.000 34.48239  ? 157 LEU   A CA  1 
ATOM   1043 C  C   . LEU   A 1 158 ? -3.25776  14.60524 -11.12293 1.000 31.44346  ? 157 LEU   A C   1 
ATOM   1044 O  O   . LEU   A 1 158 ? -3.25211  14.29273 -12.31938 1.000 36.77253  ? 157 LEU   A O   1 
ATOM   1045 C  CB  . LEU   A 1 158 ? -1.00457  14.76249 -10.07543 1.000 36.28697  ? 157 LEU   A CB  1 
ATOM   1046 C  CG  . LEU   A 1 158 ? 0.03025   14.40568 -9.01029  1.000 34.51636  ? 157 LEU   A CG  1 
ATOM   1047 C  CD1 . LEU   A 1 158 ? 1.13003   15.46588 -8.98082  1.000 33.35085  ? 157 LEU   A CD1 1 
ATOM   1048 C  CD2 . LEU   A 1 158 ? -0.62903  14.28092 -7.65577  1.000 35.51692  ? 157 LEU   A CD2 1 
ATOM   1049 N  N   . GLN   A 1 159 ? -4.07327  15.51671 -10.61768 1.000 36.09780  ? 158 GLN   A N   1 
ATOM   1050 C  CA  . GLN   A 1 159 ? -4.84025  16.37331 -11.49783 1.000 36.75196  ? 158 GLN   A CA  1 
ATOM   1051 C  C   . GLN   A 1 159 ? -3.96657  17.51918 -11.99826 1.000 32.08348  ? 158 GLN   A C   1 
ATOM   1052 O  O   . GLN   A 1 159 ? -2.89528  17.77953 -11.43834 1.000 29.80386  ? 158 GLN   A O   1 
ATOM   1053 C  CB  . GLN   A 1 159 ? -6.08068  16.88284 -10.76909 1.000 43.07721  ? 158 GLN   A CB  1 
ATOM   1054 C  CG  . GLN   A 1 159 ? -6.91538  15.75343 -10.23198 1.000 41.75564  ? 158 GLN   A CG  1 
ATOM   1055 C  CD  . GLN   A 1 159 ? -7.59961  15.00194 -11.37235 1.000 52.58696  ? 158 GLN   A CD  1 
ATOM   1056 O  OE1 . GLN   A 1 159 ? -8.06295  15.60590 -12.35186 1.000 53.46881  ? 158 GLN   A OE1 1 
ATOM   1057 N  NE2 . GLN   A 1 159 ? -7.65026  13.67883 -11.25974 1.000 52.54449  ? 158 GLN   A NE2 1 
ATOM   1058 N  N   . PRO   A 1 160 ? -4.38217  18.19370 -13.07388 1.000 30.83203  ? 159 PRO   A N   1 
ATOM   1059 C  CA  . PRO   A 1 160 ? -3.51485  19.22403 -13.67109 1.000 32.99720  ? 159 PRO   A CA  1 
ATOM   1060 C  C   . PRO   A 1 160 ? -3.07504  20.29527 -12.69696 1.000 32.89129  ? 159 PRO   A C   1 
ATOM   1061 O  O   . PRO   A 1 160 ? -1.90011  20.68271 -12.70181 1.000 33.61471  ? 159 PRO   A O   1 
ATOM   1062 C  CB  . PRO   A 1 160 ? -4.38802  19.81926 -14.78495 1.000 36.17248  ? 159 PRO   A CB  1 
ATOM   1063 C  CG  . PRO   A 1 160 ? -5.34559  18.76913 -15.12146 1.000 34.81545  ? 159 PRO   A CG  1 
ATOM   1064 C  CD  . PRO   A 1 160 ? -5.60652  17.98711 -13.87369 1.000 28.15303  ? 159 PRO   A CD  1 
ATOM   1065 N  N   . ARG   A 1 161 ? -3.98744  20.79414 -11.86228 1.000 33.14057  ? 160 ARG   A N   1 
ATOM   1066 C  CA  . ARG   A 1 161 ? -3.59858  21.81754 -10.89952 1.000 36.08495  ? 160 ARG   A CA  1 
ATOM   1067 C  C   . ARG   A 1 161 ? -2.57551  21.27979 -9.90848  1.000 35.19518  ? 160 ARG   A C   1 
ATOM   1068 O  O   . ARG   A 1 161 ? -1.67386  22.01295 -9.48283  1.000 34.23842  ? 160 ARG   A O   1 
ATOM   1069 C  CB  . ARG   A 1 161 ? -4.83940  22.35296 -10.17818 1.000 40.13008  ? 160 ARG   A CB  1 
ATOM   1070 C  CG  . ARG   A 1 161 ? -5.68794  23.32961 -11.01657 1.000 44.28526  ? 160 ARG   A CG  1 
ATOM   1071 C  CD  . ARG   A 1 161 ? -4.88867  24.54277 -11.51392 1.000 52.09322  ? 160 ARG   A CD  1 
ATOM   1072 N  NE  . ARG   A 1 161 ? -4.10093  24.26399 -12.71026 0.000 45.07297  ? 160 ARG   A NE  1 
ATOM   1073 C  CZ  . ARG   A 1 161 ? -4.59595  23.88147 -13.87944 0.000 43.86372  ? 160 ARG   A CZ  1 
ATOM   1074 N  NH1 . ARG   A 1 161 ? -5.90072  23.81798 -14.09460 0.717 44.91878  ? 160 ARG   A NH1 1 
ATOM   1075 N  NH2 . ARG   A 1 161 ? -3.75881  23.55216 -14.85823 1.000 48.06614  ? 160 ARG   A NH2 1 
ATOM   1076 N  N   . GLU   A 1 162 ? -2.66941  19.99385 -9.56338  1.000 28.59376  ? 161 GLU   A N   1 
ATOM   1077 C  CA  . GLU   A 1 162 ? -1.68369  19.40806 -8.66224  1.000 26.46214  ? 161 GLU   A CA  1 
ATOM   1078 C  C   . GLU   A 1 162 ? -0.32862  19.24948 -9.33279  1.000 30.37137  ? 161 GLU   A C   1 
ATOM   1079 O  O   . GLU   A 1 162 ? 0.70853   19.48064 -8.70263  1.000 28.99394  ? 161 GLU   A O   1 
ATOM   1080 C  CB  . GLU   A 1 162 ? -2.19725  18.07814 -8.13284  1.000 32.37300  ? 161 GLU   A CB  1 
ATOM   1081 C  CG  . GLU   A 1 162 ? -3.42113  18.24588 -7.24697  1.000 31.25049  ? 161 GLU   A CG  1 
ATOM   1082 C  CD  . GLU   A 1 162 ? -4.08667  16.93786 -6.93361  1.000 37.46423  ? 161 GLU   A CD  1 
ATOM   1083 O  OE1 . GLU   A 1 162 ? -3.97065  15.99557 -7.74160  1.000 36.88703  ? 161 GLU   A OE1 1 
ATOM   1084 O  OE2 . GLU   A 1 162 ? -4.72913  16.85198 -5.87668  1.000 43.27964  ? 161 GLU   A OE2 1 
ATOM   1085 N  N   . ARG   A 1 163 ? -0.30941  18.85090 -10.60660 1.000 27.14641  ? 162 ARG   A N   1 
ATOM   1086 C  CA  . ARG   A 1 163 ? 0.96318   18.74364 -11.30627 1.000 26.05713  ? 162 ARG   A CA  1 
ATOM   1087 C  C   . ARG   A 1 163 ? 1.68017   20.08641 -11.33832 1.000 31.90986  ? 162 ARG   A C   1 
ATOM   1088 O  O   . ARG   A 1 163 ? 2.91138   20.14278 -11.24687 1.000 32.44722  ? 162 ARG   A O   1 
ATOM   1089 C  CB  . ARG   A 1 163 ? 0.72027   18.20799 -12.72271 1.000 27.68253  ? 162 ARG   A CB  1 
ATOM   1090 C  CG  . ARG   A 1 163 ? 0.32261   16.73777 -12.72508 1.000 26.36733  ? 162 ARG   A CG  1 
ATOM   1091 C  CD  . ARG   A 1 163 ? 0.16918   16.19178 -14.14672 1.000 27.04927  ? 162 ARG   A CD  1 
ATOM   1092 N  NE  . ARG   A 1 163 ? 1.44852   16.13289 -14.84362 1.000 29.27355  ? 162 ARG   A NE  1 
ATOM   1093 C  CZ  . ARG   A 1 163 ? 2.34576   15.16385 -14.69661 1.000 32.27115  ? 162 ARG   A CZ  1 
ATOM   1094 N  NH1 . ARG   A 1 163 ? 2.14553   14.15258 -13.86057 1.000 30.85196  ? 162 ARG   A NH1 1 
ATOM   1095 N  NH2 . ARG   A 1 163 ? 3.49130   15.23782 -15.36498 1.000 30.67919  ? 162 ARG   A NH2 1 
ATOM   1096 N  N   . GLU   A 1 164 ? 0.91913   21.17809 -11.45678 1.000 29.33908  ? 163 GLU   A N   1 
ATOM   1097 C  CA  A GLU   A 1 164 ? 1.50397   22.51600 -11.46170 0.555 35.28986  ? 163 GLU   A CA  1 
ATOM   1098 C  CA  B GLU   A 1 164 ? 1.52383   22.50430 -11.46648 0.445 35.29812  ? 163 GLU   A CA  1 
ATOM   1099 C  C   . GLU   A 1 164 ? 2.10730   22.86795 -10.10543 1.000 35.04458  ? 163 GLU   A C   1 
ATOM   1100 O  O   . GLU   A 1 164 ? 3.12871   23.56270 -10.03706 1.000 35.46546  ? 163 GLU   A O   1 
ATOM   1101 C  CB  A GLU   A 1 164 ? 0.43423   23.55353 -11.81771 0.555 37.90451  ? 163 GLU   A CB  1 
ATOM   1102 C  CB  B GLU   A 1 164 ? 0.48417   23.54421 -11.88673 0.445 37.91675  ? 163 GLU   A CB  1 
ATOM   1103 C  CG  A GLU   A 1 164 ? 0.11264   23.78115 -13.30234 0.555 42.81108  ? 163 GLU   A CG  1 
ATOM   1104 C  CG  B GLU   A 1 164 ? 1.01655   24.96014 -12.00724 0.445 40.98904  ? 163 GLU   A CG  1 
ATOM   1105 C  CD  A GLU   A 1 164 ? 1.32053   24.02130 -14.18888 0.555 46.35883  ? 163 GLU   A CD  1 
ATOM   1106 C  CD  B GLU   A 1 164 ? -0.05034  25.94175 -12.45716 0.445 51.16575  ? 163 GLU   A CD  1 
ATOM   1107 O  OE1 A GLU   A 1 164 ? 2.23523   24.75702 -13.76930 0.555 50.14368  ? 163 GLU   A OE1 1 
ATOM   1108 O  OE1 B GLU   A 1 164 ? -1.21716  25.51979 -12.62929 0.445 48.66127  ? 163 GLU   A OE1 1 
ATOM   1109 O  OE2 A GLU   A 1 164 ? 1.30943   23.54317 -15.34707 0.555 45.25976  ? 163 GLU   A OE2 1 
ATOM   1110 O  OE2 B GLU   A 1 164 ? 0.28326   27.12910 -12.65995 0.445 54.96704  ? 163 GLU   A OE2 1 
ATOM   1111 N  N   . ALA   A 1 165 ? 1.49200   22.40122 -9.01960  1.000 31.56972  ? 164 ALA   A N   1 
ATOM   1112 C  CA  . ALA   A 1 165 ? 1.84222   22.85268 -7.67370  1.000 31.14057  ? 164 ALA   A CA  1 
ATOM   1113 C  C   . ALA   A 1 165 ? 2.90611   22.01834 -6.97265  1.000 35.23678  ? 164 ALA   A C   1 
ATOM   1114 O  O   . ALA   A 1 165 ? 3.41994   22.45448 -5.93330  1.000 33.06806  ? 164 ALA   A O   1 
ATOM   1115 C  CB  . ALA   A 1 165 ? 0.58828   22.87945 -6.78879  1.000 34.45778  ? 164 ALA   A CB  1 
ATOM   1116 N  N   . VAL   A 1 166 ? 3.24810   20.83201 -7.47142  1.000 30.23791  ? 165 VAL   A N   1 
ATOM   1117 C  CA  A VAL   A 1 166 ? 4.18329   19.99116 -6.73696  0.618 31.83996  ? 165 VAL   A CA  1 
ATOM   1118 C  CA  B VAL   A 1 166 ? 4.19441   19.98124 -6.75664  0.382 31.89985  ? 165 VAL   A CA  1 
ATOM   1119 C  C   . VAL   A 1 166 ? 5.58080   20.61275 -6.77255  1.000 33.90782  ? 165 VAL   A C   1 
ATOM   1120 O  O   . VAL   A 1 166 ? 5.98182   21.26420 -7.74926  1.000 35.26254  ? 165 VAL   A O   1 
ATOM   1121 C  CB  A VAL   A 1 166 ? 4.16904   18.55479 -7.29528  0.618 34.96176  ? 165 VAL   A CB  1 
ATOM   1122 C  CB  B VAL   A 1 166 ? 4.21717   18.56752 -7.35968  0.382 34.89618  ? 165 VAL   A CB  1 
ATOM   1123 C  CG1 A VAL   A 1 166 ? 4.86251   18.48434 -8.62523  0.618 34.36705  ? 165 VAL   A CG1 1 
ATOM   1124 C  CG1 B VAL   A 1 166 ? 2.91519   17.87002 -7.06705  0.382 35.28109  ? 165 VAL   A CG1 1 
ATOM   1125 C  CG2 A VAL   A 1 166 ? 4.77253   17.57474 -6.30087  0.618 31.73595  ? 165 VAL   A CG2 1 
ATOM   1126 C  CG2 B VAL   A 1 166 ? 4.44097   18.63336 -8.84338  0.382 33.54052  ? 165 VAL   A CG2 1 
ATOM   1127 N  N   . ARG   A 1 167 ? 6.32624   20.42072 -5.68584  1.000 29.52564  ? 166 ARG   A N   1 
ATOM   1128 C  CA  . ARG   A 1 167 ? 7.62719   21.03648 -5.47293  1.000 32.17460  ? 166 ARG   A CA  1 
ATOM   1129 C  C   . ARG   A 1 167 ? 8.58448   20.00945 -4.88944  1.000 33.21933  ? 166 ARG   A C   1 
ATOM   1130 O  O   . ARG   A 1 167 ? 8.15778   19.08477 -4.19221  1.000 30.81231  ? 166 ARG   A O   1 
ATOM   1131 C  CB  . ARG   A 1 167 ? 7.52925   22.24339 -4.52170  1.000 41.53010  ? 166 ARG   A CB  1 
ATOM   1132 C  CG  . ARG   A 1 167 ? 6.60479   23.36346 -4.99621  1.000 41.56564  ? 166 ARG   A CG  1 
ATOM   1133 C  CD  . ARG   A 1 167 ? 7.27641   24.25303 -6.03907  1.000 46.86257  ? 166 ARG   A CD  1 
ATOM   1134 N  NE  . ARG   A 1 167 ? 6.43989   25.36636 -6.47625  1.000 52.76277  ? 166 ARG   A NE  1 
ATOM   1135 C  CZ  . ARG   A 1 167 ? 5.55454   25.30260 -7.46532  1.000 51.50550  ? 166 ARG   A CZ  1 
ATOM   1136 N  NH1 . ARG   A 1 167 ? 5.31894   24.17312 -8.11500  1.000 48.48739  ? 166 ARG   A NH1 1 
ATOM   1137 N  NH2 . ARG   A 1 167 ? 4.89546   26.40162 -7.81808  1.000 50.05868  ? 166 ARG   A NH2 1 
ATOM   1138 N  N   . PRO   A 1 168 ? 9.87813   20.13747 -5.16638  1.000 30.52732  ? 167 PRO   A N   1 
ATOM   1139 C  CA  . PRO   A 1 168 ? 10.83824  19.15430 -4.66257  1.000 27.56683  ? 167 PRO   A CA  1 
ATOM   1140 C  C   . PRO   A 1 168 ? 11.12677  19.32738 -3.17957  1.000 23.96728  ? 167 PRO   A C   1 
ATOM   1141 O  O   . PRO   A 1 168 ? 11.15029  20.43546 -2.64591  1.000 30.62576  ? 167 PRO   A O   1 
ATOM   1142 C  CB  . PRO   A 1 168 ? 12.09609  19.43355 -5.49478  1.000 34.24704  ? 167 PRO   A CB  1 
ATOM   1143 C  CG  . PRO   A 1 168 ? 11.99317  20.89010 -5.81669  1.000 40.85322  ? 167 PRO   A CG  1 
ATOM   1144 C  CD  . PRO   A 1 168 ? 10.52541  21.18879 -5.97046  1.000 37.95909  ? 167 PRO   A CD  1 
ATOM   1145 N  N   . GLY   A 1 169 ? 11.39294  18.20053 -2.53547  1.000 27.34863  ? 168 GLY   A N   1 
ATOM   1146 C  CA  . GLY   A 1 169 ? 11.75241  18.18624 -1.13125  1.000 30.53747  ? 168 GLY   A CA  1 
ATOM   1147 C  C   . GLY   A 1 169 ? 12.76943  17.09598 -0.87929  1.000 34.18675  ? 168 GLY   A C   1 
ATOM   1148 O  O   . GLY   A 1 169 ? 13.13449  16.34930 -1.78482  1.000 29.64859  ? 168 GLY   A O   1 
ATOM   1149 N  N   . VAL   A 1 170 ? 13.24800  17.01524 0.35958   1.000 30.32268  ? 169 VAL   A N   1 
ATOM   1150 C  CA  . VAL   A 1 170 ? 14.16746  15.96049 0.76299   1.000 31.00859  ? 169 VAL   A CA  1 
ATOM   1151 C  C   . VAL   A 1 170 ? 13.62530  15.29357 2.01716   1.000 35.80215  ? 169 VAL   A C   1 
ATOM   1152 O  O   . VAL   A 1 170 ? 13.23470  15.97330 2.97640   1.000 27.17365  ? 169 VAL   A O   1 
ATOM   1153 C  CB  . VAL   A 1 170 ? 15.59751  16.49354 0.98641   1.000 36.18581  ? 169 VAL   A CB  1 
ATOM   1154 C  CG1 . VAL   A 1 170 ? 15.59724  17.70441 1.90236   1.000 30.32809  ? 169 VAL   A CG1 1 
ATOM   1155 C  CG2 . VAL   A 1 170 ? 16.48859  15.40200 1.52509   1.000 34.87574  ? 169 VAL   A CG2 1 
ATOM   1156 N  N   . LEU   A 1 171 ? 13.57244  13.96674 1.99597   1.000 31.07908  ? 170 LEU   A N   1 
ATOM   1157 C  CA  . LEU   A 1 171 ? 13.24402  13.17883 3.17885   1.000 29.86268  ? 170 LEU   A CA  1 
ATOM   1158 C  C   . LEU   A 1 171 ? 14.54777  12.90269 3.91773   1.000 36.31623  ? 170 LEU   A C   1 
ATOM   1159 O  O   . LEU   A 1 171 ? 15.42403  12.20025 3.40149   1.000 36.68019  ? 170 LEU   A O   1 
ATOM   1160 C  CB  . LEU   A 1 171 ? 12.52825  11.89126 2.78004   1.000 33.58804  ? 170 LEU   A CB  1 
ATOM   1161 C  CG  . LEU   A 1 171 ? 12.33694  10.80155 3.83284   1.000 34.38238  ? 170 LEU   A CG  1 
ATOM   1162 C  CD1 . LEU   A 1 171 ? 11.54730  11.32421 5.02252   1.000 37.02889  ? 170 LEU   A CD1 1 
ATOM   1163 C  CD2 . LEU   A 1 171 ? 11.63450  9.60525  3.21642   1.000 38.39312  ? 170 LEU   A CD2 1 
ATOM   1164 N  N   . ARG   A 1 172 ? 14.69282  13.47775 5.11278   1.000 27.97336  ? 171 ARG   A N   1 
ATOM   1165 C  CA  . ARG   A 1 172 ? 15.94946  13.39487 5.84694   1.000 30.14711  ? 171 ARG   A CA  1 
ATOM   1166 C  C   . ARG   A 1 172 ? 16.00154  12.20865 6.79938   1.000 35.86864  ? 171 ARG   A C   1 
ATOM   1167 O  O   . ARG   A 1 172 ? 17.04639  11.56376 6.91920   1.000 32.35289  ? 171 ARG   A O   1 
ATOM   1168 C  CB  . ARG   A 1 172 ? 16.20223  14.69875 6.60993   1.000 27.24801  ? 171 ARG   A CB  1 
ATOM   1169 C  CG  . ARG   A 1 172 ? 16.44846  15.89689 5.70028   1.000 29.17579  ? 171 ARG   A CG  1 
ATOM   1170 C  CD  . ARG   A 1 172 ? 17.07402  17.05638 6.45155   1.000 34.69566  ? 171 ARG   A CD  1 
ATOM   1171 N  NE  . ARG   A 1 172 ? 17.26373  18.23343 5.60797   1.000 32.59513  ? 171 ARG   A NE  1 
ATOM   1172 C  CZ  . ARG   A 1 172 ? 18.31145  18.41994 4.81449   1.000 38.70627  ? 171 ARG   A CZ  1 
ATOM   1173 N  NH1 . ARG   A 1 172 ? 19.26972  17.51348 4.71064   1.000 38.31922  ? 171 ARG   A NH1 1 
ATOM   1174 N  NH2 . ARG   A 1 172 ? 18.38850  19.53290 4.08922   1.000 35.91314  ? 171 ARG   A NH2 1 
ATOM   1175 N  N   . SER   A 1 173 ? 14.90169  11.88291 7.47229   1.000 33.35323  ? 172 SER   A N   1 
ATOM   1176 C  CA  . SER   A 1 173 ? 14.94335  10.77513 8.41537   1.000 33.40144  ? 172 SER   A CA  1 
ATOM   1177 C  C   . SER   A 1 173 ? 13.53268  10.28945 8.68837   1.000 31.14596  ? 172 SER   A C   1 
ATOM   1178 O  O   . SER   A 1 173 ? 12.54502  10.97181 8.39905   1.000 27.97150  ? 172 SER   A O   1 
ATOM   1179 C  CB  . SER   A 1 173 ? 15.63288  11.16734 9.72897   1.000 32.12289  ? 172 SER   A CB  1 
ATOM   1180 O  OG  . SER   A 1 173 ? 14.82832  12.08406 10.45451  1.000 32.13438  ? 172 SER   A OG  1 
ATOM   1181 N  N   . ARG   A 1 174 ? 13.46235  9.08056  9.24320   1.000 31.03996  ? 173 ARG   A N   1 
ATOM   1182 C  CA  . ARG   A 1 174 ? 12.18648  8.44378  9.53254   1.000 34.23632  ? 173 ARG   A CA  1 
ATOM   1183 C  C   . ARG   A 1 174 ? 12.50624  7.35923  10.55971  1.000 41.37501  ? 173 ARG   A C   1 
ATOM   1184 O  O   . ARG   A 1 174 ? 12.99952  6.28714  10.20125  1.000 45.69609  ? 173 ARG   A O   1 
ATOM   1185 C  CB  . ARG   A 1 174 ? 11.56021  7.89399  8.26621   1.000 40.57435  ? 173 ARG   A CB  1 
ATOM   1186 C  CG  . ARG   A 1 174 ? 10.21389  7.25457  8.41845   1.000 41.09885  ? 173 ARG   A CG  1 
ATOM   1187 C  CD  . ARG   A 1 174 ? 9.76600   6.67783  7.07772   1.000 43.94551  ? 173 ARG   A CD  1 
ATOM   1188 N  NE  . ARG   A 1 174 ? 8.78361   5.61821  7.24695   0.499 52.29003  ? 173 ARG   A NE  1 
ATOM   1189 C  CZ  . ARG   A 1 174 ? 9.08947   4.34029  7.41331   1.000 58.84965  ? 173 ARG   A CZ  1 
ATOM   1190 N  NH1 . ARG   A 1 174 ? 10.34724  3.92532  7.41742   1.000 60.55647  ? 173 ARG   A NH1 1 
ATOM   1191 N  NH2 . ARG   A 1 174 ? 8.11030   3.45802  7.58543   1.000 59.42735  ? 173 ARG   A NH2 1 
ATOM   1192 N  N   . ALA   A 1 175 ? 12.29633  7.68204  11.82899  1.000 30.28579  ? 174 ALA   A N   1 
ATOM   1193 C  CA  . ALA   A 1 175 ? 12.67370  6.81460  12.92886  1.000 26.96762  ? 174 ALA   A CA  1 
ATOM   1194 C  C   . ALA   A 1 175 ? 11.57271  6.83860  13.97469  1.000 30.19615  ? 174 ALA   A C   1 
ATOM   1195 O  O   . ALA   A 1 175 ? 10.68300  7.69207  13.95052  1.000 28.64921  ? 174 ALA   A O   1 
ATOM   1196 C  CB  . ALA   A 1 175 ? 14.00548  7.24426  13.55604  1.000 30.92842  ? 174 ALA   A CB  1 
ATOM   1197 N  N   . GLU   A 1 176 ? 11.64554  5.88690  14.89631  1.000 26.93731  ? 175 GLU   A N   1 
ATOM   1198 C  CA  . GLU   A 1 176 ? 10.71460  5.78422  16.01229  1.000 28.96987  ? 175 GLU   A CA  1 
ATOM   1199 C  C   . GLU   A 1 176 ? 11.36037  6.33397  17.27610  1.000 30.41732  ? 175 GLU   A C   1 
ATOM   1200 O  O   . GLU   A 1 176 ? 12.54554  6.09710  17.53619  1.000 29.69733  ? 175 GLU   A O   1 
ATOM   1201 C  CB  . GLU   A 1 176 ? 10.29474  4.32871  16.23605  1.000 30.77524  ? 175 GLU   A CB  1 
ATOM   1202 C  CG  . GLU   A 1 176 ? 9.52608   3.71689  15.07208  1.000 31.35751  ? 175 GLU   A CG  1 
ATOM   1203 C  CD  . GLU   A 1 176 ? 8.99516   2.31308  15.37534  1.000 36.06239  ? 175 GLU   A CD  1 
ATOM   1204 O  OE1 . GLU   A 1 176 ? 9.34642   1.74664  16.42870  1.000 41.79980  ? 175 GLU   A OE1 1 
ATOM   1205 O  OE2 . GLU   A 1 176 ? 8.22469   1.78000  14.55430  1.000 45.39720  ? 175 GLU   A OE2 1 
ATOM   1206 N  N   . TYR   A 1 177 ? 10.56656  7.05355  18.06901  1.000 25.72621  ? 176 TYR   A N   1 
ATOM   1207 C  CA  . TYR   A 1 177 ? 11.02943  7.72700  19.27153  1.000 24.37911  ? 176 TYR   A CA  1 
ATOM   1208 C  C   . TYR   A 1 177 ? 10.14193  7.35044  20.44787  1.000 25.06830  ? 176 TYR   A C   1 
ATOM   1209 O  O   . TYR   A 1 177 ? 8.92663   7.21519  20.29575  1.000 25.28305  ? 176 TYR   A O   1 
ATOM   1210 C  CB  . TYR   A 1 177 ? 11.02789  9.25839  19.06716  1.000 23.72081  ? 176 TYR   A CB  1 
ATOM   1211 C  CG  . TYR   A 1 177 ? 11.92254  9.68518  17.92374  1.000 26.31637  ? 176 TYR   A CG  1 
ATOM   1212 C  CD1 . TYR   A 1 177 ? 11.44899  9.70847  16.61055  1.000 25.49485  ? 176 TYR   A CD1 1 
ATOM   1213 C  CD2 . TYR   A 1 177 ? 13.25030  10.03018 18.14365  1.000 36.48597  ? 176 TYR   A CD2 1 
ATOM   1214 C  CE1 . TYR   A 1 177 ? 12.27241  10.08659 15.54917  1.000 29.81153  ? 176 TYR   A CE1 1 
ATOM   1215 C  CE2 . TYR   A 1 177 ? 14.07968  10.40954 17.08734  1.000 29.20859  ? 176 TYR   A CE2 1 
ATOM   1216 C  CZ  . TYR   A 1 177 ? 13.58697  10.43490 15.80173  1.000 30.39713  ? 176 TYR   A CZ  1 
ATOM   1217 O  OH  . TYR   A 1 177 ? 14.40969  10.80855 14.75790  1.000 32.87226  ? 176 TYR   A OH  1 
ATOM   1218 N  N   . THR   A 1 178 ? 10.75782  7.15277  21.61005  1.000 26.40292  ? 177 THR   A N   1 
ATOM   1219 C  CA  . THR   A 1 178 ? 10.05776  6.90672  22.87319  1.000 25.57589  ? 177 THR   A CA  1 
ATOM   1220 C  C   . THR   A 1 178 ? 10.55606  7.90116  23.91615  1.000 23.58485  ? 177 THR   A C   1 
ATOM   1221 O  O   . THR   A 1 178 ? 11.39543  8.76410  23.63270  1.000 28.59519  ? 177 THR   A O   1 
ATOM   1222 C  CB  . THR   A 1 178 ? 10.27625  5.47845  23.38618  1.000 34.11534  ? 177 THR   A CB  1 
ATOM   1223 O  OG1 . THR   A 1 178 ? 11.61623  5.36128  23.88944  1.000 34.29295  ? 177 THR   A OG1 1 
ATOM   1224 C  CG2 . THR   A 1 178 ? 10.04836  4.45443  22.27674  1.000 30.15665  ? 177 THR   A CG2 1 
ATOM   1225 N  N   . GLU   A 1 179 ? 10.03906  7.77018  25.14149  1.000 31.16085  ? 178 GLU   A N   1 
ATOM   1226 C  CA  . GLU   A 1 179 ? 10.45747  8.66394  26.21491  1.000 34.10350  ? 178 GLU   A CA  1 
ATOM   1227 C  C   . GLU   A 1 179 ? 11.94632  8.54289  26.50662  1.000 40.61374  ? 178 GLU   A C   1 
ATOM   1228 O  O   . GLU   A 1 179 ? 12.51651  9.43203  27.14753  1.000 44.11836  ? 178 GLU   A O   1 
ATOM   1229 C  CB  . GLU   A 1 179 ? 9.63804   8.39724  27.49238  1.000 32.46015  ? 178 GLU   A CB  1 
ATOM   1230 C  CG  . GLU   A 1 179 ? 9.69881   6.96920  28.07351  1.000 43.10739  ? 178 GLU   A CG  1 
ATOM   1231 C  CD  . GLU   A 1 179 ? 10.99125  6.66824  28.83290  0.000 44.86890  ? 178 GLU   A CD  1 
ATOM   1232 O  OE1 . GLU   A 1 179 ? 11.66240  7.61779  29.30115  1.000 53.78387  ? 178 GLU   A OE1 1 
ATOM   1233 O  OE2 . GLU   A 1 179 ? 11.34173  5.47612  28.95688  1.000 49.72148  ? 178 GLU   A OE2 1 
ATOM   1234 N  N   . ALA   A 1 180 ? 12.59070  7.47194  26.05137  1.000 36.55085  ? 179 ALA   A N   1 
ATOM   1235 C  CA  . ALA   A 1 180 ? 14.01557  7.30869  26.27838  1.000 34.89367  ? 179 ALA   A CA  1 
ATOM   1236 C  C   . ALA   A 1 180 ? 14.86916  7.94993  25.19716  1.000 36.21704  ? 179 ALA   A C   1 
ATOM   1237 O  O   . ALA   A 1 180 ? 16.09557  7.94641  25.32068  1.000 39.47419  ? 179 ALA   A O   1 
ATOM   1238 C  CB  . ALA   A 1 180 ? 14.36437  5.81667  26.38095  1.000 42.55753  ? 179 ALA   A CB  1 
ATOM   1239 N  N   . SER   A 1 181 ? 14.26140  8.50941  24.14693  1.000 34.72577  ? 180 SER   A N   1 
ATOM   1240 C  CA  . SER   A 1 181 ? 15.02538  8.98348  22.99969  1.000 32.95696  ? 180 SER   A CA  1 
ATOM   1241 C  C   . SER   A 1 181 ? 15.62404  10.37022 23.18603  1.000 35.85834  ? 180 SER   A C   1 
ATOM   1242 O  O   . SER   A 1 181 ? 16.49484  10.76378 22.40428  1.000 41.39501  ? 180 SER   A O   1 
ATOM   1243 C  CB  . SER   A 1 181 ? 14.14939  9.01677  21.74434  1.000 34.14092  ? 180 SER   A CB  1 
ATOM   1244 O  OG  . SER   A 1 181 ? 13.59580  7.74703  21.45471  1.000 32.74547  ? 180 SER   A OG  1 
ATOM   1245 N  N   . GLY   A 1 182 ? 15.16004  11.14459 24.14676  1.000 31.89767  ? 181 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 182 ? 15.61303  12.51175 24.21293  1.000 33.81445  ? 181 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 182 ? 14.92697  13.34850 23.15039  1.000 30.00613  ? 181 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 182 ? 14.29717  12.82619 22.22158  1.000 31.40799  ? 181 GLY   A O   1 
ATOM   1249 N  N   . PRO   A 1 183 ? 15.06227  14.66634 23.25442  1.000 26.19728  ? 182 PRO   A N   1 
ATOM   1250 C  CA  . PRO   A 1 183 ? 14.25714  15.55552 22.41474  1.000 24.82993  ? 182 PRO   A CA  1 
ATOM   1251 C  C   . PRO   A 1 183 ? 14.68229  15.58975 20.95743  1.000 30.18519  ? 182 PRO   A C   1 
ATOM   1252 O  O   . PRO   A 1 183 ? 15.84555  15.35666 20.59550  1.000 27.89205  ? 182 PRO   A O   1 
ATOM   1253 C  CB  . PRO   A 1 183 ? 14.44755  16.92537 23.06981  1.000 26.59384  ? 182 PRO   A CB  1 
ATOM   1254 C  CG  . PRO   A 1 183 ? 15.72831  16.82324 23.78671  1.000 33.64836  ? 182 PRO   A CG  1 
ATOM   1255 C  CD  . PRO   A 1 183 ? 15.80486  15.40872 24.28334  1.000 29.67371  ? 182 PRO   A CD  1 
ATOM   1256 N  N   . CYS   A 1 184 ? 13.69721  15.88856 20.11535  1.000 23.23323  ? 183 CYS   A N   1 
ATOM   1257 C  CA  . CYS   A 1 184 ? 13.89283  16.11486 18.68691  1.000 25.82337  ? 183 CYS   A CA  1 
ATOM   1258 C  C   . CYS   A 1 184 ? 13.74868  17.59801 18.40774  1.000 29.63350  ? 183 CYS   A C   1 
ATOM   1259 O  O   . CYS   A 1 184 ? 12.84917  18.24526 18.95141  1.000 27.80196  ? 183 CYS   A O   1 
ATOM   1260 C  CB  . CYS   A 1 184 ? 12.87148  15.35508 17.85475  1.000 30.73364  ? 183 CYS   A CB  1 
ATOM   1261 S  SG  . CYS   A 1 184 ? 13.04640  13.59956 18.06402  1.000 35.61097  ? 183 CYS   A SG  1 
ATOM   1262 N  N   . ILE   A 1 185 ? 14.62520  18.12304 17.55580  1.000 22.89204  ? 184 ILE   A N   1 
ATOM   1263 C  CA  . ILE   A 1 185 ? 14.70498  19.54863 17.25386  1.000 23.51985  ? 184 ILE   A CA  1 
ATOM   1264 C  C   . ILE   A 1 185 ? 14.36010  19.75170 15.79046  1.000 24.66901  ? 184 ILE   A C   1 
ATOM   1265 O  O   . ILE   A 1 185 ? 14.75642  18.94868 14.93987  1.000 26.32295  ? 184 ILE   A O   1 
ATOM   1266 C  CB  . ILE   A 1 185 ? 16.12496  20.09022 17.50778  1.000 32.05111  ? 184 ILE   A CB  1 
ATOM   1267 C  CG1 . ILE   A 1 185 ? 16.64944  19.56466 18.83261  1.000 45.38871  ? 184 ILE   A CG1 1 
ATOM   1268 C  CG2 . ILE   A 1 185 ? 16.16457  21.61893 17.41824  1.000 35.56066  ? 184 ILE   A CG2 1 
ATOM   1269 C  CD1 . ILE   A 1 185 ? 16.29646  20.41802 19.95360  1.000 42.29200  ? 184 ILE   A CD1 1 
ATOM   1270 N  N   . LEU   A 1 186 ? 13.68151  20.84982 15.48537  1.000 20.28458  ? 185 LEU   A N   1 
ATOM   1271 C  CA  . LEU   A 1 186 ? 13.56688  21.29791 14.10274  1.000 23.08879  ? 185 LEU   A CA  1 
ATOM   1272 C  C   . LEU   A 1 186 ? 13.87214  22.78522 14.07345  1.000 23.67383  ? 185 LEU   A C   1 
ATOM   1273 O  O   . LEU   A 1 186 ? 13.77362  23.47589 15.09071  1.000 23.76927  ? 185 LEU   A O   1 
ATOM   1274 C  CB  . LEU   A 1 186 ? 12.16910  20.99438 13.49857  1.000 23.85787  ? 185 LEU   A CB  1 
ATOM   1275 C  CG  . LEU   A 1 186 ? 10.96504  21.70275 14.11522  1.000 24.50098  ? 185 LEU   A CG  1 
ATOM   1276 C  CD1 . LEU   A 1 186 ? 10.70796  23.08134 13.49191  1.000 22.80436  ? 185 LEU   A CD1 1 
ATOM   1277 C  CD2 . LEU   A 1 186 ? 9.72990   20.84545 13.95574  1.000 25.35177  ? 185 LEU   A CD2 1 
ATOM   1278 N  N   . THR   A 1 187 ? 14.27806  23.27854 12.91220  1.000 21.85314  ? 186 THR   A N   1 
ATOM   1279 C  CA  . THR   A 1 187 ? 14.68634  24.66651 12.75484  1.000 21.37353  ? 186 THR   A CA  1 
ATOM   1280 C  C   . THR   A 1 187 ? 14.06061  25.21851 11.48735  1.000 24.15618  ? 186 THR   A C   1 
ATOM   1281 O  O   . THR   A 1 187 ? 13.41434  24.48560 10.72961  1.000 24.15351  ? 186 THR   A O   1 
ATOM   1282 C  CB  . THR   A 1 187 ? 16.22010  24.77373 12.69320  1.000 30.51476  ? 186 THR   A CB  1 
ATOM   1283 O  OG1 . THR   A 1 187 ? 16.67187  24.26770 11.43541  1.000 30.22280  ? 186 THR   A OG1 1 
ATOM   1284 C  CG2 . THR   A 1 187 ? 16.86823  23.98587 13.83499  1.000 31.83149  ? 186 THR   A CG2 1 
ATOM   1285 N  N   . PRO   A 1 188 ? 14.20413  26.52453 11.23064  1.000 24.66242  ? 187 PRO   A N   1 
ATOM   1286 C  CA  . PRO   A 1 188 ? 13.52992  27.07857 10.04961  1.000 28.55847  ? 187 PRO   A CA  1 
ATOM   1287 C  C   . PRO   A 1 188 ? 13.98935  26.43843 8.76150   1.000 29.65539  ? 187 PRO   A C   1 
ATOM   1288 O  O   . PRO   A 1 188 ? 13.19046  26.32155 7.82288   1.000 30.91274  ? 187 PRO   A O   1 
ATOM   1289 C  CB  . PRO   A 1 188 ? 13.88176  28.57153 10.11295  1.000 27.75791  ? 187 PRO   A CB  1 
ATOM   1290 C  CG  . PRO   A 1 188 ? 14.05089  28.83653 11.56152  1.000 33.09643  ? 187 PRO   A CG  1 
ATOM   1291 C  CD  . PRO   A 1 188 ? 14.71161  27.59996 12.11125  1.000 28.68870  ? 187 PRO   A CD  1 
ATOM   1292 N  N   . HIS   A 1 189 ? 15.23727  25.96836 8.70590   1.000 30.08436  ? 188 HIS   A N   1 
ATOM   1293 C  CA  . HIS   A 1 189 ? 15.80479  25.42831 7.47703   1.000 32.59843  ? 188 HIS   A CA  1 
ATOM   1294 C  C   . HIS   A 1 189 ? 16.18276  23.95632 7.56076   1.000 33.11210  ? 188 HIS   A C   1 
ATOM   1295 O  O   . HIS   A 1 189 ? 16.80768  23.44656 6.62642   1.000 33.87827  ? 188 HIS   A O   1 
ATOM   1296 C  CB  . HIS   A 1 189 ? 17.03534  26.24369 7.07312   1.000 33.30154  ? 188 HIS   A CB  1 
ATOM   1297 C  CG  . HIS   A 1 189 ? 16.74402  27.69544 6.89331   1.000 41.90129  ? 188 HIS   A CG  1 
ATOM   1298 N  ND1 . HIS   A 1 189 ? 15.93891  28.16873 5.87916   1.000 50.15952  ? 188 HIS   A ND1 1 
ATOM   1299 C  CD2 . HIS   A 1 189 ? 17.12485  28.77788 7.61088   1.000 46.80078  ? 188 HIS   A CD2 1 
ATOM   1300 C  CE1 . HIS   A 1 189 ? 15.84625  29.48302 5.97298   1.000 51.73653  ? 188 HIS   A CE1 1 
ATOM   1301 N  NE2 . HIS   A 1 189 ? 16.55597  29.87788 7.01542   1.000 55.59565  ? 188 HIS   A NE2 1 
ATOM   1302 N  N   . ARG   A 1 190 ? 15.84536  23.25013 8.63886   1.000 28.16709  ? 189 ARG   A N   1 
ATOM   1303 C  CA  . ARG   A 1 190 ? 16.19830  21.83602 8.66011   1.000 27.33774  ? 189 ARG   A CA  1 
ATOM   1304 C  C   . ARG   A 1 190 ? 15.17774  21.04088 9.44463   1.000 27.24163  ? 189 ARG   A C   1 
ATOM   1305 O  O   . ARG   A 1 190 ? 14.84966  21.40974 10.57404  1.000 26.47302  ? 189 ARG   A O   1 
ATOM   1306 C  CB  . ARG   A 1 190 ? 17.58396  21.61258 9.26301   1.000 32.79488  ? 189 ARG   A CB  1 
ATOM   1307 C  CG  . ARG   A 1 190 ? 18.16724  20.26938 8.86437   1.000 36.35139  ? 189 ARG   A CG  1 
ATOM   1308 C  CD  . ARG   A 1 190 ? 19.50895  20.03260 9.52203   1.000 42.11434  ? 189 ARG   A CD  1 
ATOM   1309 N  NE  . ARG   A 1 190 ? 20.13371  18.79889 9.06092   1.000 39.57124  ? 189 ARG   A NE  1 
ATOM   1310 C  CZ  . ARG   A 1 190 ? 20.90598  18.70988 7.98723   1.000 34.94428  ? 189 ARG   A CZ  1 
ATOM   1311 N  NH1 . ARG   A 1 190 ? 21.15379  19.76214 7.22417   1.000 40.10900  ? 189 ARG   A NH1 1 
ATOM   1312 N  NH2 . ARG   A 1 190 ? 21.44973  17.53786 7.67629   1.000 41.08198  ? 189 ARG   A NH2 1 
ATOM   1313 N  N   . ASP   A 1 191 ? 14.71934  19.93213 8.85411   1.000 26.23711  ? 190 ASP   A N   1 
ATOM   1314 C  CA  . ASP   A 1 191 ? 13.66695  19.09693 9.42815   1.000 23.73420  ? 190 ASP   A CA  1 
ATOM   1315 C  C   . ASP   A 1 191 ? 12.40358  19.91197 9.69460   1.000 23.50522  ? 190 ASP   A C   1 
ATOM   1316 O  O   . ASP   A 1 191 ? 11.63096  19.60772 10.61958  1.000 24.72716  ? 190 ASP   A O   1 
ATOM   1317 C  CB  . ASP   A 1 191 ? 14.14769  18.39943 10.71340  1.000 26.92995  ? 190 ASP   A CB  1 
ATOM   1318 C  CG  . ASP   A 1 191 ? 15.37498  17.52912 10.48342  1.000 32.34968  ? 190 ASP   A CG  1 
ATOM   1319 O  OD1 . ASP   A 1 191 ? 15.35654  16.73152 9.52144   1.000 28.19975  ? 190 ASP   A OD1 1 
ATOM   1320 O  OD2 . ASP   A 1 191 ? 16.35818  17.63540 11.26477  1.000 31.16427  ? 190 ASP   A OD2 1 
ATOM   1321 N  N   . ASN   A 1 192 ? 12.18833  20.96036 8.89021   1.000 21.59041  ? 191 ASN   A N   1 
ATOM   1322 C  CA  . ASN   A 1 192 ? 11.08954  21.88153 9.16151   1.000 20.38578  ? 191 ASN   A CA  1 
ATOM   1323 C  C   . ASN   A 1 192 ? 9.73192   21.28223 8.86837   1.000 22.37848  ? 191 ASN   A C   1 
ATOM   1324 O  O   . ASN   A 1 192 ? 8.72120   21.77360 9.39580   1.000 24.53823  ? 191 ASN   A O   1 
ATOM   1325 C  CB  . ASN   A 1 192 ? 11.27029  23.17604 8.37360   1.000 22.81947  ? 191 ASN   A CB  1 
ATOM   1326 C  CG  . ASN   A 1 192 ? 10.32190  24.27030 8.82623   1.000 22.83025  ? 191 ASN   A CG  1 
ATOM   1327 O  OD1 . ASN   A 1 192 ? 9.29164   24.53585 8.17485   1.000 23.71234  ? 191 ASN   A OD1 1 
ATOM   1328 N  ND2 . ASN   A 1 192 ? 10.62762  24.87768 9.96713   1.000 22.78356  ? 191 ASN   A ND2 1 
ATOM   1329 N  N   . LEU   A 1 193 ? 9.66955   20.22876 8.06741   1.000 21.28393  ? 192 LEU   A N   1 
ATOM   1330 C  CA  . LEU   A 1 193 ? 8.42816   19.50847 7.81807   1.000 19.97899  ? 192 LEU   A CA  1 
ATOM   1331 C  C   . LEU   A 1 193 ? 8.46841   18.20497 8.59650   1.000 22.68137  ? 192 LEU   A C   1 
ATOM   1332 O  O   . LEU   A 1 193 ? 9.46824   17.48734 8.53545   1.000 24.64926  ? 192 LEU   A O   1 
ATOM   1333 C  CB  . LEU   A 1 193 ? 8.26144   19.22246 6.31524   1.000 21.95424  ? 192 LEU   A CB  1 
ATOM   1334 C  CG  . LEU   A 1 193 ? 7.66586   20.35350 5.46436   1.000 26.44934  ? 192 LEU   A CG  1 
ATOM   1335 C  CD1 . LEU   A 1 193 ? 8.58803   21.54864 5.41063   1.000 27.32379  ? 192 LEU   A CD1 1 
ATOM   1336 C  CD2 . LEU   A 1 193 ? 7.34265   19.87134 4.04578   1.000 27.35609  ? 192 LEU   A CD2 1 
ATOM   1337 N  N   . HIS   A 1 194 ? 7.40828   17.89646 9.34972   1.000 20.85680  ? 193 HIS   A N   1 
ATOM   1338 C  CA  . HIS   A 1 194 ? 7.37112   16.57721 9.96152   1.000 20.02652  ? 193 HIS   A CA  1 
ATOM   1339 C  C   . HIS   A 1 194 ? 5.95660   16.01837 9.99835   1.000 21.70840  ? 193 HIS   A C   1 
ATOM   1340 O  O   . HIS   A 1 194 ? 4.95790   16.75517 9.99134   1.000 19.61178  ? 193 HIS   A O   1 
ATOM   1341 C  CB  . HIS   A 1 194 ? 8.03316   16.53849 11.37999  1.000 19.94669  ? 193 HIS   A CB  1 
ATOM   1342 C  CG  . HIS   A 1 194 ? 7.37495   17.37477 12.45500  1.000 20.92786  ? 193 HIS   A CG  1 
ATOM   1343 N  ND1 . HIS   A 1 194 ? 8.00343   17.61989 13.66059  1.000 21.87841  ? 193 HIS   A ND1 1 
ATOM   1344 C  CD2 . HIS   A 1 194 ? 6.17590   18.00452 12.52508  1.000 20.67060  ? 193 HIS   A CD2 1 
ATOM   1345 C  CE1 . HIS   A 1 194 ? 7.23092   18.38361 14.41734  1.000 21.13136  ? 193 HIS   A CE1 1 
ATOM   1346 N  NE2 . HIS   A 1 194 ? 6.11128   18.62752 13.75651  1.000 17.80748  ? 193 HIS   A NE2 1 
ATOM   1347 N  N   . GLN   A 1 195 ? 5.89586   14.68815 9.98292   1.000 21.17340  ? 194 GLN   A N   1 
ATOM   1348 C  CA  . GLN   A 1 195 ? 4.66978   13.92672 10.17766  1.000 21.55039  ? 194 GLN   A CA  1 
ATOM   1349 C  C   . GLN   A 1 195 ? 4.89677   13.04880 11.39920  1.000 23.22301  ? 194 GLN   A C   1 
ATOM   1350 O  O   . GLN   A 1 195 ? 6.00259   12.54222 11.60047  1.000 21.28294  ? 194 GLN   A O   1 
ATOM   1351 C  CB  . GLN   A 1 195 ? 4.35258   13.05906 8.93393   1.000 23.34900  ? 194 GLN   A CB  1 
ATOM   1352 C  CG  . GLN   A 1 195 ? 3.41325   11.89870 9.21578   1.000 25.08710  ? 194 GLN   A CG  1 
ATOM   1353 C  CD  . GLN   A 1 195 ? 2.98256   11.16725 7.96467   1.000 34.93843  ? 194 GLN   A CD  1 
ATOM   1354 O  OE1 . GLN   A 1 195 ? 3.08492   11.68970 6.85071   1.000 35.67759  ? 194 GLN   A OE1 1 
ATOM   1355 N  NE2 . GLN   A 1 195 ? 2.51398   9.93647  8.14026   1.000 32.76545  ? 194 GLN   A NE2 1 
ATOM   1356 N  N   . ILE   A 1 196 ? 3.87914   12.88863 12.24617  1.000 20.78955  ? 195 ILE   A N   1 
ATOM   1357 C  CA  . ILE   A 1 196 ? 4.04734   12.18306 13.51714  1.000 19.24309  ? 195 ILE   A CA  1 
ATOM   1358 C  C   . ILE   A 1 196 ? 2.95654   11.11909 13.62527  1.000 22.11987  ? 195 ILE   A C   1 
ATOM   1359 O  O   . ILE   A 1 196 ? 1.76854   11.45543 13.68676  1.000 22.49556  ? 195 ILE   A O   1 
ATOM   1360 C  CB  . ILE   A 1 196 ? 3.97955   13.15306 14.71209  1.000 22.79760  ? 195 ILE   A CB  1 
ATOM   1361 C  CG1 . ILE   A 1 196 ? 5.04060   14.23777 14.54086  1.000 23.00726  ? 195 ILE   A CG1 1 
ATOM   1362 C  CG2 . ILE   A 1 196 ? 4.17859   12.41075 16.05611  1.000 21.79617  ? 195 ILE   A CG2 1 
ATOM   1363 C  CD1 . ILE   A 1 196 ? 4.71824   15.49709 15.32314  1.000 25.71463  ? 195 ILE   A CD1 1 
ATOM   1364 N  N   . ASP   A 1 197 ? 3.35545   9.84437  13.64941  1.000 20.52899  ? 196 ASP   A N   1 
ATOM   1365 C  CA  . ASP   A 1 197 ? 2.42584   8.71767  13.71031  1.000 23.54519  ? 196 ASP   A CA  1 
ATOM   1366 C  C   . ASP   A 1 197 ? 2.50548   8.03053  15.06327  1.000 23.65643  ? 196 ASP   A C   1 
ATOM   1367 O  O   . ASP   A 1 197 ? 3.60050   7.72607  15.54048  1.000 23.42294  ? 196 ASP   A O   1 
ATOM   1368 C  CB  . ASP   A 1 197 ? 2.72859   7.66456  12.63025  1.000 24.91354  ? 196 ASP   A CB  1 
ATOM   1369 C  CG  . ASP   A 1 197 ? 2.93886   8.25222  11.25186  1.000 27.19467  ? 196 ASP   A CG  1 
ATOM   1370 O  OD1 . ASP   A 1 197 ? 2.12709   9.09180  10.82633  1.000 30.30341  ? 196 ASP   A OD1 1 
ATOM   1371 O  OD2 . ASP   A 1 197 ? 3.89922   7.82282  10.56270  1.000 31.52108  ? 196 ASP   A OD2 1 
ATOM   1372 N  N   . ALA   A 1 198 ? 1.35304   7.75389  15.66740  1.000 22.47951  ? 197 ALA   A N   1 
ATOM   1373 C  CA  . ALA   A 1 198 ? 1.32763   6.95901  16.89300  1.000 21.85680  ? 197 ALA   A CA  1 
ATOM   1374 C  C   . ALA   A 1 198 ? 1.54199   5.49418  16.53274  1.000 27.59598  ? 197 ALA   A C   1 
ATOM   1375 O  O   . ALA   A 1 198 ? 0.81705   4.95489  15.69712  1.000 30.43131  ? 197 ALA   A O   1 
ATOM   1376 C  CB  . ALA   A 1 198 ? -0.00989  7.12914  17.61825  1.000 23.78211  ? 197 ALA   A CB  1 
ATOM   1377 N  N   . VAL   A 1 199 ? 2.52923   4.85523  17.15892  1.000 28.02464  ? 198 VAL   A N   1 
ATOM   1378 C  CA  . VAL   A 1 199 ? 2.95811   3.50200  16.79789  1.000 25.80543  ? 198 VAL   A CA  1 
ATOM   1379 C  C   . VAL   A 1 199 ? 2.50150   2.53436  17.88569  1.000 27.48791  ? 198 VAL   A C   1 
ATOM   1380 O  O   . VAL   A 1 199 ? 2.88936   2.67190  19.05427  1.000 31.79540  ? 198 VAL   A O   1 
ATOM   1381 C  CB  . VAL   A 1 199 ? 4.48269   3.41562  16.61339  1.000 29.15742  ? 198 VAL   A CB  1 
ATOM   1382 C  CG1 . VAL   A 1 199 ? 4.89844   1.96497  16.39534  1.000 34.55758  ? 198 VAL   A CG1 1 
ATOM   1383 C  CG2 . VAL   A 1 199 ? 4.93927   4.28983  15.44201  1.000 29.97941  ? 198 VAL   A CG2 1 
ATOM   1384 N  N   . GLU   A 1 200 ? 1.72047   1.52955  17.48837  1.000 31.52515  ? 199 GLU   A N   1 
ATOM   1385 C  CA  . GLU   A 1 200 ? 1.25834   0.45524  18.37997  1.000 36.80270  ? 199 GLU   A CA  1 
ATOM   1386 C  C   . GLU   A 1 200 ? 0.58466   0.98749  19.64826  1.000 36.33166  ? 199 GLU   A C   1 
ATOM   1387 O  O   . GLU   A 1 200 ? 0.81527   0.49928  20.75650  1.000 34.91885  ? 199 GLU   A O   1 
ATOM   1388 C  CB  . GLU   A 1 200 ? 2.39517   -0.50217 18.74401  1.000 44.47641  ? 199 GLU   A CB  1 
ATOM   1389 C  CG  . GLU   A 1 200 ? 3.06446   -1.18787 17.56805  0.674 46.28727  ? 199 GLU   A CG  1 
ATOM   1390 C  CD  . GLU   A 1 200 ? 4.46084   -1.66998 17.90170  1.000 59.69816  ? 199 GLU   A CD  1 
ATOM   1391 O  OE1 . GLU   A 1 200 ? 4.95435   -1.34554 19.00393  0.446 56.39712  ? 199 GLU   A OE1 1 
ATOM   1392 O  OE2 . GLU   A 1 200 ? 5.05769   -2.38973 17.06945  0.376 55.18961  ? 199 GLU   A OE2 1 
ATOM   1393 N  N   . GLY   A 1 201 ? -0.28286  1.97954  19.47907  1.000 28.95224  ? 200 GLY   A N   1 
ATOM   1394 C  CA  . GLY   A 1 201 ? -1.06695  2.48113  20.58458  1.000 26.76923  ? 200 GLY   A CA  1 
ATOM   1395 C  C   . GLY   A 1 201 ? -0.95165  3.98450  20.74492  1.000 26.65218  ? 200 GLY   A C   1 
ATOM   1396 O  O   . GLY   A 1 201 ? -0.26124  4.64980  19.97124  1.000 23.98647  ? 200 GLY   A O   1 
ATOM   1397 N  N   . PRO   A 1 202 ? -1.61005  4.53503  21.76964  1.000 25.18684  ? 201 PRO   A N   1 
ATOM   1398 C  CA  . PRO   A 1 202 ? -1.57422  5.98397  21.99585  1.000 21.76955  ? 201 PRO   A CA  1 
ATOM   1399 C  C   . PRO   A 1 202 ? -0.17328  6.46434  22.32514  1.000 22.37531  ? 201 PRO   A C   1 
ATOM   1400 O  O   . PRO   A 1 202 ? 0.67281   5.72546  22.83398  1.000 25.19331  ? 201 PRO   A O   1 
ATOM   1401 C  CB  . PRO   A 1 202 ? -2.51268  6.18843  23.19228  1.000 23.98410  ? 201 PRO   A CB  1 
ATOM   1402 C  CG  . PRO   A 1 202 ? -3.33021  4.91436  23.28718  1.000 25.99169  ? 201 PRO   A CG  1 
ATOM   1403 C  CD  . PRO   A 1 202 ? -2.39336  3.83805  22.80364  1.000 28.52329  ? 201 PRO   A CD  1 
ATOM   1404 N  N   . ALA   A 1 203 ? 0.05798   7.74648  22.06534  1.000 18.99635  ? 202 ALA   A N   1 
ATOM   1405 C  CA  . ALA   A 1 203 ? 1.34930   8.33448  22.39536  1.000 18.88080  ? 202 ALA   A CA  1 
ATOM   1406 C  C   . ALA   A 1 203 ? 1.11806   9.79519  22.72898  1.000 20.10430  ? 202 ALA   A C   1 
ATOM   1407 O  O   . ALA   A 1 203 ? 0.07822   10.35694 22.39125  1.000 20.95536  ? 202 ALA   A O   1 
ATOM   1408 C  CB  . ALA   A 1 203 ? 2.33118   8.18613  21.22625  1.000 22.71561  ? 202 ALA   A CB  1 
ATOM   1409 N  N   . ALA   A 1 204 ? 2.08081   10.40912 23.41452  1.000 16.77743  ? 203 ALA   A N   1 
ATOM   1410 C  CA  . ALA   A 1 204 ? 1.94893   11.83427 23.67806  1.000 18.43625  ? 203 ALA   A CA  1 
ATOM   1411 C  C   . ALA   A 1 204 ? 3.32908   12.46000 23.68894  1.000 21.28297  ? 203 ALA   A C   1 
ATOM   1412 O  O   . ALA   A 1 204 ? 4.31707   11.79898 24.01793  1.000 20.72214  ? 203 ALA   A O   1 
ATOM   1413 C  CB  . ALA   A 1 204 ? 1.23439   12.09736 25.00829  1.000 20.36641  ? 203 ALA   A CB  1 
ATOM   1414 N  N   . PHE   A 1 205 ? 3.39797   13.74163 23.33924  1.000 19.49027  ? 204 PHE   A N   1 
ATOM   1415 C  CA  . PHE   A 1 205 ? 4.68168   14.41615 23.38595  1.000 18.15906  ? 204 PHE   A CA  1 
ATOM   1416 C  C   . PHE   A 1 205 ? 4.50922   15.86251 23.82105  1.000 19.66121  ? 204 PHE   A C   1 
ATOM   1417 O  O   . PHE   A 1 205 ? 3.50566   16.52056 23.51091  1.000 17.15015  ? 204 PHE   A O   1 
ATOM   1418 C  CB  . PHE   A 1 205 ? 5.41986   14.37307 22.02748  1.000 16.41780  ? 204 PHE   A CB  1 
ATOM   1419 C  CG  . PHE   A 1 205 ? 4.65715   14.98965 20.86987  1.000 18.31139  ? 204 PHE   A CG  1 
ATOM   1420 C  CD1 . PHE   A 1 205 ? 3.78115   14.22931 20.11130  1.000 20.71792  ? 204 PHE   A CD1 1 
ATOM   1421 C  CD2 . PHE   A 1 205 ? 4.84539   16.32436 20.52935  1.000 19.95875  ? 204 PHE   A CD2 1 
ATOM   1422 C  CE1 . PHE   A 1 205 ? 3.08615   14.79209 19.01694  1.000 18.62627  ? 204 PHE   A CE1 1 
ATOM   1423 C  CE2 . PHE   A 1 205 ? 4.16354   16.87999 19.45148  1.000 19.41650  ? 204 PHE   A CE2 1 
ATOM   1424 C  CZ  . PHE   A 1 205 ? 3.27810   16.10149 18.70224  1.000 20.15895  ? 204 PHE   A CZ  1 
ATOM   1425 N  N   . LEU   A 1 206 ? 5.51930   16.33785 24.53802  1.000 17.13980  ? 205 LEU   A N   1 
ATOM   1426 C  CA  A LEU   A 1 206 ? 5.67028   17.75602 24.83008  0.447 18.10209  ? 205 LEU   A CA  1 
ATOM   1427 C  CA  B LEU   A 1 206 ? 5.64114   17.76120 24.81674  0.553 18.07879  ? 205 LEU   A CA  1 
ATOM   1428 C  C   . LEU   A 1 206 ? 6.21190   18.45287 23.58884  1.000 17.84091  ? 205 LEU   A C   1 
ATOM   1429 O  O   . LEU   A 1 206 ? 7.13375   17.94355 22.93932  1.000 20.17779  ? 205 LEU   A O   1 
ATOM   1430 C  CB  A LEU   A 1 206 ? 6.62949   17.91940 26.01470  0.447 18.63227  ? 205 LEU   A CB  1 
ATOM   1431 C  CB  B LEU   A 1 206 ? 6.55706   18.00987 26.01413  0.553 18.65264  ? 205 LEU   A CB  1 
ATOM   1432 C  CG  A LEU   A 1 206 ? 6.93284   19.19915 26.80282  0.447 20.10168  ? 205 LEU   A CG  1 
ATOM   1433 C  CG  B LEU   A 1 206 ? 6.64244   19.47312 26.45795  0.553 18.04898  ? 205 LEU   A CG  1 
ATOM   1434 C  CD1 A LEU   A 1 206 ? 7.59215   20.25361 25.91782  0.447 19.36653  ? 205 LEU   A CD1 1 
ATOM   1435 C  CD1 B LEU   A 1 206 ? 5.50206   19.79821 27.40116  0.553 21.04363  ? 205 LEU   A CD1 1 
ATOM   1436 C  CD2 A LEU   A 1 206 ? 5.72134   19.74178 27.54546  0.447 20.50771  ? 205 LEU   A CD2 1 
ATOM   1437 C  CD2 B LEU   A 1 206 ? 7.99109   19.78555 27.09807  0.553 22.04469  ? 205 LEU   A CD2 1 
ATOM   1438 N  N   . ASP   A 1 207 ? 5.64920   19.62392 23.25245  1.000 16.71221  ? 206 ASP   A N   1 
ATOM   1439 C  CA  . ASP   A 1 207 ? 6.13065   20.37041 22.09644  1.000 17.18062  ? 206 ASP   A CA  1 
ATOM   1440 C  C   . ASP   A 1 207 ? 6.36317   21.81921 22.46934  1.000 20.84023  ? 206 ASP   A C   1 
ATOM   1441 O  O   . ASP   A 1 207 ? 5.54559   22.42532 23.16857  1.000 20.20243  ? 206 ASP   A O   1 
ATOM   1442 C  CB  . ASP   A 1 207 ? 5.15047   20.33054 20.90790  1.000 20.65467  ? 206 ASP   A CB  1 
ATOM   1443 C  CG  . ASP   A 1 207 ? 5.88245   20.42903 19.55605  1.000 31.18845  ? 206 ASP   A CG  1 
ATOM   1444 O  OD1 . ASP   A 1 207 ? 7.09980   20.74847 19.52894  0.464 26.55162  ? 206 ASP   A OD1 1 
ATOM   1445 O  OD2 . ASP   A 1 207 ? 5.25034   20.18049 18.51789  0.429 19.90256  ? 206 ASP   A OD2 1 
ATOM   1446 N  N   . ILE   A 1 208 ? 7.50241   22.34221 22.03247  1.000 17.83078  ? 207 ILE   A N   1 
ATOM   1447 C  CA  . ILE   A 1 208 ? 7.84321   23.75680 22.15974  1.000 17.94649  ? 207 ILE   A CA  1 
ATOM   1448 C  C   . ILE   A 1 208 ? 7.99061   24.32031 20.75576  1.000 22.71108  ? 207 ILE   A C   1 
ATOM   1449 O  O   . ILE   A 1 208 ? 8.72132   23.75297 19.93839  1.000 21.78026  ? 207 ILE   A O   1 
ATOM   1450 C  CB  . ILE   A 1 208 ? 9.14604   23.95041 22.95170  1.000 18.23472  ? 207 ILE   A CB  1 
ATOM   1451 C  CG1 . ILE   A 1 208 ? 8.97781   23.40134 24.38136  1.000 23.08046  ? 207 ILE   A CG1 1 
ATOM   1452 C  CG2 . ILE   A 1 208 ? 9.54192   25.43078 22.97629  1.000 21.74261  ? 207 ILE   A CG2 1 
ATOM   1453 C  CD1 . ILE   A 1 208 ? 10.26338  23.37638 25.15988  1.000 24.91744  ? 207 ILE   A CD1 1 
ATOM   1454 N  N   . LEU   A 1 209 ? 7.28073   25.41557 20.46262  1.000 18.94761  ? 208 LEU   A N   1 
ATOM   1455 C  CA  . LEU   A 1 209 ? 7.42830   26.10766 19.18295  1.000 18.48428  ? 208 LEU   A CA  1 
ATOM   1456 C  C   . LEU   A 1 209 ? 7.96773   27.50313 19.44792  1.000 22.17940  ? 208 LEU   A C   1 
ATOM   1457 O  O   . LEU   A 1 209 ? 7.51902   28.17323 20.38297  1.000 23.90641  ? 208 LEU   A O   1 
ATOM   1458 C  CB  . LEU   A 1 209 ? 6.09639   26.23350 18.43932  1.000 21.78192  ? 208 LEU   A CB  1 
ATOM   1459 C  CG  . LEU   A 1 209 ? 5.38417   24.93349 18.10445  1.000 26.81617  ? 208 LEU   A CG  1 
ATOM   1460 C  CD1 . LEU   A 1 209 ? 3.98771   25.24776 17.58923  1.000 30.54079  ? 208 LEU   A CD1 1 
ATOM   1461 C  CD2 . LEU   A 1 209 ? 6.19149   24.25494 17.03667  1.000 26.15030  ? 208 LEU   A CD2 1 
ATOM   1462 N  N   . ALA   A 1 210 ? 8.90878   27.94974 18.62365  1.000 20.44112  ? 209 ALA   A N   1 
