data_9BP8
# 
_entry.id   9BP8 
# 
_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   9BP8         pdb_00009bp8 10.2210/pdb9bp8/pdb 
WWPDB D_1000281924 ?            ?                   
# 
_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       2025-05-14 
_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                        9BP8 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-07 
_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                 4 
_pdbx_contact_author.email              tung-chung.mou@pfizer.com 
_pdbx_contact_author.name_first         Tung-Chung 
_pdbx_contact_author.name_last          Mou 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6554-1519 
# 
_audit_author.name               'Mou, T.-C.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0001-6554-1519 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of BRAF kinase domain with PF-07799933' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Mou, T.-C.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0001-6554-1519 
# 
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 'Serine/threonine-protein kinase B-raf' 33200.359 1   2.7.11.1 ? ? ? 
2 non-polymer syn 
;N-{(1R,2P)-6-chloro-5-[(5-chloro-3-methyl-4-oxo-3,4-dihydroquinazolin-6-yl)amino]-4-fluorocyclohexa-2,3,5-trien-1-yl}-3-fluoroazetidine-1-sulfonamide
;
490.311   1   ?        ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    4   ?        ? ? ? 
4 non-polymer syn 'SULFATE ION' 96.063    1   ?        ? ? ? 
5 water       nat water 18.015    329 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Proto-oncogene B-Raf,p94,v-Raf murine sarcoma viral oncogene homolog B1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGHHHHHHGLVPRGSDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTR
HVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT
VKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIAMV
GAGALSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGHHHHHHGLVPRGSDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTR
HVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT
VKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIAMV
GAGALSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;N-{(1R,2P)-6-chloro-5-[(5-chloro-3-methyl-4-oxo-3,4-dihydroquinazolin-6-yl)amino]-4-fluorocyclohexa-2,3,5-trien-1-yl}-3-fluoroazetidine-1-sulfonamide
;
A1AQY 
3 'DIMETHYL SULFOXIDE' DMS   
4 'SULFATE ION' SO4   
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   GLY n 
1 10  LEU n 
1 11  VAL n 
1 12  PRO n 
1 13  ARG n 
1 14  GLY n 
1 15  SER n 
1 16  ASP n 
1 17  SER n 
1 18  SER n 
1 19  ASP n 
1 20  ASP n 
1 21  TRP n 
1 22  GLU n 
1 23  ILE n 
1 24  PRO n 
1 25  ASP n 
1 26  GLY n 
1 27  GLN n 
1 28  ILE n 
1 29  THR n 
1 30  VAL n 
1 31  GLY n 
1 32  GLN n 
1 33  ARG n 
1 34  ILE n 
1 35  GLY n 
1 36  SER n 
1 37  GLY n 
1 38  SER n 
1 39  PHE n 
1 40  GLY n 
1 41  THR n 
1 42  VAL n 
1 43  TYR n 
1 44  LYS n 
1 45  GLY n 
1 46  LYS n 
1 47  TRP n 
1 48  HIS n 
1 49  GLY n 
1 50  ASP n 
1 51  VAL n 
1 52  ALA n 
1 53  VAL n 
1 54  LYS n 
1 55  MET n 
1 56  LEU n 
1 57  ASN n 
1 58  VAL n 
1 59  THR n 
1 60  ALA n 
1 61  PRO n 
1 62  THR n 
1 63  PRO n 
1 64  GLN n 
1 65  GLN n 
1 66  LEU n 
1 67  GLN n 
1 68  ALA n 
1 69  PHE n 
1 70  LYS n 
1 71  ASN n 
1 72  GLU n 
1 73  VAL n 
1 74  GLY n 
1 75  VAL n 
1 76  LEU n 
1 77  ARG n 
1 78  LYS n 
1 79  THR n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  ASN n 
1 84  ILE n 
1 85  LEU n 
1 86  LEU n 
1 87  PHE n 
1 88  MET n 
1 89  GLY n 
1 90  TYR n 
1 91  SER n 
1 92  THR n 
1 93  LYS n 
1 94  PRO n 
1 95  GLN n 
1 96  LEU n 
1 97  ALA n 
1 98  ILE n 
1 99  VAL n 
1 100 THR n 
1 101 GLN n 
1 102 TRP n 
1 103 CYS n 
1 104 GLU n 
1 105 GLY n 
1 106 SER n 
1 107 SER n 
1 108 LEU n 
1 109 TYR n 
1 110 HIS n 
1 111 HIS n 
1 112 LEU n 
1 113 HIS n 
1 114 ILE n 
1 115 ILE n 
1 116 GLU n 
1 117 THR n 
1 118 LYS n 
1 119 PHE n 
1 120 GLU n 
1 121 MET n 
1 122 ILE n 
1 123 LYS n 
1 124 LEU n 
1 125 ILE n 
1 126 ASP n 
1 127 ILE n 
1 128 ALA n 
1 129 ARG n 
1 130 GLN n 
1 131 THR n 
1 132 ALA n 
1 133 GLN n 
1 134 GLY n 
1 135 MET n 
1 136 ASP n 
1 137 TYR n 
1 138 LEU n 
1 139 HIS n 
1 140 ALA n 
1 141 LYS n 
1 142 SER n 
1 143 ILE n 
1 144 ILE n 
1 145 HIS n 
1 146 ARG n 
1 147 ASP n 
1 148 LEU n 
1 149 LYS n 
1 150 SER n 
1 151 ASN n 
1 152 ASN n 
1 153 ILE n 
1 154 PHE n 
1 155 LEU n 
1 156 HIS n 
1 157 GLU n 
1 158 ASP n 
1 159 LEU n 
1 160 THR n 
1 161 VAL n 
1 162 LYS n 
1 163 ILE n 
1 164 GLY n 
1 165 ASP n 
1 166 PHE n 
1 167 GLY n 
1 168 LEU n 
1 169 ALA n 
1 170 THR n 
1 171 VAL n 
1 172 LYS n 
1 173 SER n 
1 174 ARG n 
1 175 TRP n 
1 176 SER n 
1 177 GLY n 
1 178 SER n 
1 179 HIS n 
1 180 GLN n 
1 181 PHE n 
1 182 GLU n 
1 183 GLN n 
1 184 LEU n 
1 185 SER n 
1 186 GLY n 
1 187 SER n 
1 188 ILE n 
1 189 LEU n 
1 190 TRP n 
1 191 MET n 
1 192 ALA n 
1 193 PRO n 
1 194 GLU n 
1 195 VAL n 
1 196 ILE n 
1 197 ARG n 
1 198 MET n 
1 199 GLN n 
1 200 ASP n 
1 201 LYS n 
1 202 ASN n 
1 203 PRO n 
1 204 TYR n 
1 205 SER n 
1 206 PHE n 
1 207 GLN n 
1 208 SER n 
1 209 ASP n 
1 210 VAL n 
1 211 TYR n 
1 212 ALA n 
1 213 PHE n 
1 214 GLY n 
1 215 ILE n 
1 216 VAL n 
1 217 LEU n 
1 218 TYR n 
1 219 GLU n 
1 220 LEU n 
1 221 MET n 
1 222 THR n 
1 223 GLY n 
1 224 GLN n 
1 225 LEU n 
1 226 PRO n 
1 227 TYR n 
1 228 SER n 
1 229 ASN n 
1 230 ILE n 
1 231 ASN n 
1 232 ASN n 
1 233 ARG n 
1 234 ASP n 
1 235 GLN n 
1 236 ILE n 
1 237 ILE n 
1 238 ALA n 
1 239 MET n 
1 240 VAL n 
1 241 GLY n 
1 242 ALA n 
1 243 GLY n 
1 244 ALA n 
1 245 LEU n 
1 246 SER n 
1 247 PRO n 
1 248 ASP n 
1 249 LEU n 
1 250 SER n 
1 251 LYS n 
1 252 VAL n 
1 253 ARG n 
1 254 SER n 
1 255 ASN n 
1 256 CYS n 
1 257 PRO n 
1 258 LYS n 
1 259 ALA n 
1 260 MET n 
1 261 LYS n 
1 262 ARG n 
1 263 LEU n 
1 264 MET n 
1 265 ALA n 
1 266 GLU n 
1 267 CYS n 
1 268 LEU n 
1 269 LYS n 
1 270 LYS n 
1 271 LYS n 
1 272 ARG n 
1 273 ASP n 
1 274 GLU n 
1 275 ARG n 
1 276 PRO n 
1 277 LEU n 
1 278 PHE n 
1 279 PRO n 
1 280 GLN n 
1 281 ILE n 
1 282 LEU n 
1 283 ALA n 
1 284 SER n 
1 285 ILE n 
1 286 GLU n 
1 287 LEU n 
1 288 LEU n 
1 289 ALA n 
1 290 ARG n 
1 291 SER n 
1 292 LEU n 
1 293 PRO n 
1 294 LYS 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                   294 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BRAF, BRAF1, RAFB1' 
_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      'unidentified baculovirus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10469 
_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                   ? 
# 
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 
A1AQY non-polymer         . 
;N-{(1R,2P)-6-chloro-5-[(5-chloro-3-methyl-4-oxo-3,4-dihydroquinazolin-6-yl)amino]-4-fluorocyclohexa-2,3,5-trien-1-yl}-3-fluoroazetidine-1-sulfonamide
;
? 'C18 H15 Cl2 F2 N5 O3 S' 490.311 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'             89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'         175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'            132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'             133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'           121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'              78.133  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'           146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'             147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'             75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'         156.162 
HOH   non-polymer         . WATER ? 'H2 O'                   18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'            131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'            131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'         147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'          149.211 
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 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'                96.063  
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   MET 1   430 ?   ?   ?   A . n 
A 1 2   GLY 2   431 ?   ?   ?   A . n 
A 1 3   HIS 3   432 ?   ?   ?   A . n 
A 1 4   HIS 4   433 ?   ?   ?   A . n 
A 1 5   HIS 5   434 ?   ?   ?   A . n 
A 1 6   HIS 6   435 ?   ?   ?   A . n 
A 1 7   HIS 7   436 ?   ?   ?   A . n 
A 1 8   HIS 8   437 ?   ?   ?   A . n 
A 1 9   GLY 9   438 ?   ?   ?   A . n 
A 1 10  LEU 10  439 ?   ?   ?   A . n 
A 1 11  VAL 11  440 ?   ?   ?   A . n 
A 1 12  PRO 12  441 ?   ?   ?   A . n 
A 1 13  ARG 13  442 ?   ?   ?   A . n 
A 1 14  GLY 14  443 ?   ?   ?   A . n 
A 1 15  SER 15  444 ?   ?   ?   A . n 
A 1 16  ASP 16  445 ?   ?   ?   A . n 
A 1 17  SER 17  446 ?   ?   ?   A . n 
A 1 18  SER 18  447 ?   ?   ?   A . n 
A 1 19  ASP 19  448 ?   ?   ?   A . n 
A 1 20  ASP 20  449 449 ASP ASP A . n 
A 1 21  TRP 21  450 450 TRP TRP A . n 
A 1 22  GLU 22  451 451 GLU GLU A . n 
A 1 23  ILE 23  452 452 ILE ILE A . n 
A 1 24  PRO 24  453 453 PRO PRO A . n 
A 1 25  ASP 25  454 454 ASP ASP A . n 
A 1 26  GLY 26  455 455 GLY GLY A . n 
A 1 27  GLN 27  456 456 GLN GLN A . n 
A 1 28  ILE 28  457 457 ILE ILE A . n 
A 1 29  THR 29  458 458 THR THR A . n 
A 1 30  VAL 30  459 459 VAL VAL A . n 
A 1 31  GLY 31  460 460 GLY GLY A . n 
A 1 32  GLN 32  461 461 GLN GLN A . n 
A 1 33  ARG 33  462 462 ARG ARG A . n 
A 1 34  ILE 34  463 463 ILE ILE A . n 
A 1 35  GLY 35  464 464 GLY GLY A . n 
A 1 36  SER 36  465 465 SER SER A . n 
A 1 37  GLY 37  466 466 GLY GLY A . n 
A 1 38  SER 38  467 467 SER SER A . n 
A 1 39  PHE 39  468 468 PHE PHE A . n 
A 1 40  GLY 40  469 469 GLY GLY A . n 
A 1 41  THR 41  470 470 THR THR A . n 
A 1 42  VAL 42  471 471 VAL VAL A . n 
A 1 43  TYR 43  472 472 TYR TYR A . n 
A 1 44  LYS 44  473 473 LYS LYS A . n 
A 1 45  GLY 45  474 474 GLY GLY A . n 
A 1 46  LYS 46  475 475 LYS LYS A . n 
A 1 47  TRP 47  476 476 TRP TRP A . n 
A 1 48  HIS 48  477 477 HIS HIS A . n 
A 1 49  GLY 49  478 478 GLY GLY A . n 
A 1 50  ASP 50  479 479 ASP ASP A . n 
A 1 51  VAL 51  480 480 VAL VAL A . n 
A 1 52  ALA 52  481 481 ALA ALA A . n 
A 1 53  VAL 53  482 482 VAL VAL A . n 
A 1 54  LYS 54  483 483 LYS LYS A . n 
A 1 55  MET 55  484 484 MET MET A . n 
A 1 56  LEU 56  485 485 LEU LEU A . n 
A 1 57  ASN 57  486 486 ASN ASN A . n 
A 1 58  VAL 58  487 487 VAL VAL A . n 
A 1 59  THR 59  488 488 THR THR A . n 
A 1 60  ALA 60  489 489 ALA ALA A . n 
A 1 61  PRO 61  490 490 PRO PRO A . n 
A 1 62  THR 62  491 491 THR THR A . n 
A 1 63  PRO 63  492 492 PRO PRO A . n 
A 1 64  GLN 64  493 493 GLN GLN A . n 
A 1 65  GLN 65  494 494 GLN GLN A . n 
A 1 66  LEU 66  495 495 LEU LEU A . n 
A 1 67  GLN 67  496 496 GLN GLN A . n 
A 1 68  ALA 68  497 497 ALA ALA A . n 
A 1 69  PHE 69  498 498 PHE PHE A . n 
A 1 70  LYS 70  499 499 LYS LYS A . n 
A 1 71  ASN 71  500 500 ASN ASN A . n 
A 1 72  GLU 72  501 501 GLU GLU A . n 
A 1 73  VAL 73  502 502 VAL VAL A . n 
A 1 74  GLY 74  503 503 GLY GLY A . n 
A 1 75  VAL 75  504 504 VAL VAL A . n 
A 1 76  LEU 76  505 505 LEU LEU A . n 
A 1 77  ARG 77  506 506 ARG ARG A . n 
A 1 78  LYS 78  507 507 LYS LYS A . n 
A 1 79  THR 79  508 508 THR THR A . n 
A 1 80  ARG 80  509 509 ARG ARG A . n 
A 1 81  HIS 81  510 510 HIS HIS A . n 
A 1 82  VAL 82  511 511 VAL VAL A . n 
A 1 83  ASN 83  512 512 ASN ASN A . n 
A 1 84  ILE 84  513 513 ILE ILE A . n 
A 1 85  LEU 85  514 514 LEU LEU A . n 
A 1 86  LEU 86  515 515 LEU LEU A . n 
A 1 87  PHE 87  516 516 PHE PHE A . n 
A 1 88  MET 88  517 517 MET MET A . n 
A 1 89  GLY 89  518 518 GLY GLY A . n 
A 1 90  TYR 90  519 519 TYR TYR A . n 
A 1 91  SER 91  520 520 SER SER A . n 
A 1 92  THR 92  521 521 THR THR A . n 
A 1 93  LYS 93  522 522 LYS LYS A . n 
A 1 94  PRO 94  523 523 PRO PRO A . n 
A 1 95  GLN 95  524 524 GLN GLN A . n 
A 1 96  LEU 96  525 525 LEU LEU A . n 
A 1 97  ALA 97  526 526 ALA ALA A . n 
A 1 98  ILE 98  527 527 ILE ILE A . n 
A 1 99  VAL 99  528 528 VAL VAL A . n 
A 1 100 THR 100 529 529 THR THR A . n 
A 1 101 GLN 101 530 530 GLN GLN A . n 
A 1 102 TRP 102 531 531 TRP TRP A . n 
A 1 103 CYS 103 532 532 CYS CYS A . n 
A 1 104 GLU 104 533 533 GLU GLU A . n 
A 1 105 GLY 105 534 534 GLY GLY A . n 
A 1 106 SER 106 535 535 SER SER A . n 
A 1 107 SER 107 536 536 SER SER A . n 
A 1 108 LEU 108 537 537 LEU LEU A . n 
A 1 109 TYR 109 538 538 TYR TYR A . n 
A 1 110 HIS 110 539 539 HIS HIS A . n 
A 1 111 HIS 111 540 540 HIS HIS A . n 
A 1 112 LEU 112 541 541 LEU LEU A . n 
A 1 113 HIS 113 542 542 HIS HIS A . n 
A 1 114 ILE 114 543 543 ILE ILE A . n 
A 1 115 ILE 115 544 544 ILE ILE A . n 
A 1 116 GLU 116 545 545 GLU GLU A . n 
A 1 117 THR 117 546 546 THR THR A . n 
A 1 118 LYS 118 547 547 LYS LYS A . n 
A 1 119 PHE 119 548 548 PHE PHE A . n 
A 1 120 GLU 120 549 549 GLU GLU A . n 
A 1 121 MET 121 550 550 MET MET A . n 
A 1 122 ILE 122 551 551 ILE ILE A . n 
A 1 123 LYS 123 552 552 LYS LYS A . n 
A 1 124 LEU 124 553 553 LEU LEU A . n 
A 1 125 ILE 125 554 554 ILE ILE A . n 
A 1 126 ASP 126 555 555 ASP ASP A . n 
A 1 127 ILE 127 556 556 ILE ILE A . n 
A 1 128 ALA 128 557 557 ALA ALA A . n 
A 1 129 ARG 129 558 558 ARG ARG A . n 
A 1 130 GLN 130 559 559 GLN GLN A . n 
A 1 131 THR 131 560 560 THR THR A . n 
A 1 132 ALA 132 561 561 ALA ALA A . n 
A 1 133 GLN 133 562 562 GLN GLN A . n 
A 1 134 GLY 134 563 563 GLY GLY A . n 
A 1 135 MET 135 564 564 MET MET A . n 
A 1 136 ASP 136 565 565 ASP ASP A . n 
A 1 137 TYR 137 566 566 TYR TYR A . n 
A 1 138 LEU 138 567 567 LEU LEU A . n 
A 1 139 HIS 139 568 568 HIS HIS A . n 
A 1 140 ALA 140 569 569 ALA ALA A . n 
A 1 141 LYS 141 570 570 LYS LYS A . n 
A 1 142 SER 142 571 571 SER SER A . n 
A 1 143 ILE 143 572 572 ILE ILE A . n 
A 1 144 ILE 144 573 573 ILE ILE A . n 
A 1 145 HIS 145 574 574 HIS HIS A . n 
A 1 146 ARG 146 575 575 ARG ARG A . n 
A 1 147 ASP 147 576 576 ASP ASP A . n 
A 1 148 LEU 148 577 577 LEU LEU A . n 
A 1 149 LYS 149 578 578 LYS LYS A . n 
A 1 150 SER 150 579 579 SER SER A . n 
A 1 151 ASN 151 580 580 ASN ASN A . n 
A 1 152 ASN 152 581 581 ASN ASN A . n 
A 1 153 ILE 153 582 582 ILE ILE A . n 
A 1 154 PHE 154 583 583 PHE PHE A . n 
A 1 155 LEU 155 584 584 LEU LEU A . n 
A 1 156 HIS 156 585 585 HIS HIS A . n 
A 1 157 GLU 157 586 586 GLU GLU A . n 
A 1 158 ASP 158 587 587 ASP ASP A . n 
A 1 159 LEU 159 588 588 LEU LEU A . n 
A 1 160 THR 160 589 589 THR THR A . n 
A 1 161 VAL 161 590 590 VAL VAL A . n 
A 1 162 LYS 162 591 591 LYS LYS A . n 
A 1 163 ILE 163 592 592 ILE ILE A . n 
A 1 164 GLY 164 593 593 GLY GLY A . n 
A 1 165 ASP 165 594 594 ASP ASP A . n 
A 1 166 PHE 166 595 595 PHE PHE A . n 
A 1 167 GLY 167 596 596 GLY GLY A . n 
A 1 168 LEU 168 597 597 LEU LEU A . n 
A 1 169 ALA 169 598 598 ALA ALA A . n 
A 1 170 THR 170 599 599 THR THR A . n 
A 1 171 VAL 171 600 600 VAL VAL A . n 
A 1 172 LYS 172 601 601 LYS LYS A . n 
A 1 173 SER 173 602 602 SER SER A . n 
A 1 174 ARG 174 603 603 ARG ARG A . n 
A 1 175 TRP 175 604 604 TRP TRP A . n 
A 1 176 SER 176 605 605 SER SER A . n 
A 1 177 GLY 177 606 606 GLY GLY A . n 
A 1 178 SER 178 607 607 SER SER A . n 
A 1 179 HIS 179 608 608 HIS HIS A . n 
A 1 180 GLN 180 609 609 GLN GLN A . n 
A 1 181 PHE 181 610 610 PHE PHE A . n 
A 1 182 GLU 182 611 611 GLU GLU A . n 
A 1 183 GLN 183 612 612 GLN GLN A . n 
A 1 184 LEU 184 613 613 LEU LEU A . n 
A 1 185 SER 185 614 614 SER SER A . n 
A 1 186 GLY 186 615 615 GLY GLY A . n 
A 1 187 SER 187 616 616 SER SER A . n 
A 1 188 ILE 188 617 617 ILE ILE A . n 
A 1 189 LEU 189 618 618 LEU LEU A . n 
A 1 190 TRP 190 619 619 TRP TRP A . n 
A 1 191 MET 191 620 620 MET MET A . n 
A 1 192 ALA 192 621 621 ALA ALA A . n 
A 1 193 PRO 193 622 622 PRO PRO A . n 
A 1 194 GLU 194 623 623 GLU GLU A . n 
A 1 195 VAL 195 624 624 VAL VAL A . n 
A 1 196 ILE 196 625 625 ILE ILE A . n 
A 1 197 ARG 197 626 626 ARG ARG A . n 
A 1 198 MET 198 627 627 MET MET A . n 
A 1 199 GLN 199 628 628 GLN GLN A . n 
A 1 200 ASP 200 629 629 ASP ASP A . n 
A 1 201 LYS 201 630 630 LYS LYS A . n 
A 1 202 ASN 202 631 631 ASN ASN A . n 
A 1 203 PRO 203 632 632 PRO PRO A . n 
A 1 204 TYR 204 633 633 TYR TYR A . n 
A 1 205 SER 205 634 634 SER SER A . n 
A 1 206 PHE 206 635 635 PHE PHE A . n 
A 1 207 GLN 207 636 636 GLN GLN A . n 
A 1 208 SER 208 637 637 SER SER A . n 
A 1 209 ASP 209 638 638 ASP ASP A . n 
A 1 210 VAL 210 639 639 VAL VAL A . n 
A 1 211 TYR 211 640 640 TYR TYR A . n 
A 1 212 ALA 212 641 641 ALA ALA A . n 
A 1 213 PHE 213 642 642 PHE PHE A . n 
A 1 214 GLY 214 643 643 GLY GLY A . n 
A 1 215 ILE 215 644 644 ILE ILE A . n 
A 1 216 VAL 216 645 645 VAL VAL A . n 
A 1 217 LEU 217 646 646 LEU LEU A . n 
A 1 218 TYR 218 647 647 TYR TYR A . n 
A 1 219 GLU 219 648 648 GLU GLU A . n 
A 1 220 LEU 220 649 649 LEU LEU A . n 
A 1 221 MET 221 650 650 MET MET A . n 
A 1 222 THR 222 651 651 THR THR A . n 
A 1 223 GLY 223 652 652 GLY GLY A . n 
A 1 224 GLN 224 653 653 GLN GLN A . n 
A 1 225 LEU 225 654 654 LEU LEU A . n 
A 1 226 PRO 226 655 655 PRO PRO A . n 
A 1 227 TYR 227 656 656 TYR TYR A . n 
A 1 228 SER 228 657 657 SER SER A . n 
A 1 229 ASN 229 658 658 ASN ASN A . n 
A 1 230 ILE 230 659 659 ILE ILE A . n 
A 1 231 ASN 231 660 660 ASN ASN A . n 
A 1 232 ASN 232 661 661 ASN ASN A . n 
A 1 233 ARG 233 662 662 ARG ARG A . n 
A 1 234 ASP 234 663 663 ASP ASP A . n 
A 1 235 GLN 235 664 664 GLN GLN A . n 
A 1 236 ILE 236 665 665 ILE ILE A . n 
A 1 237 ILE 237 666 666 ILE ILE A . n 
A 1 238 ALA 238 667 667 ALA ALA A . n 
A 1 239 MET 239 668 668 MET MET A . n 
A 1 240 VAL 240 669 669 VAL VAL A . n 
A 1 241 GLY 241 670 670 GLY GLY A . n 
A 1 242 ALA 242 671 671 ALA ALA A . n 
A 1 243 GLY 243 672 672 GLY GLY A . n 
A 1 244 ALA 244 673 673 ALA ALA A . n 
A 1 245 LEU 245 674 674 LEU LEU A . n 
A 1 246 SER 246 675 675 SER SER A . n 
A 1 247 PRO 247 676 676 PRO PRO A . n 
A 1 248 ASP 248 677 677 ASP ASP A . n 
A 1 249 LEU 249 678 678 LEU LEU A . n 
A 1 250 SER 250 679 679 SER SER A . n 
A 1 251 LYS 251 680 680 LYS LYS A . n 
A 1 252 VAL 252 681 681 VAL VAL A . n 
A 1 253 ARG 253 682 682 ARG ARG A . n 
A 1 254 SER 254 683 683 SER SER A . n 
A 1 255 ASN 255 684 684 ASN ASN A . n 
A 1 256 CYS 256 685 685 CYS CYS A . n 
A 1 257 PRO 257 686 686 PRO PRO A . n 
A 1 258 LYS 258 687 687 LYS LYS A . n 
A 1 259 ALA 259 688 688 ALA ALA A . n 
A 1 260 MET 260 689 689 MET MET A . n 
A 1 261 LYS 261 690 690 LYS LYS A . n 
A 1 262 ARG 262 691 691 ARG ARG A . n 
A 1 263 LEU 263 692 692 LEU LEU A . n 
A 1 264 MET 264 693 693 MET MET A . n 
A 1 265 ALA 265 694 694 ALA ALA A . n 
A 1 266 GLU 266 695 695 GLU GLU A . n 
A 1 267 CYS 267 696 696 CYS CYS A . n 
A 1 268 LEU 268 697 697 LEU LEU A . n 
A 1 269 LYS 269 698 698 LYS LYS A . n 
A 1 270 LYS 270 699 699 LYS LYS A . n 
A 1 271 LYS 271 700 700 LYS LYS A . n 
A 1 272 ARG 272 701 701 ARG ARG A . n 
A 1 273 ASP 273 702 702 ASP ASP A . n 
A 1 274 GLU 274 703 703 GLU GLU A . n 
A 1 275 ARG 275 704 704 ARG ARG A . n 
A 1 276 PRO 276 705 705 PRO PRO A . n 
A 1 277 LEU 277 706 706 LEU LEU A . n 
A 1 278 PHE 278 707 707 PHE PHE A . n 
A 1 279 PRO 279 708 708 PRO PRO A . n 
A 1 280 GLN 280 709 709 GLN GLN A . n 
A 1 281 ILE 281 710 710 ILE ILE A . n 
A 1 282 LEU 282 711 711 LEU LEU A . n 
A 1 283 ALA 283 712 712 ALA ALA A . n 
A 1 284 SER 284 713 713 SER SER A . n 
A 1 285 ILE 285 714 714 ILE ILE A . n 
A 1 286 GLU 286 715 715 GLU GLU A . n 
A 1 287 LEU 287 716 716 LEU LEU A . n 
A 1 288 LEU 288 717 717 LEU LEU A . n 
A 1 289 ALA 289 718 718 ALA ALA A . n 
A 1 290 ARG 290 719 719 ARG ARG A . n 
A 1 291 SER 291 720 720 SER SER A . n 
A 1 292 LEU 292 721 721 LEU LEU A . n 
A 1 293 PRO 293 722 ?   ?   ?   A . n 
A 1 294 LYS 294 723 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AQY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AQY 
_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 
B 2 A1AQY 1   801  801  A1AQY SM1 A . 
C 3 DMS   1   802  901  DMS   DMS A . 
D 3 DMS   1   803  1001 DMS   DMS A . 
E 3 DMS   1   804  1101 DMS   DMS A . 
F 3 DMS   1   805  1201 DMS   DMS A . 
G 4 SO4   1   806  1    SO4   SO4 A . 
H 5 HOH   1   901  97   HOH   HOH A . 
H 5 HOH   2   902  170  HOH   HOH A . 
H 5 HOH   3   903  244  HOH   HOH A . 
H 5 HOH   4   904  113  HOH   HOH A . 
H 5 HOH   5   905  342  HOH   HOH A . 
H 5 HOH   6   906  304  HOH   HOH A . 
H 5 HOH   7   907  336  HOH   HOH A . 
H 5 HOH   8   908  252  HOH   HOH A . 
H 5 HOH   9   909  326  HOH   HOH A . 
H 5 HOH   10  910  306  HOH   HOH A . 
H 5 HOH   11  911  185  HOH   HOH A . 
H 5 HOH   12  912  193  HOH   HOH A . 
H 5 HOH   13  913  257  HOH   HOH A . 
H 5 HOH   14  914  151  HOH   HOH A . 
H 5 HOH   15  915  273  HOH   HOH A . 
H 5 HOH   16  916  211  HOH   HOH A . 
H 5 HOH   17  917  192  HOH   HOH A . 
H 5 HOH   18  918  311  HOH   HOH A . 
H 5 HOH   19  919  361  HOH   HOH A . 
H 5 HOH   20  920  109  HOH   HOH A . 
H 5 HOH   21  921  308  HOH   HOH A . 
H 5 HOH   22  922  178  HOH   HOH A . 
H 5 HOH   23  923  348  HOH   HOH A . 
H 5 HOH   24  924  229  HOH   HOH A . 
H 5 HOH   25  925  221  HOH   HOH A . 
H 5 HOH   26  926  162  HOH   HOH A . 
H 5 HOH   27  927  202  HOH   HOH A . 
H 5 HOH   28  928  60   HOH   HOH A . 
H 5 HOH   29  929  59   HOH   HOH A . 
H 5 HOH   30  930  124  HOH   HOH A . 
H 5 HOH   31  931  194  HOH   HOH A . 
H 5 HOH   32  932  125  HOH   HOH A . 
H 5 HOH   33  933  67   HOH   HOH A . 
H 5 HOH   34  934  130  HOH   HOH A . 
H 5 HOH   35  935  111  HOH   HOH A . 
H 5 HOH   36  936  141  HOH   HOH A . 
H 5 HOH   37  937  143  HOH   HOH A . 
H 5 HOH   38  938  288  HOH   HOH A . 
H 5 HOH   39  939  75   HOH   HOH A . 
H 5 HOH   40  940  225  HOH   HOH A . 
H 5 HOH   41  941  40   HOH   HOH A . 
H 5 HOH   42  942  148  HOH   HOH A . 
H 5 HOH   43  943  212  HOH   HOH A . 
H 5 HOH   44  944  259  HOH   HOH A . 
H 5 HOH   45  945  290  HOH   HOH A . 
H 5 HOH   46  946  315  HOH   HOH A . 
H 5 HOH   47  947  157  HOH   HOH A . 
H 5 HOH   48  948  107  HOH   HOH A . 
H 5 HOH   49  949  3    HOH   HOH A . 
H 5 HOH   50  950  19   HOH   HOH A . 
H 5 HOH   51  951  118  HOH   HOH A . 
H 5 HOH   52  952  21   HOH   HOH A . 
H 5 HOH   53  953  48   HOH   HOH A . 
H 5 HOH   54  954  278  HOH   HOH A . 
H 5 HOH   55  955  65   HOH   HOH A . 
H 5 HOH   56  956  76   HOH   HOH A . 
H 5 HOH   57  957  205  HOH   HOH A . 
H 5 HOH   58  958  101  HOH   HOH A . 
H 5 HOH   59  959  105  HOH   HOH A . 
H 5 HOH   60  960  96   HOH   HOH A . 
H 5 HOH   61  961  120  HOH   HOH A . 
H 5 HOH   62  962  9    HOH   HOH A . 
H 5 HOH   63  963  188  HOH   HOH A . 
H 5 HOH   64  964  146  HOH   HOH A . 
H 5 HOH   65  965  319  HOH   HOH A . 
H 5 HOH   66  966  83   HOH   HOH A . 
H 5 HOH   67  967  56   HOH   HOH A . 
H 5 HOH   68  968  180  HOH   HOH A . 
H 5 HOH   69  969  18   HOH   HOH A . 
H 5 HOH   70  970  232  HOH   HOH A . 
H 5 HOH   71  971  92   HOH   HOH A . 
H 5 HOH   72  972  166  HOH   HOH A . 
H 5 HOH   73  973  216  HOH   HOH A . 
H 5 HOH   74  974  208  HOH   HOH A . 
H 5 HOH   75  975  26   HOH   HOH A . 
H 5 HOH   76  976  78   HOH   HOH A . 
H 5 HOH   77  977  100  HOH   HOH A . 
H 5 HOH   78  978  110  HOH   HOH A . 
H 5 HOH   79  979  172  HOH   HOH A . 
H 5 HOH   80  980  284  HOH   HOH A . 
H 5 HOH   81  981  330  HOH   HOH A . 
H 5 HOH   82  982  242  HOH   HOH A . 
H 5 HOH   83  983  303  HOH   HOH A . 
H 5 HOH   84  984  46   HOH   HOH A . 
H 5 HOH   85  985  41   HOH   HOH A . 
H 5 HOH   86  986  98   HOH   HOH A . 
H 5 HOH   87  987  29   HOH   HOH A . 
H 5 HOH   88  988  77   HOH   HOH A . 
H 5 HOH   89  989  62   HOH   HOH A . 
H 5 HOH   90  990  13   HOH   HOH A . 
H 5 HOH   91  991  145  HOH   HOH A . 
H 5 HOH   92  992  35   HOH   HOH A . 
H 5 HOH   93  993  119  HOH   HOH A . 
H 5 HOH   94  994  8    HOH   HOH A . 
H 5 HOH   95  995  10   HOH   HOH A . 
H 5 HOH   96  996  337  HOH   HOH A . 
H 5 HOH   97  997  233  HOH   HOH A . 
H 5 HOH   98  998  49   HOH   HOH A . 
H 5 HOH   99  999  37   HOH   HOH A . 
H 5 HOH   100 1000 116  HOH   HOH A . 
H 5 HOH   101 1001 71   HOH   HOH A . 
H 5 HOH   102 1002 88   HOH   HOH A . 
H 5 HOH   103 1003 16   HOH   HOH A . 
H 5 HOH   104 1004 14   HOH   HOH A . 
H 5 HOH   105 1005 160  HOH   HOH A . 
H 5 HOH   106 1006 268  HOH   HOH A . 
H 5 HOH   107 1007 4    HOH   HOH A . 
H 5 HOH   108 1008 80   HOH   HOH A . 
H 5 HOH   109 1009 131  HOH   HOH A . 
H 5 HOH   110 1010 204  HOH   HOH A . 