ATOM   1463 C  CA  . ALA   A 1 210 ? 9.47948   29.26434 18.88924  1.000 21.01340  ? 209 ALA   A CA  1 
ATOM   1464 C  C   . ALA   A 1 210 ? 9.88425   29.98122 17.60812  1.000 23.85903  ? 209 ALA   A C   1 
ATOM   1465 O  O   . ALA   A 1 210 ? 10.80058  29.53088 16.91104  1.000 26.11259  ? 209 ALA   A O   1 
ATOM   1466 C  CB  . ALA   A 1 210 ? 10.69408  29.12630 19.79719  1.000 25.91873  ? 209 ALA   A CB  1 
ATOM   1467 N  N   . PRO   A 1 211 ? 9.23004   31.10330 17.26181  1.000 24.15097  ? 210 PRO   A N   1 
ATOM   1468 C  CA  . PRO   A 1 211 ? 8.04404   31.66667 17.89386  1.000 26.04610  ? 210 PRO   A CA  1 
ATOM   1469 C  C   . PRO   A 1 211 ? 6.84905   30.75930 17.63965  1.000 24.43627  ? 210 PRO   A C   1 
ATOM   1470 O  O   . PRO   A 1 211 ? 6.93258   29.85612 16.80053  1.000 28.79441  ? 210 PRO   A O   1 
ATOM   1471 C  CB  . PRO   A 1 211 ? 7.90862   33.03946 17.20718  1.000 26.25542  ? 210 PRO   A CB  1 
ATOM   1472 C  CG  . PRO   A 1 211 ? 8.50332   32.82877 15.85797  1.000 30.77188  ? 210 PRO   A CG  1 
ATOM   1473 C  CD  . PRO   A 1 211 ? 9.64136   31.87559 16.07492  1.000 29.11972  ? 210 PRO   A CD  1 
ATOM   1474 N  N   . PRO   A 1 212 ? 5.74264   30.95393 18.34193  1.000 27.51845  ? 211 PRO   A N   1 
ATOM   1475 C  CA  . PRO   A 1 212 ? 4.52454   30.21729 18.00741  1.000 23.48614  ? 211 PRO   A CA  1 
ATOM   1476 C  C   . PRO   A 1 212 ? 4.03792   30.65276 16.64001  1.000 29.81802  ? 211 PRO   A C   1 
ATOM   1477 O  O   . PRO   A 1 212 ? 4.53257   31.62161 16.05887  1.000 28.70492  ? 211 PRO   A O   1 
ATOM   1478 C  CB  . PRO   A 1 212 ? 3.53287   30.61892 19.10623  1.000 27.60288  ? 211 PRO   A CB  1 
ATOM   1479 C  CG  . PRO   A 1 212 ? 4.38175   31.20321 20.21250  1.000 31.73062  ? 211 PRO   A CG  1 
ATOM   1480 C  CD  . PRO   A 1 212 ? 5.56290   31.81555 19.52444  1.000 27.22937  ? 211 PRO   A CD  1 
ATOM   1481 N  N   . TYR   A 1 213 ? 3.06376   29.91297 16.12019  1.000 26.62668  ? 212 TYR   A N   1 
ATOM   1482 C  CA  . TYR   A 1 213 ? 2.46697   30.32696 14.86450  1.000 27.46511  ? 212 TYR   A CA  1 
ATOM   1483 C  C   . TYR   A 1 213 ? 1.77712   31.66502 15.07216  1.000 32.82187  ? 212 TYR   A C   1 
ATOM   1484 O  O   . TYR   A 1 213 ? 1.40892   32.03055 16.19167  1.000 29.84111  ? 212 TYR   A O   1 
ATOM   1485 C  CB  . TYR   A 1 213 ? 1.44348   29.30254 14.38114  1.000 25.99141  ? 212 TYR   A CB  1 
ATOM   1486 C  CG  . TYR   A 1 213 ? 1.99553   27.98279 13.86618  1.000 24.91224  ? 212 TYR   A CG  1 
ATOM   1487 C  CD1 . TYR   A 1 213 ? 2.51780   27.87001 12.58035  1.000 25.69197  ? 212 TYR   A CD1 1 
ATOM   1488 C  CD2 . TYR   A 1 213 ? 1.93876   26.83602 14.65261  1.000 24.97917  ? 212 TYR   A CD2 1 
ATOM   1489 C  CE1 . TYR   A 1 213 ? 2.99686   26.63659 12.10015  1.000 24.24736  ? 212 TYR   A CE1 1 
ATOM   1490 C  CE2 . TYR   A 1 213 ? 2.41065   25.61423 14.18142  1.000 22.54189  ? 212 TYR   A CE2 1 
ATOM   1491 C  CZ  . TYR   A 1 213 ? 2.92553   25.52593 12.91010  1.000 21.40862  ? 212 TYR   A CZ  1 
ATOM   1492 O  OH  . TYR   A 1 213 ? 3.36879   24.28731 12.46863  1.000 23.07048  ? 212 TYR   A OH  1 
ATOM   1493 N  N   . ASP   A 1 214 ? 1.60855   32.40460 13.97905  1.000 29.87113  ? 213 ASP   A N   1 
ATOM   1494 C  CA  . ASP   A 1 214 ? 0.89824   33.68323 14.00787  1.000 35.58597  ? 213 ASP   A CA  1 
ATOM   1495 C  C   . ASP   A 1 214 ? 0.33770   33.92793 12.62277  1.000 34.95228  ? 213 ASP   A C   1 
ATOM   1496 O  O   . ASP   A 1 214 ? 0.95857   34.59916 11.78898  1.000 39.70245  ? 213 ASP   A O   1 
ATOM   1497 C  CB  . ASP   A 1 214 ? 1.81459   34.83056 14.44040  1.000 38.27532  ? 213 ASP   A CB  1 
ATOM   1498 C  CG  . ASP   A 1 214 ? 1.03795   36.09747 14.79755  1.000 47.58909  ? 213 ASP   A CG  1 
ATOM   1499 O  OD1 . ASP   A 1 214 ? -0.15243  36.20377 14.43132  1.000 42.14705  ? 213 ASP   A OD1 1 
ATOM   1500 O  OD2 . ASP   A 1 214 ? 1.62991   37.00102 15.42393  1.000 53.94753  ? 213 ASP   A OD2 1 
ATOM   1501 N  N   . PRO   A 1 215 ? -0.82874  33.35800 12.32502  1.000 33.38950  ? 214 PRO   A N   1 
ATOM   1502 C  CA  . PRO   A 1 215 ? -1.39134  33.50787 10.97394  1.000 37.38961  ? 214 PRO   A CA  1 
ATOM   1503 C  C   . PRO   A 1 215 ? -1.52975  34.95161 10.52098  1.000 42.89808  ? 214 PRO   A C   1 
ATOM   1504 O  O   . PRO   A 1 215 ? -1.25446  35.25131 9.35455   1.000 44.70807  ? 214 PRO   A O   1 
ATOM   1505 C  CB  . PRO   A 1 215 ? -2.75782  32.81847 11.09768  1.000 41.24813  ? 214 PRO   A CB  1 
ATOM   1506 C  CG  . PRO   A 1 215 ? -2.55653  31.80066 12.18221  1.000 36.45525  ? 214 PRO   A CG  1 
ATOM   1507 C  CD  . PRO   A 1 215 ? -1.60653  32.42332 13.15893  1.000 33.15757  ? 214 PRO   A CD  1 
ATOM   1508 N  N   . ASP   A 1 216 ? -1.93057  35.85959 11.41472  1.000 38.52063  ? 215 ASP   A N   1 
ATOM   1509 C  CA  . ASP   A 1 216 ? -2.10875  37.25680 11.02354  1.000 49.19611  ? 215 ASP   A CA  1 
ATOM   1510 C  C   . ASP   A 1 216 ? -0.78712  37.97347 10.80027  1.000 52.30973  ? 215 ASP   A C   1 
ATOM   1511 O  O   . ASP   A 1 216 ? -0.77585  39.05250 10.19695  1.000 58.11806  ? 215 ASP   A O   1 
ATOM   1512 C  CB  . ASP   A 1 216 ? -2.93090  37.99618 12.07404  1.000 49.62656  ? 215 ASP   A CB  1 
ATOM   1513 C  CG  . ASP   A 1 216 ? -4.34935  37.48950 12.14652  1.000 53.79844  ? 215 ASP   A CG  1 
ATOM   1514 O  OD1 . ASP   A 1 216 ? -4.86383  37.05946 11.09103  1.000 58.12653  ? 215 ASP   A OD1 1 
ATOM   1515 O  OD2 . ASP   A 1 216 ? -4.94220  37.51151 13.24778  1.000 62.73179  ? 215 ASP   A OD2 1 
ATOM   1516 N  N   . ASP   A 1 217 ? 0.31500   37.40866 11.27913  1.000 45.44277  ? 216 ASP   A N   1 
ATOM   1517 C  CA  . ASP   A 1 217 ? 1.65424   37.91304 11.02207  1.000 46.19549  ? 216 ASP   A CA  1 
ATOM   1518 C  C   . ASP   A 1 217 ? 2.25112   37.20356 9.80900   1.000 46.97510  ? 216 ASP   A C   1 
ATOM   1519 O  O   . ASP   A 1 217 ? 3.35916   37.52307 9.38066   1.000 56.63008  ? 216 ASP   A O   1 
ATOM   1520 C  CB  . ASP   A 1 217 ? 2.49646   37.71329 12.30645  1.000 51.57102  ? 216 ASP   A CB  1 
ATOM   1521 C  CG  . ASP   A 1 217 ? 3.91723   38.31751 12.25843  1.000 69.90750  ? 216 ASP   A CG  1 
ATOM   1522 O  OD1 . ASP   A 1 217 ? 4.57404   38.43244 11.21034  1.000 75.36446  ? 216 ASP   A OD1 1 
ATOM   1523 O  OD2 . ASP   A 1 217 ? 4.40728   38.66767 13.35599  1.000 78.51576  ? 216 ASP   A OD2 1 
ATOM   1524 N  N   . GLY   A 1 218 ? 1.51481   36.27211 9.21093   1.000 45.89970  ? 217 GLY   A N   1 
ATOM   1525 C  CA  . GLY   A 1 218 ? 2.00778   35.55997 8.05297   1.000 47.71125  ? 217 GLY   A CA  1 
ATOM   1526 C  C   . GLY   A 1 218 ? 2.81557   34.32221 8.36001   1.000 46.90809  ? 217 GLY   A C   1 
ATOM   1527 O  O   . GLY   A 1 218 ? 3.57380   33.86458 7.49559   1.000 42.22318  ? 217 GLY   A O   1 
ATOM   1528 N  N   . ARG   A 1 219 ? 2.68384   33.77415 9.56593   1.000 43.43424  ? 218 ARG   A N   1 
ATOM   1529 C  CA  . ARG   A 1 219 ? 3.34029   32.54531 10.00786  1.000 34.30735  ? 218 ARG   A CA  1 
ATOM   1530 C  C   . ARG   A 1 219 ? 2.24648   31.50982 10.25765  1.000 30.42596  ? 218 ARG   A C   1 
ATOM   1531 O  O   . ARG   A 1 219 ? 1.68138   31.45161 11.34963  1.000 34.64521  ? 218 ARG   A O   1 
ATOM   1532 C  CB  . ARG   A 1 219 ? 4.16099   32.77810 11.28607  1.000 41.67592  ? 218 ARG   A CB  1 
ATOM   1533 C  CG  . ARG   A 1 219 ? 5.48256   32.06262 11.31375  1.000 39.73156  ? 218 ARG   A CG  1 
ATOM   1534 C  CD  . ARG   A 1 219 ? 6.38231   32.52027 12.44948  1.000 31.10825  ? 218 ARG   A CD  1 
ATOM   1535 N  NE  . ARG   A 1 219 ? 5.65410   32.89058 13.65315  1.000 31.07101  ? 218 ARG   A NE  1 
ATOM   1536 C  CZ  . ARG   A 1 219 ? 5.59980   34.12180 14.13776  1.000 42.44889  ? 218 ARG   A CZ  1 
ATOM   1537 N  NH1 . ARG   A 1 219 ? 6.10366   35.14981 13.47072  1.000 42.71259  ? 218 ARG   A NH1 1 
ATOM   1538 N  NH2 . ARG   A 1 219 ? 5.01684   34.33004 15.31228  1.000 35.56567  ? 218 ARG   A NH2 1 
ATOM   1539 N  N   . ASP   A 1 220 ? 1.95231   30.68909 9.25000   1.000 33.66189  ? 219 ASP   A N   1 
ATOM   1540 C  CA  . ASP   A 1 220 ? 0.88001   29.70758 9.35639   1.000 25.61006  ? 219 ASP   A CA  1 
ATOM   1541 C  C   . ASP   A 1 220 ? 1.40002   28.28896 9.16701   1.000 26.91119  ? 219 ASP   A C   1 
ATOM   1542 O  O   . ASP   A 1 220 ? 2.55188   28.05205 8.80387   1.000 29.70400  ? 219 ASP   A O   1 
ATOM   1543 C  CB  . ASP   A 1 220 ? -0.23425  29.97736 8.33263   1.000 30.45265  ? 219 ASP   A CB  1 
ATOM   1544 C  CG  . ASP   A 1 220 ? -1.61773  29.77641 8.91949   1.000 39.24256  ? 219 ASP   A CG  1 
ATOM   1545 O  OD1 . ASP   A 1 220 ? -1.78836  28.82697 9.71656   1.000 30.35097  ? 219 ASP   A OD1 1 
ATOM   1546 O  OD2 . ASP   A 1 220 ? -2.53434  30.55907 8.58407   1.000 35.25444  ? 219 ASP   A OD2 1 
ATOM   1547 N  N   . CYS   A 1 221 ? 0.50610   27.34419 9.40080   1.000 24.56079  ? 220 CYS   A N   1 
ATOM   1548 C  CA  . CYS   A 1 221 ? 0.80642   25.92416 9.31405   1.000 24.80066  ? 220 CYS   A CA  1 
ATOM   1549 C  C   . CYS   A 1 221 ? 0.28017   25.42104 7.97933   1.000 28.44864  ? 220 CYS   A C   1 
ATOM   1550 O  O   . CYS   A 1 221 ? -0.91017  25.56984 7.69097   1.000 29.91719  ? 220 CYS   A O   1 
ATOM   1551 C  CB  . CYS   A 1 221 ? 0.15586   25.17724 10.47794  1.000 25.21112  ? 220 CYS   A CB  1 
ATOM   1552 S  SG  . CYS   A 1 221 ? 0.36671   23.38725 10.46332  1.000 27.00381  ? 220 CYS   A SG  1 
ATOM   1553 N  N   . HIS   A 1 222 ? 1.16497   24.86236 7.15965   1.000 28.25367  ? 221 HIS   A N   1 
ATOM   1554 C  CA  . HIS   A 1 222 ? 0.80332   24.30020 5.86365   1.000 27.13705  ? 221 HIS   A CA  1 
ATOM   1555 C  C   . HIS   A 1 222 ? 0.98986   22.79469 5.89920   1.000 24.00784  ? 221 HIS   A C   1 
ATOM   1556 O  O   . HIS   A 1 222 ? 1.98949   22.30446 6.42692   1.000 27.54359  ? 221 HIS   A O   1 
ATOM   1557 C  CB  . HIS   A 1 222 ? 1.65956   24.90213 4.75125   1.000 28.23086  ? 221 HIS   A CB  1 
ATOM   1558 C  CG  . HIS   A 1 222 ? 1.76146   26.39038 4.82089   1.000 33.36539  ? 221 HIS   A CG  1 
ATOM   1559 N  ND1 . HIS   A 1 222 ? 0.94142   27.22375 4.09238   1.000 39.10742  ? 221 HIS   A ND1 1 
ATOM   1560 C  CD2 . HIS   A 1 222 ? 2.54820   27.19656 5.57169   1.000 30.42192  ? 221 HIS   A CD2 1 
ATOM   1561 C  CE1 . HIS   A 1 222 ? 1.23620   28.48094 4.37218   1.000 39.65182  ? 221 HIS   A CE1 1 
ATOM   1562 N  NE2 . HIS   A 1 222 ? 2.20708   28.49224 5.26684   1.000 35.69714  ? 221 HIS   A NE2 1 
ATOM   1563 N  N   . TYR   A 1 223 ? 0.01625   22.06583 5.36203   1.000 23.10485  ? 222 TYR   A N   1 
ATOM   1564 C  CA  . TYR   A 1 223 ? 0.05919   20.61283 5.28424   1.000 23.71087  ? 222 TYR   A CA  1 
ATOM   1565 C  C   . TYR   A 1 223 ? 0.51224   20.16900 3.89814   1.000 23.15854  ? 222 TYR   A C   1 
ATOM   1566 O  O   . TYR   A 1 223 ? 0.32793   20.88561 2.91482   1.000 29.02362  ? 222 TYR   A O   1 
ATOM   1567 C  CB  . TYR   A 1 223 ? -1.31566  20.01642 5.58211   1.000 24.06664  ? 222 TYR   A CB  1 
ATOM   1568 C  CG  . TYR   A 1 223 ? -1.69054  20.25675 7.02875   1.000 23.01910  ? 222 TYR   A CG  1 
ATOM   1569 C  CD1 . TYR   A 1 223 ? -1.26949  19.38525 8.01746   1.000 25.24365  ? 222 TYR   A CD1 1 
ATOM   1570 C  CD2 . TYR   A 1 223 ? -2.41643  21.38319 7.40080   1.000 26.14410  ? 222 TYR   A CD2 1 
ATOM   1571 C  CE1 . TYR   A 1 223 ? -1.58517  19.61284 9.34742   1.000 23.32303  ? 222 TYR   A CE1 1 
ATOM   1572 C  CE2 . TYR   A 1 223 ? -2.73226  21.62158 8.75544   1.000 26.30356  ? 222 TYR   A CE2 1 
ATOM   1573 C  CZ  . TYR   A 1 223 ? -2.30999  20.73267 9.70176   1.000 22.29186  ? 222 TYR   A CZ  1 
ATOM   1574 O  OH  . TYR   A 1 223 ? -2.61241  20.95075 11.04910  1.000 23.14256  ? 222 TYR   A OH  1 
ATOM   1575 N  N   . TYR   A 1 224 ? 1.09710   18.97505 3.83155   1.000 25.04824  ? 223 TYR   A N   1 
ATOM   1576 C  CA  . TYR   A 1 224 ? 1.66614   18.47877 2.58141   1.000 28.38712  ? 223 TYR   A CA  1 
ATOM   1577 C  C   . TYR   A 1 224 ? 1.39710   16.99695 2.40751   1.000 28.69019  ? 223 TYR   A C   1 
ATOM   1578 O  O   . TYR   A 1 224 ? 1.24773   16.25401 3.37911   1.000 27.77431  ? 223 TYR   A O   1 
ATOM   1579 C  CB  . TYR   A 1 224 ? 3.18720   18.69150 2.50761   1.000 28.14626  ? 223 TYR   A CB  1 
ATOM   1580 C  CG  . TYR   A 1 224 ? 3.58639   20.12687 2.59610   1.000 25.98048  ? 223 TYR   A CG  1 
ATOM   1581 C  CD1 . TYR   A 1 224 ? 3.74970   20.73618 3.83052   1.000 28.35581  ? 223 TYR   A CD1 1 
ATOM   1582 C  CD2 . TYR   A 1 224 ? 3.80010   20.88307 1.44518   1.000 29.60956  ? 223 TYR   A CD2 1 
ATOM   1583 C  CE1 . TYR   A 1 224 ? 4.10927   22.06751 3.92439   1.000 29.19298  ? 223 TYR   A CE1 1 
ATOM   1584 C  CE2 . TYR   A 1 224 ? 4.16771   22.21989 1.53093   1.000 33.10156  ? 223 TYR   A CE2 1 
ATOM   1585 C  CZ  . TYR   A 1 224 ? 4.32490   22.79956 2.78021   1.000 30.57809  ? 223 TYR   A CZ  1 
ATOM   1586 O  OH  . TYR   A 1 224 ? 4.68182   24.12645 2.91574   1.000 33.54576  ? 223 TYR   A OH  1 
ATOM   1587 N  N   . ARG   A 1 225 ? 1.36562   16.57327 1.14355   1.000 27.05160  ? 224 ARG   A N   1 
ATOM   1588 C  CA  . ARG   A 1 225 ? 1.41551   15.17094 0.76084   1.000 27.54122  ? 224 ARG   A CA  1 
ATOM   1589 C  C   . ARG   A 1 225 ? 2.79501   14.87200 0.18347   1.000 31.69296  ? 224 ARG   A C   1 
ATOM   1590 O  O   . ARG   A 1 225 ? 3.35701   15.69928 -0.53374  1.000 33.13187  ? 224 ARG   A O   1 
ATOM   1591 C  CB  . ARG   A 1 225 ? 0.34884   14.84445 -0.30587  1.000 31.63554  ? 224 ARG   A CB  1 
ATOM   1592 C  CG  . ARG   A 1 225 ? -1.10174  14.84460 0.18758   1.000 44.12405  ? 224 ARG   A CG  1 
ATOM   1593 C  CD  . ARG   A 1 225 ? -2.13006  14.86481 -0.94970  1.000 46.23869  ? 224 ARG   A CD  1 
ATOM   1594 N  NE  . ARG   A 1 225 ? -1.84938  13.89563 -2.00159  1.000 44.85203  ? 224 ARG   A NE  1 
ATOM   1595 C  CZ  . ARG   A 1 225 ? -2.40822  13.91789 -3.20641  1.000 52.32510  ? 224 ARG   A CZ  1 
ATOM   1596 N  NH1 . ARG   A 1 225 ? -3.31136  14.82873 -3.53253  1.000 45.26496  ? 224 ARG   A NH1 1 
ATOM   1597 N  NH2 . ARG   A 1 225 ? -2.05872  12.99950 -4.10394  1.000 52.91624  ? 224 ARG   A NH2 1 
ATOM   1598 N  N   . VAL   A 1 226 ? 3.35685   13.70905 0.50493   1.000 32.23292  ? 225 VAL   A N   1 
ATOM   1599 C  CA  A VAL   A 1 226 ? 4.56014   13.23226 -0.16442  0.631 35.91018  ? 225 VAL   A CA  1 
ATOM   1600 C  CA  B VAL   A 1 226 ? 4.56578   13.20183 -0.14732  0.369 35.94959  ? 225 VAL   A CA  1 
ATOM   1601 C  C   . VAL   A 1 226 ? 4.13829   12.23719 -1.23482  1.000 37.44248  ? 225 VAL   A C   1 
ATOM   1602 O  O   . VAL   A 1 226 ? 3.33963   11.32822 -0.98039  1.000 36.97596  ? 225 VAL   A O   1 
ATOM   1603 C  CB  A VAL   A 1 226 ? 5.56985   12.62543 0.82803   0.631 41.88139  ? 225 VAL   A CB  1 
ATOM   1604 C  CB  B VAL   A 1 226 ? 5.51298   12.50747 0.84793   0.369 41.81077  ? 225 VAL   A CB  1 
ATOM   1605 C  CG1 A VAL   A 1 226 ? 4.86223   11.80415 1.88297   0.631 47.09369  ? 225 VAL   A CG1 1 
ATOM   1606 C  CG1 B VAL   A 1 226 ? 6.12261   13.50741 1.74060   0.369 40.02566  ? 225 VAL   A CG1 1 
ATOM   1607 C  CG2 A VAL   A 1 226 ? 6.59894   11.77979 0.08308   0.631 39.86122  ? 225 VAL   A CG2 1 
ATOM   1608 C  CG2 B VAL   A 1 226 ? 4.77201   11.46407 1.67367   0.369 46.77776  ? 225 VAL   A CG2 1 
ATOM   1609 N  N   . LEU   A 1 227 ? 4.65893   12.42460 -2.44126  1.000 38.53219  ? 226 LEU   A N   1 
ATOM   1610 C  CA  . LEU   A 1 227 ? 4.15027   11.71106 -3.60123  1.000 40.67334  ? 226 LEU   A CA  1 
ATOM   1611 C  C   . LEU   A 1 227 ? 5.05408   10.55778 -4.02154  1.000 46.87568  ? 226 LEU   A C   1 
ATOM   1612 O  O   . LEU   A 1 227 ? 6.28145   10.68934 -4.05781  1.000 41.98036  ? 226 LEU   A O   1 
ATOM   1613 C  CB  . LEU   A 1 227 ? 3.96790   12.68028 -4.76268  1.000 37.09738  ? 226 LEU   A CB  1 
ATOM   1614 C  CG  . LEU   A 1 227 ? 2.99737   13.80686 -4.41385  1.000 36.97632  ? 226 LEU   A CG  1 
ATOM   1615 C  CD1 . LEU   A 1 227 ? 2.86819   14.71850 -5.60812  1.000 39.54740  ? 226 LEU   A CD1 1 
ATOM   1616 C  CD2 . LEU   A 1 227 ? 1.64978   13.25122 -4.01287  1.000 40.83493  ? 226 LEU   A CD2 1 
ATOM   1617 N  N   . GLU   A 1 228 ? 4.42728   9.42816  -4.36046  1.000 42.76716  ? 227 GLU   A N   1 
ATOM   1618 C  CA  . GLU   A 1 228 ? 5.16024   8.23591  -4.75697  1.000 50.64512  ? 227 GLU   A CA  1 
ATOM   1619 C  C   . GLU   A 1 228 ? 5.17054   8.11861  -6.27191  1.000 42.65226  ? 227 GLU   A C   1 
ATOM   1620 O  O   . GLU   A 1 228 ? 4.10975   7.87010  -6.87058  1.000 44.65970  ? 227 GLU   A O   1 
ATOM   1621 C  CB  . GLU   A 1 228 ? 4.54112   6.98752  -4.12677  1.000 52.32883  ? 227 GLU   A CB  1 
ATOM   1622 C  CG  . GLU   A 1 228 ? 4.14580   7.11347  -2.63746  1.000 49.75598  ? 227 GLU   A CG  1 
ATOM   1623 C  CD  . GLU   A 1 228 ? 5.29525   7.45310  -1.67637  0.000 47.47064  ? 227 GLU   A CD  1 
ATOM   1624 O  OE1 . GLU   A 1 228 ? 6.36152   7.95040  -2.09785  0.000 47.23235  ? 227 GLU   A OE1 1 
ATOM   1625 O  OE2 . GLU   A 1 228 ? 5.11920   7.21408  -0.46372  0.000 47.76493  ? 227 GLU   A OE2 1 
ATOM   1626 N  N   . PRO   A 1 229 ? 6.31958   8.28367  -6.92763  1.000 45.69216  ? 228 PRO   A N   1 
ATOM   1627 C  CA  . PRO   A 1 229 ? 6.37388   8.17198  -8.39474  1.000 45.34143  ? 228 PRO   A CA  1 
ATOM   1628 C  C   . PRO   A 1 229 ? 6.14670   6.74532  -8.87551  1.000 58.07647  ? 228 PRO   A C   1 
ATOM   1629 O  O   . PRO   A 1 229 ? 6.14695   5.78184  -8.10716  1.000 57.69224  ? 228 PRO   A O   1 
ATOM   1630 C  CB  . PRO   A 1 229 ? 7.79233   8.64353  -8.74155  1.000 49.30900  ? 228 PRO   A CB  1 
ATOM   1631 C  CG  . PRO   A 1 229 ? 8.26282   9.39366  -7.53733  1.000 52.70317  ? 228 PRO   A CG  1 
ATOM   1632 C  CD  . PRO   A 1 229 ? 7.60394   8.72685  -6.36445  1.000 48.50330  ? 228 PRO   A CD  1 
ATOM   1633 N  N   . VAL   A 1 230 ? 5.94270   6.62746  -10.18809 1.000 57.13619  ? 229 VAL   A N   1 
ATOM   1634 C  CA  . VAL   A 1 230 ? 5.85360   5.33253  -10.86078 1.000 61.88226  ? 229 VAL   A CA  1 
ATOM   1635 C  C   . VAL   A 1 230 ? 6.59629   5.38996  -12.19459 1.000 58.87591  ? 229 VAL   A C   1 
ATOM   1636 O  O   . VAL   A 1 230 ? 7.39437   6.29936  -12.43628 1.000 70.79331  ? 229 VAL   A O   1 
ATOM   1637 C  CB  . VAL   A 1 230 ? 4.38830   4.89117  -11.08128 1.000 60.39786  ? 229 VAL   A CB  1 
ATOM   1638 C  CG1 . VAL   A 1 230 ? 3.72568   4.54472  -9.76603  1.000 60.58632  ? 229 VAL   A CG1 1 
ATOM   1639 C  CG2 . VAL   A 1 230 ? 3.60509   5.96136  -11.79836 1.000 56.51721  ? 229 VAL   A CG2 1 
ATOM   1640 N  N   . ASP   A 1 241 ? 16.53611  4.66432  1.00174   1.000 68.79771  ? 240 ASP   A N   1 
ATOM   1641 C  CA  . ASP   A 1 241 ? 17.83586  5.12680  1.47773   1.000 75.77827  ? 240 ASP   A CA  1 
ATOM   1642 C  C   . ASP   A 1 241 ? 17.80411  6.63945  1.69958   1.000 69.11943  ? 240 ASP   A C   1 
ATOM   1643 O  O   . ASP   A 1 241 ? 17.34886  7.38699  0.83546   1.000 70.49864  ? 240 ASP   A O   1 
ATOM   1644 C  CB  . ASP   A 1 241 ? 18.93441  4.74875  0.48418   1.000 90.79845  ? 240 ASP   A CB  1 
ATOM   1645 C  CG  . ASP   A 1 241 ? 20.32619  4.92229  1.06010   1.000 99.26885  ? 240 ASP   A CG  1 
ATOM   1646 O  OD1 . ASP   A 1 241 ? 20.57797  4.40631  2.17210   1.000 95.50548  ? 240 ASP   A OD1 1 
ATOM   1647 O  OD2 . ASP   A 1 241 ? 21.16836  5.56713  0.39857   1.000 105.69503 ? 240 ASP   A OD2 1 
ATOM   1648 N  N   . LEU   A 1 242 ? 18.28974  7.09022  2.85700   1.000 65.39182  ? 241 LEU   A N   1 
ATOM   1649 C  CA  . LEU   A 1 242 ? 18.08911  8.47431  3.25421   1.000 57.12627  ? 241 LEU   A CA  1 
ATOM   1650 C  C   . LEU   A 1 242 ? 19.42097  9.18737  3.45583   1.000 58.49694  ? 241 LEU   A C   1 
ATOM   1651 O  O   . LEU   A 1 242 ? 20.39586  8.57258  3.89876   1.000 65.69022  ? 241 LEU   A O   1 
ATOM   1652 C  CB  . LEU   A 1 242 ? 17.27029  8.55449  4.54891   1.000 54.11373  ? 241 LEU   A CB  1 
ATOM   1653 C  CG  . LEU   A 1 242 ? 15.83671  8.03471  4.43534   1.000 53.48842  ? 241 LEU   A CG  1 
ATOM   1654 C  CD1 . LEU   A 1 242 ? 15.03956  8.37233  5.68210   1.000 50.69758  ? 241 LEU   A CD1 1 
ATOM   1655 C  CD2 . LEU   A 1 242 ? 15.15667  8.58603  3.19913   1.000 52.71745  ? 241 LEU   A CD2 1 
ATOM   1656 N  N   . PRO   A 1 243 ? 19.49466  10.49340 3.14882   1.000 52.80977  ? 242 PRO   A N   1 
ATOM   1657 C  CA  . PRO   A 1 243 ? 18.42887  11.35731 2.61163   1.000 49.83202  ? 242 PRO   A CA  1 
ATOM   1658 C  C   . PRO   A 1 243 ? 18.14541  11.10482 1.13385   1.000 55.56823  ? 242 PRO   A C   1 
ATOM   1659 O  O   . PRO   A 1 243 ? 19.05441  10.80550 0.36535   1.000 50.70257  ? 242 PRO   A O   1 
ATOM   1660 C  CB  . PRO   A 1 243 ? 18.98561  12.77081 2.82967   1.000 48.13529  ? 242 PRO   A CB  1 
ATOM   1661 C  CG  . PRO   A 1 243 ? 20.48027  12.59105 2.78508   1.000 47.79718  ? 242 PRO   A CG  1 
ATOM   1662 C  CD  . PRO   A 1 243 ? 20.72303  11.25686 3.43801   1.000 48.54408  ? 242 PRO   A CD  1 
ATOM   1663 N  N   . ARG   A 1 244 ? 16.89115  11.22178 0.70607   1.000 45.68938  ? 243 ARG   A N   1 
ATOM   1664 C  CA  A ARG   A 1 244 ? 16.53597  11.04375 -0.69233  0.807 48.10557  ? 243 ARG   A CA  1 
ATOM   1665 C  CA  B ARG   A 1 244 ? 16.53884  11.04635 -0.69468  0.193 48.08114  ? 243 ARG   A CA  1 
ATOM   1666 C  C   . ARG   A 1 244 ? 15.55147  12.12948 -1.09636  1.000 45.02570  ? 243 ARG   A C   1 
ATOM   1667 O  O   . ARG   A 1 244 ? 14.77067  12.61643 -0.27369  1.000 39.65080  ? 243 ARG   A O   1 
ATOM   1668 C  CB  A ARG   A 1 244 ? 15.94988  9.65003  -0.94749  0.807 49.73451  ? 243 ARG   A CB  1 
ATOM   1669 C  CB  B ARG   A 1 244 ? 15.93570  9.66342  -0.97228  0.193 49.73848  ? 243 ARG   A CB  1 
ATOM   1670 C  CG  A ARG   A 1 244 ? 14.45185  9.55334  -0.76002  0.807 49.08239  ? 243 ARG   A CG  1 
ATOM   1671 C  CG  B ARG   A 1 244 ? 14.67766  9.36794  -0.17933  0.193 48.93793  ? 243 ARG   A CG  1 
ATOM   1672 C  CD  A ARG   A 1 244 ? 13.87122  8.37268  -1.51584  0.807 52.49849  ? 243 ARG   A CD  1 
ATOM   1673 C  CD  B ARG   A 1 244 ? 14.08546  8.01871  -0.54351  0.193 50.33528  ? 243 ARG   A CD  1 
ATOM   1674 N  NE  A ARG   A 1 244 ? 12.56470  8.00562  -0.98495  0.807 50.66931  ? 243 ARG   A NE  1 
ATOM   1675 N  NE  B ARG   A 1 244 ? 12.85921  7.75630  0.19996   0.193 50.67819  ? 243 ARG   A NE  1 
ATOM   1676 C  CZ  A ARG   A 1 244 ? 12.38327  7.32760  0.14020   0.807 50.99739  ? 243 ARG   A CZ  1 
ATOM   1677 C  CZ  B ARG   A 1 244 ? 12.15441  6.63608  0.11846   0.193 50.40902  ? 243 ARG   A CZ  1 
ATOM   1678 N  NH1 A ARG   A 1 244 ? 13.40672  6.87936  0.85090   0.807 50.94515  ? 243 ARG   A NH1 1 
ATOM   1679 N  NH1 B ARG   A 1 244 ? 12.51301  5.64952  -0.68810  0.193 52.39261  ? 243 ARG   A NH1 1 
ATOM   1680 N  NH2 A ARG   A 1 244 ? 11.14573  7.09520  0.56507   0.807 46.34863  ? 243 ARG   A NH2 1 
ATOM   1681 N  NH2 B ARG   A 1 244 ? 11.05820  6.50491  0.85991   0.193 47.26635  ? 243 ARG   A NH2 1 
ATOM   1682 N  N   . GLU   A 1 245 ? 15.59825  12.51050 -2.37030  1.000 40.35546  ? 244 GLU   A N   1 
ATOM   1683 C  CA  . GLU   A 1 245 ? 14.69254  13.53915 -2.85982  1.000 41.00558  ? 244 GLU   A CA  1 
ATOM   1684 C  C   . GLU   A 1 245 ? 13.28458  12.96824 -2.96242  1.000 43.29539  ? 244 GLU   A C   1 
ATOM   1685 O  O   . GLU   A 1 245 ? 13.10134  11.79399 -3.29044  1.000 43.57841  ? 244 GLU   A O   1 
ATOM   1686 C  CB  . GLU   A 1 245 ? 15.16216  14.07383 -4.21718  1.000 46.00268  ? 244 GLU   A CB  1 
ATOM   1687 C  CG  . GLU   A 1 245 ? 14.15913  15.01136 -4.88636  1.000 56.79138  ? 244 GLU   A CG  1 
ATOM   1688 C  CD  . GLU   A 1 245 ? 14.04105  14.80095 -6.38071  0.000 54.25011  ? 244 GLU   A CD  1 
ATOM   1689 O  OE1 . GLU   A 1 245 ? 13.54809  13.73370 -6.80080  1.000 59.55937  ? 244 GLU   A OE1 1 
ATOM   1690 O  OE2 . GLU   A 1 245 ? 14.42830  15.71472 -7.13659  1.000 65.27866  ? 244 GLU   A OE2 1 
ATOM   1691 N  N   . VAL   A 1 246 ? 12.28763  13.79219 -2.62829  1.000 37.12991  ? 245 VAL   A N   1 
ATOM   1692 C  CA  . VAL   A 1 246 ? 10.88044  13.44036 -2.77291  1.000 38.40425  ? 245 VAL   A CA  1 
ATOM   1693 C  C   . VAL   A 1 246 ? 10.16110  14.60690 -3.43126  1.000 31.83633  ? 245 VAL   A C   1 
ATOM   1694 O  O   . VAL   A 1 246 ? 10.72995  15.68005 -3.63520  1.000 32.50103  ? 245 VAL   A O   1 
ATOM   1695 C  CB  . VAL   A 1 246 ? 10.20588  13.09410 -1.42790  1.000 35.53942  ? 245 VAL   A CB  1 
ATOM   1696 C  CG1 . VAL   A 1 246 ? 10.82862  11.85259 -0.82256  1.000 42.84035  ? 245 VAL   A CG1 1 
ATOM   1697 C  CG2 . VAL   A 1 246 ? 10.28071  14.28557 -0.45521  1.000 31.49873  ? 245 VAL   A CG2 1 
ATOM   1698 N  N   . TRP   A 1 247 ? 8.87787   14.39387 -3.73077  1.000 32.23039  ? 246 TRP   A N   1 
ATOM   1699 C  CA  . TRP   A 1 247 ? 8.00451   15.43772 -4.25049  1.000 29.59916  ? 246 TRP   A CA  1 
ATOM   1700 C  C   . TRP   A 1 247 ? 6.90781   15.75538 -3.24044  1.000 28.06961  ? 246 TRP   A C   1 
ATOM   1701 O  O   . TRP   A 1 247 ? 6.26983   14.84584 -2.70157  1.000 38.79940  ? 246 TRP   A O   1 
ATOM   1702 C  CB  . TRP   A 1 247 ? 7.39387   15.01875 -5.59940  1.000 32.59615  ? 246 TRP   A CB  1 
ATOM   1703 C  CG  . TRP   A 1 247 ? 8.43163   14.90026 -6.67534  1.000 32.32258  ? 246 TRP   A CG  1 
ATOM   1704 C  CD1 . TRP   A 1 247 ? 9.04561   13.75873 -7.10714  1.000 37.65563  ? 246 TRP   A CD1 1 
ATOM   1705 C  CD2 . TRP   A 1 247 ? 9.01165   15.97648 -7.41579  1.000 34.51086  ? 246 TRP   A CD2 1 
ATOM   1706 N  NE1 . TRP   A 1 247 ? 9.95936   14.06158 -8.09354  1.000 40.71009  ? 246 TRP   A NE1 1 
ATOM   1707 C  CE2 . TRP   A 1 247 ? 9.96013   15.41858 -8.29304  1.000 39.25356  ? 246 TRP   A CE2 1 
ATOM   1708 C  CE3 . TRP   A 1 247 ? 8.81180   17.36038 -7.42818  1.000 36.15324  ? 246 TRP   A CE3 1 
ATOM   1709 C  CZ2 . TRP   A 1 247 ? 10.70406  16.19551 -9.18061  1.000 42.60372  ? 246 TRP   A CZ2 1 
ATOM   1710 C  CZ3 . TRP   A 1 247 ? 9.55793   18.13015 -8.31002  1.000 44.30620  ? 246 TRP   A CZ3 1 
ATOM   1711 C  CH2 . TRP   A 1 247 ? 10.49120  17.54657 -9.16713  1.000 40.55620  ? 246 TRP   A CH2 1 
ATOM   1712 N  N   . LEU   A 1 248 ? 6.67121   17.04638 -3.02121  1.000 29.67845  ? 247 LEU   A N   1 
ATOM   1713 C  CA  . LEU   A 1 248 ? 5.75956   17.54121 -1.99877  1.000 31.54354  ? 247 LEU   A CA  1 
ATOM   1714 C  C   . LEU   A 1 248 ? 4.63315   18.33516 -2.63960  1.000 32.05081  ? 247 LEU   A C   1 
ATOM   1715 O  O   . LEU   A 1 248 ? 4.87943   19.19943 -3.48876  1.000 37.50263  ? 247 LEU   A O   1 
ATOM   1716 C  CB  . LEU   A 1 248 ? 6.49575   18.43698 -1.01098  1.000 29.49816  ? 247 LEU   A CB  1 
ATOM   1717 C  CG  . LEU   A 1 248 ? 7.59027   17.73318 -0.21280  1.000 31.81001  ? 247 LEU   A CG  1 
ATOM   1718 C  CD1 . LEU   A 1 248 ? 8.44232   18.75704 0.51672   1.000 30.74537  ? 247 LEU   A CD1 1 
ATOM   1719 C  CD2 . LEU   A 1 248 ? 6.95449   16.74525 0.74858   1.000 32.58137  ? 247 LEU   A CD2 1 
ATOM   1720 N  N   . LEU   A 1 249 ? 3.41158   18.08043 -2.19660  1.000 28.87002  ? 248 LEU   A N   1 
ATOM   1721 C  CA  . LEU   A 1 249 ? 2.23899   18.80227 -2.67108  1.000 27.12243  ? 248 LEU   A CA  1 
ATOM   1722 C  C   . LEU   A 1 249 ? 1.50178   19.38720 -1.47584  1.000 28.58713  ? 248 LEU   A C   1 
ATOM   1723 O  O   . LEU   A 1 249 ? 1.03008   18.63583 -0.61970  1.000 31.08634  ? 248 LEU   A O   1 
ATOM   1724 C  CB  . LEU   A 1 249 ? 1.32102   17.87077 -3.46112  1.000 30.78852  ? 248 LEU   A CB  1 
ATOM   1725 C  CG  . LEU   A 1 249 ? -0.00953  18.44518 -3.94121  1.000 31.37937  ? 248 LEU   A CG  1 
ATOM   1726 C  CD1 . LEU   A 1 249 ? 0.20933   19.61148 -4.90228  1.000 30.90901  ? 248 LEU   A CD1 1 
ATOM   1727 C  CD2 . LEU   A 1 249 ? -0.78861  17.34495 -4.60607  1.000 35.84290  ? 248 LEU   A CD2 1 
ATOM   1728 N  N   . GLU   A 1 250 ? 1.38242   20.71548 -1.43109  1.000 29.37738  ? 249 GLU   A N   1 
ATOM   1729 C  CA  . GLU   A 1 250 ? 0.61537   21.34812 -0.36370  1.000 31.80844  ? 249 GLU   A CA  1 
ATOM   1730 C  C   . GLU   A 1 250 ? -0.86316  20.99250 -0.49807  1.000 36.88323  ? 249 GLU   A C   1 
ATOM   1731 O  O   . GLU   A 1 250 ? -1.42276  20.97830 -1.59848  1.000 32.29668  ? 249 GLU   A O   1 
ATOM   1732 C  CB  . GLU   A 1 250 ? 0.79572   22.86474 -0.38897  1.000 32.89998  ? 249 GLU   A CB  1 
ATOM   1733 C  CG  . GLU   A 1 250 ? 0.11912   23.55274 0.81114   1.000 36.69231  ? 249 GLU   A CG  1 
ATOM   1734 C  CD  . GLU   A 1 250 ? 0.42401   25.03322 0.89995   1.000 43.29061  ? 249 GLU   A CD  1 
ATOM   1735 O  OE1 . GLU   A 1 250 ? 1.50570   25.45395 0.43496   1.000 53.22838  ? 249 GLU   A OE1 1 
ATOM   1736 O  OE2 . GLU   A 1 250 ? -0.40839  25.76933 1.46483   1.000 52.56170  ? 249 GLU   A OE2 1 
ATOM   1737 N  N   . THR   A 1 251 ? -1.50288  20.71984 0.63005   1.000 28.95346  ? 250 THR   A N   1 
ATOM   1738 C  CA  . THR   A 1 251 ? -2.83450  20.14325 0.63945   1.000 28.05937  ? 250 THR   A CA  1 
ATOM   1739 C  C   . THR   A 1 251 ? -3.58628  20.72769 1.82845   1.000 32.12044  ? 250 THR   A C   1 
ATOM   1740 O  O   . THR   A 1 251 ? -2.95417  21.18383 2.79244   1.000 27.05042  ? 250 THR   A O   1 
ATOM   1741 C  CB  . THR   A 1 251 ? -2.73021  18.60605 0.72573   1.000 33.23553  ? 250 THR   A CB  1 
ATOM   1742 O  OG1 . THR   A 1 251 ? -3.97697  17.99181 0.38139   1.000 42.50941  ? 250 THR   A OG1 1 
ATOM   1743 C  CG2 . THR   A 1 251 ? -2.29538  18.14461 2.13028   1.000 30.92051  ? 250 THR   A CG2 1 
ATOM   1744 N  N   . PRO   A 1 252 ? -4.91515  20.77882 1.77914   1.000 31.16050  ? 251 PRO   A N   1 
ATOM   1745 C  CA  . PRO   A 1 252 ? -5.65780  21.24778 2.95614   1.000 30.03734  ? 251 PRO   A CA  1 
ATOM   1746 C  C   . PRO   A 1 252 ? -5.52618  20.28327 4.12984   1.000 31.02716  ? 251 PRO   A C   1 
ATOM   1747 O  O   . PRO   A 1 252 ? -5.16193  19.11207 3.99396   1.000 28.41536  ? 251 PRO   A O   1 
ATOM   1748 C  CB  . PRO   A 1 252 ? -7.11057  21.36067 2.47289   1.000 39.10789  ? 251 PRO   A CB  1 
ATOM   1749 C  CG  . PRO   A 1 252 ? -7.17051  20.72653 1.12820   1.000 38.65447  ? 251 PRO   A CG  1 
ATOM   1750 C  CD  . PRO   A 1 252 ? -5.78463  20.51101 0.61448   1.000 35.75949  ? 251 PRO   A CD  1 
ATOM   1751 N  N   . GLN   A 1 253 ? -5.80024  20.81488 5.31805   1.000 31.23816  ? 252 GLN   A N   1 
ATOM   1752 C  CA  . GLN   A 1 253 ? -5.89060  19.96938 6.50061   1.000 26.08514  ? 252 GLN   A CA  1 
ATOM   1753 C  C   . GLN   A 1 253 ? -6.84345  18.81025 6.23832   1.000 31.41975  ? 252 GLN   A C   1 
ATOM   1754 O  O   . GLN   A 1 253 ? -7.98816  19.01820 5.82449   1.000 31.20261  ? 252 GLN   A O   1 
ATOM   1755 C  CB  . GLN   A 1 253 ? -6.38842  20.80614 7.67513   1.000 25.15273  ? 252 GLN   A CB  1 
ATOM   1756 C  CG  . GLN   A 1 253 ? -6.37174  20.10254 9.01452   1.000 25.50291  ? 252 GLN   A CG  1 
ATOM   1757 C  CD  . GLN   A 1 253 ? -7.02064  20.94988 10.07298  1.000 26.14190  ? 252 GLN   A CD  1 
ATOM   1758 O  OE1 . GLN   A 1 253 ? -6.84380  22.17006 10.09756  1.000 27.60424  ? 252 GLN   A OE1 1 
ATOM   1759 N  NE2 . GLN   A 1 253 ? -7.80707  20.31773 10.94155  1.000 25.88216  ? 252 GLN   A NE2 1 
ATOM   1760 N  N   . ALA   A 1 254 ? -6.36318  17.58871 6.47949   1.000 28.18557  ? 253 ALA   A N   1 
ATOM   1761 C  CA  . ALA   A 1 254 ? -7.14514  16.38921 6.19724   1.000 31.96158  ? 253 ALA   A CA  1 
ATOM   1762 C  C   . ALA   A 1 254 ? -8.48761  16.41747 6.92069   1.000 33.46055  ? 253 ALA   A C   1 
ATOM   1763 O  O   . ALA   A 1 254 ? -8.60468  16.91458 8.04664   1.000 30.05134  ? 253 ALA   A O   1 
ATOM   1764 C  CB  . ALA   A 1 254 ? -6.36624  15.14187 6.61797   1.000 32.06738  ? 253 ALA   A CB  1 
ATOM   1765 N  N   . ASP   A 1 255 ? -9.51034  15.85019 6.26744   1.000 30.34385  ? 254 ASP   A N   1 
ATOM   1766 C  CA  . ASP   A 1 255 ? -10.85271 15.85136 6.84182   1.000 32.48399  ? 254 ASP   A CA  1 
ATOM   1767 C  C   . ASP   A 1 255 ? -10.91655 15.06779 8.14532   1.000 33.67639  ? 254 ASP   A C   1 
ATOM   1768 O  O   . ASP   A 1 255 ? -11.70999 15.40614 9.03472   1.000 37.19893  ? 254 ASP   A O   1 
ATOM   1769 C  CB  . ASP   A 1 255 ? -11.85938 15.25755 5.85356   1.000 38.97686  ? 254 ASP   A CB  1 
ATOM   1770 C  CG  . ASP   A 1 255 ? -12.64371 16.31392 5.10810   1.000 46.68455  ? 254 ASP   A CG  1 
ATOM   1771 O  OD1 . ASP   A 1 255 ? -12.61484 17.50232 5.50510   1.000 43.63597  ? 254 ASP   A OD1 1 
ATOM   1772 O  OD2 . ASP   A 1 255 ? -13.31492 15.94169 4.12237   1.000 56.72685  ? 254 ASP   A OD2 1 
ATOM   1773 N  N   . ASP   A 1 256 ? -10.12199 14.00485 8.27553   1.000 28.67739  ? 255 ASP   A N   1 
ATOM   1774 C  CA  . ASP   A 1 256 ? -10.17022 13.19294 9.47926   1.000 30.97698  ? 255 ASP   A CA  1 
ATOM   1775 C  C   . ASP   A 1 256 ? -9.14339  13.60632 10.51837  1.000 27.77546  ? 255 ASP   A C   1 
ATOM   1776 O  O   . ASP   A 1 256 ? -9.01032  12.91245 11.53211  1.000 30.82906  ? 255 ASP   A O   1 
ATOM   1777 C  CB  . ASP   A 1 256 ? -10.00233 11.70872 9.14574   1.000 32.77225  ? 255 ASP   A CB  1 
ATOM   1778 C  CG  . ASP   A 1 256 ? -8.69436  11.40114 8.43074   1.000 41.48560  ? 255 ASP   A CG  1 
ATOM   1779 O  OD1 . ASP   A 1 256 ? -7.98603  12.34598 8.02089   1.000 39.39679  ? 255 ASP   A OD1 1 
ATOM   1780 O  OD2 . ASP   A 1 256 ? -8.38451  10.19762 8.27317   1.000 49.39236  ? 255 ASP   A OD2 1 
ATOM   1781 N  N   . PHE   A 1 257 ? -8.43769  14.72106 10.31237  1.000 26.22290  ? 256 PHE   A N   1 
ATOM   1782 C  CA  . PHE   A 1 257 ? -7.51784  15.23418 11.32170  1.000 24.23937  ? 256 PHE   A CA  1 
ATOM   1783 C  C   . PHE   A 1 257 ? -8.01112  16.56288 11.88164  1.000 22.73221  ? 256 PHE   A C   1 
ATOM   1784 O  O   . PHE   A 1 257 ? -8.29564  17.49821 11.12583  1.000 23.51639  ? 256 PHE   A O   1 
ATOM   1785 C  CB  . PHE   A 1 257 ? -6.10310  15.42672 10.76958  1.000 22.26193  ? 256 PHE   A CB  1 
ATOM   1786 C  CG  . PHE   A 1 257 ? -5.21091  16.16897 11.73339  1.000 21.60333  ? 256 PHE   A CG  1 
ATOM   1787 C  CD1 . PHE   A 1 257 ? -4.83789  15.57361 12.92316  1.000 24.10503  ? 256 PHE   A CD1 1 
ATOM   1788 C  CD2 . PHE   A 1 257 ? -4.81548  17.46966 11.49410  1.000 22.86507  ? 256 PHE   A CD2 1 
ATOM   1789 C  CE1 . PHE   A 1 257 ? -4.05570  16.24951 13.84211  1.000 22.38603  ? 256 PHE   A CE1 1 
ATOM   1790 C  CE2 . PHE   A 1 257 ? -4.01598  18.15178 12.42287  1.000 21.64580  ? 256 PHE   A CE2 1 
ATOM   1791 C  CZ  . PHE   A 1 257 ? -3.63981  17.54312 13.58274  1.000 23.30513  ? 256 PHE   A CZ  1 
ATOM   1792 N  N   . TRP   A 1 258 ? -8.11885  16.63770 13.20750  1.000 22.06829  ? 257 TRP   A N   1 
ATOM   1793 C  CA  . TRP   A 1 258 ? -8.17886  17.91639 13.89728  1.000 21.41427  ? 257 TRP   A CA  1 
ATOM   1794 C  C   . TRP   A 1 258 ? -7.80733  17.65490 15.34018  1.000 18.23450  ? 257 TRP   A C   1 
ATOM   1795 O  O   . TRP   A 1 258 ? -7.67320  16.49877 15.76898  1.000 20.07207  ? 257 TRP   A O   1 
ATOM   1796 C  CB  . TRP   A 1 258 ? -9.55088  18.60718 13.77857  1.000 26.38275  ? 257 TRP   A CB  1 
ATOM   1797 C  CG  . TRP   A 1 258 ? -10.65361 18.05512 14.63829  1.000 31.15503  ? 257 TRP   A CG  1 
ATOM   1798 C  CD1 . TRP   A 1 258 ? -11.16197 18.60841 15.80387  1.000 30.94353  ? 257 TRP   A CD1 1 
ATOM   1799 C  CD2 . TRP   A 1 258 ? -11.41260 16.86596 14.40539  1.000 29.82581  ? 257 TRP   A CD2 1 
ATOM   1800 N  NE1 . TRP   A 1 258 ? -12.17548 17.83348 16.28593  1.000 27.12923  ? 257 TRP   A NE1 1 
ATOM   1801 C  CE2 . TRP   A 1 258 ? -12.34821 16.75673 15.45264  1.000 28.60016  ? 257 TRP   A CE2 1 
ATOM   1802 C  CE3 . TRP   A 1 258 ? -11.38908 15.87840 13.41505  1.000 29.02122  ? 257 TRP   A CE3 1 
ATOM   1803 C  CZ2 . TRP   A 1 258 ? -13.25181 15.69628 15.53550  1.000 34.63952  ? 257 TRP   A CZ2 1 
ATOM   1804 C  CZ3 . TRP   A 1 258 ? -12.28184 14.82988 13.50224  1.000 34.02337  ? 257 TRP   A CZ3 1 
ATOM   1805 C  CH2 . TRP   A 1 258 ? -13.19989 14.74629 14.55357  1.000 35.43516  ? 257 TRP   A CH2 1 
ATOM   1806 N  N   . CYS   A 1 259 ? -7.61590  18.74061 16.07704  1.000 20.76236  ? 258 CYS   A N   1 
ATOM   1807 C  CA  . CYS   A 1 259 ? -7.09531  18.63292 17.42314  1.000 19.96763  ? 258 CYS   A CA  1 
ATOM   1808 C  C   . CYS   A 1 259 ? -7.92050  19.55494 18.31015  1.000 27.21630  ? 258 CYS   A C   1 
ATOM   1809 O  O   . CYS   A 1 259 ? -8.17593  20.70355 17.93040  1.000 25.59488  ? 258 CYS   A O   1 
ATOM   1810 C  CB  . CYS   A 1 259 ? -5.60879  19.02266 17.41799  1.000 21.28610  ? 258 CYS   A CB  1 
ATOM   1811 S  SG  . CYS   A 1 259 ? -4.84632  19.12999 19.04811  1.000 24.14481  ? 258 CYS   A SG  1 
ATOM   1812 N  N   . GLU   A 1 260 ? -8.36470  19.05560 19.47196  1.000 21.18285  ? 259 GLU   A N   1 
ATOM   1813 C  CA  . GLU   A 1 260 ? -9.16123  19.84261 20.40756  1.000 23.00797  ? 259 GLU   A CA  1 
ATOM   1814 C  C   . GLU   A 1 260 ? -8.38983  19.97990 21.70583  1.000 22.90160  ? 259 GLU   A C   1 
ATOM   1815 O  O   . GLU   A 1 260 ? -7.62806  19.09119 22.06984  1.000 21.61117  ? 259 GLU   A O   1 
ATOM   1816 C  CB  . GLU   A 1 260 ? -10.51895 19.19620 20.71761  1.000 25.70310  ? 259 GLU   A CB  1 
ATOM   1817 C  CG  . GLU   A 1 260 ? -11.56676 19.40798 19.64516  1.000 34.36720  ? 259 GLU   A CG  1 
ATOM   1818 C  CD  . GLU   A 1 260 ? -12.79313 18.54300 19.87051  1.000 42.54468  ? 259 GLU   A CD  1 
ATOM   1819 O  OE1 . GLU   A 1 260 ? -13.11245 18.28485 21.05160  1.000 40.60097  ? 259 GLU   A OE1 1 
ATOM   1820 O  OE2 . GLU   A 1 260 ? -13.43895 18.14341 18.86912  1.000 40.63355  ? 259 GLU   A OE2 1 
ATOM   1821 N  N   . GLY   A 1 261 ? -8.60858  21.07306 22.41748  1.000 22.41384  ? 260 GLY   A N   1 
ATOM   1822 C  CA  . GLY   A 1 261 ? -7.97403  21.21956 23.71963  1.000 21.84499  ? 260 GLY   A CA  1 
ATOM   1823 C  C   . GLY   A 1 261 ? -8.56676  20.28980 24.76288  1.000 24.80154  ? 260 GLY   A C   1 
ATOM   1824 O  O   . GLY   A 1 261 ? -9.73342  19.89373 24.70002  1.000 24.77731  ? 260 GLY   A O   1 
ATOM   1825 N  N   . GLU   A 1 262 ? -7.76039  19.94878 25.75865  1.000 21.80429  ? 261 GLU   A N   1 
ATOM   1826 C  CA  . GLU   A 1 262 ? -8.27082  19.30698 26.96222  1.000 24.77450  ? 261 GLU   A CA  1 
ATOM   1827 C  C   . GLU   A 1 262 ? -7.47968  19.84101 28.14112  1.000 21.89571  ? 261 GLU   A C   1 
ATOM   1828 O  O   . GLU   A 1 262 ? -6.40226  20.41343 27.95624  1.000 20.89648  ? 261 GLU   A O   1 
ATOM   1829 C  CB  . GLU   A 1 262 ? -8.18765  17.77780 26.88425  1.000 24.57670  ? 261 GLU   A CB  1 
ATOM   1830 C  CG  . GLU   A 1 262 ? -6.79216  17.16814 26.96666  1.000 26.47901  ? 261 GLU   A CG  1 
ATOM   1831 C  CD  . GLU   A 1 262 ? -6.85416  15.65597 27.13631  1.000 29.49694  ? 261 GLU   A CD  1 
ATOM   1832 O  OE1 . GLU   A 1 262 ? -7.17227  15.17880 28.25403  1.000 27.88470  ? 261 GLU   A OE1 1 
ATOM   1833 O  OE2 . GLU   A 1 262 ? -6.57446  14.93566 26.15702  1.000 27.38847  ? 261 GLU   A OE2 1 
ATOM   1834 N  N   . PRO   A 1 263 ? -8.02279  19.74489 29.35838  1.000 23.44858  ? 262 PRO   A N   1 
ATOM   1835 C  CA  . PRO   A 1 263 ? -7.34930  20.37088 30.50436  1.000 24.56453  ? 262 PRO   A CA  1 
ATOM   1836 C  C   . PRO   A 1 263 ? -5.97386  19.78557 30.77367  1.000 23.31834  ? 262 PRO   A C   1 
ATOM   1837 O  O   . PRO   A 1 263 ? -5.75986  18.57750 30.68652  1.000 24.80721  ? 262 PRO   A O   1 
ATOM   1838 C  CB  . PRO   A 1 263 ? -8.30396  20.09481 31.67509  1.000 26.45826  ? 262 PRO   A CB  1 
ATOM   1839 C  CG  . PRO   A 1 263 ? -9.63949  19.98711 31.02768  1.000 25.95536  ? 262 PRO   A CG  1 
ATOM   1840 C  CD  . PRO   A 1 263 ? -9.40281  19.33717 29.68762  1.000 25.41635  ? 262 PRO   A CD  1 
ATOM   1841 N  N   . TYR   A 1 264 ? -5.04716  20.67110 31.11854  1.000 22.14477  ? 263 TYR   A N   1 
ATOM   1842 C  CA  . TYR   A 1 264 ? -3.70748  20.28558 31.52950  1.000 20.89131  ? 263 TYR   A CA  1 
ATOM   1843 C  C   . TYR   A 1 264 ? -3.70600  19.99059 33.03128  1.000 23.97700  ? 263 TYR   A C   1 
ATOM   1844 O  O   . TYR   A 1 264 ? -4.06346  20.87500 33.81303  1.000 22.25502  ? 263 TYR   A O   1 
ATOM   1845 C  CB  . TYR   A 1 264 ? -2.75237  21.42255 31.21328  1.000 17.36770  ? 263 TYR   A CB  1 
ATOM   1846 C  CG  . TYR   A 1 264 ? -1.42721  21.30895 31.88292  1.000 19.46236  ? 263 TYR   A CG  1 
ATOM   1847 C  CD1 . TYR   A 1 264 ? -0.63876  20.18557 31.69878  1.000 19.54326  ? 263 TYR   A CD1 1 
ATOM   1848 C  CD2 . TYR   A 1 264 ? -0.95633  22.33169 32.70542  1.000 21.16063  ? 263 TYR   A CD2 1 
ATOM   1849 C  CE1 . TYR   A 1 264 ? 0.59386   20.06525 32.33803  1.000 20.32550  ? 263 TYR   A CE1 1 
ATOM   1850 C  CE2 . TYR   A 1 264 ? 0.27357   22.22259 33.35805  1.000 23.30039  ? 263 TYR   A CE2 1 
ATOM   1851 C  CZ  . TYR   A 1 264 ? 1.04189   21.09300 33.15934  1.000 20.42978  ? 263 TYR   A CZ  1 
ATOM   1852 O  OH  . TYR   A 1 264 ? 2.25994   20.97238 33.79766  1.000 20.94656  ? 263 TYR   A OH  1 
ATOM   1853 N  N   . PRO   A 1 265 ? -3.32309  18.78629 33.47814  1.000 20.63049  ? 264 PRO   A N   1 
ATOM   1854 C  CA  . PRO   A 1 265 ? -3.41939  18.44305 34.90892  1.000 21.54838  ? 264 PRO   A CA  1 
ATOM   1855 C  C   . PRO   A 1 265 ? -2.18209  18.72375 35.74752  1.000 26.45959  ? 264 PRO   A C   1 
ATOM   1856 O  O   . PRO   A 1 265 ? -2.23370  18.53156 36.97294  1.000 23.49005  ? 264 PRO   A O   1 
ATOM   1857 C  CB  . PRO   A 1 265 ? -3.66224  16.92776 34.86825  1.000 23.73975  ? 264 PRO   A CB  1 
ATOM   1858 C  CG  . PRO   A 1 265 ? -2.85018  16.50294 33.63436  1.000 21.84121  ? 264 PRO   A CG  1 
ATOM   1859 C  CD  . PRO   A 1 265 ? -3.11382  17.59090 32.63386  1.000 23.81818  ? 264 PRO   A CD  1 
ATOM   1860 N  N   . GLY   A 1 266 ? -1.08114  19.15069 35.14896  1.000 21.45978  ? 265 GLY   A N   1 
ATOM   1861 C  CA  . GLY   A 1 266 ? 0.17512   19.18216 35.85395  1.000 24.01824  ? 265 GLY   A CA  1 
ATOM   1862 C  C   . GLY   A 1 266 ? 0.47438   20.48645 36.56185  1.000 23.38896  ? 265 GLY   A C   1 
ATOM   1863 O  O   . GLY   A 1 266 ? -0.35025  21.40521 36.64682  1.000 22.51039  ? 265 GLY   A O   1 
ATOM   1864 N  N   . PRO   A 1 267 ? 1.68730   20.57306 37.09840  1.000 23.81481  ? 266 PRO   A N   1 
ATOM   1865 C  CA  . PRO   A 1 267 ? 2.11391   21.79703 37.78502  1.000 26.29413  ? 266 PRO   A CA  1 
ATOM   1866 C  C   . PRO   A 1 267 ? 2.01782   23.00337 36.86898  1.000 26.71469  ? 266 PRO   A C   1 
ATOM   1867 O  O   . PRO   A 1 267 ? 2.31684   22.93163 35.67432  1.000 25.15146  ? 266 PRO   A O   1 
ATOM   1868 C  CB  . PRO   A 1 267 ? 3.56963   21.50419 38.16863  1.000 25.72762  ? 266 PRO   A CB  1 
ATOM   1869 C  CG  . PRO   A 1 267 ? 3.68869   19.98656 38.13830  1.000 24.56350  ? 266 PRO   A CG  1 
ATOM   1870 C  CD  . PRO   A 1 267 ? 2.73157   19.53754 37.05399  1.000 23.00285  ? 266 PRO   A CD  1 
ATOM   1871 N  N   . LYS   A 1 268 ? 1.62340   24.13236 37.44169  1.000 25.24318  ? 267 LYS   A N   1 
ATOM   1872 C  CA  . LYS   A 1 268 ? 1.31644   25.28259 36.61316  1.000 31.61832  ? 267 LYS   A CA  1 
ATOM   1873 C  C   . LYS   A 1 268 ? 2.53888   26.16697 36.41751  1.000 34.76171  ? 267 LYS   A C   1 
ATOM   1874 O  O   . LYS   A 1 268 ? 3.41784   26.26817 37.28479  1.000 32.72797  ? 267 LYS   A O   1 
ATOM   1875 C  CB  . LYS   A 1 268 ? 0.15951   26.08087 37.20890  1.000 31.91868  ? 267 LYS   A CB  1 
ATOM   1876 C  CG  . LYS   A 1 268 ? -1.00301  25.21301 37.63556  1.000 33.05875  ? 267 LYS   A CG  1 
ATOM   1877 C  CD  . LYS   A 1 268 ? -1.58261  24.43654 36.45293  1.000 34.51920  ? 267 LYS   A CD  1 
ATOM   1878 C  CE  . LYS   A 1 268 ? -2.70706  23.50032 36.90455  1.000 32.97500  ? 267 LYS   A CE  1 
ATOM   1879 N  NZ  . LYS   A 1 268 ? -2.96639  22.41614 35.89768  1.000 25.64274  ? 267 LYS   A NZ  1 
ATOM   1880 N  N   . VAL   A 1 269 ? 2.60918   26.77821 35.24126  1.000 27.41205  ? 268 VAL   A N   1 
ATOM   1881 C  CA  . VAL   A 1 269 ? 3.66187   27.73606 34.94298  1.000 29.77255  ? 268 VAL   A CA  1 
ATOM   1882 C  C   . VAL   A 1 269 ? 3.11863   29.11787 35.28961  1.000 35.74179  ? 268 VAL   A C   1 