H 5 HOH   111 1011 147  HOH   HOH A . 
H 5 HOH   112 1012 140  HOH   HOH A . 
H 5 HOH   113 1013 66   HOH   HOH A . 
H 5 HOH   114 1014 183  HOH   HOH A . 
H 5 HOH   115 1015 237  HOH   HOH A . 
H 5 HOH   116 1016 154  HOH   HOH A . 
H 5 HOH   117 1017 58   HOH   HOH A . 
H 5 HOH   118 1018 45   HOH   HOH A . 
H 5 HOH   119 1019 314  HOH   HOH A . 
H 5 HOH   120 1020 24   HOH   HOH A . 
H 5 HOH   121 1021 352  HOH   HOH A . 
H 5 HOH   122 1022 106  HOH   HOH A . 
H 5 HOH   123 1023 28   HOH   HOH A . 
H 5 HOH   124 1024 54   HOH   HOH A . 
H 5 HOH   125 1025 142  HOH   HOH A . 
H 5 HOH   126 1026 5    HOH   HOH A . 
H 5 HOH   127 1027 52   HOH   HOH A . 
H 5 HOH   128 1028 323  HOH   HOH A . 
H 5 HOH   129 1029 17   HOH   HOH A . 
H 5 HOH   130 1030 163  HOH   HOH A . 
H 5 HOH   131 1031 287  HOH   HOH A . 
H 5 HOH   132 1032 11   HOH   HOH A . 
H 5 HOH   133 1033 61   HOH   HOH A . 
H 5 HOH   134 1034 87   HOH   HOH A . 
H 5 HOH   135 1035 73   HOH   HOH A . 
H 5 HOH   136 1036 2    HOH   HOH A . 
H 5 HOH   137 1037 190  HOH   HOH A . 
H 5 HOH   138 1038 207  HOH   HOH A . 
H 5 HOH   139 1039 248  HOH   HOH A . 
H 5 HOH   140 1040 144  HOH   HOH A . 
H 5 HOH   141 1041 23   HOH   HOH A . 
H 5 HOH   142 1042 50   HOH   HOH A . 
H 5 HOH   143 1043 121  HOH   HOH A . 
H 5 HOH   144 1044 267  HOH   HOH A . 
H 5 HOH   145 1045 36   HOH   HOH A . 
H 5 HOH   146 1046 279  HOH   HOH A . 
H 5 HOH   147 1047 53   HOH   HOH A . 
H 5 HOH   148 1048 136  HOH   HOH A . 
H 5 HOH   149 1049 165  HOH   HOH A . 
H 5 HOH   150 1050 115  HOH   HOH A . 
H 5 HOH   151 1051 243  HOH   HOH A . 
H 5 HOH   152 1052 90   HOH   HOH A . 
H 5 HOH   153 1053 30   HOH   HOH A . 
H 5 HOH   154 1054 12   HOH   HOH A . 
H 5 HOH   155 1055 269  HOH   HOH A . 
H 5 HOH   156 1056 177  HOH   HOH A . 
H 5 HOH   157 1057 258  HOH   HOH A . 
H 5 HOH   158 1058 299  HOH   HOH A . 
H 5 HOH   159 1059 199  HOH   HOH A . 
H 5 HOH   160 1060 63   HOH   HOH A . 
H 5 HOH   161 1061 325  HOH   HOH A . 
H 5 HOH   162 1062 20   HOH   HOH A . 
H 5 HOH   163 1063 301  HOH   HOH A . 
H 5 HOH   164 1064 43   HOH   HOH A . 
H 5 HOH   165 1065 313  HOH   HOH A . 
H 5 HOH   166 1066 289  HOH   HOH A . 
H 5 HOH   167 1067 198  HOH   HOH A . 
H 5 HOH   168 1068 215  HOH   HOH A . 
H 5 HOH   169 1069 34   HOH   HOH A . 
H 5 HOH   170 1070 15   HOH   HOH A . 
H 5 HOH   171 1071 51   HOH   HOH A . 
H 5 HOH   172 1072 138  HOH   HOH A . 
H 5 HOH   173 1073 68   HOH   HOH A . 
H 5 HOH   174 1074 294  HOH   HOH A . 
H 5 HOH   175 1075 85   HOH   HOH A . 
H 5 HOH   176 1076 44   HOH   HOH A . 
H 5 HOH   177 1077 70   HOH   HOH A . 
H 5 HOH   178 1078 82   HOH   HOH A . 
H 5 HOH   179 1079 235  HOH   HOH A . 
H 5 HOH   180 1080 239  HOH   HOH A . 
H 5 HOH   181 1081 33   HOH   HOH A . 
H 5 HOH   182 1082 317  HOH   HOH A . 
H 5 HOH   183 1083 363  HOH   HOH A . 
H 5 HOH   184 1084 1    HOH   HOH A . 
H 5 HOH   185 1085 103  HOH   HOH A . 
H 5 HOH   186 1086 69   HOH   HOH A . 
H 5 HOH   187 1087 129  HOH   HOH A . 
H 5 HOH   188 1088 184  HOH   HOH A . 
H 5 HOH   189 1089 197  HOH   HOH A . 
H 5 HOH   190 1090 126  HOH   HOH A . 
H 5 HOH   191 1091 74   HOH   HOH A . 
H 5 HOH   192 1092 203  HOH   HOH A . 
H 5 HOH   193 1093 153  HOH   HOH A . 
H 5 HOH   194 1094 93   HOH   HOH A . 
H 5 HOH   195 1095 72   HOH   HOH A . 
H 5 HOH   196 1096 231  HOH   HOH A . 
H 5 HOH   197 1097 245  HOH   HOH A . 
H 5 HOH   198 1098 6    HOH   HOH A . 
H 5 HOH   199 1099 135  HOH   HOH A . 
H 5 HOH   200 1100 156  HOH   HOH A . 
H 5 HOH   201 1101 238  HOH   HOH A . 
H 5 HOH   202 1102 246  HOH   HOH A . 
H 5 HOH   203 1103 191  HOH   HOH A . 
H 5 HOH   204 1104 99   HOH   HOH A . 
H 5 HOH   205 1105 42   HOH   HOH A . 
H 5 HOH   206 1106 300  HOH   HOH A . 
H 5 HOH   207 1107 321  HOH   HOH A . 
H 5 HOH   208 1108 201  HOH   HOH A . 
H 5 HOH   209 1109 181  HOH   HOH A . 
H 5 HOH   210 1110 173  HOH   HOH A . 
H 5 HOH   211 1111 260  HOH   HOH A . 
H 5 HOH   212 1112 200  HOH   HOH A . 
H 5 HOH   213 1113 122  HOH   HOH A . 
H 5 HOH   214 1114 128  HOH   HOH A . 
H 5 HOH   215 1115 168  HOH   HOH A . 
H 5 HOH   216 1116 25   HOH   HOH A . 
H 5 HOH   217 1117 196  HOH   HOH A . 
H 5 HOH   218 1118 22   HOH   HOH A . 
H 5 HOH   219 1119 95   HOH   HOH A . 
H 5 HOH   220 1120 174  HOH   HOH A . 
H 5 HOH   221 1121 91   HOH   HOH A . 
H 5 HOH   222 1122 230  HOH   HOH A . 
H 5 HOH   223 1123 57   HOH   HOH A . 
H 5 HOH   224 1124 27   HOH   HOH A . 
H 5 HOH   225 1125 249  HOH   HOH A . 
H 5 HOH   226 1126 271  HOH   HOH A . 
H 5 HOH   227 1127 31   HOH   HOH A . 
H 5 HOH   228 1128 210  HOH   HOH A . 
H 5 HOH   229 1129 64   HOH   HOH A . 
H 5 HOH   230 1130 240  HOH   HOH A . 
H 5 HOH   231 1131 305  HOH   HOH A . 
H 5 HOH   232 1132 176  HOH   HOH A . 
H 5 HOH   233 1133 276  HOH   HOH A . 
H 5 HOH   234 1134 161  HOH   HOH A . 
H 5 HOH   235 1135 132  HOH   HOH A . 
H 5 HOH   236 1136 341  HOH   HOH A . 
H 5 HOH   237 1137 236  HOH   HOH A . 
H 5 HOH   238 1138 328  HOH   HOH A . 
H 5 HOH   239 1139 256  HOH   HOH A . 
H 5 HOH   240 1140 296  HOH   HOH A . 
H 5 HOH   241 1141 228  HOH   HOH A . 
H 5 HOH   242 1142 283  HOH   HOH A . 
H 5 HOH   243 1143 353  HOH   HOH A . 
H 5 HOH   244 1144 182  HOH   HOH A . 
H 5 HOH   245 1145 307  HOH   HOH A . 
H 5 HOH   246 1146 285  HOH   HOH A . 
H 5 HOH   247 1147 158  HOH   HOH A . 
H 5 HOH   248 1148 179  HOH   HOH A . 
H 5 HOH   249 1149 312  HOH   HOH A . 
H 5 HOH   250 1150 123  HOH   HOH A . 
H 5 HOH   251 1151 297  HOH   HOH A . 
H 5 HOH   252 1152 226  HOH   HOH A . 
H 5 HOH   253 1153 286  HOH   HOH A . 
H 5 HOH   254 1154 327  HOH   HOH A . 
H 5 HOH   255 1155 7    HOH   HOH A . 
H 5 HOH   256 1156 266  HOH   HOH A . 
H 5 HOH   257 1157 354  HOH   HOH A . 
H 5 HOH   258 1158 218  HOH   HOH A . 
H 5 HOH   259 1159 331  HOH   HOH A . 
H 5 HOH   260 1160 262  HOH   HOH A . 
H 5 HOH   261 1161 281  HOH   HOH A . 
H 5 HOH   262 1162 149  HOH   HOH A . 
H 5 HOH   263 1163 362  HOH   HOH A . 
H 5 HOH   264 1164 251  HOH   HOH A . 
H 5 HOH   265 1165 81   HOH   HOH A . 
H 5 HOH   266 1166 102  HOH   HOH A . 
H 5 HOH   267 1167 358  HOH   HOH A . 
H 5 HOH   268 1168 293  HOH   HOH A . 
H 5 HOH   269 1169 347  HOH   HOH A . 
H 5 HOH   270 1170 150  HOH   HOH A . 
H 5 HOH   271 1171 112  HOH   HOH A . 
H 5 HOH   272 1172 84   HOH   HOH A . 
H 5 HOH   273 1173 309  HOH   HOH A . 
H 5 HOH   274 1174 274  HOH   HOH A . 
H 5 HOH   275 1175 241  HOH   HOH A . 
H 5 HOH   276 1176 277  HOH   HOH A . 
H 5 HOH   277 1177 187  HOH   HOH A . 
H 5 HOH   278 1178 94   HOH   HOH A . 
H 5 HOH   279 1179 359  HOH   HOH A . 
H 5 HOH   280 1180 104  HOH   HOH A . 
H 5 HOH   281 1181 335  HOH   HOH A . 
H 5 HOH   282 1182 234  HOH   HOH A . 
H 5 HOH   283 1183 250  HOH   HOH A . 
H 5 HOH   284 1184 220  HOH   HOH A . 
H 5 HOH   285 1185 302  HOH   HOH A . 
H 5 HOH   286 1186 351  HOH   HOH A . 
H 5 HOH   287 1187 298  HOH   HOH A . 
H 5 HOH   288 1188 137  HOH   HOH A . 
H 5 HOH   289 1189 261  HOH   HOH A . 
H 5 HOH   290 1190 171  HOH   HOH A . 
H 5 HOH   291 1191 139  HOH   HOH A . 
H 5 HOH   292 1192 133  HOH   HOH A . 
H 5 HOH   293 1193 272  HOH   HOH A . 
H 5 HOH   294 1194 213  HOH   HOH A . 
H 5 HOH   295 1195 217  HOH   HOH A . 
H 5 HOH   296 1196 357  HOH   HOH A . 
H 5 HOH   297 1197 265  HOH   HOH A . 
H 5 HOH   298 1198 127  HOH   HOH A . 
H 5 HOH   299 1199 159  HOH   HOH A . 
H 5 HOH   300 1200 219  HOH   HOH A . 
H 5 HOH   301 1201 270  HOH   HOH A . 
H 5 HOH   302 1202 189  HOH   HOH A . 
H 5 HOH   303 1203 47   HOH   HOH A . 
H 5 HOH   304 1204 39   HOH   HOH A . 
H 5 HOH   305 1205 222  HOH   HOH A . 
H 5 HOH   306 1206 167  HOH   HOH A . 
H 5 HOH   307 1207 292  HOH   HOH A . 
H 5 HOH   308 1208 227  HOH   HOH A . 
H 5 HOH   309 1209 295  HOH   HOH A . 
H 5 HOH   310 1210 134  HOH   HOH A . 
H 5 HOH   311 1211 254  HOH   HOH A . 
H 5 HOH   312 1212 247  HOH   HOH A . 
H 5 HOH   313 1213 169  HOH   HOH A . 
H 5 HOH   314 1214 155  HOH   HOH A . 
H 5 HOH   315 1215 209  HOH   HOH A . 
H 5 HOH   316 1216 175  HOH   HOH A . 
H 5 HOH   317 1217 195  HOH   HOH A . 
H 5 HOH   318 1218 223  HOH   HOH A . 
H 5 HOH   319 1219 253  HOH   HOH A . 
H 5 HOH   320 1220 89   HOH   HOH A . 
H 5 HOH   321 1221 206  HOH   HOH A . 
H 5 HOH   322 1222 164  HOH   HOH A . 
H 5 HOH   323 1223 263  HOH   HOH A . 
H 5 HOH   324 1224 291  HOH   HOH A . 
H 5 HOH   325 1225 55   HOH   HOH A . 
H 5 HOH   326 1226 152  HOH   HOH A . 
H 5 HOH   327 1227 280  HOH   HOH A . 
H 5 HOH   328 1228 86   HOH   HOH A . 
H 5 HOH   329 1229 264  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.19.1_4122 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.19.1_4122 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           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                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BP8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.321 
_cell.length_a_esd                 ? 
_cell.length_b                     100.321 
_cell.length_b_esd                 ? 
_cell.length_c                     69.015 
_cell.length_c_esd                 ? 
_cell.volume                       601530.744 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9BP8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            
;P 31 2"
;
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BP8 
_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             3.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.11 
_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, HANGING 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    '17% PEG5000MME, 1% PEG6000, Sodium Acetate, 0.2M NaCl, 5% Tacsimate.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-17 
_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   1.54 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU FR-X' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          20.62 
_reflns.entry_id                                       9BP8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.73 
_reflns.d_resolution_low                               54.04 
_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                                     42373 
_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                           99.96 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.66 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.087 
_reflns.pdbx_Rpim_I_all                                0.027 
_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                              ? 
_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                                    1.73 
_reflns_shell.d_res_low                                     1.792 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.45 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             37437 
_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                               ? 
_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                               0.984 
_reflns_shell.pdbx_Rpim_I_all                               0.327 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.733 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               27.82 
_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                                 9BP8 
_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                            1.73 
_refine.ls_d_res_low                             54.04 
_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                     42373 
_refine.ls_number_reflns_R_free                  2042 
_refine.ls_number_reflns_R_work                  40331 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 4.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1657 
_refine.ls_R_factor_R_free                       0.1929 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1642 
_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.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             1.1100 
_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                 20.3501 
_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                            0.1702 
_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                       1.73 
_refine_hist.d_res_low                        54.04 
_refine_hist.number_atoms_solvent             330 
_refine_hist.number_atoms_total               2550 
_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        2168 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0175  ? 2332 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.5541  ? 3163 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0959  ? 342  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0131  ? 400  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 18.4580 ? 882  ? 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.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' 1.73 1.77  . . 112 2665 99.96  . . . . 0.2607 . . . . . . . . . . . 0.2614 
'X-RAY DIFFRACTION' 1.77 1.81  . . 114 2659 100.00 . . . . 0.2329 . . . . . . . . . . . 0.2725 
'X-RAY DIFFRACTION' 1.81 1.86  . . 143 2675 100.00 . . . . 0.2100 . . . . . . . . . . . 0.2565 
'X-RAY DIFFRACTION' 1.86 1.91  . . 154 2631 100.00 . . . . 0.1902 . . . . . . . . . . . 0.2417 
'X-RAY DIFFRACTION' 1.91 1.98  . . 138 2672 100.00 . . . . 0.1866 . . . . . . . . . . . 0.2317 
'X-RAY DIFFRACTION' 1.98 2.05  . . 133 2664 100.00 . . . . 0.1790 . . . . . . . . . . . 0.2080 
'X-RAY DIFFRACTION' 2.05 2.13  . . 154 2673 100.00 . . . . 0.1820 . . . . . . . . . . . 0.2132 
'X-RAY DIFFRACTION' 2.13 2.23  . . 147 2661 100.00 . . . . 0.1708 . . . . . . . . . . . 0.1913 
'X-RAY DIFFRACTION' 2.23 2.34  . . 144 2663 100.00 . . . . 0.1668 . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 2.34 2.49  . . 95  2726 100.00 . . . . 0.1679 . . . . . . . . . . . 0.1650 
'X-RAY DIFFRACTION' 2.49 2.68  . . 154 2663 100.00 . . . . 0.1683 . . . . . . . . . . . 0.1981 
'X-RAY DIFFRACTION' 2.68 2.95  . . 154 2694 100.00 . . . . 0.1753 . . . . . . . . . . . 0.1848 
'X-RAY DIFFRACTION' 2.95 3.38  . . 107 2732 100.00 . . . . 0.1521 . . . . . . . . . . . 0.1664 
'X-RAY DIFFRACTION' 3.38 4.26  . . 124 2759 100.00 . . . . 0.1350 . . . . . . . . . . . 0.1638 
'X-RAY DIFFRACTION' 4.26 54.04 . . 169 2794 99.56  . . . . 0.1451 . . . . . . . . . . . 0.1790 
# 
_struct.entry_id                     9BP8 
_struct.title                        'Crystal structure of BRAF kinase domain with PF-07799933' 
_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        9BP8 
_struct_keywords.text            'BRAF, Encorafenib, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
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 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BRAF_HUMAN 
_struct_ref.pdbx_db_accession          P15056 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ
LAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRW
SGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSN
CPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPK
;
_struct_ref.pdbx_align_begin           445 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BP8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 16 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 294 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P15056 
_struct_ref_seq.db_align_beg                  445 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  723 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       445 
_struct_ref_seq.pdbx_auth_seq_align_end       723 
# 
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 9BP8 MET A 1   ? UNP P15056 ?   ?   'initiating methionine' 430 1  
1 9BP8 GLY A 2   ? UNP P15056 ?   ?   'expression tag'        431 2  
1 9BP8 HIS A 3   ? UNP P15056 ?   ?   'expression tag'        432 3  
1 9BP8 HIS A 4   ? UNP P15056 ?   ?   'expression tag'        433 4  
1 9BP8 HIS A 5   ? UNP P15056 ?   ?   'expression tag'        434 5  
1 9BP8 HIS A 6   ? UNP P15056 ?   ?   'expression tag'        435 6  
1 9BP8 HIS A 7   ? UNP P15056 ?   ?   'expression tag'        436 7  
1 9BP8 HIS A 8   ? UNP P15056 ?   ?   'expression tag'        437 8  
1 9BP8 GLY A 9   ? UNP P15056 ?   ?   'expression tag'        438 9  
1 9BP8 LEU A 10  ? UNP P15056 ?   ?   'expression tag'        439 10 
1 9BP8 VAL A 11  ? UNP P15056 ?   ?   'expression tag'        440 11 
1 9BP8 PRO A 12  ? UNP P15056 ?   ?   'expression tag'        441 12 
1 9BP8 ARG A 13  ? UNP P15056 ?   ?   'expression tag'        442 13 
1 9BP8 GLY A 14  ? UNP P15056 ?   ?   'expression tag'        443 14 
1 9BP8 SER A 15  ? UNP P15056 ?   ?   'expression tag'        444 15 
1 9BP8 ALA A 238 ? UNP P15056 PHE 667 'engineered mutation'   667 16 
1 9BP8 ALA A 242 ? UNP P15056 ARG 671 'engineered mutation'   671 17 
1 9BP8 ALA A 244 ? UNP P15056 TYR 673 'engineered mutation'   673 18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 THR A 62  ? ARG A 77  ? THR A 491 ARG A 506 1 ? 16 
HELX_P HELX_P2  AA2 SER A 107 ? ILE A 114 ? SER A 536 ILE A 543 1 ? 8  
HELX_P HELX_P3  AA3 GLU A 120 ? LYS A 141 ? GLU A 549 LYS A 570 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 149 ? ASN A 151 ? LYS A 578 ASN A 580 5 ? 3  
HELX_P HELX_P5  AA5 GLU A 157 ? LEU A 159 ? GLU A 586 LEU A 588 5 ? 3  
HELX_P HELX_P6  AA6 LEU A 168 ? TRP A 175 ? LEU A 597 TRP A 604 1 ? 8  
HELX_P HELX_P7  AA7 HIS A 179 ? ILE A 188 ? HIS A 608 ILE A 617 1 ? 10 
HELX_P HELX_P8  AA8 LEU A 189 ? MET A 191 ? LEU A 618 MET A 620 5 ? 3  
HELX_P HELX_P9  AA9 ALA A 192 ? MET A 198 ? ALA A 621 MET A 627 1 ? 7  
HELX_P HELX_P10 AB1 SER A 205 ? GLY A 223 ? SER A 634 GLY A 652 1 ? 19 
HELX_P HELX_P11 AB2 ASN A 232 ? ALA A 242 ? ASN A 661 ALA A 671 1 ? 11 
HELX_P HELX_P12 AB3 ASP A 248 ? VAL A 252 ? ASP A 677 VAL A 681 5 ? 5  
HELX_P HELX_P13 AB4 PRO A 257 ? LEU A 268 ? PRO A 686 LEU A 697 1 ? 12 
HELX_P HELX_P14 AB5 LYS A 271 ? ARG A 275 ? LYS A 700 ARG A 704 5 ? 5  
HELX_P HELX_P15 AB6 LEU A 277 ? SER A 291 ? LEU A 706 SER A 720 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 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 
AA2 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 THR A 29  ? SER A 36  ? THR A 458 SER A 465 
AA1 2 GLY A 40  ? LYS A 46  ? GLY A 469 LYS A 475 
AA1 3 ASP A 50  ? LEU A 56  ? ASP A 479 LEU A 485 
AA1 4 ALA A 97  ? GLN A 101 ? ALA A 526 GLN A 530 
AA1 5 PHE A 87  ? SER A 91  ? PHE A 516 SER A 520 
AA2 1 ILE A 153 ? HIS A 156 ? ILE A 582 HIS A 585 
AA2 2 THR A 160 ? ILE A 163 ? THR A 589 ILE A 592 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLY A 31  ? N GLY A 460 O LYS A 44  ? O LYS A 473 
AA1 2 3 N THR A 41  ? N THR A 470 O MET A 55  ? O MET A 484 
AA1 3 4 N LYS A 54  ? N LYS A 483 O ILE A 98  ? O ILE A 527 
AA1 4 5 O VAL A 99  ? O VAL A 528 N MET A 88  ? N MET A 517 
AA2 1 2 N PHE A 154 ? N PHE A 583 O LYS A 162 ? O LYS A 591 
# 
_pdbx_entry_details.entry_id                   9BP8 
_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   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TRP A 476 ? ? -162.26 102.64 
2 1 ASN A 486 ? ? -78.77  39.65  
3 1 GLN A 524 ? ? 176.87  165.01 
4 1 ARG A 575 ? ? 82.55   -13.02 
5 1 ASP A 576 ? ? -151.49 43.67  
6 1 ASP A 587 ? ? 55.52   19.56  
7 1 ASN A 631 ? ? 44.40   73.17  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A SO4 806  ? G SO4 . 
2 1 A HOH 1174 ? H HOH . 
3 1 A HOH 1203 ? H HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+1/3   
3 -x+y,-x,z+2/3  
4 x-y,-y,-z+2/3  
5 -x,-x+y,-z+1/3 
6 y,x,-z         
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 430 ? A MET 1   
2  1 Y 1 A GLY 431 ? A GLY 2   
3  1 Y 1 A HIS 432 ? A HIS 3   
4  1 Y 1 A HIS 433 ? A HIS 4   
5  1 Y 1 A HIS 434 ? A HIS 5   
6  1 Y 1 A HIS 435 ? A HIS 6   
7  1 Y 1 A HIS 436 ? A HIS 7   
8  1 Y 1 A HIS 437 ? A HIS 8   
9  1 Y 1 A GLY 438 ? A GLY 9   
10 1 Y 1 A LEU 439 ? A LEU 10  
11 1 Y 1 A VAL 440 ? A VAL 11  
12 1 Y 1 A PRO 441 ? A PRO 12  
13 1 Y 1 A ARG 442 ? A ARG 13  
14 1 Y 1 A GLY 443 ? A GLY 14  
15 1 Y 1 A SER 444 ? A SER 15  
16 1 Y 1 A ASP 445 ? A ASP 16  
17 1 Y 1 A SER 446 ? A SER 17  
18 1 Y 1 A SER 447 ? A SER 18  
19 1 Y 1 A ASP 448 ? A ASP 19  
20 1 Y 1 A PRO 722 ? A PRO 293 
21 1 Y 1 A LYS 723 ? A LYS 294 
# 
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 
A1AQY C18  C  Y N 1   
A1AQY C14  C  Y N 2   
A1AQY C13  C  N N 3   
A1AQY C17  C  Y N 4   
A1AQY C16  C  Y N 5   
A1AQY C15  C  Y N 6   
A1AQY C10  C  N N 7   
A1AQY C8   C  N N 8   
A1AQY C5   C  Y N 9   
A1AQY C6   C  Y N 10  
A1AQY C1   C  Y N 11  
A1AQY C4   C  Y N 12  
A1AQY C19  C  Y N 13  
A1AQY C2   C  Y N 14  
A1AQY C3   C  Y N 15  
A1AQY C24  C  N N 16  
A1AQY C25  C  N N 17  
A1AQY C26  C  N N 18  
A1AQY F20  F  N N 19  
A1AQY F29  F  N N 20  
A1AQY N12  N  N N 21  
A1AQY N21  N  N N 22  
A1AQY N23  N  N N 23  
A1AQY N7   N  N N 24  
A1AQY N9   N  N N 25  
A1AQY O11  O  N N 26  
A1AQY O27  O  N N 27  
A1AQY O28  O  N N 28  
A1AQY S22  S  N N 29  
A1AQY CL1  CL N N 30  
A1AQY CL2  CL N N 31  
A1AQY H1   H  N N 32  
A1AQY H2   H  N N 33  
A1AQY H3   H  N N 34  
A1AQY H4   H  N N 35  
A1AQY H5   H  N N 36  
A1AQY H6   H  N N 37  
A1AQY H7   H  N N 38  
A1AQY H8   H  N N 39  
A1AQY H9   H  N N 40  
A1AQY H10  H  N N 41  
A1AQY H11  H  N N 42  
A1AQY H12  H  N N 43  
A1AQY H13  H  N N 44  
A1AQY H14  H  N N 45  
A1AQY H16  H  N N 46  
ALA   N    N  N N 47  
ALA   CA   C  N S 48  
ALA   C    C  N N 49  
ALA   O    O  N N 50  
ALA   CB   C  N N 51  
ALA   OXT  O  N N 52  
ALA   H    H  N N 53  
ALA   H2   H  N N 54  
ALA   HA   H  N N 55  
ALA   HB1  H  N N 56  
ALA   HB2  H  N N 57  
ALA   HB3  H  N N 58  
ALA   HXT  H  N N 59  
ARG   N    N  N N 60  
ARG   CA   C  N S 61  
ARG   C    C  N N 62  
ARG   O    O  N N 63  
ARG   CB   C  N N 64  
ARG   CG   C  N N 65  
ARG   CD   C  N N 66  
ARG   NE   N  N N 67  
ARG   CZ   C  N N 68  
ARG   NH1  N  N N 69  
ARG   NH2  N  N N 70  
ARG   OXT  O  N N 71  
ARG   H    H  N N 72  
ARG   H2   H  N N 73  
ARG   HA   H  N N 74  
ARG   HB2  H  N N 75  
ARG   HB3  H  N N 76  
ARG   HG2  H  N N 77  
ARG   HG3  H  N N 78  
ARG   HD2  H  N N 79  
ARG   HD3  H  N N 80  
ARG   HE   H  N N 81  
ARG   HH11 H  N N 82  
ARG   HH12 H  N N 83  
ARG   HH21 H  N N 84  
ARG   HH22 H  N N 85  
ARG   HXT  H  N N 86  
ASN   N    N  N N 87  
ASN   CA   C  N S 88  
ASN   C    C  N N 89  
ASN   O    O  N N 90  
ASN   CB   C  N N 91  
ASN   CG   C  N N 92  
ASN   OD1  O  N N 93  
ASN   ND2  N  N N 94  
ASN   OXT  O  N N 95  
ASN   H    H  N N 96  
ASN   H2   H  N N 97  
ASN   HA   H  N N 98  
ASN   HB2  H  N N 99  
ASN   HB3  H  N N 100 
ASN   HD21 H  N N 101 
ASN   HD22 H  N N 102 
ASN   HXT  H  N N 103 
ASP   N    N  N N 104 
ASP   CA   C  N S 105 
ASP   C    C  N N 106 
ASP   O    O  N N 107 
ASP   CB   C  N N 108 
ASP   CG   C  N N 109 
ASP   OD1  O  N N 110 
ASP   OD2  O  N N 111 
ASP   OXT  O  N N 112 
ASP   H    H  N N 113 
ASP   H2   H  N N 114 
ASP   HA   H  N N 115 
ASP   HB2  H  N N 116 
ASP   HB3  H  N N 117 
ASP   HD2  H  N N 118 
ASP   HXT  H  N N 119 
CYS   N    N  N N 120 
CYS   CA   C  N R 121 
CYS   C    C  N N 122 
CYS   O    O  N N 123 
CYS   CB   C  N N 124 
CYS   SG   S  N N 125 
CYS   OXT  O  N N 126 
CYS   H    H  N N 127 
CYS   H2   H  N N 128 
CYS   HA   H  N N 129 
CYS   HB2  H  N N 130 
CYS   HB3  H  N N 131 
CYS   HG   H  N N 132 
CYS   HXT  H  N N 133 
DMS   S    S  N N 134 
DMS   O    O  N N 135 
DMS   C1   C  N N 136 
DMS   C2   C  N N 137 
DMS   H11  H  N N 138 
DMS   H12  H  N N 139 
DMS   H13  H  N N 140 
DMS   H21  H  N N 141 
DMS   H22  H  N N 142 
DMS   H23  H  N N 143 
GLN   N    N  N N 144 
GLN   CA   C  N S 145 
GLN   C    C  N N 146 
GLN   O    O  N N 147 
GLN   CB   C  N N 148 
GLN   CG   C  N N 149 
GLN   CD   C  N N 150 
GLN   OE1  O  N N 151 
GLN   NE2  N  N N 152 
GLN   OXT  O  N N 153 
GLN   H    H  N N 154 
GLN   H2   H  N N 155 
GLN   HA   H  N N 156 
GLN   HB2  H  N N 157 
GLN   HB3  H  N N 158 
GLN   HG2  H  N N 159 
GLN   HG3  H  N N 160 
GLN   HE21 H  N N 161 
GLN   HE22 H  N N 162 
GLN   HXT  H  N N 163 
GLU   N    N  N N 164 
GLU   CA   C  N S 165 
GLU   C    C  N N 166 
GLU   O    O  N N 167 
GLU   CB   C  N N 168 
GLU   CG   C  N N 169 