ATOM   1883 O  O   . VAL   A 1 269 ? 2.06224   29.51918 34.78714  1.000 37.63016  ? 268 VAL   A O   1 
ATOM   1884 C  CB  . VAL   A 1 269 ? 4.11135   27.63652 33.47725  1.000 31.89135  ? 268 VAL   A CB  1 
ATOM   1885 C  CG1 . VAL   A 1 269 ? 5.06980   28.76409 33.13289  1.000 32.47982  ? 268 VAL   A CG1 1 
ATOM   1886 C  CG2 . VAL   A 1 269 ? 4.77495   26.29865 33.23280  1.000 26.72226  ? 268 VAL   A CG2 1 
ATOM   1887 N  N   . PHE   A 1 270 ? 3.82012   29.81948 36.18360  1.000 38.52480  ? 269 PHE   A N   1 
ATOM   1888 C  CA  A PHE   A 1 270 ? 3.47119   31.09199 36.82502  0.434 42.84682  ? 269 PHE   A CA  1 
ATOM   1889 C  CA  B PHE   A 1 270 ? 3.40530   31.09733 36.71998  0.566 42.80947  ? 269 PHE   A CA  1 
ATOM   1890 C  C   . PHE   A 1 270 ? 4.36847   32.19492 36.29144  1.000 44.53776  ? 269 PHE   A C   1 
ATOM   1891 O  O   . PHE   A 1 270 ? 5.58212   31.98219 36.21814  1.000 43.14581  ? 269 PHE   A O   1 
ATOM   1892 C  CB  A PHE   A 1 270 ? 3.67562   31.04961 38.34884  0.434 44.12017  ? 269 PHE   A CB  1 
ATOM   1893 C  CB  B PHE   A 1 270 ? 3.30342   31.07360 38.25668  0.566 43.69798  ? 269 PHE   A CB  1 
ATOM   1894 C  CG  A PHE   A 1 270 ? 2.75526   30.13243 39.10011  0.434 46.43697  ? 269 PHE   A CG  1 
ATOM   1895 C  CG  B PHE   A 1 270 ? 4.60210   30.75692 38.97344  0.566 46.35378  ? 269 PHE   A CG  1 
ATOM   1896 C  CD1 A PHE   A 1 270 ? 2.84430   28.75989 38.95499  0.434 39.68258  ? 269 PHE   A CD1 1 
ATOM   1897 C  CD1 B PHE   A 1 270 ? 5.47527   31.77156 39.34520  0.566 48.51286  ? 269 PHE   A CD1 1 
ATOM   1898 C  CD2 A PHE   A 1 270 ? 1.87595   30.64360 40.04173  0.434 50.09145  ? 269 PHE   A CD2 1 
ATOM   1899 C  CD2 B PHE   A 1 270 ? 4.93272   29.44980 39.30138  0.566 47.20743  ? 269 PHE   A CD2 1 
ATOM   1900 C  CE1 A PHE   A 1 270 ? 2.02481   27.91574 39.67775  0.434 43.37289  ? 269 PHE   A CE1 1 
ATOM   1901 C  CE1 B PHE   A 1 270 ? 6.66013   31.48853 40.01388  0.566 49.53757  ? 269 PHE   A CE1 1 
ATOM   1902 C  CE2 A PHE   A 1 270 ? 1.05768   29.80790 40.77561  0.434 53.10808  ? 269 PHE   A CE2 1 
ATOM   1903 C  CE2 B PHE   A 1 270 ? 6.11619   29.15942 39.97200  0.566 48.38760  ? 269 PHE   A CE2 1 
ATOM   1904 C  CZ  A PHE   A 1 270 ? 1.13209   28.44068 40.59464  0.434 50.16924  ? 269 PHE   A CZ  1 
ATOM   1905 C  CZ  B PHE   A 1 270 ? 6.97826   30.18034 40.32963  0.566 46.27798  ? 269 PHE   A CZ  1 
ATOM   1906 N  N   . PRO   A 1 271 ? 3.83851   33.38389 35.96728  1.000 43.86061  ? 270 PRO   A N   1 
ATOM   1907 C  CA  . PRO   A 1 271 ? 4.69245   34.52339 35.62292  1.000 49.94740  ? 270 PRO   A CA  1 
ATOM   1908 C  C   . PRO   A 1 271 ? 5.63136   34.89388 36.76530  0.000 50.25379  ? 270 PRO   A C   1 
ATOM   1909 O  O   . PRO   A 1 271 ? 5.29448   34.73293 37.93852  0.000 50.31299  ? 270 PRO   A O   1 
ATOM   1910 C  CB  . PRO   A 1 271 ? 3.69203   35.64961 35.36610  1.000 48.76030  ? 270 PRO   A CB  1 
ATOM   1911 C  CG  . PRO   A 1 271 ? 2.44196   34.95975 34.98835  1.000 52.37123  ? 270 PRO   A CG  1 
ATOM   1912 C  CD  . PRO   A 1 271 ? 2.41373   33.66703 35.73980  1.000 39.72824  ? 270 PRO   A CD  1 
ATOM   1913 O  OXT . PRO   A 1 271 ? 6.74304   35.36611 36.54371  1.000 60.65443  ? 270 PRO   A OXT 1 
HETATM 1914 C  C   . ACE   B 2 1   ? -16.11196 24.29266 11.70427  1.000 49.07133  ? 0   ACE   B C   1 
HETATM 1915 O  O   . ACE   B 2 1   ? -16.95654 24.97555 11.11534  1.000 46.17850  ? 0   ACE   B O   1 
HETATM 1916 C  CH3 . ACE   B 2 1   ? -16.17806 22.80061 11.83344  1.000 43.97772  ? 0   ACE   B CH3 1 
ATOM   1917 N  N   . TYR   B 2 2   ? -15.05082 24.82212 12.28184  1.000 38.89922  ? 1   TYR   B N   1 
ATOM   1918 C  CA  . TYR   B 2 2   ? -14.78762 26.24810 12.29056  1.000 43.57273  ? 1   TYR   B CA  1 
ATOM   1919 C  C   . TYR   B 2 2   ? -13.26823 26.42970 12.26124  1.000 39.21119  ? 1   TYR   B C   1 
ATOM   1920 O  O   . TYR   B 2 2   ? -12.53491 25.51890 12.62165  1.000 35.42260  ? 1   TYR   B O   1 
ATOM   1921 C  CB  . TYR   B 2 2   ? -15.42445 26.90101 13.53146  1.000 37.94970  ? 1   TYR   B CB  1 
ATOM   1922 C  CG  . TYR   B 2 2   ? -14.95148 26.33411 14.84993  1.000 42.82552  ? 1   TYR   B CG  1 
ATOM   1923 C  CD1 . TYR   B 2 2   ? -13.76186 26.76119 15.41574  1.000 41.92613  ? 1   TYR   B CD1 1 
ATOM   1924 C  CD2 . TYR   B 2 2   ? -15.67744 25.35665 15.51864  1.000 40.79012  ? 1   TYR   B CD2 1 
ATOM   1925 C  CE1 . TYR   B 2 2   ? -13.30440 26.24284 16.60869  1.000 42.56785  ? 1   TYR   B CE1 1 
ATOM   1926 C  CE2 . TYR   B 2 2   ? -15.21913 24.82483 16.73120  1.000 42.12156  ? 1   TYR   B CE2 1 
ATOM   1927 C  CZ  . TYR   B 2 2   ? -14.03159 25.27875 17.26496  1.000 43.42589  ? 1   TYR   B CZ  1 
ATOM   1928 O  OH  . TYR   B 2 2   ? -13.54330 24.77927 18.46378  1.000 42.43427  ? 1   TYR   B OH  1 
ATOM   1929 N  N   . ILE   B 2 3   ? -12.78588 27.58303 11.82641  1.000 40.17106  ? 2   ILE   B N   1 
ATOM   1930 C  CA  . ILE   B 2 3   ? -11.34826 27.83847 11.76579  1.000 37.38765  ? 2   ILE   B CA  1 
ATOM   1931 C  C   . ILE   B 2 3   ? -10.97349 28.76537 12.90971  1.000 43.05363  ? 2   ILE   B C   1 
ATOM   1932 O  O   . ILE   B 2 3   ? -11.65619 29.76476 13.16307  1.000 44.81123  ? 2   ILE   B O   1 
ATOM   1933 C  CB  . ILE   B 2 3   ? -10.93397 28.40579 10.39544  1.000 41.73069  ? 2   ILE   B CB  1 
ATOM   1934 C  CG1 . ILE   B 2 3   ? -11.19391 27.35455 9.30862   1.000 45.01104  ? 2   ILE   B CG1 1 
ATOM   1935 C  CG2 . ILE   B 2 3   ? -9.46381  28.82438 10.38588  1.000 38.09193  ? 2   ILE   B CG2 1 
ATOM   1936 C  CD1 . ILE   B 2 3   ? -12.00018 27.85053 8.13659   1.000 56.34645  ? 2   ILE   B CD1 1 
ATOM   1937 N  N   . VAL   B 2 4   ? -9.92708  28.39837 13.64139  1.000 35.30244  ? 3   VAL   B N   1 
ATOM   1938 C  CA  . VAL   B 2 4   ? -9.40052  29.21439 14.72473  1.000 33.13256  ? 3   VAL   B CA  1 
ATOM   1939 C  C   . VAL   B 2 4   ? -7.92927  29.46875 14.44246  1.000 35.00285  ? 3   VAL   B C   1 
ATOM   1940 O  O   . VAL   B 2 4   ? -7.21579  28.56942 13.98191  1.000 31.42924  ? 3   VAL   B O   1 
ATOM   1941 C  CB  . VAL   B 2 4   ? -9.59569  28.53931 16.10182  1.000 40.73593  ? 3   VAL   B CB  1 
ATOM   1942 C  CG1 . VAL   B 2 4   ? -9.17051  27.08653 16.05093  1.000 39.67853  ? 3   VAL   B CG1 1 
ATOM   1943 C  CG2 . VAL   B 2 4   ? -8.81060  29.27669 17.16738  1.000 41.47443  ? 3   VAL   B CG2 1 
ATOM   1944 N  N   . LYS   B 2 5   ? -7.47962  30.70105 14.68150  1.000 33.70997  ? 4   LYS   B N   1 
ATOM   1945 C  CA  . LYS   B 2 5   ? -6.06124  31.02589 14.55133  1.000 34.72617  ? 4   LYS   B CA  1 
ATOM   1946 C  C   . LYS   B 2 5   ? -5.38910  30.64641 15.86164  1.000 36.53891  ? 4   LYS   B C   1 
ATOM   1947 O  O   . LYS   B 2 5   ? -5.45709  31.38405 16.84475  1.000 41.88344  ? 4   LYS   B O   1 
ATOM   1948 C  CB  . LYS   B 2 5   ? -5.84792  32.50051 14.21994  1.000 40.59571  ? 4   LYS   B CB  1 
ATOM   1949 C  CG  . LYS   B 2 5   ? -6.39019  32.94058 12.87650  1.000 47.50093  ? 4   LYS   B CG  1 
ATOM   1950 C  CD  . LYS   B 2 5   ? -6.41055  34.45598 12.81571  1.000 54.97579  ? 4   LYS   B CD  1 
ATOM   1951 C  CE  . LYS   B 2 5   ? -7.72061  34.99340 12.27601  1.000 64.69005  ? 4   LYS   B CE  1 
ATOM   1952 N  NZ  . LYS   B 2 5   ? -7.98796  36.36736 12.81263  1.000 67.82999  ? 4   LYS   B NZ  1 
ATOM   1953 N  N   . THR   B 2 6   ? -4.75336  29.48296 15.88422  1.000 28.90404  ? 5   THR   B N   1 
ATOM   1954 C  CA  . THR   B 2 6   ? -4.06441  28.99515 17.06338  1.000 29.56558  ? 5   THR   B CA  1 
ATOM   1955 C  C   . THR   B 2 6   ? -2.57983  29.30714 16.96097  1.000 31.10377  ? 5   THR   B C   1 
ATOM   1956 O  O   . THR   B 2 6   ? -2.01460  29.38048 15.86412  1.000 30.63676  ? 5   THR   B O   1 
ATOM   1957 C  CB  . THR   B 2 6   ? -4.24119  27.48072 17.23056  1.000 29.24625  ? 5   THR   B CB  1 
ATOM   1958 O  OG1 . THR   B 2 6   ? -3.44094  26.81816 16.23897  1.000 28.03333  ? 5   THR   B OG1 1 
ATOM   1959 C  CG2 . THR   B 2 6   ? -5.69974  27.08199 17.04236  1.000 30.73341  ? 5   THR   B CG2 1 
ATOM   1960 N  N   . PHE   B 2 7   ? -1.94310  29.45442 18.11936  1.000 32.72589  ? 6   PHE   B N   1 
ATOM   1961 C  CA  . PHE   B 2 7   ? -0.49647  29.57576 18.12382  1.000 29.58480  ? 6   PHE   B CA  1 
ATOM   1962 C  C   . PHE   B 2 7   ? 0.18715   28.21911 18.05575  1.000 26.38252  ? 6   PHE   B C   1 
ATOM   1963 O  O   . PHE   B 2 7   ? 1.38505   28.15649 17.76481  1.000 27.14175  ? 6   PHE   B O   1 
ATOM   1964 C  CB  . PHE   B 2 7   ? -0.02971  30.34511 19.36432  1.000 34.09744  ? 6   PHE   B CB  1 
ATOM   1965 C  CG  . PHE   B 2 7   ? -0.50958  29.76084 20.65446  1.000 29.62055  ? 6   PHE   B CG  1 
ATOM   1966 C  CD1 . PHE   B 2 7   ? 0.06499   28.61154 21.17452  1.000 32.11681  ? 6   PHE   B CD1 1 
ATOM   1967 C  CD2 . PHE   B 2 7   ? -1.53041  30.36593 21.35598  1.000 33.33169  ? 6   PHE   B CD2 1 
ATOM   1968 C  CE1 . PHE   B 2 7   ? -0.38723  28.07153 22.37564  1.000 35.43770  ? 6   PHE   B CE1 1 
ATOM   1969 C  CE2 . PHE   B 2 7   ? -1.98256  29.83212 22.54476  1.000 36.73602  ? 6   PHE   B CE2 1 
ATOM   1970 C  CZ  . PHE   B 2 7   ? -1.41183  28.68267 23.05155  1.000 36.13380  ? 6   PHE   B CZ  1 
ATOM   1971 N  N   . TRP   B 2 8   ? -0.55129  27.14612 18.28266  1.000 25.45888  ? 7   TRP   B N   1 
ATOM   1972 C  CA  . TRP   B 2 8   ? 0.04400   25.81964 18.38209  1.000 25.55097  ? 7   TRP   B CA  1 
ATOM   1973 C  C   . TRP   B 2 8   ? -0.10360  24.97488 17.12685  1.000 27.14910  ? 7   TRP   B C   1 
ATOM   1974 O  O   . TRP   B 2 8   ? 0.66515   24.02971 16.92382  1.000 24.14214  ? 7   TRP   B O   1 
ATOM   1975 C  CB  . TRP   B 2 8   ? -0.54339  25.06634 19.57930  1.000 26.20954  ? 7   TRP   B CB  1 
ATOM   1976 C  CG  . TRP   B 2 8   ? -2.03780  25.10797 19.73875  1.000 24.84028  ? 7   TRP   B CG  1 
ATOM   1977 C  CD1 . TRP   B 2 8   ? -2.75867  25.97235 20.53474  1.000 31.20332  ? 7   TRP   B CD1 1 
ATOM   1978 C  CD2 . TRP   B 2 8   ? -2.99775  24.26595 19.09667  1.000 23.50963  ? 7   TRP   B CD2 1 
ATOM   1979 N  NE1 . TRP   B 2 8   ? -4.09717  25.69936 20.43127  1.000 28.27408  ? 7   TRP   B NE1 1 
ATOM   1980 C  CE2 . TRP   B 2 8   ? -4.27200  24.65809 19.55389  1.000 27.66104  ? 7   TRP   B CE2 1 
ATOM   1981 C  CE3 . TRP   B 2 8   ? -2.90627  23.21027 18.17857  1.000 23.83686  ? 7   TRP   B CE3 1 
ATOM   1982 C  CZ2 . TRP   B 2 8   ? -5.44665  24.03884 19.11944  1.000 31.56579  ? 7   TRP   B CZ2 1 
ATOM   1983 C  CZ3 . TRP   B 2 8   ? -4.08996  22.60059 17.73481  1.000 25.38377  ? 7   TRP   B CZ3 1 
ATOM   1984 C  CH2 . TRP   B 2 8   ? -5.33200  23.01158 18.22024  1.000 27.93657  ? 7   TRP   B CH2 1 
HETATM 1985 C  C10 . A1BC5 B 2 9   ? 1.50515   19.66638 15.93871  1.000 26.50472  ? 8   A1BC5 B C10 1 
HETATM 1986 C  C13 . A1BC5 B 2 9   ? 3.14821   21.53894 16.32738  1.000 23.19801  ? 8   A1BC5 B C13 1 
HETATM 1987 C  C02 . A1BC5 B 2 9   ? -0.95952  19.82117 15.79954  1.000 21.96420  ? 8   A1BC5 B C02 1 
HETATM 1988 C  C03 . A1BC5 B 2 9   ? -1.74875  20.99285 15.28390  1.000 21.94368  ? 8   A1BC5 B C03 1 
HETATM 1989 C  CB  . A1BC5 B 2 9   ? -1.95838  23.41078 14.83144  1.000 23.29169  ? 8   A1BC5 B CB  1 
HETATM 1990 C  CA  . A1BC5 B 2 9   ? -1.08491  24.66349 14.80456  1.000 25.28423  ? 8   A1BC5 B CA  1 
HETATM 1991 C  C   . A1BC5 B 2 9   ? -1.71048  25.63499 13.81303  1.000 25.70891  ? 8   A1BC5 B C   1 
HETATM 1992 C  C12 . A1BC5 B 2 9   ? 2.83626   20.05715 16.56496  1.000 23.06801  ? 8   A1BC5 B C12 1 
HETATM 1993 N  N01 . A1BC5 B 2 9   ? -1.17922  22.30708 15.35517  1.000 22.25409  ? 8   A1BC5 B N01 1 
HETATM 1994 N  N   . A1BC5 B 2 9   ? -1.06934  25.30161 16.12287  1.000 22.10563  ? 8   A1BC5 B N   1 
HETATM 1995 N  N09 . A1BC5 B 2 9   ? 0.29149   20.26509 16.39440  1.000 23.43412  ? 8   A1BC5 B N09 1 
HETATM 1996 N  N15 . A1BC5 B 2 9   ? 3.86096   19.20506 15.99836  1.000 26.15002  ? 8   A1BC5 B N15 1 
HETATM 1997 O  O   . A1BC5 B 2 9   ? -2.03608  25.26777 12.73613  1.000 26.05505  ? 8   A1BC5 B O   1 
HETATM 1998 O  O11 . A1BC5 B 2 9   ? 1.44809   18.86428 15.06509  1.000 30.20156  ? 8   A1BC5 B O11 1 
HETATM 1999 O  O14 . A1BC5 B 2 9   ? -2.82720  20.83087 14.81861  1.000 27.78059  ? 8   A1BC5 B O14 1 
HETATM 2000 O  O16 . A1BC5 B 2 9   ? 3.51156   21.73929 14.97230  1.000 20.45443  ? 8   A1BC5 B O16 1 
ATOM   2001 N  N   . GLY   B 2 10  ? -1.24952  26.96810 14.03155  1.000 25.52319  ? 9   GLY   B N   1 
ATOM   2002 C  CA  . GLY   B 2 10  ? -1.73410  27.94116 13.05638  1.000 25.52501  ? 9   GLY   B CA  1 
ATOM   2003 C  C   . GLY   B 2 10  ? -3.23255  27.93605 12.79906  1.000 27.63069  ? 9   GLY   B C   1 
ATOM   2004 O  O   . GLY   B 2 10  ? -4.04007  27.61706 13.68947  1.000 28.02297  ? 9   GLY   B O   1 
ATOM   2005 N  N   . SER   B 2 11  ? -3.61136  28.32106 11.57421  1.000 27.78449  ? 10  SER   B N   1 
ATOM   2006 C  CA  . SER   B 2 11  ? -5.01589  28.30157 11.17991  1.000 31.03559  ? 10  SER   B CA  1 
ATOM   2007 C  C   . SER   B 2 11  ? -5.52368  26.86956 11.17619  1.000 31.96981  ? 10  SER   B C   1 
ATOM   2008 O  O   . SER   B 2 11  ? -5.14608  26.06519 10.31620  1.000 35.77335  ? 10  SER   B O   1 
ATOM   2009 C  CB  . SER   B 2 11  ? -5.20582  28.94233 9.80525   1.000 31.71091  ? 10  SER   B CB  1 
ATOM   2010 O  OG  . SER   B 2 11  ? -4.85433  30.31802 9.84413   1.000 33.50760  ? 10  SER   B OG  1 
ATOM   2011 N  N   . HIS   B 2 12  ? -6.37787  26.54130 12.13278  1.000 26.22661  ? 11  HIS   B N   1 
ATOM   2012 C  CA  . HIS   B 2 12  ? -6.75911  25.16105 12.38333  1.000 24.64903  ? 11  HIS   B CA  1 
ATOM   2013 C  C   . HIS   B 2 12  ? -8.26210  25.01110 12.24584  1.000 28.44510  ? 11  HIS   B C   1 
ATOM   2014 O  O   . HIS   B 2 12  ? -9.02405  25.77985 12.84442  1.000 29.70052  ? 11  HIS   B O   1 
ATOM   2015 C  CB  . HIS   B 2 12  ? -6.30426  24.71745 13.77420  1.000 23.86052  ? 11  HIS   B CB  1 
ATOM   2016 C  CG  . HIS   B 2 12  ? -6.42627  23.24366 14.00605  1.000 22.56258  ? 11  HIS   B CG  1 
ATOM   2017 N  ND1 . HIS   B 2 12  ? -5.57663  22.32826 13.42624  1.000 24.13352  ? 11  HIS   B ND1 1 
ATOM   2018 C  CD2 . HIS   B 2 12  ? -7.30303  22.52569 14.74657  1.000 25.20363  ? 11  HIS   B CD2 1 
ATOM   2019 C  CE1 . HIS   B 2 12  ? -5.92180  21.10894 13.80034  1.000 24.62832  ? 11  HIS   B CE1 1 
ATOM   2020 N  NE2 . HIS   B 2 12  ? -6.97454  21.19978 14.59432  1.000 24.29207  ? 11  HIS   B NE2 1 
ATOM   2021 N  N   . ARG   B 2 13  ? -8.68508  24.02795 11.45350  1.000 28.01007  ? 12  ARG   B N   1 
ATOM   2022 C  CA  . ARG   B 2 13  ? -10.10256 23.68216 11.35082  1.000 28.74372  ? 12  ARG   B CA  1 
ATOM   2023 C  C   . ARG   B 2 13  ? -10.42014 22.75292 12.51014  1.000 28.19473  ? 12  ARG   B C   1 
ATOM   2024 O  O   . ARG   B 2 13  ? -10.05714 21.57060 12.49264  1.000 26.54512  ? 12  ARG   B O   1 
ATOM   2025 C  CB  . ARG   B 2 13  ? -10.40634 23.02174 10.01321  1.000 29.66430  ? 12  ARG   B CB  1 
ATOM   2026 C  CG  . ARG   B 2 13  ? -11.89774 22.81269 9.77329   1.000 33.67089  ? 12  ARG   B CG  1 
ATOM   2027 C  CD  . ARG   B 2 13  ? -12.13887 21.71349 8.75010   1.000 31.89641  ? 12  ARG   B CD  1 
ATOM   2028 N  NE  . ARG   B 2 13  ? -11.84572 20.40240 9.30765   1.000 30.27242  ? 12  ARG   B NE  1 
ATOM   2029 C  CZ  . ARG   B 2 13  ? -10.87932 19.59684 8.88561   1.000 33.94393  ? 12  ARG   B CZ  1 
ATOM   2030 N  NH1 . ARG   B 2 13  ? -10.12486 19.90755 7.83703   1.000 28.08943  ? 12  ARG   B NH1 1 
ATOM   2031 N  NH2 . ARG   B 2 13  ? -10.65917 18.45515 9.53713   1.000 28.73133  ? 12  ARG   B NH2 1 
ATOM   2032 N  N   . GLN   B 2 14  ? -11.06745 23.28274 13.54871  1.000 30.18850  ? 13  GLN   B N   1 
ATOM   2033 C  CA  . GLN   B 2 14  ? -11.19180 22.53068 14.79674  1.000 28.41976  ? 13  GLN   B CA  1 
ATOM   2034 C  C   . GLN   B 2 14  ? -12.49322 21.73751 14.82528  1.000 32.79228  ? 13  GLN   B C   1 
ATOM   2035 O  O   . GLN   B 2 14  ? -13.35413 21.92158 15.68918  1.000 34.67816  ? 13  GLN   B O   1 
ATOM   2036 C  CB  . GLN   B 2 14  ? -11.09031 23.45391 16.00179  1.000 32.47578  ? 13  GLN   B CB  1 
ATOM   2037 C  CG  . GLN   B 2 14  ? -10.76279 22.69946 17.26820  1.000 31.48382  ? 13  GLN   B CG  1 
ATOM   2038 C  CD  . GLN   B 2 14  ? -10.33908 23.60865 18.38855  1.000 36.61389  ? 13  GLN   B CD  1 
ATOM   2039 O  OE1 . GLN   B 2 14  ? -11.05746 24.54064 18.74904  1.000 40.78713  ? 13  GLN   B OE1 1 
ATOM   2040 N  NE2 . GLN   B 2 14  ? -9.17089  23.35316 18.94176  1.000 31.87313  ? 13  GLN   B NE2 1 
ATOM   2041 N  N   . CYS   B 2 15  ? -12.61088 20.83631 13.86140  0.822 30.45733  ? 14  CYS   B N   1 
ATOM   2042 C  CA  . CYS   B 2 15  ? -13.79404 20.00897 13.71471  0.822 28.11262  ? 14  CYS   B CA  1 
ATOM   2043 C  C   . CYS   B 2 15  ? -13.54089 18.91094 12.68880  0.822 32.07451  ? 14  CYS   B C   1 
ATOM   2044 O  O   . CYS   B 2 15  ? -14.30177 17.94950 12.57038  0.822 33.13852  ? 14  CYS   B O   1 
ATOM   2045 C  CB  . CYS   B 2 15  ? -14.99654 20.86871 13.30115  0.822 31.26371  ? 14  CYS   B CB  1 
ATOM   2046 S  SG  . CYS   B 2 15  ? -14.65401 21.90801 11.85837  0.822 37.85269  ? 14  CYS   B SG  1 
HETATM 2047 N  N   . NH2   B 2 16  ? -12.56216 19.21004 11.69428  1.000 28.46982  ? 15  NH2   B N   1 
HETATM 2048 CO CO  . CO    C 3 .   ? 4.85876   20.23225 14.29199  1.000 19.09690  ? 301 CO    A CO  1 
HETATM 2049 CL CL  . CL    D 4 .   ? 0.56138   12.02798 -12.09095 1.000 39.03701  ? 302 CL    A CL  1 
HETATM 2050 CL CL  . CL    E 4 .   ? 9.74511   29.37961 42.39684  1.000 72.29854  ? 303 CL    A CL  1 
HETATM 2051 C  C1  . GOL   F 5 .   ? -5.89063  11.56673 11.67924  1.000 37.69605  ? 304 GOL   A C1  1 
HETATM 2052 O  O1  . GOL   F 5 .   ? -5.03245  12.39854 10.98976  1.000 46.54934  ? 304 GOL   A O1  1 
HETATM 2053 C  C2  . GOL   F 5 .   ? -5.71909  10.21190 11.01324  1.000 41.76150  ? 304 GOL   A C2  1 
HETATM 2054 O  O2  . GOL   F 5 .   ? -4.68505  9.51585  11.58816  1.000 41.28280  ? 304 GOL   A O2  1 
HETATM 2055 C  C3  . GOL   F 5 .   ? -7.08201  9.49806  11.16688  1.000 47.96822  ? 304 GOL   A C3  1 
HETATM 2056 O  O3  . GOL   F 5 .   ? -7.21659  9.18100  12.52005  1.000 54.95055  ? 304 GOL   A O3  1 
HETATM 2057 C  C1  . GOL   G 5 .   ? -5.59068  14.00256 33.43544  1.000 53.36110  ? 305 GOL   A C1  1 
HETATM 2058 O  O1  . GOL   G 5 .   ? -6.14314  14.63343 32.33750  1.000 45.28370  ? 305 GOL   A O1  1 
HETATM 2059 C  C2  . GOL   G 5 .   ? -4.87276  12.74275 32.89386  1.000 49.08633  ? 305 GOL   A C2  1 
HETATM 2060 O  O2  . GOL   G 5 .   ? -4.05357  13.03489 31.80141  1.000 38.37770  ? 305 GOL   A O2  1 
HETATM 2061 C  C3  . GOL   G 5 .   ? -4.07687  12.20957 34.10928  1.000 40.54373  ? 305 GOL   A C3  1 
HETATM 2062 O  O3  . GOL   G 5 .   ? -3.29460  11.16960 33.64229  1.000 48.74786  ? 305 GOL   A O3  1 
HETATM 2063 C  C1  . GOL   H 5 .   ? 13.86970  15.39255 14.44620  1.000 38.36193  ? 306 GOL   A C1  1 
HETATM 2064 O  O1  . GOL   H 5 .   ? 13.31953  16.68863 14.27953  1.000 34.95065  ? 306 GOL   A O1  1 
HETATM 2065 C  C2  . GOL   H 5 .   ? 15.12958  15.33240 13.52634  1.000 37.43208  ? 306 GOL   A C2  1 
HETATM 2066 O  O2  . GOL   H 5 .   ? 16.05774  16.31379 13.86794  1.000 41.78122  ? 306 GOL   A O2  1 
HETATM 2067 C  C3  . GOL   H 5 .   ? 15.72954  13.89801 13.69043  1.000 37.31856  ? 306 GOL   A C3  1 
HETATM 2068 O  O3  . GOL   H 5 .   ? 16.82711  13.83597 12.77613  1.000 42.53372  ? 306 GOL   A O3  1 
HETATM 2069 C  C1  . GOL   I 5 .   ? 3.65398   19.36420 -15.21856 1.000 49.84806  ? 307 GOL   A C1  1 
HETATM 2070 O  O1  . GOL   I 5 .   ? 4.71796   18.67606 -15.81877 1.000 52.08445  ? 307 GOL   A O1  1 
HETATM 2071 C  C2  . GOL   I 5 .   ? 4.15426   20.80784 -14.87873 1.000 60.13389  ? 307 GOL   A C2  1 
HETATM 2072 O  O2  . GOL   I 5 .   ? 5.54355   20.88366 -14.73645 1.000 64.94941  ? 307 GOL   A O2  1 
HETATM 2073 C  C3  . GOL   I 5 .   ? 3.61917   21.70912 -16.03055 1.000 67.01065  ? 307 GOL   A C3  1 
HETATM 2074 O  O3  . GOL   I 5 .   ? 4.55045   21.69846 -17.07676 1.000 68.85043  ? 307 GOL   A O3  1 
HETATM 2075 C  C1  . GOL   J 5 .   ? 9.99532   3.52146  10.68323  1.000 55.42206  ? 308 GOL   A C1  1 
HETATM 2076 O  O1  . GOL   J 5 .   ? 11.02562  3.95291  11.51849  1.000 57.39724  ? 308 GOL   A O1  1 
HETATM 2077 C  C2  . GOL   J 5 .   ? 9.49331   2.17262  11.25257  1.000 61.85260  ? 308 GOL   A C2  1 
HETATM 2078 O  O2  . GOL   J 5 .   ? 8.44570   2.34251  12.14407  1.000 54.77487  ? 308 GOL   A O2  1 
HETATM 2079 C  C3  . GOL   J 5 .   ? 9.08335   1.34343  10.01647  0.000 60.87550  ? 308 GOL   A C3  1 
HETATM 2080 O  O3  . GOL   J 5 .   ? 8.81499   0.05527  10.47162  0.000 63.38759  ? 308 GOL   A O3  1 
HETATM 2081 O  O   . HOH   K 6 .   ? 0.38443   26.18395 24.92343  1.000 42.71871  ? 401 HOH   A O   1 
HETATM 2082 O  O   . HOH   K 6 .   ? 17.47208  19.77385 36.60992  1.000 53.11828  ? 402 HOH   A O   1 
HETATM 2083 O  O   . HOH   K 6 .   ? 7.21531   26.27172 4.54103   1.000 44.72796  ? 403 HOH   A O   1 
HETATM 2084 O  O   . HOH   K 6 .   ? 17.20604  24.37501 36.09834  1.000 47.54622  ? 404 HOH   A O   1 
HETATM 2085 O  O   . HOH   K 6 .   ? 11.94783  26.27434 -7.03754  1.000 66.45451  ? 405 HOH   A O   1 
HETATM 2086 O  O   . HOH   K 6 .   ? -9.19728  2.68902  19.42127  1.000 47.20545  ? 406 HOH   A O   1 
HETATM 2087 O  O   . HOH   K 6 .   ? -16.18120 3.08497  19.55825  1.000 51.93116  ? 407 HOH   A O   1 
HETATM 2088 O  O   . HOH   K 6 .   ? -13.53896 8.55261  13.90761  1.000 42.44234  ? 408 HOH   A O   1 
HETATM 2089 O  O   . HOH   K 6 .   ? 8.81400   8.40207  -1.85876  1.000 54.49580  ? 409 HOH   A O   1 
HETATM 2090 O  O   . HOH   K 6 .   ? -5.50082  22.81531 27.77157  1.000 27.70141  ? 410 HOH   A O   1 
HETATM 2091 O  O   . HOH   K 6 .   ? 16.41145  14.24189 10.26809  1.000 36.89806  ? 411 HOH   A O   1 
HETATM 2092 O  O   . HOH   K 6 .   ? -5.17803  12.33597 8.40833   1.000 44.82361  ? 412 HOH   A O   1 
HETATM 2093 O  O   . HOH   K 6 .   ? 21.79037  19.38831 25.81464  1.000 39.19582  ? 413 HOH   A O   1 
HETATM 2094 O  O   . HOH   K 6 .   ? -13.89133 15.75512 10.40132  1.000 36.49621  ? 414 HOH   A O   1 
HETATM 2095 O  O   . HOH   K 6 .   ? 17.06656  19.17908 13.25253  1.000 37.02895  ? 415 HOH   A O   1 
HETATM 2096 O  O   . HOH   K 6 .   ? 0.73163   25.03215 -17.42676 1.000 53.42925  ? 416 HOH   A O   1 
HETATM 2097 O  O   . HOH   K 6 .   ? 7.80852   9.81167  30.46235  1.000 36.80912  ? 417 HOH   A O   1 
HETATM 2098 O  O   . HOH   K 6 .   ? -5.92426  17.16819 2.38251   1.000 39.50305  ? 418 HOH   A O   1 
HETATM 2099 O  O   . HOH   K 6 .   ? 9.93760   14.30055 -18.45674 1.000 52.51206  ? 419 HOH   A O   1 
HETATM 2100 O  O   . HOH   K 6 .   ? 9.55610   25.11620 5.60085   1.000 39.85777  ? 420 HOH   A O   1 
HETATM 2101 O  O   . HOH   K 6 .   ? -0.12542  14.05790 3.95521   1.000 41.25141  ? 421 HOH   A O   1 
HETATM 2102 O  O   . HOH   K 6 .   ? -2.67360  9.60883  23.96523  1.000 23.53735  ? 422 HOH   A O   1 
HETATM 2103 O  O   . HOH   K 6 .   ? -2.70522  35.45759 14.33352  1.000 48.40482  ? 423 HOH   A O   1 
HETATM 2104 O  O   . HOH   K 6 .   ? 0.88410   13.09395 6.32230   1.000 30.18099  ? 424 HOH   A O   1 
HETATM 2105 O  O   . HOH   K 6 .   ? -0.49115  5.44375  13.42824  1.000 34.21527  ? 425 HOH   A O   1 
HETATM 2106 O  O   . HOH   K 6 .   ? 2.48467   4.02934  21.31149  1.000 28.71655  ? 426 HOH   A O   1 
HETATM 2107 O  O   . HOH   K 6 .   ? 16.58144  16.36997 16.48352  1.000 33.68804  ? 427 HOH   A O   1 
HETATM 2108 O  O   . HOH   K 6 .   ? 0.81795   34.47475 28.12320  1.000 45.99184  ? 428 HOH   A O   1 
HETATM 2109 O  O   . HOH   K 6 .   ? 13.23966  10.94301 12.36280  1.000 31.63531  ? 429 HOH   A O   1 
HETATM 2110 O  O   . HOH   K 6 .   ? -3.85198  10.24467 31.01420  1.000 32.64096  ? 430 HOH   A O   1 
HETATM 2111 O  O   . HOH   K 6 .   ? -7.42924  16.48611 30.59495  1.000 27.17526  ? 431 HOH   A O   1 
HETATM 2112 O  O   . HOH   K 6 .   ? 7.71992   6.52062  25.63146  1.000 33.28187  ? 432 HOH   A O   1 
HETATM 2113 O  O   . HOH   K 6 .   ? -10.10868 18.85537 4.18292   1.000 41.85847  ? 433 HOH   A O   1 
HETATM 2114 O  O   . HOH   K 6 .   ? 5.93983   9.68611  10.33751  1.000 27.85233  ? 434 HOH   A O   1 
HETATM 2115 O  O   . HOH   K 6 .   ? 8.52645   20.33219 17.28858  1.000 35.47556  ? 435 HOH   A O   1 
HETATM 2116 O  O   . HOH   K 6 .   ? 1.39837   9.26611  -4.26560  1.000 46.06477  ? 436 HOH   A O   1 
HETATM 2117 O  O   . HOH   K 6 .   ? 2.63549   22.58548 -3.35396  1.000 33.13034  ? 437 HOH   A O   1 
HETATM 2118 O  O   . HOH   K 6 .   ? -4.40162  5.94952  31.43058  1.000 40.92692  ? 438 HOH   A O   1 
HETATM 2119 O  O   . HOH   K 6 .   ? 0.43147   4.00583  24.95058  1.000 35.94741  ? 439 HOH   A O   1 
HETATM 2120 O  O   . HOH   K 6 .   ? 15.88380  6.96839  20.23094  1.000 42.09165  ? 440 HOH   A O   1 
HETATM 2121 O  O   . HOH   K 6 .   ? -17.00462 16.82040 17.25433  1.000 55.41249  ? 441 HOH   A O   1 
HETATM 2122 O  O   . HOH   K 6 .   ? -1.42149  3.91278  32.43634  1.000 39.84084  ? 442 HOH   A O   1 
HETATM 2123 O  O   . HOH   K 6 .   ? -10.96273 4.29318  14.85812  1.000 53.28683  ? 443 HOH   A O   1 
HETATM 2124 O  O   . HOH   K 6 .   ? 9.58495   34.27445 26.09910  1.000 38.74188  ? 444 HOH   A O   1 
HETATM 2125 O  O   . HOH   K 6 .   ? -6.24957  12.60851 22.43647  1.000 23.65003  ? 445 HOH   A O   1 
HETATM 2126 O  O   . HOH   K 6 .   ? 15.06589  27.31784 34.24034  1.000 35.34805  ? 446 HOH   A O   1 
HETATM 2127 O  O   . HOH   K 6 .   ? 12.23563  13.77586 35.93367  1.000 47.45119  ? 447 HOH   A O   1 
HETATM 2128 O  O   . HOH   K 6 .   ? 23.36864  20.09329 23.34749  1.000 47.22731  ? 448 HOH   A O   1 
HETATM 2129 O  O   . HOH   K 6 .   ? 6.25227   20.74250 16.03090  1.000 24.23256  ? 449 HOH   A O   1 
HETATM 2130 O  O   . HOH   K 6 .   ? -0.64544  11.06888 -5.65632  1.000 46.23943  ? 450 HOH   A O   1 
HETATM 2131 O  O   . HOH   K 6 .   ? 5.00741   24.85981 39.03031  1.000 34.87115  ? 451 HOH   A O   1 
HETATM 2132 O  O   . HOH   K 6 .   ? 19.87788  15.09162 5.85209   1.000 44.61368  ? 452 HOH   A O   1 
HETATM 2133 O  O   . HOH   K 6 .   ? 19.52223  12.60251 6.33503   1.000 49.68261  ? 453 HOH   A O   1 
HETATM 2134 O  O   . HOH   K 6 .   ? 5.58363   21.33046 -10.47628 1.000 39.46606  ? 454 HOH   A O   1 
HETATM 2135 O  O   . HOH   K 6 .   ? 11.06155  33.20670 19.45777  1.000 32.20373  ? 455 HOH   A O   1 
HETATM 2136 O  O   . HOH   K 6 .   ? -1.37038  22.75156 -3.71435  1.000 45.34354  ? 456 HOH   A O   1 
HETATM 2137 O  O   . HOH   K 6 .   ? 11.10189  28.12123 7.52085   1.000 31.61799  ? 457 HOH   A O   1 
HETATM 2138 O  O   . HOH   K 6 .   ? 0.18931   33.94747 17.78858  1.000 46.76500  ? 458 HOH   A O   1 
HETATM 2139 O  O   . HOH   K 6 .   ? -1.76126  24.78829 -9.39054  1.000 41.62189  ? 459 HOH   A O   1 
HETATM 2140 O  O   . HOH   K 6 .   ? 0.45496   26.16917 33.20893  1.000 30.34359  ? 460 HOH   A O   1 
HETATM 2141 O  O   . HOH   K 6 .   ? 20.26643  28.43450 32.33392  1.000 53.09898  ? 461 HOH   A O   1 
HETATM 2142 O  O   . HOH   K 6 .   ? 18.87033  16.67978 10.51708  1.000 38.54749  ? 462 HOH   A O   1 
HETATM 2143 O  O   . HOH   K 6 .   ? -10.20978 10.83001 12.94938  1.000 40.86420  ? 463 HOH   A O   1 
HETATM 2144 O  O   . HOH   K 6 .   ? -18.53575 9.32893  20.72945  1.000 43.49931  ? 464 HOH   A O   1 
HETATM 2145 O  O   . HOH   K 6 .   ? 15.75194  32.55036 6.85973   1.000 64.70623  ? 465 HOH   A O   1 
HETATM 2146 O  O   . HOH   K 6 .   ? -12.83902 11.08209 14.46824  1.000 36.14209  ? 466 HOH   A O   1 
HETATM 2147 O  O   . HOH   K 6 .   ? 13.53600  4.33807  22.12652  1.000 40.68329  ? 467 HOH   A O   1 
HETATM 2148 O  O   . HOH   K 6 .   ? -7.55407  0.97408  20.11901  1.000 41.77645  ? 468 HOH   A O   1 
HETATM 2149 O  O   . HOH   K 6 .   ? 11.05493  17.60140 12.48941  1.000 31.87515  ? 469 HOH   A O   1 
HETATM 2150 O  O   . HOH   K 6 .   ? 10.58267  16.92450 14.89821  1.000 31.64585  ? 470 HOH   A O   1 
HETATM 2151 O  O   . HOH   K 6 .   ? -9.33857  14.81669 3.65355   1.000 41.63278  ? 471 HOH   A O   1 
HETATM 2152 O  O   . HOH   K 6 .   ? 8.89037   1.24727  20.91954  1.000 42.68401  ? 472 HOH   A O   1 
HETATM 2153 O  O   . HOH   K 6 .   ? -2.29208  23.55935 4.16578   1.000 29.53446  ? 473 HOH   A O   1 
HETATM 2154 O  O   . HOH   K 6 .   ? 23.01407  23.42029 21.12074  1.000 44.73521  ? 474 HOH   A O   1 
HETATM 2155 O  O   . HOH   K 6 .   ? 10.32633  23.18060 -2.97485  1.000 48.58000  ? 475 HOH   A O   1 
HETATM 2156 O  O   . HOH   K 6 .   ? 11.57462  11.87638 23.00452  1.000 30.81457  ? 476 HOH   A O   1 
HETATM 2157 O  O   . HOH   K 6 .   ? -2.86552  7.26751  11.05579  1.000 48.78031  ? 477 HOH   A O   1 
HETATM 2158 O  O   . HOH   K 6 .   ? -1.07025  3.24758  16.95902  1.000 30.69862  ? 478 HOH   A O   1 
HETATM 2159 O  O   . HOH   K 6 .   ? 15.97755  7.77741  9.45720   1.000 44.42430  ? 479 HOH   A O   1 
HETATM 2160 O  O   . HOH   K 6 .   ? 16.40062  29.34597 33.05470  1.000 37.46108  ? 480 HOH   A O   1 
HETATM 2161 O  O   . HOH   K 6 .   ? -5.74781  23.41986 31.47295  1.000 38.70851  ? 481 HOH   A O   1 
HETATM 2162 O  O   . HOH   K 6 .   ? -6.72469  24.28950 8.17962   1.000 41.87750  ? 482 HOH   A O   1 
HETATM 2163 O  O   . HOH   K 6 .   ? 7.15362   19.37054 36.65791  1.000 28.17465  ? 483 HOH   A O   1 
HETATM 2164 O  O   . HOH   K 6 .   ? -0.59257  28.78266 33.99602  1.000 46.45847  ? 484 HOH   A O   1 
HETATM 2165 O  O   . HOH   K 6 .   ? 5.15111   4.29642  27.19451  1.000 37.60606  ? 485 HOH   A O   1 
HETATM 2166 O  O   . HOH   K 6 .   ? 3.18290   24.21255 21.92915  1.000 31.29247  ? 486 HOH   A O   1 
HETATM 2167 O  O   . HOH   K 6 .   ? -7.97261  1.15012  27.65933  1.000 53.64160  ? 487 HOH   A O   1 
HETATM 2168 O  O   . HOH   K 6 .   ? 13.04079  4.19589  19.62729  1.000 41.19356  ? 488 HOH   A O   1 
HETATM 2169 O  O   . HOH   K 6 .   ? 12.73557  10.12856 30.21000  1.000 53.84390  ? 489 HOH   A O   1 
HETATM 2170 O  O   . HOH   K 6 .   ? 15.27581  7.03182  17.53230  1.000 41.87226  ? 490 HOH   A O   1 
HETATM 2171 O  O   . HOH   K 6 .   ? 11.98678  23.11259 4.65888   1.000 35.25849  ? 491 HOH   A O   1 
HETATM 2172 O  O   . HOH   K 6 .   ? -6.74690  23.53633 5.48903   1.000 40.60829  ? 492 HOH   A O   1 
HETATM 2173 O  O   . HOH   K 6 .   ? 3.11052   31.14800 6.62162   1.000 41.24815  ? 493 HOH   A O   1 
HETATM 2174 O  O   . HOH   K 6 .   ? 17.58536  26.73844 10.21295  1.000 41.59570  ? 494 HOH   A O   1 
HETATM 2175 O  O   . HOH   K 6 .   ? 29.25744  27.38744 21.60087  1.000 53.49783  ? 495 HOH   A O   1 
HETATM 2176 O  O   . HOH   K 6 .   ? 16.76393  22.01228 4.10723   1.000 42.24799  ? 496 HOH   A O   1 
HETATM 2177 O  O   . HOH   K 6 .   ? 6.89477   25.44797 40.23826  1.000 44.00215  ? 497 HOH   A O   1 
HETATM 2178 O  O   . HOH   K 6 .   ? -5.94804  10.53745 24.31205  1.000 33.30288  ? 498 HOH   A O   1 
HETATM 2179 O  O   . HOH   K 6 .   ? -1.84204  31.92636 25.76356  1.000 58.88493  ? 499 HOH   A O   1 
HETATM 2180 O  O   . HOH   K 6 .   ? 4.53259   9.63604  -18.78127 1.000 52.22735  ? 500 HOH   A O   1 
HETATM 2181 O  O   . HOH   K 6 .   ? 0.99747   1.05038  14.68862  1.000 39.36221  ? 501 HOH   A O   1 
HETATM 2182 O  O   . HOH   K 6 .   ? 8.58528   18.79493 38.81184  1.000 35.07076  ? 502 HOH   A O   1 
HETATM 2183 O  O   . HOH   K 6 .   ? 0.17766   33.88338 33.18784  1.000 41.15377  ? 503 HOH   A O   1 
HETATM 2184 O  O   . HOH   K 6 .   ? 18.44902  9.47483  8.43107   1.000 49.36470  ? 504 HOH   A O   1 
HETATM 2185 O  O   . HOH   K 6 .   ? 25.88754  23.30656 21.89335  1.000 40.24211  ? 505 HOH   A O   1 
HETATM 2186 O  O   . HOH   K 6 .   ? 19.69578  15.73550 31.20360  1.000 43.59164  ? 506 HOH   A O   1 
HETATM 2187 O  O   . HOH   K 6 .   ? -6.81280  19.98446 -11.62145 1.000 42.45991  ? 507 HOH   A O   1 
HETATM 2188 O  O   . HOH   K 6 .   ? 19.19907  14.01298 24.87455  1.000 44.24322  ? 508 HOH   A O   1 
HETATM 2189 O  O   . HOH   K 6 .   ? -0.24188  31.06143 28.45605  1.000 37.05080  ? 509 HOH   A O   1 
HETATM 2190 O  O   . HOH   K 6 .   ? -0.14716  20.48737 12.61939  1.000 25.61930  ? 510 HOH   A O   1 
HETATM 2191 O  O   . HOH   K 6 .   ? 1.66442   12.17573 2.38720   1.000 38.89481  ? 511 HOH   A O   1 
HETATM 2192 O  O   . HOH   K 6 .   ? -3.98357  24.32428 33.87544  1.000 31.01004  ? 512 HOH   A O   1 
HETATM 2193 O  O   . HOH   K 6 .   ? 7.56258   -0.79559 17.00524  1.000 54.30971  ? 513 HOH   A O   1 
HETATM 2194 O  O   . HOH   K 6 .   ? 13.72063  3.78596  14.54953  1.000 43.63307  ? 514 HOH   A O   1 
HETATM 2195 O  O   . HOH   K 6 .   ? -6.84382  4.83807  21.77475  1.000 29.89989  ? 515 HOH   A O   1 
HETATM 2196 O  O   . HOH   K 6 .   ? -16.77642 15.42319 13.34413  1.000 41.15312  ? 516 HOH   A O   1 
HETATM 2197 O  O   . HOH   K 6 .   ? 6.42246   9.02965  34.06169  1.000 38.70269  ? 517 HOH   A O   1 
HETATM 2198 O  O   . HOH   K 6 .   ? 6.68482   37.72744 25.01156  1.000 47.32943  ? 518 HOH   A O   1 
HETATM 2199 O  O   . HOH   K 6 .   ? 2.01828   36.13703 30.19772  1.000 39.10024  ? 519 HOH   A O   1 
HETATM 2200 O  O   . HOH   K 6 .   ? -1.07656  11.47319 7.85606   1.000 39.31928  ? 520 HOH   A O   1 
HETATM 2201 O  O   . HOH   K 6 .   ? -3.47820  17.01754 5.80440   1.000 36.61365  ? 521 HOH   A O   1 
HETATM 2202 O  O   . HOH   K 6 .   ? 10.78686  18.81395 16.80648  1.000 28.75871  ? 522 HOH   A O   1 
HETATM 2203 O  O   . HOH   K 6 .   ? -10.85089 13.41984 23.25605  1.000 38.91523  ? 523 HOH   A O   1 
HETATM 2204 O  O   . HOH   K 6 .   ? 27.35884  31.30189 21.66803  1.000 60.50244  ? 524 HOH   A O   1 
HETATM 2205 O  O   . HOH   K 6 .   ? 15.03434  11.23067 27.42479  1.000 43.05195  ? 525 HOH   A O   1 
HETATM 2206 O  O   . HOH   K 6 .   ? 6.00810   6.82040  30.12056  1.000 47.88015  ? 526 HOH   A O   1 
HETATM 2207 O  O   . HOH   K 6 .   ? -1.97862  33.10348 6.94118   1.000 55.10250  ? 527 HOH   A O   1 
HETATM 2208 O  O   . HOH   K 6 .   ? -12.11282 4.54763  20.98588  1.000 47.87104  ? 528 HOH   A O   1 
HETATM 2209 O  O   . HOH   K 6 .   ? 19.46219  32.67811 23.73757  1.000 45.01963  ? 529 HOH   A O   1 
HETATM 2210 O  O   . HOH   K 6 .   ? 21.66772  18.32673 2.80223   1.000 59.14778  ? 530 HOH   A O   1 
HETATM 2211 O  O   . HOH   K 6 .   ? -6.48411  5.99053  24.36169  1.000 41.34123  ? 531 HOH   A O   1 
HETATM 2212 O  O   . HOH   K 6 .   ? -1.37458  12.32073 -14.08779 1.000 41.80367  ? 532 HOH   A O   1 
HETATM 2213 O  O   . HOH   K 6 .   ? 9.44126   33.90932 12.34901  1.000 55.80446  ? 533 HOH   A O   1 
HETATM 2214 O  O   . HOH   K 6 .   ? 10.42135  7.52060  -11.89366 1.000 67.75887  ? 534 HOH   A O   1 
HETATM 2215 O  O   . HOH   K 6 .   ? 17.24709  10.48550 27.11330  1.000 54.29517  ? 535 HOH   A O   1 
HETATM 2216 O  O   . HOH   K 6 .   ? 16.87224  25.97631 34.63394  1.000 47.68051  ? 536 HOH   A O   1 
HETATM 2217 O  O   . HOH   K 6 .   ? 20.20051  17.10649 26.05513  1.000 40.34727  ? 537 HOH   A O   1 
HETATM 2218 O  O   . HOH   K 6 .   ? 17.04967  23.28745 0.21940   1.000 63.40322  ? 538 HOH   A O   1 
HETATM 2219 O  O   . HOH   K 6 .   ? 5.66668   40.24440 25.20037  1.000 35.97382  ? 539 HOH   A O   1 
HETATM 2220 O  O   . HOH   K 6 .   ? -12.07360 15.67636 23.03253  1.000 47.05403  ? 540 HOH   A O   1 
HETATM 2221 O  O   . HOH   K 6 .   ? 11.85918  24.88032 -13.73204 1.000 57.85469  ? 541 HOH   A O   1 
HETATM 2222 O  O   . HOH   K 6 .   ? 14.60767  10.96387 34.36046  1.000 53.80079  ? 542 HOH   A O   1 
HETATM 2223 O  O   . HOH   K 6 .   ? 26.63292  24.79515 23.79289  1.000 60.78341  ? 543 HOH   A O   1 
HETATM 2224 O  O   . HOH   K 6 .   ? 8.31402   36.73307 17.66912  1.000 59.80324  ? 544 HOH   A O   1 
HETATM 2225 O  O   . HOH   K 6 .   ? -5.10868  34.51200 8.57840   1.000 54.42793  ? 545 HOH   A O   1 
HETATM 2226 O  O   . HOH   K 6 .   ? -17.06928 1.14512  22.34839  1.000 56.68765  ? 546 HOH   A O   1 
HETATM 2227 O  O   . HOH   K 6 .   ? 7.11577   33.06407 7.75894   1.000 55.68471  ? 547 HOH   A O   1 
HETATM 2228 O  O   . HOH   K 6 .   ? -2.77342  21.85965 -5.91866  1.000 42.49694  ? 548 HOH   A O   1 
HETATM 2229 O  O   . HOH   K 6 .   ? 5.64432   31.56777 5.36286   1.000 59.76636  ? 549 HOH   A O   1 
HETATM 2230 O  O   . HOH   K 6 .   ? 30.71755  26.08575 23.39678  1.000 54.68779  ? 550 HOH   A O   1 
HETATM 2231 O  O   . HOH   K 6 .   ? -4.17743  24.17784 6.06763   1.000 44.89359  ? 551 HOH   A O   1 
HETATM 2232 O  O   . HOH   K 6 .   ? 13.99632  15.71887 37.55065  1.000 51.35059  ? 552 HOH   A O   1 
HETATM 2233 O  O   . HOH   K 6 .   ? 0.81688   26.31616 -8.52185  1.000 52.07672  ? 553 HOH   A O   1 
HETATM 2234 O  O   . HOH   K 6 .   ? -9.11360  23.58809 26.22155  1.000 45.98842  ? 554 HOH   A O   1 
HETATM 2235 O  O   . HOH   K 6 .   ? 10.01141  4.49765  -10.12223 1.000 66.43709  ? 555 HOH   A O   1 
HETATM 2236 O  O   . HOH   K 6 .   ? -5.29334  8.15865  23.97271  1.000 43.24817  ? 556 HOH   A O   1 
HETATM 2237 O  O   . HOH   K 6 .   ? 19.17185  11.08229 25.35325  1.000 50.84919  ? 557 HOH   A O   1 
HETATM 2238 O  O   . HOH   K 6 .   ? 19.21381  14.56868 9.18275   1.000 45.24178  ? 558 HOH   A O   1 
HETATM 2239 O  O   . HOH   K 6 .   ? 15.54445  23.23441 47.51611  1.000 76.62104  ? 559 HOH   A O   1 
HETATM 2240 O  O   . HOH   K 6 .   ? -5.60621  8.36739  31.57999  1.000 46.50707  ? 560 HOH   A O   1 
HETATM 2241 O  O   . HOH   K 6 .   ? 13.59965  32.84121 9.98505   1.000 56.95381  ? 561 HOH   A O   1 
HETATM 2242 O  O   . HOH   K 6 .   ? -6.13091  24.39999 25.28750  1.000 44.21622  ? 562 HOH   A O   1 
HETATM 2243 O  O   . HOH   K 6 .   ? -0.72008  32.88978 29.88594  1.000 54.56640  ? 563 HOH   A O   1 
HETATM 2244 O  O   . HOH   K 6 .   ? -4.75754  14.84077 2.87877   1.000 49.66748  ? 564 HOH   A O   1 
HETATM 2245 O  O   . HOH   K 6 .   ? -4.55552  28.06323 6.02994   1.000 54.54803  ? 565 HOH   A O   1 
HETATM 2246 O  O   . HOH   K 6 .   ? -9.19687  5.70069  20.09938  1.000 40.17007  ? 566 HOH   A O   1 
HETATM 2247 O  O   . HOH   K 6 .   ? -3.62811  28.02574 -14.97659 1.000 70.71407  ? 567 HOH   A O   1 
HETATM 2248 O  O   . HOH   K 6 .   ? 20.91450  12.96193 -2.86761  1.000 65.22513  ? 568 HOH   A O   1 
HETATM 2249 O  O   . HOH   K 6 .   ? -5.44607  22.75892 -2.02926  1.000 54.37987  ? 569 HOH   A O   1 
HETATM 2250 O  O   . HOH   K 6 .   ? 8.15239   24.60108 -2.36779  1.000 52.33926  ? 570 HOH   A O   1 
HETATM 2251 O  O   . HOH   K 6 .   ? 16.25044  4.95932  15.43478  1.000 53.02486  ? 571 HOH   A O   1 
HETATM 2252 O  O   . HOH   K 6 .   ? 17.02816  5.94402  11.98591  1.000 51.56715  ? 572 HOH   A O   1 
HETATM 2253 O  O   . HOH   K 6 .   ? -8.56925  17.76441 -7.91916  1.000 67.58569  ? 573 HOH   A O   1 
HETATM 2254 O  O   . HOH   K 6 .   ? -3.16586  14.83516 4.96397   1.000 39.69350  ? 574 HOH   A O   1 
HETATM 2255 O  O   . HOH   K 6 .   ? 27.98539  25.11561 21.30147  1.000 43.94326  ? 575 HOH   A O   1 
HETATM 2256 O  O   . HOH   K 6 .   ? 7.72023   8.64381  4.01932   1.000 58.14903  ? 576 HOH   A O   1 
HETATM 2257 O  O   . HOH   K 6 .   ? -8.31803  24.02548 31.93174  1.000 43.16822  ? 577 HOH   A O   1 
HETATM 2258 O  O   . HOH   K 6 .   ? -3.53459  12.55897 6.14344   1.000 48.55840  ? 578 HOH   A O   1 
HETATM 2259 O  O   . HOH   K 6 .   ? -6.84051  9.46452  3.64852   1.000 64.17638  ? 579 HOH   A O   1 
HETATM 2260 O  O   . HOH   K 6 .   ? -0.45897  37.43717 30.33884  1.000 41.34062  ? 580 HOH   A O   1 
HETATM 2261 O  O   . HOH   K 6 .   ? -10.51281 21.57984 1.80086   1.000 58.86049  ? 581 HOH   A O   1 
HETATM 2262 O  O   . HOH   K 6 .   ? -12.98962 21.50198 31.18555  1.000 52.74832  ? 582 HOH   A O   1 
HETATM 2263 O  O   . HOH   K 6 .   ? 16.00959  25.72393 51.59307  1.000 64.39621  ? 583 HOH   A O   1 
HETATM 2264 O  O   . HOH   K 6 .   ? -6.29441  27.82399 31.33912  1.000 70.12617  ? 584 HOH   A O   1 
HETATM 2265 O  O   . HOH   K 6 .   ? 9.61443   19.62366 -22.47863 1.000 47.42180  ? 585 HOH   A O   1 
HETATM 2266 O  O   . HOH   K 6 .   ? 18.78148  1.36125  8.42780   1.000 66.59268  ? 586 HOH   A O   1 
HETATM 2267 O  O   . HOH   K 6 .   ? 17.53423  18.17245 45.24677  1.000 69.40692  ? 587 HOH   A O   1 
HETATM 2268 O  O   . HOH   L 6 .   ? -3.36866  25.27762 8.73382   1.000 40.76634  ? 101 HOH   B O   1 
HETATM 2269 O  O   . HOH   L 6 .   ? 1.44340   22.41189 13.64544  1.000 23.89652  ? 102 HOH   B O   1 
HETATM 2270 O  O   . HOH   L 6 .   ? -6.59350  31.99673 8.94580   1.000 47.37982  ? 103 HOH   B O   1 
HETATM 2271 O  O   . HOH   L 6 .   ? -3.63330  23.45926 11.56867  1.000 24.27421  ? 104 HOH   B O   1 
HETATM 2272 O  O   . HOH   L 6 .   ? -9.90766  22.12077 6.07707   1.000 41.55966  ? 105 HOH   B O   1 
HETATM 2273 O  O   . HOH   L 6 .   ? -16.65498 17.96666 14.31746  1.000 41.63676  ? 106 HOH   B O   1 
HETATM 2274 O  O   . HOH   L 6 .   ? -9.43105  32.60517 15.77579  1.000 48.87908  ? 107 HOH   B O   1 
HETATM 2275 O  O   . HOH   L 6 .   ? -4.21513  29.58777 20.21386  1.000 40.24346  ? 108 HOH   B O   1 
HETATM 2276 O  O   . HOH   L 6 .   ? -7.87167  39.79553 13.16157  1.000 71.64645  ? 109 HOH   B O   1 
HETATM 2277 O  O   . HOH   L 6 .   ? -14.98544 23.98273 8.40019   1.000 50.22396  ? 110 HOH   B O   1 
HETATM 2278 O  O   . HOH   L 6 .   ? -2.45457  33.68754 17.20080  1.000 55.32798  ? 111 HOH   B O   1 
HETATM 2279 O  O   . HOH   L 6 .   ? -15.97635 22.37597 6.72621   1.000 47.17779  ? 112 HOH   B O   1 
HETATM 2280 O  O   . HOH   L 6 .   ? -14.66559 28.94724 6.04094   1.000 63.84949  ? 113 HOH   B 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   . ASN   A 6   ? 0.96919 1.10890 0.88686 -0.04629 -0.00705 -0.06798 5   ASN   A N   
2    C  CA  . ASN   A 6   ? 1.10101 1.23814 1.02254 -0.05240 -0.00933 -0.07460 5   ASN   A CA  
3    C  C   . ASN   A 6   ? 1.12002 1.24781 1.05326 -0.05096 -0.00943 -0.06899 5   ASN   A C   
4    O  O   . ASN   A 6   ? 1.18272 1.30427 1.12028 -0.05574 -0.00980 -0.07402 5   ASN   A O   
5    C  CB  . ASN   A 6   ? 1.02273 1.17931 0.94093 -0.05683 -0.01524 -0.07563 5   ASN   A CB  
6    N  N   . MET   A 7   ? 0.94328 1.06984 0.88122 -0.04474 -0.00891 -0.05873 6   MET   A N   
7    C  CA  . MET   A 7   ? 0.93404 1.05418 0.88225 -0.04277 -0.00943 -0.05269 6   MET   A CA  
8    C  C   . MET   A 7   ? 0.90631 1.01032 0.85764 -0.03856 -0.00470 -0.05046 6   MET   A C   
9    O  O   . MET   A 7   ? 0.76057 0.86462 0.70939 -0.03420 -0.00280 -0.04583 6   MET   A O   
10   C  CB  . MET   A 7   ? 0.95451 1.08699 0.90576 -0.03900 -0.01339 -0.04263 6   MET   A CB  
11   C  CG  . MET   A 7   ? 0.88280 1.01030 0.84414 -0.03650 -0.01410 -0.03665 6   MET   A CG  
12   S  SD  . MET   A 7   ? 0.97784 1.09877 0.94559 -0.04254 -0.01380 -0.04379 6   MET   A SD  
13   C  CE  . MET   A 7   ? 0.61019 0.73917 0.58747 -0.03936 -0.01714 -0.03554 6   MET   A CE  
14   N  N   . ALA   A 8   ? 0.68571 0.77682 0.64245 -0.04016 -0.00284 -0.05353 7   ALA   A N   
15   C  CA  . ALA   A 8   ? 0.55252 0.62926 0.51286 -0.03615 0.00112  -0.05123 7   ALA   A CA  
16   C  C   . ALA   A 8   ? 0.52264 0.60045 0.48872 -0.03131 0.00016  -0.04105 7   ALA   A C   
17   O  O   . ALA   A 8   ? 0.47958 0.56561 0.44883 -0.03114 -0.00333 -0.03634 7   ALA   A O   
18   C  CB  . ALA   A 8   ? 0.49099 0.55429 0.45534 -0.03913 0.00286  -0.05609 7   ALA   A CB  
19   N  N   . SER   A 9   ? 0.45398 0.52342 0.42150 -0.02724 0.00330  -0.03789 8   SER   A N   
20   C  CA  . SER   A 9   ? 0.44193 0.51048 0.41451 -0.02329 0.00260  -0.02903 8   SER   A CA  
21   C  C   . SER   A 9   ? 0.31783 0.38163 0.29745 -0.02386 0.00118  -0.02745 8   SER   A C   
22   O  O   . SER   A 9   ? 0.36356 0.42142 0.34488 -0.02692 0.00194  -0.03259 8   SER   A O   
23   C  CB  . SER   A 9   ? 0.39612 0.45689 0.36957 -0.01988 0.00622  -0.02691 8   SER   A CB  
24   O  OG  . SER   A 9   ? 0.38616 0.43521 0.36256 -0.02011 0.00870  -0.03119 8   SER   A OG  