GLU   CD   C  N N 170 
GLU   OE1  O  N N 171 
GLU   OE2  O  N N 172 
GLU   OXT  O  N N 173 
GLU   H    H  N N 174 
GLU   H2   H  N N 175 
GLU   HA   H  N N 176 
GLU   HB2  H  N N 177 
GLU   HB3  H  N N 178 
GLU   HG2  H  N N 179 
GLU   HG3  H  N N 180 
GLU   HE2  H  N N 181 
GLU   HXT  H  N N 182 
GLY   N    N  N N 183 
GLY   CA   C  N N 184 
GLY   C    C  N N 185 
GLY   O    O  N N 186 
GLY   OXT  O  N N 187 
GLY   H    H  N N 188 
GLY   H2   H  N N 189 
GLY   HA2  H  N N 190 
GLY   HA3  H  N N 191 
GLY   HXT  H  N N 192 
HIS   N    N  N N 193 
HIS   CA   C  N S 194 
HIS   C    C  N N 195 
HIS   O    O  N N 196 
HIS   CB   C  N N 197 
HIS   CG   C  Y N 198 
HIS   ND1  N  Y N 199 
HIS   CD2  C  Y N 200 
HIS   CE1  C  Y N 201 
HIS   NE2  N  Y N 202 
HIS   OXT  O  N N 203 
HIS   H    H  N N 204 
HIS   H2   H  N N 205 
HIS   HA   H  N N 206 
HIS   HB2  H  N N 207 
HIS   HB3  H  N N 208 
HIS   HD1  H  N N 209 
HIS   HD2  H  N N 210 
HIS   HE1  H  N N 211 
HIS   HE2  H  N N 212 
HIS   HXT  H  N N 213 
HOH   O    O  N N 214 
HOH   H1   H  N N 215 
HOH   H2   H  N N 216 
ILE   N    N  N N 217 
ILE   CA   C  N S 218 
ILE   C    C  N N 219 
ILE   O    O  N N 220 
ILE   CB   C  N S 221 
ILE   CG1  C  N N 222 
ILE   CG2  C  N N 223 
ILE   CD1  C  N N 224 
ILE   OXT  O  N N 225 
ILE   H    H  N N 226 
ILE   H2   H  N N 227 
ILE   HA   H  N N 228 
ILE   HB   H  N N 229 
ILE   HG12 H  N N 230 
ILE   HG13 H  N N 231 
ILE   HG21 H  N N 232 
ILE   HG22 H  N N 233 
ILE   HG23 H  N N 234 
ILE   HD11 H  N N 235 
ILE   HD12 H  N N 236 
ILE   HD13 H  N N 237 
ILE   HXT  H  N N 238 
LEU   N    N  N N 239 
LEU   CA   C  N S 240 
LEU   C    C  N N 241 
LEU   O    O  N N 242 
LEU   CB   C  N N 243 
LEU   CG   C  N N 244 
LEU   CD1  C  N N 245 
LEU   CD2  C  N N 246 
LEU   OXT  O  N N 247 
LEU   H    H  N N 248 
LEU   H2   H  N N 249 
LEU   HA   H  N N 250 
LEU   HB2  H  N N 251 
LEU   HB3  H  N N 252 
LEU   HG   H  N N 253 
LEU   HD11 H  N N 254 
LEU   HD12 H  N N 255 
LEU   HD13 H  N N 256 
LEU   HD21 H  N N 257 
LEU   HD22 H  N N 258 
LEU   HD23 H  N N 259 
LEU   HXT  H  N N 260 
LYS   N    N  N N 261 
LYS   CA   C  N S 262 
LYS   C    C  N N 263 
LYS   O    O  N N 264 
LYS   CB   C  N N 265 
LYS   CG   C  N N 266 
LYS   CD   C  N N 267 
LYS   CE   C  N N 268 
LYS   NZ   N  N N 269 
LYS   OXT  O  N N 270 
LYS   H    H  N N 271 
LYS   H2   H  N N 272 
LYS   HA   H  N N 273 
LYS   HB2  H  N N 274 
LYS   HB3  H  N N 275 
LYS   HG2  H  N N 276 
LYS   HG3  H  N N 277 
LYS   HD2  H  N N 278 
LYS   HD3  H  N N 279 
LYS   HE2  H  N N 280 
LYS   HE3  H  N N 281 
LYS   HZ1  H  N N 282 
LYS   HZ2  H  N N 283 
LYS   HZ3  H  N N 284 
LYS   HXT  H  N N 285 
MET   N    N  N N 286 
MET   CA   C  N S 287 
MET   C    C  N N 288 
MET   O    O  N N 289 
MET   CB   C  N N 290 
MET   CG   C  N N 291 
MET   SD   S  N N 292 
MET   CE   C  N N 293 
MET   OXT  O  N N 294 
MET   H    H  N N 295 
MET   H2   H  N N 296 
MET   HA   H  N N 297 
MET   HB2  H  N N 298 
MET   HB3  H  N N 299 
MET   HG2  H  N N 300 
MET   HG3  H  N N 301 
MET   HE1  H  N N 302 
MET   HE2  H  N N 303 
MET   HE3  H  N N 304 
MET   HXT  H  N N 305 
PHE   N    N  N N 306 
PHE   CA   C  N S 307 
PHE   C    C  N N 308 
PHE   O    O  N N 309 
PHE   CB   C  N N 310 
PHE   CG   C  Y N 311 
PHE   CD1  C  Y N 312 
PHE   CD2  C  Y N 313 
PHE   CE1  C  Y N 314 
PHE   CE2  C  Y N 315 
PHE   CZ   C  Y N 316 
PHE   OXT  O  N N 317 
PHE   H    H  N N 318 
PHE   H2   H  N N 319 
PHE   HA   H  N N 320 
PHE   HB2  H  N N 321 
PHE   HB3  H  N N 322 
PHE   HD1  H  N N 323 
PHE   HD2  H  N N 324 
PHE   HE1  H  N N 325 
PHE   HE2  H  N N 326 
PHE   HZ   H  N N 327 
PHE   HXT  H  N N 328 
PRO   N    N  N N 329 
PRO   CA   C  N S 330 
PRO   C    C  N N 331 
PRO   O    O  N N 332 
PRO   CB   C  N N 333 
PRO   CG   C  N N 334 
PRO   CD   C  N N 335 
PRO   OXT  O  N N 336 
PRO   H    H  N N 337 
PRO   HA   H  N N 338 
PRO   HB2  H  N N 339 
PRO   HB3  H  N N 340 
PRO   HG2  H  N N 341 
PRO   HG3  H  N N 342 
PRO   HD2  H  N N 343 
PRO   HD3  H  N N 344 
PRO   HXT  H  N N 345 
SER   N    N  N N 346 
SER   CA   C  N S 347 
SER   C    C  N N 348 
SER   O    O  N N 349 
SER   CB   C  N N 350 
SER   OG   O  N N 351 
SER   OXT  O  N N 352 
SER   H    H  N N 353 
SER   H2   H  N N 354 
SER   HA   H  N N 355 
SER   HB2  H  N N 356 
SER   HB3  H  N N 357 
SER   HG   H  N N 358 
SER   HXT  H  N N 359 
SO4   S    S  N N 360 
SO4   O1   O  N N 361 
SO4   O2   O  N N 362 
SO4   O3   O  N N 363 
SO4   O4   O  N N 364 
THR   N    N  N N 365 
THR   CA   C  N S 366 
THR   C    C  N N 367 
THR   O    O  N N 368 
THR   CB   C  N R 369 
THR   OG1  O  N N 370 
THR   CG2  C  N N 371 
THR   OXT  O  N N 372 
THR   H    H  N N 373 
THR   H2   H  N N 374 
THR   HA   H  N N 375 
THR   HB   H  N N 376 
THR   HG1  H  N N 377 
THR   HG21 H  N N 378 
THR   HG22 H  N N 379 
THR   HG23 H  N N 380 
THR   HXT  H  N N 381 
TRP   N    N  N N 382 
TRP   CA   C  N S 383 
TRP   C    C  N N 384 
TRP   O    O  N N 385 
TRP   CB   C  N N 386 
TRP   CG   C  Y N 387 
TRP   CD1  C  Y N 388 
TRP   CD2  C  Y N 389 
TRP   NE1  N  Y N 390 
TRP   CE2  C  Y N 391 
TRP   CE3  C  Y N 392 
TRP   CZ2  C  Y N 393 
TRP   CZ3  C  Y N 394 
TRP   CH2  C  Y N 395 
TRP   OXT  O  N N 396 
TRP   H    H  N N 397 
TRP   H2   H  N N 398 
TRP   HA   H  N N 399 
TRP   HB2  H  N N 400 
TRP   HB3  H  N N 401 
TRP   HD1  H  N N 402 
TRP   HE1  H  N N 403 
TRP   HE3  H  N N 404 
TRP   HZ2  H  N N 405 
TRP   HZ3  H  N N 406 
TRP   HH2  H  N N 407 
TRP   HXT  H  N N 408 
TYR   N    N  N N 409 
TYR   CA   C  N S 410 
TYR   C    C  N N 411 
TYR   O    O  N N 412 
TYR   CB   C  N N 413 
TYR   CG   C  Y N 414 
TYR   CD1  C  Y N 415 
TYR   CD2  C  Y N 416 
TYR   CE1  C  Y N 417 
TYR   CE2  C  Y N 418 
TYR   CZ   C  Y N 419 
TYR   OH   O  N N 420 
TYR   OXT  O  N N 421 
TYR   H    H  N N 422 
TYR   H2   H  N N 423 
TYR   HA   H  N N 424 
TYR   HB2  H  N N 425 
TYR   HB3  H  N N 426 
TYR   HD1  H  N N 427 
TYR   HD2  H  N N 428 
TYR   HE1  H  N N 429 
TYR   HE2  H  N N 430 
TYR   HH   H  N N 431 
TYR   HXT  H  N N 432 
VAL   N    N  N N 433 
VAL   CA   C  N S 434 
VAL   C    C  N N 435 
VAL   O    O  N N 436 
VAL   CB   C  N N 437 
VAL   CG1  C  N N 438 
VAL   CG2  C  N N 439 
VAL   OXT  O  N N 440 
VAL   H    H  N N 441 
VAL   H2   H  N N 442 
VAL   HA   H  N N 443 
VAL   HB   H  N N 444 
VAL   HG11 H  N N 445 
VAL   HG12 H  N N 446 
VAL   HG13 H  N N 447 
VAL   HG21 H  N N 448 
VAL   HG22 H  N N 449 
VAL   HG23 H  N N 450 
VAL   HXT  H  N N 451 
# 
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 
A1AQY C1  C2   doub Y N 1   
A1AQY C1  C6   sing Y N 2   
A1AQY C2  C3   sing Y N 3   
A1AQY C3  C4   doub Y N 4   
A1AQY C4  C5   sing Y N 5   
A1AQY C5  C6   doub Y N 6   
A1AQY C14 C15  doub Y N 7   
A1AQY C14 C19  sing Y N 8   
A1AQY C15 C16  sing Y N 9   
A1AQY C16 C17  doub Y N 10  
A1AQY C17 C18  sing Y N 11  
A1AQY C18 C19  doub Y N 12  
A1AQY C1  N7   sing N N 13  
A1AQY C2  C10  sing N N 14  
A1AQY C3  CL1  sing N N 15  
A1AQY C15 CL2  sing N N 16  
A1AQY C4  N12  sing N N 17  
A1AQY C14 N12  sing N N 18  
A1AQY C16 N21  sing N N 19  
A1AQY N7  C8   doub N N 20  
A1AQY C8  N9   sing N N 21  
A1AQY C10 N9   sing N N 22  
A1AQY N9  C13  sing N N 23  
A1AQY C10 O11  doub N N 24  
A1AQY C19 F20  sing N N 25  
A1AQY N21 S22  sing N N 26  
A1AQY S22 N23  sing N N 27  
A1AQY S22 O27  doub N N 28  
A1AQY S22 O28  doub N N 29  
A1AQY N23 C24  sing N N 30  
A1AQY N23 C26  sing N N 31  
A1AQY C24 C25  sing N N 32  
A1AQY C25 C26  sing N N 33  
A1AQY C25 F29  sing N N 34  
A1AQY C13 H1   sing N N 35  
A1AQY C13 H2   sing N N 36  
A1AQY C13 H3   sing N N 37  
A1AQY C8  H4   sing N N 38  
A1AQY C5  H5   sing N N 39  
A1AQY C6  H6   sing N N 40  
A1AQY C24 H7   sing N N 41  
A1AQY C24 H8   sing N N 42  
A1AQY C25 H9   sing N N 43  
A1AQY C26 H10  sing N N 44  
A1AQY C26 H11  sing N N 45  
A1AQY N12 H12  sing N N 46  
A1AQY N21 H13  sing N N 47  
A1AQY C17 H14  sing N N 48  
A1AQY C18 H16  sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
DMS   S   O    doub N N 132 
DMS   S   C1   sing N N 133 
DMS   S   C2   sing N N 134 
DMS   C1  H11  sing N N 135 
DMS   C1  H12  sing N N 136 
DMS   C1  H13  sing N N 137 
DMS   C2  H21  sing N N 138 
DMS   C2  H22  sing N N 139 
DMS   C2  H23  sing N N 140 
GLN   N   CA   sing N N 141 
GLN   N   H    sing N N 142 
GLN   N   H2   sing N N 143 
GLN   CA  C    sing N N 144 
GLN   CA  CB   sing N N 145 
GLN   CA  HA   sing N N 146 
GLN   C   O    doub N N 147 
GLN   C   OXT  sing N N 148 
GLN   CB  CG   sing N N 149 
GLN   CB  HB2  sing N N 150 
GLN   CB  HB3  sing N N 151 
GLN   CG  CD   sing N N 152 
GLN   CG  HG2  sing N N 153 
GLN   CG  HG3  sing N N 154 
GLN   CD  OE1  doub N N 155 
GLN   CD  NE2  sing N N 156 
GLN   NE2 HE21 sing N N 157 
GLN   NE2 HE22 sing N N 158 
GLN   OXT HXT  sing N N 159 
GLU   N   CA   sing N N 160 
GLU   N   H    sing N N 161 
GLU   N   H2   sing N N 162 
GLU   CA  C    sing N N 163 
GLU   CA  CB   sing N N 164 
GLU   CA  HA   sing N N 165 
GLU   C   O    doub N N 166 
GLU   C   OXT  sing N N 167 
GLU   CB  CG   sing N N 168 
GLU   CB  HB2  sing N N 169 
GLU   CB  HB3  sing N N 170 
GLU   CG  CD   sing N N 171 
GLU   CG  HG2  sing N N 172 
GLU   CG  HG3  sing N N 173 
GLU   CD  OE1  doub N N 174 
GLU   CD  OE2  sing N N 175 
GLU   OE2 HE2  sing N N 176 
GLU   OXT HXT  sing N N 177 
GLY   N   CA   sing N N 178 
GLY   N   H    sing N N 179 
GLY   N   H2   sing N N 180 
GLY   CA  C    sing N N 181 
GLY   CA  HA2  sing N N 182 
GLY   CA  HA3  sing N N 183 
GLY   C   O    doub N N 184 
GLY   C   OXT  sing N N 185 
GLY   OXT HXT  sing N N 186 
HIS   N   CA   sing N N 187 
HIS   N   H    sing N N 188 
HIS   N   H2   sing N N 189 
HIS   CA  C    sing N N 190 
HIS   CA  CB   sing N N 191 
HIS   CA  HA   sing N N 192 
HIS   C   O    doub N N 193 
HIS   C   OXT  sing N N 194 
HIS   CB  CG   sing N N 195 
HIS   CB  HB2  sing N N 196 
HIS   CB  HB3  sing N N 197 
HIS   CG  ND1  sing Y N 198 
HIS   CG  CD2  doub Y N 199 
HIS   ND1 CE1  doub Y N 200 
HIS   ND1 HD1  sing N N 201 
HIS   CD2 NE2  sing Y N 202 
HIS   CD2 HD2  sing N N 203 
HIS   CE1 NE2  sing Y N 204 
HIS   CE1 HE1  sing N N 205 
HIS   NE2 HE2  sing N N 206 
HIS   OXT HXT  sing N N 207 
HOH   O   H1   sing N N 208 
HOH   O   H2   sing N N 209 
ILE   N   CA   sing N N 210 
ILE   N   H    sing N N 211 
ILE   N   H2   sing N N 212 
ILE   CA  C    sing N N 213 
ILE   CA  CB   sing N N 214 
ILE   CA  HA   sing N N 215 
ILE   C   O    doub N N 216 
ILE   C   OXT  sing N N 217 
ILE   CB  CG1  sing N N 218 
ILE   CB  CG2  sing N N 219 
ILE   CB  HB   sing N N 220 
ILE   CG1 CD1  sing N N 221 
ILE   CG1 HG12 sing N N 222 
ILE   CG1 HG13 sing N N 223 
ILE   CG2 HG21 sing N N 224 
ILE   CG2 HG22 sing N N 225 
ILE   CG2 HG23 sing N N 226 
ILE   CD1 HD11 sing N N 227 
ILE   CD1 HD12 sing N N 228 
ILE   CD1 HD13 sing N N 229 
ILE   OXT HXT  sing N N 230 
LEU   N   CA   sing N N 231 
LEU   N   H    sing N N 232 
LEU   N   H2   sing N N 233 
LEU   CA  C    sing N N 234 
LEU   CA  CB   sing N N 235 
LEU   CA  HA   sing N N 236 
LEU   C   O    doub N N 237 
LEU   C   OXT  sing N N 238 
LEU   CB  CG   sing N N 239 
LEU   CB  HB2  sing N N 240 
LEU   CB  HB3  sing N N 241 
LEU   CG  CD1  sing N N 242 
LEU   CG  CD2  sing N N 243 
LEU   CG  HG   sing N N 244 
LEU   CD1 HD11 sing N N 245 
LEU   CD1 HD12 sing N N 246 
LEU   CD1 HD13 sing N N 247 
LEU   CD2 HD21 sing N N 248 
LEU   CD2 HD22 sing N N 249 
LEU   CD2 HD23 sing N N 250 
LEU   OXT HXT  sing N N 251 
LYS   N   CA   sing N N 252 
LYS   N   H    sing N N 253 
LYS   N   H2   sing N N 254 
LYS   CA  C    sing N N 255 
LYS   CA  CB   sing N N 256 
LYS   CA  HA   sing N N 257 
LYS   C   O    doub N N 258 
LYS   C   OXT  sing N N 259 
LYS   CB  CG   sing N N 260 
LYS   CB  HB2  sing N N 261 
LYS   CB  HB3  sing N N 262 
LYS   CG  CD   sing N N 263 
LYS   CG  HG2  sing N N 264 
LYS   CG  HG3  sing N N 265 
LYS   CD  CE   sing N N 266 
LYS   CD  HD2  sing N N 267 
LYS   CD  HD3  sing N N 268 
LYS   CE  NZ   sing N N 269 
LYS   CE  HE2  sing N N 270 
LYS   CE  HE3  sing N N 271 
LYS   NZ  HZ1  sing N N 272 
LYS   NZ  HZ2  sing N N 273 
LYS   NZ  HZ3  sing N N 274 
LYS   OXT HXT  sing N N 275 
MET   N   CA   sing N N 276 
MET   N   H    sing N N 277 
MET   N   H2   sing N N 278 
MET   CA  C    sing N N 279 
MET   CA  CB   sing N N 280 
MET   CA  HA   sing N N 281 
MET   C   O    doub N N 282 
MET   C   OXT  sing N N 283 
MET   CB  CG   sing N N 284 
MET   CB  HB2  sing N N 285 
MET   CB  HB3  sing N N 286 
MET   CG  SD   sing N N 287 
MET   CG  HG2  sing N N 288 
MET   CG  HG3  sing N N 289 
MET   SD  CE   sing N N 290 
MET   CE  HE1  sing N N 291 
MET   CE  HE2  sing N N 292 
MET   CE  HE3  sing N N 293 
MET   OXT HXT  sing N N 294 
PHE   N   CA   sing N N 295 
PHE   N   H    sing N N 296 
PHE   N   H2   sing N N 297 
PHE   CA  C    sing N N 298 
PHE   CA  CB   sing N N 299 
PHE   CA  HA   sing N N 300 
PHE   C   O    doub N N 301 
PHE   C   OXT  sing N N 302 
PHE   CB  CG   sing N N 303 
PHE   CB  HB2  sing N N 304 
PHE   CB  HB3  sing N N 305 
PHE   CG  CD1  doub Y N 306 
PHE   CG  CD2  sing Y N 307 
PHE   CD1 CE1  sing Y N 308 
PHE   CD1 HD1  sing N N 309 
PHE   CD2 CE2  doub Y N 310 
PHE   CD2 HD2  sing N N 311 
PHE   CE1 CZ   doub Y N 312 
PHE   CE1 HE1  sing N N 313 
PHE   CE2 CZ   sing Y N 314 
PHE   CE2 HE2  sing N N 315 
PHE   CZ  HZ   sing N N 316 
PHE   OXT HXT  sing N N 317 
PRO   N   CA   sing N N 318 
PRO   N   CD   sing N N 319 
PRO   N   H    sing N N 320 
PRO   CA  C    sing N N 321 
PRO   CA  CB   sing N N 322 
PRO   CA  HA   sing N N 323 
PRO   C   O    doub N N 324 
PRO   C   OXT  sing N N 325 
PRO   CB  CG   sing N N 326 
PRO   CB  HB2  sing N N 327 
PRO   CB  HB3  sing N N 328 
PRO   CG  CD   sing N N 329 
PRO   CG  HG2  sing N N 330 
PRO   CG  HG3  sing N N 331 
PRO   CD  HD2  sing N N 332 
PRO   CD  HD3  sing N N 333 
PRO   OXT HXT  sing N N 334 
SER   N   CA   sing N N 335 
SER   N   H    sing N N 336 
SER   N   H2   sing N N 337 
SER   CA  C    sing N N 338 
SER   CA  CB   sing N N 339 
SER   CA  HA   sing N N 340 
SER   C   O    doub N N 341 
SER   C   OXT  sing N N 342 
SER   CB  OG   sing N N 343 
SER   CB  HB2  sing N N 344 
SER   CB  HB3  sing N N 345 
SER   OG  HG   sing N N 346 
SER   OXT HXT  sing N N 347 
SO4   S   O1   doub N N 348 
SO4   S   O2   doub N N 349 
SO4   S   O3   sing N N 350 
SO4   S   O4   sing N N 351 
THR   N   CA   sing N N 352 
THR   N   H    sing N N 353 
THR   N   H2   sing N N 354 
THR   CA  C    sing N N 355 
THR   CA  CB   sing N N 356 
THR   CA  HA   sing N N 357 
THR   C   O    doub N N 358 
THR   C   OXT  sing N N 359 
THR   CB  OG1  sing N N 360 
THR   CB  CG2  sing N N 361 
THR   CB  HB   sing N N 362 
THR   OG1 HG1  sing N N 363 
THR   CG2 HG21 sing N N 364 
THR   CG2 HG22 sing N N 365 
THR   CG2 HG23 sing N N 366 
THR   OXT HXT  sing N N 367 
TRP   N   CA   sing N N 368 
TRP   N   H    sing N N 369 
TRP   N   H2   sing N N 370 
TRP   CA  C    sing N N 371 
TRP   CA  CB   sing N N 372 
TRP   CA  HA   sing N N 373 
TRP   C   O    doub N N 374 
TRP   C   OXT  sing N N 375 
TRP   CB  CG   sing N N 376 
TRP   CB  HB2  sing N N 377 
TRP   CB  HB3  sing N N 378 
TRP   CG  CD1  doub Y N 379 
TRP   CG  CD2  sing Y N 380 
TRP   CD1 NE1  sing Y N 381 
TRP   CD1 HD1  sing N N 382 
TRP   CD2 CE2  doub Y N 383 
TRP   CD2 CE3  sing Y N 384 
TRP   NE1 CE2  sing Y N 385 
TRP   NE1 HE1  sing N N 386 
TRP   CE2 CZ2  sing Y N 387 
TRP   CE3 CZ3  doub Y N 388 
TRP   CE3 HE3  sing N N 389 
TRP   CZ2 CH2  doub Y N 390 
TRP   CZ2 HZ2  sing N N 391 
TRP   CZ3 CH2  sing Y N 392 
TRP   CZ3 HZ3  sing N N 393 
TRP   CH2 HH2  sing N N 394 
TRP   OXT HXT  sing N N 395 
TYR   N   CA   sing N N 396 
TYR   N   H    sing N N 397 
TYR   N   H2   sing N N 398 
TYR   CA  C    sing N N 399 
TYR   CA  CB   sing N N 400 
TYR   CA  HA   sing N N 401 
TYR   C   O    doub N N 402 
TYR   C   OXT  sing N N 403 
TYR   CB  CG   sing N N 404 
TYR   CB  HB2  sing N N 405 
TYR   CB  HB3  sing N N 406 
TYR   CG  CD1  doub Y N 407 
TYR   CG  CD2  sing Y N 408 
TYR   CD1 CE1  sing Y N 409 
TYR   CD1 HD1  sing N N 410 
TYR   CD2 CE2  doub Y N 411 
TYR   CD2 HD2  sing N N 412 
TYR   CE1 CZ   doub Y N 413 
TYR   CE1 HE1  sing N N 414 
TYR   CE2 CZ   sing Y N 415 
TYR   CE2 HE2  sing N N 416 
TYR   CZ  OH   sing N N 417 
TYR   OH  HH   sing N N 418 
TYR   OXT HXT  sing N N 419 
VAL   N   CA   sing N N 420 
VAL   N   H    sing N N 421 
VAL   N   H2   sing N N 422 
VAL   CA  C    sing N N 423 
VAL   CA  CB   sing N N 424 
VAL   CA  HA   sing N N 425 
VAL   C   O    doub N N 426 
VAL   C   OXT  sing N N 427 
VAL   CB  CG1  sing N N 428 
VAL   CB  CG2  sing N N 429 
VAL   CB  HB   sing N N 430 
VAL   CG1 HG11 sing N N 431 
VAL   CG1 HG12 sing N N 432 
VAL   CG1 HG13 sing N N 433 
VAL   CG2 HG21 sing N N 434 
VAL   CG2 HG22 sing N N 435 
VAL   CG2 HG23 sing N N 436 
VAL   OXT HXT  sing N N 437 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4MNF 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 31 2 1' 
_space_group.name_Hall        
;P 31 2"
;
_space_group.IT_number        152 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BP8 
_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]   0.009968 
_atom_sites.fract_transf_matrix[1][2]   0.005755 
_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]   0.011510 
_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]   0.014490 
_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.
;
? 
F  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 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   . ASP   A 1 20  ? -62.81500 2.84400   30.96100  1.000 70.37000  ? 449  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 20  ? -62.96900 4.09000   30.21100  1.000 44.51000  ? 449  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 20  ? -61.64600 4.84000   30.09200  1.000 27.39000  ? 449  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 20  ? -60.75800 4.65100   30.91200  1.000 27.18000  ? 449  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 20  ? -63.97100 5.00900   30.87800  1.000 59.22000  ? 449  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 20  ? -64.41700 6.09900   29.96700  1.000 49.70000  ? 449  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 20  ? -64.97400 5.73800   28.89900  1.000 50.19000  ? 449  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 20  ? -64.09600 7.28300   30.27900  1.000 33.06000  ? 449  ASP   A OD2 1 
ATOM   9    N  N   . TRP   A 1 21  ? -61.52800 5.71900   29.09600  1.000 23.38000  ? 450  TRP   A N   1 
ATOM   10   C  CA  . TRP   A 1 21  ? -60.22800 6.32000   28.78500  1.000 20.32000  ? 450  TRP   A CA  1 
ATOM   11   C  C   . TRP   A 1 21  ? -60.10200 7.74900   29.28100  1.000 21.04000  ? 450  TRP   A C   1 
ATOM   12   O  O   . TRP   A 1 21  ? -59.02800 8.33600   29.12600  1.000 18.30000  ? 450  TRP   A O   1 
ATOM   13   C  CB  . TRP   A 1 21  ? -59.95200 6.29200   27.25600  1.000 20.50000  ? 450  TRP   A CB  1 
ATOM   14   C  CG  . TRP   A 1 21  ? -59.90800 4.85100   26.80400  1.000 19.28000  ? 450  TRP   A CG  1 
ATOM   15   C  CD1 . TRP   A 1 21  ? -60.86300 4.17400   26.06100  1.000 24.01000  ? 450  TRP   A CD1 1 
ATOM   16   C  CD2 . TRP   A 1 21  ? -58.89300 3.92000   27.11800  1.000 18.46000  ? 450  TRP   A CD2 1 
ATOM   17   N  NE1 . TRP   A 1 21  ? -60.47400 2.85700   25.90000  1.000 20.66000  ? 450  TRP   A NE1 1 
ATOM   18   C  CE2 . TRP   A 1 21  ? -59.27200 2.66900   26.53600  1.000 17.72000  ? 450  TRP   A CE2 1 
ATOM   19   C  CE3 . TRP   A 1 21  ? -57.69600 4.00100   27.83400  1.000 18.23000  ? 450  TRP   A CE3 1 
ATOM   20   C  CZ2 . TRP   A 1 21  ? -58.49000 1.51300   26.67500  1.000 20.39000  ? 450  TRP   A CZ2 1 
ATOM   21   C  CZ3 . TRP   A 1 21  ? -56.93900 2.83800   28.02400  1.000 18.80000  ? 450  TRP   A CZ3 1 
ATOM   22   C  CH2 . TRP   A 1 21  ? -57.33700 1.60500   27.39800  1.000 21.14000  ? 450  TRP   A CH2 1 
ATOM   23   N  N   . GLU   A 1 22  ? -61.14600 8.31300   29.89800  1.000 17.58000  ? 451  GLU   A N   1 
ATOM   24   C  CA  . GLU   A 1 22  ? -60.96900 9.63300   30.49400  1.000 18.55000  ? 451  GLU   A CA  1 
ATOM   25   C  C   . GLU   A 1 22  ? -60.14200 9.53400   31.76500  1.000 20.35000  ? 451  GLU   A C   1 
ATOM   26   O  O   . GLU   A 1 22  ? -60.42100 8.70100   32.62800  1.000 23.79000  ? 451  GLU   A O   1 
ATOM   27   C  CB  . GLU   A 1 22  ? -62.34300 10.25600  30.79700  1.000 20.62000  ? 451  GLU   A CB  1 
ATOM   28   C  CG  . GLU   A 1 22  ? -62.08700 11.73300  31.24900  1.000 19.57000  ? 451  GLU   A CG  1 
ATOM   29   C  CD  . GLU   A 1 22  ? -63.38600 12.58400  31.42200  1.000 33.06000  ? 451  GLU   A CD  1 
ATOM   30   O  OE1 . GLU   A 1 22  ? -64.48700 12.18200  30.99200  1.000 31.77000  ? 451  GLU   A OE1 1 
ATOM   31   O  OE2 . GLU   A 1 22  ? -63.27200 13.70400  31.97000  1.000 33.83000  ? 451  GLU   A OE2 1 
ATOM   32   N  N   . ILE   A 1 23  ? -59.12700 10.37900  31.90800  1.000 18.13000  ? 452  ILE   A N   1 
ATOM   33   C  CA  . ILE   A 1 23  ? -58.31300 10.42700  33.12300  1.000 20.66000  ? 452  ILE   A CA  1 
ATOM   34   C  C   . ILE   A 1 23  ? -58.90600 11.49000  34.04400  1.000 22.92000  ? 452  ILE   A C   1 
ATOM   35   O  O   . ILE   A 1 23  ? -58.94400 12.67200  33.66400  1.000 24.44000  ? 452  ILE   A O   1 
ATOM   36   C  CB  . ILE   A 1 23  ? -56.84700 10.74500  32.78900  1.000 18.94000  ? 452  ILE   A CB  1 
ATOM   37   C  CG1 . ILE   A 1 23  ? -56.27200 9.60900   31.91500  1.000 20.65000  ? 452  ILE   A CG1 1 
ATOM   38   C  CG2 . ILE   A 1 23  ? -56.02100 10.96500  34.05500  1.000 19.66000  ? 452  ILE   A CG2 1 
ATOM   39   C  CD1 . ILE   A 1 23  ? -54.94400 9.91400   31.21200  1.000 17.01000  ? 452  ILE   A CD1 1 
ATOM   40   N  N   . PRO   A 1 24  ? -59.31300 11.14800  35.27000  1.000 29.73000  ? 453  PRO   A N   1 
ATOM   41   C  CA  . PRO   A 1 24  ? -59.92900 12.16800  36.13900  1.000 35.42000  ? 453  PRO   A CA  1 
ATOM   42   C  C   . PRO   A 1 24  ? -58.93500 13.26400  36.49300  1.000 31.45000  ? 453  PRO   A C   1 
ATOM   43   O  O   . PRO   A 1 24  ? -57.74300 12.98600  36.65100  1.000 26.39000  ? 453  PRO   A O   1 
ATOM   44   C  CB  . PRO   A 1 24  ? -60.34000 11.36400  37.39000  1.000 38.84000  ? 453  PRO   A CB  1 
ATOM   45   C  CG  . PRO   A 1 24  ? -60.35300 9.92200   36.95600  1.000 35.89000  ? 453  PRO   A CG  1 
ATOM   46   C  CD  . PRO   A 1 24  ? -59.32700 9.79900   35.84000  1.000 31.23000  ? 453  PRO   A CD  1 
ATOM   47   N  N   . ASP   A 1 25  ? -59.41200 14.51600  36.64800  1.000 30.62000  ? 454  ASP   A N   1 
ATOM   48   C  CA  . ASP   A 1 25  ? -58.48800 15.61200  37.00100  1.000 37.70000  ? 454  ASP   A CA  1 
ATOM   49   C  C   . ASP   A 1 25  ? -57.83100 15.29700  38.33600  1.000 28.07000  ? 454  ASP   A C   1 
ATOM   50   O  O   . ASP   A 1 25  ? -58.37500 14.54500  39.16000  1.000 30.12000  ? 454  ASP   A O   1 
ATOM   51   C  CB  . ASP   A 1 25  ? -59.17700 17.00500  37.11600  1.000 49.08000  ? 454  ASP   A CB  1 
ATOM   52   C  CG  . ASP   A 1 25  ? -58.14700 18.20600  37.09200  1.000 62.02000  ? 454  ASP   A CG  1 
ATOM   53   O  OD1 . ASP   A 1 25  ? -56.99400 17.98200  36.64100  1.000 55.59000  ? 454  ASP   A OD1 1 
ATOM   54   O  OD2 . ASP   A 1 25  ? -58.45000 19.36000  37.55700  1.000 50.15000  ? 454  ASP   A OD2 1 
ATOM   55   N  N   . GLY   A 1 26  ? -56.64200 15.85700  38.53800  1.000 27.57000  ? 455  GLY   A N   1 
ATOM   56   C  CA  . GLY   A 1 26  ? -55.88600 15.60300  39.72200  1.000 28.99000  ? 455  GLY   A CA  1 
ATOM   57   C  C   . GLY   A 1 26  ? -54.92600 14.45200  39.61200  1.000 30.97000  ? 455  GLY   A C   1 
ATOM   58   O  O   . GLY   A 1 26  ? -54.03800 14.33900  40.45400  1.000 31.33000  ? 455  GLY   A O   1 
ATOM   59   N  N   . GLN   A 1 27  ? -55.06400 13.58900  38.58200  1.000 22.35000  ? 456  GLN   A N   1 
ATOM   60   C  CA  . GLN   A 1 27  ? -54.17300 12.44400  38.50300  1.000 21.26000  ? 456  GLN   A CA  1 
ATOM   61   C  C   . GLN   A 1 27  ? -52.91200 12.71600  37.69100  1.000 18.95000  ? 456  GLN   A C   1 
ATOM   62   O  O   . GLN   A 1 27  ? -51.86900 12.12800  37.96900  1.000 22.14000  ? 456  GLN   A O   1 
ATOM   63   C  CB  . GLN   A 1 27  ? -54.93200 11.24800  37.88300  1.000 21.47000  ? 456  GLN   A CB  1 