25   N  N   . LEU   A 10  ? 0.33126 0.39730 0.31467 -0.02089 -0.00065 -0.02019 9   LEU   A N   
26   C  CA  . LEU   A 10  ? 0.33856 0.40109 0.32839 -0.02076 -0.00166 -0.01854 9   LEU   A CA  
27   C  C   . LEU   A 10  ? 0.33819 0.38768 0.33104 -0.02070 0.00132  -0.02036 9   LEU   A C   
28   O  O   . LEU   A 10  ? 0.28992 0.33575 0.28614 -0.02285 0.00142  -0.02250 9   LEU   A O   
29   C  CB  . LEU   A 10  ? 0.27835 0.34381 0.27099 -0.01666 -0.00365 -0.01076 9   LEU   A CB  
30   C  CG  . LEU   A 10  ? 0.34896 0.41140 0.34791 -0.01550 -0.00437 -0.00883 9   LEU   A CG  
31   C  CD1 . LEU   A 10  ? 0.34663 0.41648 0.34775 -0.01909 -0.00597 -0.01286 9   LEU   A CD1 
32   C  CD2 . LEU   A 10  ? 0.33468 0.39854 0.33549 -0.01079 -0.00609 -0.00166 9   LEU   A CD2 
33   N  N   . ILE   A 11  ? 0.31306 0.35630 0.30480 -0.01835 0.00381  -0.01930 10  ILE   A N   
34   C  CA  . ILE   A 11  ? 0.29514 0.32709 0.28978 -0.01771 0.00627  -0.02050 10  ILE   A CA  
35   C  C   . ILE   A 11  ? 0.32848 0.35496 0.32110 -0.02080 0.00807  -0.02760 10  ILE   A C   
36   O  O   . ILE   A 11  ? 0.30372 0.32204 0.29902 -0.02181 0.00906  -0.02881 10  ILE   A O   
37   C  CB  . ILE   A 11  ? 0.30123 0.32966 0.29618 -0.01428 0.00818  -0.01720 10  ILE   A CB  
38   C  CG1 . ILE   A 11  ? 0.25291 0.27136 0.25158 -0.01298 0.00987  -0.01707 10  ILE   A CG1 
39   C  CG2 . ILE   A 11  ? 0.30108 0.33245 0.29127 -0.01395 0.01028  -0.02016 10  ILE   A CG2 
40   C  CD1 . ILE   A 11  ? 0.26153 0.27742 0.26439 -0.01306 0.00821  -0.01408 10  ILE   A CD1 
41   N  N   . GLN   A 12  ? 0.30226 0.33263 0.28959 -0.02252 0.00858  -0.03246 11  GLN   A N   
42   C  CA  . GLN   A 12  ? 0.30350 0.32823 0.28822 -0.02632 0.00991  -0.04006 11  GLN   A CA  
43   C  C   . GLN   A 12  ? 0.35545 0.38145 0.34287 -0.03106 0.00785  -0.04142 11  GLN   A C   
44   O  O   . GLN   A 12  ? 0.37327 0.38972 0.36171 -0.03385 0.00933  -0.04479 11  GLN   A O   
45   C  CB  . GLN   A 12  ? 0.39960 0.43082 0.37741 -0.02792 0.01010  -0.04539 11  GLN   A CB  
46   C  CG  . GLN   A 12  ? 0.47651 0.50009 0.44988 -0.03145 0.01215  -0.05465 11  GLN   A CG  
47   C  CD  . GLN   A 12  ? 0.49353 0.50151 0.46793 -0.02906 0.01596  -0.05691 11  GLN   A CD  
48   O  OE1 . GLN   A 12  ? 0.47753 0.48324 0.45212 -0.02388 0.01832  -0.05490 11  GLN   A OE1 
49   N  NE2 . GLN   A 12  ? 0.55554 0.55315 0.53047 -0.03299 0.01660  -0.06110 11  GLN   A NE2 
50   N  N   . ARG   A 13  ? 0.32274 0.36104 0.31129 -0.03208 0.00452  -0.03873 12  ARG   A N   
51   C  CA  A ARG   A 13  ? 0.31920 0.36208 0.31105 -0.03661 0.00248  -0.03995 12  ARG   A CA  
52   C  CA  B ARG   A 13  ? 0.31913 0.36187 0.31095 -0.03664 0.00252  -0.04003 12  ARG   A CA  
53   C  C   . ARG   A 13  ? 0.35644 0.39245 0.35422 -0.03562 0.00337  -0.03625 12  ARG   A C   
54   O  O   . ARG   A 13  ? 0.34828 0.38193 0.34841 -0.04011 0.00366  -0.03864 12  ARG   A O   
55   C  CB  A ARG   A 13  ? 0.36198 0.42105 0.35425 -0.03641 -0.00136 -0.03708 12  ARG   A CB  
56   C  CB  B ARG   A 13  ? 0.36237 0.42136 0.35448 -0.03664 -0.00133 -0.03739 12  ARG   A CB  
57   C  CG  A ARG   A 13  ? 0.40703 0.47494 0.39261 -0.03808 -0.00267 -0.04079 12  ARG   A CG  
58   C  CG  B ARG   A 13  ? 0.40921 0.47692 0.39487 -0.03961 -0.00272 -0.04236 12  ARG   A CG  
59   C  CD  A ARG   A 13  ? 0.41816 0.50171 0.40396 -0.03602 -0.00654 -0.03578 12  ARG   A CD  
60   C  CD  B ARG   A 13  ? 0.43479 0.51959 0.42113 -0.03934 -0.00697 -0.03902 12  ARG   A CD  
61   N  NE  A ARG   A 13  ? 0.40861 0.50070 0.40016 -0.03815 -0.00922 -0.03477 12  ARG   A NE  
62   N  NE  B ARG   A 13  ? 0.42518 0.51397 0.40980 -0.03336 -0.00769 -0.03223 12  ARG   A NE  
63   C  CZ  A ARG   A 13  ? 0.47268 0.57427 0.46803 -0.03419 -0.01187 -0.02835 12  ARG   A CZ  
64   C  CZ  B ARG   A 13  ? 0.43107 0.52698 0.41937 -0.02945 -0.01014 -0.02522 12  ARG   A CZ  
65   N  NH1 A ARG   A 13  ? 0.47244 0.57472 0.46612 -0.02835 -0.01235 -0.02202 12  ARG   A NH1 
66   N  NH1 B ARG   A 13  ? 0.47377 0.57529 0.46809 -0.03021 -0.01206 -0.02416 12  ARG   A NH1 
67   N  NH2 A ARG   A 13  ? 0.44044 0.55101 0.44148 -0.03610 -0.01393 -0.02820 12  ARG   A NH2 
68   N  NH2 B ARG   A 13  ? 0.40062 0.49791 0.38655 -0.02461 -0.01047 -0.01908 12  ARG   A NH2 
69   N  N   . ILE   A 14  ? 0.29405 0.32724 0.29402 -0.03022 0.00383  -0.03044 13  ILE   A N   
70   C  CA  . ILE   A 14  ? 0.31448 0.34082 0.31896 -0.02894 0.00487  -0.02725 13  ILE   A CA  
71   C  C   . ILE   A 14  ? 0.31225 0.32540 0.31584 -0.03064 0.00784  -0.03038 13  ILE   A C   
72   O  O   . ILE   A 14  ? 0.31918 0.32800 0.32519 -0.03340 0.00860  -0.03060 13  ILE   A O   
73   C  CB  . ILE   A 14  ? 0.28923 0.31462 0.29522 -0.02326 0.00467  -0.02129 13  ILE   A CB  
74   C  CG1 . ILE   A 14  ? 0.27827 0.31430 0.28620 -0.02141 0.00182  -0.01741 13  ILE   A CG1 
75   C  CG2 . ILE   A 14  ? 0.27504 0.29114 0.28393 -0.02179 0.00631  -0.01910 13  ILE   A CG2 
76   C  CD1 . ILE   A 14  ? 0.27662 0.31131 0.28465 -0.01645 0.00143  -0.01195 13  ILE   A CD1 
77   N  N   . ALA   A 15  ? 0.28855 0.29532 0.28854 -0.02883 0.00974  -0.03266 14  ALA   A N   
78   C  CA  . ALA   A 15  ? 0.33928 0.33262 0.33827 -0.02926 0.01263  -0.03532 14  ALA   A CA  
79   C  C   . ALA   A 15  ? 0.36641 0.35603 0.36391 -0.03576 0.01306  -0.04090 14  ALA   A C   
80   O  O   . ALA   A 15  ? 0.35710 0.33679 0.35576 -0.03780 0.01466  -0.04096 14  ALA   A O   
81   C  CB  . ALA   A 15  ? 0.37202 0.36118 0.36766 -0.02542 0.01468  -0.03718 14  ALA   A CB  
82   N  N   . ARG   A 16  ? 0.36019 0.35766 0.35475 -0.03949 0.01159  -0.04553 15  ARG   A N   
83   C  CA  A ARG   A 16  ? 0.43564 0.43062 0.42880 -0.04688 0.01163  -0.05140 15  ARG   A CA  
84   C  CA  B ARG   A 16  ? 0.43554 0.43035 0.42871 -0.04688 0.01167  -0.05140 15  ARG   A CA  
85   C  C   . ARG   A 16  ? 0.42801 0.42671 0.42641 -0.05098 0.01055  -0.04865 15  ARG   A C   
86   O  O   . ARG   A 16  ? 0.41160 0.40160 0.41036 -0.05616 0.01207  -0.05092 15  ARG   A O   
87   C  CB  A ARG   A 16  ? 0.43007 0.43621 0.41928 -0.05023 0.00948  -0.05649 15  ARG   A CB  
88   C  CB  B ARG   A 16  ? 0.43051 0.43596 0.41956 -0.05035 0.00962  -0.05675 15  ARG   A CB  
89   C  CG  A ARG   A 16  ? 0.45621 0.45531 0.43876 -0.04972 0.01154  -0.06290 15  ARG   A CG  
90   C  CG  B ARG   A 16  ? 0.44160 0.44371 0.42848 -0.05890 0.00965  -0.06410 15  ARG   A CG  
91   C  CD  A ARG   A 16  ? 0.49322 0.50470 0.47123 -0.05394 0.00907  -0.06822 15  ARG   A CD  
92   C  CD  B ARG   A 16  ? 0.47175 0.47941 0.45201 -0.06126 0.00871  -0.07116 15  ARG   A CD  
93   N  NE  A ARG   A 16  ? 0.50552 0.51604 0.47692 -0.05079 0.01067  -0.07223 15  ARG   A NE  
94   N  NE  B ARG   A 16  ? 0.51732 0.54305 0.49747 -0.05867 0.00542  -0.06791 15  ARG   A NE  
95   C  CZ  A ARG   A 16  ? 0.45793 0.48215 0.42504 -0.05074 0.00861  -0.07344 15  ARG   A CZ  
96   C  CZ  B ARG   A 16  ? 0.50903 0.55051 0.49128 -0.06262 0.00167  -0.06748 15  ARG   A CZ  
97   N  NH1 A ARG   A 16  ? 0.46989 0.50982 0.43885 -0.05305 0.00454  -0.07056 15  ARG   A NH1 
98   N  NH1 B ARG   A 16  ? 0.51114 0.55434 0.49573 -0.07043 0.00064  -0.07107 15  ARG   A NH1 
99   N  NH2 A ARG   A 16  ? 0.51434 0.53706 0.47504 -0.04799 0.01077  -0.07748 15  ARG   A NH2 
100  N  NH2 B ARG   A 16  ? 0.45418 0.51041 0.43627 -0.05871 -0.00112 -0.06310 15  ARG   A NH2 
101  N  N   . GLN   A 17  ? 0.37301 0.38468 0.37536 -0.04879 0.00811  -0.04376 16  GLN   A N   
102  C  CA  . GLN   A 17  ? 0.33294 0.35021 0.34063 -0.05190 0.00738  -0.04117 16  GLN   A CA  
103  C  C   . GLN   A 17  ? 0.39786 0.40365 0.40760 -0.05005 0.00994  -0.03732 16  GLN   A C   
104  O  O   . GLN   A 17  ? 0.37042 0.37471 0.38267 -0.05481 0.01090  -0.03713 16  GLN   A O   
105  C  CB  . GLN   A 17  ? 0.34896 0.38237 0.36019 -0.04863 0.00436  -0.03701 16  GLN   A CB  
106  C  CG  . GLN   A 17  ? 0.31093 0.35309 0.32821 -0.05113 0.00370  -0.03468 16  GLN   A CG  
107  C  CD  . GLN   A 17  ? 0.41245 0.46079 0.43092 -0.05999 0.00307  -0.03953 16  GLN   A CD  
108  O  OE1 . GLN   A 17  ? 0.42187 0.47361 0.43693 -0.06382 0.00165  -0.04459 16  GLN   A OE1 
109  N  NE2 . GLN   A 17  ? 0.37761 0.42825 0.40079 -0.06372 0.00414  -0.03817 16  GLN   A NE2 
110  N  N   . ALA   A 18  ? 0.32538 0.32397 0.33405 -0.04351 0.01104  -0.03403 17  ALA   A N   
111  C  CA  . ALA   A 18  ? 0.37204 0.35997 0.38179 -0.04162 0.01322  -0.03050 17  ALA   A CA  
112  C  C   . ALA   A 18  ? 0.40064 0.37476 0.40793 -0.04592 0.01578  -0.03367 17  ALA   A C   
113  O  O   . ALA   A 18  ? 0.37630 0.34453 0.38493 -0.04822 0.01729  -0.03133 17  ALA   A O   
114  C  CB  . ALA   A 18  ? 0.33045 0.31426 0.33940 -0.03432 0.01360  -0.02707 17  ALA   A CB  
115  N  N   . SER   A 19  ? 0.42615 0.39446 0.42937 -0.04704 0.01649  -0.03900 18  SER   A N   
116  C  CA  . SER   A 19  ? 0.46021 0.41306 0.46050 -0.05081 0.01909  -0.04251 18  SER   A CA  
117  C  C   . SER   A 19  ? 0.49932 0.45358 0.50109 -0.05993 0.01900  -0.04451 18  SER   A C   
118  O  O   . SER   A 19  ? 0.58107 0.52370 0.58269 -0.06315 0.02121  -0.04325 18  SER   A O   
119  C  CB  . SER   A 19  ? 0.53422 0.48151 0.52948 -0.05001 0.01991  -0.04887 18  SER   A CB  
120  O  OG  . SER   A 19  ? 0.61049 0.53927 0.60280 -0.04944 0.02304  -0.05062 18  SER   A OG  
121  N  N   . LEU   A 20  ? 0.43860 0.40780 0.44191 -0.06430 0.01642  -0.04724 19  LEU   A N   
122  C  CA  A LEU   A 20  ? 0.47217 0.44678 0.47815 -0.07342 0.01597  -0.04897 19  LEU   A CA  
123  C  CA  B LEU   A 20  ? 0.47253 0.44673 0.47843 -0.07343 0.01603  -0.04900 19  LEU   A CA  
124  C  C   . LEU   A 20  ? 0.49583 0.47382 0.50674 -0.07348 0.01675  -0.04257 19  LEU   A C   
125  O  O   . LEU   A 20  ? 0.47282 0.44669 0.48503 -0.08044 0.01836  -0.04247 19  LEU   A O   
126  C  CB  A LEU   A 20  ? 0.47333 0.46697 0.48084 -0.07655 0.01246  -0.05215 19  LEU   A CB  
127  C  CB  B LEU   A 20  ? 0.47364 0.46620 0.48078 -0.07689 0.01259  -0.05259 19  LEU   A CB  
128  C  CG  A LEU   A 20  ? 0.51368 0.50872 0.51669 -0.08176 0.01119  -0.06021 19  LEU   A CG  
129  C  CG  B LEU   A 20  ? 0.46650 0.46997 0.47784 -0.08619 0.01147  -0.05415 19  LEU   A CG  
130  C  CD1 A LEU   A 20  ? 0.44981 0.46740 0.45572 -0.08367 0.00716  -0.06078 19  LEU   A CD1 
131  C  CD1 B LEU   A 20  ? 0.50810 0.49726 0.51649 -0.09541 0.01365  -0.05945 19  LEU   A CD1 
132  C  CD2 A LEU   A 20  ? 0.44874 0.43178 0.45000 -0.09137 0.01309  -0.06533 19  LEU   A CD2 
133  C  CD2 B LEU   A 20  ? 0.46428 0.48810 0.47700 -0.08759 0.00748  -0.05676 19  LEU   A CD2 
134  N  N   . THR   A 21  ? 0.40321 0.38892 0.41664 -0.06614 0.01575  -0.03731 20  THR   A N   
135  C  CA  . THR   A 21  ? 0.39549 0.38682 0.41326 -0.06572 0.01636  -0.03192 20  THR   A CA  
136  C  C   . THR   A 21  ? 0.43485 0.41051 0.45071 -0.06497 0.01946  -0.02838 20  THR   A C   
137  O  O   . THR   A 21  ? 0.45315 0.42913 0.47101 -0.06926 0.02108  -0.02577 20  THR   A O   
138  C  CB  . THR   A 21  ? 0.37249 0.37494 0.39265 -0.05793 0.01439  -0.02814 20  THR   A CB  
139  O  OG1 . THR   A 21  ? 0.37894 0.39602 0.40068 -0.05839 0.01141  -0.03058 20  THR   A OG1 
140  C  CG2 . THR   A 21  ? 0.36654 0.37476 0.39056 -0.05674 0.01527  -0.02329 20  THR   A CG2 
141  N  N   . PHE   A 22  ? 0.45999 0.42284 0.47203 -0.05948 0.02036  -0.02792 21  PHE   A N   
142  C  CA  . PHE   A 22  ? 0.52378 0.47245 0.53376 -0.05698 0.02282  -0.02377 21  PHE   A CA  
143  C  C   . PHE   A 22  ? 0.65347 0.58494 0.65905 -0.05873 0.02472  -0.02736 21  PHE   A C   
144  O  O   . PHE   A 22  ? 0.72668 0.65288 0.72977 -0.05338 0.02461  -0.02938 21  PHE   A O   
145  C  CB  . PHE   A 22  ? 0.46518 0.41499 0.47515 -0.04797 0.02204  -0.01962 21  PHE   A CB  
146  C  CG  . PHE   A 22  ? 0.46374 0.42856 0.47733 -0.04555 0.02019  -0.01690 21  PHE   A CG  
147  C  CD1 . PHE   A 22  ? 0.38957 0.35833 0.40505 -0.04698 0.02114  -0.01311 21  PHE   A CD1 
148  C  CD2 . PHE   A 22  ? 0.42175 0.39583 0.43638 -0.04141 0.01780  -0.01793 21  PHE   A CD2 
149  C  CE1 . PHE   A 22  ? 0.39053 0.37207 0.40902 -0.04397 0.01976  -0.01118 21  PHE   A CE1 
150  C  CE2 . PHE   A 22  ? 0.41744 0.40311 0.43505 -0.03857 0.01626  -0.01540 21  PHE   A CE2 
151  C  CZ  . PHE   A 22  ? 0.34998 0.33918 0.36956 -0.03959 0.01726  -0.01240 21  PHE   A CZ  
152  N  N   . ARG   A 23  ? 0.78651 0.70903 0.79110 -0.06617 0.02669  -0.02820 22  ARG   A N   
153  C  CA  . ARG   A 23  ? 0.82312 0.72783 0.82322 -0.06864 0.02863  -0.03250 22  ARG   A CA  
154  C  C   . ARG   A 23  ? 0.94698 0.83359 0.94439 -0.06611 0.03146  -0.02744 22  ARG   A C   
155  O  O   . ARG   A 23  ? 0.84253 0.72592 0.83924 -0.05743 0.03154  -0.02343 22  ARG   A O   
156  C  CB  . ARG   A 23  ? 0.86522 0.77059 0.86540 -0.07983 0.02874  -0.03800 22  ARG   A CB  
157  C  CG  . ARG   A 23  ? 0.76600 0.68360 0.76629 -0.08186 0.02608  -0.04504 22  ARG   A CG  
158  C  CD  . ARG   A 23  ? 0.80358 0.70715 0.79814 -0.08145 0.02707  -0.05203 22  ARG   A CD  
159  N  NE  . ARG   A 23  ? 0.81988 0.71557 0.81209 -0.07082 0.02803  -0.05013 22  ARG   A NE  
160  C  CZ  . ARG   A 23  ? 0.84732 0.72351 0.83629 -0.06722 0.03088  -0.04899 22  ARG   A CZ  
161  N  NH1 . ARG   A 23  ? 0.89103 0.75113 0.87795 -0.07334 0.03324  -0.04930 22  ARG   A NH1 
162  N  NH2 . ARG   A 23  ? 0.81314 0.68607 0.80108 -0.05722 0.03142  -0.04718 22  ARG   A NH2 
163  N  N   . ALA   A 42  ? 0.97803 0.93206 0.99254 -0.06929 0.03064  -0.00435 41  ALA   A N   
164  C  CA  . ALA   A 42  ? 0.95160 0.91541 0.96782 -0.07014 0.03212  0.00008  41  ALA   A CA  
165  C  C   . ALA   A 42  ? 1.00453 0.98522 1.02637 -0.07674 0.03230  -0.00197 41  ALA   A C   
166  O  O   . ALA   A 42  ? 1.01683 1.00066 1.04099 -0.08206 0.03118  -0.00673 41  ALA   A O   
167  N  N   . PRO   A 43  ? 0.88703 0.87956 0.91103 -0.07629 0.03371  0.00141  42  PRO   A N   
168  C  CA  . PRO   A 43  ? 0.89360 0.90491 0.92396 -0.08168 0.03408  -0.00020 42  PRO   A CA  
169  C  C   . PRO   A 43  ? 0.97508 0.98449 1.00704 -0.09337 0.03579  -0.00159 42  PRO   A C   
170  O  O   . PRO   A 43  ? 0.94716 0.97124 0.98479 -0.09847 0.03470  -0.00512 42  PRO   A O   
171  C  CB  . PRO   A 43  ? 0.83322 0.85336 0.86386 -0.07893 0.03642  0.00438  42  PRO   A CB  
172  C  CG  . PRO   A 43  ? 0.80693 0.81731 0.83231 -0.06983 0.03550  0.00664  42  PRO   A CG  
173  C  CD  . PRO   A 43  ? 0.88627 0.87723 0.90705 -0.07023 0.03486  0.00641  42  PRO   A CD  
174  N  N   . MET   A 44  ? 1.01285 1.00430 1.03990 -0.09781 0.03830  0.00116  43  MET   A N   
175  C  CA  . MET   A 44  ? 1.06863 1.05705 1.09677 -0.10997 0.04074  0.00100  43  MET   A CA  
176  C  C   . MET   A 44  ? 1.08184 1.07127 1.11240 -0.11626 0.03848  -0.00607 43  MET   A C   
177  O  O   . MET   A 44  ? 1.14428 1.14485 1.17963 -0.12603 0.03902  -0.00811 43  MET   A O   
178  C  CB  . MET   A 44  ? 1.00825 0.97365 1.02957 -0.11213 0.04366  0.00569  43  MET   A CB  
179  N  N   . GLN   A 45  ? 1.06427 1.04329 1.09153 -0.11112 0.03599  -0.01000 44  GLN   A N   
180  C  CA  . GLN   A 45  ? 1.02506 1.00316 1.05295 -0.11707 0.03398  -0.01713 44  GLN   A CA  
181  C  C   . GLN   A 45  ? 1.01900 1.02266 1.05420 -0.11993 0.03144  -0.02047 44  GLN   A C   
182  O  O   . GLN   A 45  ? 0.88754 0.90677 0.92623 -0.11242 0.03004  -0.01858 44  GLN   A O   
183  C  CB  . GLN   A 45  ? 1.04980 1.01597 1.07299 -0.10920 0.03183  -0.02053 44  GLN   A CB  
184  C  CG  . GLN   A 45  ? 1.11621 1.07769 1.13793 -0.11520 0.03027  -0.02827 44  GLN   A CG  
185  C  CD  . GLN   A 45  ? 1.29033 1.22919 1.30514 -0.11080 0.03087  -0.03046 44  GLN   A CD  
186  O  OE1 . GLN   A 45  ? 1.27089 1.20580 1.28353 -0.10040 0.03030  -0.02821 44  GLN   A OE1 
187  N  NE2 . GLN   A 45  ? 1.33958 1.26360 1.35103 -0.11879 0.03213  -0.03509 44  GLN   A NE2 
188  N  N   . PRO   A 46  ? 1.10524 1.11397 1.14296 -0.13064 0.03077  -0.02536 45  PRO   A N   
189  C  CA  . PRO   A 46  ? 0.96028 0.99400 1.00479 -0.13251 0.02753  -0.02898 45  PRO   A CA  
190  C  C   . PRO   A 46  ? 0.89661 0.93150 0.93886 -0.12597 0.02352  -0.03377 45  PRO   A C   
191  O  O   . PRO   A 46  ? 0.96186 0.97820 0.99755 -0.12347 0.02341  -0.03628 45  PRO   A O   
192  C  CB  . PRO   A 46  ? 1.00362 1.04035 1.05076 -0.14748 0.02821  -0.03271 45  PRO   A CB  
193  C  CG  . PRO   A 46  ? 1.07450 1.08862 1.11687 -0.15319 0.03260  -0.02933 45  PRO   A CG  
194  C  CD  . PRO   A 46  ? 1.15113 1.14416 1.18607 -0.14237 0.03308  -0.02728 45  PRO   A CD  
195  N  N   . GLY   A 47  ? 0.65903 0.71680 0.70685 -0.12287 0.02035  -0.03473 46  GLY   A N   
196  C  CA  . GLY   A 47  ? 0.52054 0.58191 0.56637 -0.11525 0.01664  -0.03751 46  GLY   A CA  
197  C  C   . GLY   A 47  ? 0.47911 0.53366 0.52206 -0.10249 0.01672  -0.03335 46  GLY   A C   
198  O  O   . GLY   A 47  ? 0.44851 0.50870 0.49066 -0.09566 0.01375  -0.03444 46  GLY   A O   
199  N  N   . PHE   A 48  ? 0.45930 0.50237 0.50045 -0.09941 0.01994  -0.02845 47  PHE   A N   
200  C  CA  . PHE   A 48  ? 0.42615 0.46345 0.46467 -0.08804 0.01982  -0.02477 47  PHE   A CA  
201  C  C   . PHE   A 48  ? 0.43008 0.48564 0.47319 -0.08064 0.01756  -0.02300 47  PHE   A C   
202  O  O   . PHE   A 48  ? 0.39178 0.44594 0.43274 -0.07308 0.01536  -0.02318 47  PHE   A O   
203  C  CB  . PHE   A 48  ? 0.50669 0.53144 0.54273 -0.08691 0.02343  -0.01971 47  PHE   A CB  
204  C  CG  . PHE   A 48  ? 0.45300 0.47351 0.48667 -0.07622 0.02315  -0.01612 47  PHE   A CG  
205  C  CD1 . PHE   A 48  ? 0.47761 0.48407 0.50626 -0.07095 0.02237  -0.01677 47  PHE   A CD1 
206  C  CD2 . PHE   A 48  ? 0.44839 0.47975 0.48497 -0.07158 0.02373  -0.01249 47  PHE   A CD2 
207  C  CE1 . PHE   A 48  ? 0.46736 0.47104 0.49428 -0.06206 0.02190  -0.01365 47  PHE   A CE1 
208  C  CE2 . PHE   A 48  ? 0.51883 0.54587 0.55288 -0.06253 0.02329  -0.00983 47  PHE   A CE2 
209  C  CZ  . PHE   A 48  ? 0.45514 0.46854 0.48453 -0.05817 0.02223  -0.01031 47  PHE   A CZ  
210  N  N   . PRO   A 49  ? 0.41312 0.48564 0.46245 -0.08197 0.01815  -0.02114 48  PRO   A N   
211  C  CA  . PRO   A 49  ? 0.32938 0.41676 0.38254 -0.07324 0.01626  -0.01930 48  PRO   A CA  
212  C  C   . PRO   A 49  ? 0.38612 0.48295 0.44029 -0.07086 0.01207  -0.02214 48  PRO   A C   
213  O  O   . PRO   A 49  ? 0.37851 0.47659 0.43182 -0.06196 0.01020  -0.02058 48  PRO   A O   
214  C  CB  . PRO   A 49  ? 0.43102 0.53596 0.49117 -0.07661 0.01807  -0.01768 48  PRO   A CB  
215  C  CG  . PRO   A 49  ? 0.43037 0.52605 0.48902 -0.08618 0.02160  -0.01717 48  PRO   A CG  
216  C  CD  . PRO   A 49  ? 0.47619 0.55644 0.52975 -0.09145 0.02054  -0.02083 48  PRO   A CD  
217  N  N   . GLU   A 50  ? 0.34713 0.45056 0.40268 -0.07903 0.01050  -0.02623 49  GLU   A N   
218  C  CA  . GLU   A 50  ? 0.36698 0.48005 0.42251 -0.07727 0.00632  -0.02894 49  GLU   A CA  
219  C  C   . GLU   A 50  ? 0.38463 0.48145 0.43262 -0.07261 0.00545  -0.02996 49  GLU   A C   
220  O  O   . GLU   A 50  ? 0.36632 0.46838 0.41339 -0.06590 0.00272  -0.02913 49  GLU   A O   
221  C  CB  . GLU   A 50  ? 0.39391 0.51719 0.45175 -0.08814 0.00477  -0.03383 49  GLU   A CB  
222  C  CG  . GLU   A 50  ? 0.41331 0.55802 0.48002 -0.09289 0.00496  -0.03295 49  GLU   A CG  
223  C  CD  . GLU   A 50  ? 0.59503 0.73317 0.66325 -0.09956 0.00951  -0.03136 49  GLU   A CD  
224  O  OE1 . GLU   A 50  ? 0.57820 0.69424 0.64023 -0.10089 0.01223  -0.03101 49  GLU   A OE1 
225  O  OE2 . GLU   A 50  ? 0.67513 0.83102 0.75084 -0.10327 0.01045  -0.03009 49  GLU   A OE2 
226  N  N   . ASN   A 51  ? 0.33366 0.41094 0.37631 -0.07579 0.00792  -0.03136 50  ASN   A N   
227  C  CA  . ASN   A 51  ? 0.34770 0.41078 0.38378 -0.07110 0.00750  -0.03240 50  ASN   A CA  
228  C  C   . ASN   A 51  ? 0.35634 0.41548 0.39170 -0.06098 0.00775  -0.02753 50  ASN   A C   
229  O  O   . ASN   A 51  ? 0.36445 0.42240 0.39699 -0.05537 0.00598  -0.02729 50  ASN   A O   
230  C  CB  . ASN   A 51  ? 0.39314 0.43656 0.42424 -0.07613 0.01025  -0.03496 50  ASN   A CB  
231  C  CG  . ASN   A 51  ? 0.42166 0.46525 0.45078 -0.08490 0.00926  -0.04153 50  ASN   A CG  
232  O  OD1 . ASN   A 51  ? 0.47380 0.53000 0.50313 -0.08533 0.00607  -0.04446 50  ASN   A OD1 
233  N  ND2 . ASN   A 51  ? 0.44086 0.47070 0.46783 -0.09215 0.01190  -0.04380 50  ASN   A ND2 
234  N  N   . LEU   A 52  ? 0.33020 0.38769 0.36779 -0.05903 0.00997  -0.02372 51  LEU   A N   
235  C  CA  . LEU   A 52  ? 0.29870 0.35302 0.33561 -0.05015 0.01011  -0.01965 51  LEU   A CA  
236  C  C   . LEU   A 52  ? 0.33429 0.40283 0.37437 -0.04438 0.00730  -0.01831 51  LEU   A C   
237  O  O   . LEU   A 52  ? 0.31790 0.38249 0.35580 -0.03760 0.00620  -0.01637 51  LEU   A O   
238  C  CB  . LEU   A 52  ? 0.32492 0.37647 0.36316 -0.04998 0.01304  -0.01647 51  LEU   A CB  
239  C  CG  . LEU   A 52  ? 0.36812 0.41305 0.40422 -0.04193 0.01342  -0.01308 51  LEU   A CG  
240  C  CD1 . LEU   A 52  ? 0.35181 0.38018 0.38246 -0.04060 0.01392  -0.01305 51  LEU   A CD1 
241  C  CD2 . LEU   A 52  ? 0.41933 0.46651 0.45701 -0.04162 0.01599  -0.01037 51  LEU   A CD2 
242  N  N   . SER   A 53  ? 0.31729 0.40266 0.36273 -0.04697 0.00612  -0.01903 52  SER   A N   
243  C  CA  A SER   A 53  ? 0.31898 0.41832 0.36761 -0.04087 0.00326  -0.01738 52  SER   A CA  
244  C  CA  B SER   A 53  ? 0.32028 0.41946 0.36886 -0.04079 0.00327  -0.01735 52  SER   A CA  
245  C  C   . SER   A 53  ? 0.28902 0.38746 0.33374 -0.03922 0.00029  -0.01853 52  SER   A C   
246  O  O   . SER   A 53  ? 0.35065 0.44966 0.39437 -0.03194 -0.00135 -0.01571 52  SER   A O   
247  C  CB  A SER   A 53  ? 0.37979 0.49914 0.43546 -0.04440 0.00245  -0.01812 52  SER   A CB  
248  C  CB  B SER   A 53  ? 0.37924 0.49850 0.43493 -0.04401 0.00247  -0.01795 52  SER   A CB  
249  O  OG  A SER   A 53  ? 0.38793 0.52116 0.44688 -0.03763 -0.00047 -0.01611 52  SER   A OG  
250  O  OG  B SER   A 53  ? 0.37997 0.50240 0.43949 -0.04300 0.00535  -0.01592 52  SER   A OG  
251  N  N   . LYS   A 54  ? 0.29290 0.38951 0.33491 -0.04616 -0.00026 -0.02272 53  LYS   A N   
252  C  CA  A LYS   A 54  ? 0.32242 0.41862 0.35977 -0.04508 -0.00271 -0.02432 53  LYS   A CA  
253  C  CA  B LYS   A 54  ? 0.32216 0.41837 0.35952 -0.04508 -0.00271 -0.02432 53  LYS   A CA  
254  C  C   . LYS   A 54  ? 0.35874 0.43946 0.39090 -0.03960 -0.00155 -0.02239 53  LYS   A C   
255  O  O   . LYS   A 54  ? 0.30629 0.38890 0.33606 -0.03474 -0.00345 -0.02053 53  LYS   A O   
256  C  CB  A LYS   A 54  ? 0.34339 0.43901 0.37813 -0.05403 -0.00298 -0.03026 53  LYS   A CB  
257  C  CB  B LYS   A 54  ? 0.34321 0.43874 0.37793 -0.05399 -0.00297 -0.03024 53  LYS   A CB  
258  C  CG  A LYS   A 54  ? 0.36386 0.46211 0.39336 -0.05384 -0.00555 -0.03288 53  LYS   A CG  
259  C  CG  B LYS   A 54  ? 0.33767 0.45195 0.37707 -0.05988 -0.00535 -0.03264 53  LYS   A CG  
260  C  CD  A LYS   A 54  ? 0.45567 0.56972 0.48700 -0.04792 -0.00916 -0.02920 53  LYS   A CD  
261  C  CD  B LYS   A 54  ? 0.42119 0.53097 0.45795 -0.07033 -0.00476 -0.03914 53  LYS   A CD  
262  C  CE  A LYS   A 54  ? 0.43283 0.54821 0.45768 -0.04698 -0.01130 -0.03073 53  LYS   A CE  
263  C  CE  B LYS   A 54  ? 0.40613 0.53616 0.44620 -0.07665 -0.00821 -0.04248 53  LYS   A CE  
264  N  NZ  A LYS   A 54  ? 0.40400 0.51153 0.42366 -0.05439 -0.01016 -0.03768 53  LYS   A NZ  
265  N  NZ  B LYS   A 54  ? 0.48603 0.61291 0.52662 -0.08838 -0.00679 -0.04790 53  LYS   A NZ  
266  N  N   . LEU   A 55  ? 0.28249 0.34849 0.31292 -0.04048 0.00152  -0.02243 54  LEU   A N   
267  C  CA  . LEU   A 55  ? 0.28283 0.33598 0.30930 -0.03541 0.00253  -0.02047 54  LEU   A CA  
268  C  C   . LEU   A 55  ? 0.26998 0.32597 0.29811 -0.02803 0.00153  -0.01571 54  LEU   A C   
269  O  O   . LEU   A 55  ? 0.27900 0.33154 0.30432 -0.02385 0.00066  -0.01391 54  LEU   A O   
270  C  CB  . LEU   A 55  ? 0.28807 0.32692 0.31315 -0.03726 0.00571  -0.02073 54  LEU   A CB  
271  C  CG  . LEU   A 55  ? 0.25744 0.28384 0.27919 -0.03256 0.00687  -0.01882 54  LEU   A CG  
272  C  CD1 . LEU   A 55  ? 0.26302 0.28706 0.28075 -0.03165 0.00615  -0.02090 54  LEU   A CD1 
273  C  CD2 . LEU   A 55  ? 0.29550 0.30970 0.31619 -0.03477 0.00970  -0.01890 54  LEU   A CD2 
274  N  N   . LYS   A 56  ? 0.26477 0.32682 0.29733 -0.02649 0.00188  -0.01374 55  LYS   A N   
275  C  CA  . LYS   A 56  ? 0.26543 0.32886 0.29934 -0.01933 0.00117  -0.00988 55  LYS   A CA  
276  C  C   . LYS   A 56  ? 0.30219 0.37439 0.33608 -0.01569 -0.00189 -0.00824 55  LYS   A C   
277  O  O   . LYS   A 56  ? 0.29992 0.36764 0.33207 -0.01028 -0.00265 -0.00514 55  LYS   A O   
278  C  CB  . LYS   A 56  ? 0.31555 0.38616 0.35430 -0.01836 0.00230  -0.00898 55  LYS   A CB  
279  C  CG  . LYS   A 56  ? 0.37380 0.43602 0.41207 -0.02015 0.00541  -0.00901 55  LYS   A CG  
280  C  CD  . LYS   A 56  ? 0.42044 0.49281 0.46348 -0.01842 0.00655  -0.00807 55  LYS   A CD  
281  C  CE  . LYS   A 56  ? 0.57569 0.64466 0.61879 -0.02308 0.00979  -0.00850 55  LYS   A CE  
282  N  NZ  . LYS   A 56  ? 0.59474 0.67121 0.64103 -0.02003 0.01164  -0.00727 55  LYS   A NZ  
283  N  N   . SER   A 57  ? 0.29921 0.38437 0.33498 -0.01883 -0.00379 -0.01002 56  SER   A N   
284  C  CA  . SER   A 57  ? 0.27970 0.37458 0.31506 -0.01523 -0.00702 -0.00790 56  SER   A CA  
285  C  C   . SER   A 57  ? 0.33331 0.42065 0.36239 -0.01501 -0.00761 -0.00771 56  SER   A C   
286  O  O   . SER   A 57  ? 0.34626 0.43474 0.37357 -0.01001 -0.00932 -0.00388 56  SER   A O   
287  C  CB  . SER   A 57  ? 0.37582 0.48796 0.41456 -0.01936 -0.00921 -0.01021 56  SER   A CB  
288  O  OG  . SER   A 57  ? 0.51542 0.63431 0.55078 -0.01902 -0.01221 -0.00993 56  SER   A OG  
289  N  N   . LEU   A 58  ? 0.28831 0.36759 0.31388 -0.02014 -0.00596 -0.01159 57  LEU   A N   
290  C  CA  . LEU   A 58  ? 0.31972 0.39192 0.33960 -0.01941 -0.00578 -0.01156 57  LEU   A CA  
291  C  C   . LEU   A 58  ? 0.30570 0.36728 0.32472 -0.01429 -0.00459 -0.00745 57  LEU   A C   
292  O  O   . LEU   A 58  ? 0.30821 0.36916 0.32433 -0.01124 -0.00551 -0.00443 57  LEU   A O   
293  C  CB  . LEU   A 58  ? 0.33195 0.39679 0.34864 -0.02503 -0.00378 -0.01693 57  LEU   A CB  
294  C  CG  . LEU   A 58  ? 0.33514 0.40906 0.35115 -0.03124 -0.00510 -0.02201 57  LEU   A CG  
295  C  CD1 . LEU   A 58  ? 0.39327 0.45615 0.40631 -0.03652 -0.00250 -0.02752 57  LEU   A CD1 
296  C  CD2 . LEU   A 58  ? 0.39409 0.47852 0.40643 -0.03022 -0.00794 -0.02171 57  LEU   A CD2 
297  N  N   . LEU   A 59  ? 0.27843 0.33169 0.29958 -0.01386 -0.00251 -0.00728 58  LEU   A N   
298  C  CA  A LEU   A 59  ? 0.27427 0.31800 0.29462 -0.00978 -0.00164 -0.00399 58  LEU   A CA  
299  C  CA  B LEU   A 59  ? 0.27506 0.31878 0.29545 -0.00978 -0.00163 -0.00400 58  LEU   A CA  
300  C  C   . LEU   A 59  ? 0.30695 0.35417 0.32851 -0.00450 -0.00346 0.00036  58  LEU   A C   
301  O  O   . LEU   A 59  ? 0.31270 0.35368 0.33220 -0.00173 -0.00359 0.00341  58  LEU   A O   
302  C  CB  A LEU   A 59  ? 0.29833 0.33434 0.32038 -0.01031 0.00054  -0.00469 58  LEU   A CB  
303  C  CB  B LEU   A 59  ? 0.29826 0.33458 0.32045 -0.01034 0.00053  -0.00472 58  LEU   A CB  
304  C  CG  A LEU   A 59  ? 0.33424 0.35965 0.35372 -0.01163 0.00244  -0.00572 58  LEU   A CG  
305  C  CG  B LEU   A 59  ? 0.28639 0.31577 0.30702 -0.01451 0.00263  -0.00790 58  LEU   A CG  
306  C  CD1 A LEU   A 59  ? 0.35551 0.38086 0.37348 -0.01628 0.00337  -0.00980 58  LEU   A CD1 
307  C  CD1 B LEU   A 59  ? 0.27656 0.30002 0.29871 -0.01468 0.00449  -0.00750 58  LEU   A CD1 
308  C  CD2 A LEU   A 59  ? 0.23770 0.25633 0.25834 -0.01086 0.00398  -0.00496 58  LEU   A CD2 
309  C  CD2 B LEU   A 59  ? 0.32871 0.35152 0.34591 -0.01364 0.00316  -0.00771 58  LEU   A CD2 
310  N  N   . THR   A 60  ? 0.29651 0.35363 0.32159 -0.00303 -0.00479 0.00081  59  THR   A N   
311  C  CA  . THR   A 60  ? 0.31250 0.37233 0.33884 0.00303  -0.00643 0.00504  59  THR   A CA  
312  C  C   . THR   A 60  ? 0.33455 0.39574 0.35716 0.00471  -0.00838 0.00834  59  THR   A C   
313  O  O   . THR   A 60  ? 0.39295 0.44856 0.41435 0.00913  -0.00893 0.01258  59  THR   A O   
314  C  CB  . THR   A 60  ? 0.35622 0.42918 0.38759 0.00453  -0.00752 0.00471  59  THR   A CB  
315  O  OG1 . THR   A 60  ? 0.39228 0.46326 0.42678 0.00355  -0.00521 0.00253  59  THR   A OG1 
316  C  CG2 . THR   A 60  ? 0.38583 0.46230 0.41849 0.01183  -0.00942 0.00928  59  THR   A CG2 
317  N  N   . GLN   A 61  ? 0.33497 0.40286 0.35513 0.00086  -0.00926 0.00634  60  GLN   A N   
318  C  CA  . GLN   A 61  ? 0.36316 0.43423 0.37889 0.00180  -0.01094 0.00929  60  GLN   A CA  
319  C  C   . GLN   A 61  ? 0.38774 0.44803 0.39924 0.00101  -0.00920 0.01045  60  GLN   A C   
320  O  O   . GLN   A 61  ? 0.40740 0.46863 0.41527 0.00259  -0.01016 0.01442  60  GLN   A O   
321  C  CB  . GLN   A 61  ? 0.37570 0.45840 0.38961 -0.00252 -0.01235 0.00573  60  GLN   A CB  
322  C  CG  . GLN   A 61  ? 0.43223 0.52844 0.45070 -0.00310 -0.01433 0.00415  60  GLN   A CG  
323  C  CD  . GLN   A 61  ? 0.56288 0.66889 0.57918 -0.00915 -0.01550 -0.00083 60  GLN   A CD  
324  O  OE1 . GLN   A 61  ? 0.63947 0.74820 0.65021 -0.01014 -0.01651 -0.00079 60  GLN   A OE1 
325  N  NE2 . GLN   A 61  ? 0.50043 0.61227 0.52083 -0.01356 -0.01533 -0.00524 60  GLN   A NE2 
326  N  N   . LEU   A 62  ? 0.31977 0.37101 0.33171 -0.00143 -0.00667 0.00741  61  LEU   A N   
327  C  CA  . LEU   A 62  ? 0.34776 0.39142 0.35650 -0.00252 -0.00495 0.00793  61  LEU   A CA  
328  C  C   . LEU   A 62  ? 0.36542 0.40238 0.37373 0.00075  -0.00516 0.01338  61  LEU   A C   
329  O  O   . LEU   A 62  ? 0.45392 0.48597 0.46489 0.00338  -0.00540 0.01485  61  LEU   A O   
330  C  CB  . LEU   A 62  ? 0.31818 0.35434 0.32820 -0.00503 -0.00248 0.00392  61  LEU   A CB  
331  C  CG  . LEU   A 62  ? 0.35769 0.38764 0.36554 -0.00596 -0.00049 0.00375  61  LEU   A CG  
332  C  CD1 . LEU   A 62  ? 0.32239 0.35776 0.32637 -0.00806 -0.00000 0.00129  61  LEU   A CD1 
333  C  CD2 . LEU   A 62  ? 0.34228 0.36483 0.35226 -0.00703 0.00142  0.00094  61  LEU   A CD2 
334  N  N   . ARG   A 63  ? 0.34638 0.38289 0.35103 0.00026  -0.00487 0.01618  62  ARG   A N   
335  C  CA  . ARG   A 63  ? 0.37066 0.39945 0.37465 0.00181  -0.00465 0.02117  62  ARG   A CA  
336  C  C   . ARG   A 63  ? 0.31369 0.33905 0.31627 -0.00109 -0.00239 0.02058  62  ARG   A C   
337  O  O   . ARG   A 63  ? 0.31597 0.34568 0.31713 -0.00328 -0.00108 0.01698  62  ARG   A O   
338  C  CB  . ARG   A 63  ? 0.44841 0.48051 0.44957 0.00440  -0.00658 0.02725  62  ARG   A CB  
339  C  CG  . ARG   A 63  ? 0.47488 0.51716 0.47643 0.00680  -0.00904 0.02733  62  ARG   A CG  
340  C  CD  . ARG   A 63  ? 0.60979 0.65955 0.60664 0.00795  -0.01079 0.03240  62  ARG   A CD  
341  N  NE  . ARG   A 63  ? 0.68928 0.74700 0.68214 0.00410  -0.01007 0.02937  62  ARG   A NE  
342  C  CZ  . ARG   A 63  ? 0.63024 0.69689 0.61803 0.00417  -0.01140 0.03237  62  ARG   A CZ  
343  N  NH1 . ARG   A 63  ? 0.65161 0.72052 0.63778 0.00806  -0.01374 0.03936  62  ARG   A NH1 
344  N  NH2 . ARG   A 63  ? 0.66440 0.73768 0.64822 0.00056  -0.01032 0.02830  62  ARG   A NH2 
345  N  N   . ALA   A 64  ? 0.30742 0.32514 0.31049 -0.00107 -0.00191 0.02397  63  ALA   A N   
346  C  CA  . ALA   A 64  ? 0.30199 0.31813 0.30479 -0.00380 0.00016  0.02387  63  ALA   A CA  
347  C  C   . ALA   A 64  ? 0.35338 0.37753 0.35236 -0.00522 0.00118  0.02482  63  ALA   A C   
348  O  O   . ALA   A 64  ? 0.28652 0.31341 0.28544 -0.00686 0.00331  0.02183  63  ALA   A O   
349  C  CB  . ALA   A 64  ? 0.34927 0.35730 0.35293 -0.00443 0.00010  0.02800  63  ALA   A CB  
350  N  N   . GLU   A 65  ? 0.34916 0.37765 0.34465 -0.00415 -0.00025 0.02895  64  GLU   A N   
351  C  CA  . GLU   A 65  ? 0.34788 0.38464 0.33871 -0.00562 0.00083  0.03024  64  GLU   A CA  
352  C  C   . GLU   A 65  ? 0.32179 0.36589 0.31113 -0.00643 0.00163  0.02360  64  GLU   A C   
353  O  O   . GLU   A 65  ? 0.32655 0.37654 0.31247 -0.00788 0.00358  0.02231  64  GLU   A O   
354  C  CB  . GLU   A 65  ? 0.40183 0.44231 0.38855 -0.00400 -0.00122 0.03646  64  GLU   A CB  
355  C  CG  . GLU   A 65  ? 0.47958 0.52144 0.46748 -0.00072 -0.00422 0.03629  64  GLU   A CG  
356  C  CD  . GLU   A 65  ? 0.72101 0.76683 0.70505 0.00189  -0.00653 0.04323  64  GLU   A CD  
357  O  OE1 . GLU   A 65  ? 0.69005 0.74520 0.66883 0.00087  -0.00659 0.04473  64  GLU   A OE1 
358  O  OE2 . GLU   A 65  ? 0.73312 0.77268 0.71906 0.00533  -0.00823 0.04720  64  GLU   A OE2 
359  N  N   . ASP   A 66  ? 0.32783 0.37170 0.31939 -0.00573 0.00034  0.01922  65  ASP   A N   
360  C  CA  . ASP   A 66  ? 0.28506 0.33393 0.27515 -0.00730 0.00109  0.01248  65  ASP   A CA  
361  C  C   . ASP   A 66  ? 0.29239 0.33678 0.28395 -0.00840 0.00417  0.00812  65  ASP   A C   
362  O  O   . ASP   A 66  ? 0.29803 0.34493 0.28751 -0.00959 0.00548  0.00244  65  ASP   A O   
363  C  CB  . ASP   A 66  ? 0.32164 0.37121 0.31439 -0.00713 -0.00090 0.00925  65  ASP   A CB  
364  C  CG  . ASP   A 66  ? 0.43624 0.49205 0.42846 -0.00511 -0.00413 0.01338  65  ASP   A CG  
365  O  OD1 . ASP   A 66  ? 0.48119 0.54488 0.46876 -0.00500 -0.00523 0.01584  65  ASP   A OD1 
366  O  OD2 . ASP   A 66  ? 0.43320 0.48690 0.42953 -0.00333 -0.00554 0.01407  65  ASP   A OD2 
367  N  N   . LEU   A 67  ? 0.26295 0.30067 0.25805 -0.00789 0.00521  0.01044  66  LEU   A N   
368  C  CA  . LEU   A 67  ? 0.27195 0.30651 0.26911 -0.00812 0.00788  0.00744  66  LEU   A CA  
369  C  C   . LEU   A 67  ? 0.26711 0.30460 0.26379 -0.00857 0.00981  0.01085  66  LEU   A C   
370  O  O   . LEU   A 67  ? 0.23556 0.27168 0.23502 -0.00829 0.01187  0.00945  66  LEU   A O   
371  C  CB  . LEU   A 67  ? 0.23794 0.26435 0.23993 -0.00747 0.00740  0.00704  66  LEU   A CB  
372  C  CG  . LEU   A 67  ? 0.24980 0.27393 0.25281 -0.00739 0.00588  0.00423  66  LEU   A CG  
373  C  CD1 . LEU   A 67  ? 0.26730 0.28401 0.27429 -0.00674 0.00585  0.00413  66  LEU   A CD1 
374  C  CD2 . LEU   A 67  ? 0.29405 0.32036 0.29494 -0.00859 0.00695  -0.00162 66  LEU   A CD2 
375  N  N   . ASN   A 68  ? 0.27918 0.32122 0.27262 -0.00925 0.00918  0.01575  67  ASN   A N   
376  C  CA  . ASN   A 68  ? 0.31110 0.35649 0.30404 -0.01056 0.01104  0.02018  67  ASN   A CA  
377  C  C   . ASN   A 68  ? 0.31779 0.35692 0.31601 -0.01144 0.01108  0.02282  67  ASN   A C   
378  O  O   . ASN   A 68  ? 0.28098 0.32343 0.28105 -0.01279 0.01324  0.02410  67  ASN   A O   
379  C  CB  . ASN   A 68  ? 0.29174 0.34467 0.28263 -0.01057 0.01439  0.01644  67  ASN   A CB  
380  C  CG  . ASN   A 68  ? 0.36073 0.42101 0.34497 -0.01053 0.01435  0.01433  67  ASN   A CG  
381  O  OD1 . ASN   A 68  ? 0.32841 0.38934 0.31101 -0.00984 0.01486  0.00772  67  ASN   A OD1 
382  N  ND2 . ASN   A 68  ? 0.34163 0.40708 0.32161 -0.01152 0.01361  0.02004  67  ASN   A ND2 
383  N  N   . ILE   A 69  ? 0.28458 0.31567 0.28519 -0.01083 0.00869  0.02356  68  ILE   A N   
384  C  CA  . ILE   A 69  ? 0.28098 0.30570 0.28578 -0.01198 0.00826  0.02541  68  ILE   A CA  
385  C  C   . ILE   A 69  ? 0.32441 0.34406 0.32789 -0.01312 0.00659  0.03137  68  ILE   A C   
386  O  O   . ILE   A 69  ? 0.35808 0.37347 0.36019 -0.01113 0.00450  0.03228  68  ILE   A O   
387  C  CB  . ILE   A 69  ? 0.28479 0.30336 0.29268 -0.01040 0.00712  0.02142  68  ILE   A CB  
388  C  CG1 . ILE   A 69  ? 0.26567 0.28733 0.27461 -0.00920 0.00893  0.01614  68  ILE   A CG1 
389  C  CG2 . ILE   A 69  ? 0.33722 0.34998 0.34845 -0.01189 0.00636  0.02319  68  ILE   A CG2 
390  C  CD1 . ILE   A 69  ? 0.28885 0.30467 0.29993 -0.00778 0.00804  0.01261  68  ILE   A CD1 
391  N  N   . ALA   A 70  ? 0.34237 0.36241 0.34647 -0.01626 0.00762  0.03552  69  ALA   A N   
392  C  CA  . ALA   A 70  ? 0.39386 0.40637 0.39654 -0.01767 0.00616  0.04125  69  ALA   A CA  
393  C  C   . ALA   A 70  ? 0.36457 0.36673 0.37046 -0.01788 0.00449  0.03980  69  ALA   A C   
394  O  O   . ALA   A 70  ? 0.33103 0.33387 0.34064 -0.01919 0.00496  0.03658  69  ALA   A O   
395  C  CB  . ALA   A 70  ? 0.38767 0.40353 0.38967 -0.02206 0.00797  0.04658  69  ALA   A CB  
396  N  N   . PRO   A 71  ? 0.36844 0.36133 0.37272 -0.01628 0.00255  0.04209  70  PRO   A N   
397  C  CA  . PRO   A 71  ? 0.39258 0.37535 0.39907 -0.01647 0.00120  0.04013  70  PRO   A CA  
398  C  C   . PRO   A 71  ? 0.39197 0.37225 0.40052 -0.02193 0.00179  0.04156  70  PRO   A C   
399  O  O   . PRO   A 71  ? 0.38364 0.36493 0.39104 -0.02553 0.00276  0.04647  70  PRO   A O   
400  C  CB  . PRO   A 71  ? 0.40330 0.37695 0.40701 -0.01341 -0.00045 0.04331  70  PRO   A CB  
401  C  CG  . PRO   A 71  ? 0.44475 0.42660 0.44592 -0.01006 -0.00058 0.04472  70  PRO   A CG  
402  C  CD  . PRO   A 71  ? 0.41866 0.41047 0.41894 -0.01335 0.00141  0.04604  70  PRO   A CD  
403  N  N   . ARG   A 72  ? 0.35100 0.32951 0.36267 -0.02291 0.00122  0.03733  71  ARG   A N   
404  C  CA  . ARG   A 72  ? 0.36393 0.34174 0.37822 -0.02845 0.00128  0.03786  71  ARG   A CA  
405  C  C   . ARG   A 72  ? 0.37452 0.33848 0.38752 -0.03017 -0.00051 0.03795  71  ARG   A C   
406  O  O   . ARG   A 72  ? 0.39697 0.35405 0.40871 -0.02633 -0.00175 0.03487  71  ARG   A O   
407  C  CB  . ARG   A 72  ? 0.31073 0.29657 0.32907 -0.02852 0.00153  0.03336  71  ARG   A CB  
408  C  CG  . ARG   A 72  ? 0.32957 0.32769 0.34894 -0.02667 0.00372  0.03304  71  ARG   A CG  
409  C  CD  . ARG   A 72  ? 0.35041 0.35610 0.37387 -0.02600 0.00420  0.02945  71  ARG   A CD  
410  N  NE  . ARG   A 72  ? 0.32754 0.34311 0.35134 -0.02361 0.00661  0.02876  71  ARG   A NE  
411  C  CZ  . ARG   A 72  ? 0.32621 0.34864 0.35308 -0.02143 0.00765  0.02582  71  ARG   A CZ  
412  N  NH1 . ARG   A 72  ? 0.31542 0.33742 0.34547 -0.02143 0.00629  0.02395  71  ARG   A NH1 
413  N  NH2 . ARG   A 72  ? 0.33403 0.36372 0.36036 -0.01890 0.01010  0.02469  71  ARG   A NH2 
414  N  N   . LYS   A 73  ? 0.37492 0.33471 0.38803 -0.03610 -0.00043 0.04139  72  LYS   A N   
415  C  CA  . LYS   A 73  ? 0.40884 0.35369 0.42014 -0.03856 -0.00195 0.04130  72  LYS   A CA  
416  C  C   . LYS   A 73  ? 0.37501 0.32136 0.38955 -0.04513 -0.00273 0.03871  72  LYS   A C   
417  O  O   . LYS   A 73  ? 0.39772 0.35713 0.41627 -0.04824 -0.00186 0.03884  72  LYS   A O   
418  C  CB  . LYS   A 73  ? 0.39913 0.33461 0.40694 -0.04054 -0.00146 0.04795  72  LYS   A CB  
419  C  CG  . LYS   A 73  ? 0.44920 0.38676 0.45398 -0.03416 -0.00093 0.05127  72  LYS   A CG  
420  C  CD  . LYS   A 73  ? 0.55599 0.47944 0.55639 -0.03323 -0.00137 0.05693  72  LYS   A CD  
421  C  CE  . LYS   A 73  ? 0.68568 0.61369 0.68323 -0.02675 -0.00129 0.06055  72  LYS   A CE  
422  N  NZ  . LYS   A 73  ? 0.66444 0.58358 0.65769 -0.02738 -0.00111 0.06886  72  LYS   A NZ  
423  N  N   . ALA   A 74  ? 0.39368 0.32705 0.40643 -0.04699 -0.00442 0.03607  73  ALA   A N   
424  C  CA  . ALA   A 74  ? 0.46005 0.39498 0.47532 -0.05295 -0.00584 0.03235  73  ALA   A CA  
425  C  C   . ALA   A 74  ? 0.45929 0.39917 0.47749 -0.06173 -0.00519 0.03633  73  ALA   A C   
426  O  O   . ALA   A 74  ? 0.47765 0.41196 0.49409 -0.06451 -0.00395 0.04195  73  ALA   A O   
427  C  CB  . ALA   A 74  ? 0.47992 0.39852 0.49146 -0.05340 -0.00766 0.02827  73  ALA   A CB  
428  N  N   . THR   A 75  ? 0.42992 0.38128 0.45276 -0.06616 -0.00603 0.03377  74  THR   A N   
429  C  CA  . THR   A 75  ? 0.50146 0.45974 0.52819 -0.07527 -0.00556 0.03696  74  THR   A CA  
430  C  C   . THR   A 75  ? 0.44949 0.39537 0.47489 -0.08362 -0.00760 0.03523  74  THR   A C   
431  O  O   . THR   A 75  ? 0.44013 0.38740 0.46770 -0.09239 -0.00703 0.03885  74  THR   A O   
432  C  CB  . THR   A 75  ? 0.51476 0.49366 0.54805 -0.07581 -0.00554 0.03531  74  THR   A CB  
433  O  OG1 . THR   A 75  ? 0.48795 0.46700 0.52195 -0.07626 -0.00846 0.02947  74  THR   A OG1 
434  C  CG2 . THR   A 75  ? 0.55414 0.54316 0.58811 -0.06718 -0.00355 0.03572  74  THR   A CG2 
435  N  N   . LEU   A 76  ? 0.42662 0.36094 0.44840 -0.08146 -0.00981 0.02953  75  LEU   A N   
436  C  CA  . LEU   A 76  ? 0.49283 0.41537 0.51267 -0.08896 -0.01208 0.02580  75  LEU   A CA  
437  C  C   . LEU   A 76  ? 0.51447 0.45214 0.54003 -0.09710 -0.01388 0.02365  75  LEU   A C   
438  O  O   . LEU   A 76  ? 0.47487 0.40526 0.49948 -0.10534 -0.01595 0.02060  75  LEU   A O   
439  C  CB  . LEU   A 76  ? 0.43471 0.33909 0.45091 -0.09438 -0.01115 0.03007  75  LEU   A CB  
440  C  CG  . LEU   A 76  ? 0.45135 0.34198 0.46225 -0.08570 -0.00957 0.03316  75  LEU   A CG  
441  C  CD1 . LEU   A 76  ? 0.48968 0.36004 0.49634 -0.09049 -0.00886 0.03771  75  LEU   A CD1 
442  C  CD2 . LEU   A 76  ? 0.47552 0.35925 0.48280 -0.07705 -0.01073 0.02687  75  LEU   A CD2 
443  N  N   . GLN   A 77  ? 0.47773 0.43674 0.50927 -0.09471 -0.01326 0.02484  76  GLN   A N   
444  C  CA  . GLN   A 77  ? 0.48871 0.46473 0.52640 -0.10071 -0.01522 0.02285  76  GLN   A CA  
445  C  C   . GLN   A 77  ? 0.52331 0.50722 0.56109 -0.09429 -0.01737 0.01760  76  GLN   A C   
446  O  O   . GLN   A 77  ? 0.46690 0.44946 0.50231 -0.08475 -0.01625 0.01711  76  GLN   A O   
447  C  CB  . GLN   A 77  ? 0.47474 0.47043 0.51971 -0.10249 -0.01285 0.02823  76  GLN   A CB  
448  C  CG  . GLN   A 77  ? 0.49395 0.48415 0.53840 -0.10744 -0.00994 0.03471  76  GLN   A CG  
449  C  CD  . GLN   A 77  ? 0.56937 0.54543 0.61176 -0.11864 -0.01126 0.03487  76  GLN   A CD  
450  O  OE1 . GLN   A 77  ? 0.63112 0.58963 0.66839 -0.12004 -0.00988 0.03831  76  GLN   A OE1 
451  N  NE2 . GLN   A 77  ? 0.58708 0.57068 0.63337 -0.12679 -0.01407 0.03124  76  GLN   A NE2 
452  N  N   . PRO   A 78  ? 0.49371 0.48648 0.53404 -0.09945 -0.02055 0.01384  77  PRO   A N   
453  C  CA  . PRO   A 78  ? 0.43150 0.43329 0.47176 -0.09309 -0.02254 0.00999  77  PRO   A CA  
454  C  C   . PRO   A 78  ? 0.51249 0.53155 0.55830 -0.08587 -0.02055 0.01348  77  PRO   A C   
455  O  O   . PRO   A 78  ? 0.50933 0.53899 0.56069 -0.08770 -0.01836 0.01795  77  PRO   A O   
456  C  CB  . PRO   A 78  ? 0.54377 0.55420 0.58635 -0.10154 -0.02653 0.00629  77  PRO   A CB  
457  C  CG  . PRO   A 78  ? 0.56206 0.57190 0.60793 -0.11275 -0.02632 0.00866  77  PRO   A CG  
458  C  CD  . PRO   A 78  ? 0.56975 0.56780 0.61398 -0.11159 -0.02237 0.01379  77  PRO   A CD  
459  N  N   . LEU   A 79  ? 0.43672 0.45786 0.48053 -0.07750 -0.02104 0.01133  78  LEU   A N   
460  C  CA  . LEU   A 79  ? 0.44428 0.47884 0.49238 -0.06994 -0.01911 0.01401  78  LEU   A CA  
461  C  C   . LEU   A 79  ? 0.37316 0.42735 0.42762 -0.07115 -0.02149 0.01386  78  LEU   A C   
462  O  O   . LEU   A 79  ? 0.41427 0.46985 0.46664 -0.07141 -0.02483 0.01049  78  LEU   A O   
463  C  CB  . LEU   A 79  ? 0.45711 0.48354 0.50004 -0.06069 -0.01820 0.01241  78  LEU   A CB  
464  C  CG  . LEU   A 79  ? 0.48685 0.52452 0.53284 -0.05265 -0.01685 0.01388  78  LEU   A CG  
465  C  CD1 . LEU   A 79  ? 0.43767 0.47606 0.48545 -0.04983 -0.01301 0.01727  78  LEU   A CD1 
466  C  CD2 . LEU   A 79  ? 0.49522 0.52558 0.53581 -0.04605 -0.01730 0.01137  78  LEU   A CD2 
467  N  N   . PRO   A 80  ? 0.41321 0.48356 0.47529 -0.07165 -0.01990 0.01743  79  PRO   A N   
468  C  CA  . PRO   A 80  ? 0.43916 0.53030 0.50847 -0.07277 -0.02230 0.01773  79  PRO   A CA  
469  C  C   . PRO   A 80  ? 0.36295 0.45940 0.43171 -0.06305 -0.02316 0.01706  79  PRO   A C   
470  O  O   . PRO   A 80  ? 0.39090 0.47886 0.45603 -0.05516 -0.02060 0.01747  79  PRO   A O   
471  C  CB  . PRO   A 80  ? 0.45824 0.56398 0.53547 -0.07390 -0.01909 0.02205  79  PRO   A CB  
472  C  CG  . PRO   A 80  ? 0.48735 0.57865 0.56046 -0.07545 -0.01553 0.02394  79  PRO   A CG  
473  C  CD  . PRO   A 80  ? 0.41196 0.48367 0.47628 -0.07018 -0.01564 0.02142  79  PRO   A CD  
474  N  N   . PRO   A 81  ? 0.34823 0.45931 0.42070 -0.06350 -0.02673 0.01644  80  PRO   A N   
475  C  CA  . PRO   A 81  ? 0.39515 0.50918 0.46571 -0.05456 -0.02800 0.01622  80  PRO   A CA  
476  C  C   . PRO   A 81  ? 0.34307 0.46204 0.41693 -0.04464 -0.02439 0.01939  80  PRO   A C   
477  O  O   . PRO   A 81  ? 0.34109 0.45609 0.41149 -0.03684 -0.02439 0.01944  80  PRO   A O   
478  C  CB  . PRO   A 81  ? 0.45140 0.58364 0.52665 -0.05803 -0.03271 0.01589  80  PRO   A CB  
479  C  CG  . PRO   A 81  ? 0.43820 0.57144 0.51509 -0.07025 -0.03453 0.01405  80  PRO   A CG  
480  C  CD  . PRO   A 81  ? 0.42940 0.55488 0.50757 -0.07275 -0.03006 0.01603  80  PRO   A CD  
481  N  N   . ASN   A 82  ? 0.28707 0.41472 0.36725 -0.04480 -0.02122 0.02193  81  ASN   A N   
482  C  CA  . ASN   A 82  ? 0.30119 0.43446 0.38460 -0.03529 -0.01774 0.02418  81  ASN   A CA  
483  C  C   . ASN   A 82  ? 0.34722 0.46412 0.42491 -0.03148 -0.01368 0.02372  81  ASN   A C   
484  O  O   . ASN   A 82  ? 0.42909 0.54759 0.50798 -0.02369 -0.01062 0.02469  81  ASN   A O   
485  C  CB  . ASN   A 82  ? 0.31436 0.46797 0.40776 -0.03637 -0.01605 0.02681  81  ASN   A CB  
486  C  CG  . ASN   A 82  ? 0.37521 0.52718 0.46960 -0.04451 -0.01360 0.02755  81  ASN   A CG  
487  O  OD1 . ASN   A 82  ? 0.34866 0.49013 0.43894 -0.05282 -0.01528 0.02624  81  ASN   A OD1 
488  N  ND2 . ASN   A 82  ? 0.35476 0.51700 0.45435 -0.04200 -0.00944 0.02976  81  ASN   A ND2 
489  N  N   . LEU   A 83  ? 0.30527 0.40628 0.37658 -0.03653 -0.01368 0.02208  82  LEU   A N   
490  C  CA  . LEU   A 83  ? 0.30500 0.39290 0.37141 -0.03246 -0.01016 0.02189  82  LEU   A CA  
491  C  C   . LEU   A 83  ? 0.32569 0.39856 0.38460 -0.02914 -0.01126 0.01957  82  LEU   A C   
492  O  O   . LEU   A 83  ? 0.28456 0.35202 0.34005 -0.03289 -0.01430 0.01767  82  LEU   A O   
493  C  CB  . LEU   A 83  ? 0.39312 0.47442 0.45795 -0.03873 -0.00843 0.02271  82  LEU   A CB  
494  C  CG  . LEU   A 83  ? 0.49372 0.58984 0.56559 -0.04386 -0.00718 0.02538  82  LEU   A CG  
495  C  CD1 . LEU   A 83  ? 0.51490 0.60252 0.58421 -0.05176 -0.00630 0.02676  82  LEU   A CD1 
496  C  CD2 . LEU   A 83  ? 0.43336 0.54136 0.50977 -0.03728 -0.00352 0.02691  82  LEU   A CD2 
497  N  N   . PRO   A 84  ? 0.32093 0.38698 0.37697 -0.02258 -0.00867 0.01938  83  PRO   A N   
498  C  CA  . PRO   A 84  ? 0.29513 0.34886 0.34477 -0.01962 -0.00942 0.01751  83  PRO   A CA  
499  C  C   . PRO   A 84  ? 0.27696 0.31764 0.32133 -0.02376 -0.00960 0.01589  83  PRO   A C   
500  O  O   . PRO   A 84  ? 0.31893 0.35734 0.36366 -0.02688 -0.00808 0.01677  83  PRO   A O   
501  C  CB  . PRO   A 84  ? 0.30536 0.35648 0.35438 -0.01257 -0.00621 0.01786  83  PRO   A CB  
502  C  CG  . PRO   A 84  ? 0.32386 0.38036 0.37625 -0.01333 -0.00336 0.01895  83  PRO   A CG  
503  C  CD  . PRO   A 84  ? 0.35584 0.42528 0.41410 -0.01818 -0.00478 0.02051  83  PRO   A CD  
504  N  N   . PRO   A 85  ? 0.26610 0.29800 0.30523 -0.02335 -0.01121 0.01374  84  PRO   A N   
505  C  CA  . PRO   A 85  ? 0.28955 0.30866 0.32373 -0.02564 -0.01099 0.01205  84  PRO   A CA  
506  C  C   . PRO   A 85  ? 0.26097 0.27350 0.29310 -0.02170 -0.00808 0.01244  84  PRO   A C   
507  O  O   . PRO   A 85  ? 0.27581 0.28018 0.30537 -0.02326 -0.00749 0.01219  84  PRO   A O   
508  C  CB  . PRO   A 85  ? 0.27474 0.28902 0.30424 -0.02535 -0.01324 0.00935  84  PRO   A CB  
509  C  CG  . PRO   A 85  ? 0.28064 0.30252 0.31136 -0.02067 -0.01354 0.01046  84  PRO   A CG  
510  C  CD  . PRO   A 85  ? 0.28847 0.32274 0.32592 -0.02073 -0.01331 0.01300  84  PRO   A CD  
511  N  N   . VAL   A 86  ? 0.27431 0.28995 0.30739 -0.01667 -0.00639 0.01302  85  VAL   A N   
512  C  CA  . VAL   A 86  ? 0.23376 0.24359 0.26453 -0.01333 -0.00396 0.01265  85  VAL   A CA  
513  C  C   . VAL   A 86  ? 0.21961 0.23598 0.25358 -0.01024 -0.00167 0.01375  85  VAL   A C   
514  O  O   . VAL   A 86  ? 0.23066 0.25440 0.26789 -0.00833 -0.00192 0.01458  85  VAL   A O   
515  C  CB  . VAL   A 86  ? 0.27002 0.27378 0.29694 -0.01043 -0.00415 0.01107  85  VAL   A CB  
516  C  CG1 . VAL   A 86  ? 0.26567 0.26453 0.29072 -0.00793 -0.00184 0.01047  85  VAL   A CG1 
517  C  CG2 . VAL   A 86  ? 0.26813 0.26633 0.29163 -0.01294 -0.00615 0.00937  85  VAL   A CG2 
518  N  N   . THR   A 87  ? 0.22645 0.24064 0.25938 -0.00943 0.00055  0.01365  86  THR   A N   
519  C  CA  . THR   A 87  ? 0.23552 0.25447 0.27028 -0.00610 0.00310  0.01360  86  THR   A CA  
520  C  C   . THR   A 87  ? 0.23846 0.25054 0.26960 -0.00376 0.00466  0.01173  86  THR   A C   
521  O  O   . THR   A 87  ? 0.22866 0.23436 0.25668 -0.00494 0.00389  0.01103  86  THR   A O   
522  C  CB  . THR   A 87  ? 0.27911 0.30536 0.31634 -0.00817 0.00455  0.01508  86  THR   A CB  
523  O  OG1 . THR   A 87  ? 0.26407 0.28548 0.29836 -0.01145 0.00435  0.01581  86  THR   A OG1 
524  C  CG2 . THR   A 87  ? 0.28636 0.32177 0.32842 -0.01078 0.00323  0.01690  86  THR   A CG2 
525  N  N   . TYR   A 88  ? 0.24661 0.26030 0.27835 -0.00034 0.00688  0.01066  87  TYR   A N   
526  C  CA  . TYR   A 88  ? 0.22757 0.23503 0.25612 0.00139  0.00839  0.00835  87  TYR   A CA  
527  C  C   . TYR   A 88  ? 0.23510 0.24590 0.26340 0.00258  0.01101  0.00683  87  TYR   A C   
528  O  O   . TYR   A 88  ? 0.24050 0.25678 0.27145 0.00512  0.01257  0.00685  87  TYR   A O   
529  C  CB  . TYR   A 88  ? 0.23420 0.23705 0.26239 0.00453  0.00864  0.00782  87  TYR   A CB  
530  C  CG  . TYR   A 88  ? 0.26079 0.25656 0.28586 0.00531  0.01031  0.00532  87  TYR   A CG  
531  C  CD1 . TYR   A 88  ? 0.24967 0.24124 0.27204 0.00271  0.00961  0.00440  87  TYR   A CD1 
532  C  CD2 . TYR   A 88  ? 0.28619 0.27956 0.31117 0.00855  0.01263  0.00368  87  TYR   A CD2 
533  C  CE1 . TYR   A 88  ? 0.27417 0.26061 0.29421 0.00242  0.01095  0.00204  87  TYR   A CE1 
534  C  CE2 . TYR   A 88  ? 0.25485 0.24084 0.27672 0.00816  0.01408  0.00095  87  TYR   A CE2 
535  C  CZ  . TYR   A 88  ? 0.27234 0.25559 0.29196 0.00465  0.01311  0.00023  87  TYR   A CZ  
536  O  OH  . TYR   A 88  ? 0.32017 0.29756 0.33725 0.00324  0.01433  -0.00252 87  TYR   A OH  
537  N  N   . MET   A 89  ? 0.22346 0.23183 0.24847 0.00107  0.01150  0.00535  88  MET   A N   
538  C  CA  . MET   A 89  ? 0.20742 0.21797 0.23064 0.00216  0.01396  0.00286  88  MET   A CA  
539  C  C   . MET   A 89  ? 0.29526 0.29867 0.31575 0.00328  0.01490  -0.00067 88  MET   A C   
540  O  O   . MET   A 89  ? 0.26334 0.26261 0.28177 0.00124  0.01368  -0.00129 88  MET   A O   
541  C  CB  . MET   A 89  ? 0.27705 0.29189 0.29806 -0.00048 0.01393  0.00370  88  MET   A CB  
542  C  CG  . MET   A 89  ? 0.26975 0.28854 0.29249 -0.00315 0.01253  0.00780  88  MET   A CG  
543  S  SD  . MET   A 89  ? 0.25816 0.27861 0.27700 -0.00582 0.01205  0.00966  88  MET   A SD  
544  C  CE  . MET   A 89  ? 0.32086 0.34783 0.34220 -0.00860 0.01237  0.01423  88  MET   A CE  
545  N  N   . HIS   A 90  ? 0.24454 0.24652 0.26528 0.00653  0.01718  -0.00296 89  HIS   A N   
546  C  CA  . HIS   A 90  ? 0.28334 0.27702 0.30128 0.00719  0.01845  -0.00659 89  HIS   A CA  
547  C  C   . HIS   A 90  ? 0.29209 0.28703 0.30616 0.00523  0.01955  -0.01042 89  HIS   A C   
548  O  O   . HIS   A 90  ? 0.28379 0.28507 0.29717 0.00622  0.02116  -0.01154 89  HIS   A O   
549  C  CB  . HIS   A 90  ? 0.31365 0.30392 0.33304 0.01203  0.02058  -0.00751 89  HIS   A CB  
550  C  CG  . HIS   A 90  ? 0.40663 0.38679 0.42269 0.01270  0.02248  -0.01167 89  HIS   A CG  
551  N  ND1 . HIS   A 90  ? 0.49873 0.46978 0.51327 0.01073  0.02171  -0.01157 89  HIS   A ND1 
552  C  CD2 . HIS   A 90  ? 0.52559 0.50297 0.53925 0.01469  0.02531  -0.01633 89  HIS   A CD2 
553  C  CE1 . HIS   A 90  ? 0.38987 0.35226 0.40142 0.01098  0.02386  -0.01576 89  HIS   A CE1 
554  N  NE2 . HIS   A 90  ? 0.55501 0.52054 0.56576 0.01354  0.02601  -0.01905 89  HIS   A NE2 
555  N  N   . ILE   A 91  ? 0.25990 0.25008 0.27136 0.00225  0.01868  -0.01243 90  ILE   A N   
556  C  CA  . ILE   A 91  ? 0.24958 0.24146 0.25706 -0.00013 0.01921  -0.01651 90  ILE   A CA  
557  C  C   . ILE   A 91  ? 0.27219 0.25533 0.27706 -0.00026 0.02114  -0.02171 90  ILE   A C   
558  O  O   . ILE   A 91  ? 0.30245 0.28586 0.30431 0.00055  0.02321  -0.02614 90  ILE   A O   
559  C  CB  . ILE   A 91  ? 0.23604 0.23151 0.24276 -0.00386 0.01652  -0.01508 90  ILE   A CB  
560  C  CG1 . ILE   A 91  ? 0.28422 0.28657 0.29269 -0.00352 0.01500  -0.01019 90  ILE   A CG1 
561  C  CG2 . ILE   A 91  ? 0.27137 0.26978 0.27391 -0.00653 0.01660  -0.01943 90  ILE   A CG2 
562  C  CD1 . ILE   A 91  ? 0.26097 0.26651 0.26891 -0.00582 0.01239  -0.00810 90  ILE   A CD1 
563  N  N   . TYR   A 92  ? 0.26515 0.24008 0.27066 -0.00157 0.02068  -0.02141 91  TYR   A N   
564  C  CA  . TYR   A 92  ? 0.26994 0.23443 0.27288 -0.00216 0.02271  -0.02595 91  TYR   A CA  
565  C  C   . TYR   A 92  ? 0.32606 0.28157 0.33059 -0.00236 0.02253  -0.02320 91  TYR   A C   
566  O  O   . TYR   A 92  ? 0.31641 0.27492 0.32309 -0.00372 0.02054  -0.01918 91  TYR   A O   
567  C  CB  . TYR   A 92  ? 0.28218 0.24748 0.28145 -0.00741 0.02227  -0.03094 91  TYR   A CB  
568  C  CG  . TYR   A 92  ? 0.34510 0.30113 0.34053 -0.00739 0.02499  -0.03730 91  TYR   A CG  
569  C  CD1 . TYR   A 92  ? 0.36531 0.32362 0.35840 -0.00393 0.02712  -0.04074 91  TYR   A CD1 
570  C  CD2 . TYR   A 92  ? 0.44556 0.39000 0.43960 -0.01075 0.02575  -0.03984 91  TYR   A CD2 
571  C  CE1 . TYR   A 92  ? 0.45459 0.40339 0.44367 -0.00327 0.02992  -0.04729 91  TYR   A CE1 
572  C  CE2 . TYR   A 92  ? 0.44748 0.38115 0.43749 -0.01078 0.02841  -0.04613 91  TYR   A CE2 
573  C  CZ  . TYR   A 92  ? 0.42216 0.35781 0.40961 -0.00670 0.03047  -0.05008 91  TYR   A CZ  
574  O  OH  . TYR   A 92  ? 0.50239 0.42655 0.48540 -0.00607 0.03340  -0.05701 91  TYR   A OH  
575  N  N   . GLU   A 93  ? 0.30402 0.24791 0.30694 -0.00094 0.02481  -0.02545 92  GLU   A N   
576  C  CA  . GLU   A 93  ? 0.33388 0.26819 0.33724 -0.00183 0.02493  -0.02265 92  GLU   A CA  
577  C  C   . GLU   A 93  ? 0.41831 0.33889 0.41817 -0.00373 0.02732  -0.02712 92  GLU   A C   
578  O  O   . GLU   A 93  ? 0.41043 0.32606 0.40821 -0.00067 0.02951  -0.03129 92  GLU   A O   
579  C  CB  . GLU   A 93  ? 0.39966 0.33295 0.40572 0.00404  0.02493  -0.01734 92  GLU   A CB  
580  C  CG  . GLU   A 93  ? 0.45925 0.38344 0.46507 0.00356  0.02498  -0.01346 92  GLU   A CG  
581  C  CD  . GLU   A 93  ? 0.64750 0.56049 0.65259 0.00914  0.02716  -0.01247 92  GLU   A CD  
582  O  OE1 . GLU   A 93  ? 0.75599 0.66860 0.76111 0.01359  0.02882  -0.01549 92  GLU   A OE1 
583  O  OE2 . GLU   A 93  ? 0.68521 0.59011 0.68957 0.00948  0.02733  -0.00843 92  GLU   A OE2 
584  N  N   . THR   A 94  ? 0.41318 0.32776 0.41229 -0.00904 0.02707  -0.02648 93  THR   A N   
585  C  CA  . THR   A 94  ? 0.42925 0.32828 0.42523 -0.01177 0.02934  -0.02935 93  THR   A CA  
586  C  C   . THR   A 94  ? 0.49456 0.38555 0.49133 -0.01139 0.02966  -0.02314 93  THR   A C   
587  O  O   . THR   A 94  ? 0.47603 0.37386 0.47542 -0.00837 0.02816  -0.01743 93  THR   A O   
588  C  CB  . THR   A 94  ? 0.47840 0.37830 0.47235 -0.02027 0.02892  -0.03473 93  THR   A CB  
589  O  OG1 . THR   A 94  ? 0.46285 0.36977 0.45927 -0.02533 0.02707  -0.03116 93  THR   A OG1 
590  C  CG2 . THR   A 94  ? 0.47521 0.38597 0.46800 -0.02077 0.02796  -0.03988 93  THR   A CG2 
591  N  N   . ASP   A 95  ? 0.53314 0.40904 0.52711 -0.01468 0.03170  -0.02423 94  ASP   A N   
592  C  CA  . ASP   A 95  ? 0.48978 0.35907 0.48384 -0.01586 0.03203  -0.01789 94  ASP   A CA  
593  C  C   . ASP   A 95  ? 0.47377 0.35409 0.46980 -0.02245 0.03025  -0.01586 94  ASP   A C   
594  O  O   . ASP   A 95  ? 0.50206 0.38272 0.49868 -0.02242 0.03002  -0.00988 94  ASP   A O   
595  C  CB  . ASP   A 95  ? 0.59641 0.44562 0.58667 -0.01851 0.03489  -0.01911 94  ASP   A CB  
596  C  CG  . ASP   A 95  ? 0.53070 0.36704 0.51928 -0.00986 0.03693  -0.01872 94  ASP   A CG  
597  O  OD1 . ASP   A 95  ? 0.54492 0.38949 0.53589 -0.00194 0.03605  -0.01674 94  ASP   A OD1 
598  O  OD2 . ASP   A 95  ? 0.58226 0.40015 0.56729 -0.01102 0.03950  -0.02041 94  ASP   A OD2 
599  N  N   . GLY   A 96  ? 0.46036 0.35059 0.45729 -0.02757 0.02899  -0.02064 95  GLY   A N   
600  C  CA  . GLY   A 96  ? 0.39054 0.29193 0.38985 -0.03331 0.02750  -0.01918 95  GLY   A CA  
601  C  C   . GLY   A 96  ? 0.36606 0.28279 0.36851 -0.02959 0.02502  -0.01624 95  GLY   A C   
602  O  O   . GLY   A 96  ? 0.36651 0.29019 0.37083 -0.03155 0.02427  -0.01288 95  GLY   A O   
603  N  N   . PHE   A 97  ? 0.34521 0.26722 0.34812 -0.02446 0.02394  -0.01760 96  PHE   A N   
604  C  CA  . PHE   A 97  ? 0.31018 0.24541 0.31578 -0.02175 0.02159  -0.01509 96  PHE   A CA  
605  C  C   . PHE   A 97  ? 0.34093 0.27817 0.34677 -0.01546 0.02118  -0.01488 96  PHE   A C   
606  O  O   . PHE   A 97  ? 0.35217 0.28371 0.35633 -0.01336 0.02261  -0.01792 96  PHE   A O   
607  C  CB  . PHE   A 97  ? 0.30384 0.25060 0.31082 -0.02600 0.01989  -0.01789 96  PHE   A CB  
608  C  CG  . PHE   A 97  ? 0.31361 0.26324 0.31908 -0.02608 0.01952  -0.02283 96  PHE   A CG  
609  C  CD1 . PHE   A 97  ? 0.40534 0.34834 0.40813 -0.03026 0.02085  -0.02809 96  PHE   A CD1 
610  C  CD2 . PHE   A 97  ? 0.31881 0.27704 0.32492 -0.02223 0.01804  -0.02229 96  PHE   A CD2 
611  C  CE1 . PHE   A 97  ? 0.40861 0.35453 0.40907 -0.03037 0.02063  -0.03311 96  PHE   A CE1 
612  C  CE2 . PHE   A 97  ? 0.35878 0.32016 0.36271 -0.02234 0.01798  -0.02654 96  PHE   A CE2 
613  C  CZ  . PHE   A 97  ? 0.44733 0.40296 0.44824 -0.02621 0.01926  -0.03216 96  PHE   A CZ  
614  N  N   . SER   A 98  ? 0.29779 0.24338 0.30578 -0.01260 0.01936  -0.01144 97  SER   A N   
615  C  CA  A SER   A 98  ? 0.29440 0.24493 0.30342 -0.00795 0.01866  -0.01093 97  SER   A CA  
616  C  CA  B SER   A 98  ? 0.29488 0.24539 0.30388 -0.00797 0.01867  -0.01096 97  SER   A CA  
617  C  C   . SER   A 98  ? 0.29864 0.26024 0.30894 -0.00914 0.01658  -0.01104 97  SER   A C   
618  O  O   . SER   A 98  ? 0.30836 0.27402 0.31959 -0.01145 0.01535  -0.00979 97  SER   A O   
619  C  CB  A SER   A 98  ? 0.34125 0.29079 0.35158 -0.00350 0.01825  -0.00630 97  SER   A CB  
620  C  CB  B SER   A 98  ? 0.34115 0.29054 0.35144 -0.00352 0.01829  -0.00637 97  SER   A CB  
621  O  OG  A SER   A 98  ? 0.32216 0.27723 0.33360 -0.00450 0.01639  -0.00329 97  SER   A OG  
622  O  OG  B SER   A 98  ? 0.35105 0.30649 0.36299 0.00009  0.01767  -0.00597 97  SER   A OG  
623  N  N   . LEU   A 99  ? 0.28567 0.25212 0.29593 -0.00721 0.01640  -0.01226 98  LEU   A N   
624  C  CA  . LEU   A 99  ? 0.26858 0.24441 0.27933 -0.00818 0.01460  -0.01200 98  LEU   A CA  
625  C  C   . LEU   A 99  ? 0.27520 0.25540 0.28711 -0.00486 0.01428  -0.00979 98  LEU   A C   
626  O  O   . LEU   A 99  ? 0.25803 0.23774 0.26938 -0.00272 0.01589  -0.01131 98  LEU   A O   
627  C  CB  . LEU   A 99  ? 0.26148 0.24000 0.26983 -0.01107 0.01486  -0.01643 98  LEU   A CB  
628  C  CG  . LEU   A 99  ? 0.26182 0.25017 0.26963 -0.01177 0.01312  -0.01624 98  LEU   A CG  
629  C  CD1 . LEU   A 99  ? 0.31420 0.30710 0.32399 -0.01308 0.01099  -0.01371 98  LEU   A CD1 
630  C  CD2 . LEU   A 99  ? 0.29471 0.28522 0.29920 -0.01453 0.01358  -0.02130 98  LEU   A CD2 
631  N  N   . GLY   A 100 ? 0.23104 0.21557 0.24460 -0.00457 0.01243  -0.00645 99  GLY   A N   
632  C  CA  . GLY   A 100 ? 0.23475 0.22367 0.24960 -0.00266 0.01211  -0.00426 99  GLY   A CA  
633  C  C   . GLY   A 100 ? 0.24062 0.23274 0.25645 -0.00345 0.00995  -0.00123 99  GLY   A C   
634  O  O   . GLY   A 100 ? 0.24825 0.23985 0.26376 -0.00466 0.00881  -0.00108 99  GLY   A O   
635  N  N   . VAL   A 101 ? 0.21069 0.20608 0.22787 -0.00277 0.00954  0.00110  100 VAL   A N   
636  C  CA  . VAL   A 101 ? 0.20800 0.20468 0.22571 -0.00378 0.00765  0.00388  100 VAL   A CA  
637  C  C   . VAL   A 101 ? 0.21894 0.21496 0.23879 -0.00342 0.00688  0.00573  100 VAL   A C   
638  O  O   . VAL   A 101 ? 0.21227 0.21129 0.23390 -0.00251 0.00776  0.00614  100 VAL   A O   
639  C  CB  . VAL   A 101 ? 0.21839 0.21990 0.23518 -0.00468 0.00766  0.00536  100 VAL   A CB  
640  C  CG1 . VAL   A 101 ? 0.22835 0.22870 0.24550 -0.00577 0.00580  0.00863  100 VAL   A CG1 
641  C  CG2 . VAL   A 101 ? 0.25401 0.25759 0.26822 -0.00511 0.00792  0.00347  100 VAL   A CG2 
642  N  N   . PHE   A 102 ? 0.20500 0.19801 0.22468 -0.00403 0.00523  0.00660  101 PHE   A N   
643  C  CA  . PHE   A 102 ? 0.20343 0.19647 0.22452 -0.00459 0.00394  0.00805  101 PHE   A CA  
644  C  C   . PHE   A 102 ? 0.22084 0.21379 0.24185 -0.00670 0.00270  0.00981  101 PHE   A C   
645  O  O   . PHE   A 102 ? 0.22459 0.21465 0.24390 -0.00681 0.00218  0.01000  101 PHE   A O   
646  C  CB  . PHE   A 102 ? 0.18442 0.17371 0.20444 -0.00401 0.00307  0.00736  101 PHE   A CB  
647  C  CG  . PHE   A 102 ? 0.20360 0.19221 0.22367 -0.00223 0.00422  0.00681  101 PHE   A CG  
648  C  CD1 . PHE   A 102 ? 0.25847 0.24949 0.28021 -0.00097 0.00396  0.00797  101 PHE   A CD1 
649  C  CD2 . PHE   A 102 ? 0.21986 0.20560 0.23849 -0.00185 0.00555  0.00539  101 PHE   A CD2 
650  C  CE1 . PHE   A 102 ? 0.26024 0.24938 0.28178 0.00140  0.00509  0.00809  101 PHE   A CE1 
651  C  CE2 . PHE   A 102 ? 0.27872 0.26186 0.29701 -0.00047 0.00685  0.00521  101 PHE   A CE2 
652  C  CZ  . PHE   A 102 ? 0.26635 0.25051 0.28588 0.00153  0.00665  0.00677  101 PHE   A CZ  
653  N  N   . LEU   A 103 ? 0.23240 0.22863 0.25547 -0.00838 0.00227  0.01135  102 LEU   A N   
654  C  CA  . LEU   A 103 ? 0.22515 0.22052 0.24819 -0.01133 0.00134  0.01344  102 LEU   A CA  
655  C  C   . LEU   A 103 ? 0.25020 0.24404 0.27415 -0.01365 -0.00058 0.01340  102 LEU   A C   
656  O  O   . LEU   A 103 ? 0.24040 0.23989 0.26707 -0.01425 -0.00085 0.01355  102 LEU   A O   
657  C  CB  . LEU   A 103 ? 0.23114 0.23304 0.25577 -0.01264 0.00277  0.01546  102 LEU   A CB  
658  C  CG  . LEU   A 103 ? 0.22070 0.22456 0.24348 -0.01050 0.00455  0.01476  102 LEU   A CG  
659  C  CD1 . LEU   A 103 ? 0.22847 0.23713 0.25278 -0.00808 0.00641  0.01272  102 LEU   A CD1 
660  C  CD2 . LEU   A 103 ? 0.29418 0.30080 0.31567 -0.01242 0.00523  0.01769  102 LEU   A CD2 
661  N  N   . LEU   A 104 ? 0.26915 0.25569 0.29073 -0.01469 -0.00194 0.01293  103 LEU   A N   
662  C  CA  . LEU   A 104 ? 0.26265 0.24619 0.28375 -0.01705 -0.00391 0.01170  103 LEU   A CA  
663  C  C   . LEU   A 104 ? 0.24367 0.22472 0.26524 -0.02167 -0.00475 0.01347  103 LEU   A C   
664  O  O   . LEU   A 104 ? 0.27948 0.25499 0.29938 -0.02191 -0.00429 0.01515  103 LEU   A O   
665  C  CB  . LEU   A 104 ? 0.24037 0.21649 0.25794 -0.01501 -0.00451 0.00922  103 LEU   A CB  
666  C  CG  . LEU   A 104 ? 0.28824 0.26644 0.30496 -0.01195 -0.00406 0.00737  103 LEU   A CG  
667  C  CD1 . LEU   A 104 ? 0.32515 0.30609 0.34274 -0.00928 -0.00210 0.00809  103 LEU   A CD1 
668  C  CD2 . LEU   A 104 ? 0.30890 0.28100 0.32213 -0.01062 -0.00451 0.00487  103 LEU   A CD2 
669  N  N   . LYS   A 105 ? 0.24837 0.23371 0.27222 -0.02551 -0.00607 0.01341  104 LYS   A N   
670  C  CA  . LYS   A 105 ? 0.31947 0.30166 0.34372 -0.03113 -0.00690 0.01493  104 LYS   A CA  
671  C  C   . LYS   A 105 ? 0.35384 0.32392 0.37399 -0.03253 -0.00855 0.01239  104 LYS   A C   
672  O  O   . LYS   A 105 ? 0.31745 0.28383 0.33483 -0.02915 -0.00902 0.00929  104 LYS   A O   
673  C  CB  . LYS   A 105 ? 0.31541 0.30820 0.34426 -0.03544 -0.00777 0.01568  104 LYS   A CB  
674  C  CG  . LYS   A 105 ? 0.32742 0.33220 0.36045 -0.03342 -0.00565 0.01803  104 LYS   A CG  
675  C  CD  . LYS   A 105 ? 0.31633 0.33370 0.35484 -0.03669 -0.00647 0.01875  104 LYS   A CD  
676  C  CE  . LYS   A 105 ? 0.32203 0.35105 0.36468 -0.03431 -0.00383 0.02095  104 LYS   A CE  
677  N  NZ  . LYS   A 105 ? 0.35302 0.38451 0.39556 -0.02716 -0.00272 0.01948  104 LYS   A NZ  
678  N  N   . SER   A 106 ? 0.35384 0.31706 0.37329 -0.03754 -0.00910 0.01374  105 SER   A N   
679  C  CA  . SER   A 106 ? 0.35269 0.30244 0.36784 -0.03883 -0.01044 0.01088  105 SER   A CA  
680  C  C   . SER   A 106 ? 0.32902 0.28033 0.34293 -0.03992 -0.01250 0.00604  105 SER   A C   
681  O  O   . SER   A 106 ? 0.36815 0.32955 0.38516 -0.04342 -0.01381 0.00576  105 SER   A O   
682  C  CB  . SER   A 106 ? 0.39978 0.34163 0.41460 -0.04546 -0.01086 0.01308  105 SER   A CB  
683  O  OG  . SER   A 106 ? 0.50399 0.44412 0.51903 -0.04449 -0.00902 0.01816  105 SER   A OG  
684  N  N   . GLY   A 107 ? 0.38730 0.32955 0.39656 -0.03664 -0.01277 0.00227  106 GLY   A N   
685  C  CA  . GLY   A 107 ? 0.39113 0.33361 0.39765 -0.03782 -0.01467 -0.00265 106 GLY   A CA  
686  C  C   . GLY   A 107 ? 0.39623 0.35077 0.40398 -0.03464 -0.01488 -0.00314 106 GLY   A C   
687  O  O   . GLY   A 107 ? 0.44478 0.40206 0.45030 -0.03603 -0.01676 -0.00647 106 GLY   A O   
688  N  N   . THR   A 108 ? 0.33021 0.29160 0.34094 -0.03049 -0.01306 0.00008  107 THR   A N   
689  C  CA  . THR   A 108 ? 0.30252 0.27384 0.31440 -0.02755 -0.01311 0.00022  107 THR   A CA  
690  C  C   . THR   A 108 ? 0.32627 0.29432 0.33489 -0.02200 -0.01155 -0.00117 107 THR   A C   
691  O  O   . THR   A 108 ? 0.32713 0.28778 0.33402 -0.01962 -0.01015 -0.00162 107 THR   A O   
692  C  CB  . THR   A 108 ? 0.32149 0.30259 0.33871 -0.02668 -0.01195 0.00412  107 THR   A CB  
693  O  OG1 . THR   A 108 ? 0.31649 0.29441 0.33409 -0.02365 -0.00953 0.00606  107 THR   A OG1 
694  C  CG2 . THR   A 108 ? 0.35930 0.34582 0.38052 -0.03236 -0.01308 0.00583  107 THR   A CG2 
695  N  N   . SER   A 109 ? 0.37010 0.34456 0.37815 -0.01994 -0.01179 -0.00142 108 SER   A N   
696  C  CA  A SER   A 109 ? 0.32414 0.29742 0.32946 -0.01549 -0.01013 -0.00222 108 SER   A CA  
697  C  CA  B SER   A 109 ? 0.32421 0.29748 0.32955 -0.01547 -0.01011 -0.00220 108 SER   A CA  
698  C  C   . SER   A 109 ? 0.35487 0.33591 0.36244 -0.01325 -0.00945 0.00050  108 SER   A C   
699  O  O   . SER   A 109 ? 0.32149 0.30924 0.33115 -0.01451 -0.01097 0.00187  108 SER   A O   
700  C  CB  A SER   A 109 ? 0.36323 0.33347 0.36298 -0.01564 -0.01113 -0.00614 108 SER   A CB  
701  C  CB  B SER   A 109 ? 0.36309 0.33344 0.36286 -0.01542 -0.01101 -0.00605 108 SER   A CB  
702  O  OG  A SER   A 109 ? 0.43516 0.40853 0.43255 -0.01231 -0.00988 -0.00603 108 SER   A OG  
703  O  OG  B SER   A 109 ? 0.37228 0.33350 0.36939 -0.01672 -0.01131 -0.00920 108 SER   A OG  
704  N  N   . ILE   A 110 ? 0.26818 0.24830 0.27553 -0.00990 -0.00717 0.00130  109 ILE   A N   
705  C  CA  . ILE   A 110 ? 0.24328 0.22772 0.25090 -0.00760 -0.00630 0.00325  109 ILE   A CA  
706  C  C   . ILE   A 110 ? 0.25711 0.24091 0.25975 -0.00671 -0.00639 0.00181  109 ILE   A C   
707  O  O   . ILE   A 110 ? 0.26913 0.24918 0.26944 -0.00571 -0.00492 -0.00004 109 ILE   A O   
708  C  CB  . ILE   A 110 ? 0.24911 0.23259 0.25875 -0.00549 -0.00375 0.00461  109 ILE   A CB  
709  C  CG1 . ILE   A 110 ? 0.24576 0.23072 0.25943 -0.00626 -0.00347 0.00582  109 ILE   A CG1 
710  C  CG2 . ILE   A 110 ? 0.27422 0.25984 0.28354 -0.00343 -0.00277 0.00659  109 ILE   A CG2 
711  C  CD1 . ILE   A 110 ? 0.26076 0.24455 0.27547 -0.00470 -0.00119 0.00617  109 ILE   A CD1 
712  N  N   . PRO   A 111 ? 0.26895 0.25728 0.26981 -0.00688 -0.00806 0.00268  110 PRO   A N   
713  C  CA  . PRO   A 111 ? 0.32716 0.31578 0.32226 -0.00633 -0.00820 0.00139  110 PRO   A CA  
714  C  C   . PRO   A 111 ? 0.31817 0.30535 0.31166 -0.00393 -0.00524 0.00280  110 PRO   A C   
715  O  O   . PRO   A 111 ? 0.27836 0.26506 0.27487 -0.00267 -0.00357 0.00540  110 PRO   A O   
716  C  CB  . PRO   A 111 ? 0.30450 0.29999 0.29880 -0.00664 -0.01083 0.00342  110 PRO   A CB  
717  C  CG  . PRO   A 111 ? 0.34363 0.34233 0.34335 -0.00855 -0.01264 0.00400  110 PRO   A CG  
718  C  CD  . PRO   A 111 ? 0.29449 0.28920 0.29853 -0.00756 -0.01009 0.00489  110 PRO   A CD  
719  N  N   . LEU   A 112 ? 0.29869 0.28552 0.28698 -0.00365 -0.00452 0.00082  111 LEU   A N   
720  C  CA  . LEU   A 112 ? 0.28644 0.27321 0.27273 -0.00221 -0.00155 0.00201  111 LEU   A CA  
721  C  C   . LEU   A 112 ? 0.26526 0.25346 0.25228 -0.00133 -0.00079 0.00690  111 LEU   A C   
722  O  O   . LEU   A 112 ? 0.27469 0.26600 0.25973 -0.00091 -0.00264 0.00932  111 LEU   A O   
723  C  CB  . LEU   A 112 ? 0.28346 0.27201 0.26307 -0.00216 -0.00138 -0.00051 111 LEU   A CB  
724  C  CG  . LEU   A 112 ? 0.29849 0.28845 0.27551 -0.00115 0.00203  0.00023  111 LEU   A CG  
725  C  CD1 . LEU   A 112 ? 0.32917 0.31701 0.31039 -0.00043 0.00441  -0.00135 111 LEU   A CD1 
726  C  CD2 . LEU   A 112 ? 0.31722 0.31000 0.28682 -0.00097 0.00205  -0.00280 111 LEU   A CD2 
727  N  N   . HIS   A 113 ? 0.26096 0.24674 0.25065 -0.00101 0.00186  0.00837  112 HIS   A N   
728  C  CA  . HIS   A 113 ? 0.28849 0.27297 0.27885 -0.00027 0.00293  0.01269  112 HIS   A CA  
729  C  C   . HIS   A 113 ? 0.28856 0.27073 0.27916 -0.00125 0.00629  0.01328  112 HIS   A C   
730  O  O   . HIS   A 113 ? 0.28766 0.27036 0.27991 -0.00209 0.00750  0.01038  112 HIS   A O   
731  C  CB  . HIS   A 113 ? 0.24150 0.22470 0.23684 0.00062  0.00195  0.01372  112 HIS   A CB  
732  C  CG  . HIS   A 113 ? 0.24358 0.22491 0.24313 -0.00024 0.00284  0.01112  112 HIS   A CG  
733  N  ND1 . HIS   A 113 ? 0.23248 0.21491 0.23363 -0.00100 0.00133  0.00838  112 HIS   A ND1 
734  C  CD2 . HIS   A 113 ? 0.26632 0.24484 0.26831 -0.00067 0.00495  0.01102  112 HIS   A CD2 
735  C  CE1 . HIS   A 113 ? 0.24308 0.22396 0.24737 -0.00137 0.00243  0.00726  112 HIS   A CE1 
736  N  NE2 . HIS   A 113 ? 0.23535 0.21446 0.24020 -0.00127 0.00451  0.00849  112 HIS   A NE2 
737  N  N   . ASP   A 114 ? 0.28061 0.26025 0.26983 -0.00119 0.00773  0.01729  113 ASP   A N   
738  C  CA  . ASP   A 114 ? 0.28625 0.26344 0.27570 -0.00324 0.01096  0.01826  113 ASP   A CA  
739  C  C   . ASP   A 114 ? 0.27421 0.24567 0.26750 -0.00358 0.01185  0.01898  113 ASP   A C   
740  O  O   . ASP   A 114 ? 0.31369 0.28359 0.30941 -0.00160 0.01025  0.01886  113 ASP   A O   
741  C  CB  . ASP   A 114 ? 0.28753 0.26493 0.27160 -0.00391 0.01256  0.02227  113 ASP   A CB  
742  C  CG  . ASP   A 114 ? 0.39304 0.36642 0.37493 -0.00190 0.01165  0.02746  113 ASP   A CG  
743  O  OD1 . ASP   A 114 ? 0.35751 0.32814 0.34258 0.00025  0.01008  0.02778  113 ASP   A OD1 
744  O  OD2 . ASP   A 114 ? 0.46374 0.43729 0.44046 -0.00212 0.01263  0.03161  113 ASP   A OD2 
745  N  N   . HIS   A 115 ? 0.27733 0.24638 0.27127 -0.00643 0.01456  0.01916  114 HIS   A N   
746  C  CA  . HIS   A 115 ? 0.27042 0.23352 0.26730 -0.00771 0.01575  0.01870  114 HIS   A CA  
747  C  C   . HIS   A 115 ? 0.29219 0.25033 0.28697 -0.01095 0.01864  0.02159  114 HIS   A C   
748  O  O   . HIS   A 115 ? 0.31258 0.27214 0.30900 -0.01494 0.02052  0.01988  114 HIS   A O   
749  C  CB  . HIS   A 115 ? 0.25627 0.22281 0.25727 -0.00921 0.01562  0.01419  114 HIS   A CB  
750  C  CG  . HIS   A 115 ? 0.25109 0.22256 0.25357 -0.00686 0.01318  0.01178  114 HIS   A CG  
751  N  ND1 . HIS   A 115 ? 0.23918 0.21585 0.24037 -0.00627 0.01251  0.01065  114 HIS   A ND1 
752  C  CD2 . HIS   A 115 ? 0.26269 0.23410 0.26762 -0.00523 0.01151  0.01028  114 HIS   A CD2 
753  C  CE1 . HIS   A 115 ? 0.27293 0.25116 0.27564 -0.00461 0.01037  0.00867  114 HIS   A CE1 
754  N  NE2 . HIS   A 115 ? 0.22995 0.20564 0.23506 -0.00419 0.00976  0.00871  114 HIS   A NE2 
755  N  N   . PRO   A 116 ? 0.30667 0.25924 0.29786 -0.00950 0.01901  0.02638  115 PRO   A N   
756  C  CA  . PRO   A 116 ? 0.35372 0.30211 0.34162 -0.01292 0.02186  0.03031  115 PRO   A CA  
757  C  C   . PRO   A 116 ? 0.33641 0.27767 0.32656 -0.01738 0.02425  0.02899  115 PRO   A C   
758  O  O   . PRO   A 116 ? 0.38266 0.31537 0.37401 -0.01618 0.02417  0.02831  115 PRO   A O   
759  C  CB  . PRO   A 116 ? 0.37745 0.32008 0.36120 -0.00919 0.02114  0.03611  115 PRO   A CB  
760  C  CG  . PRO   A 116 ? 0.37293 0.32220 0.35723 -0.00447 0.01764  0.03490  115 PRO   A CG  
761  C  CD  . PRO   A 116 ? 0.30420 0.25592 0.29397 -0.00459 0.01664  0.02898  115 PRO   A CD  
762  N  N   . GLY   A 117 ? 0.35047 0.29576 0.34110 -0.02270 0.02649  0.02839  116 GLY   A N   
763  C  CA  . GLY   A 117 ? 0.42707 0.36661 0.41970 -0.02826 0.02866  0.02696  116 GLY   A CA  
764  C  C   . GLY   A 117 ? 0.40446 0.34554 0.40170 -0.02862 0.02735  0.02098  116 GLY   A C   
765  O  O   . GLY   A 117 ? 0.39200 0.32630 0.39033 -0.03253 0.02856  0.01904  116 GLY   A O   
766  N  N   . MET   A 118 ? 0.36310 0.31264 0.36259 -0.02491 0.02491  0.01798  117 MET   A N   
767  C  CA  . MET   A 118 ? 0.33079 0.28212 0.33390 -0.02458 0.02347  0.01307  117 MET   A CA  
768  C  C   . MET   A 118 ? 0.31355 0.27715 0.32006 -0.02580 0.02271  0.00988  117 MET   A C   
769  O  O   . MET   A 118 ? 0.32097 0.29197 0.32715 -0.02462 0.02269  0.01085  117 MET   A O   
770  C  CB  . MET   A 118 ? 0.32589 0.27518 0.32900 -0.01873 0.02118  0.01263  117 MET   A CB  
771  C  CG  . MET   A 118 ? 0.34639 0.28493 0.34694 -0.01586 0.02165  0.01578  117 MET   A CG  
772  S  SD  . MET   A 118 ? 0.35471 0.29629 0.35488 -0.00890 0.01891  0.01784  117 MET   A SD  
773  C  CE  . MET   A 118 ? 0.33449 0.28087 0.33871 -0.00746 0.01727  0.01271  117 MET   A CE  
774  N  N   . HIS   A 119 ? 0.31756 0.28319 0.32703 -0.02777 0.02209  0.00597  118 HIS   A N   
775  C  CA  . HIS   A 119 ? 0.29909 0.27575 0.31202 -0.02725 0.02058  0.00300  118 HIS   A CA  
776  C  C   . HIS   A 119 ? 0.29542 0.27179 0.30855 -0.02239 0.01815  0.00174  118 HIS   A C   
777  O  O   . HIS   A 119 ? 0.31410 0.28304 0.32583 -0.02079 0.01787  0.00177  118 HIS   A O   
778  C  CB  . HIS   A 119 ? 0.31567 0.29613 0.33140 -0.03259 0.02099  -0.00019 118 HIS   A CB  
779  C  CG  . HIS   A 119 ? 0.40071 0.38362 0.41725 -0.03852 0.02341  0.00086  118 HIS   A CG  
780  N  ND1 . HIS   A 119 ? 0.44069 0.43682 0.46102 -0.04065 0.02369  0.00002  118 HIS   A ND1 
781  C  CD2 . HIS   A 119 ? 0.41428 0.38834 0.42851 -0.04291 0.02581  0.00298  118 HIS   A CD2 
782  C  CE1 . HIS   A 119 ? 0.45662 0.45317 0.47723 -0.04660 0.02628  0.00148  118 HIS   A CE1 
783  N  NE2 . HIS   A 119 ? 0.49649 0.47895 0.51313 -0.04836 0.02760  0.00344  118 HIS   A NE2 
784  N  N   . GLY   A 120 ? 0.27508 0.25957 0.29009 -0.01997 0.01659  0.00076  119 GLY   A N   
785  C  CA  . GLY   A 120 ? 0.24755 0.23203 0.26284 -0.01628 0.01443  -0.00008 119 GLY   A CA  
786  C  C   . GLY   A 120 ? 0.29736 0.29051 0.31534 -0.01564 0.01309  -0.00177 119 GLY   A C   
787  O  O   . GLY   A 120 ? 0.29271 0.29266 0.31242 -0.01612 0.01358  -0.00188 119 GLY   A O   
788  N  N   . MET   A 121 ? 0.26576 0.25933 0.28413 -0.01427 0.01152  -0.00281 120 MET   A N   
789  C  CA  A MET   A 121 ? 0.26040 0.26151 0.28077 -0.01282 0.00990  -0.00348 120 MET   A CA  
790  C  CA  B MET   A 121 ? 0.26210 0.26317 0.28245 -0.01273 0.00990  -0.00343 120 MET   A CA  
791  C  C   . MET   A 121 ? 0.33495 0.33352 0.35427 -0.00957 0.00831  -0.00249 120 MET   A C   
792  O  O   . MET   A 121 ? 0.39488 0.38924 0.41291 -0.00981 0.00839  -0.00266 120 MET   A O   
793  C  CB  A MET   A 121 ? 0.32512 0.33162 0.34688 -0.01609 0.00961  -0.00574 120 MET   A CB  
794  C  CB  B MET   A 121 ? 0.32430 0.33106 0.34616 -0.01591 0.00959  -0.00562 120 MET   A CB  
795  C  CG  A MET   A 121 ? 0.28289 0.29972 0.30730 -0.01461 0.00798  -0.00579 120 MET   A CG  
796  C  CG  B MET   A 121 ? 0.27134 0.28020 0.29442 -0.02055 0.01125  -0.00677 120 MET   A CG  
797  S  SD  A MET   A 121 ? 0.35866 0.38463 0.38465 -0.01889 0.00698  -0.00857 120 MET   A SD  
798  S  SD  B MET   A 121 ? 0.36345 0.37626 0.38697 -0.02517 0.01054  -0.01028 120 MET   A SD  
799  C  CE  A MET   A 121 ? 0.35335 0.38097 0.38129 -0.02475 0.00924  -0.01003 120 MET   A CE  
800  C  CE  B MET   A 121 ? 0.35490 0.38314 0.38243 -0.02380 0.00841  -0.01019 120 MET   A CE  
801  N  N   . LEU   A 122 ? 0.22628 0.22724 0.24621 -0.00659 0.00710  -0.00146 121 LEU   A N   
802  C  CA  A LEU   A 122 ? 0.26456 0.26237 0.28346 -0.00422 0.00571  -0.00009 121 LEU   A CA  
803  C  CA  B LEU   A 122 ? 0.26441 0.26240 0.28332 -0.00443 0.00571  -0.00017 121 LEU   A CA  
804  C  C   . LEU   A 122 ? 0.27700 0.27951 0.29691 -0.00234 0.00422  0.00065  121 LEU   A C   
805  O  O   . LEU   A 122 ? 0.31262 0.32013 0.33424 -0.00098 0.00409  0.00043  121 LEU   A O   
806  C  CB  A LEU   A 122 ? 0.29391 0.28745 0.31162 -0.00248 0.00567  0.00064  121 LEU   A CB  
807  C  CB  B LEU   A 122 ? 0.30233 0.29505 0.31987 -0.00293 0.00557  0.00080  121 LEU   A CB  
808  C  CG  A LEU   A 122 ? 0.33391 0.32287 0.35039 -0.00119 0.00439  0.00179  121 LEU   A CG  
809  C  CG  B LEU   A 122 ? 0.26629 0.25919 0.28364 -0.00059 0.00532  0.00071  121 LEU   A CG  
810  C  CD1 A LEU   A 122 ? 0.23908 0.22465 0.25379 -0.00108 0.00466  0.00155  121 LEU   A CD1 
811  C  CD1 B LEU   A 122 ? 0.26656 0.25742 0.28370 0.00173  0.00375  0.00169  121 LEU   A CD1 
812  C  CD2 A LEU   A 122 ? 0.29249 0.28144 0.30922 0.00110  0.00314  0.00252  121 LEU   A CD2 
813  C  CD2 B LEU   A 122 ? 0.31998 0.30887 0.33518 -0.00083 0.00584  0.00063  121 LEU   A CD2 
814  N  N   . LYS   A 123 ? 0.22825 0.22972 0.24716 -0.00191 0.00319  0.00195  122 LYS   A N   
815  C  CA  A LYS   A 123 ? 0.21582 0.22071 0.23493 0.00025  0.00165  0.00376  122 LYS   A CA  
816  C  CA  B LYS   A 123 ? 0.21333 0.21820 0.23245 0.00027  0.00165  0.00376  122 LYS   A CA  
817  C  C   . LYS   A 123 ? 0.26753 0.26672 0.28503 0.00117  0.00093  0.00619  122 LYS   A C   
818  O  O   . LYS   A 123 ? 0.24603 0.24395 0.26251 -0.00066 0.00131  0.00650  122 LYS   A O   
819  C  CB  A LYS   A 123 ? 0.26018 0.27219 0.27920 -0.00130 0.00111  0.00317  122 LYS   A CB  
820  C  CB  B LYS   A 123 ? 0.25928 0.27134 0.27833 -0.00127 0.00111  0.00316  122 LYS   A CB  
821  C  CG  A LYS   A 123 ? 0.30459 0.32037 0.32295 0.00108  -0.00071 0.00604  122 LYS   A CG  
822  C  CG  B LYS   A 123 ? 0.30513 0.32098 0.32352 0.00110  -0.00072 0.00603  122 LYS   A CG  
823  C  CD  A LYS   A 123 ? 0.32609 0.34712 0.34687 0.00431  -0.00173 0.00682  122 LYS   A CD  
824  C  CD  B LYS   A 123 ? 0.32660 0.34686 0.34734 0.00455  -0.00170 0.00696  122 LYS   A CD  
825  C  CE  A LYS   A 123 ? 0.36301 0.38739 0.38289 0.00745  -0.00374 0.01051  122 LYS   A CE  
826  C  CE  B LYS   A 123 ? 0.37322 0.39395 0.39287 0.00815  -0.00352 0.01101  122 LYS   A CE  
827  N  NZ  A LYS   A 123 ? 0.34209 0.35690 0.35974 0.00918  -0.00391 0.01378  122 LYS   A NZ  
828  N  NZ  B LYS   A 123 ? 0.33633 0.36477 0.35435 0.00677  -0.00476 0.01195  122 LYS   A NZ  
829  N  N   . VAL   A 124 ? 0.24805 0.24376 0.26543 0.00391  0.00007  0.00780  123 VAL   A N   
830  C  CA  . VAL   A 124 ? 0.26431 0.25363 0.28012 0.00386  -0.00062 0.01021  123 VAL   A CA  
831  C  C   . VAL   A 124 ? 0.30835 0.30082 0.32309 0.00354  -0.00133 0.01313  123 VAL   A C   
832  O  O   . VAL   A 124 ? 0.30789 0.30564 0.32278 0.00552  -0.00218 0.01427  123 VAL   A O   
833  C  CB  . VAL   A 124 ? 0.28301 0.26597 0.29836 0.00682  -0.00122 0.01074  123 VAL   A CB  
834  C  CG1 . VAL   A 124 ? 0.28009 0.25523 0.29365 0.00574  -0.00198 0.01337  123 VAL   A CG1 
835  C  CG2 . VAL   A 124 ? 0.26260 0.24350 0.27811 0.00697  -0.00032 0.00754  123 VAL   A CG2 
836  N  N   . LEU   A 125 ? 0.23745 0.22798 0.25112 0.00108  -0.00099 0.01455  124 LEU   A N   
837  C  CA  . LEU   A 125 ? 0.27661 0.27066 0.28859 0.00030  -0.00122 0.01755  124 LEU   A CA  
838  C  C   . LEU   A 125 ? 0.33349 0.32157 0.34400 0.00065  -0.00203 0.02200  124 LEU   A C   
839  O  O   . LEU   A 125 ? 0.32492 0.31525 0.33362 0.00189  -0.00280 0.02555  124 LEU   A O   
840  C  CB  . LEU   A 125 ? 0.31289 0.31017 0.32469 -0.00261 0.00023  0.01640  124 LEU   A CB  
841  C  CG  . LEU   A 125 ? 0.29208 0.29349 0.30461 -0.00311 0.00127  0.01218  124 LEU   A CG  
842  C  CD1 . LEU   A 125 ? 0.29752 0.30055 0.30997 -0.00485 0.00295  0.01104  124 LEU   A CD1 
843  C  CD2 . LEU   A 125 ? 0.30092 0.30897 0.31226 -0.00253 0.00062  0.01156  124 LEU   A CD2 
844  N  N   . TYR   A 126 ? 0.29015 0.27060 0.30105 -0.00081 -0.00196 0.02203  125 TYR   A N   
845  C  CA  . TYR   A 126 ? 0.31195 0.28407 0.32136 -0.00094 -0.00272 0.02572  125 TYR   A CA  
846  C  C   . TYR   A 126 ? 0.34070 0.30436 0.35066 -0.00157 -0.00299 0.02317  125 TYR   A C   
847  O  O   . TYR   A 126 ? 0.28173 0.24735 0.29307 -0.00270 -0.00255 0.01949  125 TYR   A O   
848  C  CB  . TYR   A 126 ? 0.28577 0.25879 0.29406 -0.00476 -0.00215 0.02961  125 TYR   A CB  
849  C  CG  . TYR   A 126 ? 0.27209 0.24825 0.28231 -0.00882 -0.00105 0.02774  125 TYR   A CG  
850  C  CD1 . TYR   A 126 ? 0.30045 0.27053 0.31178 -0.01166 -0.00142 0.02697  125 TYR   A CD1 
851  C  CD2 . TYR   A 126 ? 0.26855 0.25418 0.27946 -0.00957 0.00030  0.02655  125 TYR   A CD2 
852  C  CE1 . TYR   A 126 ? 0.29724 0.27213 0.31096 -0.01489 -0.00073 0.02559  125 TYR   A CE1 
853  C  CE2 . TYR   A 126 ? 0.27171 0.26095 0.28487 -0.01214 0.00138  0.02511  125 TYR   A CE2 
854  C  CZ  . TYR   A 126 ? 0.27201 0.25663 0.28691 -0.01469 0.00074  0.02491  125 TYR   A CZ  
855  O  OH  . TYR   A 126 ? 0.28927 0.27928 0.30701 -0.01679 0.00152  0.02373  125 TYR   A OH  
856  N  N   . GLY   A 127 ? 0.33996 0.29365 0.34829 -0.00092 -0.00372 0.02523  126 GLY   A N   
857  C  CA  . GLY   A 127 ? 0.29675 0.24180 0.30471 -0.00176 -0.00406 0.02210  126 GLY   A CA  
858  C  C   . GLY   A 127 ? 0.30397 0.24846 0.31209 0.00303  -0.00399 0.01836  126 GLY   A C   
859  O  O   . GLY   A 127 ? 0.35514 0.30551 0.36417 0.00711  -0.00383 0.01867  126 GLY   A O   
860  N  N   . THR   A 128 ? 0.30712 0.24545 0.31431 0.00220  -0.00410 0.01465  127 THR   A N   
861  C  CA  . THR   A 128 ? 0.31413 0.25178 0.32091 0.00623  -0.00363 0.01058  127 THR   A CA  
862  C  C   . THR   A 128 ? 0.32737 0.26848 0.33415 0.00336  -0.00340 0.00672  127 THR   A C   
863  O  O   . THR   A 128 ? 0.32213 0.25993 0.32806 -0.00104 -0.00417 0.00606  127 THR   A O   
864  C  CB  . THR   A 128 ? 0.40237 0.32716 0.40646 0.00889  -0.00390 0.00946  127 THR   A CB  
865  O  OG1 . THR   A 128 ? 0.43604 0.35651 0.43986 0.01193  -0.00425 0.01404  127 THR   A OG1 
866  C  CG2 . THR   A 128 ? 0.39210 0.31756 0.39567 0.01381  -0.00291 0.00491  127 THR   A CG2 
867  N  N   . VAL   A 129 ? 0.30567 0.25375 0.31336 0.00566  -0.00242 0.00444  128 VAL   A N   
868  C  CA  . VAL   A 129 ? 0.28048 0.23108 0.28731 0.00375  -0.00214 0.00129  128 VAL   A CA  
869  C  C   . VAL   A 129 ? 0.32237 0.27196 0.32746 0.00745  -0.00114 -0.00220 128 VAL   A C   
870  O  O   . VAL   A 129 ? 0.36030 0.31268 0.36670 0.01165  -0.00016 -0.00201 128 VAL   A O   
871  C  CB  . VAL   A 129 ? 0.29261 0.25251 0.30161 0.00213  -0.00149 0.00209  128 VAL   A CB  
872  C  CG1 . VAL   A 129 ? 0.36757 0.32919 0.37807 -0.00141 -0.00215 0.00479  128 VAL   A CG1 
873  C  CG2 . VAL   A 129 ? 0.30474 0.27091 0.31564 0.00490  -0.00034 0.00260  128 VAL   A CG2 
874  N  N   . ARG   A 130 ? 0.31673 0.26373 0.31890 0.00589  -0.00136 -0.00542 129 ARG   A N   
875  C  CA  . ARG   A 130 ? 0.29836 0.24691 0.29831 0.00880  0.00004  -0.00899 129 ARG   A CA  
876  C  C   . ARG   A 130 ? 0.31631 0.27398 0.31697 0.00726  0.00091  -0.00856 129 ARG   A C   
877  O  O   . ARG   A 130 ? 0.32308 0.28198 0.32300 0.00372  -0.00014 -0.00802 129 ARG   A O   
878  C  CB  . ARG   A 130 ? 0.34625 0.28682 0.34143 0.00789  -0.00069 -0.01310 129 ARG   A CB  
879  C  CG  . ARG   A 130 ? 0.40598 0.34877 0.39799 0.01110  0.00110  -0.01718 129 ARG   A CG  
880  C  CD  . ARG   A 130 ? 0.45072 0.38588 0.43702 0.00969  0.00024  -0.02204 129 ARG   A CD  
881  N  NE  . ARG   A 130 ? 0.53056 0.45324 0.51583 0.00993  -0.00077 -0.02304 129 ARG   A NE  
882  C  CZ  . ARG   A 130 ? 0.57928 0.49547 0.56377 0.00468  -0.00305 -0.02264 129 ARG   A CZ  
883  N  NH1 . ARG   A 130 ? 0.48627 0.40846 0.47127 -0.00067 -0.00474 -0.02154 129 ARG   A NH1 
884  N  NH2 . ARG   A 130 ? 0.55951 0.46314 0.54299 0.00484  -0.00360 -0.02300 129 ARG   A NH2 
885  N  N   . ILE   A 131 ? 0.28274 0.24701 0.28506 0.00980  0.00280  -0.00845 130 ILE   A N   
886  C  CA  . ILE   A 131 ? 0.26741 0.23876 0.26997 0.00802  0.00393  -0.00775 130 ILE   A CA  
887  C  C   . ILE   A 131 ? 0.32111 0.29469 0.32052 0.00990  0.00570  -0.01061 130 ILE   A C   
888  O  O   . ILE   A 131 ? 0.30527 0.28102 0.30557 0.01355  0.00727  -0.01206 130 ILE   A O   
889  C  CB  . ILE   A 131 ? 0.28392 0.26175 0.29068 0.00792  0.00490  -0.00537 130 ILE   A CB  
890  C  CG1 . ILE   A 131 ? 0.30922 0.28521 0.31822 0.00635  0.00334  -0.00293 130 ILE   A CG1 
891  C  CG2 . ILE   A 131 ? 0.30794 0.29047 0.31439 0.00548  0.00617  -0.00451 130 ILE   A CG2 
892  C  CD1 . ILE   A 131 ? 0.28767 0.26977 0.30011 0.00619  0.00397  -0.00135 130 ILE   A CD1 
893  N  N   . SER   A 132 ? 0.29235 0.26642 0.28809 0.00773  0.00547  -0.01124 131 SER   A N   
894  C  CA  . SER   A 132 ? 0.31743 0.29509 0.30925 0.00886  0.00737  -0.01343 131 SER   A CA  
895  C  C   . SER   A 132 ? 0.34382 0.32853 0.33676 0.00709  0.00909  -0.01042 131 SER   A C   
896  O  O   . SER   A 132 ? 0.34292 0.32736 0.33614 0.00437  0.00800  -0.00763 131 SER   A O   
897  C  CB  . SER   A 132 ? 0.33138 0.30536 0.31741 0.00737  0.00576  -0.01590 131 SER   A CB  
898  O  OG  . SER   A 132 ? 0.37499 0.34074 0.35993 0.00806  0.00415  -0.01887 131 SER   A OG  
899  N  N   . CYS   A 133 ? 0.33921 0.33013 0.33295 0.00865  0.01191  -0.01089 132 CYS   A N   
900  C  CA  . CYS   A 133 ? 0.28808 0.28521 0.28360 0.00630  0.01391  -0.00790 132 CYS   A CA  
901  C  C   . CYS   A 133 ? 0.35839 0.36005 0.34912 0.00600  0.01622  -0.00820 132 CYS   A C   
902  O  O   . CYS   A 133 ? 0.34878 0.35336 0.33743 0.00887  0.01787  -0.01140 132 CYS   A O   
903  C  CB  . CYS   A 133 ? 0.29254 0.29540 0.29381 0.00727  0.01538  -0.00766 132 CYS   A CB  
904  S  SG  . CYS   A 133 ? 0.37070 0.36936 0.37667 0.00763  0.01265  -0.00679 132 CYS   A SG  
905  N  N   . MET   A 134 ? 0.30856 0.31083 0.29732 0.00286  0.01660  -0.00471 133 MET   A N   
906  C  CA  . MET   A 134 ? 0.32142 0.32745 0.30426 0.00231  0.01843  -0.00412 133 MET   A CA  
907  C  C   . MET   A 134 ? 0.33703 0.34525 0.32041 -0.00118 0.02032  0.00077  133 MET   A C   
908  O  O   . MET   A 134 ? 0.31015 0.31519 0.29768 -0.00313 0.01964  0.00311  133 MET   A O   
909  C  CB  . MET   A 134 ? 0.32584 0.32776 0.30277 0.00241  0.01570  -0.00475 133 MET   A CB  
910  C  CG  . MET   A 134 ? 0.43254 0.43057 0.40832 0.00475  0.01379  -0.00972 133 MET   A CG  
911  S  SD  . MET   A 134 ? 0.41735 0.41268 0.38612 0.00360  0.01047  -0.01089 133 MET   A SD  
912  C  CE  . MET   A 134 ? 0.47706 0.46441 0.44843 0.00441  0.00760  -0.01513 133 MET   A CE  
913  N  N   . ASP   A 135 ? 0.30371 0.31681 0.28230 -0.00211 0.02285  0.00226  134 ASP   A N   
914  C  CA  . ASP   A 135 ? 0.31915 0.33266 0.29689 -0.00578 0.02474  0.00763  134 ASP   A CA  
915  C  C   . ASP   A 135 ? 0.31170 0.32699 0.28118 -0.00596 0.02537  0.01002  134 ASP   A C   
916  O  O   . ASP   A 135 ? 0.37299 0.39267 0.33778 -0.00378 0.02584  0.00671  134 ASP   A O   
917  C  CB  . ASP   A 135 ? 0.36989 0.39031 0.35188 -0.00825 0.02851  0.00830  134 ASP   A CB  
918  C  CG  . ASP   A 135 ? 0.35109 0.36996 0.34080 -0.00943 0.02769  0.00748  134 ASP   A CG  
919  O  OD1 . ASP   A 135 ? 0.34886 0.36092 0.34002 -0.01187 0.02651  0.01013  134 ASP   A OD1 
920  O  OD2 . ASP   A 135 ? 0.34679 0.37162 0.34088 -0.00752 0.02825  0.00407  134 ASP   A OD2 
921  N  N   . LYS   A 136 ? 0.36077 0.37235 0.32811 -0.00833 0.02542  0.01576  135 LYS   A N   
922  C  CA  . LYS   A 136 ? 0.42024 0.43431 0.37946 -0.00882 0.02635  0.01956  135 LYS   A CA  
923  C  C   . LYS   A 136 ? 0.48983 0.51130 0.44787 -0.01148 0.03125  0.02126  135 LYS   A C   
924  O  O   . LYS   A 136 ? 0.44741 0.46940 0.41117 -0.01449 0.03360  0.02237  135 LYS   A O   
925  C  CB  . LYS   A 136 ? 0.47129 0.47800 0.42890 -0.00964 0.02457  0.02580  135 LYS   A CB  
926  C  CG  . LYS   A 136 ? 0.55370 0.55766 0.50963 -0.00659 0.01987  0.02464  135 LYS   A CG  
927  C  CD  . LYS   A 136 ? 0.65451 0.65140 0.61137 -0.00605 0.01777  0.03004  135 LYS   A CD  