ATOM   64   C  CG  . GLN   A 1 27  ? -56.03100 10.71400  38.82600  1.000 23.68000  ? 456  GLN   A CG  1 
ATOM   65   C  CD  . GLN   A 1 27  ? -56.49100 9.27800   38.37600  1.000 29.78000  ? 456  GLN   A CD  1 
ATOM   66   O  OE1 . GLN   A 1 27  ? -55.89100 8.65900   37.47400  1.000 25.01000  ? 456  GLN   A OE1 1 
ATOM   67   N  NE2 . GLN   A 1 27  ? -57.57700 8.78400   38.97200  1.000 31.69000  ? 456  GLN   A NE2 1 
ATOM   68   N  N   . ILE   A 1 28  ? -52.95700 13.60300  36.70500  1.000 18.87000  ? 457  ILE   A N   1 
ATOM   69   C  CA  . ILE   A 1 28  ? -51.76400 13.87400  35.91900  1.000 17.06000  ? 457  ILE   A CA  1 
ATOM   70   C  C   . ILE   A 1 28  ? -50.95300 14.98800  36.56300  1.000 22.63000  ? 457  ILE   A C   1 
ATOM   71   O  O   . ILE   A 1 28  ? -51.51800 16.02100  36.96100  1.000 25.51000  ? 457  ILE   A O   1 
ATOM   72   C  CB  . ILE   A 1 28  ? -52.15100 14.24800  34.48800  1.000 18.62000  ? 457  ILE   A CB  1 
ATOM   73   C  CG1 . ILE   A 1 28  ? -52.93700 13.09200  33.84500  1.000 20.50000  ? 457  ILE   A CG1 1 
ATOM   74   C  CG2 . ILE   A 1 28  ? -50.86300 14.58300  33.66900  1.000 23.56000  ? 457  ILE   A CG2 1 
ATOM   75   C  CD1 . ILE   A 1 28  ? -53.70500 13.60100  32.62900  1.000 25.62000  ? 457  ILE   A CD1 1 
ATOM   76   N  N   . THR   A 1 29  ? -49.65300 14.77800  36.70100  1.000 17.51000  ? 458  THR   A N   1 
ATOM   77   C  CA  . THR   A 1 29  ? -48.74700 15.87700  37.10000  1.000 18.65000  ? 458  THR   A CA  1 
ATOM   78   C  C   . THR   A 1 29  ? -48.03500 16.44000  35.87700  1.000 20.02000  ? 458  THR   A C   1 
ATOM   79   O  O   . THR   A 1 29  ? -47.26600 15.72500  35.22200  1.000 20.24000  ? 458  THR   A O   1 
ATOM   80   C  CB  . THR   A 1 29  ? -47.73200 15.40500  38.12000  1.000 20.41000  ? 458  THR   A CB  1 
ATOM   81   O  OG1 . THR   A 1 29  ? -48.44800 14.95400  39.25600  1.000 21.65000  ? 458  THR   A OG1 1 
ATOM   82   C  CG2 . THR   A 1 29  ? -46.85300 16.56700  38.60600  1.000 23.34000  ? 458  THR   A CG2 1 
ATOM   83   N  N   . VAL   A 1 30  ? -48.22900 17.74600  35.60300  1.000 18.45000  ? 459  VAL   A N   1 
ATOM   84   C  CA  . VAL   A 1 30  ? -47.58700 18.35100  34.41900  1.000 17.23000  ? 459  VAL   A CA  1 
ATOM   85   C  C   . VAL   A 1 30  ? -46.13900 18.71800  34.73700  1.000 17.49000  ? 459  VAL   A C   1 
ATOM   86   O  O   . VAL   A 1 30  ? -45.85400 19.26500  35.81800  1.000 17.48000  ? 459  VAL   A O   1 
ATOM   87   C  CB  . VAL   A 1 30  ? -48.39400 19.58800  33.95200  1.000 21.01000  ? 459  VAL   A CB  1 
ATOM   88   C  CG1 . VAL   A 1 30  ? -47.61500 20.44200  32.88600  1.000 18.87000  ? 459  VAL   A CG1 1 
ATOM   89   C  CG2 . VAL   A 1 30  ? -49.77000 19.14400  33.39500  1.000 19.89000  ? 459  VAL   A CG2 1 
ATOM   90   N  N   . GLY   A 1 31  ? -45.22100 18.48500  33.77200  1.000 16.87000  ? 460  GLY   A N   1 
ATOM   91   C  CA  . GLY   A 1 31  ? -43.79400 18.78200  33.85700  1.000 14.34000  ? 460  GLY   A CA  1 
ATOM   92   C  C   . GLY   A 1 31  ? -43.34600 19.66900  32.70700  1.000 16.97000  ? 460  GLY   A C   1 
ATOM   93   O  O   . GLY   A 1 31  ? -44.04200 20.58500  32.29800  1.000 16.08000  ? 460  GLY   A O   1 
ATOM   94   N  N   . GLN   A 1 32  ? -42.15300 19.34600  32.18600  1.000 15.82000  ? 461  GLN   A N   1 
ATOM   95   C  CA  . GLN   A 1 32  ? -41.45700 20.18200  31.19200  1.000 16.62000  ? 461  GLN   A CA  1 
ATOM   96   C  C   . GLN   A 1 32  ? -42.34500 20.52500  30.00300  1.000 18.84000  ? 461  GLN   A C   1 
ATOM   97   O  O   . GLN   A 1 32  ? -42.90500 19.61500  29.38300  1.000 16.25000  ? 461  GLN   A O   1 
ATOM   98   C  CB  . GLN   A 1 32  ? -40.28600 19.40100  30.60300  1.000 18.54000  ? 461  GLN   A CB  1 
ATOM   99   C  CG  . GLN   A 1 32  ? -39.27900 20.32400  29.95600  1.000 21.54000  ? 461  GLN   A CG  1 
ATOM   100  C  CD  . GLN   A 1 32  ? -38.08800 19.51000  29.45100  1.000 33.39000  ? 461  GLN   A CD  1 
ATOM   101  O  OE1 . GLN   A 1 32  ? -37.78600 18.43400  29.96800  1.000 34.12000  ? 461  GLN   A OE1 1 
ATOM   102  N  NE2 . GLN   A 1 32  ? -37.46100 19.99900  28.38000  1.000 31.38000  ? 461  GLN   A NE2 1 
ATOM   103  N  N   . ARG   A 1 33  ? -42.39900 21.82200  29.61000  1.000 14.43000  ? 462  ARG   A N   1 
ATOM   104  C  CA  . ARG   A 1 33  ? -43.05500 22.17900  28.34500  1.000 16.12000  ? 462  ARG   A CA  1 
ATOM   105  C  C   . ARG   A 1 33  ? -42.14900 21.80300  27.17200  1.000 16.39000  ? 462  ARG   A C   1 
ATOM   106  O  O   . ARG   A 1 33  ? -41.02100 22.29100  27.07800  1.000 17.68000  ? 462  ARG   A O   1 
ATOM   107  C  CB  . ARG   A 1 33  ? -43.40300 23.68200  28.28100  1.000 17.14000  ? 462  ARG   A CB  1 
ATOM   108  C  CG  . ARG   A 1 33  ? -44.22400 24.05400  27.01900  1.000 16.21000  ? 462  ARG   A CG  1 
ATOM   109  C  CD  . ARG   A 1 33  ? -44.73100 25.56300  27.03600  1.000 19.22000  ? 462  ARG   A CD  1 
ATOM   110  N  NE  . ARG   A 1 33  ? -43.57300 26.44200  26.91300  1.000 18.87000  ? 462  ARG   A NE  1 
ATOM   111  C  CZ  . ARG   A 1 33  ? -43.07400 26.80700  25.72000  1.000 19.61000  ? 462  ARG   A CZ  1 
ATOM   112  N  NH1 . ARG   A 1 33  ? -43.70800 26.52500  24.57600  1.000 19.61000  ? 462  ARG   A NH1 1 
ATOM   113  N  NH2 . ARG   A 1 33  ? -41.89100 27.40100  25.66400  1.000 20.60000  ? 462  ARG   A NH2 1 
ATOM   114  N  N   . ILE   A 1 34  ? -42.64000 20.92900  26.27500  1.000 13.98000  ? 463  ILE   A N   1 
ATOM   115  C  CA  . ILE   A 1 34  ? -41.80700 20.46400  25.17400  1.000 14.57000  ? 463  ILE   A CA  1 
ATOM   116  C  C   . ILE   A 1 34  ? -41.90300 21.40400  23.98700  1.000 16.02000  ? 463  ILE   A C   1 
ATOM   117  O  O   . ILE   A 1 34  ? -40.90700 21.61600  23.27900  1.000 17.96000  ? 463  ILE   A O   1 
ATOM   118  C  CB  . ILE   A 1 34  ? -42.21400 19.02700  24.78600  1.000 17.39000  ? 463  ILE   A CB  1 
ATOM   119  C  CG1 . ILE   A 1 34  ? -42.09800 18.12300  26.05300  1.000 16.58000  ? 463  ILE   A CG1 1 
ATOM   120  C  CG2 . ILE   A 1 34  ? -41.32200 18.50300  23.60900  1.000 20.67000  ? 463  ILE   A CG2 1 
ATOM   121  C  CD1 . ILE   A 1 34  ? -40.69400 18.19800  26.73600  1.000 17.86000  ? 463  ILE   A CD1 1 
ATOM   122  N  N   . GLY   A 1 35  ? -43.07900 21.96500  23.75400  1.000 16.04000  ? 464  GLY   A N   1 
ATOM   123  C  CA  . GLY   A 1 35  ? -43.19000 22.89800  22.64300  1.000 17.56000  ? 464  GLY   A CA  1 
ATOM   124  C  C   . GLY   A 1 35  ? -44.63900 23.20100  22.37500  1.000 21.09000  ? 464  GLY   A C   1 
ATOM   125  O  O   . GLY   A 1 35  ? -45.53100 22.41100  22.70700  1.000 18.37000  ? 464  GLY   A O   1 
ATOM   126  N  N   . SER   A 1 36  ? -44.88400 24.36500  21.75700  1.000 18.74000  ? 465  SER   A N   1 
ATOM   127  C  CA  . SER   A 1 36  ? -46.23500 24.82700  21.47700  1.000 20.84000  ? 465  SER   A CA  1 
ATOM   128  C  C   . SER   A 1 36  ? -46.33100 24.92200  19.96800  1.000 25.15000  ? 465  SER   A C   1 
ATOM   129  O  O   . SER   A 1 36  ? -45.60200 25.70700  19.35000  1.000 24.62000  ? 465  SER   A O   1 
ATOM   130  C  CB  . SER   A 1 36  ? -46.52200 26.17900  22.12700  1.000 19.13000  ? 465  SER   A CB  1 
ATOM   131  O  OG  . SER   A 1 36  ? -46.50600 26.06300  23.53400  1.000 20.95000  ? 465  SER   A OG  1 
ATOM   132  N  N   . GLY   A 1 37  ? -47.17100 24.09600  19.35900  1.000 23.22000  ? 466  GLY   A N   1 
ATOM   133  C  CA  . GLY   A 1 37  ? -47.33000 24.12400  17.91800  1.000 22.77000  ? 466  GLY   A CA  1 
ATOM   134  C  C   . GLY   A 1 37  ? -48.60100 24.84100  17.50200  1.000 32.16000  ? 466  GLY   A C   1 
ATOM   135  O  O   . GLY   A 1 37  ? -49.22700 25.56800  18.28400  1.000 32.59000  ? 466  GLY   A O   1 
ATOM   136  N  N   A SER   A 1 38  ? -49.01700 24.58900  16.25500  0.438 28.55000  ? 467  SER   A N   1 
ATOM   137  N  N   B SER   A 1 38  ? -49.02300 24.58100  16.26100  0.562 28.49000  ? 467  SER   A N   1 
ATOM   138  C  CA  A SER   A 1 38  ? -50.22000 25.23200  15.72800  0.438 30.59000  ? 467  SER   A CA  1 
ATOM   139  C  CA  B SER   A 1 38  ? -50.22800 25.22200  15.73700  0.562 30.56000  ? 467  SER   A CA  1 
ATOM   140  C  C   A SER   A 1 38  ? -51.48600 24.82000  16.46900  0.438 31.55000  ? 467  SER   A C   1 
ATOM   141  C  C   B SER   A 1 38  ? -51.47900 24.82900  16.50400  0.562 31.63000  ? 467  SER   A C   1 
ATOM   142  O  O   A SER   A 1 38  ? -52.41400 25.62500  16.59200  0.438 31.99000  ? 467  SER   A O   1 
ATOM   143  O  O   B SER   A 1 38  ? -52.38300 25.65100  16.68300  0.562 32.02000  ? 467  SER   A O   1 
ATOM   144  C  CB  A SER   A 1 38  ? -50.36400 24.93200  14.23600  0.438 32.63000  ? 467  SER   A CB  1 
ATOM   145  C  CB  B SER   A 1 38  ? -50.39200 24.86800  14.26800  0.562 32.67000  ? 467  SER   A CB  1 
ATOM   146  O  OG  A SER   A 1 38  ? -50.48100 23.53900  14.00000  0.438 24.52000  ? 467  SER   A OG  1 
ATOM   147  O  OG  B SER   A 1 38  ? -49.29400 25.37900  13.54800  0.562 33.23000  ? 467  SER   A OG  1 
ATOM   148  N  N   . PHE   A 1 39  ? -51.56000 23.59700  17.00200  1.000 23.42000  ? 468  PHE   A N   1 
ATOM   149  C  CA  . PHE   A 1 39  ? -52.81700 23.17400  17.58900  1.000 22.83000  ? 468  PHE   A CA  1 
ATOM   150  C  C   . PHE   A 1 39  ? -52.77300 22.87000  19.07900  1.000 31.77000  ? 468  PHE   A C   1 
ATOM   151  O  O   . PHE   A 1 39  ? -53.83100 22.75500  19.69700  1.000 41.95000  ? 468  PHE   A O   1 
ATOM   152  C  CB  . PHE   A 1 39  ? -53.39400 21.95100  16.87700  1.000 26.55000  ? 468  PHE   A CB  1 
ATOM   153  C  CG  . PHE   A 1 39  ? -54.81100 21.67300  17.27100  1.000 27.12000  ? 468  PHE   A CG  1 
ATOM   154  C  CD1 . PHE   A 1 39  ? -55.80900 22.65300  17.08900  1.000 28.86000  ? 468  PHE   A CD1 1 
ATOM   155  C  CD2 . PHE   A 1 39  ? -55.13200 20.48900  17.91300  1.000 37.80000  ? 468  PHE   A CD2 1 
ATOM   156  C  CE1 . PHE   A 1 39  ? -57.11900 22.41300  17.48300  1.000 35.45000  ? 468  PHE   A CE1 1 
ATOM   157  C  CE2 . PHE   A 1 39  ? -56.42600 20.22800  18.30200  1.000 40.45000  ? 468  PHE   A CE2 1 
ATOM   158  C  CZ  . PHE   A 1 39  ? -57.42700 21.18300  18.09700  1.000 37.72000  ? 468  PHE   A CZ  1 
ATOM   159  N  N   . GLY   A 1 40  ? -51.61900 22.69800  19.66700  1.000 31.13000  ? 469  GLY   A N   1 
ATOM   160  C  CA  . GLY   A 1 40  ? -51.68800 22.52800  21.11000  1.000 27.72000  ? 469  GLY   A CA  1 
ATOM   161  C  C   . GLY   A 1 40  ? -50.28700 22.63000  21.63500  1.000 28.41000  ? 469  GLY   A C   1 
ATOM   162  O  O   . GLY   A 1 40  ? -49.34900 22.87000  20.88200  1.000 26.24000  ? 469  GLY   A O   1 
ATOM   163  N  N   . THR   A 1 41  ? -50.14200 22.41100  22.93500  1.000 17.08000  ? 470  THR   A N   1 
ATOM   164  C  CA  . THR   A 1 41  ? -48.81800 22.43800  23.55400  1.000 14.36000  ? 470  THR   A CA  1 
ATOM   165  C  C   . THR   A 1 41  ? -48.57800 21.09200  24.21000  1.000 15.88000  ? 470  THR   A C   1 
ATOM   166  O  O   . THR   A 1 41  ? -49.45900 20.60000  24.91100  1.000 16.63000  ? 470  THR   A O   1 
ATOM   167  C  CB  . THR   A 1 41  ? -48.76300 23.52800  24.61400  1.000 20.71000  ? 470  THR   A CB  1 
ATOM   168  O  OG1 . THR   A 1 41  ? -48.95700 24.79200  23.94300  1.000 23.01000  ? 470  THR   A OG1 1 
ATOM   169  C  CG2 . THR   A 1 41  ? -47.44200 23.51100  25.41500  1.000 20.74000  ? 470  THR   A CG2 1 
ATOM   170  N  N   . VAL   A 1 42  ? -47.38800 20.55400  24.03600  1.000 16.28000  ? 471  VAL   A N   1 
ATOM   171  C  CA  . VAL   A 1 42  ? -47.04400 19.24600  24.60400  1.000 14.01000  ? 471  VAL   A CA  1 
ATOM   172  C  C   . VAL   A 1 42  ? -46.18300 19.48000  25.83300  1.000 14.79000  ? 471  VAL   A C   1 
ATOM   173  O  O   . VAL   A 1 42  ? -45.21400 20.27400  25.78300  1.000 14.89000  ? 471  VAL   A O   1 
ATOM   174  C  CB  . VAL   A 1 42  ? -46.31200 18.37400  23.57400  1.000 15.83000  ? 471  VAL   A CB  1 
ATOM   175  C  CG1 . VAL   A 1 42  ? -45.72500 17.10300  24.30200  1.000 15.37000  ? 471  VAL   A CG1 1 
ATOM   176  C  CG2 . VAL   A 1 42  ? -47.34900 18.02600  22.46500  1.000 17.37000  ? 471  VAL   A CG2 1 
ATOM   177  N  N   . TYR   A 1 43  ? -46.51600 18.77400  26.93300  1.000 14.12000  ? 472  TYR   A N   1 
ATOM   178  C  CA  . TYR   A 1 43  ? -45.73700 18.75600  28.17300  1.000 15.64000  ? 472  TYR   A CA  1 
ATOM   179  C  C   . TYR   A 1 43  ? -45.33600 17.32800  28.48800  1.000 16.88000  ? 472  TYR   A C   1 
ATOM   180  O  O   . TYR   A 1 43  ? -46.09200 16.41600  28.19200  1.000 17.55000  ? 472  TYR   A O   1 
ATOM   181  C  CB  . TYR   A 1 43  ? -46.55200 19.27300  29.40500  1.000 16.88000  ? 472  TYR   A CB  1 
ATOM   182  C  CG  . TYR   A 1 43  ? -47.02800 20.69900  29.24600  1.000 16.54000  ? 472  TYR   A CG  1 
ATOM   183  C  CD1 . TYR   A 1 43  ? -48.15400 20.98000  28.50700  1.000 16.69000  ? 472  TYR   A CD1 1 
ATOM   184  C  CD2 . TYR   A 1 43  ? -46.32500 21.75300  29.82300  1.000 14.57000  ? 472  TYR   A CD2 1 
ATOM   185  C  CE1 . TYR   A 1 43  ? -48.61200 22.32800  28.33900  1.000 14.27000  ? 472  TYR   A CE1 1 
ATOM   186  C  CE2 . TYR   A 1 43  ? -46.74500 23.09200  29.65100  1.000 15.89000  ? 472  TYR   A CE2 1 
ATOM   187  C  CZ  . TYR   A 1 43  ? -47.87500 23.33400  28.90500  1.000 18.57000  ? 472  TYR   A CZ  1 
ATOM   188  O  OH  . TYR   A 1 43  ? -48.35300 24.59600  28.71700  1.000 18.55000  ? 472  TYR   A OH  1 
ATOM   189  N  N   . LYS   A 1 44  ? -44.14400 17.13100  29.04800  1.000 13.60000  ? 473  LYS   A N   1 
ATOM   190  C  CA  . LYS   A 1 44  ? -43.89500 15.85500  29.72300  1.000 14.69000  ? 473  LYS   A CA  1 
ATOM   191  C  C   . LYS   A 1 44  ? -44.75200 15.80900  30.98600  1.000 18.44000  ? 473  LYS   A C   1 
ATOM   192  O  O   . LYS   A 1 44  ? -45.02100 16.84700  31.62600  1.000 21.02000  ? 473  LYS   A O   1 
ATOM   193  C  CB  . LYS   A 1 44  ? -42.38200 15.74300  30.01300  1.000 17.87000  ? 473  LYS   A CB  1 
ATOM   194  C  CG  . LYS   A 1 44  ? -41.96000 14.35900  30.55600  1.000 23.68000  ? 473  LYS   A CG  1 
ATOM   195  C  CD  . LYS   A 1 44  ? -40.41600 14.26800  30.47100  1.000 21.51000  ? 473  LYS   A CD  1 
ATOM   196  C  CE  . LYS   A 1 44  ? -40.04300 12.79300  30.58900  1.000 27.96000  ? 473  LYS   A CE  1 
ATOM   197  N  NZ  . LYS   A 1 44  ? -38.59700 12.61300  30.96600  1.000 28.57000  ? 473  LYS   A NZ  1 
ATOM   198  N  N   . GLY   A 1 45  ? -45.22900 14.61100  31.36300  1.000 16.06000  ? 474  GLY   A N   1 
ATOM   199  C  CA  . GLY   A 1 45  ? -46.12200 14.51500  32.49200  1.000 16.11000  ? 474  GLY   A CA  1 
ATOM   200  C  C   . GLY   A 1 45  ? -45.85400 13.22100  33.24600  1.000 15.96000  ? 474  GLY   A C   1 
ATOM   201  O  O   . GLY   A 1 45  ? -45.06300 12.37100  32.80600  1.000 15.24000  ? 474  GLY   A O   1 
ATOM   202  N  N   . LYS   A 1 46  ? -46.53600 13.09200  34.38200  1.000 16.89000  ? 475  LYS   A N   1 
ATOM   203  C  CA  . LYS   A 1 46  ? -46.46700 11.86200  35.18400  1.000 16.52000  ? 475  LYS   A CA  1 
ATOM   204  C  C   . LYS   A 1 46  ? -47.87700 11.35000  35.32900  1.000 18.73000  ? 475  LYS   A C   1 
ATOM   205  O  O   . LYS   A 1 46  ? -48.75800 12.06000  35.82500  1.000 18.44000  ? 475  LYS   A O   1 
ATOM   206  C  CB  . LYS   A 1 46  ? -45.85400 12.06900  36.58000  1.000 18.24000  ? 475  LYS   A CB  1 
ATOM   207  C  CG  . LYS   A 1 46  ? -44.37200 12.42400  36.53600  1.000 21.54000  ? 475  LYS   A CG  1 
ATOM   208  C  CD  . LYS   A 1 46  ? -43.51800 11.28000  36.09500  1.000 25.38000  ? 475  LYS   A CD  1 
ATOM   209  C  CE  . LYS   A 1 46  ? -42.06000 11.61300  36.45800  1.000 33.36000  ? 475  LYS   A CE  1 
ATOM   210  N  NZ  . LYS   A 1 46  ? -41.21800 10.39800  36.22300  1.000 39.53000  ? 475  LYS   A NZ  1 
ATOM   211  N  N   . TRP   A 1 47  ? -48.09300 10.09600  34.90500  1.000 15.40000  ? 476  TRP   A N   1 
ATOM   212  C  CA  . TRP   A 1 47  ? -49.37600 9.44100   35.14100  1.000 15.79000  ? 476  TRP   A CA  1 
ATOM   213  C  C   . TRP   A 1 47  ? -49.07500 7.95800   34.94000  1.000 19.21000  ? 476  TRP   A C   1 
ATOM   214  O  O   . TRP   A 1 47  ? -48.85600 7.53300   33.79400  1.000 16.27000  ? 476  TRP   A O   1 
ATOM   215  C  CB  . TRP   A 1 47  ? -50.44600 9.92400   34.16800  1.000 17.72000  ? 476  TRP   A CB  1 
ATOM   216  C  CG  . TRP   A 1 47  ? -51.80800 9.27300   34.48400  1.000 16.02000  ? 476  TRP   A CG  1 
ATOM   217  C  CD1 . TRP   A 1 47  ? -52.67400 9.60000   35.50900  1.000 16.18000  ? 476  TRP   A CD1 1 
ATOM   218  C  CD2 . TRP   A 1 47  ? -52.43300 8.19400   33.76200  1.000 16.72000  ? 476  TRP   A CD2 1 
ATOM   219  N  NE1 . TRP   A 1 47  ? -53.79200 8.79300   35.47800  1.000 17.49000  ? 476  TRP   A NE1 1 
ATOM   220  C  CE2 . TRP   A 1 47  ? -53.67900 7.93400   34.40300  1.000 16.46000  ? 476  TRP   A CE2 1 
ATOM   221  C  CE3 . TRP   A 1 47  ? -52.05500 7.42900   32.64800  1.000 16.24000  ? 476  TRP   A CE3 1 
ATOM   222  C  CZ2 . TRP   A 1 47  ? -54.56000 6.93100   33.98900  1.000 20.55000  ? 476  TRP   A CZ2 1 
ATOM   223  C  CZ3 . TRP   A 1 47  ? -52.97600 6.41100   32.20300  1.000 17.95000  ? 476  TRP   A CZ3 1 
ATOM   224  C  CH2 . TRP   A 1 47  ? -54.20900 6.19100   32.88800  1.000 18.55000  ? 476  TRP   A CH2 1 
ATOM   225  N  N   . HIS   A 1 48  ? -48.94600 7.21300   36.04600  1.000 18.27000  ? 477  HIS   A N   1 
ATOM   226  C  CA  . HIS   A 1 48  ? -48.39900 5.83200   35.96000  1.000 14.50000  ? 477  HIS   A CA  1 
ATOM   227  C  C   . HIS   A 1 48  ? -47.09800 5.82500   35.19200  1.000 18.16000  ? 477  HIS   A C   1 
ATOM   228  O  O   . HIS   A 1 48  ? -46.84500 4.97300   34.32000  1.000 19.06000  ? 477  HIS   A O   1 
ATOM   229  C  CB  . HIS   A 1 48  ? -49.43300 4.88700   35.30100  1.000 15.54000  ? 477  HIS   A CB  1 
ATOM   230  C  CG  . HIS   A 1 48  ? -50.70200 4.82300   36.06600  1.000 19.28000  ? 477  HIS   A CG  1 
ATOM   231  N  ND1 . HIS   A 1 48  ? -50.76200 4.31100   37.35200  1.000 21.76000  ? 477  HIS   A ND1 1 
ATOM   232  C  CD2 . HIS   A 1 48  ? -51.93800 5.28800   35.78000  1.000 17.02000  ? 477  HIS   A CD2 1 
ATOM   233  C  CE1 . HIS   A 1 48  ? -51.99400 4.46500   37.81400  1.000 20.14000  ? 477  HIS   A CE1 1 
ATOM   234  N  NE2 . HIS   A 1 48  ? -52.73100 5.03900   36.88100  1.000 21.13000  ? 477  HIS   A NE2 1 
ATOM   235  N  N   . GLY   A 1 49  ? -46.20700 6.75500   35.55600  1.000 14.87000  ? 478  GLY   A N   1 
ATOM   236  C  CA  . GLY   A 1 49  ? -44.91400 6.84600   34.93200  1.000 13.77000  ? 478  GLY   A CA  1 
ATOM   237  C  C   . GLY   A 1 49  ? -44.88800 8.03700   33.97600  1.000 16.66000  ? 478  GLY   A C   1 
ATOM   238  O  O   . GLY   A 1 49  ? -45.81000 8.84800   33.92000  1.000 18.95000  ? 478  GLY   A O   1 
ATOM   239  N  N   . ASP   A 1 50  ? -43.81700 8.11900   33.21400  1.000 14.73000  ? 479  ASP   A N   1 
ATOM   240  C  CA  . ASP   A 1 50  ? -43.73000 9.21300   32.22600  1.000 16.17000  ? 479  ASP   A CA  1 
ATOM   241  C  C   . ASP   A 1 50  ? -44.82300 9.09600   31.16500  1.000 14.16000  ? 479  ASP   A C   1 
ATOM   242  O  O   . ASP   A 1 50  ? -45.11600 7.98800   30.65100  1.000 16.32000  ? 479  ASP   A O   1 
ATOM   243  C  CB  . ASP   A 1 50  ? -42.36500 9.18900   31.53100  1.000 18.65000  ? 479  ASP   A CB  1 
ATOM   244  C  CG  . ASP   A 1 50  ? -41.21700 9.47300   32.48700  1.000 24.95000  ? 479  ASP   A CG  1 
ATOM   245  O  OD1 . ASP   A 1 50  ? -41.36700 10.26600  33.43300  1.000 21.33000  ? 479  ASP   A OD1 1 
ATOM   246  O  OD2 . ASP   A 1 50  ? -40.15300 8.93200   32.23800  1.000 25.77000  ? 479  ASP   A OD2 1 
ATOM   247  N  N   . VAL   A 1 51  ? -45.39400 10.23700  30.76300  1.000 13.78000  ? 480  VAL   A N   1 
ATOM   248  C  CA  . VAL   A 1 51  ? -46.35900 10.32200  29.66100  1.000 11.84000  ? 480  VAL   A CA  1 
ATOM   249  C  C   . VAL   A 1 51  ? -46.10200 11.65400  28.96800  1.000 14.76000  ? 480  VAL   A C   1 
ATOM   250  O  O   . VAL   A 1 51  ? -45.33800 12.50200  29.46000  1.000 15.76000  ? 480  VAL   A O   1 
ATOM   251  C  CB  . VAL   A 1 51  ? -47.85600 10.29800  30.08200  1.000 12.55000  ? 480  VAL   A CB  1 
ATOM   252  C  CG1 . VAL   A 1 51  ? -48.20100 8.92100   30.76600  1.000 13.19000  ? 480  VAL   A CG1 1 
ATOM   253  C  CG2 . VAL   A 1 51  ? -48.18300 11.45300  31.06900  1.000 13.50000  ? 480  VAL   A CG2 1 
ATOM   254  N  N   . ALA   A 1 52  ? -46.69400 11.79300  27.78400  1.000 13.15000  ? 481  ALA   A N   1 
ATOM   255  C  CA  . ALA   A 1 52  ? -46.77900 13.08400  27.09800  1.000 11.66000  ? 481  ALA   A CA  1 
ATOM   256  C  C   . ALA   A 1 52  ? -48.21100 13.55500  27.23900  1.000 15.36000  ? 481  ALA   A C   1 
ATOM   257  O  O   . ALA   A 1 52  ? -49.14400 12.77400  27.09500  1.000 15.36000  ? 481  ALA   A O   1 
ATOM   258  C  CB  . ALA   A 1 52  ? -46.41900 12.97900  25.59000  1.000 13.72000  ? 481  ALA   A CB  1 
ATOM   259  N  N   . VAL   A 1 53  ? -48.41000 14.83800  27.49400  1.000 14.20000  ? 482  VAL   A N   1 
ATOM   260  C  CA  . VAL   A 1 53  ? -49.74900 15.41500  27.61800  1.000 11.93000  ? 482  VAL   A CA  1 
ATOM   261  C  C   . VAL   A 1 53  ? -49.84500 16.54900  26.59200  1.000 14.17000  ? 482  VAL   A C   1 
ATOM   262  O  O   . VAL   A 1 53  ? -49.13200 17.54600  26.73800  1.000 15.65000  ? 482  VAL   A O   1 
ATOM   263  C  CB  . VAL   A 1 53  ? -49.98000 16.00100  29.02900  1.000 17.74000  ? 482  VAL   A CB  1 
ATOM   264  C  CG1 . VAL   A 1 53  ? -51.42300 16.46000  29.12100  1.000 19.24000  ? 482  VAL   A CG1 1 
ATOM   265  C  CG2 . VAL   A 1 53  ? -49.62700 14.92100  30.12000  1.000 18.46000  ? 482  VAL   A CG2 1 
ATOM   266  N  N   . LYS   A 1 54  ? -50.75100 16.43000  25.62400  1.000 12.76000  ? 483  LYS   A N   1 
ATOM   267  C  CA  . LYS   A 1 54  ? -50.94700 17.50300  24.63200  1.000 15.60000  ? 483  LYS   A CA  1 
ATOM   268  C  C   . LYS   A 1 54  ? -52.20000 18.26300  25.02500  1.000 16.34000  ? 483  LYS   A C   1 
ATOM   269  O  O   . LYS   A 1 54  ? -53.31500 17.74100  24.92800  1.000 17.43000  ? 483  LYS   A O   1 
ATOM   270  C  CB  . LYS   A 1 54  ? -51.04700 16.96800  23.20200  1.000 16.68000  ? 483  LYS   A CB  1 
ATOM   271  C  CG  . LYS   A 1 54  ? -51.20500 18.12900  22.13600  1.000 17.78000  ? 483  LYS   A CG  1 
ATOM   272  C  CD  . LYS   A 1 54  ? -51.28600 17.30300  20.82300  1.000 26.85000  ? 483  LYS   A CD  1 
ATOM   273  C  CE  . LYS   A 1 54  ? -50.28900 17.53500  19.79700  1.000 33.84000  ? 483  LYS   A CE  1 
ATOM   274  N  NZ  . LYS   A 1 54  ? -50.80900 16.83900  18.52500  1.000 24.87000  ? 483  LYS   A NZ  1 
ATOM   275  N  N   A MET   A 1 55  ? -52.00500 19.49400  25.53800  0.515 14.76000  ? 484  MET   A N   1 
ATOM   276  N  N   B MET   A 1 55  ? -52.03100 19.50800  25.46000  0.485 14.78000  ? 484  MET   A N   1 
ATOM   277  C  CA  A MET   A 1 55  ? -53.11900 20.37500  25.83800  0.515 17.81000  ? 484  MET   A CA  1 
ATOM   278  C  CA  B MET   A 1 55  ? -53.15500 20.30700  25.90600  0.485 17.74000  ? 484  MET   A CA  1 
ATOM   279  C  C   A MET   A 1 55  ? -53.59100 20.98700  24.53500  0.515 23.95000  ? 484  MET   A C   1 
ATOM   280  C  C   B MET   A 1 55  ? -53.64000 21.13400  24.72600  0.485 23.27000  ? 484  MET   A C   1 
ATOM   281  O  O   A MET   A 1 55  ? -52.78600 21.49600  23.74500  0.515 23.15000  ? 484  MET   A O   1 
ATOM   282  O  O   B MET   A 1 55  ? -52.88300 21.97800  24.23200  0.485 23.75000  ? 484  MET   A O   1 
ATOM   283  C  CB  A MET   A 1 55  ? -52.68900 21.46200  26.82900  0.515 20.81000  ? 484  MET   A CB  1 
ATOM   284  C  CB  B MET   A 1 55  ? -52.69500 21.22000  27.02500  0.485 20.53000  ? 484  MET   A CB  1 
ATOM   285  C  CG  A MET   A 1 55  ? -51.97000 20.86600  27.98100  0.515 19.65000  ? 484  MET   A CG  1 
ATOM   286  C  CG  B MET   A 1 55  ? -52.28300 20.57300  28.32300  0.485 22.97000  ? 484  MET   A CG  1 
ATOM   287  S  SD  A MET   A 1 55  ? -53.10900 20.16000  29.22400  0.515 27.38000  ? 484  MET   A SD  1 
ATOM   288  S  SD  B MET   A 1 55  ? -52.29900 21.93200  29.49500  0.485 27.79000  ? 484  MET   A SD  1 
ATOM   289  C  CE  A MET   A 1 55  ? -52.01900 20.28700  30.62700  0.515 19.85000  ? 484  MET   A CE  1 
ATOM   290  C  CE  B MET   A 1 55  ? -52.86500 23.14300  28.33000  0.485 35.35000  ? 484  MET   A CE  1 
ATOM   291  N  N   . LEU   A 1 56  ? -54.88700 20.88200  24.27400  1.000 20.94000  ? 485  LEU   A N   1 
ATOM   292  C  CA  . LEU   A 1 56  ? -55.43700 21.51400  23.09500  1.000 24.08000  ? 485  LEU   A CA  1 
ATOM   293  C  C   . LEU   A 1 56  ? -55.55900 23.02100  23.29100  1.000 26.74000  ? 485  LEU   A C   1 