928  C  CE  . LYS   A 136 ? 0.59284 0.58472 0.54993 -0.00865 0.02089  0.03604  135 LYS   A CE  
929  N  NZ  . LYS   A 136 ? 0.60562 0.58924 0.56383 -0.00696 0.01892  0.04067  135 LYS   A NZ  
930  N  N   . LEU   A 137 ? 0.43411 0.46246 0.38475 -0.01066 0.03288  0.02107  136 LEU   A N   
931  C  CA  . LEU   A 137 ? 0.57233 0.60950 0.52131 -0.01324 0.03798  0.02297  136 LEU   A CA  
932  C  C   . LEU   A 137 ? 0.70209 0.73700 0.64510 -0.01656 0.03932  0.03135  136 LEU   A C   
933  O  O   . LEU   A 137 ? 0.78901 0.82342 0.72390 -0.01495 0.03752  0.03370  136 LEU   A O   
934  C  CB  . LEU   A 137 ? 0.52546 0.57222 0.46951 -0.01014 0.03972  0.01756  136 LEU   A CB  
935  C  CG  . LEU   A 137 ? 0.50170 0.54984 0.45139 -0.00626 0.03894  0.00959  136 LEU   A CG  
936  C  CD1 . LEU   A 137 ? 0.61283 0.66888 0.55665 -0.00266 0.04098  0.00396  136 LEU   A CD1 
937  C  CD2 . LEU   A 137 ? 0.56392 0.61541 0.52342 -0.00799 0.04123  0.00953  136 LEU   A CD2 
938  N  N   . ASP   A 138 ? 0.83151 0.86475 0.77836 -0.02133 0.04227  0.03599  137 ASP   A N   
939  C  CA  . ASP   A 138 ? 0.96922 0.99817 0.91052 -0.02478 0.04389  0.04470  137 ASP   A CA  
940  C  C   . ASP   A 138 ? 1.02268 1.06120 0.96232 -0.02945 0.04966  0.04770  137 ASP   A C   
941  O  O   . ASP   A 138 ? 1.16128 1.19711 1.09590 -0.03315 0.05192  0.05549  137 ASP   A O   
942  C  CB  . ASP   A 138 ? 1.10585 1.12158 1.05194 -0.02712 0.04250  0.04859  137 ASP   A CB  
943  C  CG  . ASP   A 138 ? 1.12386 1.13937 1.07996 -0.02989 0.04344  0.04440  137 ASP   A CG  
944  O  OD1 . ASP   A 138 ? 1.07061 1.09143 1.03143 -0.02699 0.04204  0.03744  137 ASP   A OD1 
945  O  OD2 . ASP   A 138 ? 1.14968 1.15931 1.10862 -0.03509 0.04545  0.04816  137 ASP   A OD2 
946  N  N   . ARG   A 146 ? 0.97463 1.02875 0.86894 -0.01381 0.03891  0.04781  145 ARG   A N   
947  C  CA  . ARG   A 146 ? 0.93852 1.00387 0.82301 -0.01220 0.03989  0.04356  145 ARG   A CA  
948  C  C   . ARG   A 146 ? 0.91004 0.97524 0.78790 -0.00900 0.03390  0.04111  145 ARG   A C   
949  O  O   . ARG   A 146 ? 0.70166 0.75933 0.58502 -0.00739 0.02903  0.03940  145 ARG   A O   
950  C  CB  . ARG   A 146 ? 0.95196 1.02352 0.84073 -0.01096 0.04288  0.03372  145 ARG   A CB  
951  C  CG  . ARG   A 146 ? 0.93218 1.01692 0.81234 -0.01108 0.04785  0.03204  145 ARG   A CG  
952  C  CD  . ARG   A 146 ? 1.00111 1.09216 0.88684 -0.00913 0.05152  0.02307  145 ARG   A CD  
953  N  NE  . ARG   A 146 ? 0.82528 0.90870 0.71880 -0.00590 0.04775  0.01528  145 ARG   A NE  
954  C  CZ  . ARG   A 146 ? 0.87342 0.95631 0.76298 -0.00207 0.04521  0.00661  145 ARG   A CZ  
955  N  NH1 . ARG   A 146 ? 0.85774 0.94703 0.73530 -0.00093 0.04536  0.00402  145 ARG   A NH1 
956  N  NH2 . ARG   A 146 ? 0.78810 0.86353 0.68542 0.00038  0.04247  0.00038  145 ARG   A NH2 
957  N  N   . ALA   A 147 ? 0.84857 0.92328 0.71450 -0.00844 0.03437  0.04078  146 ALA   A N   
958  C  CA  . ALA   A 147 ? 0.66283 0.73991 0.52082 -0.00628 0.02871  0.03895  146 ALA   A CA  
959  C  C   . ALA   A 147 ? 0.61073 0.69106 0.46723 -0.00436 0.02731  0.02632  146 ALA   A C   
960  O  O   . ALA   A 147 ? 0.59740 0.68274 0.45299 -0.00399 0.03189  0.02013  146 ALA   A O   
961  C  CB  . ALA   A 147 ? 0.77417 0.85997 0.61863 -0.00693 0.02951  0.04611  146 ALA   A CB  
962  N  N   . LEU   A 148 ? 0.50341 0.58079 0.35982 -0.00315 0.02108  0.02258  147 LEU   A N   
963  C  CA  . LEU   A 148 ? 0.54705 0.62621 0.40019 -0.00199 0.01911  0.01085  147 LEU   A CA  
964  C  C   . LEU   A 148 ? 0.50870 0.59907 0.34742 -0.00192 0.02087  0.00803  147 LEU   A C   
965  O  O   . LEU   A 148 ? 0.55451 0.65122 0.38426 -0.00261 0.01898  0.01473  147 LEU   A O   
966  C  CB  . LEU   A 148 ? 0.50777 0.58285 0.36306 -0.00194 0.01185  0.00886  147 LEU   A CB  
967  C  CG  . LEU   A 148 ? 0.44916 0.52488 0.30011 -0.00192 0.00865  -0.00268 147 LEU   A CG  
968  C  CD1 . LEU   A 148 ? 0.42829 0.49487 0.28890 -0.00103 0.01034  -0.01047 147 LEU   A CD1 
969  C  CD2 . LEU   A 148 ? 0.43387 0.51020 0.28442 -0.00301 0.00128  -0.00157 147 LEU   A CD2 
970  N  N   . PRO   A 149 ? 0.44965 0.54299 0.28541 -0.00066 0.02451  -0.00160 148 PRO   A N   
971  C  CA  . PRO   A 149 ? 0.48443 0.58874 0.30558 -0.00033 0.02634  -0.00560 148 PRO   A CA  
972  C  C   . PRO   A 149 ? 0.48284 0.58954 0.29499 -0.00114 0.01954  -0.00866 148 PRO   A C   
973  O  O   . PRO   A 149 ? 0.44483 0.54416 0.26219 -0.00142 0.01441  -0.01405 148 PRO   A O   
974  C  CB  . PRO   A 149 ? 0.54441 0.64811 0.36672 0.00218  0.03062  -0.01739 148 PRO   A CB  
975  C  CG  . PRO   A 149 ? 0.52645 0.61982 0.36425 0.00310  0.03129  -0.01798 148 PRO   A CG  
976  C  CD  . PRO   A 149 ? 0.54967 0.63779 0.39545 0.00090  0.02845  -0.00730 148 PRO   A CD  
977  N  N   . PRO   A 150 ? 0.48109 0.59895 0.27945 -0.00184 0.01934  -0.00558 149 PRO   A N   
978  C  CA  . PRO   A 150 ? 0.46110 0.58334 0.25087 -0.00301 0.01213  -0.00723 149 PRO   A CA  
979  C  C   . PRO   A 150 ? 0.49119 0.60936 0.27970 -0.00340 0.00865  -0.02137 149 PRO   A C   
980  O  O   . PRO   A 150 ? 0.47328 0.58961 0.26332 -0.00511 0.00170  -0.02262 149 PRO   A O   
981  C  CB  . PRO   A 150 ? 0.47174 0.60799 0.24536 -0.00333 0.01423  -0.00347 149 PRO   A CB  
982  C  CG  . PRO   A 150 ? 0.58131 0.71916 0.35737 -0.00297 0.02165  0.00489  149 PRO   A CG  
983  C  CD  . PRO   A 150 ? 0.48637 0.61444 0.27628 -0.00189 0.02567  -0.00026 149 PRO   A CD  
984  N  N   . GLU   A 151 ? 0.42037 0.53725 0.20593 -0.00190 0.01331  -0.03209 150 GLU   A N   
985  C  CA  . GLU   A 151 ? 0.48449 0.59648 0.26646 -0.00247 0.01017  -0.04588 150 GLU   A CA  
986  C  C   . GLU   A 151 ? 0.51664 0.61395 0.31272 -0.00246 0.00808  -0.04998 150 GLU   A C   
987  O  O   . GLU   A 151 ? 0.57148 0.66267 0.36583 -0.00390 0.00447  -0.06017 150 GLU   A O   
988  C  CB  . GLU   A 151 ? 0.55944 0.67483 0.33175 -0.00006 0.01607  -0.05644 150 GLU   A CB  
989  N  N   . GLN   A 152 ? 0.50286 0.59441 0.31221 -0.00131 0.01016  -0.04230 151 GLN   A N   
990  C  CA  . GLN   A 152 ? 0.55424 0.63260 0.37660 -0.00109 0.00863  -0.04562 151 GLN   A CA  
991  C  C   . GLN   A 152 ? 0.60900 0.68380 0.43352 -0.00448 0.00084  -0.04656 151 GLN   A C   
992  O  O   . GLN   A 152 ? 0.51270 0.59435 0.33547 -0.00630 -0.00340 -0.03897 151 GLN   A O   
993  C  CB  . GLN   A 152 ? 0.47700 0.55167 0.31215 0.00022  0.01176  -0.03645 151 GLN   A CB  
994  C  CG  . GLN   A 152 ? 0.65489 0.71701 0.50241 0.00135  0.01183  -0.04083 151 GLN   A CG  
995  C  CD  . GLN   A 152 ? 0.69651 0.75534 0.54287 0.00472  0.01667  -0.05054 151 GLN   A CD  
996  O  OE1 . GLN   A 152 ? 0.82914 0.89225 0.67739 0.00739  0.02262  -0.04877 151 GLN   A OE1 
997  N  NE2 . GLN   A 152 ? 0.79892 0.85024 0.64216 0.00463  0.01420  -0.06091 151 GLN   A NE2 
998  N  N   . GLN   A 153 ? 0.59327 0.65757 0.42171 -0.00520 -0.00085 -0.05582 152 GLN   A N   
999  C  CA  . GLN   A 153 ? 0.56221 0.62225 0.39298 -0.00918 -0.00767 -0.05913 152 GLN   A CA  
1000 C  C   . GLN   A 153 ? 0.53313 0.58029 0.37797 -0.00886 -0.00763 -0.05904 152 GLN   A C   
1001 O  O   . GLN   A 153 ? 0.61022 0.65014 0.45965 -0.00551 -0.00267 -0.06144 152 GLN   A O   
1002 C  CB  . GLN   A 153 ? 0.58962 0.64782 0.40961 -0.01128 -0.00939 -0.07202 152 GLN   A CB  
1003 C  CG  . GLN   A 153 ? 0.67760 0.73788 0.49496 -0.01686 -0.01696 -0.07517 152 GLN   A CG  
1004 C  CD  . GLN   A 153 ? 0.73798 0.80142 0.54032 -0.01903 -0.01811 -0.08655 152 GLN   A CD  
1005 O  OE1 . GLN   A 153 ? 0.87314 0.93504 0.67246 -0.02422 -0.02362 -0.09336 152 GLN   A OE1 
1006 N  NE2 . GLN   A 153 ? 0.78191 0.84974 0.57470 -0.01530 -0.01260 -0.08929 152 GLN   A NE2 
1007 N  N   . PHE   A 154 ? 0.49673 0.54213 0.34837 -0.01218 -0.01312 -0.05617 153 PHE   A N   
1008 C  CA  . PHE   A 154 ? 0.49333 0.52720 0.35747 -0.01249 -0.01350 -0.05610 153 PHE   A CA  
1009 C  C   . PHE   A 154 ? 0.61614 0.64582 0.48068 -0.01768 -0.01923 -0.06226 153 PHE   A C   
1010 O  O   . PHE   A 154 ? 0.61281 0.65039 0.46967 -0.02131 -0.02369 -0.06482 153 PHE   A O   
1011 C  CB  . PHE   A 154 ? 0.45775 0.49347 0.33270 -0.01131 -0.01354 -0.04464 153 PHE   A CB  
1012 C  CG  . PHE   A 154 ? 0.49010 0.52836 0.36615 -0.00733 -0.00791 -0.03833 153 PHE   A CG  
1013 C  CD1 . PHE   A 154 ? 0.45397 0.48494 0.33580 -0.00446 -0.00300 -0.04002 153 PHE   A CD1 
1014 C  CD2 . PHE   A 154 ? 0.57703 0.62552 0.44794 -0.00669 -0.00757 -0.03059 153 PHE   A CD2 
1015 C  CE1 . PHE   A 154 ? 0.51479 0.54937 0.39814 -0.00176 0.00205  -0.03444 153 PHE   A CE1 
1016 C  CE2 . PHE   A 154 ? 0.50794 0.55835 0.37983 -0.00410 -0.00223 -0.02467 153 PHE   A CE2 
1017 C  CZ  . PHE   A 154 ? 0.48847 0.53240 0.36677 -0.00198 0.00257  -0.02688 153 PHE   A CZ  
1018 N  N   . GLU   A 155 ? 0.60274 0.62044 0.47627 -0.01842 -0.01918 -0.06440 154 GLU   A N   
1019 C  CA  . GLU   A 155 ? 0.63410 0.64676 0.50945 -0.02415 -0.02421 -0.06949 154 GLU   A CA  
1020 C  C   . GLU   A 155 ? 0.66188 0.67122 0.55072 -0.02480 -0.02530 -0.06248 154 GLU   A C   
1021 O  O   . GLU   A 155 ? 0.64221 0.64223 0.53789 -0.02158 -0.02152 -0.06112 154 GLU   A O   
1022 C  CB  . GLU   A 155 ? 0.81191 0.81071 0.68262 -0.02497 -0.02273 -0.08097 154 GLU   A CB  
1023 C  CG  . GLU   A 155 ? 0.87499 0.87305 0.73868 -0.03192 -0.02794 -0.08949 154 GLU   A CG  
1024 C  CD  . GLU   A 155 ? 0.99864 0.99794 0.87092 -0.03811 -0.03331 -0.08618 154 GLU   A CD  
1025 O  OE1 . GLU   A 155 ? 1.08733 1.07523 0.96853 -0.03875 -0.03248 -0.08534 154 GLU   A OE1 
1026 O  OE2 . GLU   A 155 ? 1.06582 1.07846 0.93584 -0.04228 -0.03837 -0.08429 154 GLU   A OE2 
1027 N  N   . PRO   A 156 ? 0.62443 0.64224 0.51755 -0.02844 -0.03022 -0.05768 155 PRO   A N   
1028 C  CA  . PRO   A 156 ? 0.69930 0.73062 0.58604 -0.03201 -0.03542 -0.05770 155 PRO   A CA  
1029 C  C   . PRO   A 156 ? 0.66233 0.70527 0.54260 -0.02786 -0.03411 -0.05167 155 PRO   A C   
1030 O  O   . PRO   A 156 ? 0.59532 0.63695 0.47896 -0.02291 -0.02973 -0.04525 155 PRO   A O   
1031 C  CB  . PRO   A 156 ? 0.66515 0.70175 0.56240 -0.03515 -0.03973 -0.05202 155 PRO   A CB  
1032 C  CG  . PRO   A 156 ? 0.64850 0.67819 0.55626 -0.03098 -0.03577 -0.04552 155 PRO   A CG  
1033 C  CD  . PRO   A 156 ? 0.67246 0.68791 0.57821 -0.02882 -0.03089 -0.05137 155 PRO   A CD  
1034 N  N   . PRO   A 157 ? 0.62583 0.68022 0.49642 -0.03017 -0.03788 -0.05352 156 PRO   A N   
1035 C  CA  . PRO   A 157 ? 0.56536 0.63073 0.42853 -0.02638 -0.03662 -0.04725 156 PRO   A CA  
1036 C  C   . PRO   A 157 ? 0.51808 0.58991 0.38940 -0.02326 -0.03729 -0.03469 156 PRO   A C   
1037 O  O   . PRO   A 157 ? 0.54686 0.62069 0.42746 -0.02482 -0.04084 -0.03127 156 PRO   A O   
1038 C  CB  . PRO   A 157 ? 0.55536 0.63233 0.40694 -0.03039 -0.04179 -0.05222 156 PRO   A CB  
1039 C  CG  . PRO   A 157 ? 0.67005 0.74245 0.52396 -0.03687 -0.04607 -0.06093 156 PRO   A CG  
1040 C  CD  . PRO   A 157 ? 0.68211 0.73858 0.54671 -0.03669 -0.04297 -0.06263 156 PRO   A CD  
1041 N  N   . LEU   A 158 ? 0.48256 0.55751 0.35017 -0.01879 -0.03354 -0.02786 157 LEU   A N   
1042 C  CA  . LEU   A 158 ? 0.45246 0.53145 0.32627 -0.01528 -0.03345 -0.01588 157 LEU   A CA  
1043 C  C   . LEU   A 158 ? 0.41105 0.50499 0.27867 -0.01517 -0.03854 -0.01023 157 LEU   A C   
1044 O  O   . LEU   A 158 ? 0.47985 0.58188 0.33545 -0.01666 -0.04019 -0.01380 157 LEU   A O   
1045 C  CB  . LEU   A 158 ? 0.47721 0.55144 0.35009 -0.01121 -0.02683 -0.01075 157 LEU   A CB  
1046 C  CG  . LEU   A 158 ? 0.45659 0.51798 0.33689 -0.01017 -0.02155 -0.01392 157 LEU   A CG  
1047 C  CD1 . LEU   A 158 ? 0.44226 0.50218 0.32273 -0.00683 -0.01588 -0.00683 157 LEU   A CD1 
1048 C  CD2 . LEU   A 158 ? 0.46717 0.52220 0.36011 -0.01097 -0.02343 -0.01311 157 LEU   A CD2 
1049 N  N   . GLN   A 159 ? 0.46596 0.56391 0.34168 -0.01297 -0.04101 -0.00134 158 GLN   A N   
1050 C  CA  . GLN   A 159 ? 0.47133 0.58306 0.34202 -0.01096 -0.04512 0.00657  158 GLN   A CA  
1051 C  C   . GLN   A 159 ? 0.41449 0.52521 0.27933 -0.00646 -0.04061 0.01537  158 GLN   A C   
1052 O  O   . GLN   A 159 ? 0.38834 0.48795 0.25612 -0.00501 -0.03456 0.01618  158 GLN   A O   
1053 C  CB  . GLN   A 159 ? 0.54600 0.66276 0.42798 -0.00956 -0.04938 0.01256  158 GLN   A CB  
1054 C  CG  . GLN   A 159 ? 0.52672 0.64479 0.41502 -0.01489 -0.05335 0.00432  158 GLN   A CG  
1055 C  CD  . GLN   A 159 ? 0.66262 0.79382 0.54163 -0.01962 -0.05922 -0.00165 158 GLN   A CD  
1056 O  OE1 . GLN   A 159 ? 0.67154 0.81633 0.54370 -0.01773 -0.06276 0.00380  158 GLN   A OE1 
1057 N  NE2 . GLN   A 159 ? 0.66383 0.79061 0.54201 -0.02587 -0.06033 -0.01288 158 GLN   A NE2 
1058 N  N   . PRO   A 160 ? 0.39754 0.52019 0.25375 -0.00459 -0.04349 0.02212  159 PRO   A N   
1059 C  CA  . PRO   A 160 ? 0.42773 0.54931 0.27670 -0.00117 -0.03897 0.03063  159 PRO   A CA  
1060 C  C   . PRO   A 160 ? 0.42707 0.53715 0.28550 0.00248  -0.03451 0.03899  159 PRO   A C   
1061 O  O   . PRO   A 160 ? 0.43951 0.54220 0.29549 0.00294  -0.02840 0.04091  159 PRO   A O   
1062 C  CB  . PRO   A 160 ? 0.46567 0.60253 0.30618 0.00075  -0.04434 0.03812  159 PRO   A CB  
1063 C  CG  . PRO   A 160 ? 0.44554 0.59298 0.28431 -0.00328 -0.05085 0.02959  159 PRO   A CG  
1064 C  CD  . PRO   A 160 ? 0.35984 0.49842 0.21142 -0.00600 -0.05100 0.02208  159 PRO   A CD  
1065 N  N   . ARG   A 161 ? 0.42703 0.53594 0.29622 0.00493  -0.03730 0.04375  160 ARG   A N   
1066 C  CA  . ARG   A 161 ? 0.46542 0.56246 0.34319 0.00829  -0.03308 0.05081  160 ARG   A CA  
1067 C  C   . ARG   A 161 ? 0.45632 0.54069 0.34024 0.00582  -0.02781 0.04378  160 ARG   A C   
1068 O  O   . ARG   A 161 ? 0.44667 0.52149 0.33274 0.00700  -0.02254 0.04795  160 ARG   A O   
1069 C  CB  . ARG   A 161 ? 0.51254 0.61162 0.40060 0.01178  -0.03709 0.05593  160 ARG   A CB  
1070 C  CG  . ARG   A 161 ? 0.56330 0.67255 0.44679 0.01659  -0.04107 0.06665  160 ARG   A CG  
1071 C  CD  . ARG   A 161 ? 0.66667 0.76921 0.54342 0.01979  -0.03665 0.07681  160 ARG   A CD  
1072 N  NE  . ARG   A 161 ? 0.58067 0.68816 0.44374 0.01700  -0.03502 0.07570  160 ARG   A NE  
1073 C  CZ  . ARG   A 161 ? 0.56382 0.68606 0.41673 0.01626  -0.03959 0.07526  160 ARG   A CZ  
1074 N  NH1 . ARG   A 161 ? 0.57243 0.70705 0.42723 0.01821  -0.04653 0.07699  160 ARG   A NH1 
1075 N  NH2 . ARG   A 161 ? 0.62000 0.74578 0.46052 0.01343  -0.03713 0.07280  160 ARG   A NH2 
1076 N  N   . GLU   A 162 ? 0.37194 0.45614 0.25834 0.00218  -0.02918 0.03323  161 GLU   A N   
1077 C  CA  . GLU   A 162 ? 0.34695 0.41985 0.23864 0.00040  -0.02447 0.02675  161 GLU   A CA  
1078 C  C   . GLU   A 162 ? 0.39987 0.47103 0.28308 -0.00045 -0.01933 0.02431  161 GLU   A C   
1079 O  O   . GLU   A 162 ? 0.38387 0.44658 0.27118 -0.00013 -0.01411 0.02451  161 GLU   A O   
1080 C  CB  . GLU   A 162 ? 0.42053 0.49275 0.31675 -0.00301 -0.02740 0.01696  161 GLU   A CB  
1081 C  CG  . GLU   A 162 ? 0.40233 0.47604 0.30901 -0.00246 -0.03134 0.01942  161 GLU   A CG  
1082 C  CD  . GLU   A 162 ? 0.47952 0.55471 0.38924 -0.00687 -0.03491 0.01061  161 GLU   A CD  
1083 O  OE1 . GLU   A 162 ? 0.47389 0.55214 0.37551 -0.01021 -0.03634 0.00337  161 GLU   A OE1 
1084 O  OE2 . GLU   A 162 ? 0.55050 0.62348 0.47045 -0.00723 -0.03611 0.01082  161 GLU   A OE2 
1085 N  N   . ARG   A 163 ? 0.35995 0.44015 0.23133 -0.00160 -0.02068 0.02176  162 ARG   A N   
1086 C  CA  . ARG   A 163 ? 0.34893 0.42928 0.21184 -0.00201 -0.01537 0.01972  162 ARG   A CA  
1087 C  C   . ARG   A 163 ? 0.42400 0.50164 0.28679 -0.00002 -0.01079 0.03018  162 ARG   A C   
1088 O  O   . ARG   A 163 ? 0.43218 0.50595 0.29472 -0.00052 -0.00493 0.02918  162 ARG   A O   
1089 C  CB  . ARG   A 163 ? 0.37028 0.46213 0.21940 -0.00337 -0.01795 0.01591  162 ARG   A CB  
1090 C  CG  . ARG   A 163 ? 0.35391 0.44596 0.20197 -0.00639 -0.02113 0.00342  162 ARG   A CG  
1091 C  CD  . ARG   A 163 ? 0.36379 0.46687 0.19709 -0.00811 -0.02336 -0.00160 162 ARG   A CD  
1092 N  NE  . ARG   A 163 ? 0.39467 0.49857 0.21901 -0.00727 -0.01722 -0.00376 162 ARG   A NE  
1093 C  CZ  . ARG   A 163 ? 0.43488 0.53271 0.25856 -0.00767 -0.01314 -0.01370 162 ARG   A CZ  
1094 N  NH1 . ARG   A 163 ? 0.41749 0.50622 0.24852 -0.00903 -0.01448 -0.02219 162 ARG   A NH1 
1095 N  NH2 . ARG   A 163 ? 0.41628 0.51715 0.23223 -0.00635 -0.00727 -0.01456 162 ARG   A NH2 
1096 N  N   . GLU   A 164 ? 0.39063 0.47020 0.25392 0.00223  -0.01335 0.04036  163 GLU   A N   
1097 C  CA  A GLU   A 164 ? 0.46764 0.54244 0.33078 0.00382  -0.00922 0.05094  163 GLU   A CA  
1098 C  CA  B GLU   A 164 ? 0.46777 0.54257 0.33083 0.00378  -0.00914 0.05082  163 GLU   A CA  
1099 C  C   . GLU   A 164 ? 0.46479 0.52698 0.33976 0.00366  -0.00533 0.05101  163 GLU   A C   
1100 O  O   . GLU   A 164 ? 0.47183 0.52903 0.34666 0.00286  0.00002  0.05524  163 GLU   A O   
1101 C  CB  A GLU   A 164 ? 0.50015 0.57831 0.36173 0.00717  -0.01332 0.06165  163 GLU   A CB  
1102 C  CB  B GLU   A 164 ? 0.50042 0.57896 0.36128 0.00706  -0.01315 0.06163  163 GLU   A CB  
1103 C  CG  A GLU   A 164 ? 0.56277 0.65320 0.41066 0.00794  -0.01577 0.06677  163 GLU   A CG  
1104 C  CG  B GLU   A 164 ? 0.54201 0.61416 0.40122 0.00862  -0.00908 0.07333  163 GLU   A CG  
1105 C  CD  A GLU   A 164 ? 0.61056 0.70289 0.44797 0.00614  -0.01013 0.06907  163 GLU   A CD  
1106 C  CD  B GLU   A 164 ? 0.67073 0.74599 0.52735 0.01293  -0.01327 0.08429  163 GLU   A CD  
1107 O  OE1 A GLU   A 164 ? 0.66042 0.74369 0.50112 0.00557  -0.00449 0.07377  163 GLU   A OE1 
1108 O  OE1 B GLU   A 164 ? 0.63590 0.71999 0.49302 0.01473  -0.01952 0.08260  163 GLU   A OE1 
1109 O  OE2 A GLU   A 164 ? 0.59680 0.70062 0.42224 0.00516  -0.01146 0.06675  163 GLU   A OE2 
1110 O  OE2 B GLU   A 164 ? 0.72177 0.79092 0.57580 0.01447  -0.01033 0.09477  163 GLU   A OE2 
1111 N  N   . ALA   A 165 ? 0.41894 0.47657 0.30400 0.00397  -0.00794 0.04642  164 ALA   A N   
1112 C  CA  . ALA   A 165 ? 0.41353 0.45999 0.30968 0.00425  -0.00519 0.04735  164 ALA   A CA  
1113 C  C   . ALA   A 165 ? 0.46546 0.50727 0.36611 0.00191  -0.00142 0.03906  164 ALA   A C   
1114 O  O   . ALA   A 165 ? 0.43809 0.47164 0.34671 0.00167  0.00146  0.04007  164 ALA   A O   
1115 C  CB  . ALA   A 165 ? 0.45321 0.49786 0.35816 0.00622  -0.00969 0.04764  164 ALA   A CB  
1116 N  N   . VAL   A 166 ? 0.40213 0.44876 0.29802 0.00045  -0.00143 0.03074  165 VAL   A N   
1117 C  CA  A VAL   A 166 ? 0.42229 0.46423 0.32326 -0.00066 0.00177  0.02308  165 VAL   A CA  
1118 C  CA  B VAL   A 166 ? 0.42306 0.46512 0.32387 -0.00067 0.00180  0.02302  165 VAL   A CA  
1119 C  C   . VAL   A 166 ? 0.44901 0.48964 0.34970 -0.00134 0.00800  0.02604  165 VAL   A C   
1120 O  O   . VAL   A 166 ? 0.46712 0.51263 0.36007 -0.00174 0.01028  0.03127  165 VAL   A O   
1121 C  CB  A VAL   A 166 ? 0.46228 0.50832 0.35779 -0.00147 0.00030  0.01321  165 VAL   A CB  
1122 C  CB  B VAL   A 166 ? 0.46151 0.50789 0.35649 -0.00147 0.00050  0.01327  165 VAL   A CB  
1123 C  CG1 A VAL   A 166 ? 0.45600 0.50977 0.34002 -0.00167 0.00298  0.01245  165 VAL   A CG1 
1124 C  CG1 B VAL   A 166 ? 0.46553 0.51189 0.36309 -0.00210 -0.00540 0.00951  165 VAL   A CG1 
1125 C  CG2 A VAL   A 166 ? 0.42127 0.46059 0.32396 -0.00164 0.00207  0.00550  165 VAL   A CG2 
1126 C  CG2 B VAL   A 166 ? 0.44551 0.50104 0.32784 -0.00166 0.00125  0.01408  165 VAL   A CG2 
1127 N  N   . ARG   A 167 ? 0.39259 0.42738 0.30187 -0.00179 0.01071  0.02301  166 ARG   A N   
1128 C  CA  . ARG   A 167 ? 0.42565 0.45956 0.33728 -0.00308 0.01628  0.02564  166 ARG   A CA  
1129 C  C   . ARG   A 167 ? 0.43730 0.47121 0.35368 -0.00286 0.01878  0.01757  166 ARG   A C   
1130 O  O   . ARG   A 167 ? 0.40657 0.43675 0.32740 -0.00178 0.01609  0.01169  166 ARG   A O   
1131 C  CB  . ARG   A 167 ? 0.54432 0.57032 0.46331 -0.00385 0.01686  0.03238  166 ARG   A CB  
1132 C  CG  . ARG   A 167 ? 0.54664 0.57084 0.46182 -0.00303 0.01469  0.04121  166 ARG   A CG  
1133 C  CD  . ARG   A 167 ? 0.61525 0.64266 0.52265 -0.00462 0.01839  0.04829  166 ARG   A CD  
1134 N  NE  . ARG   A 167 ? 0.69224 0.71667 0.59583 -0.00324 0.01647  0.05770  166 ARG   A NE  
1135 C  CZ  . ARG   A 167 ? 0.67690 0.70749 0.57259 -0.00109 0.01288  0.06047  166 ARG   A CZ  
1136 N  NH1 . ARG   A 167 ? 0.63742 0.67700 0.52788 -0.00070 0.01057  0.05385  166 ARG   A NH1 
1137 N  NH2 . ARG   A 167 ? 0.66059 0.68813 0.55328 0.00078  0.01149  0.07005  166 ARG   A NH2 
1138 N  N   . PRO   A 168 ? 0.40191 0.44043 0.31756 -0.00374 0.02394  0.01746  167 PRO   A N   
1139 C  CA  . PRO   A 168 ? 0.36239 0.40230 0.28272 -0.00250 0.02640  0.01009  167 PRO   A CA  
1140 C  C   . PRO   A 168 ? 0.31508 0.34882 0.24676 -0.00296 0.02646  0.01017  167 PRO   A C   
1141 O  O   . PRO   A 168 ? 0.39920 0.42944 0.33500 -0.00521 0.02709  0.01619  167 PRO   A O   
1142 C  CB  . PRO   A 168 ? 0.44528 0.49446 0.36149 -0.00341 0.03211  0.01130  167 PRO   A CB  
1143 C  CG  . PRO   A 168 ? 0.52982 0.57857 0.44385 -0.00659 0.03324  0.02114  167 PRO   A CG  
1144 C  CD  . PRO   A 168 ? 0.49612 0.53944 0.40671 -0.00588 0.02790  0.02451  167 PRO   A CD  
1145 N  N   . GLY   A 169 ? 0.35693 0.38915 0.29304 -0.00074 0.02596  0.00323  168 GLY   A N   
1146 C  CA  . GLY   A 169 ? 0.39541 0.42328 0.34159 -0.00076 0.02596  0.00260  168 GLY   A CA  
1147 C  C   . GLY   A 169 ? 0.43948 0.47079 0.38867 0.00209  0.02821  -0.00381 168 GLY   A C   
1148 O  O   . GLY   A 169 ? 0.38235 0.41835 0.32581 0.00431  0.02986  -0.00820 168 GLY   A O   
1149 N  N   . VAL   A 170 ? 0.38827 0.41757 0.34628 0.00243  0.02835  -0.00437 169 VAL   A N   
1150 C  CA  . VAL   A 170 ? 0.39470 0.42681 0.35668 0.00607  0.02996  -0.00982 169 VAL   A CA  
1151 C  C   . VAL   A 170 ? 0.45632 0.48005 0.42394 0.00753  0.02642  -0.01184 169 VAL   A C   
1152 O  O   . VAL   A 170 ? 0.34666 0.36660 0.31922 0.00514  0.02469  -0.00824 169 VAL   A O   
1153 C  CB  . VAL   A 170 ? 0.45522 0.49698 0.42270 0.00524  0.03433  -0.00808 169 VAL   A CB  
1154 C  CG1 . VAL   A 170 ? 0.37967 0.41956 0.35310 0.00072  0.03387  -0.00257 169 VAL   A CG1 
1155 C  CG2 . VAL   A 170 ? 0.43576 0.48093 0.40843 0.01000  0.03548  -0.01321 169 VAL   A CG2 
1156 N  N   . LEU   A 171 ? 0.39811 0.41835 0.36440 0.01139  0.02548  -0.01758 170 LEU   A N   
1157 C  CA  . LEU   A 171 ? 0.38353 0.39613 0.35498 0.01312  0.02275  -0.01939 170 LEU   A CA  
1158 C  C   . LEU   A 171 ? 0.46120 0.47911 0.43954 0.01623  0.02520  -0.02019 170 LEU   A C   
1159 O  O   . LEU   A 171 ? 0.46463 0.48714 0.44191 0.02037  0.02791  -0.02402 170 LEU   A O   
1160 C  CB  . LEU   A 171 ? 0.43504 0.43980 0.40135 0.01526  0.02051  -0.02483 170 LEU   A CB  
1161 C  CG  . LEU   A 171 ? 0.44666 0.44269 0.41703 0.01765  0.01838  -0.02728 170 LEU   A CG  
1162 C  CD1 . LEU   A 171 ? 0.47973 0.47180 0.45540 0.01450  0.01544  -0.02280 170 LEU   A CD1 
1163 C  CD2 . LEU   A 171 ? 0.50240 0.48998 0.46639 0.01861  0.01654  -0.03293 170 LEU   A CD2 
1164 N  N   . ARG   A 172 ? 0.35307 0.37137 0.33842 0.01445  0.02430  -0.01672 171 ARG   A N   
1165 C  CA  . ARG   A 172 ? 0.37574 0.40157 0.36814 0.01667  0.02624  -0.01671 171 ARG   A CA  
1166 C  C   . ARG   A 172 ? 0.44882 0.46933 0.44469 0.02127  0.02430  -0.01909 171 ARG   A C   
1167 O  O   . ARG   A 172 ? 0.40132 0.42750 0.40044 0.02609  0.02614  -0.02116 171 ARG   A O   
1168 C  CB  . ARG   A 172 ? 0.33585 0.36599 0.33346 0.01181  0.02642  -0.01203 171 ARG   A CB  
1169 C  CG  . ARG   A 172 ? 0.35927 0.39511 0.35417 0.00740  0.02915  -0.00900 171 ARG   A CG  
1170 C  CD  . ARG   A 172 ? 0.42550 0.46648 0.42630 0.00277  0.03017  -0.00545 171 ARG   A CD  
1171 N  NE  . ARG   A 172 ? 0.39875 0.44308 0.39664 -0.00206 0.03286  -0.00186 171 ARG   A NE  
1172 C  CZ  . ARG   A 172 ? 0.47256 0.52777 0.47033 -0.00280 0.03686  -0.00161 171 ARG   A CZ  
1173 N  NH1 . ARG   A 172 ? 0.46357 0.52816 0.46422 0.00162  0.03875  -0.00517 171 ARG   A NH1 
1174 N  NH2 . ARG   A 172 ? 0.43773 0.49450 0.43231 -0.00782 0.03922  0.00256  171 ARG   A NH2 
1175 N  N   . SER   A 173 ? 0.42061 0.43073 0.41594 0.02018  0.02075  -0.01853 172 SER   A N   
1176 C  CA  . SER   A 173 ? 0.42218 0.42652 0.42041 0.02414  0.01900  -0.01982 172 SER   A CA  
1177 C  C   . SER   A 173 ? 0.39869 0.39089 0.39383 0.02215  0.01558  -0.01994 172 SER   A C   
1178 O  O   . SER   A 173 ? 0.36003 0.35018 0.35258 0.01769  0.01423  -0.01835 172 SER   A O   
1179 C  CB  . SER   A 173 ? 0.40149 0.41183 0.40721 0.02420  0.01864  -0.01673 172 SER   A CB  
1180 O  OG  . SER   A 173 ? 0.40204 0.40998 0.40894 0.01898  0.01663  -0.01336 172 SER   A OG  
1181 N  N   . ARG   A 174 ? 0.39975 0.38422 0.39540 0.02567  0.01427  -0.02158 173 ARG   A N   
1182 C  CA  . ARG   A 174 ? 0.44494 0.41788 0.43801 0.02348  0.01124  -0.02183 173 ARG   A CA  
1183 C  C   . ARG   A 174 ? 0.53648 0.50317 0.53242 0.02754  0.01036  -0.02148 173 ARG   A C   
1184 O  O   . ARG   A 174 ? 0.59357 0.55508 0.58759 0.03248  0.01133  -0.02487 173 ARG   A O   
1185 C  CB  . ARG   A 174 ? 0.52949 0.49670 0.51545 0.02274  0.01101  -0.02624 173 ARG   A CB  
1186 C  CG  . ARG   A 174 ? 0.54054 0.49717 0.52386 0.01933  0.00783  -0.02693 173 ARG   A CG  
1187 C  CD  . ARG   A 174 ? 0.58053 0.53283 0.55637 0.01856  0.00762  -0.03230 173 ARG   A CD  
1188 N  NE  . ARG   A 174 ? 0.69102 0.63131 0.66446 0.01625  0.00495  -0.03450 173 ARG   A NE  
1189 C  CZ  . ARG   A 174 ? 0.77817 0.70767 0.75018 0.01954  0.00523  -0.03784 173 ARG   A CZ  
1190 N  NH1 . ARG   A 174 ? 0.79934 0.72927 0.77227 0.02626  0.00801  -0.03951 173 ARG   A NH1 
1191 N  NH2 . ARG   A 174 ? 0.79002 0.70808 0.75987 0.01602  0.00274  -0.03936 173 ARG   A NH2 
1192 N  N   . ALA   A 175 ? 0.39429 0.36186 0.39457 0.02590  0.00878  -0.01727 174 ALA   A N   
1193 C  CA  . ALA   A 175 ? 0.35264 0.31622 0.35579 0.02971  0.00789  -0.01549 174 ALA   A CA  
1194 C  C   . ALA   A 175 ? 0.39508 0.35331 0.39893 0.02550  0.00530  -0.01197 174 ALA   A C   
1195 O  O   . ALA   A 175 ? 0.37499 0.33508 0.37846 0.02026  0.00449  -0.01083 174 ALA   A O   
1196 C  CB  . ALA   A 175 ? 0.39701 0.37239 0.40574 0.03324  0.00916  -0.01353 174 ALA   A CB  
1197 N  N   . GLU   A 176 ? 0.35561 0.30745 0.36043 0.02822  0.00420  -0.00998 175 GLU   A N   
1198 C  CA  . GLU   A 176 ? 0.38256 0.33011 0.38805 0.02468  0.00213  -0.00610 175 GLU   A CA  
1199 C  C   . GLU   A 176 ? 0.39639 0.35309 0.40624 0.02588  0.00183  -0.00210 175 GLU   A C   
1200 O  O   . GLU   A 176 ? 0.38475 0.34655 0.39706 0.03114  0.00248  -0.00163 175 GLU   A O   
1201 C  CB  . GLU   A 176 ? 0.41105 0.34440 0.41386 0.02611  0.00108  -0.00585 175 GLU   A CB  
1202 C  CG  . GLU   A 176 ? 0.42339 0.34670 0.42135 0.02367  0.00092  -0.01036 175 GLU   A CG  
1203 C  CD  . GLU   A 176 ? 0.48916 0.39670 0.48435 0.02352  -0.00021 -0.01000 175 GLU   A CD  
1204 O  OE1 . GLU   A 176 ? 0.56251 0.46639 0.55930 0.02652  -0.00059 -0.00586 175 GLU   A OE1 
1205 O  OE2 . GLU   A 176 ? 0.61167 0.51040 0.60281 0.02009  -0.00080 -0.01375 175 GLU   A OE2 
1206 N  N   . TYR   A 177 ? 0.33575 0.29522 0.34651 0.02112  0.00079  0.00056  176 TYR   A N   
1207 C  CA  . TYR   A 177 ? 0.31459 0.28315 0.32855 0.02102  0.00038  0.00362  176 TYR   A CA  
1208 C  C   . TYR   A 177 ? 0.32499 0.28933 0.33816 0.01875  -0.00114 0.00742  176 TYR   A C   
1209 O  O   . TYR   A 177 ? 0.33038 0.28858 0.34168 0.01479  -0.00159 0.00753  176 TYR   A O   
1210 C  CB  . TYR   A 177 ? 0.30273 0.28035 0.31821 0.01723  0.00129  0.00247  176 TYR   A CB  
1211 C  CG  . TYR   A 177 ? 0.33371 0.31639 0.34980 0.01875  0.00312  -0.00053 176 TYR   A CG  
1212 C  CD1 . TYR   A 177 ? 0.32571 0.30415 0.33883 0.01758  0.00398  -0.00322 176 TYR   A CD1 
1213 C  CD2 . TYR   A 177 ? 0.45798 0.45079 0.47753 0.02118  0.00399  -0.00058 176 TYR   A CD2 
1214 C  CE1 . TYR   A 177 ? 0.37864 0.36238 0.39168 0.01888  0.00599  -0.00564 176 TYR   A CE1 
1215 C  CE2 . TYR   A 177 ? 0.36361 0.36224 0.38395 0.02218  0.00608  -0.00304 176 TYR   A CE2 
1216 C  CZ  . TYR   A 177 ? 0.38145 0.37525 0.39826 0.02110  0.00723  -0.00543 176 TYR   A CZ  
1217 O  OH  . TYR   A 177 ? 0.41059 0.41083 0.42757 0.02198  0.00961  -0.00752 176 TYR   A OH  
1218 N  N   . THR   A 178 ? 0.33996 0.30866 0.35457 0.02123  -0.00194 0.01073  177 THR   A N   
1219 C  CA  . THR   A 178 ? 0.33032 0.29755 0.34390 0.01916  -0.00313 0.01496  177 THR   A CA  
1220 C  C   . THR   A 178 ? 0.30037 0.27994 0.31581 0.01837  -0.00347 0.01616  177 THR   A C   
1221 O  O   . THR   A 178 ? 0.36013 0.34843 0.37793 0.01879  -0.00287 0.01369  177 THR   A O   
1222 C  CB  . THR   A 178 ? 0.44178 0.40065 0.45380 0.02320  -0.00410 0.01866  177 THR   A CB  
1223 O  OG1 . THR   A 178 ? 0.44080 0.40723 0.45494 0.02892  -0.00462 0.02023  177 THR   A OG1 
1224 C  CG2 . THR   A 178 ? 0.39671 0.34246 0.40664 0.02465  -0.00364 0.01630  177 THR   A CG2 
1225 N  N   . GLU   A 179 ? 0.39648 0.37696 0.41053 0.01679  -0.00436 0.01988  178 GLU   A N   
1226 C  CA  . GLU   A 179 ? 0.42966 0.42166 0.44446 0.01574  -0.00484 0.02054  178 GLU   A CA  
1227 C  C   . GLU   A 179 ? 0.50853 0.50906 0.52555 0.02039  -0.00584 0.02111  178 GLU   A C   
1228 O  O   . GLU   A 179 ? 0.54879 0.56048 0.56703 0.01907  -0.00632 0.02018  178 GLU   A O   
1229 C  CB  . GLU   A 179 ? 0.40985 0.40161 0.42188 0.01364  -0.00546 0.02468  178 GLU   A CB  
1230 C  CG  . GLU   A 179 ? 0.54757 0.53284 0.55748 0.01689  -0.00665 0.03025  178 GLU   A CG  
1231 C  CD  . GLU   A 179 ? 0.56712 0.56012 0.57757 0.02204  -0.00832 0.03308  178 GLU   A CD  
1232 O  OE1 . GLU   A 179 ? 0.67539 0.68089 0.68726 0.02152  -0.00883 0.03123  178 GLU   A OE1 
1233 O  OE2 . GLU   A 179 ? 0.63107 0.61757 0.64055 0.02664  -0.00922 0.03715  178 GLU   A OE2 
1234 N  N   . ALA   A 180 ? 0.45837 0.45431 0.47608 0.02583  -0.00619 0.02235  179 ALA   A N   
1235 C  CA  . ALA   A 180 ? 0.43317 0.43874 0.45389 0.03114  -0.00712 0.02310  179 ALA   A CA  
1236 C  C   . ALA   A 180 ? 0.44654 0.45857 0.47097 0.03177  -0.00570 0.01842  179 ALA   A C   
1237 O  O   . ALA   A 180 ? 0.48304 0.50576 0.51104 0.03566  -0.00625 0.01856  179 ALA   A O   
1238 C  CB  . ALA   A 180 ? 0.53314 0.53085 0.55299 0.03799  -0.00800 0.02709  179 ALA   A CB  
1239 N  N   . SER   A 181 ? 0.42955 0.43653 0.45333 0.02801  -0.00389 0.01465  180 SER   A N   
1240 C  CA  . SER   A 181 ? 0.40465 0.41645 0.43111 0.02872  -0.00216 0.01082  180 SER   A CA  
1241 C  C   . SER   A 181 ? 0.43620 0.46074 0.46551 0.02460  -0.00173 0.00884  180 SER   A C   
1242 O  O   . SER   A 181 ? 0.50305 0.53447 0.53530 0.02516  -0.00030 0.00648  180 SER   A O   
1243 C  CB  . SER   A 181 ? 0.42391 0.42550 0.44779 0.02638  -0.00053 0.00796  180 SER   A CB  
1244 O  OG  . SER   A 181 ? 0.41137 0.40040 0.43241 0.02920  -0.00086 0.00884  180 SER   A OG  
1245 N  N   . GLY   A 182 ? 0.38543 0.41285 0.41368 0.02008  -0.00264 0.00941  181 GLY   A N   
1246 C  CA  . GLY   A 182 ? 0.40604 0.44251 0.43625 0.01528  -0.00198 0.00676  181 GLY   A CA  
1247 C  C   . GLY   A 182 ? 0.36043 0.39034 0.38932 0.01124  0.00019  0.00409  181 GLY   A C   
1248 O  O   . GLY   A 182 ? 0.38183 0.40267 0.40886 0.01264  0.00106  0.00391  181 GLY   A O   
1249 N  N   . PRO   A 183 ? 0.31052 0.34478 0.34008 0.00614  0.00098  0.00198  182 PRO   A N   
1250 C  CA  . PRO   A 183 ? 0.29627 0.32322 0.32393 0.00247  0.00283  0.00035  182 PRO   A CA  
1251 C  C   . PRO   A 183 ? 0.36401 0.39039 0.39249 0.00316  0.00476  -0.00068 182 PRO   A C   
1252 O  O   . PRO   A 183 ? 0.33125 0.36574 0.36279 0.00499  0.00535  -0.00112 182 PRO   A O   
1253 C  CB  . PRO   A 183 ? 0.31706 0.34829 0.34509 -0.00283 0.00314  -0.00155 182 PRO   A CB  
1254 C  CG  . PRO   A 183 ? 0.40118 0.44483 0.43247 -0.00259 0.00185  -0.00176 182 PRO   A CG  
1255 C  CD  . PRO   A 183 ? 0.35042 0.39527 0.38178 0.00322  -0.00005 0.00110  182 PRO   A CD  
1256 N  N   . CYS   A 184 ? 0.27981 0.29750 0.30545 0.00184  0.00580  -0.00095 183 CYS   A N   
1257 C  CA  . CYS   A 184 ? 0.31323 0.32976 0.33819 0.00165  0.00776  -0.00177 183 CYS   A CA  
1258 C  C   . CYS   A 184 ? 0.36196 0.37765 0.38633 -0.00337 0.00926  -0.00222 183 CYS   A C   
1259 O  O   . CYS   A 184 ? 0.34099 0.35150 0.36385 -0.00554 0.00882  -0.00202 183 CYS   A O   
1260 C  CB  . CYS   A 184 ? 0.37953 0.38713 0.40108 0.00380  0.00751  -0.00154 183 CYS   A CB  
1261 S  SG  . CYS   A 184 ? 0.44205 0.44741 0.46359 0.00940  0.00610  -0.00123 183 CYS   A SG  
1262 N  N   . ILE   A 185 ? 0.27460 0.29511 0.30009 -0.00502 0.01128  -0.00266 184 ILE   A N   
1263 C  CA  . ILE   A 185 ? 0.28308 0.30247 0.30810 -0.01021 0.01303  -0.00261 184 ILE   A CA  
1264 C  C   . ILE   A 185 ? 0.30013 0.31520 0.32199 -0.01010 0.01481  -0.00151 184 ILE   A C   
1265 O  O   . ILE   A 185 ? 0.32014 0.33843 0.34159 -0.00711 0.01551  -0.00175 184 ILE   A O   
1266 C  CB  . ILE   A 185 ? 0.38620 0.41630 0.41529 -0.01360 0.01411  -0.00351 184 ILE   A CB  
1267 C  CG1 . ILE   A 185 ? 0.55157 0.58915 0.58385 -0.01238 0.01187  -0.00446 184 ILE   A CG1 
1268 C  CG2 . ILE   A 185 ? 0.43201 0.45878 0.46036 -0.02004 0.01578  -0.00355 184 ILE   A CG2 
1269 C  CD1 . ILE   A 185 ? 0.51338 0.54852 0.54500 -0.01634 0.01085  -0.00556 184 ILE   A CD1 
1270 N  N   . LEU   A 186 ? 0.24775 0.25587 0.26711 -0.01311 0.01566  -0.00033 185 LEU   A N   
1271 C  CA  . LEU   A 186 ? 0.28514 0.29079 0.30134 -0.01388 0.01756  0.00146  185 LEU   A CA  
1272 C  C   . LEU   A 186 ? 0.29343 0.29656 0.30950 -0.01923 0.01950  0.00270  185 LEU   A C   
1273 O  O   . LEU   A 186 ? 0.29518 0.29538 0.31257 -0.02181 0.01902  0.00173  185 LEU   A O   
1274 C  CB  . LEU   A 186 ? 0.29882 0.29674 0.31093 -0.01106 0.01629  0.00267  185 LEU   A CB  
1275 C  CG  . LEU   A 186 ? 0.30988 0.29993 0.32111 -0.01155 0.01518  0.00360  185 LEU   A CG  
1276 C  CD1 . LEU   A 186 ? 0.29110 0.27546 0.29990 -0.01405 0.01689  0.00617  185 LEU   A CD1 
1277 C  CD2 . LEU   A 186 ? 0.32225 0.30919 0.33181 -0.00813 0.01301  0.00378  185 LEU   A CD2 
1278 N  N   . THR   A 187 ? 0.27076 0.27474 0.28483 -0.02115 0.02186  0.00477  186 THR   A N   
1279 C  CA  . THR   A 187 ? 0.26586 0.26671 0.27953 -0.02686 0.02413  0.00655  186 THR   A CA  
1280 C  C   . THR   A 187 ? 0.30507 0.29928 0.31347 -0.02662 0.02549  0.01045  186 THR   A C   
1281 O  O   . THR   A 187 ? 0.30608 0.30022 0.31143 -0.02234 0.02453  0.01117  186 THR   A O   
1282 C  CB  . THR   A 187 ? 0.37656 0.38873 0.39413 -0.03096 0.02622  0.00578  186 THR   A CB  
1283 O  OG1 . THR   A 187 ? 0.37122 0.38987 0.38724 -0.02929 0.02812  0.00720  186 THR   A OG1 
1284 C  CG2 . THR   A 187 ? 0.38840 0.40983 0.41122 -0.02969 0.02435  0.00233  186 THR   A CG2 
1285 N  N   . PRO   A 188 ? 0.31408 0.30209 0.32088 -0.03130 0.02758  0.01316  187 PRO   A N   
1286 C  CA  . PRO   A 188 ? 0.36757 0.34874 0.36879 -0.03043 0.02860  0.01782  187 PRO   A CA  
1287 C  C   . PRO   A 188 ? 0.37953 0.36912 0.37812 -0.02921 0.02997  0.01935  187 PRO   A C   
1288 O  O   . PRO   A 188 ? 0.39809 0.38482 0.39164 -0.02610 0.02938  0.02202  187 PRO   A O   
1289 C  CB  . PRO   A 188 ? 0.36039 0.33341 0.36088 -0.03644 0.03104  0.02044  187 PRO   A CB  
1290 C  CG  . PRO   A 188 ? 0.42732 0.39822 0.43198 -0.03873 0.03003  0.01625  187 PRO   A CG  
1291 C  CD  . PRO   A 188 ? 0.36557 0.34972 0.37475 -0.03713 0.02859  0.01215  187 PRO   A CD  
1292 N  N   . HIS   A 189 ? 0.38006 0.38109 0.38192 -0.03115 0.03167  0.01739  188 HIS   A N   
1293 C  CA  . HIS   A 189 ? 0.40977 0.41977 0.40905 -0.03010 0.03376  0.01838  188 HIS   A CA  
1294 C  C   . HIS   A 189 ? 0.41223 0.43195 0.41393 -0.02525 0.03274  0.01393  188 HIS   A C   
1295 O  O   . HIS   A 189 ? 0.41959 0.44796 0.41967 -0.02405 0.03489  0.01366  188 HIS   A O   
1296 C  CB  . HIS   A 189 ? 0.41615 0.43236 0.41680 -0.03659 0.03773  0.02072  188 HIS   A CB  
1297 C  CG  . HIS   A 189 ? 0.52982 0.53482 0.52742 -0.04171 0.03917  0.02556  188 HIS   A CG  
1298 N  ND1 . HIS   A 189 ? 0.63934 0.63661 0.62989 -0.04035 0.03957  0.03056  188 HIS   A ND1 
1299 C  CD2 . HIS   A 189 ? 0.59287 0.59218 0.59317 -0.04802 0.04018  0.02615  188 HIS   A CD2 
1300 C  CE1 . HIS   A 189 ? 0.66337 0.64988 0.65251 -0.04510 0.04095  0.03453  188 HIS   A CE1 
1301 N  NE2 . HIS   A 189 ? 0.71021 0.69709 0.70508 -0.05009 0.04144  0.03160  188 HIS   A NE2 
1302 N  N   . ARG   A 190 ? 0.34888 0.36726 0.35409 -0.02224 0.02980  0.01051  189 ARG   A N   
1303 C  CA  . ARG   A 190 ? 0.33536 0.36106 0.34229 -0.01722 0.02899  0.00684  189 ARG   A CA  
1304 C  C   . ARG   A 190 ? 0.33632 0.35531 0.34343 -0.01318 0.02529  0.00478  189 ARG   A C   
1305 O  O   . ARG   A 190 ? 0.32705 0.34188 0.33693 -0.01453 0.02361  0.00458  189 ARG   A O   
1306 C  CB  . ARG   A 190 ? 0.39833 0.43583 0.41189 -0.01834 0.03031  0.00482  189 ARG   A CB  
1307 C  CG  . ARG   A 190 ? 0.44019 0.48629 0.45470 -0.01263 0.03082  0.00185  189 ARG   A CG  
1308 C  CD  . ARG   A 190 ? 0.50635 0.56555 0.52826 -0.01277 0.03179  0.00022  189 ARG   A CD  
1309 N  NE  . ARG   A 190 ? 0.47105 0.53851 0.49396 -0.00641 0.03283  -0.00248 189 ARG   A NE  
1310 C  CZ  . ARG   A 190 ? 0.40955 0.48652 0.43165 -0.00578 0.03650  -0.00269 189 ARG   A CZ  
1311 N  NH1 . ARG   A 190 ? 0.47475 0.55443 0.49477 -0.01157 0.03948  0.00026  189 ARG   A NH1 
1312 N  NH2 . ARG   A 190 ? 0.48470 0.56837 0.50786 0.00099  0.03745  -0.00581 189 ARG   A NH2 
1313 N  N   . ASP   A 191 ? 0.32486 0.34318 0.32885 -0.00858 0.02421  0.00299  190 ASP   A N   
1314 C  CA  . ASP   A 191 ? 0.29553 0.30719 0.29907 -0.00536 0.02086  0.00138  190 ASP   A CA  
1315 C  C   . ASP   A 191 ? 0.29610 0.29912 0.29788 -0.00711 0.01912  0.00386  190 ASP   A C   
1316 O  O   . ASP   A 191 ? 0.31248 0.31108 0.31595 -0.00605 0.01672  0.00315  190 ASP   A O   
1317 C  CB  . ASP   A 191 ? 0.33333 0.34758 0.34230 -0.00360 0.01955  -0.00079 190 ASP   A CB  
1318 C  CG  . ASP   A 191 ? 0.39819 0.42142 0.40953 -0.00050 0.02112  -0.00308 190 ASP   A CG  
1319 O  OD1 . ASP   A 191 ? 0.34677 0.37012 0.35457 0.00274  0.02182  -0.00483 190 ASP   A OD1 
1320 O  OD2 . ASP   A 191 ? 0.37889 0.40960 0.39561 -0.00108 0.02163  -0.00338 190 ASP   A OD2 
1321 N  N   . ASN   A 192 ? 0.27369 0.27458 0.27208 -0.00950 0.02052  0.00711  191 ASN   A N   
1322 C  CA  . ASN   A 192 ? 0.26146 0.25436 0.25875 -0.01048 0.01926  0.00984  191 ASN   A CA  
1323 C  C   . ASN   A 192 ? 0.28879 0.27812 0.28337 -0.00744 0.01640  0.00976  191 ASN   A C   
1324 O  O   . ASN   A 192 ? 0.31763 0.30175 0.31297 -0.00709 0.01486  0.01117  191 ASN   A O   
1325 C  CB  . ASN   A 192 ? 0.29405 0.28470 0.28828 -0.01348 0.02160  0.01406  191 ASN   A CB  
1326 C  CG  . ASN   A 192 ? 0.29733 0.27882 0.29130 -0.01407 0.02081  0.01684  191 ASN   A CG  
1327 O  OD1 . ASN   A 192 ? 0.31102 0.28863 0.30132 -0.01201 0.01962  0.01970  191 ASN   A OD1 
1328 N  ND2 . ASN   A 192 ? 0.29646 0.27490 0.29431 -0.01644 0.02132  0.01572  191 ASN   A ND2 
1329 N  N   . LEU   A 193 ? 0.27489 0.26729 0.26651 -0.00533 0.01566  0.00780  192 LEU   A N   
1330 C  CA  . LEU   A 193 ? 0.25991 0.24989 0.24931 -0.00334 0.01264  0.00693  192 LEU   A CA  
1331 C  C   . LEU   A 193 ? 0.29326 0.28301 0.28552 -0.00176 0.01117  0.00303  192 LEU   A C   
1332 O  O   . LEU   A 193 ? 0.31697 0.30981 0.30978 -0.00065 0.01247  0.00043  192 LEU   A O   
1333 C  CB  . LEU   A 193 ? 0.28618 0.27888 0.26910 -0.00265 0.01260  0.00703  192 LEU   A CB  
1334 C  CG  . LEU   A 193 ? 0.34474 0.33665 0.32356 -0.00340 0.01264  0.01193  192 LEU   A CG  
1335 C  CD1 . LEU   A 193 ? 0.35575 0.34749 0.33494 -0.00569 0.01602  0.01539  192 LEU   A CD1 
1336 C  CD2 . LEU   A 193 ? 0.35732 0.35303 0.32906 -0.00254 0.01176  0.01151  192 LEU   A CD2 
1337 N  N   . HIS   A 194 ? 0.27065 0.25694 0.26488 -0.00145 0.00866  0.00291  193 HIS   A N   
1338 C  CA  . HIS   A 194 ? 0.26001 0.24497 0.25593 -0.00023 0.00726  -0.00013 193 HIS   A CA  
1339 C  C   . HIS   A 194 ? 0.28244 0.26465 0.27772 -0.00056 0.00432  -0.00034 193 HIS   A C   
1340 O  O   . HIS   A 194 ? 0.25576 0.23804 0.25135 -0.00130 0.00324  0.00214  193 HIS   A O   
1341 C  CB  . HIS   A 194 ? 0.25723 0.24246 0.25819 -0.00011 0.00785  -0.00037 193 HIS   A CB  
1342 C  CG  . HIS   A 194 ? 0.26921 0.25283 0.27313 -0.00144 0.00729  0.00165  193 HIS   A CG  
1343 N  ND1 . HIS   A 194 ? 0.27964 0.26454 0.28710 -0.00193 0.00795  0.00150  193 HIS   A ND1 
1344 C  CD2 . HIS   A 194 ? 0.26667 0.24824 0.27048 -0.00200 0.00625  0.00354  193 HIS   A CD2 
1345 C  CE1 . HIS   A 194 ? 0.27039 0.25332 0.27919 -0.00290 0.00758  0.00277  193 HIS   A CE1 
1346 N  NE2 . HIS   A 194 ? 0.22959 0.21046 0.23656 -0.00263 0.00667  0.00412  193 HIS   A NE2 
1347 N  N   . GLN   A 195 ? 0.27673 0.25662 0.27114 0.00005  0.00312  -0.00334 194 GLN   A N   
1348 C  CA  . GLN   A 195 ? 0.28238 0.25954 0.27691 -0.00124 0.00038  -0.00400 194 GLN   A CA  
1349 C  C   . GLN   A 195 ? 0.30366 0.27722 0.30149 -0.00083 0.00018  -0.00470 194 GLN   A C   
1350 O  O   . GLN   A 195 ? 0.27936 0.25187 0.27743 0.00125  0.00155  -0.00615 194 GLN   A O   
1351 C  CB  . GLN   A 195 ? 0.30728 0.28334 0.29654 -0.00172 -0.00098 -0.00721 194 GLN   A CB  
1352 C  CG  . GLN   A 195 ? 0.33063 0.30243 0.32013 -0.00373 -0.00355 -0.00914 194 GLN   A CG  
1353 C  CD  . GLN   A 195 ? 0.45759 0.42846 0.44145 -0.00512 -0.00524 -0.01284 194 GLN   A CD  
1354 O  OE1 . GLN   A 195 ? 0.46695 0.44208 0.44656 -0.00471 -0.00501 -0.01312 194 GLN   A OE1 
1355 N  NE2 . GLN   A 195 ? 0.43225 0.39718 0.41551 -0.00710 -0.00692 -0.01574 194 GLN   A NE2 
1356 N  N   . ILE   A 196 ? 0.27229 0.24482 0.27280 -0.00253 -0.00139 -0.00323 195 ILE   A N   
1357 C  CA  . ILE   A 196 ? 0.25275 0.22235 0.25605 -0.00234 -0.00146 -0.00274 195 ILE   A CA  
1358 C  C   . ILE   A 196 ? 0.29057 0.25629 0.29359 -0.00488 -0.00359 -0.00323 195 ILE   A C   
1359 O  O   . ILE   A 196 ? 0.29384 0.26258 0.29831 -0.00728 -0.00487 -0.00181 195 ILE   A O   
1360 C  CB  . ILE   A 196 ? 0.29538 0.26840 0.30242 -0.00244 -0.00061 -0.00001 195 ILE   A CB  
1361 C  CG1 . ILE   A 196 ? 0.29693 0.27312 0.30412 -0.00112 0.00142  0.00017  195 ILE   A CG1 
1362 C  CG2 . ILE   A 196 ? 0.28264 0.25375 0.29177 -0.00221 -0.00076 0.00094  195 ILE   A CG2 
1363 C  CD1 . ILE   A 196 ? 0.32961 0.30824 0.33918 -0.00184 0.00221  0.00210  195 ILE   A CD1 
1364 N  N   . ASP   A 197 ? 0.27318 0.23227 0.27455 -0.00436 -0.00390 -0.00515 196 ASP   A N   
1365 C  CA  . ASP   A 197 ? 0.31354 0.26695 0.31412 -0.00758 -0.00578 -0.00589 196 ASP   A CA  
1366 C  C   . ASP   A 197 ? 0.31560 0.26477 0.31847 -0.00762 -0.00559 -0.00336 196 ASP   A C   
1367 O  O   . ASP   A 197 ? 0.31350 0.26006 0.31641 -0.00402 -0.00442 -0.00304 196 ASP   A O   
1368 C  CB  . ASP   A 197 ? 0.33484 0.28114 0.33062 -0.00730 -0.00629 -0.01038 196 ASP   A CB  
1369 C  CG  . ASP   A 197 ? 0.36346 0.31415 0.35567 -0.00645 -0.00607 -0.01304 196 ASP   A CG  
1370 O  OD1 . ASP   A 197 ? 0.40048 0.35784 0.39306 -0.00851 -0.00713 -0.01178 196 ASP   A OD1 
1371 O  OD2 . ASP   A 197 ? 0.42043 0.36806 0.40917 -0.00345 -0.00478 -0.01634 196 ASP   A OD2 
1372 N  N   . ALA   A 198 ? 0.30001 0.24933 0.30478 -0.01165 -0.00676 -0.00128 197 ALA   A N   
1373 C  CA  . ALA   A 198 ? 0.29328 0.23790 0.29927 -0.01237 -0.00660 0.00162  197 ALA   A CA  
1374 C  C   . ALA   A 198 ? 0.37113 0.30360 0.37380 -0.01288 -0.00730 -0.00037 197 ALA   A C   
1375 O  O   . ALA   A 198 ? 0.40894 0.33766 0.40965 -0.01663 -0.00871 -0.00311 197 ALA   A O   
1376 C  CB  . ALA   A 198 ? 0.31498 0.26458 0.32405 -0.01695 -0.00720 0.00461  197 ALA   A CB  
1377 N  N   . VAL   A 199 ? 0.37887 0.30513 0.38080 -0.00902 -0.00641 0.00091  198 VAL   A N   
1378 C  CA  . VAL   A 199 ? 0.35634 0.26935 0.35479 -0.00767 -0.00663 -0.00118 198 VAL   A CA  
1379 C  C   . VAL   A 199 ? 0.38025 0.28525 0.37892 -0.01021 -0.00705 0.00309  198 VAL   A C   
1380 O  O   . VAL   A 199 ? 0.43325 0.34111 0.43372 -0.00798 -0.00639 0.00771  198 VAL   A O   
1381 C  CB  . VAL   A 199 ? 0.39956 0.31123 0.39706 -0.00029 -0.00519 -0.00265 198 VAL   A CB  
1382 C  CG1 . VAL   A 199 ? 0.47409 0.37081 0.46813 0.00214  -0.00517 -0.00443 198 VAL   A CG1 
1383 C  CG2 . VAL   A 199 ? 0.40776 0.32688 0.40445 0.00153  -0.00443 -0.00674 198 VAL   A CG2 
1384 N  N   . GLU   A 200 ? 0.43557 0.33030 0.43194 -0.01509 -0.00815 0.00155  199 GLU   A N   
1385 C  CA  . GLU   A 200 ? 0.50602 0.39049 0.50182 -0.01844 -0.00842 0.00565  199 GLU   A CA  
1386 C  C   . GLU   A 200 ? 0.49563 0.38970 0.49511 -0.02152 -0.00810 0.01176  199 GLU   A C   
1387 O  O   . GLU   A 200 ? 0.47912 0.36924 0.47839 -0.02049 -0.00750 0.01699  199 GLU   A O   
1388 C  CB  . GLU   A 200 ? 0.60829 0.48014 0.60147 -0.01217 -0.00760 0.00694  199 GLU   A CB  
1389 C  CG  . GLU   A 200 ? 0.63624 0.49705 0.62541 -0.00849 -0.00742 0.00067  199 GLU   A CG  
1390 C  CD  . GLU   A 200 ? 0.80840 0.66321 0.79665 0.00069  -0.00618 0.00186  199 GLU   A CD  
1391 O  OE1 . GLU   A 200 ? 0.76356 0.62482 0.75445 0.00409  -0.00579 0.00751  199 GLU   A OE1 
1392 O  OE2 . GLU   A 200 ? 0.75598 0.60017 0.74080 0.00472  -0.00560 -0.00298 199 GLU   A OE2 
1393 N  N   . GLY   A 201 ? 0.39687 0.30377 0.39942 -0.02508 -0.00842 0.01120  200 GLY   A N   
1394 C  CA  . GLY   A 201 ? 0.36487 0.28143 0.37081 -0.02821 -0.00783 0.01607  200 GLY   A CA  
1395 C  C   . GLY   A 201 ? 0.35754 0.28873 0.36640 -0.02515 -0.00703 0.01581  200 GLY   A C   
1396 O  O   . GLY   A 201 ? 0.32311 0.25681 0.33145 -0.02113 -0.00700 0.01231  200 GLY   A O   
1397 N  N   . PRO   A 202 ? 0.33494 0.27547 0.34658 -0.02705 -0.00611 0.01952  201 PRO   A N   
1398 C  CA  . PRO   A 202 ? 0.28668 0.23967 0.30079 -0.02425 -0.00513 0.01899  201 PRO   A CA  
1399 C  C   . PRO   A 202 ? 0.29481 0.24785 0.30750 -0.01811 -0.00435 0.01865  201 PRO   A C   
1400 O  O   . PRO   A 202 ? 0.33335 0.27995 0.34393 -0.01567 -0.00434 0.02055  201 PRO   A O   
1401 C  CB  . PRO   A 202 ? 0.31125 0.27227 0.32776 -0.02739 -0.00394 0.02310  201 PRO   A CB  
1402 C  CG  . PRO   A 202 ? 0.33891 0.29351 0.35514 -0.03355 -0.00459 0.02550  201 PRO   A CG  
1403 C  CD  . PRO   A 202 ? 0.37729 0.31694 0.38953 -0.03182 -0.00560 0.02443  201 PRO   A CD  
1404 N  N   . ALA   A 203 ? 0.24893 0.20983 0.26302 -0.01567 -0.00373 0.01650  202 ALA   A N   
1405 C  CA  . ALA   A 203 ? 0.24707 0.20988 0.26044 -0.01094 -0.00299 0.01593  202 ALA   A CA  
1406 C  C   . ALA   A 203 ? 0.25876 0.23105 0.27406 -0.01041 -0.00183 0.01519  202 ALA   A C   
1407 O  O   . ALA   A 203 ? 0.26753 0.24400 0.28467 -0.01240 -0.00169 0.01460  202 ALA   A O   
1408 C  CB  . ALA   A 203 ? 0.29772 0.25575 0.30961 -0.00793 -0.00342 0.01254  202 ALA   A CB  
1409 N  N   . ALA   A 204 ? 0.21559 0.19135 0.23052 -0.00767 -0.00107 0.01515  203 ALA   A N   
1410 C  CA  . ALA   A 204 ? 0.23391 0.21653 0.25005 -0.00723 0.00017  0.01365  203 ALA   A CA  
1411 C  C   . ALA   A 204 ? 0.26969 0.25370 0.28526 -0.00461 0.00050  0.01183  203 ALA   A C   
1412 O  O   . ALA   A 204 ? 0.26329 0.24610 0.27795 -0.00286 -0.00013 0.01272  203 ALA   A O   
1413 C  CB  . ALA   A 204 ? 0.25637 0.24464 0.27282 -0.00855 0.00122  0.01567  203 ALA   A CB  
1414 N  N   . PHE   A 205 ? 0.24583 0.23258 0.26214 -0.00437 0.00149  0.00952  204 PHE   A N   
1415 C  CA  . PHE   A 205 ? 0.22835 0.21714 0.24447 -0.00309 0.00194  0.00774  204 PHE   A CA  
1416 C  C   . PHE   A 205 ? 0.24625 0.23817 0.26261 -0.00386 0.00337  0.00595  204 PHE   A C   
1417 O  O   . PHE   A 205 ? 0.21447 0.20573 0.23143 -0.00424 0.00416  0.00558  204 PHE   A O   
1418 C  CB  . PHE   A 205 ? 0.20719 0.19329 0.22332 -0.00201 0.00183  0.00621  204 PHE   A CB  
1419 C  CG  . PHE   A 205 ? 0.23186 0.21594 0.24795 -0.00274 0.00223  0.00531  204 PHE   A CG  
1420 C  CD1 . PHE   A 205 ? 0.26352 0.24451 0.27915 -0.00331 0.00119  0.00582  204 PHE   A CD1 
1421 C  CD2 . PHE   A 205 ? 0.25231 0.23747 0.26857 -0.00302 0.00349  0.00409  204 PHE   A CD2 
1422 C  CE1 . PHE   A 205 ? 0.23723 0.21789 0.25260 -0.00375 0.00112  0.00529  204 PHE   A CE1 
1423 C  CE2 . PHE   A 205 ? 0.24617 0.22956 0.26201 -0.00309 0.00368  0.00412  204 PHE   A CE2 
1424 C  CZ  . PHE   A 205 ? 0.25618 0.23816 0.27160 -0.00326 0.00234  0.00481  204 PHE   A CZ  
1425 N  N   . LEU   A 206 ? 0.21331 0.20869 0.22924 -0.00393 0.00361  0.00470  205 LEU   A N   
1426 C  CA  A LEU   A 206 ? 0.22517 0.22179 0.24084 -0.00507 0.00500  0.00202  205 LEU   A CA  
1427 C  CA  B LEU   A 206 ? 0.22490 0.22143 0.24057 -0.00506 0.00502  0.00203  205 LEU   A CA  
1428 C  C   . LEU   A 206 ? 0.22264 0.21625 0.23899 -0.00538 0.00566  0.00072  205 LEU   A C   
1429 O  O   . LEU   A 206 ? 0.25182 0.24607 0.26878 -0.00490 0.00507  0.00098  205 LEU   A O   
1430 C  CB  A LEU   A 206 ? 0.23037 0.23249 0.24508 -0.00589 0.00461  0.00086  205 LEU   A CB  
1431 C  CB  B LEU   A 206 ? 0.23071 0.23262 0.24538 -0.00597 0.00475  0.00071  205 LEU   A CB  
1432 C  CG  A LEU   A 206 ? 0.24868 0.25297 0.26212 -0.00790 0.00568  -0.00262 205 LEU   A CG  
1433 C  CG  B LEU   A 206 ? 0.22337 0.22535 0.23706 -0.00785 0.00624  -0.00288 205 LEU   A CG  
1434 C  CD1 A LEU   A 206 ? 0.24011 0.24126 0.25448 -0.00952 0.00668  -0.00495 205 LEU   A CD1 
1435 C  CD1 B LEU   A 206 ? 0.26165 0.26420 0.27370 -0.00758 0.00736  -0.00348 205 LEU   A CD1 
1436 C  CD2 A LEU   A 206 ? 0.25460 0.25814 0.26645 -0.00780 0.00712  -0.00359 205 LEU   A CD2 
1437 C  CD2 B LEU   A 206 ? 0.27228 0.27972 0.28560 -0.00976 0.00552  -0.00498 205 LEU   A CD2 
1438 N  N   . ASP   A 207 ? 0.20951 0.19987 0.22561 -0.00587 0.00708  -0.00044 206 ASP   A N   
1439 C  CA  . ASP   A 207 ? 0.21654 0.20358 0.23266 -0.00648 0.00793  -0.00089 206 ASP   A CA  
1440 C  C   . ASP   A 207 ? 0.26400 0.24847 0.27936 -0.00825 0.00961  -0.00317 206 ASP   A C   
1441 O  O   . ASP   A 207 ? 0.25673 0.23945 0.27142 -0.00768 0.01047  -0.00425 206 ASP   A O   
1442 C  CB  . ASP   A 207 ? 0.26178 0.24521 0.27779 -0.00499 0.00784  0.00093  206 ASP   A CB  
1443 C  CG  . ASP   A 207 ? 0.39592 0.37785 0.41125 -0.00533 0.00810  0.00145  206 ASP   A CG  
1444 O  OD1 . ASP   A 207 ? 0.33663 0.32008 0.35213 -0.00695 0.00886  0.00039  206 ASP   A OD1 
1445 O  OD2 . ASP   A 207 ? 0.25376 0.23410 0.26835 -0.00422 0.00755  0.00290  206 ASP   A OD2 
1446 N  N   . ILE   A 208 ? 0.22587 0.21026 0.24136 -0.01054 0.01023  -0.00410 207 ILE   A N   
1447 C  CA  . ILE   A 208 ? 0.22912 0.20911 0.24366 -0.01325 0.01196  -0.00621 207 ILE   A CA  
1448 C  C   . ILE   A 208 ? 0.29125 0.26630 0.30537 -0.01372 0.01311  -0.00426 207 ILE   A C   
1449 O  O   . ILE   A 208 ? 0.27802 0.25663 0.29290 -0.01411 0.01279  -0.00293 207 ILE   A O   
1450 C  CB  . ILE   A 208 ? 0.23079 0.21614 0.24590 -0.01694 0.01172  -0.00892 207 ILE   A CB  
1451 C  CG1 . ILE   A 208 ? 0.29047 0.28141 0.30507 -0.01628 0.01040  -0.01042 207 ILE   A CG1 
1452 C  CG2 . ILE   A 208 ? 0.27760 0.25698 0.29154 -0.02092 0.01358  -0.01141 207 ILE   A CG2 
1453 C  CD1 . ILE   A 208 ? 0.31086 0.30973 0.32616 -0.01941 0.00937  -0.01260 207 ILE   A CD1 
1454 N  N   . LEU   A 209 ? 0.24678 0.21373 0.25941 -0.01321 0.01458  -0.00385 208 LEU   A N   
1455 C  CA  . LEU   A 209 ? 0.24313 0.20462 0.25457 -0.01385 0.01582  -0.00131 208 LEU   A CA  
1456 C  C   . LEU   A 209 ? 0.29277 0.24699 0.30295 -0.01760 0.01789  -0.00302 208 LEU   A C   
1457 O  O   . LEU   A 209 ? 0.31650 0.26597 0.32587 -0.01742 0.01858  -0.00572 208 LEU   A O   
1458 C  CB  . LEU   A 209 ? 0.28663 0.24387 0.29711 -0.00959 0.01563  0.00173  208 LEU   A CB  
1459 C  CG  . LEU   A 209 ? 0.34803 0.31135 0.35951 -0.00662 0.01351  0.00322  208 LEU   A CG  
1460 C  CD1 . LEU   A 209 ? 0.39623 0.35678 0.40740 -0.00282 0.01317  0.00573  208 LEU   A CD1 
1461 C  CD2 . LEU   A 209 ? 0.33862 0.30548 0.34949 -0.00773 0.01304  0.00455  208 LEU   A CD2 
1462 N  N   . ALA   A 210 ? 0.27130 0.22432 0.28106 -0.02120 0.01909  -0.00162 209 ALA   A N   
1463 C  CA  . ALA   A 210 ? 0.28153 0.22681 0.29008 -0.02598 0.02111  -0.00331 209 ALA   A CA  
1464 C  C   . ALA   A 210 ? 0.32001 0.25961 0.32691 -0.02834 0.02300  0.00062  209 ALA   A C   
1465 O  O   . ALA   A 210 ? 0.34575 0.29268 0.35372 -0.03080 0.02319  0.00213  209 ALA   A O   
1466 C  CB  . ALA   A 210 ? 0.34047 0.29333 0.35100 -0.03119 0.02066  -0.00733 209 ALA   A CB  
1467 N  N   . PRO   A 211 ? 0.32894 0.25564 0.33304 -0.02734 0.02461  0.00264  210 PRO   A N   
1468 C  CA  . PRO   A 211 ? 0.35629 0.27419 0.35915 -0.02295 0.02479  0.00139  210 PRO   A CA  
1469 C  C   . PRO   A 211 ? 0.33375 0.25718 0.33754 -0.01603 0.02285  0.00355  210 PRO   A C   
1470 O  O   . PRO   A 211 ? 0.38618 0.31732 0.39056 -0.01502 0.02154  0.00631  210 PRO   A O   
1471 C  CB  . PRO   A 211 ? 0.36499 0.26796 0.36464 -0.02373 0.02720  0.00458  210 PRO   A CB  
1472 C  CG  . PRO   A 211 ? 0.42129 0.32777 0.42014 -0.02573 0.02754  0.00976  210 PRO   A CG  
1473 C  CD  . PRO   A 211 ? 0.39481 0.31502 0.39659 -0.03003 0.02662  0.00718  210 PRO   A CD  
1474 N  N   . PRO   A 212 ? 0.37376 0.29408 0.37774 -0.01148 0.02273  0.00205  211 PRO   A N   
1475 C  CA  . PRO   A 212 ? 0.32045 0.24619 0.32573 -0.00546 0.02103  0.00461  211 PRO   A CA  
1476 C  C   . PRO   A 212 ? 0.40277 0.32390 0.40629 -0.00260 0.02114  0.01032  211 PRO   A C   
1477 O  O   . PRO   A 212 ? 0.39255 0.30457 0.39353 -0.00470 0.02290  0.01255  211 PRO   A O   
1478 C  CB  . PRO   A 212 ? 0.37332 0.29621 0.37925 -0.00163 0.02171  0.00162  211 PRO   A CB  
1479 C  CG  . PRO   A 212 ? 0.42739 0.34609 0.43214 -0.00626 0.02317  -0.00379 211 PRO   A CG  
1480 C  CD  . PRO   A 212 ? 0.37287 0.28576 0.37596 -0.01185 0.02423  -0.00262 211 PRO   A CD  
1481 N  N   . TYR   A 213 ? 0.35970 0.28760 0.36439 0.00182  0.01913  0.01292  212 TYR   A N   
1482 C  CA  . TYR   A 213 ? 0.37191 0.29694 0.37470 0.00520  0.01876  0.01849  212 TYR   A CA  
1483 C  C   . TYR   A 213 ? 0.44389 0.35742 0.44577 0.00923  0.02056  0.01983  212 TYR   A C   
1484 O  O   . TYR   A 213 ? 0.40671 0.31705 0.41006 0.01080  0.02167  0.01598  212 TYR   A O   
1485 C  CB  . TYR   A 213 ? 0.34920 0.28463 0.35373 0.00894  0.01591  0.02030  212 TYR   A CB  
1486 C  CG  . TYR   A 213 ? 0.33245 0.27724 0.33686 0.00592  0.01406  0.01969  212 TYR   A CG  
1487 C  CD1 . TYR   A 213 ? 0.34308 0.28888 0.34422 0.00447  0.01378  0.02280  212 TYR   A CD1 
1488 C  CD2 . TYR   A 213 ? 0.32988 0.28216 0.33706 0.00493  0.01273  0.01615  212 TYR   A CD2 
1489 C  CE1 . TYR   A 213 ? 0.32225 0.27610 0.32294 0.00240  0.01235  0.02152  212 TYR   A CE1 
1490 C  CE2 . TYR   A 213 ? 0.29686 0.25591 0.30371 0.00285  0.01118  0.01544  212 TYR   A CE2 
1491 C  CZ  . TYR   A 213 ? 0.28337 0.24303 0.28703 0.00181  0.01104  0.01775  212 TYR   A CZ  
1492 O  OH  . TYR   A 213 ? 0.30256 0.26837 0.30564 0.00035  0.00974  0.01626  212 TYR   A OH  
1493 N  N   . ASP   A 214 ? 0.40965 0.31666 0.40866 0.01123  0.02100  0.02542  213 ASP   A N   
1494 C  CA  . ASP   A 214 ? 0.48647 0.38131 0.48432 0.01631  0.02265  0.02784  213 ASP   A CA  
1495 C  C   . ASP   A 214 ? 0.47922 0.37406 0.47475 0.02043  0.02141  0.03541  213 ASP   A C   
1496 O  O   . ASP   A 214 ? 0.54350 0.43014 0.53487 0.01815  0.02269  0.03978  213 ASP   A O   
1497 C  CB  . ASP   A 214 ? 0.52654 0.40610 0.52165 0.01194  0.02587  0.02595  213 ASP   A CB  
1498 C  CG  . ASP   A 214 ? 0.64961 0.51479 0.64376 0.01772  0.02791  0.02654  213 ASP   A CG  
1499 O  OD1 . ASP   A 214 ? 0.57963 0.44676 0.57500 0.02570  0.02687  0.03026  213 ASP   A OD1 
1500 O  OD2 . ASP   A 214 ? 0.73524 0.58712 0.72740 0.01434  0.03057  0.02320  213 ASP   A OD2 
1501 N  N   . PRO   A 215 ? 0.45515 0.36032 0.45318 0.02610  0.01878  0.03738  214 PRO   A N   
1502 C  CA  . PRO   A 215 ? 0.50578 0.41348 0.50138 0.03002  0.01694  0.04465  214 PRO   A CA  
1503 C  C   . PRO   A 215 ? 0.58172 0.47437 0.57384 0.03395  0.01893  0.05027  214 PRO   A C   
1504 O  O   . PRO   A 215 ? 0.60694 0.49727 0.59450 0.03344  0.01862  0.05651  214 PRO   A O   
1505 C  CB  . PRO   A 215 ? 0.54867 0.46963 0.54894 0.03569  0.01401  0.04451  214 PRO   A CB  
1506 C  CG  . PRO   A 215 ? 0.48418 0.41273 0.48823 0.03179  0.01380  0.03752  214 PRO   A CG  
1507 C  CD  . PRO   A 215 ? 0.44661 0.36357 0.44966 0.02803  0.01712  0.03317  214 PRO   A CD  
1508 N  N   . ASP   A 216 ? 0.52942 0.41112 0.52307 0.03791  0.02118  0.04826  215 ASP   A N   
1509 C  CA  . ASP   A 216 ? 0.67133 0.53636 0.66154 0.04237  0.02326  0.05365  215 ASP   A CA  
1510 C  C   . ASP   A 216 ? 0.71741 0.56764 0.70248 0.03488  0.02616  0.05453  215 ASP   A C   
1511 O  O   . ASP   A 216 ? 0.79712 0.63304 0.77806 0.03708  0.02776  0.06063  215 ASP   A O   
1512 C  CB  . ASP   A 216 ? 0.67847 0.53545 0.67167 0.04924  0.02513  0.05036  215 ASP   A CB  
1513 C  CG  . ASP   A 216 ? 0.72460 0.59632 0.72317 0.05762  0.02260  0.05118  215 ASP   A CG  
1514 O  OD1 . ASP   A 216 ? 0.77578 0.65839 0.77437 0.06026  0.01944  0.05710  215 ASP   A OD1 
1515 O  OD2 . ASP   A 216 ? 0.83580 0.70924 0.83848 0.06119  0.02377  0.04583  215 ASP   A OD2 
1516 N  N   . ASP   A 217 ? 0.62918 0.48281 0.61462 0.02612  0.02688  0.04894  216 ASP   A N   
1517 C  CA  . ASP   A 217 ? 0.64324 0.48719 0.62479 0.01765  0.02936  0.04956  216 ASP   A CA  
1518 C  C   . ASP   A 217 ? 0.65032 0.50513 0.62939 0.01364  0.02798  0.05405  216 ASP   A C   
1519 O  O   . ASP   A 217 ? 0.77524 0.62527 0.75117 0.00659  0.03001  0.05573  216 ASP   A O   
1520 C  CB  . ASP   A 217 ? 0.71067 0.55416 0.69464 0.01089  0.03077  0.04057  216 ASP   A CB  
1521 C  CG  . ASP   A 217 ? 0.94704 0.78101 0.92812 0.00118  0.03349  0.03995  216 ASP   A CG  
1522 O  OD1 . ASP   A 217 ? 1.01729 0.85099 0.99523 -0.00283 0.03413  0.04549  216 ASP   A OD1 
1523 O  OD2 . ASP   A 217 ? 1.05781 0.88553 1.03990 -0.00305 0.03506  0.03329  216 ASP   A OD2 
1524 N  N   . GLY   A 218 ? 0.63141 0.50096 0.61161 0.01792  0.02470  0.05600  217 GLY   A N   
1525 C  CA  . GLY   A 218 ? 0.65185 0.53195 0.62901 0.01472  0.02340  0.05944  217 GLY   A CA  
1526 C  C   . GLY   A 218 ? 0.63666 0.52940 0.61623 0.00887  0.02270  0.05327  217 GLY   A C   
1527 O  O   . GLY   A 218 ? 0.57618 0.47530 0.55281 0.00480  0.02285  0.05503  217 GLY   A O   
1528 N  N   . ARG   A 219 ? 0.58974 0.48627 0.57429 0.00870  0.02214  0.04629  218 ARG   A N   
1529 C  CA  . ARG   A 219 ? 0.46938 0.37746 0.45669 0.00438  0.02120  0.04051  218 ARG   A CA  
1530 C  C   . ARG   A 219 ? 0.41541 0.33453 0.40611 0.00904  0.01797  0.03843  218 ARG   A C   
1531 O  O   . ARG   A 219 ? 0.46763 0.38660 0.46213 0.01120  0.01774  0.03464  218 ARG   A O   
1532 C  CB  . ARG   A 219 ? 0.56341 0.46676 0.55332 -0.00039 0.02321  0.03448  218 ARG   A CB  
1533 C  CG  . ARG   A 219 ? 0.53602 0.44697 0.52663 -0.00700 0.02374  0.03140  218 ARG   A CG  
1534 C  CD  . ARG   A 219 ? 0.42776 0.33389 0.42032 -0.01236 0.02566  0.02640  218 ARG   A CD  
1535 N  NE  . ARG   A 219 ? 0.42850 0.32903 0.42302 -0.00947 0.02556  0.02256  218 ARG   A NE  
1536 C  CZ  . ARG   A 219 ? 0.57767 0.46439 0.57080 -0.01005 0.02771  0.02189  218 ARG   A CZ  
1537 N  NH1 . ARG   A 219 ? 0.58584 0.46145 0.57559 -0.01318 0.02996  0.02579  218 ARG   A NH1 
1538 N  NH2 . ARG   A 219 ? 0.49103 0.37449 0.48581 -0.00749 0.02779  0.01721  218 ARG   A NH2 
1539 N  N   . ASP   A 220 ? 0.45367 0.38262 0.44271 0.01011  0.01558  0.04072  219 ASP   A N   
1540 C  CA  . ASP   A 220 ? 0.34720 0.28664 0.33923 0.01359  0.01233  0.03913  219 ASP   A CA  
1541 C  C   . ASP   A 220 ? 0.36026 0.30977 0.35247 0.00997  0.01085  0.03542  219 ASP   A C   
1542 O  O   . ASP   A 220 ? 0.39630 0.34614 0.38618 0.00577  0.01224  0.03454  219 ASP   A O   
1543 C  CB  . ASP   A 220 ? 0.40811 0.35075 0.39820 0.01893  0.01003  0.04493  219 ASP   A CB  
1544 C  CG  . ASP   A 220 ? 0.51589 0.46416 0.51098 0.02411  0.00791  0.04408  219 ASP   A CG  
1545 O  OD1 . ASP   A 220 ? 0.39974 0.35463 0.39883 0.02250  0.00698  0.03905  219 ASP   A OD1 
1546 O  OD2 . ASP   A 220 ? 0.46591 0.41251 0.46108 0.02990  0.00725  0.04877  219 ASP   A OD2 
1547 N  N   . CYS   A 221 ? 0.32675 0.28456 0.32189 0.01181  0.00812  0.03333  220 CYS   A N   
1548 C  CA  . CYS   A 221 ? 0.32702 0.29280 0.32250 0.00902  0.00650  0.02953  220 CYS   A CA  
1549 C  C   . CYS   A 221 ? 0.37214 0.34481 0.36397 0.01004  0.00385  0.03192  220 CYS   A C   
1550 O  O   . CYS   A 221 ? 0.38912 0.36575 0.38185 0.01347  0.00154  0.03447  220 CYS   A O   
1551 C  CB  . CYS   A 221 ? 0.32919 0.29883 0.32989 0.00944  0.00530  0.02571  220 CYS   A CB  
1552 S  SG  . CYS   A 221 ? 0.34926 0.32632 0.35044 0.00637  0.00320  0.02141  220 CYS   A SG  
1553 N  N   . HIS   A 222 ? 0.37031 0.34524 0.35796 0.00723  0.00421  0.03100  221 HIS   A N   
1554 C  CA  . HIS   A 222 ? 0.35546 0.33723 0.33839 0.00755  0.00182  0.03220  221 HIS   A CA  
1555 C  C   . HIS   A 222 ? 0.31401 0.30095 0.29723 0.00517  0.00035  0.02657  221 HIS   A C   
1556 O  O   . HIS   A 222 ? 0.35909 0.34396 0.34349 0.00297  0.00225  0.02299  221 HIS   A O   
1557 C  CB  . HIS   A 222 ? 0.37200 0.35212 0.34853 0.00653  0.00383  0.03577  221 HIS   A CB  
1558 C  CG  . HIS   A 222 ? 0.43997 0.41183 0.41593 0.00787  0.00611  0.04122  221 HIS   A CG  
1559 N  ND1 . HIS   A 222 ? 0.51390 0.48505 0.48696 0.01152  0.00487  0.04747  221 HIS   A ND1 
1560 C  CD2 . HIS   A 222 ? 0.40488 0.36819 0.38283 0.00606  0.00941  0.04128  221 HIS   A CD2 
1561 C  CE1 . HIS   A 222 ? 0.52421 0.48516 0.49722 0.01211  0.00760  0.05132  221 HIS   A CE1 
1562 N  NE2 . HIS   A 222 ? 0.47483 0.43079 0.45071 0.00839  0.01038  0.04734  221 HIS   A NE2 
1563 N  N   . TYR   A 223 ? 0.30067 0.29423 0.28298 0.00563  -0.00313 0.02579  222 TYR   A N   
1564 C  CA  . TYR   A 223 ? 0.30738 0.30435 0.28918 0.00318  -0.00478 0.02040  222 TYR   A CA  
1565 C  C   . TYR   A 223 ? 0.30173 0.30216 0.27602 0.00215  -0.00522 0.01941  222 TYR   A C   
1566 O  O   . TYR   A 223 ? 0.37669 0.37978 0.34629 0.00345  -0.00563 0.02360  222 TYR   A O   
1567 C  CB  . TYR   A 223 ? 0.30889 0.31114 0.29438 0.00314  -0.00838 0.01942  222 TYR   A CB  
1568 C  CG  . TYR   A 223 ? 0.29408 0.29381 0.28673 0.00390  -0.00747 0.01945  222 TYR   A CG  
1569 C  CD1 . TYR   A 223 ? 0.32222 0.31907 0.31785 0.00174  -0.00662 0.01548  222 TYR   A CD1 
1570 C  CD2 . TYR   A 223 ? 0.33251 0.33248 0.32837 0.00723  -0.00723 0.02356  222 TYR   A CD2 
1571 C  CE1 . TYR   A 223 ? 0.29652 0.29185 0.29780 0.00232  -0.00564 0.01558  222 TYR   A CE1 
1572 C  CE2 . TYR   A 223 ? 0.33321 0.33118 0.33502 0.00812  -0.00596 0.02297  222 TYR   A CE2 
1573 C  CZ  . TYR   A 223 ? 0.28222 0.27838 0.28640 0.00539  -0.00521 0.01899  222 TYR   A CZ  
1574 O  OH  . TYR   A 223 ? 0.29168 0.28675 0.30089 0.00611  -0.00389 0.01843  222 TYR   A OH  
1575 N  N   . TYR   A 224 ? 0.32624 0.32644 0.29903 0.00015  -0.00503 0.01391  223 TYR   A N   
1576 C  CA  . TYR   A 224 ? 0.37006 0.37319 0.33533 -0.00060 -0.00475 0.01174  223 TYR   A CA  
1577 C  C   . TYR   A 224 ? 0.37413 0.37809 0.33787 -0.00243 -0.00700 0.00536  223 TYR   A C   
1578 O  O   . TYR   A 224 ? 0.36210 0.36242 0.33078 -0.00339 -0.00751 0.00240  223 TYR   A O   
1579 C  CB  . TYR   A 224 ? 0.36841 0.36899 0.33204 -0.00064 -0.00040 0.01121  223 TYR   A CB  
1580 C  CG  . TYR   A 224 ? 0.34140 0.33998 0.30576 -0.00001 0.00216  0.01714  223 TYR   A CG  
1581 C  CD1 . TYR   A 224 ? 0.37103 0.36448 0.34188 0.00006  0.00357  0.01847  223 TYR   A CD1 
1582 C  CD2 . TYR   A 224 ? 0.38860 0.38986 0.34656 0.00023  0.00323  0.02144  223 TYR   A CD2 
1583 C  CE1 . TYR   A 224 ? 0.38271 0.37258 0.35390 0.00009  0.00596  0.02339  223 TYR   A CE1 
1584 C  CE2 . TYR   A 224 ? 0.43393 0.43148 0.39231 0.00031  0.00576  0.02727  223 TYR   A CE2 
1585 C  CZ  . TYR   A 224 ? 0.40181 0.39307 0.36694 0.00010  0.00711  0.02790  223 TYR   A CZ  
1586 O  OH  . TYR   A 224 ? 0.44112 0.42691 0.40655 -0.00035 0.00964  0.03303  223 TYR   A OH  
1587 N  N   . ARG   A 225 ? 0.35448 0.36271 0.31065 -0.00309 -0.00819 0.00325  224 ARG   A N   
1588 C  CA  . ARG   A 225 ? 0.36218 0.36949 0.31477 -0.00491 -0.00944 -0.00386 224 ARG   A CA  
1589 C  C   . ARG   A 225 ? 0.41691 0.42290 0.36438 -0.00377 -0.00567 -0.00700 224 ARG   A C   
1590 O  O   . ARG   A 225 ? 0.43525 0.44502 0.37859 -0.00267 -0.00347 -0.00359 224 ARG   A O   
1591 C  CB  . ARG   A 225 ? 0.41367 0.42774 0.36060 -0.00676 -0.01371 -0.00516 224 ARG   A CB  
1592 C  CG  . ARG   A 225 ? 0.56884 0.58644 0.52123 -0.00838 -0.01791 -0.00340 224 ARG   A CG  
1593 C  CD  . ARG   A 225 ? 0.59411 0.62154 0.54121 -0.00978 -0.02232 -0.00294 224 ARG   A CD  
1594 N  NE  . ARG   A 225 ? 0.57921 0.60748 0.51748 -0.01209 -0.02323 -0.00957 224 ARG   A NE  
1595 C  CZ  . ARG   A 225 ? 0.67333 0.71054 0.60425 -0.01322 -0.02645 -0.00993 224 ARG   A CZ  
1596 N  NH1 . ARG   A 225 ? 0.58049 0.62711 0.51226 -0.01196 -0.02939 -0.00350 224 ARG   A NH1 
1597 N  NH2 . ARG   A 225 ? 0.68380 0.72070 0.60608 -0.01534 -0.02679 -0.01701 224 ARG   A NH2 
1598 N  N   . VAL   A 226 ? 0.42536 0.42611 0.37324 -0.00380 -0.00468 -0.01312 225 VAL   A N   
1599 C  CA  A VAL   A 226 ? 0.47368 0.47442 0.41633 -0.00212 -0.00132 -0.01726 225 VAL   A CA  
1600 C  CA  B VAL   A 226 ? 0.47421 0.47478 0.41693 -0.00211 -0.00132 -0.01740 225 VAL   A CA  
1601 C  C   . VAL   A 226 ? 0.49556 0.49710 0.42998 -0.00342 -0.00347 -0.02359 225 VAL   A C   
1602 O  O   . VAL   A 226 ? 0.49085 0.48807 0.42600 -0.00565 -0.00665 -0.02751 225 VAL   A O   
1603 C  CB  A VAL   A 226 ? 0.54949 0.54421 0.49760 -0.00015 0.00148  -0.01989 225 VAL   A CB  
1604 C  CB  B VAL   A 226 ? 0.54879 0.54296 0.49687 -0.00024 0.00123  -0.02039 225 VAL   A CB  
1605 C  CG1 A VAL   A 226 ? 0.61610 0.60374 0.56950 -0.00142 -0.00116 -0.02173 225 VAL   A CG1 
1606 C  CG1 B VAL   A 226 ? 0.52370 0.51868 0.47842 0.00071  0.00364  -0.01504 225 VAL   A CG1 
1607 C  CG2 A VAL   A 226 ? 0.52580 0.52035 0.46840 0.00216  0.00431  -0.02591 225 VAL   A CG2 
1608 C  CG2 B VAL   A 226 ? 0.61294 0.59975 0.56465 -0.00169 -0.00163 -0.02356 225 VAL   A CG2 
1609 N  N   . LEU   A 227 ? 0.51019 0.51745 0.43641 -0.00253 -0.00169 -0.02463 226 LEU   A N   
1610 C  CA  . LEU   A 227 ? 0.53952 0.54947 0.45641 -0.00415 -0.00408 -0.03018 226 LEU   A CA  
1611 C  C   . LEU   A 227 ? 0.62121 0.62687 0.53298 -0.00232 -0.00133 -0.03876 226 LEU   A C   
1612 O  O   . LEU   A 227 ? 0.55882 0.56552 0.47073 0.00097  0.00339  -0.03892 226 LEU   A O   
1613 C  CB  . LEU   A 227 ? 0.49327 0.51344 0.40282 -0.00435 -0.00439 -0.02556 226 LEU   A CB  
1614 C  CG  . LEU   A 227 ? 0.48898 0.51275 0.40320 -0.00522 -0.00730 -0.01706 226 LEU   A CG  
1615 C  CD1 . LEU   A 227 ? 0.52112 0.55421 0.42729 -0.00485 -0.00756 -0.01195 226 LEU   A CD1 
1616 C  CD2 . LEU   A 227 ? 0.53705 0.55981 0.45468 -0.00802 -0.01260 -0.01894 226 LEU   A CD2 
1617 N  N   . GLU   A 228 ? 0.57221 0.57327 0.47948 -0.00455 -0.00428 -0.04609 227 GLU   A N   
1618 C  CA  . GLU   A 228 ? 0.67589 0.67064 0.57776 -0.00253 -0.00192 -0.05520 227 GLU   A CA  
1619 C  C   . GLU   A 228 ? 0.57645 0.57830 0.46585 -0.00304 -0.00188 -0.05987 227 GLU   A C   
1620 O  O   . GLU   A 228 ? 0.60293 0.60705 0.48689 -0.00722 -0.00644 -0.06239 227 GLU   A O   
1621 C  CB  . GLU   A 228 ? 0.70049 0.68305 0.60472 -0.00492 -0.00476 -0.06100 227 GLU   A CB  
1622 C  CG  . GLU   A 228 ? 0.66594 0.64287 0.58169 -0.00589 -0.00609 -0.05569 227 GLU   A CG  
1623 C  CD  . GLU   A 228 ? 0.63518 0.61007 0.55842 -0.00111 -0.00183 -0.05182 227 GLU   A CD  
1624 O  OE1 . GLU   A 228 ? 0.63081 0.61149 0.55232 0.00260  0.00217  -0.05086 227 GLU   A OE1 
1625 O  OE2 . GLU   A 228 ? 0.63850 0.60678 0.56957 -0.00142 -0.00257 -0.04960 227 GLU   A OE2 
1626 N  N   . PRO   A 229 ? 0.61496 0.62168 0.49945 0.00083  0.00307  -0.06121 228 PRO   A N   
1627 C  CA  . PRO   A 229 ? 0.61227 0.62669 0.48381 0.00051  0.00355  -0.06581 228 PRO   A CA  
1628 C  C   . PRO   A 229 ? 0.77879 0.78503 0.64282 -0.00033 0.00221  -0.07770 228 PRO   A C   
1629 O  O   . PRO   A 229 ? 0.77664 0.77007 0.64533 0.00012  0.00184  -0.08251 228 PRO   A O   
1630 C  CB  . PRO   A 229 ? 0.66072 0.68182 0.53097 0.00519  0.01014  -0.06413 228 PRO   A CB  
1631 C  CG  . PRO   A 229 ? 0.70001 0.71976 0.58270 0.00655  0.01195  -0.05612 228 PRO   A CG  
1632 C  CD  . PRO   A 229 ? 0.64808 0.65594 0.53888 0.00527  0.00845  -0.05761 228 PRO   A CD  
1633 N  N   . VAL   A 230 ? 0.76863 0.78211 0.62018 -0.00173 0.00145  -0.08240 229 VAL   A N   
1634 C  CA  . VAL   A 230 ? 0.83427 0.84076 0.67622 -0.00246 0.00085  -0.09490 229 VAL   A CA  
1635 C  C   . VAL   A 230 ? 0.79720 0.81338 0.62644 0.00032  0.00479  -0.09940 229 VAL   A C   
1636 O  O   . VAL   A 230 ? 0.94458 0.97111 0.77413 0.00348  0.00903  -0.09295 229 VAL   A O   
1637 C  CB  . VAL   A 230 ? 0.81721 0.82188 0.65575 -0.00960 -0.00633 -0.09828 229 VAL   A CB  
1638 C  CG1 . VAL   A 230 ? 0.81937 0.81291 0.66972 -0.01234 -0.00942 -0.09597 229 VAL   A CG1 
1639 C  CG2 . VAL   A 230 ? 0.76415 0.78469 0.59856 -0.01284 -0.01004 -0.09115 229 VAL   A CG2 
1640 N  N   . ASP   A 241 ? 0.89098 0.87737 0.84565 0.05247  0.03283  -0.06244 240 ASP   A N   
1641 C  CA  . ASP   A 241 ? 0.97195 0.97218 0.93510 0.05659  0.03611  -0.05896 240 ASP   A CA  
1642 C  C   . ASP   A 241 ? 0.88223 0.89448 0.84951 0.04982  0.03579  -0.05163 240 ASP   A C   
1643 O  O   . ASP   A 241 ? 0.90019 0.91663 0.86180 0.04475  0.03605  -0.05076 240 ASP   A O   
1644 C  CB  . ASP   A 241 ? 1.16005 1.16954 1.12034 0.06323  0.04147  -0.06443 240 ASP   A CB  
1645 C  CG  . ASP   A 241 ? 1.25937 1.28288 1.22952 0.06888  0.04473  -0.06177 240 ASP   A CG  
1646 O  OD1 . ASP   A 241 ? 1.21099 1.22969 1.18809 0.07290  0.04304  -0.05994 240 ASP   A OD1 
1647 O  OD2 . ASP   A 241 ? 1.33494 1.37508 1.30591 0.06911  0.04894  -0.06128 240 ASP   A OD2 
1648 N  N   . LEU   A 242 ? 0.83017 0.84754 0.80688 0.04976  0.03515  -0.04637 241 LEU   A N   
1649 C  CA  . LEU   A 242 ? 0.72184 0.74641 0.70229 0.04274  0.03414  -0.03977 241 LEU   A CA  
1650 C  C   . LEU   A 242 ? 0.73114 0.77256 0.71891 0.04361  0.03764  -0.03688 241 LEU   A C   
1651 O  O   . LEU   A 242 ? 0.81860 0.86532 0.81201 0.04988  0.03922  -0.03828 241 LEU   A O   
1652 C  CB  . LEU   A 242 ? 0.68539 0.70066 0.67003 0.03969  0.02963  -0.03593 241 LEU   A CB  
1653 C  CG  . LEU   A 242 ? 0.68445 0.68485 0.66302 0.03694  0.02591  -0.03765 241 LEU   A CG  
1654 C  CD1 . LEU   A 242 ? 0.64952 0.64415 0.63261 0.03303  0.02213  -0.03294 241 LEU   A CD1 
1655 C  CD2 . LEU   A 242 ? 0.67685 0.67864 0.64753 0.03257  0.02605  -0.03855 241 LEU   A CD2 
1656 N  N   . PRO   A 243 ? 0.65606 0.70634 0.64413 0.03728  0.03886  -0.03256 242 PRO   A N   
1657 C  CA  . PRO   A 243 ? 0.62198 0.66751 0.60390 0.03048  0.03722  -0.02983 242 PRO   A CA  
1658 C  C   . PRO   A 243 ? 0.69797 0.74357 0.66981 0.03101  0.03903  -0.03348 242 PRO   A C   
1659 O  O   . PRO   A 243 ? 0.63385 0.68864 0.60398 0.03470  0.04322  -0.03660 242 PRO   A O   
1660 C  CB  . PRO   A 243 ? 0.59532 0.65153 0.58207 0.02494  0.03896  -0.02400 242 PRO   A CB  
1661 C  CG  . PRO   A 243 ? 0.58425 0.65512 0.57671 0.02868  0.04316  -0.02526 242 PRO   A CG  
1662 C  CD  . PRO   A 243 ? 0.59411 0.66047 0.58987 0.03634  0.04190  -0.02942 242 PRO   A CD  
1663 N  N   . ARG   A 244 ? 0.57812 0.61479 0.54308 0.02745  0.03595  -0.03326 243 ARG   A N   
1664 C  CA  A ARG   A 244 ? 0.61191 0.64939 0.56649 0.02726  0.03702  -0.03652 243 ARG   A CA  
1665 C  CA  B ARG   A 244 ? 0.61159 0.64911 0.56616 0.02726  0.03704  -0.03651 243 ARG   A CA  
1666 C  C   . ARG   A 244 ? 0.57465 0.61124 0.52488 0.02091  0.03480  -0.03124 243 ARG   A C   
1667 O  O   . ARG   A 244 ? 0.50740 0.53772 0.46142 0.01767  0.03129  -0.02720 243 ARG   A O   
1668 C  CB  A ARG   A 244 ? 0.63813 0.66438 0.58718 0.03093  0.03499  -0.04387 243 ARG   A CB  
1669 C  CB  B ARG   A 244 ? 0.63822 0.66453 0.58708 0.03084  0.03498  -0.04385 243 ARG   A CB  
1670 C  CG  A ARG   A 244 ? 0.63478 0.64948 0.58065 0.02678  0.02965  -0.04333 243 ARG   A CG  
1671 C  CG  B ARG   A 244 ? 0.63211 0.64517 0.58214 0.02812  0.02956  -0.04303 243 ARG   A CG  
1672 C  CD  A ARG   A 244 ? 0.68373 0.68997 0.62101 0.02844  0.02829  -0.05105 243 ARG   A CD  
1673 C  CD  B ARG   A 244 ? 0.65569 0.65729 0.59953 0.03039  0.02769  -0.05042 243 ARG   A CD  
1674 N  NE  A ARG   A 244 ? 0.66447 0.65902 0.60171 0.02496  0.02308  -0.05102 243 ARG   A NE  
1675 N  NE  B ARG   A 244 ? 0.66333 0.65356 0.60865 0.02686  0.02269  -0.04920 243 ARG   A NE  
1676 C  CZ  A ARG   A 244 ? 0.66992 0.65471 0.61304 0.02619  0.02110  -0.05125 243 ARG   A CZ  
1677 C  CZ  B ARG   A 244 ? 0.66525 0.64361 0.60645 0.02699  0.02021  -0.05461 243 ARG   A CZ  
1678 N  NH1 A ARG   A 244 ? 0.66731 0.65190 0.61647 0.03144  0.02347  -0.05174 243 ARG   A NH1 
1679 N  NH1 B ARG   A 244 ? 0.69384 0.66841 0.62844 0.03075  0.02205  -0.06228 243 ARG   A NH1 
1680 N  NH2 A ARG   A 244 ? 0.61400 0.59000 0.55704 0.02208  0.01663  -0.05060 243 ARG   A NH2 
1681 N  NH2 B ARG   A 244 ? 0.62741 0.59745 0.57104 0.02301  0.01595  -0.05249 243 ARG   A NH2 
1682 N  N   . GLU   A 245 ? 0.51598 0.55932 0.45802 0.01962  0.03699  -0.03111 244 GLU   A N   
1683 C  CA  . GLU   A 245 ? 0.52593 0.56896 0.46313 0.01445  0.03494  -0.02551 244 GLU   A CA  
1684 C  C   . GLU   A 245 ? 0.55987 0.59295 0.49221 0.01365  0.02972  -0.02811 244 GLU   A C   
1685 O  O   . GLU   A 245 ? 0.56637 0.59499 0.49442 0.01639  0.02887  -0.03528 244 GLU   A O   
1686 C  CB  . GLU   A 245 ? 0.58836 0.64211 0.51743 0.01340  0.03879  -0.02406 244 GLU   A CB  
1687 C  CG  . GLU   A 245 ? 0.72749 0.78057 0.64976 0.00905  0.03636  -0.01827 244 GLU   A CG  
1688 C  CD  . GLU   A 245 ? 0.69731 0.75670 0.60725 0.00945  0.03762  -0.02067 244 GLU   A CD  
1689 O  OE1 . GLU   A 245 ? 0.76772 0.82342 0.67185 0.01168  0.03555  -0.02796 244 GLU   A OE1 
1690 O  OE2 . GLU   A 245 ? 0.83562 0.90344 0.74123 0.00714  0.04068  -0.01519 244 GLU   A OE2 
1691 N  N   . VAL   A 246 ? 0.48261 0.51201 0.41615 0.00984  0.02623  -0.02243 245 VAL   A N   
1692 C  CA  . VAL   A 246 ? 0.50225 0.52508 0.43186 0.00827  0.02115  -0.02370 245 VAL   A CA  
1693 C  C   . VAL   A 246 ? 0.41927 0.44603 0.34434 0.00507  0.01973  -0.01702 245 VAL   A C   
1694 O  O   . VAL   A 246 ? 0.42579 0.45788 0.35122 0.00384  0.02264  -0.01115 245 VAL   A O   
1695 C  CB  . VAL   A 246 ? 0.46640 0.47997 0.40397 0.00783  0.01760  -0.02361 245 VAL   A CB  
1696 C  CG1 . VAL   A 246 ? 0.55941 0.56789 0.50044 0.01140  0.01858  -0.02973 245 VAL   A CG1 
1697 C  CG2 . VAL   A 246 ? 0.41252 0.42637 0.35792 0.00597  0.01788  -0.01638 245 VAL   A CG2 
1698 N  N   . TRP   A 247 ? 0.42651 0.45048 0.34763 0.00360  0.01506  -0.01762 246 TRP   A N   
1699 C  CA  . TRP   A 247 ? 0.39328 0.42051 0.31084 0.00142  0.01272  -0.01089 246 TRP   A CA  
1700 C  C   . TRP   A 247 ? 0.37347 0.39491 0.29813 0.00024  0.00861  -0.00756 246 TRP   A C   
1701 O  O   . TRP   A 247 ? 0.51012 0.52658 0.43751 -0.00001 0.00559  -0.01210 246 TRP   A O   
1702 C  CB  . TRP   A 247 ? 0.43327 0.46563 0.33961 0.00087  0.01053  -0.01390 246 TRP   A CB  
1703 C  CG  . TRP   A 247 ? 0.43007 0.46967 0.32837 0.00208  0.01503  -0.01627 246 TRP   A CG  
1704 C  CD1 . TRP   A 247 ? 0.49893 0.53893 0.39288 0.00411  0.01709  -0.02505 246 TRP   A CD1 
1705 C  CD2 . TRP   A 247 ? 0.45668 0.50405 0.35052 0.00147  0.01849  -0.00960 246 TRP   A CD2 
1706 N  NE1 . TRP   A 247 ? 0.53690 0.58596 0.42394 0.00502  0.02173  -0.02454 246 TRP   A NE1 
1707 C  CE2 . TRP   A 247 ? 0.51689 0.57078 0.40379 0.00302  0.02267  -0.01479 246 TRP   A CE2 
1708 C  CE3 . TRP   A 247 ? 0.47668 0.52550 0.37148 -0.00019 0.01864  0.00039  246 TRP   A CE3 
1709 C  CZ2 . TRP   A 247 ? 0.55821 0.62136 0.43917 0.00242  0.02704  -0.00999 246 TRP   A CZ2 
1710 C  CZ3 . TRP   A 247 ? 0.57947 0.63579 0.46818 -0.00096 0.02283  0.00541  246 TRP   A CZ3 
1711 C  CH2 . TRP   A 247 ? 0.53164 0.59567 0.41364 0.00007  0.02701  0.00039  246 TRP   A CH2 
1712 N  N   . LEU   A 248 ? 0.39282 0.41477 0.32005 -0.00052 0.00870  0.00038  247 LEU   A N   
1713 C  CA  . LEU   A 248 ? 0.41565 0.43271 0.35015 -0.00093 0.00583  0.00406  247 LEU   A CA  
1714 C  C   . LEU   A 248 ? 0.42224 0.44262 0.35293 -0.00109 0.00261  0.00979  247 LEU   A C   
1715 O  O   . LEU   A 248 ? 0.49187 0.51607 0.41699 -0.00097 0.00417  0.01508  247 LEU   A O   
1716 C  CB  . LEU   A 248 ? 0.38856 0.40193 0.33030 -0.00107 0.00896  0.00816  247 LEU   A CB  
1717 C  CG  . LEU   A 248 ? 0.41677 0.42816 0.36371 -0.00056 0.01169  0.00336  247 LEU   A CG  
1718 C  CD1 . LEU   A 248 ? 0.40178 0.41206 0.35434 -0.00158 0.01494  0.00760  247 LEU   A CD1 
1719 C  CD2 . LEU   A 248 ? 0.42662 0.43276 0.37856 -0.00006 0.00866  -0.00100 247 LEU   A CD2 
1720 N  N   . LEU   A 249 ? 0.38114 0.40054 0.31525 -0.00124 -0.00175 0.00937  248 LEU   A N   
1721 C  CA  . LEU   A 249 ? 0.35822 0.38192 0.29039 -0.00061 -0.00531 0.01494  248 LEU   A CA  
1722 C  C   . LEU   A 249 ? 0.37512 0.39459 0.31647 0.00038  -0.00662 0.01846  248 LEU   A C   
1723 O  O   . LEU   A 249 ? 0.40559 0.42288 0.35268 -0.00048 -0.00837 0.01439  248 LEU   A O   
1724 C  CB  . LEU   A 249 ? 0.40432 0.43426 0.33124 -0.00188 -0.00984 0.01051  248 LEU   A CB  
1725 C  CG  . LEU   A 249 ? 0.40988 0.44686 0.33554 -0.00111 -0.01447 0.01567  248 LEU   A CG  
1726 C  CD1 . LEU   A 249 ? 0.40484 0.44582 0.32375 0.00089  -0.01326 0.02348  248 LEU   A CD1 
1727 C  CD2 . LEU   A 249 ? 0.46579 0.50916 0.38692 -0.00362 -0.01895 0.00958  248 LEU   A CD2 
1728 N  N   . GLU   A 250 ? 0.38530 0.40328 0.32762 0.00222  -0.00562 0.02601  249 GLU   A N   
1729 C  CA  . GLU   A 250 ? 0.41468 0.42889 0.36501 0.00391  -0.00668 0.02916  249 GLU   A CA  
1730 C  C   . GLU   A 250 ? 0.47620 0.49719 0.42801 0.00473  -0.01181 0.02911  249 GLU   A C   
1731 O  O   . GLU   A 250 ? 0.41756 0.44621 0.36335 0.00515  -0.01469 0.03088  249 GLU   A O   
1732 C  CB  . GLU   A 250 ? 0.43008 0.43981 0.38016 0.00604  -0.00439 0.03707  249 GLU   A CB  
1733 C  CG  . GLU   A 250 ? 0.47715 0.48155 0.43544 0.00828  -0.00469 0.03938  249 GLU   A CG  
1734 C  CD  . GLU   A 250 ? 0.56335 0.56012 0.52138 0.01013  -0.00186 0.04623  249 GLU   A CD  
1735 O  OE1 . GLU   A 250 ? 0.69173 0.68530 0.64541 0.00816  0.00152  0.04809  249 GLU   A OE1 
1736 O  OE2 . GLU   A 250 ? 0.68034 0.67406 0.64271 0.01344  -0.00277 0.04956  249 GLU   A OE2 
1737 N  N   . THR   A 251 ? 0.37362 0.39299 0.33349 0.00476  -0.01299 0.02724  250 THR   A N   
1738 C  CA  . THR   A 251 ? 0.35884 0.38580 0.32150 0.00432  -0.01761 0.02586  250 THR   A CA  
1739 C  C   . THR   A 251 ? 0.40777 0.43325 0.37941 0.00666  -0.01765 0.02855  250 THR   A C   
1740 O  O   . THR   A 251 ? 0.34503 0.36228 0.32049 0.00740  -0.01416 0.02886  250 THR   A O   
1741 C  CB  . THR   A 251 ? 0.42446 0.45170 0.38664 0.00007  -0.01885 0.01782  250 THR   A CB  
1742 O  OG1 . THR   A 251 ? 0.53876 0.57484 0.50157 -0.00176 -0.02369 0.01622  250 THR   A OG1 
1743 C  CG2 . THR   A 251 ? 0.39544 0.41487 0.36453 -0.00102 -0.01647 0.01456  250 THR   A CG2 
1744 N  N   . PRO   A 252 ? 0.39157 0.42572 0.36666 0.00801  -0.02140 0.03050  251 PRO   A N   
1745 C  CA  . PRO   A 252 ? 0.37448 0.40838 0.35843 0.01050  -0.02105 0.03233  251 PRO   A CA  
1746 C  C   . PRO   A 252 ? 0.38636 0.41685 0.37568 0.00693  -0.02002 0.02670  251 PRO   A C   
1747 O  O   . PRO   A 252 ? 0.35431 0.38398 0.34137 0.00257  -0.02067 0.02140  251 PRO   A O   
1748 C  CB  . PRO   A 252 ? 0.48421 0.53118 0.47053 0.01250  -0.02563 0.03534  251 PRO   A CB  
1749 C  CG  . PRO   A 252 ? 0.47852 0.53288 0.45729 0.00974  -0.02901 0.03385  251 PRO   A CG  
1750 C  CD  . PRO   A 252 ? 0.44731 0.49315 0.41823 0.00766  -0.02605 0.03145  251 PRO   A CD  
1751 N  N   . GLN   A 253 ? 0.38772 0.41540 0.38379 0.00917  -0.01815 0.02801  252 GLN   A N   
1752 C  CA  . GLN   A 253 ? 0.32113 0.34739 0.32260 0.00618  -0.01746 0.02385  252 GLN   A CA  
1753 C  C   . GLN   A 253 ? 0.38509 0.42054 0.38818 0.00217  -0.02136 0.02103  252 GLN   A C   
1754 O  O   . GLN   A 253 ? 0.37796 0.42414 0.38346 0.00337  -0.02445 0.02347  252 GLN   A O   
1755 C  CB  . GLN   A 253 ? 0.30734 0.33282 0.31553 0.00976  -0.01552 0.02619  252 GLN   A CB  
1756 C  CG  . GLN   A 253 ? 0.31079 0.33432 0.32389 0.00709  -0.01410 0.02272  252 GLN   A CG  
1757 C  CD  . GLN   A 253 ? 0.31641 0.34131 0.33555 0.01097  -0.01232 0.02478  252 GLN   A CD  
1758 O  OE1 . GLN   A 253 ? 0.33665 0.35695 0.35523 0.01556  -0.01038 0.02767  252 GLN   A OE1 
1759 N  NE2 . GLN   A 253 ? 0.30919 0.34028 0.33393 0.00913  -0.01278 0.02332  252 GLN   A NE2 
1760 N  N   . ALA   A 254 ? 0.34596 0.37715 0.34782 -0.00264 -0.02125 0.01595  253 ALA   A N   
1761 C  CA  . ALA   A 254 ? 0.39152 0.42889 0.39398 -0.00771 -0.02475 0.01254  253 ALA   A CA  
1762 C  C   . ALA   A 254 ? 0.40453 0.45160 0.41522 -0.00821 -0.02635 0.01437  253 ALA   A C   
1763 O  O   . ALA   A 254 ? 0.35996 0.40569 0.37616 -0.00582 -0.02384 0.01626  253 ALA   A O   
1764 C  CB  . ALA   A 254 ? 0.39656 0.42468 0.39718 -0.01201 -0.02354 0.00729  253 ALA   A CB  
1765 N  N   . ASP   A 255 ? 0.36119 0.41907 0.37267 -0.01167 -0.03054 0.01344  254 ASP   A N   
1766 C  CA  . ASP   A 255 ? 0.38141 0.45151 0.40133 -0.01253 -0.03226 0.01531  254 ASP   A CA  
1767 C  C   . ASP   A 255 ? 0.39618 0.46223 0.42114 -0.01652 -0.03024 0.01324  254 ASP   A C   
1768 O  O   . ASP   A 255 ? 0.43586 0.50921 0.46832 -0.01521 -0.02933 0.01570  254 ASP   A O   
1769 C  CB  . ASP   A 255 ? 0.45936 0.54259 0.47900 -0.01691 -0.03749 0.01403  254 ASP   A CB  
1770 C  CG  . ASP   A 255 ? 0.55209 0.64862 0.57310 -0.01147 -0.04007 0.01908  254 ASP   A CG  
1771 O  OD1 . ASP   A 255 ? 0.51282 0.60859 0.53655 -0.00419 -0.03764 0.02385  254 ASP   A OD1 
1772 O  OD2 . ASP   A 255 ? 0.67611 0.78391 0.69533 -0.01448 -0.04471 0.01823  254 ASP   A OD2 
1773 N  N   . ASP   A 256 ? 0.33793 0.39289 0.35879 -0.02114 -0.02943 0.00896  255 ASP   A N   
1774 C  CA  . ASP   A 256 ? 0.36723 0.41772 0.39204 -0.02507 -0.02769 0.00770  255 ASP   A CA  
1775 C  C   . ASP   A 256 ? 0.33028 0.37014 0.35492 -0.02127 -0.02329 0.00863  255 ASP   A C   
1776 O  O   . ASP   A 256 ? 0.36991 0.40488 0.39657 -0.02411 -0.02169 0.00788  255 ASP   A O   
1777 C  CB  . ASP   A 256 ? 0.39344 0.43734 0.41442 -0.03235 -0.02945 0.00284  255 ASP   A CB  
1778 C  CG  . ASP   A 256 ? 0.51082 0.54224 0.52321 -0.03116 -0.02859 -0.00062 255 ASP   A CG  
1779 O  OD1 . ASP   A 256 ? 0.48591 0.51581 0.49518 -0.02555 -0.02712 0.00098  255 ASP   A OD1 
1780 O  OD2 . ASP   A 256 ? 0.61495 0.63799 0.62374 -0.03591 -0.02923 -0.00496 255 ASP   A OD2 
1781 N  N   . PHE   A 257 ? 0.31253 0.34907 0.33475 -0.01530 -0.02140 0.01048  256 PHE   A N   
1782 C  CA  . PHE   A 257 ? 0.29013 0.31823 0.31262 -0.01208 -0.01748 0.01121  256 PHE   A CA  
1783 C  C   . PHE   A 257 ? 0.26785 0.30107 0.29479 -0.00677 -0.01577 0.01482  256 PHE   A C   
1784 O  O   . PHE   A 257 ? 0.27668 0.31389 0.30295 -0.00283 -0.01660 0.01725  256 PHE   A O   
1785 C  CB  . PHE   A 257 ? 0.27054 0.28876 0.28656 -0.01019 -0.01597 0.00982  256 PHE   A CB  
1786 C  CG  . PHE   A 257 ? 0.26410 0.27586 0.28087 -0.00693 -0.01231 0.01082  256 PHE   A CG  
1787 C  CD1 . PHE   A 257 ? 0.29660 0.30403 0.31525 -0.00857 -0.01065 0.00967  256 PHE   A CD1 
1788 C  CD2 . PHE   A 257 ? 0.28095 0.29128 0.29653 -0.00259 -0.01068 0.01310  256 PHE   A CD2 
1789 C  CE1 . PHE   A 257 ? 0.27614 0.27909 0.29534 -0.00605 -0.00770 0.01022  256 PHE   A CE1 
1790 C  CE2 . PHE   A 257 ? 0.26725 0.27167 0.28352 -0.00055 -0.00748 0.01337  256 PHE   A CE2 
1791 C  CZ  . PHE   A 257 ? 0.28866 0.29012 0.30672 -0.00232 -0.00615 0.01169  256 PHE   A CZ  
1792 N  N   . TRP   A 258 ? 0.25824 0.29100 0.28926 -0.00640 -0.01331 0.01522  257 TRP   A N   
1793 C  CA  . TRP   A 258 ? 0.24902 0.28208 0.28254 -0.00091 -0.01059 0.01731  257 TRP   A CA  
1794 C  C   . TRP   A 258 ? 0.20953 0.23871 0.24459 -0.00203 -0.00777 0.01618  257 TRP   A C   
1795 O  O   . TRP   A 258 ? 0.23340 0.26097 0.26828 -0.00674 -0.00817 0.01479  257 TRP   A O   
1796 C  CB  . TRP   A 258 ? 0.30604 0.35131 0.34507 0.00250  -0.01159 0.02012  257 TRP   A CB  
1797 C  CG  . TRP   A 258 ? 0.36078 0.41657 0.40640 0.00005  -0.01160 0.02034  257 TRP   A CG  
1798 C  CD1 . TRP   A 258 ? 0.35505 0.41522 0.40544 0.00308  -0.00870 0.02118  257 TRP   A CD1 
1799 C  CD2 . TRP   A 258 ? 0.34045 0.40424 0.38855 -0.00626 -0.01440 0.01964  257 TRP   A CD2 
1800 N  NE1 . TRP   A 258 ? 0.30117 0.37257 0.35705 -0.00089 -0.00937 0.02152  257 TRP   A NE1 
1801 C  CE2 . TRP   A 258 ? 0.31948 0.39294 0.37425 -0.00704 -0.01293 0.02069  257 TRP   A CE2 
1802 C  CE3 . TRP   A 258 ? 0.33137 0.39488 0.37642 -0.01168 -0.01786 0.01789  257 TRP   A CE3 
1803 C  CZ2 . TRP   A 258 ? 0.39142 0.47440 0.45033 -0.01366 -0.01484 0.02059  257 TRP   A CZ2 
1804 C  CZ3 . TRP   A 258 ? 0.39076 0.46243 0.43954 -0.01821 -0.01994 0.01721  257 TRP   A CZ3 
1805 C  CH2 . TRP   A 258 ? 0.40304 0.48442 0.45892 -0.01945 -0.01844 0.01882  257 TRP   A CH2 
1806 N  N   . CYS   A 259 ? 0.24197 0.26896 0.27794 0.00234  -0.00491 0.01680  258 CYS   A N   
1807 C  CA  . CYS   A 259 ? 0.23318 0.25625 0.26925 0.00162  -0.00221 0.01546  258 CYS   A CA  
1808 C  C   . CYS   A 259 ? 0.32166 0.35055 0.36188 0.00565  0.00011  0.01627  258 CYS   A C   
1809 O  O   . CYS   A 259 ? 0.30100 0.32975 0.34174 0.01068  0.00076  0.01731  258 CYS   A O   
1810 C  CB  . CYS   A 259 ? 0.25519 0.26728 0.28631 0.00233  -0.00078 0.01396  258 CYS   A CB  
1811 S  SG  . CYS   A 259 ? 0.29292 0.30101 0.32346 0.00204  0.00224  0.01220  258 CYS   A SG  
1812 N  N   . GLU   A 260 ? 0.24267 0.27659 0.28559 0.00375  0.00152  0.01596  259 GLU   A N   
1813 C  CA  . GLU   A 260 ? 0.26233 0.30286 0.30900 0.00763  0.00422  0.01614  259 GLU   A CA  
1814 C  C   . GLU   A 260 ? 0.26373 0.29886 0.30757 0.00736  0.00713  0.01405  259 GLU   A C   
1815 O  O   . GLU   A 260 ? 0.24975 0.28063 0.29075 0.00313  0.00665  0.01353  259 GLU   A O   
1816 C  CB  . GLU   A 260 ? 0.28978 0.34434 0.34248 0.00556  0.00376  0.01778  259 GLU   A CB  
1817 C  CG  . GLU   A 260 ? 0.39486 0.45899 0.45194 0.00743  0.00127  0.01981  259 GLU   A CG  
1818 C  CD  . GLU   A 260 ? 0.49149 0.57027 0.55474 0.00330  0.00029  0.02127  259 GLU   A CD  
1819 O  OE1 . GLU   A 260 ? 0.46454 0.54818 0.52994 0.00189  0.00295  0.02121  259 GLU   A OE1 
1820 O  OE2 . GLU   A 260 ? 0.46401 0.55008 0.52980 0.00117  -0.00311 0.02251  259 GLU   A OE2 
1821 N  N   . GLY   A 261 ? 0.25721 0.29277 0.30165 0.01207  0.01006  0.01277  260 GLY   A N   
1822 C  CA  . GLY   A 261 ? 0.25213 0.28433 0.29355 0.01155  0.01272  0.01031  260 GLY   A CA  
1823 C  C   . GLY   A 261 ? 0.28587 0.32730 0.32918 0.00827  0.01366  0.01117  260 GLY   A C   
1824 O  O   . GLY   A 261 ? 0.28029 0.33255 0.32859 0.00772  0.01345  0.01321  260 GLY   A O   
1825 N  N   . GLU   A 262 ? 0.25037 0.28840 0.28969 0.00586  0.01474  0.00991  261 GLU   A N   
1826 C  CA  . GLU   A 262 ? 0.28501 0.33139 0.32492 0.00352  0.01649  0.01085  261 GLU   A CA  
1827 C  C   . GLU   A 262 ? 0.25136 0.29431 0.28627 0.00460  0.01883  0.00785  261 GLU   A C   
1828 O  O   . GLU   A 262 ? 0.24306 0.27663 0.27428 0.00552  0.01836  0.00541  261 GLU   A O   
1829 C  CB  . GLU   A 262 ? 0.28231 0.32934 0.32216 -0.00260 0.01427  0.01404  261 GLU   A CB  