ATOM   294  O  O   . LEU   A 1 56  ? -56.09600 23.51100  24.28600  1.000 30.87000  ? 485  LEU   A O   1 
ATOM   295  C  CB  . LEU   A 1 56  ? -56.81800 20.96500  22.74800  1.000 27.73000  ? 485  LEU   A CB  1 
ATOM   296  C  CG  . LEU   A 1 56  ? -56.86100 19.68900  21.94500  1.000 39.99000  ? 485  LEU   A CG  1 
ATOM   297  C  CD1 . LEU   A 1 56  ? -56.21500 18.64300  22.74500  1.000 31.88000  ? 485  LEU   A CD1 1 
ATOM   298  C  CD2 . LEU   A 1 56  ? -58.33300 19.32700  21.69500  1.000 30.34000  ? 485  LEU   A CD2 1 
ATOM   299  N  N   . ASN   A 1 57  ? -55.13400 23.71200  22.29300  1.000 22.97000  ? 486  ASN   A N   1 
ATOM   300  C  CA  . ASN   A 1 57  ? -55.08400 25.16600  22.16000  1.000 34.25000  ? 486  ASN   A CA  1 
ATOM   301  C  C   . ASN   A 1 57  ? -56.48000 25.72300  21.80900  1.000 46.44000  ? 486  ASN   A C   1 
ATOM   302  O  O   . ASN   A 1 57  ? -56.59500 26.61100  20.96300  1.000 38.39000  ? 486  ASN   A O   1 
ATOM   303  C  CB  . ASN   A 1 57  ? -54.03800 25.35900  21.03700  1.000 39.78000  ? 486  ASN   A CB  1 
ATOM   304  C  CG  . ASN   A 1 57  ? -53.49100 26.79500  20.79900  1.000 74.23000  ? 486  ASN   A CG  1 
ATOM   305  O  OD1 . ASN   A 1 57  ? -52.67800 27.00500  19.86500  1.000 61.02000  ? 486  ASN   A OD1 1 
ATOM   306  N  ND2 . ASN   A 1 57  ? -53.88000 27.74200  21.60600  1.000 69.67000  ? 486  ASN   A ND2 1 
ATOM   307  N  N   . VAL   A 1 58  ? -57.57800 25.20100  22.39500  1.000 43.57000  ? 487  VAL   A N   1 
ATOM   308  C  CA  . VAL   A 1 58  ? -58.91300 25.55300  21.89900  1.000 45.49000  ? 487  VAL   A CA  1 
ATOM   309  C  C   . VAL   A 1 58  ? -59.82000 26.05000  23.01000  1.000 53.01000  ? 487  VAL   A C   1 
ATOM   310  O  O   . VAL   A 1 58  ? -59.65900 25.70300  24.18800  1.000 55.57000  ? 487  VAL   A O   1 
ATOM   311  C  CB  . VAL   A 1 58  ? -59.63200 24.39500  21.17000  1.000 40.13000  ? 487  VAL   A CB  1 
ATOM   312  C  CG1 . VAL   A 1 58  ? -58.88500 24.01400  19.91100  1.000 40.16000  ? 487  VAL   A CG1 1 
ATOM   313  C  CG2 . VAL   A 1 58  ? -59.92000 23.22000  22.10100  1.000 42.02000  ? 487  VAL   A CG2 1 
ATOM   314  N  N   . THR   A 1 59  ? -60.79600 26.87000  22.59500  0.866 64.76000  ? 488  THR   A N   1 
ATOM   315  C  CA  . THR   A 1 59  ? -61.85900 27.39700  23.44400  0.866 70.11000  ? 488  THR   A CA  1 
ATOM   316  C  C   . THR   A 1 59  ? -62.60900 26.24900  24.11500  0.866 57.57000  ? 488  THR   A C   1 
ATOM   317  O  O   . THR   A 1 59  ? -62.67800 25.12300  23.59200  0.866 57.91000  ? 488  THR   A O   1 
ATOM   318  C  CB  . THR   A 1 59  ? -62.84700 28.26700  22.62500  0.866 76.27000  ? 488  THR   A CB  1 
ATOM   319  O  OG1 . THR   A 1 59  ? -63.40700 27.53300  21.50800  0.866 57.99000  ? 488  THR   A OG1 1 
ATOM   320  C  CG2 . THR   A 1 59  ? -62.14500 29.52600  22.07600  0.866 53.93000  ? 488  THR   A CG2 1 
ATOM   321  N  N   . ALA   A 1 60  ? -63.14900 26.53200  25.29600  1.000 62.32000  ? 489  ALA   A N   1 
ATOM   322  C  CA  . ALA   A 1 60  ? -63.89700 25.51100  26.00700  1.000 50.74000  ? 489  ALA   A CA  1 
ATOM   323  C  C   . ALA   A 1 60  ? -64.98700 24.97000  25.08200  1.000 63.57000  ? 489  ALA   A C   1 
ATOM   324  O  O   . ALA   A 1 60  ? -65.66100 25.75100  24.38500  1.000 50.71000  ? 489  ALA   A O   1 
ATOM   325  C  CB  . ALA   A 1 60  ? -64.49300 26.06200  27.29900  1.000 52.45000  ? 489  ALA   A CB  1 
ATOM   326  N  N   . PRO   A 1 61  ? -65.13200 23.66100  24.97400  1.000 56.02000  ? 490  PRO   A N   1 
ATOM   327  C  CA  . PRO   A 1 61  ? -66.04100 23.10700  23.96800  1.000 41.22000  ? 490  PRO   A CA  1 
ATOM   328  C  C   . PRO   A 1 61  ? -67.48300 23.25500  24.43000  1.000 43.57000  ? 490  PRO   A C   1 
ATOM   329  O  O   . PRO   A 1 61  ? -67.77700 23.26900  25.62500  1.000 48.03000  ? 490  PRO   A O   1 
ATOM   330  C  CB  . PRO   A 1 61  ? -65.67000 21.62200  23.90900  1.000 43.69000  ? 490  PRO   A CB  1 
ATOM   331  C  CG  . PRO   A 1 61  ? -64.68200 21.38300  25.02800  1.000 52.08000  ? 490  PRO   A CG  1 
ATOM   332  C  CD  . PRO   A 1 61  ? -64.33000 22.65400  25.69100  1.000 46.24000  ? 490  PRO   A CD  1 
ATOM   333  N  N   . THR   A 1 62  ? -68.39100 23.30600  23.46500  1.000 35.44000  ? 491  THR   A N   1 
ATOM   334  C  CA  . THR   A 1 62  ? -69.80000 23.09700  23.77500  1.000 45.23000  ? 491  THR   A CA  1 
ATOM   335  C  C   . THR   A 1 62  ? -70.08000 21.62700  24.08000  1.000 49.02000  ? 491  THR   A C   1 
ATOM   336  O  O   . THR   A 1 62  ? -69.24900 20.76100  23.81100  1.000 41.52000  ? 491  THR   A O   1 
ATOM   337  C  CB  . THR   A 1 62  ? -70.66500 23.54900  22.60900  1.000 36.20000  ? 491  THR   A CB  1 
ATOM   338  O  OG1 . THR   A 1 62  ? -70.49300 22.62600  21.53300  1.000 39.42000  ? 491  THR   A OG1 1 
ATOM   339  C  CG2 . THR   A 1 62  ? -70.37200 24.98000  22.19300  1.000 42.20000  ? 491  THR   A CG2 1 
ATOM   340  N  N   . PRO   A 1 63  ? -71.25200 21.31100  24.64300  1.000 42.47000  ? 492  PRO   A N   1 
ATOM   341  C  CA  . PRO   A 1 63  ? -71.63200 19.89300  24.78100  1.000 43.04000  ? 492  PRO   A CA  1 
ATOM   342  C  C   . PRO   A 1 63  ? -71.52900 19.10900  23.48100  1.000 42.33000  ? 492  PRO   A C   1 
ATOM   343  O  O   . PRO   A 1 63  ? -71.01800 17.98100  23.46600  1.000 40.84000  ? 492  PRO   A O   1 
ATOM   344  C  CB  . PRO   A 1 63  ? -73.07100 19.98600  25.29100  1.000 47.38000  ? 492  PRO   A CB  1 
ATOM   345  C  CG  . PRO   A 1 63  ? -73.00800 21.20400  26.18600  1.000 35.80000  ? 492  PRO   A CG  1 
ATOM   346  C  CD  . PRO   A 1 63  ? -72.16600 22.19300  25.40500  1.000 43.88000  ? 492  PRO   A CD  1 
ATOM   347  N  N   . GLN   A 1 64  ? -71.98400 19.69600  22.37900  1.000 35.54000  ? 493  GLN   A N   1 
ATOM   348  C  CA  . GLN   A 1 64  ? -71.87900 19.03400  21.08600  1.000 52.18000  ? 493  GLN   A CA  1 
ATOM   349  C  C   . GLN   A 1 64  ? -70.42200 18.84400  20.68600  1.000 47.10000  ? 493  GLN   A C   1 
ATOM   350  O  O   . GLN   A 1 64  ? -70.05300 17.80800  20.12200  1.000 34.38000  ? 493  GLN   A O   1 
ATOM   351  C  CB  . GLN   A 1 64  ? -72.64800 19.85300  20.04700  1.000 57.52000  ? 493  GLN   A CB  1 
ATOM   352  C  CG  . GLN   A 1 64  ? -74.16200 19.82100  20.27500  1.000 83.21000  ? 493  GLN   A CG  1 
ATOM   353  C  CD  . GLN   A 1 64  ? -74.92700 20.78800  19.38300  1.000 100.69000 ? 493  GLN   A CD  1 
ATOM   354  O  OE1 . GLN   A 1 64  ? -74.37700 21.80100  18.94000  1.000 91.72000  ? 493  GLN   A OE1 1 
ATOM   355  N  NE2 . GLN   A 1 64  ? -76.20500 20.49900  19.14300  1.000 106.38000 ? 493  GLN   A NE2 1 
ATOM   356  N  N   . GLN   A 1 65  ? -69.57800 19.82900  20.97200  1.000 33.78000  ? 494  GLN   A N   1 
ATOM   357  C  CA  . GLN   A 1 65  ? -68.18000 19.69900  20.60400  1.000 31.83000  ? 494  GLN   A CA  1 
ATOM   358  C  C   . GLN   A 1 65  ? -67.48300 18.68300  21.47900  1.000 31.25000  ? 494  GLN   A C   1 
ATOM   359  O  O   . GLN   A 1 65  ? -66.57900 17.97500  21.00700  1.000 28.60000  ? 494  GLN   A O   1 
ATOM   360  C  CB  . GLN   A 1 65  ? -67.48900 21.04500  20.71900  1.000 31.52000  ? 494  GLN   A CB  1 
ATOM   361  C  CG  . GLN   A 1 65  ? -67.82100 21.90000  19.50400  1.000 30.78000  ? 494  GLN   A CG  1 
ATOM   362  C  CD  . GLN   A 1 65  ? -67.14700 23.25300  19.59000  1.000 45.67000  ? 494  GLN   A CD  1 
ATOM   363  O  OE1 . GLN   A 1 65  ? -66.95700 23.77300  20.68400  1.000 38.92000  ? 494  GLN   A OE1 1 
ATOM   364  N  NE2 . GLN   A 1 65  ? -66.77200 23.82700  18.42800  1.000 41.02000  ? 494  GLN   A NE2 1 
ATOM   365  N  N   . LEU   A 1 66  ? -67.86500 18.63900  22.75900  1.000 28.51000  ? 495  LEU   A N   1 
ATOM   366  C  CA  . LEU   A 1 66  ? -67.27300 17.66900  23.67600  1.000 36.54000  ? 495  LEU   A CA  1 
ATOM   367  C  C   . LEU   A 1 66  ? -67.56100 16.26700  23.19300  1.000 39.30000  ? 495  LEU   A C   1 
ATOM   368  O  O   . LEU   A 1 66  ? -66.67700 15.40700  23.20400  1.000 26.87000  ? 495  LEU   A O   1 
ATOM   369  C  CB  . LEU   A 1 66  ? -67.81100 17.86100  25.09400  1.000 36.11000  ? 495  LEU   A CB  1 
ATOM   370  C  CG  . LEU   A 1 66  ? -67.22900 16.98300  26.19100  1.000 36.66000  ? 495  LEU   A CG  1 
ATOM   371  C  CD1 . LEU   A 1 66  ? -65.69600 17.08000  26.21100  1.000 38.77000  ? 495  LEU   A CD1 1 
ATOM   372  C  CD2 . LEU   A 1 66  ? -67.87900 17.19600  27.57600  1.000 39.82000  ? 495  LEU   A CD2 1 
ATOM   373  N  N   . GLN   A 1 67  ? -68.79400 16.02200  22.75400  1.000 29.37000  ? 496  GLN   A N   1 
ATOM   374  C  CA  . GLN   A 1 67  ? -69.13600 14.71700  22.18200  1.000 34.54000  ? 496  GLN   A CA  1 
ATOM   375  C  C   . GLN   A 1 67  ? -68.34300 14.44900  20.90700  1.000 42.74000  ? 496  GLN   A C   1 
ATOM   376  O  O   . GLN   A 1 67  ? -67.90500 13.31300  20.66600  1.000 29.95000  ? 496  GLN   A O   1 
ATOM   377  C  CB  . GLN   A 1 67  ? -70.64200 14.63300  21.89400  1.000 33.81000  ? 496  GLN   A CB  1 
ATOM   378  C  CG  . GLN   A 1 67  ? -71.18700 13.22900  21.71700  1.000 37.23000  ? 496  GLN   A CG  1 
ATOM   379  C  CD  . GLN   A 1 67  ? -70.60100 12.25300  22.71900  1.000 42.92000  ? 496  GLN   A CD  1 
ATOM   380  O  OE1 . GLN   A 1 67  ? -70.84000 12.36800  23.92600  1.000 43.30000  ? 496  GLN   A OE1 1 
ATOM   381  N  NE2 . GLN   A 1 67  ? -69.85700 11.25900  22.22600  1.000 39.26000  ? 496  GLN   A NE2 1 
ATOM   382  N  N   . ALA   A 1 68  ? -68.19800 15.46500  20.04900  1.000 30.76000  ? 497  ALA   A N   1 
ATOM   383  C  CA  . ALA   A 1 68  ? -67.39200 15.29400  18.84900  1.000 26.20000  ? 497  ALA   A CA  1 
ATOM   384  C  C   . ALA   A 1 68  ? -65.95600 14.90100  19.21200  1.000 29.06000  ? 497  ALA   A C   1 
ATOM   385  O  O   . ALA   A 1 68  ? -65.35600 14.03500  18.55700  1.000 28.78000  ? 497  ALA   A O   1 
ATOM   386  C  CB  . ALA   A 1 68  ? -67.38300 16.59300  18.02700  1.000 33.76000  ? 497  ALA   A CB  1 
ATOM   387  N  N   . PHE   A 1 69  ? -65.39000 15.55300  20.23400  1.000 28.26000  ? 498  PHE   A N   1 
ATOM   388  C  CA  . PHE   A 1 69  ? -64.03800 15.23700  20.71600  1.000 25.17000  ? 498  PHE   A CA  1 
ATOM   389  C  C   . PHE   A 1 69  ? -63.96400 13.78700  21.18600  1.000 23.36000  ? 498  PHE   A C   1 
ATOM   390  O  O   . PHE   A 1 69  ? -63.05200 13.04300  20.79700  1.000 23.03000  ? 498  PHE   A O   1 
ATOM   391  C  CB  . PHE   A 1 69  ? -63.64000 16.21600  21.83400  1.000 22.58000  ? 498  PHE   A CB  1 
ATOM   392  C  CG  . PHE   A 1 69  ? -62.34700 15.89400  22.54100  1.000 23.80000  ? 498  PHE   A CG  1 
ATOM   393  C  CD1 . PHE   A 1 69  ? -61.11700 16.25300  22.00100  1.000 23.27000  ? 498  PHE   A CD1 1 
ATOM   394  C  CD2 . PHE   A 1 69  ? -62.35600 15.20600  23.75000  1.000 26.80000  ? 498  PHE   A CD2 1 
ATOM   395  C  CE1 . PHE   A 1 69  ? -59.89100 15.98100  22.69100  1.000 25.28000  ? 498  PHE   A CE1 1 
ATOM   396  C  CE2 . PHE   A 1 69  ? -61.16000 14.88500  24.40200  1.000 25.85000  ? 498  PHE   A CE2 1 
ATOM   397  C  CZ  . PHE   A 1 69  ? -59.92900 15.27800  23.89000  1.000 27.88000  ? 498  PHE   A CZ  1 
ATOM   398  N  N   . LYS   A 1 70  ? -64.92900 13.36100  22.00800  1.000 23.72000  ? 499  LYS   A N   1 
ATOM   399  C  CA  . LYS   A 1 70  ? -64.93900 11.95700  22.45000  1.000 23.55000  ? 499  LYS   A CA  1 
ATOM   400  C  C   . LYS   A 1 70  ? -65.07800 11.00000  21.26500  1.000 28.76000  ? 499  LYS   A C   1 
ATOM   401  O  O   . LYS   A 1 70  ? -64.48500 9.91800   21.26100  1.000 22.78000  ? 499  LYS   A O   1 
ATOM   402  C  CB  . LYS   A 1 70  ? -66.07600 11.73900  23.47200  1.000 26.43000  ? 499  LYS   A CB  1 
ATOM   403  C  CG  . LYS   A 1 70  ? -65.82400 12.48200  24.82800  1.000 21.48000  ? 499  LYS   A CG  1 
ATOM   404  C  CD  . LYS   A 1 70  ? -66.98800 12.20500  25.79700  1.000 30.77000  ? 499  LYS   A CD  1 
ATOM   405  C  CE  . LYS   A 1 70  ? -66.74800 12.92800  27.10200  1.000 35.28000  ? 499  LYS   A CE  1 
ATOM   406  N  NZ  . LYS   A 1 70  ? -67.94800 12.82400  28.03100  1.000 41.25000  ? 499  LYS   A NZ  1 
ATOM   407  N  N   . ASN   A 1 71  ? -65.84400 11.37800  20.23300  1.000 25.05000  ? 500  ASN   A N   1 
ATOM   408  C  CA  . ASN   A 1 71  ? -65.95900 10.51700  19.05400  1.000 28.14000  ? 500  ASN   A CA  1 
ATOM   409  C  C   . ASN   A 1 71  ? -64.63400 10.42800  18.30700  1.000 25.92000  ? 500  ASN   A C   1 
ATOM   410  O  O   . ASN   A 1 71  ? -64.28200 9.37200   17.76300  1.000 32.70000  ? 500  ASN   A O   1 
ATOM   411  C  CB  . ASN   A 1 71  ? -67.03900 11.04900  18.10000  1.000 34.06000  ? 500  ASN   A CB  1 
ATOM   412  C  CG  . ASN   A 1 71  ? -68.45000 10.92400  18.67900  1.000 29.67000  ? 500  ASN   A CG  1 
ATOM   413  O  OD1 . ASN   A 1 71  ? -68.67500 10.25600  19.68800  1.000 37.34000  ? 500  ASN   A OD1 1 
ATOM   414  N  ND2 . ASN   A 1 71  ? -69.41300 11.60500  18.03600  1.000 38.85000  ? 500  ASN   A ND2 1 
ATOM   415  N  N   . GLU   A 1 72  ? -63.86900 11.50800  18.28500  1.000 25.20000  ? 501  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 72  ? -62.58700 11.41400  17.62000  1.000 27.80000  ? 501  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 72  ? -61.62700 10.57800  18.44300  1.000 19.36000  ? 501  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 72  ? -60.70900 9.97300   17.89000  1.000 23.02000  ? 501  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 72  ? -62.05000 12.80900  17.37700  1.000 37.21000  ? 501  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 72  ? -63.05200 13.52700  16.51500  1.000 54.68000  ? 501  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 72  ? -62.43500 14.19000  15.34000  1.000 43.87000  ? 501  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 72  ? -61.74300 15.18200  15.59500  1.000 35.73000  ? 501  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 72  ? -62.59100 13.71900  14.18500  1.000 54.52000  ? 501  GLU   A OE2 1 
ATOM   424  N  N   . VAL   A 1 73  ? -61.79200 10.57600  19.75800  1.000 18.00000  ? 502  VAL   A N   1 
ATOM   425  C  CA  . VAL   A 1 73  ? -60.96600 9.69600   20.58500  1.000 20.15000  ? 502  VAL   A CA  1 
ATOM   426  C  C   . VAL   A 1 73  ? -61.28100 8.24600   20.22000  1.000 21.09000  ? 502  VAL   A C   1 
ATOM   427  O  O   . VAL   A 1 73  ? -60.40400 7.37000   20.29200  1.000 19.80000  ? 502  VAL   A O   1 
ATOM   428  C  CB  . VAL   A 1 73  ? -61.22600 9.97000   22.06500  1.000 22.33000  ? 502  VAL   A CB  1 
ATOM   429  C  CG1 . VAL   A 1 73  ? -60.60100 8.86300   22.92300  1.000 21.58000  ? 502  VAL   A CG1 1 
ATOM   430  C  CG2 . VAL   A 1 73  ? -60.65200 11.35600  22.45600  1.000 22.45000  ? 502  VAL   A CG2 1 
ATOM   431  N  N   . GLY   A 1 74  ? -62.52700 7.98200   19.78300  1.000 20.70000  ? 503  GLY   A N   1 
ATOM   432  C  CA  . GLY   A 1 74  ? -62.86000 6.67400   19.20300  1.000 22.34000  ? 503  GLY   A CA  1 
ATOM   433  C  C   . GLY   A 1 74  ? -61.91600 6.22300   18.09600  1.000 24.52000  ? 503  GLY   A C   1 
ATOM   434  O  O   . GLY   A 1 74  ? -61.54700 5.04500   18.02800  1.000 24.74000  ? 503  GLY   A O   1 
ATOM   435  N  N   . VAL   A 1 75  ? -61.51000 7.14400   17.20000  1.000 22.84000  ? 504  VAL   A N   1 
ATOM   436  C  CA  . VAL   A 1 75  ? -60.49700 6.82700   16.17200  1.000 26.71000  ? 504  VAL   A CA  1 
ATOM   437  C  C   . VAL   A 1 75  ? -59.16000 6.43500   16.76800  1.000 25.64000  ? 504  VAL   A C   1 
ATOM   438  O  O   . VAL   A 1 75  ? -58.54500 5.43800   16.35600  1.000 23.61000  ? 504  VAL   A O   1 
ATOM   439  C  CB  . VAL   A 1 75  ? -60.32900 8.01300   15.20100  1.000 31.34000  ? 504  VAL   A CB  1 
ATOM   440  C  CG1 . VAL   A 1 75  ? -59.33900 7.65700   14.09800  1.000 32.27000  ? 504  VAL   A CG1 1 
ATOM   441  C  CG2 . VAL   A 1 75  ? -61.63800 8.26400   14.54600  1.000 28.65000  ? 504  VAL   A CG2 1 
ATOM   442  N  N   . LEU   A 1 76  ? -58.63000 7.26300   17.67500  1.000 22.02000  ? 505  LEU   A N   1 
ATOM   443  C  CA  . LEU   A 1 76  ? -57.36600 6.96300   18.35700  1.000 20.59000  ? 505  LEU   A CA  1 
ATOM   444  C  C   . LEU   A 1 76  ? -57.41500 5.56300   18.93000  1.000 22.12000  ? 505  LEU   A C   1 
ATOM   445  O  O   . LEU   A 1 76  ? -56.43300 4.82800   18.86800  1.000 25.60000  ? 505  LEU   A O   1 
ATOM   446  C  CB  . LEU   A 1 76  ? -57.10600 7.96200   19.54000  1.000 19.25000  ? 505  LEU   A CB  1 
ATOM   447  C  CG  . LEU   A 1 76  ? -57.05600 9.38900   18.97600  1.000 24.36000  ? 505  LEU   A CG  1 
ATOM   448  C  CD1 . LEU   A 1 76  ? -56.73100 10.35700  20.07800  1.000 19.70000  ? 505  LEU   A CD1 1 
ATOM   449  C  CD2 . LEU   A 1 76  ? -55.97100 9.40600   17.89700  1.000 26.37000  ? 505  LEU   A CD2 1 
ATOM   450  N  N   . ARG   A 1 77  ? -58.53200 5.21600   19.56700  1.000 17.74000  ? 506  ARG   A N   1 
ATOM   451  C  CA  . ARG   A 1 77  ? -58.65000 3.94200   20.28100  1.000 15.22000  ? 506  ARG   A CA  1 
ATOM   452  C  C   . ARG   A 1 77  ? -58.49900 2.73900   19.34100  1.000 18.18000  ? 506  ARG   A C   1 
ATOM   453  O  O   . ARG   A 1 77  ? -58.31600 1.61500   19.83800  1.000 19.76000  ? 506  ARG   A O   1 
ATOM   454  C  CB  . ARG   A 1 77  ? -59.99300 3.89600   20.98000  1.000 17.05000  ? 506  ARG   A CB  1 
ATOM   455  C  CG  . ARG   A 1 77  ? -59.97600 4.67800   22.33100  1.000 24.42000  ? 506  ARG   A CG  1 
ATOM   456  C  CD  . ARG   A 1 77  ? -61.40800 4.99800   22.81900  1.000 26.13000  ? 506  ARG   A CD  1 
ATOM   457  N  NE  . ARG   A 1 77  ? -62.24300 3.80300   22.94400  1.000 24.57000  ? 506  ARG   A NE  1 
ATOM   458  C  CZ  . ARG   A 1 77  ? -63.56600 3.84600   22.98200  1.000 35.23000  ? 506  ARG   A CZ  1 
ATOM   459  N  NH1 . ARG   A 1 77  ? -64.21800 4.99900   22.95100  1.000 44.45000  ? 506  ARG   A NH1 1 
ATOM   460  N  NH2 . ARG   A 1 77  ? -64.25400 2.71100   23.04900  1.000 43.46000  ? 506  ARG   A NH2 1 
ATOM   461  N  N   . LYS   A 1 78  ? -58.66800 2.93600   18.03800  1.000 18.82000  ? 507  LYS   A N   1 
ATOM   462  C  CA  . LYS   A 1 78  ? -58.52900 1.84400   17.05700  1.000 19.24000  ? 507  LYS   A CA  1 
ATOM   463  C  C   . LYS   A 1 78  ? -57.09500 1.42900   16.85100  1.000 18.75000  ? 507  LYS   A C   1 
ATOM   464  O  O   . LYS   A 1 78  ? -56.86900 0.46200   16.09300  1.000 18.03000  ? 507  LYS   A O   1 
ATOM   465  C  CB  . LYS   A 1 78  ? -59.15900 2.27800   15.72500  1.000 18.90000  ? 507  LYS   A CB  1 
ATOM   466  C  CG  . LYS   A 1 78  ? -60.69500 2.34800   15.80500  1.000 23.86000  ? 507  LYS   A CG  1 
ATOM   467  C  CD  . LYS   A 1 78  ? -61.26400 2.80300   14.40400  1.000 32.45000  ? 507  LYS   A CD  1 
ATOM   468  C  CE  . LYS   A 1 78  ? -60.52200 2.25700   13.19400  1.000 48.47000  ? 507  LYS   A CE  1 
ATOM   469  N  NZ  . LYS   A 1 78  ? -61.44900 1.69900   12.12900  1.000 57.66000  ? 507  LYS   A NZ  1 
ATOM   470  N  N   . THR   A 1 79  ? -56.10800 2.11800   17.46200  1.000 16.87000  ? 508  THR   A N   1 
ATOM   471  C  CA  . THR   A 1 79  ? -54.69700 1.92000   17.10100  1.000 11.97000  ? 508  THR   A CA  1 
ATOM   472  C  C   . THR   A 1 79  ? -53.96500 1.21800   18.21900  1.000 16.34000  ? 508  THR   A C   1 
ATOM   473  O  O   . THR   A 1 79  ? -53.88100 1.71900   19.34800  1.000 15.61000  ? 508  THR   A O   1 
ATOM   474  C  CB  . THR   A 1 79  ? -53.96200 3.21200   16.70100  1.000 16.19000  ? 508  THR   A CB  1 
ATOM   475  O  OG1 . THR   A 1 79  ? -54.02000 4.16100   17.77400  1.000 15.78000  ? 508  THR   A OG1 1 
ATOM   476  C  CG2 . THR   A 1 79  ? -54.71200 3.80200   15.48600  1.000 18.61000  ? 508  THR   A CG2 1 
ATOM   477  N  N   . ARG   A 1 80  ? -53.43800 0.03800   17.88800  1.000 13.97000  ? 509  ARG   A N   1 
ATOM   478  C  CA  . ARG   A 1 80  ? -52.63400 -0.76700  18.80900  1.000 14.32000  ? 509  ARG   A CA  1 
ATOM   479  C  C   . ARG   A 1 80  ? -51.50100 -1.37700  17.98300  1.000 13.71000  ? 509  ARG   A C   1 
ATOM   480  O  O   . ARG   A 1 80  ? -51.63600 -2.50900  17.48100  1.000 15.25000  ? 509  ARG   A O   1 
ATOM   481  C  CB  . ARG   A 1 80  ? -53.49200 -1.87100  19.45900  1.000 13.26000  ? 509  ARG   A CB  1 
ATOM   482  C  CG  . ARG   A 1 80  ? -54.37900 -1.31300  20.62100  1.000 14.08000  ? 509  ARG   A CG  1 
ATOM   483  C  CD  . ARG   A 1 80  ? -55.20900 -2.51000  21.16300  1.000 15.92000  ? 509  ARG   A CD  1 
ATOM   484  N  NE  . ARG   A 1 80  ? -55.87100 -2.15300  22.40700  1.000 15.27000  ? 509  ARG   A NE  1 
ATOM   485  C  CZ  . ARG   A 1 80  ? -55.26100 -2.20700  23.60200  1.000 14.58000  ? 509  ARG   A CZ  1 
ATOM   486  N  NH1 . ARG   A 1 80  ? -53.99400 -2.66300  23.73600  1.000 14.84000  ? 509  ARG   A NH1 1 
ATOM   487  N  NH2 . ARG   A 1 80  ? -55.94800 -1.84200  24.67800  1.000 18.52000  ? 509  ARG   A NH2 1 
ATOM   488  N  N   . HIS   A 1 81  ? -50.39600 -0.65600  17.82700  1.000 13.03000  ? 510  HIS   A N   1 
ATOM   489  C  CA  . HIS   A 1 81  ? -49.30400 -1.12900  16.96900  1.000 14.92000  ? 510  HIS   A CA  1 
ATOM   490  C  C   . HIS   A 1 81  ? -48.02900 -0.44700  17.42700  1.000 15.43000  ? 510  HIS   A C   1 
ATOM   491  O  O   . HIS   A 1 81  ? -48.04100 0.75000   17.79100  1.000 14.90000  ? 510  HIS   A O   1 
ATOM   492  C  CB  . HIS   A 1 81  ? -49.57800 -0.78900  15.48200  1.000 13.24000  ? 510  HIS   A CB  1 
ATOM   493  C  CG  . HIS   A 1 81  ? -48.60300 -1.40900  14.53600  1.000 11.53000  ? 510  HIS   A CG  1 
ATOM   494  N  ND1 . HIS   A 1 81  ? -47.36100 -0.88000  14.29000  1.000 13.30000  ? 510  HIS   A ND1 1 
ATOM   495  C  CD2 . HIS   A 1 81  ? -48.70000 -2.53100  13.77100  1.000 14.67000  ? 510  HIS   A CD2 1 
ATOM   496  C  CE1 . HIS   A 1 81  ? -46.71100 -1.65200  13.41600  1.000 14.58000  ? 510  HIS   A CE1 1 
ATOM   497  N  NE2 . HIS   A 1 81  ? -47.53500 -2.64200  13.05500  1.000 13.29000  ? 510  HIS   A NE2 1 
ATOM   498  N  N   A VAL   A 1 82  ? -46.90700 -1.19000  17.43100  0.779 12.65000  ? 511  VAL   A N   1 
ATOM   499  N  N   B VAL   A 1 82  ? -46.92400 -1.18300  17.36400  0.221 12.74000  ? 511  VAL   A N   1 
ATOM   500  C  CA  A VAL   A 1 82  ? -45.64500 -0.63900  17.95300  0.779 12.73000  ? 511  VAL   A CA  1 
ATOM   501  C  CA  B VAL   A 1 82  ? -45.70100 -0.64800  17.93800  0.221 12.89000  ? 511  VAL   A CA  1 
ATOM   502  C  C   A VAL   A 1 82  ? -45.08900 0.53200   17.13000  0.779 13.81000  ? 511  VAL   A C   1 
ATOM   503  C  C   B VAL   A 1 82  ? -45.26700 0.62800   17.21000  0.221 13.85000  ? 511  VAL   A C   1 
ATOM   504  O  O   A VAL   A 1 82  ? -44.18400 1.23200   17.60600  0.779 14.84000  ? 511  VAL   A O   1 
ATOM   505  O  O   B VAL   A 1 82  ? -44.70700 1.53100   17.83900  0.221 12.97000  ? 511  VAL   A O   1 
ATOM   506  C  CB  A VAL   A 1 82  ? -44.53000 -1.70300  18.09800  0.779 17.94000  ? 511  VAL   A CB  1 
ATOM   507  C  CB  B VAL   A 1 82  ? -44.60700 -1.73100  17.95200  0.221 17.74000  ? 511  VAL   A CB  1 
ATOM   508  C  CG1 A VAL   A 1 82  ? -44.98100 -2.79800  19.10800  0.779 18.73000  ? 511  VAL   A CG1 1 
ATOM   509  C  CG1 B VAL   A 1 82  ? -43.34100 -1.16300  18.48800  0.221 11.69000  ? 511  VAL   A CG1 1 
ATOM   510  C  CG2 A VAL   A 1 82  ? -44.07600 -2.27600  16.72400  0.779 15.92000  ? 511  VAL   A CG2 1 
ATOM   511  C  CG2 B VAL   A 1 82  ? -45.04500 -2.91000  18.81800  0.221 17.67000  ? 511  VAL   A CG2 1 
ATOM   512  N  N   . ASN   A 1 83  ? -45.56600 0.76700   15.90300  1.000 14.65000  ? 512  ASN   A N   1 
ATOM   513  C  CA  . ASN   A 1 83  ? -45.10700 1.94600   15.16400  1.000 13.37000  ? 512  ASN   A CA  1 
ATOM   514  C  C   . ASN   A 1 83  ? -46.12600 3.08700   15.19600  1.000 13.43000  ? 512  ASN   A C   1 
ATOM   515  O  O   . ASN   A 1 83  ? -45.90200 4.11700   14.52600  1.000 14.11000  ? 512  ASN   A O   1 
ATOM   516  C  CB  . ASN   A 1 83  ? -44.77000 1.58800   13.68700  1.000 13.33000  ? 512  ASN   A CB  1 
ATOM   517  C  CG  . ASN   A 1 83  ? -43.58300 0.69400   13.60500  1.000 16.32000  ? 512  ASN   A CG  1 
ATOM   518  O  OD1 . ASN   A 1 83  ? -43.65700 -0.33600  12.93600  1.000 16.07000  ? 512  ASN   A OD1 1 
ATOM   519  N  ND2 . ASN   A 1 83  ? -42.45500 1.06600   14.24400  1.000 14.56000  ? 512  ASN   A ND2 1 
ATOM   520  N  N   . ILE   A 1 84  ? -47.12500 2.98000   16.07000  1.000 13.36000  ? 513  ILE   A N   1 
ATOM   521  C  CA  . ILE   A 1 84  ? -48.09900 4.05600   16.31200  1.000 14.10000  ? 513  ILE   A CA  1 
ATOM   522  C  C   . ILE   A 1 84  ? -47.92400 4.52700   17.74400  1.000 15.13000  ? 513  ILE   A C   1 
ATOM   523  O  O   . ILE   A 1 84  ? -47.97300 3.73100   18.67500  1.000 14.01000  ? 513  ILE   A O   1 
ATOM   524  C  CB  . ILE   A 1 84  ? -49.54100 3.58000   16.06300  1.000 13.33000  ? 513  ILE   A CB  1 
ATOM   525  C  CG1 . ILE   A 1 84  ? -49.71400 3.04400   14.61500  1.000 16.26000  ? 513  ILE   A CG1 1 
ATOM   526  C  CG2 . ILE   A 1 84  ? -50.54300 4.77300   16.34800  1.000 13.96000  ? 513  ILE   A CG2 1 
ATOM   527  C  CD1 . ILE   A 1 84  ? -49.23500 4.10800   13.52800  1.000 13.68000  ? 513  ILE   A CD1 1 
ATOM   528  N  N   . LEU   A 1 85  ? -47.70000 5.83000   17.93100  1.000 13.90000  ? 514  LEU   A N   1 
ATOM   529  C  CA  . LEU   A 1 85  ? -47.59800 6.40500   19.27800  1.000 12.37000  ? 514  LEU   A CA  1 
ATOM   530  C  C   . LEU   A 1 85  ? -48.77800 5.95800   20.11700  1.000 11.54000  ? 514  LEU   A C   1 
ATOM   531  O  O   . LEU   A 1 85  ? -49.92300 6.02600   19.68500  1.000 13.72000  ? 514  LEU   A O   1 
ATOM   532  C  CB  . LEU   A 1 85  ? -47.59900 7.94900   19.13000  1.000 12.58000  ? 514  LEU   A CB  1 
ATOM   533  C  CG  . LEU   A 1 85  ? -47.49400 8.70500   20.44200  1.000 11.69000  ? 514  LEU   A CG  1 
ATOM   534  C  CD1 . LEU   A 1 85  ? -46.13400 8.49800   21.05800  1.000 12.63000  ? 514  LEU   A CD1 1 
ATOM   535  C  CD2 . LEU   A 1 85  ? -47.71100 10.23200  20.01600  1.000 13.15000  ? 514  LEU   A CD2 1 
ATOM   536  N  N   . LEU   A 1 86  ? -48.49400 5.48100   21.35500  1.000 11.97000  ? 515  LEU   A N   1 
ATOM   537  C  CA  . LEU   A 1 86  ? -49.51600 4.80100   22.15500  1.000 11.55000  ? 515  LEU   A CA  1 
ATOM   538  C  C   . LEU   A 1 86  ? -50.46800 5.79900   22.82700  1.000 10.85000  ? 515  LEU   A C   1 
ATOM   539  O  O   . LEU   A 1 86  ? -50.05900 6.49000   23.75400  1.000 14.98000  ? 515  LEU   A O   1 
ATOM   540  C  CB  . LEU   A 1 86  ? -48.83400 3.91800   23.21100  1.000 12.94000  ? 515  LEU   A CB  1 
ATOM   541  C  CG  . LEU   A 1 86  ? -49.79600 3.10400   24.09100  1.000 13.89000  ? 515  LEU   A CG  1 
ATOM   542  C  CD1 . LEU   A 1 86  ? -50.47000 1.97400   23.30000  1.000 15.92000  ? 515  LEU   A CD1 1 
ATOM   543  C  CD2 . LEU   A 1 86  ? -48.93900 2.58300   25.26800  1.000 16.44000  ? 515  LEU   A CD2 1 
ATOM   544  N  N   . PHE   A 1 87  ? -51.71100 5.83400   22.36900  1.000 11.75000  ? 516  PHE   A N   1 
ATOM   545  C  CA  . PHE   A 1 87  ? -52.76800 6.52600   23.09600  1.000 10.84000  ? 516  PHE   A CA  1 
ATOM   546  C  C   . PHE   A 1 87  ? -52.92300 5.88000   24.47000  1.000 14.90000  ? 516  PHE   A C   1 
ATOM   547  O  O   . PHE   A 1 87  ? -52.94200 4.65300   24.60000  1.000 13.42000  ? 516  PHE   A O   1 
ATOM   548  C  CB  . PHE   A 1 87  ? -54.10300 6.46900   22.30100  1.000 12.53000  ? 516  PHE   A CB  1 
ATOM   549  C  CG  . PHE   A 1 87  ? -55.27900 6.94600   23.10200  1.000 13.64000  ? 516  PHE   A CG  1 
ATOM   550  C  CD1 . PHE   A 1 87  ? -55.45000 8.30900   23.32500  1.000 15.07000  ? 516  PHE   A CD1 1 
ATOM   551  C  CD2 . PHE   A 1 87  ? -56.22000 6.03500   23.64200  1.000 15.19000  ? 516  PHE   A CD2 1 
ATOM   552  C  CE1 . PHE   A 1 87  ? -56.56000 8.78200   24.08800  1.000 15.33000  ? 516  PHE   A CE1 1 
ATOM   553  C  CE2 . PHE   A 1 87  ? -57.32000 6.47500   24.38400  1.000 16.91000  ? 516  PHE   A CE2 1 
ATOM   554  C  CZ  . PHE   A 1 87  ? -57.49500 7.86500   24.61400  1.000 15.59000  ? 516  PHE   A CZ  1 
ATOM   555  N  N   . MET   A 1 88  ? -52.98500 6.71500   25.52700  1.000 12.20000  ? 517  MET   A N   1 
ATOM   556  C  CA  . MET   A 1 88  ? -53.20400 6.25800   26.91000  1.000 11.18000  ? 517  MET   A CA  1 
ATOM   557  C  C   . MET   A 1 88  ? -54.45300 6.80300   27.57500  1.000 15.03000  ? 517  MET   A C   1 
ATOM   558  O  O   . MET   A 1 88  ? -54.96400 6.17400   28.50600  1.000 15.16000  ? 517  MET   A O   1 
ATOM   559  C  CB  . MET   A 1 88  ? -51.97400 6.53700   27.81400  1.000 12.13000  ? 517  MET   A CB  1 
ATOM   560  C  CG  . MET   A 1 88  ? -50.71500 5.76000   27.34000  1.000 12.01000  ? 517  MET   A CG  1 
ATOM   561  S  SD  . MET   A 1 88  ? -49.26400 6.12400   28.32200  1.000 15.53000  ? 517  MET   A SD  1 
ATOM   562  C  CE  . MET   A 1 88  ? -49.76800 5.51100   29.94500  1.000 15.14000  ? 517  MET   A CE  1 
ATOM   563  N  N   . GLY   A 1 89  ? -54.98600 7.94200   27.13500  1.000 15.20000  ? 518  GLY   A N   1 
ATOM   564  C  CA  . GLY   A 1 89  ? -56.13200 8.46000   27.85000  1.000 16.13000  ? 518  GLY   A CA  1 
ATOM   565  C  C   . GLY   A 1 89  ? -56.38700 9.87500   27.38400  1.000 17.53000  ? 518  GLY   A C   1 
ATOM   566  O  O   . GLY   A 1 89  ? -55.63700 10.40100  26.58600  1.000 13.93000  ? 518  GLY   A O   1 
ATOM   567  N  N   . TYR   A 1 90  ? -57.47200 10.47200  27.87200  1.000 14.23000  ? 519  TYR   A N   1 
ATOM   568  C  CA  . TYR   A 1 90  ? -57.69100 11.88600  27.54600  1.000 16.00000  ? 519  TYR   A CA  1 
ATOM   569  C  C   . TYR   A 1 90  ? -58.19200 12.58900  28.79600  1.000 16.27000  ? 519  TYR   A C   1 
ATOM   570  O  O   . TYR   A 1 90  ? -58.62300 11.96500  29.75100  1.000 15.51000  ? 519  TYR   A O   1 
ATOM   571  C  CB  . TYR   A 1 90  ? -58.67800 12.07400  26.39300  1.000 15.21000  ? 519  TYR   A CB  1 
ATOM   572  C  CG  . TYR   A 1 90  ? -60.07800 11.65700  26.70800  1.000 15.59000  ? 519  TYR   A CG  1 
ATOM   573  C  CD1 . TYR   A 1 90  ? -60.50100 10.30900  26.50200  1.000 18.45000  ? 519  TYR   A CD1 1 
ATOM   574  C  CD2 . TYR   A 1 90  ? -61.02200 12.58900  27.18700  1.000 18.32000  ? 519  TYR   A CD2 1 
ATOM   575  C  CE1 . TYR   A 1 90  ? -61.80700 9.93400   26.75400  1.000 22.36000  ? 519  TYR   A CE1 1 
ATOM   576  C  CE2 . TYR   A 1 90  ? -62.34000 12.18800  27.47000  1.000 22.25000  ? 519  TYR   A CE2 1 
ATOM   577  C  CZ  . TYR   A 1 90  ? -62.71900 10.85000  27.19600  1.000 25.12000  ? 519  TYR   A CZ  1 
ATOM   578  O  OH  . TYR   A 1 90  ? -64.02100 10.44600  27.45900  1.000 27.19000  ? 519  TYR   A OH  1 
ATOM   579  N  N   . SER   A 1 91  ? -58.03800 13.91700  28.81500  1.000 14.53000  ? 520  SER   A N   1 
ATOM   580  C  CA  . SER   A 1 91  ? -58.59100 14.74600  29.87900  1.000 17.26000  ? 520  SER   A CA  1 
ATOM   581  C  C   . SER   A 1 91  ? -59.60600 15.71100  29.29200  1.000 20.45000  ? 520  SER   A C   1 
ATOM   582  O  O   . SER   A 1 91  ? -59.47000 16.16400  28.14900  1.000 17.62000  ? 520  SER   A O   1 
ATOM   583  C  CB  . SER   A 1 91  ? -57.53900 15.62400  30.59000  1.000 24.31000  ? 520  SER   A CB  1 
ATOM   584  O  OG  . SER   A 1 91  ? -56.37500 14.90700  30.97800  1.000 31.59000  ? 520  SER   A OG  1 
ATOM   585  N  N   . THR   A 1 92  ? -60.59200 16.10700  30.13400  1.000 23.85000  ? 521  THR   A N   1 
ATOM   586  C  CA  . THR   A 1 92  ? -61.47700 17.21800  29.76900  1.000 26.09000  ? 521  THR   A CA  1 
ATOM   587  C  C   . THR   A 1 92  ? -61.49500 18.32500  30.81000  1.000 39.24000  ? 521  THR   A C   1 
ATOM   588  O  O   . THR   A 1 92  ? -61.50200 19.50800  30.44900  1.000 35.25000  ? 521  THR   A O   1 
ATOM   589  C  CB  . THR   A 1 92  ? -62.94900 16.76300  29.59900  1.000 27.92000  ? 521  THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 92  ? -63.47000 16.38400  30.88200  1.000 34.89000  ? 521  THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 92  ? -63.13600 15.60900  28.66600  1.000 25.40000  ? 521  THR   A CG2 1 
ATOM   592  N  N   . LYS   A 1 93  ? -61.50900 17.98400  32.10100  1.000 40.54000  ? 522  LYS   A N   1 
ATOM   593  C  CA  . LYS   A 1 93  ? -62.05700 18.95400  33.06000  1.000 66.20000  ? 522  LYS   A CA  1 
ATOM   594  C  C   . LYS   A 1 93  ? -61.02400 19.99600  33.46700  1.000 57.91000  ? 522  LYS   A C   1 
ATOM   595  O  O   . LYS   A 1 93  ? -61.39900 21.14600  33.73400  1.000 69.15000  ? 522  LYS   A O   1 
ATOM   596  C  CB  . LYS   A 1 93  ? -62.65800 18.27800  34.30300  1.000 46.64000  ? 522  LYS   A CB  1 
ATOM   597  C  CG  . LYS   A 1 93  ? -64.04300 17.62700  34.05800  1.000 46.22000  ? 522  LYS   A CG  1 
ATOM   598  C  CD  . LYS   A 1 93  ? -65.00000 17.94600  35.21500  1.000 50.26000  ? 522  LYS   A CD  1 
ATOM   599  C  CE  . LYS   A 1 93  ? -66.40200 17.29700  35.10800  1.000 42.97000  ? 522  LYS   A CE  1 
ATOM   600  N  NZ  . LYS   A 1 93  ? -66.69600 16.45300  36.32400  1.000 39.09000  ? 522  LYS   A NZ  1 
ATOM   601  N  N   . PRO   A 1 94  ? -59.74000 19.66200  33.52900  1.000 49.25000  ? 523  PRO   A N   1 
ATOM   602  C  CA  . PRO   A 1 94  ? -58.71900 20.72100  33.43200  1.000 60.21000  ? 523  PRO   A CA  1 
ATOM   603  C  C   . PRO   A 1 94  ? -58.90200 21.56000  32.16800  1.000 69.37000  ? 523  PRO   A C   1 
ATOM   604  O  O   . PRO   A 1 94  ? -59.12000 22.77200  32.20400  1.000 63.15000  ? 523  PRO   A O   1 
ATOM   605  C  CB  . PRO   A 1 94  ? -57.38900 19.95300  33.41400  1.000 50.00000  ? 523  PRO   A CB  1 
ATOM   606  C  CG  . PRO   A 1 94  ? -57.75000 18.44700  33.48200  1.000 48.23000  ? 523  PRO   A CG  1 
ATOM   607  C  CD  . PRO   A 1 94  ? -59.19000 18.36600  33.95000  1.000 36.61000  ? 523  PRO   A CD  1 
ATOM   608  N  N   . GLN   A 1 95  ? -58.83900 20.88200  31.03200  1.000 70.29000  ? 524  GLN   A N   1 
ATOM   609  C  CA  . GLN   A 1 95  ? -59.01200 21.40300  29.68000  1.000 53.17000  ? 524  GLN   A CA  1 
ATOM   610  C  C   . GLN   A 1 95  ? -58.76200 20.22300  28.75300  1.000 31.82000  ? 524  GLN   A C   1 
ATOM   611  O  O   . GLN   A 1 95  ? -58.24100 19.20700  29.21600  1.000 30.34000  ? 524  GLN   A O   1 
ATOM   612  C  CB  . GLN   A 1 95  ? -58.06200 22.51100  29.38300  1.000 39.04000  ? 524  GLN   A CB  1 
ATOM   613  C  CG  . GLN   A 1 95  ? -56.70500 22.07900  28.96900  1.000 47.56000  ? 524  GLN   A CG  1 
ATOM   614  C  CD  . GLN   A 1 95  ? -56.21700 23.02300  27.89800  1.000 53.93000  ? 524  GLN   A CD  1 
ATOM   615  O  OE1 . GLN   A 1 95  ? -55.68500 24.10100  28.18800  1.000 63.57000  ? 524  GLN   A OE1 1 
ATOM   616  N  NE2 . GLN   A 1 95  ? -56.49300 22.66700  26.64100  1.000 43.49000  ? 524  GLN   A NE2 1 
ATOM   617  N  N   . LEU   A 1 96  ? -59.14900 20.33500  27.47600  1.000 26.52000  ? 525  LEU   A N   1 
ATOM   618  C  CA  . LEU   A 1 96  ? -59.07200 19.12800  26.63500  1.000 20.66000  ? 525  LEU   A CA  1 
ATOM   619  C  C   . LEU   A 1 96  ? -57.60700 18.73600  26.44300  1.000 20.52000  ? 525  LEU   A C   1 
ATOM   620  O  O   . LEU   A 1 96  ? -56.74700 19.59500  26.24200  1.000 22.23000  ? 525  LEU   A O   1 
ATOM   621  C  CB  . LEU   A 1 96  ? -59.67100 19.36800  25.27800  1.000 16.62000  ? 525  LEU   A CB  1 
ATOM   622  C  CG  . LEU   A 1 96  ? -61.18300 19.64300  25.28100  1.000 23.95000  ? 525  LEU   A CG  1 
ATOM   623  C  CD1 . LEU   A 1 96  ? -61.65000 19.86000  23.84900  1.000 26.36000  ? 525  LEU   A CD1 1 
ATOM   624  C  CD2 . LEU   A 1 96  ? -61.95400 18.49000  25.90300  1.000 27.99000  ? 525  LEU   A CD2 1 
ATOM   625  N  N   . ALA   A 1 97  ? -57.31400 17.42700  26.52000  1.000 18.44000  ? 526  ALA   A N   1 
ATOM   626  C  CA  . ALA   A 1 97  ? -55.91500 17.03200  26.37400  1.000 15.71000  ? 526  ALA   A CA  1 
ATOM   627  C  C   . ALA   A 1 97  ? -55.88200 15.57600  25.92600  1.000 15.20000  ? 526  ALA   A C   1 
ATOM   628  O  O   . ALA   A 1 97  ? -56.75400 14.80100  26.28200  1.000 16.91000  ? 526  ALA   A O   1 
ATOM   629  C  CB  . ALA   A 1 97  ? -55.13500 17.17600  27.69900  1.000 17.02000  ? 526  ALA   A CB  1 
ATOM   630  N  N   . ILE   A 1 98  ? -54.84400 15.21100  25.18200  1.000 14.98000  ? 527  ILE   A N   1 
ATOM   631  C  CA  . ILE   A 1 98  ? -54.61800 13.81200  24.83000  1.000 13.57000  ? 527  ILE   A CA  1 
ATOM   632  C  C   . ILE   A 1 98  ? -53.34100 13.35600  25.49800  1.000 12.69000  ? 527  ILE   A C   1 
ATOM   633  O  O   . ILE   A 1 98  ? -52.32600 14.04200  25.42700  1.000 14.65000  ? 527  ILE   A O   1 
ATOM   634  C  CB  . ILE   A 1 98  ? -54.51600 13.63700  23.30000  1.000 17.38000  ? 527  ILE   A CB  1 
ATOM   635  C  CG1 . ILE   A 1 98  ? -55.79500 14.08800  22.53300  1.000 17.40000  ? 527  ILE   A CG1 1 
ATOM   636  C  CG2 . ILE   A 1 98  ? -54.15200 12.16900  22.96800  1.000 16.16000  ? 527  ILE   A CG2 1 
ATOM   637  C  CD1 . ILE   A 1 98  ? -57.01400 13.24400  22.83400  1.000 19.01000  ? 527  ILE   A CD1 1 
ATOM   638  N  N   . VAL   A 1 99  ? -53.37200 12.17300  26.15300  1.000 11.85000  ? 528  VAL   A N   1 
ATOM   639  C  CA  . VAL   A 1 99  ? -52.21000 11.63700  26.85400  1.000 11.55000  ? 528  VAL   A CA  1 
ATOM   640  C  C   . VAL   A 1 99  ? -51.66700 10.43000  26.08100  1.000 13.84000  ? 528  VAL   A C   1 
ATOM   641  O  O   . VAL   A 1 99  ? -52.43000 9.52200   25.73000  1.000 13.54000  ? 528  VAL   A O   1 
ATOM   642  C  CB  . VAL   A 1 99  ? -52.56700 11.21400  28.29300  1.000 14.17000  ? 528  VAL   A CB  1 
ATOM   643  C  CG1 . VAL   A 1 99  ? -51.36700 10.60700  29.05500  1.000 16.43000  ? 528  VAL   A CG1 1 
ATOM   644  C  CG2 . VAL   A 1 99  ? -53.19400 12.47900  29.03300  1.000 14.19000  ? 528  VAL   A CG2 1 
ATOM   645  N  N   . THR   A 1 100 ? -50.36700 10.41000  25.85600  1.000 14.06000  ? 529  THR   A N   1 
ATOM   646  C  CA  . THR   A 1 100 ? -49.76100 9.26400   25.15900  1.000 13.92000  ? 529  THR   A CA  1 
ATOM   647  C  C   . THR   A 1 100 ? -48.57800 8.77400   25.97700  1.000 12.47000  ? 529  THR   A C   1 
ATOM   648  O  O   . THR   A 1 100 ? -48.08600 9.42600   26.93400  1.000 14.17000  ? 529  THR   A O   1 
ATOM   649  C  CB  . THR   A 1 100 ? -49.29400 9.59700   23.72300  1.000 12.83000  ? 529  THR   A CB  1 
ATOM   650  O  OG1 . THR   A 1 100 ? -48.17400 10.53800  23.82600  1.000 12.93000  ? 529  THR   A OG1 1 
ATOM   651  C  CG2 . THR   A 1 100 ? -50.43600 10.17700  22.86400  1.000 15.03000  ? 529  THR   A CG2 1 
ATOM   652  N  N   . GLN   A 1 101 ? -48.01300 7.63500   25.53700  1.000 13.25000  ? 530  GLN   A N   1 
ATOM   653  C  CA  . GLN   A 1 101 ? -46.67800 7.33700   26.05500  1.000 12.96000  ? 530  GLN   A CA  1 
ATOM   654  C  C   . GLN   A 1 101 ? -45.68200 8.48300   25.83100  1.000 16.64000  ? 530  GLN   A C   1 
ATOM   655  O  O   . GLN   A 1 101 ? -45.82700 9.29300   24.90400  1.000 14.40000  ? 530  GLN   A O   1 
ATOM   656  C  CB  . GLN   A 1 101 ? -46.10200 6.07200   25.37000  1.000 13.15000  ? 530  GLN   A CB  1 
ATOM   657  C  CG  . GLN   A 1 101 ? -45.75400 6.32500   23.91700  1.000 14.98000  ? 530  GLN   A CG  1 
ATOM   658  C  CD  . GLN   A 1 101 ? -45.29200 5.05200   23.19100  1.000 16.48000  ? 530  GLN   A CD  1 
ATOM   659  O  OE1 . GLN   A 1 101 ? -45.83300 4.71800   22.12300  1.000 16.71000  ? 530  GLN   A OE1 1 
ATOM   660  N  NE2 . GLN   A 1 101 ? -44.32700 4.32000   23.78900  1.000 16.82000  ? 530  GLN   A NE2 1 
ATOM   661  N  N   . TRP   A 1 102 ? -44.64000 8.52000   26.66900  1.000 16.17000  ? 531  TRP   A N   1 
ATOM   662  C  CA  . TRP   A 1 102 ? -43.47700 9.40200   26.48800  1.000 15.31000  ? 531  TRP   A CA  1 
ATOM   663  C  C   . TRP   A 1 102 ? -42.40400 8.69700   25.65900  1.000 16.51000  ? 531  TRP   A C   1 
ATOM   664  O  O   . TRP   A 1 102 ? -41.87400 7.66800   26.07900  1.000 18.24000  ? 531  TRP   A O   1 
ATOM   665  C  CB  . TRP   A 1 102 ? -42.92100 9.80000   27.87900  1.000 15.59000  ? 531  TRP   A CB  1 
ATOM   666  C  CG  . TRP   A 1 102 ? -41.69400 10.68900  27.70000  1.000 16.14000  ? 531  TRP   A CG  1 
ATOM   667  C  CD1 . TRP   A 1 102 ? -40.38300 10.37100  27.93600  1.000 19.49000  ? 531  TRP   A CD1 1 
ATOM   668  C  CD2 . TRP   A 1 102 ? -41.70800 12.00200  27.18000  1.000 17.31000  ? 531  TRP   A CD2 1 
ATOM   669  N  NE1 . TRP   A 1 102 ? -39.57200 11.43500  27.59300  1.000 18.51000  ? 531  TRP   A NE1 1 
ATOM   670  C  CE2 . TRP   A 1 102 ? -40.36600 12.44800  27.13000  1.000 18.18000  ? 531  TRP   A CE2 1 
ATOM   671  C  CE3 . TRP   A 1 102 ? -42.73700 12.87800  26.81200  1.000 17.33000  ? 531  TRP   A CE3 1 
ATOM   672  C  CZ2 . TRP   A 1 102 ? -40.01000 13.72900  26.64700  1.000 19.65000  ? 531  TRP   A CZ2 1 
ATOM   673  C  CZ3 . TRP   A 1 102 ? -42.38000 14.16200  26.30200  1.000 21.46000  ? 531  TRP   A CZ3 1 
ATOM   674  C  CH2 . TRP   A 1 102 ? -41.02800 14.55900  26.24700  1.000 23.95000  ? 531  TRP   A CH2 1 
ATOM   675  N  N   . CYS   A 1 103 ? -42.03500 9.27100   24.50400  1.000 13.59000  ? 532  CYS   A N   1 
ATOM   676  C  CA  . CYS   A 1 103 ? -40.95800 8.67700   23.69400  1.000 15.50000  ? 532  CYS   A CA  1 
ATOM   677  C  C   . CYS   A 1 103 ? -39.59800 9.12200   24.19700  1.000 19.31000  ? 532  CYS   A C   1 
ATOM   678  O  O   . CYS   A 1 103 ? -39.36900 10.31000  24.45500  1.000 19.76000  ? 532  CYS   A O   1 
ATOM   679  C  CB  . CYS   A 1 103 ? -41.13400 9.09100   22.21600  1.000 20.63000  ? 532  CYS   A CB  1 
ATOM   680  S  SG  . CYS   A 1 103 ? -42.67600 8.45900   21.53200  1.000 19.08000  ? 532  CYS   A SG  1 
ATOM   681  N  N   . GLU   A 1 104 ? -38.66900 8.18600   24.31000  1.000 17.08000  ? 533  GLU   A N   1 
ATOM   682  C  CA  . GLU   A 1 104 ? -37.31900 8.50700   24.77600  1.000 18.41000  ? 533  GLU   A CA  1 
ATOM   683  C  C   . GLU   A 1 104 ? -36.52600 8.76900   23.50800  1.000 21.45000  ? 533  GLU   A C   1 
ATOM   684  O  O   . GLU   A 1 104 ? -36.09400 7.84000   22.84200  1.000 26.34000  ? 533  GLU   A O   1 
ATOM   685  C  CB  . GLU   A 1 104 ? -36.74500 7.33000   25.55100  1.000 26.85000  ? 533  GLU   A CB  1 
ATOM   686  C  CG  . GLU   A 1 104 ? -37.43900 7.12500   26.87900  1.000 31.00000  ? 533  GLU   A CG  1 
ATOM   687  C  CD  . GLU   A 1 104 ? -37.17700 8.22600   27.87900  1.000 32.26000  ? 533  GLU   A CD  1 
ATOM   688  O  OE1 . GLU   A 1 104 ? -36.15500 8.92800   27.70800  1.000 32.01000  ? 533  GLU   A OE1 1 
ATOM   689  O  OE2 . GLU   A 1 104 ? -37.93400 8.28600   28.89800  1.000 33.83000  ? 533  GLU   A OE2 1 
ATOM   690  N  N   . GLY   A 1 105 ? -36.28200 10.01900  23.19800  1.000 23.28000  ? 534  GLY   A N   1 
ATOM   691  C  CA  . GLY   A 1 105 ? -35.53000 10.34800  22.01100  1.000 27.79000  ? 534  GLY   A CA  1 
ATOM   692  C  C   . GLY   A 1 105 ? -36.14700 11.57700  21.37900  1.000 26.78000  ? 534  GLY   A C   1 
ATOM   693  O  O   . GLY   A 1 105 ? -36.86100 12.32500  22.05100  1.000 25.49000  ? 534  GLY   A O   1 
ATOM   694  N  N   . SER   A 1 106 ? -35.86600 11.79000  20.09400  1.000 20.11000  ? 535  SER   A N   1 
ATOM   695  C  CA  . SER   A 1 106 ? -36.31000 12.99500  19.38100  1.000 18.89000  ? 535  SER   A CA  1 
ATOM   696  C  C   . SER   A 1 106 ? -37.18100 12.64500  18.18700  1.000 23.74000  ? 535  SER   A C   1 
ATOM   697  O  O   . SER   A 1 106 ? -37.20200 11.48800  17.72700  1.000 19.83000  ? 535  SER   A O   1 
ATOM   698  C  CB  . SER   A 1 106 ? -35.08000 13.79100  18.87600  1.000 23.89000  ? 535  SER   A CB  1 
ATOM   699  O  OG  . SER   A 1 106 ? -34.22900 14.05500  19.99200  1.000 28.49000  ? 535  SER   A OG  1 
ATOM   700  N  N   . SER   A 1 107 ? -37.85400 13.66800  17.63300  1.000 17.33000  ? 536  SER   A N   1 
ATOM   701  C  CA  . SER   A 1 107 ? -38.59400 13.48400  16.39500  1.000 19.24000  ? 536  SER   A CA  1 
ATOM   702  C  C   . SER   A 1 107 ? -37.60700 13.36500  15.23500  1.000 16.73000  ? 536  SER   A C   1 
ATOM   703  O  O   . SER   A 1 107 ? -36.43500 13.75800  15.33800  1.000 19.33000  ? 536  SER   A O   1 
ATOM   704  C  CB  . SER   A 1 107 ? -39.53200 14.66400  16.12300  1.000 20.20000  ? 536  SER   A CB  1 
ATOM   705  O  OG  . SER   A 1 107 ? -38.73000 15.82400  15.76700  1.000 21.05000  ? 536  SER   A OG  1 
ATOM   706  N  N   A LEU   A 1 108 ? -38.08300 12.82200  14.11500  0.512 16.33000  ? 537  LEU   A N   1 
ATOM   707  N  N   B LEU   A 1 108 ? -38.08300 12.80600  14.12500  0.488 16.32000  ? 537  LEU   A N   1 
ATOM   708  C  CA  A LEU   A 1 108 ? -37.22400 12.73600  12.92800  0.512 14.20000  ? 537  LEU   A CA  1 
ATOM   709  C  CA  B LEU   A 1 108 ? -37.24500 12.73400  12.92300  0.488 14.23000  ? 537  LEU   A CA  1 
ATOM   710  C  C   A LEU   A 1 108 ? -36.83700 14.12800  12.43200  0.512 18.81000  ? 537  LEU   A C   1 
ATOM   711  C  C   B LEU   A 1 108 ? -36.84300 14.12500  12.43800  0.488 18.81000  ? 537  LEU   A C   1 
ATOM   712  O  O   A LEU   A 1 108 ? -35.70600 14.34200  11.97700  0.512 19.85000  ? 537  LEU   A O   1 
ATOM   713  O  O   B LEU   A 1 108 ? -35.70800 14.33200  11.98900  0.488 19.84000  ? 537  LEU   A O   1 
ATOM   714  C  CB  A LEU   A 1 108 ? -37.95700 11.95500  11.83700  0.512 16.27000  ? 537  LEU   A CB  1 
ATOM   715  C  CB  B LEU   A 1 108 ? -38.00700 11.98300  11.83600  0.488 16.30000  ? 537  LEU   A CB  1 
ATOM   716  C  CG  A LEU   A 1 108 ? -38.09100 10.45500  12.02800  0.512 21.46000  ? 537  LEU   A CG  1 
ATOM   717  C  CG  B LEU   A 1 108 ? -37.25200 11.66100  10.57000  0.488 17.86000  ? 537  LEU   A CG  1 
ATOM   718  C  CD1 A LEU   A 1 108 ? -38.60000 9.86100   10.69000  0.512 16.98000  ? 537  LEU   A CD1 1 
ATOM   719  C  CD1 B LEU   A 1 108 ? -35.96900 10.84400  10.89400  0.488 19.36000  ? 537  LEU   A CD1 1 
ATOM   720  C  CD2 A LEU   A 1 108 ? -36.74800 9.82900   12.40500  0.512 15.89000  ? 537  LEU   A CD2 1 
ATOM   721  C  CD2 B LEU   A 1 108 ? -38.18200 10.90200  9.66100   0.488 19.11000  ? 537  LEU   A CD2 1 
ATOM   722  N  N   . TYR   A 1 109 ? -37.75700 15.09800  12.54400  1.000 19.03000  ? 538  TYR   A N   1 
ATOM   723  C  CA  . TYR   A 1 109 ? -37.44100 16.48900  12.17000  1.000 16.96000  ? 538  TYR   A CA  1 
ATOM   724  C  C   . TYR   A 1 109 ? -36.24900 17.00400  12.96700  1.000 18.46000  ? 538  TYR   A C   1 
ATOM   725  O  O   . TYR   A 1 109 ? -35.28800 17.54800  12.41200  1.000 20.92000  ? 538  TYR   A O   1 
ATOM   726  C  CB  . TYR   A 1 109 ? -38.67300 17.35400  12.42200  1.000 18.34000  ? 538  TYR   A CB  1 
ATOM   727  C  CG  . TYR   A 1 109 ? -38.43900 18.78600  11.96900  1.000 19.48000  ? 538  TYR   A CG  1 
ATOM   728  C  CD1 . TYR   A 1 109 ? -37.70800 19.69000  12.74500  1.000 30.06000  ? 538  TYR   A CD1 1 
ATOM   729  C  CD2 . TYR   A 1 109 ? -38.96700 19.19400  10.78100  1.000 20.29000  ? 538  TYR   A CD2 1 
ATOM   730  C  CE1 . TYR   A 1 109 ? -37.51200 21.01100  12.30700  1.000 26.81000  ? 538  TYR   A CE1 1 
ATOM   731  C  CE2 . TYR   A 1 109 ? -38.77400 20.53900  10.34000  1.000 22.41000  ? 538  TYR   A CE2 1 
ATOM   732  C  CZ  . TYR   A 1 109 ? -38.02800 21.38400  11.11000  1.000 26.79000  ? 538  TYR   A CZ  1 
ATOM   733  O  OH  . TYR   A 1 109 ? -37.87600 22.68300  10.64700  1.000 39.09000  ? 538  TYR   A OH  1 
ATOM   734  N  N   . HIS   A 1 110 ? -36.26900 16.79800  14.28800  1.000 17.11000  ? 539  HIS   A N   1 
ATOM   735  C  CA  . HIS   A 1 110 ? -35.16400 17.21100  15.13200  1.000 20.97000  ? 539  HIS   A CA  1 
ATOM   736  C  C   . HIS   A 1 110 ? -33.85900 16.52800  14.72300  1.000 25.73000  ? 539  HIS   A C   1 
ATOM   737  O  O   . HIS   A 1 110 ? -32.81000 17.17200  14.63300  1.000 21.45000  ? 539  HIS   A O   1 
ATOM   738  C  CB  . HIS   A 1 110 ? -35.52000 16.86800  16.57800  1.000 21.34000  ? 539  HIS   A CB  1 
ATOM   739  C  CG  . HIS   A 1 110 ? -34.61400 17.48800  17.57000  1.000 20.98000  ? 539  HIS   A CG  1 
ATOM   740  N  ND1 . HIS   A 1 110 ? -34.72100 18.82600  17.91600  1.000 24.32000  ? 539  HIS   A ND1 1 
ATOM   741  C  CD2 . HIS   A 1 110 ? -33.61300 16.96500  18.32100  1.000 24.85000  ? 539  HIS   A CD2 1 
ATOM   742  C  CE1 . HIS   A 1 110 ? -33.80200 19.08800  18.83900  1.000 24.90000  ? 539  HIS   A CE1 1 
ATOM   743  N  NE2 . HIS   A 1 110 ? -33.11300 17.99000  19.09000  1.000 27.68000  ? 539  HIS   A NE2 1 
ATOM   744  N  N   . HIS   A 1 111 ? -33.89700 15.20700  14.48200  1.000 18.62000  ? 540  HIS   A N   1 
ATOM   745  C  CA  . HIS   A 1 111 ? -32.68500 14.51000  14.08600  1.000 20.32000  ? 540  HIS   A CA  1 
ATOM   746  C  C   . HIS   A 1 111 ? -32.14200 15.04700  12.77400  1.000 19.38000  ? 540  HIS   A C   1 
ATOM   747  O  O   . HIS   A 1 111 ? -30.93400 15.30700  12.65100  1.000 24.25000  ? 540  HIS   A O   1 
ATOM   748  C  CB  . HIS   A 1 111 ? -32.98800 13.02300  13.93900  1.000 18.43000  ? 540  HIS   A CB  1 
ATOM   749  C  CG  . HIS   A 1 111 ? -32.96000 12.27000  15.22400  1.000 19.78000  ? 540  HIS   A CG  1 
ATOM   750  N  ND1 . HIS   A 1 111 ? -31.78900 12.04200  15.92800  1.000 23.31000  ? 540  HIS   A ND1 1 
ATOM   751  C  CD2 . HIS   A 1 111 ? -33.94700 11.63000  15.90600  1.000 20.56000  ? 540  HIS   A CD2 1 
ATOM   752  C  CE1 . HIS   A 1 111 ? -32.06800 11.30900  16.99900  1.000 22.76000  ? 540  HIS   A CE1 1 
ATOM   753  N  NE2 . HIS   A 1 111 ? -33.37300 11.06800  17.01500  1.000 21.66000  ? 540  HIS   A NE2 1 