1830 C  CG  . GLU   A 262 ? 0.31148 0.34850 0.34610 -0.00508 0.01272  0.01384  261 GLU   A CG  
1831 C  CD  . GLU   A 262 ? 0.34971 0.38696 0.38408 -0.01041 0.01125  0.01725  261 GLU   A CD  
1832 O  OE1 . GLU   A 262 ? 0.32774 0.37033 0.36142 -0.01246 0.01288  0.01918  261 GLU   A OE1 
1833 O  OE2 . GLU   A 262 ? 0.32492 0.35643 0.35929 -0.01259 0.00860  0.01801  261 GLU   A OE2 
1834 N  N   . PRO   A 263 ? 0.26832 0.31966 0.30296 0.00443  0.02151  0.00774  262 PRO   A N   
1835 C  CA  . PRO   A 263 ? 0.28495 0.33417 0.31422 0.00571  0.02378  0.00412  262 PRO   A CA  
1836 C  C   . PRO   A 263 ? 0.27319 0.31551 0.29729 0.00217  0.02173  0.00429  262 PRO   A C   
1837 O  O   . PRO   A 263 ? 0.29200 0.33454 0.31602 -0.00169 0.01970  0.00804  262 PRO   A O   
1838 C  CB  . PRO   A 263 ? 0.30455 0.36624 0.33451 0.00540  0.02684  0.00502  262 PRO   A CB  
1839 C  CG  . PRO   A 263 ? 0.29287 0.36323 0.33009 0.00660  0.02714  0.00747  262 PRO   A CG  
1840 C  CD  . PRO   A 263 ? 0.28719 0.35171 0.32681 0.00390  0.02308  0.01022  262 PRO   A CD  
1841 N  N   . TYR   A 264 ? 0.26176 0.29800 0.28164 0.00360  0.02231  0.00007  263 TYR   A N   
1842 C  CA  . TYR   A 264 ? 0.24882 0.28093 0.26403 0.00081  0.02056  -0.00036 263 TYR   A CA  
1843 C  C   . TYR   A 264 ? 0.28682 0.32642 0.29778 -0.00045 0.02213  -0.00056 263 TYR   A C   
1844 O  O   . TYR   A 264 ? 0.26464 0.30748 0.27347 0.00173  0.02500  -0.00453 263 TYR   A O   
1845 C  CB  . TYR   A 264 ? 0.20779 0.23133 0.22077 0.00208  0.02046  -0.00494 263 TYR   A CB  
1846 C  CG  . TYR   A 264 ? 0.23633 0.25852 0.24464 -0.00046 0.01920  -0.00662 263 TYR   A CG  
1847 C  CD1 . TYR   A 264 ? 0.23744 0.25962 0.24550 -0.00298 0.01640  -0.00303 263 TYR   A CD1 
1848 C  CD2 . TYR   A 264 ? 0.25958 0.28073 0.26371 -0.00020 0.02074  -0.01204 263 TYR   A CD2 
1849 C  CE1 . TYR   A 264 ? 0.24834 0.27125 0.25269 -0.00477 0.01499  -0.00419 263 TYR   A CE1 
1850 C  CE2 . TYR   A 264 ? 0.28776 0.30976 0.28779 -0.00296 0.01917  -0.01367 263 TYR   A CE2 
1851 C  CZ  . TYR   A 264 ? 0.25070 0.27432 0.25122 -0.00500 0.01622  -0.00944 263 TYR   A CZ  
1852 O  OH  . TYR   A 264 ? 0.25750 0.28374 0.25463 -0.00715 0.01441  -0.01064 263 TYR   A OH  
1853 N  N   . PRO   A 265 ? 0.24418 0.28639 0.25329 -0.00362 0.02048  0.00363  264 PRO   A N   
1854 C  CA  . PRO   A 265 ? 0.25458 0.30499 0.25917 -0.00484 0.02200  0.00456  264 PRO   A CA  
1855 C  C   . PRO   A 265 ? 0.31900 0.36894 0.31741 -0.00544 0.02103  0.00181  264 PRO   A C   
1856 O  O   . PRO   A 265 ? 0.28045 0.33794 0.27413 -0.00627 0.02222  0.00228  264 PRO   A O   
1857 C  CB  . PRO   A 265 ? 0.28133 0.33355 0.28712 -0.00804 0.02046  0.01157  264 PRO   A CB  
1858 C  CG  . PRO   A 265 ? 0.25982 0.30218 0.26787 -0.00848 0.01706  0.01257  264 PRO   A CG  
1859 C  CD  . PRO   A 265 ? 0.28501 0.32337 0.29659 -0.00592 0.01760  0.00845  264 PRO   A CD  
1860 N  N   . GLY   A 266 ? 0.25816 0.30082 0.25640 -0.00538 0.01889  -0.00083 265 GLY   A N   
1861 C  CA  . GLY   A 266 ? 0.29178 0.33562 0.28518 -0.00673 0.01714  -0.00242 265 GLY   A CA  
1862 C  C   . GLY   A 266 ? 0.28492 0.32960 0.27415 -0.00637 0.01879  -0.00964 265 GLY   A C   
1863 O  O   . GLY   A 266 ? 0.27398 0.31791 0.26340 -0.00439 0.02185  -0.01366 265 GLY   A O   
1864 N  N   . PRO   A 267 ? 0.29103 0.33745 0.27637 -0.00823 0.01668  -0.01157 266 PRO   A N   
1865 C  CA  . PRO   A 267 ? 0.32389 0.37054 0.30463 -0.00902 0.01779  -0.01920 266 PRO   A CA  
1866 C  C   . PRO   A 267 ? 0.33173 0.36797 0.31534 -0.00806 0.01926  -0.02418 266 PRO   A C   
1867 O  O   . PRO   A 267 ? 0.31262 0.34207 0.30095 -0.00800 0.01793  -0.02214 266 PRO   A O   
1868 C  CB  . PRO   A 267 ? 0.31632 0.36678 0.29443 -0.01175 0.01420  -0.01920 266 PRO   A CB  
1869 C  CG  . PRO   A 267 ? 0.29969 0.35438 0.27923 -0.01131 0.01189  -0.01081 266 PRO   A CG  
1870 C  CD  . PRO   A 267 ? 0.28013 0.32843 0.26544 -0.00956 0.01307  -0.00692 266 PRO   A CD  
1871 N  N   . LYS   A 268 ? 0.31481 0.34934 0.29498 -0.00719 0.02213  -0.03078 267 LYS   A N   
1872 C  CA  . LYS   A 268 ? 0.39843 0.42184 0.38108 -0.00535 0.02408  -0.03473 267 LYS   A CA  
1873 C  C   . LYS   A 268 ? 0.44127 0.45742 0.42209 -0.00883 0.02275  -0.03987 267 LYS   A C   
1874 O  O   . LYS   A 268 ? 0.41550 0.43640 0.39161 -0.01236 0.02134  -0.04336 267 LYS   A O   
1875 C  CB  . LYS   A 268 ? 0.40293 0.42636 0.38348 -0.00163 0.02834  -0.03917 267 LYS   A CB  
1876 C  CG  . LYS   A 268 ? 0.41345 0.44723 0.39540 0.00082  0.02996  -0.03449 267 LYS   A CG  
1877 C  CD  . LYS   A 268 ? 0.42981 0.46259 0.41917 0.00214  0.02880  -0.02737 267 LYS   A CD  
1878 C  CE  . LYS   A 268 ? 0.40601 0.44981 0.39708 0.00318  0.03025  -0.02243 267 LYS   A CE  
1879 N  NZ  . LYS   A 268 ? 0.31117 0.35495 0.30819 0.00223  0.02792  -0.01519 267 LYS   A NZ  
1880 N  N   . VAL   A 269 ? 0.35050 0.35588 0.33515 -0.00823 0.02303  -0.03986 268 VAL   A N   
1881 C  CA  . VAL   A 269 ? 0.38358 0.38066 0.36698 -0.01198 0.02240  -0.04450 268 VAL   A CA  
1882 C  C   . VAL   A 269 ? 0.46351 0.45106 0.44345 -0.01036 0.02595  -0.05158 268 VAL   A C   
1883 O  O   . VAL   A 269 ? 0.48869 0.47017 0.47092 -0.00538 0.02851  -0.05069 268 VAL   A O   
1884 C  CB  . VAL   A 269 ? 0.41083 0.40134 0.39955 -0.01259 0.02097  -0.04018 268 VAL   A CB  
1885 C  CG1 . VAL   A 269 ? 0.42182 0.40289 0.40938 -0.01679 0.02110  -0.04477 268 VAL   A CG1 
1886 C  CG2 . VAL   A 269 ? 0.34151 0.34092 0.33289 -0.01401 0.01765  -0.03444 268 VAL   A CG2 
1887 N  N   . PHE   A 270 ? 0.50091 0.48765 0.47521 -0.01435 0.02604  -0.05875 269 PHE   A N   
1888 C  CA  A PHE   A 270 ? 0.56029 0.53838 0.52931 -0.01366 0.02933  -0.06728 269 PHE   A CA  
1889 C  CA  B PHE   A 270 ? 0.55988 0.53726 0.52942 -0.01324 0.02944  -0.06684 269 PHE   A CA  
1890 C  C   . PHE   A 270 ? 0.58650 0.55090 0.55483 -0.01834 0.02918  -0.07168 269 PHE   A C   
1891 O  O   . PHE   A 270 ? 0.56748 0.53569 0.53618 -0.02457 0.02610  -0.07149 269 PHE   A O   
1892 C  CB  A PHE   A 270 ? 0.57559 0.56347 0.53731 -0.01595 0.02933  -0.07317 269 PHE   A CB  
1893 C  CB  B PHE   A 270 ? 0.57037 0.55718 0.53278 -0.01402 0.03026  -0.07258 269 PHE   A CB  
1894 C  CG  A PHE   A 270 ? 0.60087 0.60195 0.56157 -0.01189 0.03030  -0.06984 269 PHE   A CG  
1895 C  CG  B PHE   A 270 ? 0.60223 0.59808 0.56092 -0.02091 0.02663  -0.07477 269 PHE   A CG  
1896 C  CD1 A PHE   A 270 ? 0.51041 0.52279 0.47456 -0.01200 0.02756  -0.06148 269 PHE   A CD1 
1897 C  CD1 B PHE   A 270 ? 0.63320 0.62275 0.58731 -0.02659 0.02629  -0.08302 269 PHE   A CD1 
1898 C  CD2 A PHE   A 270 ? 0.64842 0.65085 0.60397 -0.00846 0.03407  -0.07548 269 PHE   A CD2 
1899 C  CD2 B PHE   A 270 ? 0.60774 0.61851 0.56742 -0.02169 0.02352  -0.06858 269 PHE   A CD2 
1900 C  CE1 A PHE   A 270 ? 0.55371 0.57770 0.51657 -0.00923 0.02858  -0.05801 269 PHE   A CE1 
1901 C  CE1 B PHE   A 270 ? 0.64368 0.64370 0.59482 -0.03303 0.02260  -0.08507 269 PHE   A CE1 
1902 C  CE2 A PHE   A 270 ? 0.68255 0.69837 0.63694 -0.00545 0.03528  -0.07220 269 PHE   A CE2 
1903 C  CE2 B PHE   A 270 ? 0.62051 0.64094 0.57706 -0.02717 0.01994  -0.07012 269 PHE   A CE2 
1904 C  CZ  A PHE   A 270 ? 0.64057 0.66701 0.59862 -0.00621 0.03248  -0.06317 269 PHE   A CZ  
1905 C  CZ  B PHE   A 270 ? 0.59657 0.61271 0.54907 -0.03288 0.01936  -0.07842 269 PHE   A CZ  
1906 N  N   . PRO   A 271 ? 0.58349 0.53231 0.55070 -0.01571 0.03250  -0.07568 270 PRO   A N   
1907 C  CA  . PRO   A 271 ? 0.66607 0.60035 0.63136 -0.02112 0.03278  -0.08057 270 PRO   A CA  
1908 C  C   . PRO   A 271 ? 0.67094 0.60868 0.62980 -0.02836 0.03161  -0.08901 270 PRO   A C   
1909 O  O   . PRO   A 271 ? 0.67060 0.61670 0.62437 -0.02721 0.03226  -0.09356 270 PRO   A O   
1910 C  CB  . PRO   A 271 ? 0.65704 0.57460 0.62103 -0.01512 0.03710  -0.08365 270 PRO   A CB  
1911 C  CG  . PRO   A 271 ? 0.69904 0.62317 0.66766 -0.00667 0.03814  -0.07707 270 PRO   A CG  
1912 C  CD  . PRO   A 271 ? 0.53229 0.47612 0.50108 -0.00727 0.03604  -0.07450 270 PRO   A CD  
1913 O  OXT . PRO   A 271 ? 0.80430 0.73748 0.76281 -0.03582 0.02998  -0.09149 270 PRO   A OXT 
1914 C  C   . ACE   B 1   ? 0.56172 0.67292 0.62984 0.04465  -0.01726 0.04341  0   ACE   B C   
1915 O  O   . ACE   B 1   ? 0.52053 0.64192 0.59212 0.05159  -0.01920 0.04776  0   ACE   B O   
1916 C  CH3 . ACE   B 1   ? 0.49464 0.61252 0.56379 0.03420  -0.01928 0.03980  0   ACE   B CH3 
1917 N  N   . TYR   B 2   ? 0.44063 0.53365 0.50371 0.04579  -0.01325 0.04165  1   TYR   B N   
1918 C  CA  . TYR   B 2   ? 0.50430 0.58609 0.56518 0.05457  -0.01055 0.04427  1   TYR   B CA  
1919 C  C   . TYR   B 2   ? 0.45874 0.52021 0.51089 0.05120  -0.00841 0.04232  1   TYR   B C   
1920 O  O   . TYR   B 2   ? 0.41296 0.47031 0.46262 0.04365  -0.00803 0.03839  1   TYR   B O   
1921 C  CB  . TYR   B 2   ? 0.43015 0.51446 0.49731 0.06080  -0.00649 0.04317  1   TYR   B CB  
1922 C  CG  . TYR   B 2   ? 0.49335 0.57316 0.56067 0.05540  -0.00307 0.03783  1   TYR   B CG  
1923 C  CD1 . TYR   B 2   ? 0.49013 0.55156 0.55131 0.05438  0.00030  0.03497  1   TYR   B CD1 
1924 C  CD2 . TYR   B 2   ? 0.46065 0.55515 0.53404 0.05083  -0.00334 0.03596  1   TYR   B CD2 
1925 C  CE1 . TYR   B 2   ? 0.49945 0.55770 0.56024 0.04963  0.00303  0.03045  1   TYR   B CE1 
1926 C  CE2 . TYR   B 2   ? 0.47916 0.56941 0.55186 0.04594  -0.00024 0.03182  1   TYR   B CE2 
1927 C  CZ  . TYR   B 2   ? 0.50379 0.57616 0.57003 0.04571  0.00279  0.02912  1   TYR   B CZ  
1928 O  OH  . TYR   B 2   ? 0.49282 0.56166 0.55783 0.04121  0.00553  0.02533  1   TYR   B OH  
1929 N  N   . ILE   B 3   ? 0.47654 0.52559 0.52419 0.05663  -0.00701 0.04531  2   ILE   B N   
1930 C  CA  . ILE   B 3   ? 0.44984 0.48091 0.48981 0.05314  -0.00485 0.04381  2   ILE   B CA  
1931 C  C   . ILE   B 3   ? 0.52578 0.54416 0.56590 0.05653  -0.00001 0.04145  2   ILE   B C   
1932 O  O   . ILE   B 3   ? 0.54741 0.56479 0.59042 0.06460  0.00163  0.04349  2   ILE   B O   
1933 C  CB  . ILE   B 3   ? 0.50889 0.53416 0.54253 0.05492  -0.00662 0.04886  2   ILE   B CB  
1934 C  CG1 . ILE   B 3   ? 0.54669 0.58458 0.57895 0.05030  -0.01142 0.04975  2   ILE   B CG1 
1935 C  CG2 . ILE   B 3   ? 0.47119 0.47844 0.49769 0.05154  -0.00373 0.04770  2   ILE   B CG2 
1936 C  CD1 . ILE   B 3   ? 0.68746 0.73415 0.71930 0.05590  -0.01491 0.05609  2   ILE   B CD1 
1937 N  N   . VAL   B 4   ? 0.43154 0.44106 0.46873 0.05057  0.00219  0.03679  3   VAL   B N   
1938 C  CA  . VAL   B 4   ? 0.40860 0.40561 0.44468 0.05219  0.00652  0.03359  3   VAL   B CA  
1939 C  C   . VAL   B 4   ? 0.43954 0.42170 0.46871 0.04744  0.00769  0.03274  3   VAL   B C   
1940 O  O   . VAL   B 4   ? 0.39459 0.37846 0.42112 0.04110  0.00593  0.03198  3   VAL   B O   
1941 C  CB  . VAL   B 4   ? 0.50161 0.50474 0.54143 0.04942  0.00821  0.02848  3   VAL   B CB  
1942 C  CG1 . VAL   B 4   ? 0.48627 0.49577 0.52557 0.04117  0.00593  0.02664  3   VAL   B CG1 
1943 C  CG2 . VAL   B 4   ? 0.51639 0.50616 0.55330 0.04940  0.01228  0.02432  3   VAL   B CG2 
1944 N  N   . LYS   B 5   ? 0.42896 0.39659 0.45527 0.05049  0.01075  0.03284  4   LYS   B N   
1945 C  CA  . LYS   B 5   ? 0.44831 0.40235 0.46877 0.04527  0.01232  0.03169  4   LYS   B CA  
1946 C  C   . LYS   B 5   ? 0.47182 0.42390 0.49259 0.04043  0.01437  0.02522  4   LYS   B C   
1947 O  O   . LYS   B 5   ? 0.54163 0.48698 0.56277 0.04278  0.01727  0.02202  4   LYS   B O   
1948 C  CB  . LYS   B 5   ? 0.52902 0.46745 0.54598 0.04952  0.01464  0.03473  4   LYS   B CB  
1949 C  CG  . LYS   B 5   ? 0.61666 0.55599 0.63217 0.05442  0.01258  0.04217  4   LYS   B CG  
1950 C  CD  . LYS   B 5   ? 0.71770 0.64051 0.73062 0.06016  0.01536  0.04519  4   LYS   B CD  
1951 C  CE  . LYS   B 5   ? 0.83818 0.76582 0.85392 0.07019  0.01396  0.05097  4   LYS   B CE  
1952 N  NZ  . LYS   B 5   ? 0.88331 0.79524 0.89868 0.07742  0.01755  0.05121  4   LYS   B NZ  
1953 N  N   . THR   B 6   ? 0.37327 0.33137 0.39359 0.03399  0.01282  0.02320  5   THR   B N   
1954 C  CA  . THR   B 6   ? 0.38173 0.33954 0.40209 0.02935  0.01417  0.01789  5   THR   B CA  
1955 C  C   . THR   B 6   ? 0.40604 0.35382 0.42194 0.02421  0.01537  0.01647  5   THR   B C   
1956 O  O   . THR   B 6   ? 0.40205 0.34687 0.41514 0.02250  0.01456  0.01957  5   THR   B O   
1957 C  CB  . THR   B 6   ? 0.37281 0.34285 0.39557 0.02569  0.01180  0.01680  5   THR   B CB  
1958 O  OG1 . THR   B 6   ? 0.35835 0.32847 0.37831 0.02155  0.00987  0.01818  5   THR   B OG1 
1959 C  CG2 . THR   B 6   ? 0.38617 0.36794 0.41362 0.02944  0.01005  0.01903  5   THR   B CG2 
1960 N  N   . PHE   B 7   ? 0.42801 0.37210 0.44332 0.02144  0.01729  0.01171  6   PHE   B N   
1961 C  CA  . PHE   B 7   ? 0.39133 0.32927 0.40349 0.01563  0.01807  0.00992  6   PHE   B CA  
1962 C  C   . PHE   B 7   ? 0.34769 0.29438 0.36035 0.01104  0.01606  0.00911  6   PHE   B C   
1963 O  O   . PHE   B 7   ? 0.35872 0.30312 0.36942 0.00667  0.01628  0.00862  6   PHE   B O   
1964 C  CB  . PHE   B 7   ? 0.45130 0.38203 0.46222 0.01412  0.02063  0.00488  6   PHE   B CB  
1965 C  CG  . PHE   B 7   ? 0.39134 0.32980 0.40431 0.01476  0.02074  0.00100  6   PHE   B CG  
1966 C  CD1 . PHE   B 7   ? 0.41992 0.36687 0.43350 0.01059  0.01929  -0.00071 6   PHE   B CD1 
1967 C  CD2 . PHE   B 7   ? 0.43834 0.37569 0.45242 0.01989  0.02252  -0.00068 6   PHE   B CD2 
1968 C  CE1 . PHE   B 7   ? 0.45917 0.41328 0.47401 0.01102  0.01950  -0.00349 6   PHE   B CE1 
1969 C  CE2 . PHE   B 7   ? 0.47826 0.42374 0.49380 0.02029  0.02299  -0.00398 6   PHE   B CE2 
1970 C  CZ  . PHE   B 7   ? 0.46781 0.42160 0.48351 0.01557  0.02142  -0.00511 6   PHE   B CZ  
1971 N  N   . TRP   B 8   ? 0.33182 0.28831 0.34719 0.01204  0.01427  0.00915  7   TRP   B N   
1972 C  CA  . TRP   B 8   ? 0.33066 0.29377 0.34639 0.00824  0.01258  0.00809  7   TRP   B CA  
1973 C  C   . TRP   B 8   ? 0.34954 0.31704 0.36496 0.00792  0.01022  0.01095  7   TRP   B C   
1974 O  O   . TRP   B 8   ? 0.31088 0.28090 0.32551 0.00492  0.00921  0.01011  7   TRP   B O   
1975 C  CB  . TRP   B 8   ? 0.33590 0.30585 0.35410 0.00835  0.01231  0.00602  7   TRP   B CB  
1976 C  CG  . TRP   B 8   ? 0.31580 0.29095 0.33706 0.01234  0.01218  0.00733  7   TRP   B CG  
1977 C  CD1 . TRP   B 8   ? 0.39632 0.37051 0.41876 0.01593  0.01430  0.00597  7   TRP   B CD1 
1978 C  CD2 . TRP   B 8   ? 0.29547 0.27851 0.31928 0.01311  0.00991  0.00994  7   TRP   B CD2 
1979 N  NE1 . TRP   B 8   ? 0.35525 0.33758 0.38145 0.01921  0.01359  0.00795  7   TRP   B NE1 
1980 C  CE2 . TRP   B 8   ? 0.34524 0.33331 0.37245 0.01709  0.01072  0.01045  7   TRP   B CE2 
1981 C  CE3 . TRP   B 8   ? 0.29854 0.28513 0.32202 0.01067  0.00730  0.01147  7   TRP   B CE3 
1982 C  CZ2 . TRP   B 8   ? 0.39022 0.38800 0.42114 0.01816  0.00880  0.01282  7   TRP   B CZ2 
1983 C  CZ3 . TRP   B 8   ? 0.31443 0.30919 0.34084 0.01144  0.00527  0.01339  7   TRP   B CZ3 
1984 C  CH2 . TRP   B 8   ? 0.34340 0.34427 0.37379 0.01484  0.00593  0.01420  7   TRP   B CH2 
1985 C  C10 . A1BC5 B 9   ? 0.33748 0.31847 0.35111 -0.00053 0.00369  0.00796  8   A1BC5 B C10 
1986 C  C13 . A1BC5 B 9   ? 0.29796 0.27316 0.31030 -0.00123 0.00740  0.00727  8   A1BC5 B C13 
1987 C  C02 . A1BC5 B 9   ? 0.27674 0.26397 0.29383 0.00155  0.00167  0.01059  8   A1BC5 B C02 
1988 C  C03 . A1BC5 B 9   ? 0.27608 0.26401 0.29367 0.00462  0.00189  0.01295  8   A1BC5 B C03 
1989 C  CB  . A1BC5 B 9   ? 0.29577 0.27700 0.31221 0.01005  0.00438  0.01637  8   A1BC5 B CB  
1990 C  CA  . A1BC5 B 9   ? 0.32485 0.29710 0.33873 0.01058  0.00691  0.01682  8   A1BC5 B CA  
1991 C  C   . A1BC5 B 9   ? 0.33139 0.30152 0.34392 0.01435  0.00668  0.02100  8   A1BC5 B C   
1992 C  C12 . A1BC5 B 9   ? 0.29477 0.27363 0.30807 -0.00148 0.00551  0.00651  8   A1BC5 B C12 
1993 N  N01 . A1BC5 B 9   ? 0.28243 0.26447 0.29866 0.00634  0.00416  0.01352  8   A1BC5 B N01 
1994 N  N   . A1BC5 B 9   ? 0.28521 0.25390 0.30080 0.01130  0.00914  0.01448  8   A1BC5 B N   
1995 N  N09 . A1BC5 B 9   ? 0.29723 0.28000 0.31315 0.00104  0.00372  0.00917  8   A1BC5 B N09 
1996 N  N15 . A1BC5 B 9   ? 0.33413 0.31348 0.34597 -0.00229 0.00519  0.00549  8   A1BC5 B N15 
1997 O  O   . A1BC5 B 9   ? 0.33484 0.30923 0.34590 0.01472  0.00459  0.02335  8   A1BC5 B O   
1998 O  O11 . A1BC5 B 9   ? 0.38450 0.36642 0.39661 -0.00106 0.00224  0.00784  8   A1BC5 B O11 
1999 O  O14 . A1BC5 B 9   ? 0.34773 0.34093 0.36688 0.00557  0.00014  0.01444  8   A1BC5 B O14 
2000 O  O16 . A1BC5 B 9   ? 0.26442 0.23862 0.27413 -0.00131 0.00750  0.00876  8   A1BC5 B O16 
2001 N  N   . GLY   B 10  ? 0.33288 0.29308 0.34380 0.01553  0.00937  0.02170  9   GLY   B N   
2002 C  CA  . GLY   B 10  ? 0.33486 0.29118 0.34379 0.01941  0.00933  0.02656  9   GLY   B CA  
2003 C  C   . GLY   B 10  ? 0.35808 0.32172 0.37003 0.02478  0.00730  0.02926  9   GLY   B C   
2004 O  O   . GLY   B 10  ? 0.35965 0.32903 0.37607 0.02647  0.00711  0.02712  9   GLY   B O   
2005 N  N   . SER   B 11  ? 0.36055 0.32505 0.37008 0.02752  0.00581  0.03429  10  SER   B N   
2006 C  CA  . SER   B 11  ? 0.39764 0.37136 0.41022 0.03269  0.00329  0.03740  10  SER   B CA  
2007 C  C   . SER   B 11  ? 0.40415 0.39100 0.41956 0.02962  0.00029  0.03492  10  SER   B C   
2008 O  O   . SER   B 11  ? 0.45213 0.44275 0.46435 0.02594  -0.00176 0.03480  10  SER   B O   
2009 C  CB  . SER   B 11  ? 0.40787 0.38063 0.41637 0.03586  0.00189  0.04369  10  SER   B CB  
2010 O  OG  . SER   B 11  ? 0.43599 0.39512 0.44202 0.03895  0.00481  0.04663  10  SER   B OG  
2011 N  N   . HIS   B 12  ? 0.32730 0.32081 0.34838 0.03090  0.00024  0.03278  11  HIS   B N   
2012 C  CA  . HIS   B 12  ? 0.30294 0.30674 0.32688 0.02672  -0.00193 0.02998  11  HIS   B CA  
2013 C  C   . HIS   B 12  ? 0.34479 0.36185 0.37414 0.02996  -0.00433 0.03205  11  HIS   B C   
2014 O  O   . HIS   B 12  ? 0.35866 0.37764 0.39219 0.03534  -0.00285 0.03317  11  HIS   B O   
2015 C  CB  . HIS   B 12  ? 0.29322 0.29430 0.31907 0.02369  0.00037  0.02550  11  HIS   B CB  
2016 C  CG  . HIS   B 12  ? 0.27388 0.28210 0.30129 0.01852  -0.00150 0.02301  11  HIS   B CG  
2017 N  ND1 . HIS   B 12  ? 0.29581 0.30176 0.31939 0.01386  -0.00279 0.02148  11  HIS   B ND1 
2018 C  CD2 . HIS   B 12  ? 0.30278 0.31980 0.33505 0.01727  -0.00209 0.02191  11  HIS   B CD2 
2019 C  CE1 . HIS   B 12  ? 0.29953 0.31097 0.32526 0.01009  -0.00421 0.01951  11  HIS   B CE1 
2020 N  NE2 . HIS   B 12  ? 0.29118 0.30961 0.32220 0.01162  -0.00386 0.02000  11  HIS   B NE2 
2021 N  N   . ARG   B 13  ? 0.33609 0.36273 0.36543 0.02668  -0.00797 0.03224  12  ARG   B N   
2022 C  CA  . ARG   B 13  ? 0.33837 0.38016 0.37360 0.02802  -0.01072 0.03364  12  ARG   B CA  
2023 C  C   . ARG   B 13  ? 0.32818 0.37489 0.36820 0.02386  -0.00988 0.03004  12  ARG   B C   
2024 O  O   . ARG   B 13  ? 0.30780 0.35452 0.34627 0.01735  -0.01112 0.02723  12  ARG   B O   
2025 C  CB  . ARG   B 13  ? 0.34816 0.39813 0.38081 0.02530  -0.01517 0.03486  12  ARG   B CB  
2026 C  CG  . ARG   B 13  ? 0.39099 0.45836 0.42998 0.02680  -0.01850 0.03684  12  ARG   B CG  
2027 C  CD  . ARG   B 13  ? 0.36646 0.44237 0.40309 0.02084  -0.02304 0.03553  12  ARG   B CD  
2028 N  NE  . ARG   B 13  ? 0.34639 0.42049 0.38333 0.01304  -0.02291 0.03053  12  ARG   B NE  
2029 C  CZ  . ARG   B 13  ? 0.39784 0.46347 0.42841 0.00786  -0.02322 0.02719  12  ARG   B CZ  
2030 N  NH1 . ARG   B 13  ? 0.32803 0.38797 0.35127 0.00891  -0.02376 0.02799  12  ARG   B NH1 
2031 N  NH2 . ARG   B 13  ? 0.33248 0.39526 0.36392 0.00179  -0.02274 0.02317  12  ARG   B NH2 
2032 N  N   . GLN   B 14  ? 0.35048 0.40064 0.39590 0.02774  -0.00747 0.03013  13  GLN   B N   
2033 C  CA  . GLN   B 14  ? 0.32600 0.37902 0.37480 0.02389  -0.00573 0.02703  13  GLN   B CA  
2034 C  C   . GLN   B 14  ? 0.37356 0.44342 0.42898 0.02153  -0.00807 0.02773  13  GLN   B C   
2035 O  O   . GLN   B 14  ? 0.39242 0.47128 0.45391 0.02385  -0.00632 0.02797  13  GLN   B O   
2036 C  CB  . GLN   B 14  ? 0.37868 0.42642 0.42883 0.02846  -0.00140 0.02591  13  GLN   B CB  
2037 C  CG  . GLN   B 14  ? 0.36624 0.41314 0.41686 0.02378  0.00068  0.02261  13  GLN   B CG  
2038 C  CD  . GLN   B 14  ? 0.43416 0.47334 0.48366 0.02735  0.00485  0.02050  13  GLN   B CD  
2039 O  OE1 . GLN   B 14  ? 0.48495 0.52719 0.53759 0.03363  0.00685  0.02103  13  GLN   B OE1 
2040 N  NE2 . GLN   B 14  ? 0.37890 0.40830 0.42383 0.02362  0.00615  0.01785  13  GLN   B NE2 
2041 N  N   . CYS   B 15  ? 0.34294 0.41734 0.39696 0.01648  -0.01195 0.02774  14  CYS   B N   
2042 C  CA  . CYS   B 15  ? 0.30596 0.39637 0.36582 0.01262  -0.01483 0.02816  14  CYS   B CA  
2043 C  C   . CYS   B 15  ? 0.35771 0.44761 0.41337 0.00559  -0.01877 0.02653  14  CYS   B C   
2044 O  O   . CYS   B 15  ? 0.36662 0.46677 0.42572 -0.00030 -0.02134 0.02569  14  CYS   B O   
2045 C  CB  . CYS   B 15  ? 0.33910 0.44388 0.40491 0.01929  -0.01621 0.03187  14  CYS   B CB  
2046 S  SG  . CYS   B 15  ? 0.42608 0.52591 0.48624 0.02567  -0.01844 0.03538  14  CYS   B SG  
2047 N  N   . NH2   B 16  ? 0.31816 0.39752 0.36604 0.00685  -0.01964 0.02644  15  NH2   B N   
2048 CO CO  . CO    C .   ? 0.24657 0.22431 0.25471 -0.00269 0.00698  0.00671  301 CO    A CO  
2049 CL CL  . CL    D .   ? 0.52141 0.59339 0.36843 -0.01496 -0.02274 -0.03736 302 CL    A CL  
2050 CL CL  . CL    E .   ? 0.91750 0.96792 0.86159 -0.04588 0.00933  -0.08252 303 CL    A CL  
2051 C  C1  . GOL   F .   ? 0.47124 0.47537 0.48567 -0.02364 -0.01773 0.00188  304 GOL   A C1  
2052 O  O1  . GOL   F .   ? 0.58521 0.58762 0.59584 -0.01920 -0.01668 0.00187  304 GOL   A O1  
2053 C  C2  . GOL   F .   ? 0.52652 0.52376 0.53647 -0.02814 -0.01954 -0.00240 304 GOL   A C2  
2054 O  O2  . GOL   F .   ? 0.52493 0.51086 0.53277 -0.02751 -0.01752 -0.00373 304 GOL   A O2  
2055 C  C3  . GOL   F .   ? 0.60181 0.60514 0.61563 -0.03451 -0.02211 -0.00240 304 GOL   A C3  
2056 O  O3  . GOL   F .   ? 0.68954 0.69072 0.70760 -0.03584 -0.02023 -0.00003 304 GOL   A O3  
2057 C  C1  . GOL   G .   ? 0.65319 0.70522 0.66907 -0.01600 0.01823  0.02504  305 GOL   A C1  
2058 O  O1  . GOL   G .   ? 0.54945 0.60068 0.57044 -0.01433 0.01802  0.02227  305 GOL   A O1  
2059 C  C2  . GOL   G .   ? 0.60259 0.64493 0.61753 -0.01855 0.01502  0.02885  305 GOL   A C2  
2060 O  O2  . GOL   G .   ? 0.46952 0.50331 0.48534 -0.01646 0.01270  0.02581  305 GOL   A O2  
2061 C  C3  . GOL   G .   ? 0.49625 0.53914 0.50508 -0.01896 0.01492  0.03193  305 GOL   A C3  
2062 O  O3  . GOL   G .   ? 0.60371 0.63696 0.61152 -0.01982 0.01210  0.03499  305 GOL   A O3  
2063 C  C1  . GOL   H .   ? 0.47636 0.48702 0.49419 0.00539  0.01226  -0.00406 306 GOL   A C1  
2064 O  O1  . GOL   H .   ? 0.43434 0.44276 0.45087 0.00091  0.01285  -0.00273 306 GOL   A O1  
2065 C  C2  . GOL   H .   ? 0.46142 0.48053 0.48030 0.00685  0.01490  -0.00527 306 GOL   A C2  
2066 O  O2  . GOL   H .   ? 0.51234 0.54014 0.53501 0.00348  0.01625  -0.00452 306 GOL   A O2  
2067 C  C3  . GOL   H .   ? 0.45893 0.47972 0.47929 0.01299  0.01445  -0.00687 306 GOL   A C3  
2068 O  O3  . GOL   H .   ? 0.52178 0.55119 0.54312 0.01492  0.01727  -0.00832 306 GOL   A O3  
2069 C  C1  . GOL   I .   ? 0.65599 0.75992 0.47809 -0.00236 -0.00325 0.02424  307 GOL   A C1  
2070 O  O1  . GOL   I .   ? 0.68559 0.79307 0.50031 -0.00305 0.00169  0.01685  307 GOL   A O1  
2071 C  C2  . GOL   I .   ? 0.78641 0.88551 0.61290 -0.00132 0.00073  0.03694  307 GOL   A C2  
2072 O  O2  . GOL   I .   ? 0.84786 0.94435 0.67556 -0.00220 0.00798  0.03597  307 GOL   A O2  
2073 C  C3  . GOL   I .   ? 0.87419 0.98248 0.68943 -0.00037 -0.00152 0.04739  307 GOL   A C3  
2074 O  O3  . GOL   I .   ? 0.89882 1.01485 0.70234 -0.00147 0.00326  0.04751  307 GOL   A O3  
2075 C  C1  . GOL   J .   ? 0.73293 0.65497 0.71789 0.02585  0.00471  -0.02780 308 GOL   A C1  
2076 O  O1  . GOL   J .   ? 0.75333 0.68373 0.74378 0.03004  0.00592  -0.02411 308 GOL   A O1  
2077 C  C2  . GOL   J .   ? 0.82021 0.72631 0.80360 0.02583  0.00318  -0.02790 308 GOL   A C2  
2078 O  O2  . GOL   J .   ? 0.73038 0.63492 0.71590 0.02010  0.00088  -0.02347 308 GOL   A O2  
2079 C  C3  . GOL   J .   ? 0.81356 0.70951 0.78991 0.02470  0.00314  -0.03488 308 GOL   A C3  
2080 O  O3  . GOL   J .   ? 0.85139 0.73106 0.82600 0.02521  0.00226  -0.03543 308 GOL   A O3  
2081 O  O   . HOH   K .   ? 0.54618 0.51668 0.56026 0.00484  0.01838  -0.00882 401 HOH   A O   
2082 O  O   . HOH   K .   ? 0.63036 0.75179 0.63611 -0.02509 -0.01735 -0.01561 402 HOH   A O   
2083 O  O   . HOH   K .   ? 0.58501 0.55695 0.55750 -0.00769 0.01861  0.03550  403 HOH   A O   
2084 O  O   . HOH   K .   ? 0.56900 0.66719 0.57035 -0.04758 -0.01052 -0.03970 404 HOH   A O   
2085 O  O   . HOH   K .   ? 0.86147 0.89806 0.76543 -0.01814 0.03955  0.05961  405 HOH   A O   
2086 O  O   . HOH   K .   ? 0.59965 0.56667 0.62727 -0.06949 -0.01361 0.01688  406 HOH   A O   
2087 O  O   . HOH   K .   ? 0.61979 0.67070 0.68266 -0.10228 -0.01718 0.02388  407 HOH   A O   
2088 O  O   . HOH   K .   ? 0.50133 0.56163 0.54965 -0.05792 -0.02648 0.00859  408 HOH   A O   
2089 O  O   . HOH   K .   ? 0.71935 0.70604 0.64521 0.01093  0.01093  -0.04921 409 HOH   A O   
2090 O  O   . HOH   K .   ? 0.33520 0.35489 0.36244 0.01178  0.02073  -0.00122 410 HOH   A O   
2091 O  O   . HOH   K .   ? 0.45411 0.48127 0.46657 0.01323  0.02088  -0.01003 411 HOH   A O   
2092 O  O   . HOH   K .   ? 0.56476 0.57206 0.56628 -0.02011 -0.02075 -0.00152 412 HOH   A O   
2093 O  O   . HOH   K .   ? 0.44144 0.55498 0.49284 -0.01923 -0.00200 -0.00955 413 HOH   A O   
2094 O  O   . HOH   K .   ? 0.41357 0.51074 0.46238 -0.01455 -0.02933 0.02001  414 HOH   A O   
2095 O  O   . HOH   K .   ? 0.44884 0.48486 0.47324 -0.00854 0.02075  -0.00203 415 HOH   A O   
2096 O  O   . HOH   K .   ? 0.70216 0.82126 0.50665 0.00859  -0.01427 0.08627  416 HOH   A O   
2097 O  O   . HOH   K .   ? 0.46211 0.46807 0.46840 0.00516  -0.00461 0.02786  417 HOH   A O   
2098 O  O   . HOH   K .   ? 0.49340 0.53449 0.47304 -0.00471 -0.02730 0.01413  418 HOH   A O   
2099 O  O   . HOH   K .   ? 0.69547 0.82149 0.47827 0.00209  0.02856  -0.03189 419 HOH   A O   
2100 O  O   . HOH   K .   ? 0.51790 0.49891 0.49760 -0.01278 0.02215  0.02660  420 HOH   A O   
2101 O  O   . HOH   K .   ? 0.53251 0.53074 0.50411 -0.00804 -0.01260 -0.00518 421 HOH   A O   
2102 O  O   . HOH   K .   ? 0.29578 0.28154 0.31699 -0.02065 -0.00076 0.02069  422 HOH   A O   
2103 O  O   . HOH   K .   ? 0.65007 0.53658 0.65251 0.04037  0.02320  0.03350  423 HOH   A O   
2104 O  O   . HOH   K .   ? 0.39335 0.37922 0.37417 -0.00768 -0.00925 -0.00735 424 HOH   A O   
2105 O  O   . HOH   K .   ? 0.45544 0.39149 0.45309 -0.02200 -0.01162 -0.00935 425 HOH   A O   
2106 O  O   . HOH   K .   ? 0.38660 0.31239 0.39210 -0.00918 -0.00546 0.01603  426 HOH   A O   
2107 O  O   . HOH   K .   ? 0.40533 0.43981 0.43485 0.00260  0.01279  -0.00378 427 HOH   A O   
2108 O  O   . HOH   K .   ? 0.61692 0.51992 0.61064 0.00871  0.03512  -0.03960 428 HOH   A O   
2109 O  O   . HOH   K .   ? 0.40065 0.39273 0.40862 0.01912  0.01109  -0.01142 429 HOH   A O   
2110 O  O   . HOH   K .   ? 0.40186 0.42095 0.41740 -0.02265 0.00879  0.03419  430 HOH   A O   
2111 O  O   . HOH   K .   ? 0.31609 0.37023 0.34622 -0.00829 0.01888  0.01646  431 HOH   A O   
2112 O  O   . HOH   K .   ? 0.43002 0.39483 0.43971 0.01104  -0.00455 0.02472  432 HOH   A O   
2113 O  O   . HOH   K .   ? 0.50402 0.57612 0.51029 0.00303  -0.03310 0.02654  433 HOH   A O   
2114 O  O   . HOH   K .   ? 0.36917 0.32930 0.35979 0.00262  -0.00018 -0.01406 434 HOH   A O   
2115 O  O   . HOH   K .   ? 0.44936 0.43483 0.46371 -0.00710 0.00977  0.00136  435 HOH   A O   
2116 O  O   . HOH   K .   ? 0.61192 0.61690 0.52142 -0.01418 -0.01599 -0.04450 436 HOH   A O   
2117 O  O   . HOH   K .   ? 0.43673 0.45700 0.36507 0.00293  -0.00031 0.03797  437 HOH   A O   
2118 O  O   . HOH   K .   ? 0.51538 0.51288 0.52677 -0.03493 0.00661  0.05036  438 HOH   A O   
2119 O  O   . HOH   K .   ? 0.47320 0.41164 0.48100 -0.01836 -0.00391 0.03056  439 HOH   A O   
2120 O  O   . HOH   K .   ? 0.52526 0.52312 0.55090 0.04030  0.00130  0.00562  440 HOH   A O   
2121 O  O   . HOH   K .   ? 0.62936 0.76252 0.71354 -0.00768 -0.01160 0.02700  441 HOH   A O   
2122 O  O   . HOH   K .   ? 0.51354 0.48710 0.51313 -0.02677 0.00290  0.05950  442 HOH   A O   
2123 O  O   . HOH   K .   ? 0.66566 0.66319 0.69580 -0.07181 -0.02388 0.00233  443 HOH   A O   
2124 O  O   . HOH   K .   ? 0.52206 0.43278 0.51717 -0.04197 0.02608  -0.03905 444 HOH   A O   
2125 O  O   . HOH   K .   ? 0.28328 0.29822 0.31708 -0.01990 -0.00002 0.01767  445 HOH   A O   
2126 O  O   . HOH   K .   ? 0.43237 0.48075 0.42995 -0.05289 0.00039  -0.04913 446 HOH   A O   
2127 O  O   . HOH   K .   ? 0.57748 0.65048 0.57497 0.00083  -0.01184 0.01776  447 HOH   A O   
2128 O  O   . HOH   K .   ? 0.53666 0.66074 0.59702 -0.02367 0.00395  -0.01014 448 HOH   A O   
2129 O  O   . HOH   K .   ? 0.31034 0.28878 0.32161 -0.00481 0.00888  0.00441  449 HOH   A O   
2130 O  O   . HOH   K .   ? 0.60741 0.63753 0.51194 -0.01733 -0.02398 -0.03346 450 HOH   A O   
2131 O  O   . HOH   K .   ? 0.43768 0.48037 0.40689 -0.01772 0.01578  -0.04088 451 HOH   A O   
2132 O  O   . HOH   K .   ? 0.54055 0.60646 0.54811 0.01407  0.03640  -0.01290 452 HOH   A O   
2133 O  O   . HOH   K .   ? 0.60891 0.66330 0.61550 0.02633  0.03331  -0.01984 453 HOH   A O   
2134 O  O   . HOH   K .   ? 0.52229 0.58572 0.39152 -0.00157 0.00866  0.03524  454 HOH   A O   
2135 O  O   . HOH   K .   ? 0.43490 0.35027 0.43842 -0.04267 0.02745  -0.00856 455 HOH   A O   
2136 O  O   . HOH   K .   ? 0.58540 0.62045 0.51700 0.00911  -0.01458 0.04430  456 HOH   A O   
2137 O  O   . HOH   K .   ? 0.41647 0.38135 0.40352 -0.02392 0.02800  0.02968  457 HOH   A O   
2138 O  O   . HOH   K .   ? 0.62694 0.51963 0.63029 0.01858  0.02578  0.01129  458 HOH   A O   
2139 O  O   . HOH   K .   ? 0.54272 0.60824 0.43048 0.01443  -0.01955 0.06991  459 HOH   A O   
2140 O  O   . HOH   K .   ? 0.38546 0.38630 0.38116 0.00005  0.02473  -0.02981 460 HOH   A O   
2141 O  O   . HOH   K .   ? 0.63868 0.72107 0.65777 -0.07675 -0.00384 -0.05145 461 HOH   A O   
2142 O  O   . HOH   K .   ? 0.46280 0.51623 0.48559 0.00405  0.02620  -0.00625 462 HOH   A O   
2143 O  O   . HOH   K .   ? 0.49428 0.53080 0.52757 -0.03629 -0.02238 0.00697  463 HOH   A O   
2144 O  O   . HOH   K .   ? 0.47597 0.61063 0.56618 -0.06535 -0.00959 0.03002  464 HOH   A O   
2145 O  O   . HOH   K .   ? 0.83810 0.79440 0.82604 -0.05689 0.04390  0.04062  465 HOH   A O   
2146 O  O   . HOH   K .   ? 0.41939 0.48458 0.46927 -0.04067 -0.02198 0.01287  466 HOH   A O   
2147 O  O   . HOH   K .   ? 0.52174 0.48570 0.53834 0.04055  -0.00287 0.01516  467 HOH   A O   
2148 O  O   . HOH   K .   ? 0.54440 0.48006 0.56286 -0.06765 -0.01216 0.01877  468 HOH   A O   
2149 O  O   . HOH   K .   ? 0.40235 0.39846 0.41030 -0.00154 0.01250  -0.00051 469 HOH   A O   
2150 O  O   . HOH   K .   ? 0.39847 0.39258 0.41135 -0.00066 0.00953  -0.00086 470 HOH   A O   
2151 O  O   . HOH   K .   ? 0.50742 0.57012 0.50431 -0.01721 -0.03661 0.00787  471 HOH   A O   
2152 O  O   . HOH   K .   ? 0.57160 0.47691 0.57329 0.02528  -0.00386 0.01443  472 HOH   A O   
2153 O  O   . HOH   K .   ? 0.37976 0.38169 0.36073 0.01262  -0.00790 0.03628  473 HOH   A O   
2154 O  O   . HOH   K .   ? 0.51377 0.61611 0.56986 -0.04413 0.01270  -0.01279 474 HOH   A O   
2155 O  O   . HOH   K .   ? 0.63036 0.65255 0.56291 -0.00927 0.02713  0.03313  475 HOH   A O   
2156 O  O   . HOH   K .   ? 0.38264 0.38492 0.40326 0.01083  -0.00046 0.00741  476 HOH   A O   
2157 O  O   . HOH   K .   ? 0.63130 0.59289 0.62925 -0.02808 -0.01658 -0.01142 477 HOH   A O   
2158 O  O   . HOH   K .   ? 0.41490 0.33410 0.41741 -0.02763 -0.01047 0.00153  478 HOH   A O   
2159 O  O   . HOH   K .   ? 0.56426 0.55782 0.56584 0.03845  0.01840  -0.02477 479 HOH   A O   
2160 O  O   . HOH   K .   ? 0.46146 0.49891 0.46298 -0.06620 0.00266  -0.05566 480 HOH   A O   
2161 O  O   . HOH   K .   ? 0.47320 0.50521 0.49233 0.01268  0.02788  -0.00908 481 HOH   A O   
2162 O  O   . HOH   K .   ? 0.52149 0.53715 0.53251 0.02377  -0.01062 0.03689  482 HOH   A O   
2163 O  O   . HOH   K .   ? 0.34363 0.39695 0.32993 -0.01345 0.00353  -0.00877 483 HOH   A O   
2164 O  O   . HOH   K .   ? 0.59571 0.58320 0.58630 0.00602  0.03165  -0.04198 484 HOH   A O   
2165 O  O   . HOH   K .   ? 0.49250 0.43977 0.49659 0.00288  -0.00484 0.03609  485 HOH   A O   
2166 O  O   . HOH   K .   ? 0.40100 0.37239 0.41559 -0.00267 0.01294  -0.00219 486 HOH   A O   
2167 O  O   . HOH   K .   ? 0.68587 0.64609 0.70617 -0.06731 0.00103  0.05247  487 HOH   A O   
2168 O  O   . HOH   K .   ? 0.53303 0.48580 0.54634 0.03898  -0.00009 0.00608  488 HOH   A O   
2169 O  O   . HOH   K .   ? 0.66692 0.69774 0.68117 0.01634  -0.00935 0.02458  489 HOH   A O   
2170 O  O   . HOH   K .   ? 0.52758 0.51524 0.54814 0.03825  0.00501  -0.00232 490 HOH   A O   
2171 O  O   . HOH   K .   ? 0.45275 0.45449 0.43243 -0.01351 0.02612  0.01921  491 HOH   A O   
2172 O  O   . HOH   K .   ? 0.50540 0.53197 0.50556 0.02096  -0.01649 0.03954  492 HOH   A O   
2173 O  O   . HOH   K .   ? 0.55345 0.48258 0.53121 0.00621  0.01705  0.05074  493 HOH   A O   
2174 O  O   . HOH   K .   ? 0.51773 0.53195 0.53077 -0.04196 0.03426  0.01370  494 HOH   A O   
2175 O  O   . HOH   K .   ? 0.58928 0.76776 0.67564 -0.09272 0.01566  -0.02127 495 HOH   A O   
2176 O  O   . HOH   K .   ? 0.52614 0.56400 0.51509 -0.01717 0.03729  0.01255  496 HOH   A O   
2177 O  O   . HOH   K .   ? 0.55253 0.60471 0.51464 -0.02498 0.01180  -0.04853 497 HOH   A O   
2178 O  O   . HOH   K .   ? 0.40858 0.41749 0.43929 -0.02623 0.00102  0.02269  498 HOH   A O   
2179 O  O   . HOH   K .   ? 0.76570 0.69743 0.77423 0.02176  0.03038  -0.01975 499 HOH   A O   
2180 O  O   . HOH   K .   ? 0.70464 0.80799 0.47177 -0.01012 -0.00482 -0.07582 500 HOH   A O   
2181 O  O   . HOH   K .   ? 0.53913 0.42753 0.52892 -0.02029 -0.01034 -0.01093 501 HOH   A O   
2182 O  O   . HOH   K .   ? 0.42683 0.50077 0.40493 -0.01494 -0.00104 -0.00742 502 HOH   A O   
2183 O  O   . HOH   K .   ? 0.55044 0.48125 0.53197 0.00810  0.03907  -0.06102 503 HOH   A O   
2184 O  O   . HOH   K .   ? 0.61357 0.64023 0.62184 0.03899  0.02563  -0.02409 504 HOH   A O   
2185 O  O   . HOH   K .   ? 0.43713 0.58341 0.50847 -0.04986 0.01057  -0.01471 505 HOH   A O   
2186 O  O   . HOH   K .   ? 0.50227 0.61736 0.53666 -0.00007 -0.01483 0.00312  506 HOH   A O   
2187 O  O   . HOH   K .   ? 0.53447 0.66472 0.41409 0.00340  -0.05117 0.04038  507 HOH   A O   
2188 O  O   . HOH   K .   ? 0.52032 0.59785 0.56287 0.01264  -0.00311 0.00357  508 HOH   A O   
2189 O  O   . HOH   K .   ? 0.48747 0.43081 0.48948 0.01080  0.03009  -0.03052 509 HOH   A O   
2190 O  O   . HOH   K .   ? 0.32670 0.31124 0.33547 0.00245  0.00057  0.01328  510 HOH   A O   
2191 O  O   . HOH   K .   ? 0.50926 0.50076 0.46780 -0.00794 -0.01007 -0.01672 511 HOH   A O   
2192 O  O   . HOH   K .   ? 0.38133 0.41026 0.38665 0.00969  0.03014  -0.01910 512 HOH   A O   
2193 O  O   . HOH   K .   ? 0.73473 0.60392 0.72487 0.01998  -0.00300 -0.00352 513 HOH   A O   
2194 O  O   . HOH   K .   ? 0.56924 0.51443 0.57419 0.04358  0.00664  -0.01340 514 HOH   A O   
2195 O  O   . HOH   K .   ? 0.37961 0.35136 0.40509 -0.04908 -0.00721 0.02295  515 HOH   A O   
2196 O  O   . HOH   K .   ? 0.45277 0.58404 0.52683 -0.01835 -0.02539 0.02415  516 HOH   A O   
2197 O  O   . HOH   K .   ? 0.48590 0.50319 0.48143 0.00168  -0.00439 0.03955  517 HOH   A O   
2198 O  O   . HOH   K .   ? 0.65287 0.50606 0.63937 -0.02780 0.03514  -0.03765 518 HOH   A O   
2199 O  O   . HOH   K .   ? 0.53841 0.42613 0.52110 0.00046  0.03843  -0.05658 519 HOH   A O   
2200 O  O   . HOH   K .   ? 0.50752 0.49033 0.49610 -0.01400 -0.01362 -0.00881 520 HOH   A O   
2201 O  O   . HOH   K .   ? 0.46257 0.47601 0.45257 -0.00393 -0.01631 0.01063  521 HOH   A O   
2202 O  O   . HOH   K .   ? 0.36002 0.35605 0.37663 -0.00557 0.01005  -0.00022 522 HOH   A O   
2203 O  O   . HOH   K .   ? 0.45629 0.51378 0.50852 -0.02327 0.00254  0.02248  523 HOH   A O   
2204 O  O   . HOH   K .   ? 0.70601 0.81978 0.77303 -0.11825 0.02059  -0.02684 524 HOH   A O   
2205 O  O   . HOH   K .   ? 0.52367 0.56324 0.54887 0.01832  -0.00714 0.01512  525 HOH   A O   
2206 O  O   . HOH   K .   ? 0.61143 0.59307 0.61473 0.00384  -0.00454 0.03798  526 HOH   A O   
2207 O  O   . HOH   K .   ? 0.72849 0.65221 0.71294 0.03384  0.01070  0.06270  527 HOH   A O   
2208 O  O   . HOH   K .   ? 0.58579 0.60167 0.63142 -0.07363 -0.01055 0.02492  528 HOH   A O   
2209 O  O   . HOH   K .   ? 0.56285 0.56026 0.58743 -0.08944 0.01992  -0.03320 529 HOH   A O   
2210 O  O   . HOH   K .   ? 0.71720 0.81185 0.71830 -0.00212 0.04954  -0.00309 530 HOH   A O   
2211 O  O   . HOH   K .   ? 0.51992 0.50441 0.54645 -0.04314 -0.00229 0.02983  531 HOH   A O   
2212 O  O   . HOH   K .   ? 0.55346 0.65100 0.38389 -0.01964 -0.03392 -0.03554 532 HOH   A O   
2213 O  O   . HOH   K .   ? 0.74340 0.64233 0.73458 -0.03042 0.03151  0.02564  533 HOH   A O   
2214 O  O   . HOH   K .   ? 0.89817 0.93696 0.73940 0.01492  0.02409  -0.08292 534 HOH   A O   
2215 O  O   . HOH   K .   ? 0.65873 0.71342 0.69081 0.02652  -0.00847 0.01618  535 HOH   A O   
2216 O  O   . HOH   K .   ? 0.57725 0.65361 0.58079 -0.05328 -0.00543 -0.04463 536 HOH   A O   
2217 O  O   . HOH   K .   ? 0.46362 0.56049 0.50890 -0.00485 -0.00362 -0.00335 537 HOH   A O   
2218 O  O   . HOH   K .   ? 0.79771 0.84543 0.76589 -0.02169 0.04541  0.02323  538 HOH   A O   
2219 O  O   . HOH   K .   ? 0.52470 0.33844 0.50370 -0.02269 0.04115  -0.04253 539 HOH   A O   
2220 O  O   . HOH   K .   ? 0.55148 0.62551 0.61085 -0.01269 0.00470  0.02151  540 HOH   A O   
2221 O  O   . HOH   K .   ? 0.75520 0.84352 0.59949 -0.01436 0.04331  0.06396  541 HOH   A O   
2222 O  O   . HOH   K .   ? 0.65469 0.72665 0.66284 0.01561  -0.01631 0.02882  542 HOH   A O   
2223 O  O   . HOH   K .   ? 0.69308 0.85024 0.76617 -0.06478 0.00650  -0.02091 543 HOH   A O   
2224 O  O   . HOH   K .   ? 0.80671 0.66669 0.79885 -0.03178 0.03390  0.00238  544 HOH   A O   
2225 O  O   . HOH   K .   ? 0.71656 0.63809 0.71336 0.05445  0.00999  0.06411  545 HOH   A O   
2226 O  O   . HOH   K .   ? 0.68050 0.72702 0.74636 -0.11945 -0.01033 0.03668  546 HOH   A O   
2227 O  O   . HOH   K .   ? 0.74301 0.65181 0.72094 -0.01417 0.02794  0.04713  547 HOH   A O   
2228 O  O   . HOH   K .   ? 0.54635 0.60398 0.46435 0.00841  -0.02328 0.04338  548 HOH   A O   
2229 O  O   . HOH   K .   ? 0.79072 0.71874 0.76139 -0.00496 0.02265  0.05409  549 HOH   A O   
2230 O  O   . HOH   K .   ? 0.58691 0.80638 0.68459 -0.08724 0.00786  -0.02364 550 HOH   A O   
2231 O  O   . HOH   K .   ? 0.56912 0.57310 0.56354 0.01801  -0.00900 0.03743  551 HOH   A O   
2232 O  O   . HOH   K .   ? 0.61911 0.71845 0.61352 -0.00599 -0.01544 0.00797  552 HOH   A O   
2233 O  O   . HOH   K .   ? 0.68245 0.72334 0.57289 0.01165  -0.00583 0.07629  553 HOH   A O   
2234 O  O   . HOH   K .   ? 0.55546 0.59404 0.59785 0.02276  0.02183  0.00415  554 HOH   A O   
2235 O  O   . HOH   K .   ? 0.89139 0.89093 0.74198 0.01828  0.02033  -0.10144 555 HOH   A O   
2236 O  O   . HOH   K .   ? 0.54204 0.53302 0.56817 -0.03196 -0.00151 0.02476  556 HOH   A O   
2237 O  O   . HOH   K .   ? 0.60705 0.67676 0.64823 0.02837  -0.00581 0.01096  557 HOH   A O   
2238 O  O   . HOH   K .   ? 0.54868 0.60300 0.56731 0.01530  0.02803  -0.01138 558 HOH   A O   
2239 O  O   . HOH   K .   ? 0.93281 1.11282 0.86563 -0.04833 -0.02428 -0.05104 559 HOH   A O   
2240 O  O   . HOH   K .   ? 0.57620 0.59734 0.59351 -0.03233 0.01003  0.04319  560 HOH   A O   
2241 O  O   . HOH   K .   ? 0.74588 0.67919 0.73892 -0.04878 0.03697  0.03005  561 HOH   A O   
2242 O  O   . HOH   K .   ? 0.54622 0.55600 0.57780 0.01909  0.01953  0.00084  562 HOH   A O   
2243 O  O   . HOH   K .   ? 0.71564 0.64622 0.71141 0.01459  0.03545  -0.04129 563 HOH   A O   
2244 O  O   . HOH   K .   ? 0.62764 0.65511 0.60439 -0.01208 -0.02555 0.00215  564 HOH   A O   
2245 O  O   . HOH   K .   ? 0.69820 0.68284 0.69154 0.03135  -0.00415 0.05220  565 HOH   A O   
2246 O  O   . HOH   K .   ? 0.49885 0.49423 0.53320 -0.05577 -0.01054 0.01903  566 HOH   A O   
2247 O  O   . HOH   K .   ? 0.91422 1.01881 0.75378 0.02848  -0.03088 0.11547  567 HOH   A O   
2248 O  O   . HOH   K .   ? 0.80843 0.90283 0.76700 0.02795  0.05704  -0.03150 568 HOH   A O   
2249 O  O   . HOH   K .   ? 0.68720 0.73803 0.64095 0.01543  -0.02646 0.04696  569 HOH   A O   
2250 O  O   . HOH   K .   ? 0.68207 0.69018 0.61641 -0.00709 0.02099  0.04228  570 HOH   A O   
2251 O  O   . HOH   K .   ? 0.67413 0.65001 0.69056 0.05075  0.00863  -0.00978 571 HOH   A O   
2252 O  O   . HOH   K .   ? 0.65332 0.64151 0.66449 0.04998  0.01565  -0.02071 572 HOH   A O   
2253 O  O   . HOH   K .   ? 0.84364 0.96340 0.76091 -0.00564 -0.05445 0.02268  573 HOH   A O   
2254 O  O   . HOH   K .   ? 0.50460 0.51551 0.48806 -0.00995 -0.01868 0.00172  574 HOH   A O   
2255 O  O   . HOH   K .   ? 0.47277 0.64245 0.55442 -0.06895 0.01415  -0.01687 575 HOH   A O   
2256 O  O   . HOH   K .   ? 0.76029 0.72707 0.72204 0.00813  0.00490  -0.03281 576 HOH   A O   
2257 O  O   . HOH   K .   ? 0.52162 0.57042 0.54817 0.02065  0.03337  -0.00906 577 HOH   A O   
2258 O  O   . HOH   K .   ? 0.61817 0.62114 0.60569 -0.01672 -0.02005 -0.00535 578 HOH   A O   
2259 O  O   . HOH   K .   ? 0.81345 0.83161 0.79335 -0.03618 -0.03431 -0.01856 579 HOH   A O   
2260 O  O   . HOH   K .   ? 0.57122 0.44554 0.55400 0.01836  0.04481  -0.05849 580 HOH   A O   
2261 O  O   . HOH   K .   ? 0.71932 0.80121 0.71590 0.01737  -0.03613 0.04200  581 HOH   A O   
2262 O  O   . HOH   K .   ? 0.61731 0.71744 0.66945 0.01849  0.03418  0.00653  582 HOH   A O   
2263 O  O   . HOH   K .   ? 0.77933 0.99107 0.67637 -0.06607 -0.02828 -0.08168 583 HOH   A O   
2264 O  O   . HOH   K .   ? 0.88000 0.88833 0.89614 0.02810  0.03576  -0.02324 584 HOH   A O   
2265 O  O   . HOH   K .   ? 0.62995 0.80130 0.37056 -0.00511 0.03232  0.02508  585 HOH   A O   
2266 O  O   . HOH   K .   ? 0.85832 0.81821 0.85369 0.07974  0.02523  -0.04374 586 HOH   A O   
2267 O  O   . HOH   K .   ? 0.82718 1.02138 0.78858 -0.02371 -0.03377 -0.00816 587 HOH   A O   
2268 O  O   . HOH   L .   ? 0.51978 0.50706 0.52210 0.01900  -0.00224 0.03422  101 HOH   B O   
2269 O  O   . HOH   L .   ? 0.30815 0.28304 0.31676 0.00259  0.00558  0.01337  102 HOH   B O   
2270 O  O   . HOH   L .   ? 0.61175 0.56982 0.61865 0.05316  0.00348  0.05738  103 HOH   B O   
2271 O  O   . HOH   L .   ? 0.30584 0.29782 0.31865 0.01413  -0.00147 0.02424  104 HOH   B O   
2272 O  O   . HOH   L .   ? 0.50187 0.55997 0.51724 0.01983  -0.02430 0.03754  105 HOH   B O   
2273 O  O   . HOH   L .   ? 0.45821 0.58830 0.53550 0.00027  -0.01903 0.02846  106 HOH   B O   
2274 O  O   . HOH   L .   ? 0.61955 0.58477 0.65286 0.06788  0.01508  0.03352  107 HOH   B O   
2275 O  O   . HOH   L .   ? 0.51729 0.47245 0.53933 0.03036  0.01969  0.00731  108 HOH   B O   
2276 O  O   . HOH   L .   ? 0.95074 0.81280 0.95869 0.09091  0.02579  0.05505  109 HOH   B O   
2277 O  O   . HOH   L .   ? 0.58424 0.68902 0.63502 0.03995  -0.02589 0.04762  110 HOH   B O   
2278 O  O   . HOH   L .   ? 0.72946 0.63434 0.73841 0.03336  0.02357  0.01752  111 HOH   B O   
2279 O  O   . HOH   L .   ? 0.53763 0.66714 0.58777 0.03041  -0.03528 0.04662  112 HOH   B O   
2280 O  O   . HOH   L .   ? 0.76995 0.84869 0.80735 0.07250  -0.02398 0.07125  113 HOH   B O   
# 