ATOM   754  N  N   . LEU   A 1 112 ? -33.01800 15.18100  11.77300  1.000 17.36000  ? 541  LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 112 ? -32.56400 15.43900  10.41000  1.000 20.43000  ? 541  LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 112 ? -32.16400 16.89200  10.24000  1.000 24.39000  ? 541  LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 112 ? -31.15400 17.18700  9.59400   1.000 24.42000  ? 541  LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 112 ? -33.64100 15.08900  9.36500   1.000 19.56000  ? 541  LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 112 ? -33.95000 13.58000  9.26800   1.000 20.18000  ? 541  LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 112 ? -35.07500 13.24400  8.29300   1.000 20.21000  ? 541  LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 112 ? -32.67400 12.83300  8.87100   1.000 22.61000  ? 541  LEU   A CD2 1 
ATOM   762  N  N   . HIS   A 1 113 ? -32.92500 17.80500  10.83100  1.000 22.54000  ? 542  HIS   A N   1 
ATOM   763  C  CA  . HIS   A 1 113 ? -32.81100 19.21200  10.45600  1.000 21.06000  ? 542  HIS   A CA  1 
ATOM   764  C  C   . HIS   A 1 113 ? -32.30100 20.11300  11.54900  1.000 25.60000  ? 542  HIS   A C   1 
ATOM   765  O  O   . HIS   A 1 113 ? -31.87500 21.23600  11.24000  1.000 27.60000  ? 542  HIS   A O   1 
ATOM   766  C  CB  . HIS   A 1 113 ? -34.16400 19.74800  9.96400   1.000 21.03000  ? 542  HIS   A CB  1 
ATOM   767  C  CG  . HIS   A 1 113 ? -34.77400 18.88200  8.91300   1.000 24.52000  ? 542  HIS   A CG  1 
ATOM   768  N  ND1 . HIS   A 1 113 ? -34.09900 18.53400  7.75500   1.000 22.53000  ? 542  HIS   A ND1 1 
ATOM   769  C  CD2 . HIS   A 1 113 ? -35.97800 18.27200  8.85200   1.000 17.87000  ? 542  HIS   A CD2 1 
ATOM   770  C  CE1 . HIS   A 1 113 ? -34.88300 17.75800  7.01700   1.000 19.70000  ? 542  HIS   A CE1 1 
ATOM   771  N  NE2 . HIS   A 1 113 ? -36.01300 17.55200  7.68100   1.000 18.44000  ? 542  HIS   A NE2 1 
ATOM   772  N  N   . ILE   A 1 114 ? -32.27600 19.65900  12.79000  1.000 21.85000  ? 543  ILE   A N   1 
ATOM   773  C  CA  . ILE   A 1 114 ? -31.83900 20.48000  13.92400  1.000 20.82000  ? 543  ILE   A CA  1 
ATOM   774  C  C   . ILE   A 1 114 ? -30.49100 20.02100  14.46500  1.000 33.43000  ? 543  ILE   A C   1 
ATOM   775  O  O   . ILE   A 1 114 ? -29.52800 20.79400  14.50300  1.000 31.27000  ? 543  ILE   A O   1 
ATOM   776  C  CB  . ILE   A 1 114 ? -32.90900 20.53000  15.04200  1.000 22.20000  ? 543  ILE   A CB  1 
ATOM   777  C  CG1 . ILE   A 1 114 ? -34.23700 21.02600  14.49300  1.000 22.15000  ? 543  ILE   A CG1 1 
ATOM   778  C  CG2 . ILE   A 1 114 ? -32.39600 21.44700  16.20100  1.000 26.68000  ? 543  ILE   A CG2 1 
ATOM   779  C  CD1 . ILE   A 1 114 ? -34.20300 22.42800  13.88500  1.000 27.37000  ? 543  ILE   A CD1 1 
ATOM   780  N  N   . ILE   A 1 115 ? -30.39800 18.77400  14.91700  1.000 24.33000  ? 544  ILE   A N   1 
ATOM   781  C  CA  . ILE   A 1 115 ? -29.12400 18.28800  15.42400  1.000 21.70000  ? 544  ILE   A CA  1 
ATOM   782  C  C   . ILE   A 1 115 ? -28.33800 17.52900  14.35000  1.000 27.55000  ? 544  ILE   A C   1 
ATOM   783  O  O   . ILE   A 1 115 ? -27.20100 17.13500  14.59900  1.000 32.84000  ? 544  ILE   A O   1 
ATOM   784  C  CB  . ILE   A 1 115 ? -29.30300 17.46300  16.71900  1.000 33.42000  ? 544  ILE   A CB  1 
ATOM   785  C  CG1 . ILE   A 1 115 ? -30.17800 16.22700  16.51000  1.000 27.43000  ? 544  ILE   A CG1 1 
ATOM   786  C  CG2 . ILE   A 1 115 ? -29.89800 18.34200  17.81400  1.000 32.20000  ? 544  ILE   A CG2 1 
ATOM   787  C  CD1 . ILE   A 1 115 ? -30.25200 15.28600  17.72700  1.000 30.06000  ? 544  ILE   A CD1 1 
ATOM   788  N  N   . GLU   A 1 116 ? -28.91000 17.35900  13.15700  1.000 27.10000  ? 545  GLU   A N   1 
ATOM   789  C  CA  . GLU   A 1 116 ? -28.22600 16.79600  11.98900  1.000 34.32000  ? 545  GLU   A CA  1 
ATOM   790  C  C   . GLU   A 1 116 ? -27.51500 15.50300  12.34400  1.000 33.77000  ? 545  GLU   A C   1 
ATOM   791  O  O   . GLU   A 1 116 ? -26.33600 15.30400  12.07300  1.000 35.90000  ? 545  GLU   A O   1 
ATOM   792  C  CB  . GLU   A 1 116 ? -27.27700 17.82400  11.37600  1.000 38.32000  ? 545  GLU   A CB  1 
ATOM   793  C  CG  . GLU   A 1 116 ? -28.08700 18.93800  10.75400  1.000 42.81000  ? 545  GLU   A CG  1 
ATOM   794  C  CD  . GLU   A 1 116 ? -27.25100 20.09500  10.28800  1.000 58.85000  ? 545  GLU   A CD  1 
ATOM   795  O  OE1 . GLU   A 1 116 ? -26.09300 20.22000  10.74200  1.000 71.32000  ? 545  GLU   A OE1 1 
ATOM   796  O  OE2 . GLU   A 1 116 ? -27.75100 20.85700  9.43600   1.000 72.24000  ? 545  GLU   A OE2 1 
ATOM   797  N  N   . THR   A 1 117 ? -28.26100 14.61700  12.98800  1.000 26.63000  ? 546  THR   A N   1 
ATOM   798  C  CA  . THR   A 1 117 ? -27.81200 13.25500  13.19400  1.000 29.11000  ? 546  THR   A CA  1 
ATOM   799  C  C   . THR   A 1 117 ? -27.41100 12.64200  11.85300  1.000 32.24000  ? 546  THR   A C   1 
ATOM   800  O  O   . THR   A 1 117 ? -28.07200 12.86000  10.83300  1.000 40.69000  ? 546  THR   A O   1 
ATOM   801  C  CB  . THR   A 1 117 ? -28.96100 12.45600  13.84100  1.000 27.65000  ? 546  THR   A CB  1 
ATOM   802  O  OG1 . THR   A 1 117 ? -29.31800 13.07500  15.08500  1.000 25.26000  ? 546  THR   A OG1 1 
ATOM   803  C  CG2 . THR   A 1 117 ? -28.54600 11.03800  14.11100  1.000 31.13000  ? 546  THR   A CG2 1 
ATOM   804  N  N   . LYS   A 1 118 ? -26.32100 11.89700  11.85000  1.000 36.49000  ? 547  LYS   A N   1 
ATOM   805  C  CA  . LYS   A 1 118 ? -25.84900 11.26300  10.61900  1.000 46.53000  ? 547  LYS   A CA  1 
ATOM   806  C  C   . LYS   A 1 118 ? -26.19900 9.78200   10.74200  1.000 37.87000  ? 547  LYS   A C   1 
ATOM   807  O  O   . LYS   A 1 118 ? -25.47600 9.00400   11.37100  1.000 44.10000  ? 547  LYS   A O   1 
ATOM   808  C  CB  . LYS   A 1 118 ? -24.34200 11.50700  10.40000  1.000 46.21000  ? 547  LYS   A CB  1 
ATOM   809  C  CG  . LYS   A 1 118 ? -23.98300 12.96100  10.00300  1.000 50.88000  ? 547  LYS   A CG  1 
ATOM   810  C  CD  . LYS   A 1 118 ? -24.83700 13.49400  8.84300   1.000 52.58000  ? 547  LYS   A CD  1 
ATOM   811  C  CE  . LYS   A 1 118 ? -25.32000 14.94300  9.08800   1.000 53.92000  ? 547  LYS   A CE  1 
ATOM   812  N  NZ  . LYS   A 1 118 ? -26.40700 15.39100  8.12300   1.000 54.32000  ? 547  LYS   A NZ  1 
ATOM   813  N  N   . PHE   A 1 119 ? -27.35000 9.40900   10.18700  1.000 31.68000  ? 548  PHE   A N   1 
ATOM   814  C  CA  . PHE   A 1 119 ? -27.75100 8.01100   10.16400  1.000 28.67000  ? 548  PHE   A CA  1 
ATOM   815  C  C   . PHE   A 1 119 ? -27.05100 7.30100   9.00000   1.000 34.36000  ? 548  PHE   A C   1 
ATOM   816  O  O   . PHE   A 1 119 ? -26.93200 7.85900   7.91100   1.000 34.07000  ? 548  PHE   A O   1 
ATOM   817  C  CB  . PHE   A 1 119 ? -29.26900 7.90700   9.98300   1.000 24.73000  ? 548  PHE   A CB  1 
ATOM   818  C  CG  . PHE   A 1 119 ? -30.07900 8.41600   11.16800  1.000 25.64000  ? 548  PHE   A CG  1 
ATOM   819  C  CD1 . PHE   A 1 119 ? -29.98700 7.79600   12.41600  1.000 30.80000  ? 548  PHE   A CD1 1 
ATOM   820  C  CD2 . PHE   A 1 119 ? -30.97400 9.46400   11.00000  1.000 26.56000  ? 548  PHE   A CD2 1 
ATOM   821  C  CE1 . PHE   A 1 119 ? -30.74900 8.24500   13.50100  1.000 32.46000  ? 548  PHE   A CE1 1 
ATOM   822  C  CE2 . PHE   A 1 119 ? -31.73400 9.92700   12.07400  1.000 22.79000  ? 548  PHE   A CE2 1 
ATOM   823  C  CZ  . PHE   A 1 119 ? -31.61400 9.31500   13.32100  1.000 24.60000  ? 548  PHE   A CZ  1 
ATOM   824  N  N   . GLU   A 1 120 ? -26.62100 6.06100   9.22400   1.000 26.94000  ? 549  GLU   A N   1 
ATOM   825  C  CA  . GLU   A 1 120 ? -26.20700 5.22400   8.09900   1.000 31.72000  ? 549  GLU   A CA  1 
ATOM   826  C  C   . GLU   A 1 120 ? -27.39200 4.95100   7.19000   1.000 30.37000  ? 549  GLU   A C   1 
ATOM   827  O  O   . GLU   A 1 120 ? -28.54800 4.94400   7.63200   1.000 26.65000  ? 549  GLU   A O   1 
ATOM   828  C  CB  . GLU   A 1 120 ? -25.63900 3.90400   8.60500   1.000 39.19000  ? 549  GLU   A CB  1 
ATOM   829  C  CG  . GLU   A 1 120 ? -24.48600 4.01700   9.58000   1.000 47.59000  ? 549  GLU   A CG  1 
ATOM   830  C  CD  . GLU   A 1 120 ? -23.20900 4.63700   9.00000   1.000 66.07000  ? 549  GLU   A CD  1 
ATOM   831  O  OE1 . GLU   A 1 120 ? -23.24700 5.46400   8.06300   1.000 73.85000  ? 549  GLU   A OE1 1 
ATOM   832  O  OE2 . GLU   A 1 120 ? -22.12400 4.26800   9.49500   1.000 81.99000  ? 549  GLU   A OE2 1 
ATOM   833  N  N   . MET   A 1 121 ? -27.10800 4.67600   5.91000   1.000 24.97000  ? 550  MET   A N   1 
ATOM   834  C  CA  . MET   A 1 121 ? -28.19700 4.32500   4.98000   1.000 25.46000  ? 550  MET   A CA  1 
ATOM   835  C  C   . MET   A 1 121 ? -29.03900 3.14600   5.44000   1.000 25.26000  ? 550  MET   A C   1 
ATOM   836  O  O   . MET   A 1 121 ? -30.27200 3.15300   5.26700   1.000 25.58000  ? 550  MET   A O   1 
ATOM   837  C  CB  . MET   A 1 121 ? -27.64900 4.09900   3.57400   1.000 27.97000  ? 550  MET   A CB  1 
ATOM   838  C  CG  . MET   A 1 121 ? -28.75000 3.76200   2.59800   1.000 28.49000  ? 550  MET   A CG  1 
ATOM   839  S  SD  . MET   A 1 121 ? -29.91100 5.15500   2.28900   1.000 29.63000  ? 550  MET   A SD  1 
ATOM   840  C  CE  . MET   A 1 121 ? -28.78700 6.56400   2.18500   1.000 29.64000  ? 550  MET   A CE  1 
ATOM   841  N  N   . ILE   A 1 122 ? -28.42200 2.10500   6.01400   1.000 20.47000  ? 551  ILE   A N   1 
ATOM   842  C  CA  . ILE   A 1 122 ? -29.22600 0.98000   6.49100   1.000 24.88000  ? 551  ILE   A CA  1 
ATOM   843  C  C   . ILE   A 1 122 ? -30.24500 1.44900   7.53800   1.000 23.53000  ? 551  ILE   A C   1 
ATOM   844  O  O   . ILE   A 1 122 ? -31.35300 0.91900   7.60500   1.000 23.20000  ? 551  ILE   A O   1 
ATOM   845  C  CB  . ILE   A 1 122 ? -28.33400 -0.14900  7.05800   1.000 31.94000  ? 551  ILE   A CB  1 
ATOM   846  C  CG1 . ILE   A 1 122 ? -29.17200 -1.38200  7.34400   1.000 36.05000  ? 551  ILE   A CG1 1 
ATOM   847  C  CG2 . ILE   A 1 122 ? -27.65100 0.26200   8.33100   1.000 31.70000  ? 551  ILE   A CG2 1 
ATOM   848  C  CD1 . ILE   A 1 122 ? -28.36800 -2.51900  7.84400   1.000 37.86000  ? 551  ILE   A CD1 1 
ATOM   849  N  N   . LYS   A 1 123 ? -29.86600 2.41000   8.37600   1.000 22.34000  ? 552  LYS   A N   1 
ATOM   850  C  CA  . LYS   A 1 123 ? -30.77700 2.91200   9.40200   1.000 22.58000  ? 552  LYS   A CA  1 
ATOM   851  C  C   . LYS   A 1 123 ? -31.83200 3.82600   8.78200   1.000 20.68000  ? 552  LYS   A C   1 
ATOM   852  O  O   . LYS   A 1 123 ? -32.99300 3.81000   9.20600   1.000 20.94000  ? 552  LYS   A O   1 
ATOM   853  C  CB  . LYS   A 1 123 ? -29.97600 3.63300   10.49300  1.000 29.20000  ? 552  LYS   A CB  1 
ATOM   854  C  CG  . LYS   A 1 123 ? -30.78300 4.29300   11.64600  1.000 31.32000  ? 552  LYS   A CG  1 
ATOM   855  C  CD  . LYS   A 1 123 ? -31.19800 3.28800   12.67300  1.000 35.00000  ? 552  LYS   A CD  1 
ATOM   856  C  CE  . LYS   A 1 123 ? -31.64400 3.91100   14.04400  1.000 37.87000  ? 552  LYS   A CE  1 
ATOM   857  N  NZ  . LYS   A 1 123 ? -30.53700 4.29400   14.96600  1.000 53.95000  ? 552  LYS   A NZ  1 
ATOM   858  N  N   . LEU   A 1 124 ? -31.43800 4.64200   7.80100   1.000 24.59000  ? 553  LEU   A N   1 
ATOM   859  C  CA  . LEU   A 1 124 ? -32.40500 5.48500   7.10000   1.000 22.37000  ? 553  LEU   A CA  1 
ATOM   860  C  C   . LEU   A 1 124 ? -33.48800 4.64500   6.46700   1.000 22.26000  ? 553  LEU   A C   1 
ATOM   861  O  O   . LEU   A 1 124 ? -34.67000 5.02400   6.48800   1.000 19.29000  ? 553  LEU   A O   1 
ATOM   862  C  CB  . LEU   A 1 124 ? -31.68500 6.37200   6.04800   1.000 19.28000  ? 553  LEU   A CB  1 
ATOM   863  C  CG  . LEU   A 1 124 ? -30.74900 7.46200   6.59500   1.000 23.15000  ? 553  LEU   A CG  1 
ATOM   864  C  CD1 . LEU   A 1 124 ? -29.90200 8.05800   5.43800   1.000 25.08000  ? 553  LEU   A CD1 1 
ATOM   865  C  CD2 . LEU   A 1 124 ? -31.54900 8.58700   7.28300   1.000 25.99000  ? 553  LEU   A CD2 1 
ATOM   866  N  N   . ILE   A 1 125 ? -33.10300 3.51100   5.84000   1.000 19.04000  ? 554  ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 125 ? -34.07300 2.65700   5.18700   1.000 19.52000  ? 554  ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 125 ? -34.92900 1.98400   6.23700   1.000 19.15000  ? 554  ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 125 ? -36.12600 1.79000   6.03300   1.000 17.94000  ? 554  ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 125 ? -33.32500 1.62300   4.29300   1.000 18.45000  ? 554  ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 125 ? -32.71300 2.38900   3.10600   1.000 24.83000  ? 554  ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 125 ? -34.24000 0.54800   3.79200   1.000 19.68000  ? 554  ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 125 ? -31.67000 1.52600   2.31500   1.000 31.77000  ? 554  ILE   A CD1 1 
ATOM   874  N  N   . ASP   A 1 126 ? -34.33100 1.63700   7.37700   1.000 19.72000  ? 555  ASP   A N   1 
ATOM   875  C  CA  . ASP   A 1 126 ? -35.13300 0.99800   8.42600   1.000 17.76000  ? 555  ASP   A CA  1 
ATOM   876  C  C   . ASP   A 1 126 ? -36.16200 1.97100   8.99600   1.000 21.56000  ? 555  ASP   A C   1 
ATOM   877  O  O   . ASP   A 1 126 ? -37.28900 1.58700   9.27200   1.000 18.30000  ? 555  ASP   A O   1 
ATOM   878  C  CB  . ASP   A 1 126 ? -34.22800 0.49100   9.54700   1.000 19.00000  ? 555  ASP   A CB  1 
ATOM   879  C  CG  . ASP   A 1 126 ? -35.00700 -0.34200  10.54700  1.000 25.53000  ? 555  ASP   A CG  1 
ATOM   880  O  OD1 . ASP   A 1 126 ? -35.58500 -1.35900  10.12100  1.000 33.12000  ? 555  ASP   A OD1 1 
ATOM   881  O  OD2 . ASP   A 1 126 ? -35.07400 0.07000   11.70800  1.000 26.53000  ? 555  ASP   A OD2 1 
ATOM   882  N  N   . ILE   A 1 127 ? -35.79000 3.23500   9.15400   1.000 18.97000  ? 556  ILE   A N   1 
ATOM   883  C  CA  . ILE   A 1 127 ? -36.77400 4.24200   9.58600   1.000 18.22000  ? 556  ILE   A CA  1 
ATOM   884  C  C   . ILE   A 1 127 ? -37.89100 4.38100   8.56100   1.000 18.96000  ? 556  ILE   A C   1 
ATOM   885  O  O   . ILE   A 1 127 ? -39.07900 4.46100   8.91700   1.000 16.08000  ? 556  ILE   A O   1 
ATOM   886  C  CB  . ILE   A 1 127 ? -36.04400 5.57700   9.84300   1.000 18.23000  ? 556  ILE   A CB  1 
ATOM   887  C  CG1 . ILE   A 1 127 ? -35.18700 5.41700   11.10900  1.000 18.51000  ? 556  ILE   A CG1 1 
ATOM   888  C  CG2 . ILE   A 1 127 ? -37.03900 6.78900   9.95500   1.000 17.16000  ? 556  ILE   A CG2 1 
ATOM   889  C  CD1 . ILE   A 1 127 ? -34.18600 6.60100   11.29700  1.000 23.31000  ? 556  ILE   A CD1 1 
ATOM   890  N  N   . ALA   A 1 128 ? -37.54000 4.43200   7.26300   1.000 16.17000  ? 557  ALA   A N   1 
ATOM   891  C  CA  . ALA   A 1 128 ? -38.58100 4.48700   6.23800   1.000 17.05000  ? 557  ALA   A CA  1 
ATOM   892  C  C   . ALA   A 1 128 ? -39.49700 3.26600   6.30200   1.000 18.23000  ? 557  ALA   A C   1 
ATOM   893  O  O   . ALA   A 1 128 ? -40.71900 3.37000   6.10000   1.000 16.04000  ? 557  ALA   A O   1 
ATOM   894  C  CB  . ALA   A 1 128 ? -37.91900 4.59600   4.84200   1.000 18.19000  ? 557  ALA   A CB  1 
ATOM   895  N  N   . ARG   A 1 129 ? -38.89500 2.08600   6.50000   1.000 18.42000  ? 558  ARG   A N   1 
ATOM   896  C  CA  . ARG   A 1 129 ? -39.65700 0.83200   6.55800   1.000 14.96000  ? 558  ARG   A CA  1 
ATOM   897  C  C   . ARG   A 1 129 ? -40.63300 0.83400   7.71500   1.000 15.35000  ? 558  ARG   A C   1 
ATOM   898  O  O   . ARG   A 1 129 ? -41.82200 0.54900   7.54000   1.000 15.30000  ? 558  ARG   A O   1 
ATOM   899  C  CB  . ARG   A 1 129 ? -38.65900 -0.33300  6.70500   1.000 16.30000  ? 558  ARG   A CB  1 
ATOM   900  C  CG  . ARG   A 1 129 ? -39.40600 -1.70100  6.54000   1.000 20.56000  ? 558  ARG   A CG  1 
ATOM   901  C  CD  . ARG   A 1 129 ? -38.39800 -2.79800  6.96900   1.000 32.18000  ? 558  ARG   A CD  1 
ATOM   902  N  NE  . ARG   A 1 129 ? -37.90300 -2.61800  8.33200   1.000 38.24000  ? 558  ARG   A NE  1 
ATOM   903  C  CZ  . ARG   A 1 129 ? -38.66400 -2.76100  9.41400   1.000 33.33000  ? 558  ARG   A CZ  1 
ATOM   904  N  NH1 . ARG   A 1 129 ? -39.93000 -3.08900  9.31300   1.000 43.29000  ? 558  ARG   A NH1 1 
ATOM   905  N  NH2 . ARG   A 1 129 ? -38.12400 -2.61700  10.62800  1.000 31.54000  ? 558  ARG   A NH2 1 
ATOM   906  N  N   . GLN   A 1 130 ? -40.15200 1.22200   8.90900   1.000 16.21000  ? 559  GLN   A N   1 
ATOM   907  C  CA  . GLN   A 1 130 ? -41.04100 1.26800   10.07200  1.000 13.43000  ? 559  GLN   A CA  1 
ATOM   908  C  C   . GLN   A 1 130 ? -42.12900 2.31600   9.90800   1.000 14.96000  ? 559  GLN   A C   1 
ATOM   909  O  O   . GLN   A 1 130 ? -43.24400 2.12500   10.37400  1.000 16.80000  ? 559  GLN   A O   1 
ATOM   910  C  CB  . GLN   A 1 130 ? -40.24300 1.58300   11.31900  1.000 14.20000  ? 559  GLN   A CB  1 
ATOM   911  C  CG  . GLN   A 1 130 ? -39.23300 0.48700   11.71900  1.000 20.03000  ? 559  GLN   A CG  1 
ATOM   912  C  CD  . GLN   A 1 130 ? -38.72000 0.77900   13.12000  1.000 19.90000  ? 559  GLN   A CD  1 
ATOM   913  O  OE1 . GLN   A 1 130 ? -39.49800 1.09100   14.01200  1.000 17.01000  ? 559  GLN   A OE1 1 
ATOM   914  N  NE2 . GLN   A 1 130 ? -37.40500 0.72000   13.30500  1.000 19.10000  ? 559  GLN   A NE2 1 
ATOM   915  N  N   . THR   A 1 131 ? -41.79300 3.45700   9.30100   1.000 15.05000  ? 560  THR   A N   1 
ATOM   916  C  CA  . THR   A 1 131 ? -42.82800 4.47300   9.05400   1.000 14.41000  ? 560  THR   A CA  1 
ATOM   917  C  C   . THR   A 1 131 ? -43.88300 3.93300   8.09500   1.000 15.35000  ? 560  THR   A C   1 
ATOM   918  O  O   . THR   A 1 131 ? -45.09100 4.10100   8.32500   1.000 15.60000  ? 560  THR   A O   1 
ATOM   919  C  CB  . THR   A 1 131 ? -42.14500 5.76700   8.50100   1.000 13.66000  ? 560  THR   A CB  1 
ATOM   920  O  OG1 . THR   A 1 131 ? -41.17300 6.24300   9.45200   1.000 14.27000  ? 560  THR   A OG1 1 
ATOM   921  C  CG2 . THR   A 1 131 ? -43.20300 6.85100   8.24400   1.000 15.34000  ? 560  THR   A CG2 1 
ATOM   922  N  N   . ALA   A 1 132 ? -43.45200 3.20800   7.03100   1.000 15.58000  ? 561  ALA   A N   1 
ATOM   923  C  CA  . ALA   A 1 132 ? -44.40700 2.59700   6.13800   1.000 15.93000  ? 561  ALA   A CA  1 
ATOM   924  C  C   . ALA   A 1 132 ? -45.21400 1.54600   6.88500   1.000 13.85000  ? 561  ALA   A C   1 
ATOM   925  O  O   . ALA   A 1 132 ? -46.39400 1.32700   6.59900   1.000 15.36000  ? 561  ALA   A O   1 
ATOM   926  C  CB  . ALA   A 1 132 ? -43.67800 1.97800   4.90800   1.000 16.10000  ? 561  ALA   A CB  1 
ATOM   927  N  N   . GLN   A 1 133 ? -44.56200 0.82600   7.79200   1.000 16.75000  ? 562  GLN   A N   1 
ATOM   928  C  CA  . GLN   A 1 133 ? -45.27900 -0.20000  8.54600   1.000 13.15000  ? 562  GLN   A CA  1 
ATOM   929  C  C   . GLN   A 1 133 ? -46.39300 0.41000   9.38200   1.000 15.01000  ? 562  GLN   A C   1 
ATOM   930  O  O   . GLN   A 1 133 ? -47.52800 -0.09300  9.40400   1.000 15.38000  ? 562  GLN   A O   1 
ATOM   931  C  CB  . GLN   A 1 133 ? -44.28900 -0.95300  9.46200   1.000 15.40000  ? 562  GLN   A CB  1 
ATOM   932  C  CG  . GLN   A 1 133 ? -44.93500 -2.24100  10.08100  1.000 18.49000  ? 562  GLN   A CG  1 
ATOM   933  C  CD  . GLN   A 1 133 ? -44.65600 -3.43600  9.17200   1.000 22.47000  ? 562  GLN   A CD  1 
ATOM   934  O  OE1 . GLN   A 1 133 ? -45.55600 -3.95500  8.58300   1.000 24.63000  ? 562  GLN   A OE1 1 
ATOM   935  N  NE2 . GLN   A 1 133 ? -43.40800 -3.84000  9.09000   1.000 27.83000  ? 562  GLN   A NE2 1 
ATOM   936  N  N   . GLY   A 1 134 ? -46.11700 1.55600   10.02300  1.000 15.47000  ? 563  GLY   A N   1 
ATOM   937  C  CA  . GLY   A 1 134 ? -47.17600 2.18000   10.79100  1.000 14.79000  ? 563  GLY   A CA  1 
ATOM   938  C  C   . GLY   A 1 134 ? -48.26800 2.74000   9.89700   1.000 17.29000  ? 563  GLY   A C   1 
ATOM   939  O  O   . GLY   A 1 134 ? -49.45000 2.64900   10.20600  1.000 14.18000  ? 563  GLY   A O   1 
ATOM   940  N  N   . MET   A 1 135 ? -47.89100 3.31300   8.75800   1.000 14.63000  ? 564  MET   A N   1 
ATOM   941  C  CA  . MET   A 1 135 ? -48.90500 3.92500   7.89500   1.000 11.40000  ? 564  MET   A CA  1 
ATOM   942  C  C   . MET   A 1 135 ? -49.78200 2.83200   7.26000   1.000 15.42000  ? 564  MET   A C   1 
ATOM   943  O  O   . MET   A 1 135 ? -50.99500 2.98700   7.12400   1.000 16.48000  ? 564  MET   A O   1 
ATOM   944  C  CB  . MET   A 1 135 ? -48.12600 4.67700   6.79400   1.000 16.54000  ? 564  MET   A CB  1 
ATOM   945  C  CG  . MET   A 1 135 ? -47.64500 6.05100   7.19600   1.000 16.42000  ? 564  MET   A CG  1 
ATOM   946  S  SD  . MET   A 1 135 ? -48.77800 7.16800   8.07700   1.000 16.65000  ? 564  MET   A SD  1 
ATOM   947  C  CE  . MET   A 1 135 ? -49.79000 7.62000   6.64200   1.000 18.13000  ? 564  MET   A CE  1 
ATOM   948  N  N   . ASP   A 1 136 ? -49.17000 1.68000   6.93700   1.000 17.45000  ? 565  ASP   A N   1 
ATOM   949  C  CA  . ASP   A 1 136 ? -49.93400 0.55300   6.39900   1.000 18.21000  ? 565  ASP   A CA  1 
ATOM   950  C  C   . ASP   A 1 136 ? -50.96000 0.08400   7.40500   1.000 20.90000  ? 565  ASP   A C   1 
ATOM   951  O  O   . ASP   A 1 136 ? -52.09600 -0.23700  7.04300   1.000 17.58000  ? 565  ASP   A O   1 
ATOM   952  C  CB  . ASP   A 1 136 ? -48.94200 -0.55900  6.05800   1.000 15.17000  ? 565  ASP   A CB  1 
ATOM   953  C  CG  . ASP   A 1 136 ? -49.62700 -1.86100  5.62800   1.000 29.54000  ? 565  ASP   A CG  1 
ATOM   954  O  OD1 . ASP   A 1 136 ? -50.26500 -1.86500  4.59200   1.000 27.97000  ? 565  ASP   A OD1 1 
ATOM   955  O  OD2 . ASP   A 1 136 ? -49.51600 -2.83500  6.36500   1.000 34.73000  ? 565  ASP   A OD2 1 
ATOM   956  N  N   . TYR   A 1 137 ? -50.56900 0.07400   8.69100   1.000 14.94000  ? 566  TYR   A N   1 
ATOM   957  C  CA  . TYR   A 1 137 ? -51.49300 -0.29300  9.75200   1.000 12.70000  ? 566  TYR   A CA  1 
ATOM   958  C  C   . TYR   A 1 137 ? -52.61900 0.70900   9.85200   1.000 13.89000  ? 566  TYR   A C   1 
ATOM   959  O  O   . TYR   A 1 137 ? -53.79900 0.34000   9.98600   1.000 17.71000  ? 566  TYR   A O   1 
ATOM   960  C  CB  . TYR   A 1 137 ? -50.70500 -0.39200  11.07000  1.000 13.56000  ? 566  TYR   A CB  1 
ATOM   961  C  CG  . TYR   A 1 137 ? -51.59800 -0.70000  12.23900  1.000 15.38000  ? 566  TYR   A CG  1 
ATOM   962  C  CD1 . TYR   A 1 137 ? -51.98800 -2.03600  12.56100  1.000 14.57000  ? 566  TYR   A CD1 1 
ATOM   963  C  CD2 . TYR   A 1 137 ? -52.10600 0.31500   13.02100  1.000 15.63000  ? 566  TYR   A CD2 1 
ATOM   964  C  CE1 . TYR   A 1 137 ? -52.81100 -2.31200  13.60700  1.000 14.34000  ? 566  TYR   A CE1 1 
ATOM   965  C  CE2 . TYR   A 1 137 ? -52.96300 0.03300   14.06800  1.000 15.22000  ? 566  TYR   A CE2 1 
ATOM   966  C  CZ  . TYR   A 1 137 ? -53.30500 -1.27700  14.39900  1.000 13.20000  ? 566  TYR   A CZ  1 
ATOM   967  O  OH  . TYR   A 1 137 ? -54.15100 -1.51900  15.46800  1.000 15.98000  ? 566  TYR   A OH  1 
ATOM   968  N  N   . LEU   A 1 138 ? -52.28900 2.01800   9.84200   1.000 17.16000  ? 567  LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 138 ? -53.37400 2.99300   9.92400   1.000 16.30000  ? 567  LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 138 ? -54.35100 2.80300   8.77600   1.000 13.13000  ? 567  LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 138 ? -55.57900 2.77600   8.97900   1.000 16.44000  ? 567  LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 138 ? -52.82400 4.44800   9.89800   1.000 14.89000  ? 567  LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 138 ? -52.07500 4.90000   11.14300  1.000 16.53000  ? 567  LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 138 ? -51.56500 6.36100   10.97400  1.000 16.70000  ? 567  LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 138 ? -52.95600 4.75400   12.43600  1.000 18.76000  ? 567  LEU   A CD2 1 
ATOM   976  N  N   . HIS   A 1 139 ? -53.83100 2.65800   7.55800   1.000 16.57000  ? 568  HIS   A N   1 
ATOM   977  C  CA  . HIS   A 1 139 ? -54.73300 2.55100   6.43000   1.000 16.02000  ? 568  HIS   A CA  1 
ATOM   978  C  C   . HIS   A 1 139 ? -55.51400 1.27100   6.48600   1.000 16.86000  ? 568  HIS   A C   1 
ATOM   979  O  O   . HIS   A 1 139 ? -56.69700 1.24600   6.10600   1.000 18.41000  ? 568  HIS   A O   1 
ATOM   980  C  CB  . HIS   A 1 139 ? -53.94800 2.64500   5.13300   1.000 15.21000  ? 568  HIS   A CB  1 
ATOM   981  C  CG  . HIS   A 1 139 ? -53.48800 4.04100   4.84400   1.000 16.69000  ? 568  HIS   A CG  1 
ATOM   982  N  ND1 . HIS   A 1 139 ? -52.86200 4.38800   3.66200   1.000 16.43000  ? 568  HIS   A ND1 1 
ATOM   983  C  CD2 . HIS   A 1 139 ? -53.54300 5.17400   5.60200   1.000 17.01000  ? 568  HIS   A CD2 1 
ATOM   984  C  CE1 . HIS   A 1 139 ? -52.57100 5.68500   3.70100   1.000 17.82000  ? 568  HIS   A CE1 1 
ATOM   985  N  NE2 . HIS   A 1 139 ? -52.93400 6.17300   4.87900   1.000 16.31000  ? 568  HIS   A NE2 1 
ATOM   986  N  N   . ALA   A 1 140 ? -54.91500 0.22200   7.06800   1.000 16.49000  ? 569  ALA   A N   1 
ATOM   987  C  CA  . ALA   A 1 140 ? -55.68800 -1.01300  7.19700   1.000 19.00000  ? 569  ALA   A CA  1 
ATOM   988  C  C   . ALA   A 1 140 ? -56.83800 -0.85800  8.17000   1.000 22.73000  ? 569  ALA   A C   1 
ATOM   989  O  O   . ALA   A 1 140 ? -57.80800 -1.62000  8.09900   1.000 21.44000  ? 569  ALA   A O   1 
ATOM   990  C  CB  . ALA   A 1 140 ? -54.75700 -2.16400  7.64500   1.000 17.41000  ? 569  ALA   A CB  1 
ATOM   991  N  N   . LYS   A 1 141 ? -56.72900 0.07300   9.11800   1.000 20.40000  ? 570  LYS   A N   1 
ATOM   992  C  CA  . LYS   A 1 141 ? -57.80200 0.39800   10.06000  1.000 21.38000  ? 570  LYS   A CA  1 
ATOM   993  C  C   . LYS   A 1 141 ? -58.68300 1.53100   9.50800   1.000 25.15000  ? 570  LYS   A C   1 
ATOM   994  O  O   . LYS   A 1 141 ? -59.50200 2.10100   10.24100  1.000 25.14000  ? 570  LYS   A O   1 
ATOM   995  C  CB  . LYS   A 1 141 ? -57.20700 0.81700   11.41600  1.000 22.80000  ? 570  LYS   A CB  1 
ATOM   996  C  CG  . LYS   A 1 141 ? -56.43400 -0.31000  12.17400  1.000 26.57000  ? 570  LYS   A CG  1 
ATOM   997  C  CD  . LYS   A 1 141 ? -57.43700 -1.21800  12.81200  1.000 20.95000  ? 570  LYS   A CD  1 
ATOM   998  C  CE  . LYS   A 1 141 ? -56.75900 -2.27300  13.70300  1.000 31.88000  ? 570  LYS   A CE  1 
ATOM   999  N  NZ  . LYS   A 1 141 ? -57.75000 -3.19500  14.27800  1.000 31.90000  ? 570  LYS   A NZ  1 
ATOM   1000 N  N   . SER   A 1 142 ? -58.50000 1.86600   8.23000   1.000 19.63000  ? 571  SER   A N   1 
ATOM   1001 C  CA  . SER   A 1 142 ? -59.28900 2.89600   7.53400   1.000 20.99000  ? 571  SER   A CA  1 
ATOM   1002 C  C   . SER   A 1 142 ? -59.08800 4.28200   8.15100   1.000 25.41000  ? 571  SER   A C   1 
ATOM   1003 O  O   . SER   A 1 142 ? -60.00900 5.10500   8.15300   1.000 26.37000  ? 571  SER   A O   1 
ATOM   1004 C  CB  . SER   A 1 142 ? -60.78900 2.55500   7.53700   1.000 33.30000  ? 571  SER   A CB  1 
ATOM   1005 O  OG  . SER   A 1 142 ? -61.01500 1.36300   6.80400   1.000 29.75000  ? 571  SER   A OG  1 
ATOM   1006 N  N   . ILE   A 1 143 ? -57.89900 4.56800   8.68300   1.000 17.61000  ? 572  ILE   A N   1 
ATOM   1007 C  CA  . ILE   A 1 143 ? -57.59100 5.88500   9.23500   1.000 16.75000  ? 572  ILE   A CA  1 
ATOM   1008 C  C   . ILE   A 1 143 ? -56.71100 6.62400   8.24300   1.000 17.82000  ? 572  ILE   A C   1 
ATOM   1009 O  O   . ILE   A 1 143 ? -55.58600 6.18000   7.96600   1.000 17.68000  ? 572  ILE   A O   1 
ATOM   1010 C  CB  . ILE   A 1 143 ? -56.87100 5.76700   10.60100  1.000 18.33000  ? 572  ILE   A CB  1 
ATOM   1011 C  CG1 . ILE   A 1 143 ? -57.82100 5.16200   11.65300  1.000 21.97000  ? 572  ILE   A CG1 1 
ATOM   1012 C  CG2 . ILE   A 1 143 ? -56.32100 7.12600   11.05400  1.000 19.84000  ? 572  ILE   A CG2 1 
ATOM   1013 C  CD1 . ILE   A 1 143 ? -57.07500 4.77700   12.93400  1.000 21.29000  ? 572  ILE   A CD1 1 
ATOM   1014 N  N   . ILE   A 1 144 ? -57.18300 7.79700   7.73900   1.000 15.75000  ? 573  ILE   A N   1 
ATOM   1015 C  CA  . ILE   A 1 144 ? -56.31400 8.70600   6.97500   1.000 17.42000  ? 573  ILE   A CA  1 
ATOM   1016 C  C   . ILE   A 1 144 ? -55.61200 9.61400   7.99000   1.000 16.47000  ? 573  ILE   A C   1 
ATOM   1017 O  O   . ILE   A 1 144 ? -56.27100 10.23100  8.83300   1.000 16.96000  ? 573  ILE   A O   1 
ATOM   1018 C  CB  . ILE   A 1 144 ? -57.13100 9.55500   5.98300   1.000 15.87000  ? 573  ILE   A CB  1 
ATOM   1019 C  CG1 . ILE   A 1 144 ? -57.87800 8.67400   4.96900   1.000 20.16000  ? 573  ILE   A CG1 1 
ATOM   1020 C  CG2 . ILE   A 1 144 ? -56.23600 10.58900  5.26800   1.000 16.87000  ? 573  ILE   A CG2 1 
ATOM   1021 C  CD1 . ILE   A 1 144 ? -59.09500 9.40500   4.28300   1.000 19.66000  ? 573  ILE   A CD1 1 
ATOM   1022 N  N   . HIS   A 1 145 ? -54.30800 9.68600   7.90800   1.000 14.94000  ? 574  HIS   A N   1 
ATOM   1023 C  CA  . HIS   A 1 145 ? -53.53200 10.40300  8.91100   1.000 16.30000  ? 574  HIS   A CA  1 
ATOM   1024 C  C   . HIS   A 1 145 ? -53.82500 11.88200  8.82400   1.000 17.31000  ? 574  HIS   A C   1 
ATOM   1025 O  O   . HIS   A 1 145 ? -54.19600 12.52400  9.82600   1.000 17.02000  ? 574  HIS   A O   1 
ATOM   1026 C  CB  . HIS   A 1 145 ? -52.04000 10.12100  8.70200   1.000 15.36000  ? 574  HIS   A CB  1 
ATOM   1027 C  CG  . HIS   A 1 145 ? -51.17000 10.68100  9.77700   1.000 14.84000  ? 574  HIS   A CG  1 
ATOM   1028 N  ND1 . HIS   A 1 145 ? -51.10700 12.03900  10.05600  1.000 16.22000  ? 574  HIS   A ND1 1 
ATOM   1029 C  CD2 . HIS   A 1 145 ? -50.30600 10.08000  10.63900  1.000 12.35000  ? 574  HIS   A CD2 1 
ATOM   1030 C  CE1 . HIS   A 1 145 ? -50.23400 12.24600  11.04300  1.000 15.74000  ? 574  HIS   A CE1 1 
ATOM   1031 N  NE2 . HIS   A 1 145 ? -49.73300 11.07400  11.41900  1.000 16.26000  ? 574  HIS   A NE2 1 
ATOM   1032 N  N   . ARG   A 1 146 ? -53.67700 12.43300  7.61900   1.000 14.24000  ? 575  ARG   A N   1 
ATOM   1033 C  CA  . ARG   A 1 146 ? -53.97200 13.83200  7.23000   1.000 13.95000  ? 575  ARG   A CA  1 
ATOM   1034 C  C   . ARG   A 1 146 ? -52.87300 14.81500  7.55300   1.000 18.14000  ? 575  ARG   A C   1 
ATOM   1035 O  O   . ARG   A 1 146 ? -52.93500 15.96700  7.06300   1.000 21.68000  ? 575  ARG   A O   1 
ATOM   1036 C  CB  . ARG   A 1 146 ? -55.28000 14.37900  7.84600   1.000 15.80000  ? 575  ARG   A CB  1 
ATOM   1037 C  CG  . ARG   A 1 146 ? -56.50900 13.58600  7.49700   1.000 19.29000  ? 575  ARG   A CG  1 
ATOM   1038 C  CD  . ARG   A 1 146 ? -57.78100 14.03100  8.27500   1.000 26.28000  ? 575  ARG   A CD  1 
ATOM   1039 N  NE  . ARG   A 1 146 ? -58.06200 15.46300  8.16600   1.000 33.71000  ? 575  ARG   A NE  1 
ATOM   1040 C  CZ  . ARG   A 1 146 ? -58.95500 16.00900  7.34300   1.000 43.13000  ? 575  ARG   A CZ  1 
ATOM   1041 N  NH1 . ARG   A 1 146 ? -59.70600 15.25900  6.53600   1.000 38.30000  ? 575  ARG   A NH1 1 
ATOM   1042 N  NH2 . ARG   A 1 146 ? -59.08900 17.34000  7.32100   1.000 33.95000  ? 575  ARG   A NH2 1 
ATOM   1043 N  N   . ASP   A 1 147 ? -51.87200 14.46900  8.36100   1.000 14.30000  ? 576  ASP   A N   1 
ATOM   1044 C  CA  . ASP   A 1 147 ? -50.81600 15.44700  8.65800   1.000 19.33000  ? 576  ASP   A CA  1 
ATOM   1045 C  C   . ASP   A 1 147 ? -49.49700 14.75100  8.96100   1.000 17.86000  ? 576  ASP   A C   1 
ATOM   1046 O  O   . ASP   A 1 147 ? -48.80300 15.10000  9.91800   1.000 19.63000  ? 576  ASP   A O   1 
ATOM   1047 C  CB  . ASP   A 1 147 ? -51.23700 16.38400  9.80800   1.000 22.10000  ? 576  ASP   A CB  1 
ATOM   1048 C  CG  . ASP   A 1 147 ? -50.41300 17.65300  9.83700   1.000 28.64000  ? 576  ASP   A CG  1 
ATOM   1049 O  OD1 . ASP   A 1 147 ? -49.70700 17.96100  8.84900   1.000 24.33000  ? 576  ASP   A OD1 1 
ATOM   1050 O  OD2 . ASP   A 1 147 ? -50.44700 18.29600  10.87400  1.000 30.49000  ? 576  ASP   A OD2 1 
ATOM   1051 N  N   . LEU   A 1 148 ? -49.14400 13.73000  8.16100   1.000 16.29000  ? 577  LEU   A N   1 
ATOM   1052 C  CA  . LEU   A 1 148 ? -47.87700 13.03800  8.38200   1.000 15.92000  ? 577  LEU   A CA  1 
ATOM   1053 C  C   . LEU   A 1 148 ? -46.72700 13.97400  8.05800   1.000 19.11000  ? 577  LEU   A C   1 
ATOM   1054 O  O   . LEU   A 1 148 ? -46.71200 14.59300  6.98200   1.000 18.77000  ? 577  LEU   A O   1 
ATOM   1055 C  CB  . LEU   A 1 148 ? -47.79300 11.77600  7.50200   1.000 14.24000  ? 577  LEU   A CB  1 
ATOM   1056 C  CG  . LEU   A 1 148 ? -46.48400 11.01700  7.70300   1.000 15.34000  ? 577  LEU   A CG  1 
ATOM   1057 C  CD1 . LEU   A 1 148 ? -46.43300 10.36300  9.08800   1.000 17.96000  ? 577  LEU   A CD1 1 
ATOM   1058 C  CD2 . LEU   A 1 148 ? -46.34500 9.90700   6.58900   1.000 18.15000  ? 577  LEU   A CD2 1 
ATOM   1059 N  N   . LYS   A 1 149 ? -45.78400 14.10300  8.99200   1.000 16.97000  ? 578  LYS   A N   1 
ATOM   1060 C  CA  . LYS   A 1 149 ? -44.59900 14.91000  8.72900   1.000 20.13000  ? 578  LYS   A CA  1 
ATOM   1061 C  C   . LYS   A 1 149 ? -43.55300 14.56600  9.76000   1.000 20.01000  ? 578  LYS   A C   1 
ATOM   1062 O  O   . LYS   A 1 149 ? -43.85400 13.98000  10.80600  1.000 22.86000  ? 578  LYS   A O   1 
ATOM   1063 C  CB  . LYS   A 1 149 ? -44.92700 16.42600  8.75700   1.000 23.33000  ? 578  LYS   A CB  1 
ATOM   1064 C  CG  . LYS   A 1 149 ? -45.53700 16.91700  10.00900  1.000 23.44000  ? 578  LYS   A CG  1 
ATOM   1065 C  CD  . LYS   A 1 149 ? -46.05900 18.41100  9.81100   1.000 24.21000  ? 578  LYS   A CD  1 
ATOM   1066 C  CE  . LYS   A 1 149 ? -46.67400 18.88600  11.13600  1.000 28.17000  ? 578  LYS   A CE  1 
ATOM   1067 N  NZ  . LYS   A 1 149 ? -47.89100 19.69100  11.02600  1.000 36.37000  ? 578  LYS   A NZ  1 
ATOM   1068 N  N   . SER   A 1 150 ? -42.31400 14.96400  9.48100   1.000 19.51000  ? 579  SER   A N   1 
ATOM   1069 C  CA  . SER   A 1 150 ? -41.23700 14.42800  10.29200  1.000 14.78000  ? 579  SER   A CA  1 
ATOM   1070 C  C   . SER   A 1 150 ? -41.27200 14.92700  11.72100  1.000 14.63000  ? 579  SER   A C   1 
ATOM   1071 O  O   . SER   A 1 150 ? -40.66800 14.27900  12.60700  1.000 18.18000  ? 579  SER   A O   1 
ATOM   1072 C  CB  . SER   A 1 150 ? -39.89700 14.73000  9.59200   1.000 21.18000  ? 579  SER   A CB  1 
ATOM   1073 O  OG  . SER   A 1 150 ? -39.66200 16.14600  9.55200   1.000 18.32000  ? 579  SER   A OG  1 
ATOM   1074 N  N   . ASN   A 1 151 ? -41.93900 16.06600  12.03200  1.000 16.45000  ? 580  ASN   A N   1 
ATOM   1075 C  CA  . ASN   A 1 151 ? -41.81200 16.37300  13.44200  1.000 17.55000  ? 580  ASN   A CA  1 
ATOM   1076 C  C   . ASN   A 1 151 ? -42.85400 15.65000  14.27800  1.000 18.83000  ? 580  ASN   A C   1 
ATOM   1077 O  O   . ASN   A 1 151 ? -42.84500 15.84200  15.49400  1.000 22.54000  ? 580  ASN   A O   1 
ATOM   1078 C  CB  . ASN   A 1 151 ? -41.95200 17.84200  13.83700  1.000 28.04000  ? 580  ASN   A CB  1 
ATOM   1079 C  CG  . ASN   A 1 151 ? -42.94700 18.51000  13.07400  1.000 42.70000  ? 580  ASN   A CG  1 
ATOM   1080 O  OD1 . ASN   A 1 151 ? -44.08600 18.04600  13.04500  1.000 35.12000  ? 580  ASN   A OD1 1 
ATOM   1081 N  ND2 . ASN   A 1 151 ? -42.58000 19.60800  12.42000  1.000 49.97000  ? 580  ASN   A ND2 1 
ATOM   1082 N  N   . ASN   A 1 152 ? -43.70700 14.81600  13.68100  1.000 18.18000  ? 581  ASN   A N   1 
ATOM   1083 C  CA  . ASN   A 1 152 ? -44.55100 13.95800  14.51500  1.000 18.62000  ? 581  ASN   A CA  1 
ATOM   1084 C  C   . ASN   A 1 152 ? -44.32400 12.48500  14.19700  1.000 17.10000  ? 581  ASN   A C   1 
ATOM   1085 O  O   . ASN   A 1 152 ? -45.22300 11.62900  14.33300  1.000 19.14000  ? 581  ASN   A O   1 
ATOM   1086 C  CB  . ASN   A 1 152 ? -46.01500 14.40700  14.42500  1.000 26.75000  ? 581  ASN   A CB  1 
ATOM   1087 C  CG  . ASN   A 1 152 ? -46.23400 15.74900  15.24800  1.000 36.38000  ? 581  ASN   A CG  1 
ATOM   1088 O  OD1 . ASN   A 1 152 ? -46.00100 15.80400  16.49600  1.000 29.16000  ? 581  ASN   A OD1 1 
ATOM   1089 N  ND2 . ASN   A 1 152 ? -46.60700 16.81300  14.56100  1.000 34.11000  ? 581  ASN   A ND2 1 
ATOM   1090 N  N   . ILE   A 1 153 ? -43.08300 12.18400  13.84100  1.000 16.09000  ? 582  ILE   A N   1 
ATOM   1091 C  CA  . ILE   A 1 153 ? -42.55600 10.82400  13.78100  1.000 15.56000  ? 582  ILE   A CA  1 
ATOM   1092 C  C   . ILE   A 1 153 ? -41.42200 10.75600  14.78500  1.000 15.80000  ? 582  ILE   A C   1 
ATOM   1093 O  O   . ILE   A 1 153 ? -40.43800 11.48300  14.63700  1.000 18.10000  ? 582  ILE   A O   1 
ATOM   1094 C  CB  . ILE   A 1 153 ? -42.05900 10.45900  12.37000  1.000 18.33000  ? 582  ILE   A CB  1 
ATOM   1095 C  CG1 . ILE   A 1 153 ? -43.19300 10.54800  11.30700  1.000 16.19000  ? 582  ILE   A CG1 1 
ATOM   1096 C  CG2 . ILE   A 1 153 ? -41.44000 9.03100   12.43500  1.000 18.82000  ? 582  ILE   A CG2 1 
ATOM   1097 C  CD1 . ILE   A 1 153 ? -42.68900 10.44900  9.86100   1.000 18.53000  ? 582  ILE   A CD1 1 
ATOM   1098 N  N   . PHE   A 1 154 ? -41.55900 9.92800   15.83800  1.000 13.27000  ? 583  PHE   A N   1 
ATOM   1099 C  CA  . PHE   A 1 154 ? -40.58100 9.92200   16.93500  1.000 16.86000  ? 583  PHE   A CA  1 
ATOM   1100 C  C   . PHE   A 1 154 ? -39.71000 8.67400   16.88800  1.000 18.88000  ? 583  PHE   A C   1 
ATOM   1101 O  O   . PHE   A 1 154 ? -40.22300 7.59000   16.59100  1.000 18.60000  ? 583  PHE   A O   1 
ATOM   1102 C  CB  . PHE   A 1 154 ? -41.31400 9.99300   18.29800  1.000 17.76000  ? 583  PHE   A CB  1 
ATOM   1103 C  CG  . PHE   A 1 154 ? -42.20800 11.21000  18.38000  1.000 15.40000  ? 583  PHE   A CG  1 
ATOM   1104 C  CD1 . PHE   A 1 154 ? -41.63700 12.44900  18.68500  1.000 18.76000  ? 583  PHE   A CD1 1 
ATOM   1105 C  CD2 . PHE   A 1 154 ? -43.56800 11.10900  18.10200  1.000 16.47000  ? 583  PHE   A CD2 1 
ATOM   1106 C  CE1 . PHE   A 1 154 ? -42.49000 13.59700  18.70400  1.000 17.92000  ? 583  PHE   A CE1 1 
ATOM   1107 C  CE2 . PHE   A 1 154 ? -44.40900 12.24000  18.13200  1.000 19.17000  ? 583  PHE   A CE2 1 
ATOM   1108 C  CZ  . PHE   A 1 154 ? -43.83100 13.47700  18.41300  1.000 17.66000  ? 583  PHE   A CZ  1 
ATOM   1109 N  N   . LEU   A 1 155 ? -38.40900 8.81700   17.19300  1.000 18.18000  ? 584  LEU   A N   1 
ATOM   1110 C  CA  . LEU   A 1 155 ? -37.50300 7.65000   17.18500  1.000 17.87000  ? 584  LEU   A CA  1 
ATOM   1111 C  C   . LEU   A 1 155 ? -37.27100 7.19700   18.62100  1.000 17.39000  ? 584  LEU   A C   1 
ATOM   1112 O  O   . LEU   A 1 155 ? -36.35600 7.67000   19.30800  1.000 20.85000  ? 584  LEU   A O   1 
ATOM   1113 C  CB  . LEU   A 1 155 ? -36.19000 7.97700   16.46200  1.000 20.66000  ? 584  LEU   A CB  1 
ATOM   1114 C  CG  . LEU   A 1 155 ? -35.32900 6.72400   16.19200  1.000 27.61000  ? 584  LEU   A CG  1 
ATOM   1115 C  CD1 . LEU   A 1 155 ? -36.07600 5.63200   15.35100  1.000 24.23000  ? 584  LEU   A CD1 1 
ATOM   1116 C  CD2 . LEU   A 1 155 ? -33.97500 7.20400   15.56500  1.000 30.58000  ? 584  LEU   A CD2 1 
ATOM   1117 N  N   . HIS   A 1 156 ? -38.15800 6.32100   19.11900  1.000 17.22000  ? 585  HIS   A N   1 
ATOM   1118 C  CA  . HIS   A 1 156 ? -38.13300 5.91500   20.51800  1.000 16.57000  ? 585  HIS   A CA  1 
ATOM   1119 C  C   . HIS   A 1 156 ? -36.94500 5.00300   20.81300  1.000 24.54000  ? 585  HIS   A C   1 
ATOM   1120 O  O   . HIS   A 1 156 ? -36.74500 3.97100   20.13800  1.000 19.59000  ? 585  HIS   A O   1 
ATOM   1121 C  CB  . HIS   A 1 156 ? -39.45000 5.21000   20.86400  1.000 16.54000  ? 585  HIS   A CB  1 
ATOM   1122 C  CG  . HIS   A 1 156 ? -39.53100 4.69700   22.27200  1.000 19.56000  ? 585  HIS   A CG  1 
ATOM   1123 N  ND1 . HIS   A 1 156 ? -39.39800 5.50100   23.40000  1.000 18.09000  ? 585  HIS   A ND1 1 
ATOM   1124 C  CD2 . HIS   A 1 156 ? -39.74100 3.44200   22.73200  1.000 21.54000  ? 585  HIS   A CD2 1 
ATOM   1125 C  CE1 . HIS   A 1 156 ? -39.52200 4.74900   24.48500  1.000 22.08000  ? 585  HIS   A CE1 1 
ATOM   1126 N  NE2 . HIS   A 1 156 ? -39.74400 3.50200   24.10900  1.000 22.10000  ? 585  HIS   A NE2 1 
ATOM   1127 N  N   . GLU   A 1 157 ? -36.17100 5.38800   21.84000  1.000 21.31000  ? 586  GLU   A N   1 
ATOM   1128 C  CA  . GLU   A 1 157 ? -34.94900 4.65100   22.26500  1.000 19.55000  ? 586  GLU   A CA  1 
ATOM   1129 C  C   . GLU   A 1 157 ? -33.96300 4.53000   21.12400  1.000 23.18000  ? 586  GLU   A C   1 
ATOM   1130 O  O   . GLU   A 1 157 ? -33.25400 3.53500   21.02400  1.000 30.08000  ? 586  GLU   A O   1 
ATOM   1131 C  CB  . GLU   A 1 157 ? -35.29700 3.25900   22.81300  1.000 25.18000  ? 586  GLU   A CB  1 
ATOM   1132 C  CG  . GLU   A 1 157 ? -36.18000 3.31500   24.08800  1.000 23.55000  ? 586  GLU   A CG  1 
ATOM   1133 C  CD  . GLU   A 1 157 ? -35.48800 3.86900   25.34800  1.000 46.31000  ? 586  GLU   A CD  1 
ATOM   1134 O  OE1 . GLU   A 1 157 ? -34.31100 4.24200   25.29400  1.000 36.21000  ? 586  GLU   A OE1 1 
ATOM   1135 O  OE2 . GLU   A 1 157 ? -36.12800 3.91400   26.41800  1.000 42.52000  ? 586  GLU   A OE2 1 
ATOM   1136 N  N   . ASP   A 1 158 ? -33.98700 5.51700   20.22300  1.000 24.15000  ? 587  ASP   A N   1 
ATOM   1137 C  CA  . ASP   A 1 158 ? -33.21400 5.55000   18.98000  1.000 24.22000  ? 587  ASP   A CA  1 
ATOM   1138 C  C   . ASP   A 1 158 ? -33.44500 4.33700   18.09400  1.000 28.20000  ? 587  ASP   A C   1 
ATOM   1139 O  O   . ASP   A 1 158 ? -32.63800 4.07600   17.20600  1.000 29.56000  ? 587  ASP   A O   1 
ATOM   1140 C  CB  . ASP   A 1 158 ? -31.70700 5.72100   19.23500  1.000 32.79000  ? 587  ASP   A CB  1 
ATOM   1141 C  CG  . ASP   A 1 158 ? -31.38000 7.02800   19.97400  1.000 58.21000  ? 587  ASP   A CG  1 
ATOM   1142 O  OD1 . ASP   A 1 158 ? -32.15000 8.02100   19.85000  1.000 47.77000  ? 587  ASP   A OD1 1 
ATOM   1143 O  OD2 . ASP   A 1 158 ? -30.36400 7.05400   20.70100  1.000 70.61000  ? 587  ASP   A OD2 1 
ATOM   1144 N  N   . LEU   A 1 159 ? -34.55000 3.59800   18.28300  1.000 22.81000  ? 588  LEU   A N   1 
ATOM   1145 C  CA  . LEU   A 1 159 ? -34.75000 2.33700   17.56100  1.000 24.73000  ? 588  LEU   A CA  1 
ATOM   1146 C  C   . LEU   A 1 159 ? -36.10300 2.21900   16.87700  1.000 27.65000  ? 588  LEU   A C   1 
ATOM   1147 O  O   . LEU   A 1 159 ? -36.17600 1.71200   15.75800  1.000 24.11000  ? 588  LEU   A O   1 
ATOM   1148 C  CB  . LEU   A 1 159 ? -34.63800 1.13000   18.49000  1.000 27.93000  ? 588  LEU   A CB  1 
ATOM   1149 C  CG  . LEU   A 1 159 ? -33.43500 0.93200   19.41400  1.000 50.59000  ? 588  LEU   A CG  1 
ATOM   1150 C  CD1 . LEU   A 1 159 ? -33.77300 0.00500   20.59100  1.000 50.10000  ? 588  LEU   A CD1 1 
ATOM   1151 C  CD2 . LEU   A 1 159 ? -32.27700 0.38600   18.62100  1.000 51.39000  ? 588  LEU   A CD2 1 
ATOM   1152 N  N   . THR   A 1 160 ? -37.18200 2.59200   17.54600  1.000 17.41000  ? 589  THR   A N   1 
ATOM   1153 C  CA  . THR   A 1 160 ? -38.52400 2.21400   17.09700  1.000 13.88000  ? 589  THR   A CA  1 
ATOM   1154 C  C   . THR   A 1 160 ? -39.26300 3.46900   16.70700  1.000 16.28000  ? 589  THR   A C   1 
ATOM   1155 O  O   . THR   A 1 160 ? -39.41300 4.37500   17.55000  1.000 17.42000  ? 589  THR   A O   1 
ATOM   1156 C  CB  . THR   A 1 160 ? -39.31000 1.48900   18.18900  1.000 17.26000  ? 589  THR   A CB  1 
ATOM   1157 O  OG1 . THR   A 1 160 ? -38.55800 0.30400   18.60300  1.000 21.31000  ? 589  THR   A OG1 1 
ATOM   1158 C  CG2 . THR   A 1 160 ? -40.67800 1.08400   17.66400  1.000 18.32000  ? 589  THR   A CG2 1 
ATOM   1159 N  N   . VAL   A 1 161 ? -39.74300 3.49500   15.46600  1.000 15.44000  ? 590  VAL   A N   1 
ATOM   1160 C  CA  . VAL   A 1 161 ? -40.50800 4.64900   14.95800  1.000 14.63000  ? 590  VAL   A CA  1 
ATOM   1161 C  C   . VAL   A 1 161 ? -41.87700 4.64900   15.60700  1.000 15.51000  ? 590  VAL   A C   1 
ATOM   1162 O  O   . VAL   A 1 161 ? -42.56200 3.62700   15.62200  1.000 17.37000  ? 590  VAL   A O   1 
ATOM   1163 C  CB  . VAL   A 1 161 ? -40.65500 4.54800   13.43900  1.000 12.79000  ? 590  VAL   A CB  1 
ATOM   1164 C  CG1 . VAL   A 1 161 ? -41.82100 5.46600   12.89700  1.000 16.11000  ? 590  VAL   A CG1 1 
ATOM   1165 C  CG2 . VAL   A 1 161 ? -39.28300 4.87700   12.76300  1.000 17.39000  ? 590  VAL   A CG2 1 
ATOM   1166 N  N   . LYS   A 1 162 ? -42.33300 5.81900   16.06900  1.000 14.56000  ? 591  LYS   A N   1 
ATOM   1167 C  CA  . LYS   A 1 162 ? -43.71400 5.96000   16.53400  1.000 14.66000  ? 591  LYS   A CA  1 
ATOM   1168 C  C   . LYS   A 1 162 ? -44.37200 7.10800   15.80100  1.000 16.51000  ? 591  LYS   A C   1 
ATOM   1169 O  O   . LYS   A 1 162 ? -43.94500 8.25500   15.97300  1.000 15.05000  ? 591  LYS   A O   1 
ATOM   1170 C  CB  . LYS   A 1 162 ? -43.79500 6.32000   18.03000  1.000 15.81000  ? 591  LYS   A CB  1 
ATOM   1171 C  CG  . LYS   A 1 162 ? -42.91200 5.46500   18.92600  1.000 20.62000  ? 591  LYS   A CG  1 
ATOM   1172 C  CD  . LYS   A 1 162 ? -43.59100 4.15600   19.18500  1.000 17.33000  ? 591  LYS   A CD  1 
ATOM   1173 C  CE  . LYS   A 1 162 ? -42.86000 3.29700   20.28000  1.000 16.96000  ? 591  LYS   A CE  1 
ATOM   1174 N  NZ  . LYS   A 1 162 ? -43.54200 1.87300   20.20800  1.000 16.82000  ? 591  LYS   A NZ  1 
ATOM   1175 N  N   . ILE   A 1 163 ? -45.43900 6.84200   15.11800  1.000 14.12000  ? 592  ILE   A N   1 
ATOM   1176 C  CA  . ILE   A 1 163 ? -46.14300 7.89600   14.36100  1.000 12.87000  ? 592  ILE   A CA  1 
ATOM   1177 C  C   . ILE   A 1 163 ? -47.24700 8.47900   15.25800  1.000 14.52000  ? 592  ILE   A C   1 
ATOM   1178 O  O   . ILE   A 1 163 ? -48.08200 7.74600   15.81000  1.000 14.46000  ? 592  ILE   A O   1 
ATOM   1179 C  CB  . ILE   A 1 163 ? -46.75800 7.34200   13.05800  1.000 11.64000  ? 592  ILE   A CB  1 
ATOM   1180 C  CG1 . ILE   A 1 163 ? -45.65400 6.85000   12.10600  1.000 13.18000  ? 592  ILE   A CG1 1 
ATOM   1181 C  CG2 . ILE   A 1 163 ? -47.62700 8.44600   12.39100  1.000 15.74000  ? 592  ILE   A CG2 1 
ATOM   1182 C  CD1 . ILE   A 1 163 ? -46.28700 6.10800   10.88300  1.000 18.31000  ? 592  ILE   A CD1 1 
ATOM   1183 N  N   . GLY   A 1 164 ? -47.27100 9.82000   15.34400  1.000 14.66000  ? 593  GLY   A N   1 
ATOM   1184 C  CA  . GLY   A 1 164 ? -48.33000 10.52800  16.05100  1.000 15.33000  ? 593  GLY   A CA  1 
ATOM   1185 C  C   . GLY   A 1 164 ? -48.98800 11.65900  15.25200  1.000 15.68000  ? 593  GLY   A C   1 
ATOM   1186 O  O   . GLY   A 1 164 ? -48.81300 11.76000  14.03800  1.000 16.37000  ? 593  GLY   A O   1 
ATOM   1187 N  N   . ASP   A 1 165 ? -49.86000 12.39500  15.95900  1.000 13.71000  ? 594  ASP   A N   1 
ATOM   1188 C  CA  . ASP   A 1 165 ? -50.53400 13.60800  15.45100  1.000 13.17000  ? 594  ASP   A CA  1 
ATOM   1189 C  C   . ASP   A 1 165 ? -51.51200 13.31800  14.31600  1.000 18.99000  ? 594  ASP   A C   1 
ATOM   1190 O  O   . ASP   A 1 165 ? -51.69200 14.14400  13.38800  1.000 18.72000  ? 594  ASP   A O   1 
ATOM   1191 C  CB  . ASP   A 1 165 ? -49.48600 14.65700  15.03900  1.000 18.66000  ? 594  ASP   A CB  1 
ATOM   1192 C  CG  . ASP   A 1 165 ? -50.09500 16.06500  14.96900  1.000 26.05000  ? 594  ASP   A CG  1 
ATOM   1193 O  OD1 . ASP   A 1 165 ? -51.07700 16.31700  15.68400  1.000 22.02000  ? 594  ASP   A OD1 1 
ATOM   1194 O  OD2 . ASP   A 1 165 ? -49.62700 16.87200  14.16300  1.000 24.60000  ? 594  ASP   A OD2 1 
ATOM   1195 N  N   . PHE   A 1 166 ? -52.19400 12.16400  14.36800  1.000 15.55000  ? 595  PHE   A N   1 
ATOM   1196 C  CA  . PHE   A 1 166 ? -53.30300 11.90800  13.47800  1.000 14.37000  ? 595  PHE   A CA  1 
ATOM   1197 C  C   . PHE   A 1 166 ? -54.64400 12.09700  14.22400  1.000 18.13000  ? 595  PHE   A C   1 
ATOM   1198 O  O   . PHE   A 1 166 ? -55.71100 12.04300  13.59600  1.000 23.93000  ? 595  PHE   A O   1 
ATOM   1199 C  CB  . PHE   A 1 166 ? -53.18100 10.48500  12.82200  1.000 15.13000  ? 595  PHE   A CB  1 
ATOM   1200 C  CG  . PHE   A 1 166 ? -53.09400 9.35600   13.84900  1.000 14.59000  ? 595  PHE   A CG  1 
ATOM   1201 C  CD1 . PHE   A 1 166 ? -54.24200 8.74300   14.33500  1.000 16.65000  ? 595  PHE   A CD1 1 
ATOM   1202 C  CD2 . PHE   A 1 166 ? -51.82200 8.96300   14.34400  1.000 15.76000  ? 595  PHE   A CD2 1 
ATOM   1203 C  CE1 . PHE   A 1 166 ? -54.11700 7.73700   15.32000  1.000 16.95000  ? 595  PHE   A CE1 1 
ATOM   1204 C  CE2 . PHE   A 1 166 ? -51.70400 8.00300   15.31600  1.000 17.84000  ? 595  PHE   A CE2 1 
ATOM   1205 C  CZ  . PHE   A 1 166 ? -52.83500 7.39200   15.80000  1.000 15.70000  ? 595  PHE   A CZ  1 
ATOM   1206 N  N   . GLY   A 1 167 ? -54.61300 12.28500  15.53700  1.000 23.21000  ? 596  GLY   A N   1 
ATOM   1207 C  CA  . GLY   A 1 167 ? -55.84600 12.40900  16.27700  1.000 23.53000  ? 596  GLY   A CA  1 
ATOM   1208 C  C   . GLY   A 1 167 ? -56.52800 13.74400  16.02800  1.000 28.10000  ? 596  GLY   A C   1 
ATOM   1209 O  O   . GLY   A 1 167 ? -55.89100 14.70700  15.59600  1.000 31.51000  ? 596  GLY   A O   1 
ATOM   1210 N  N   . LEU   A 1 168 ? -57.85200 13.76800  16.25500  1.000 35.54000  ? 597  LEU   A N   1 
ATOM   1211 C  CA  . LEU   A 1 168 ? -58.66800 15.00900  16.29300  1.000 30.72000  ? 597  LEU   A CA  1 
ATOM   1212 C  C   . LEU   A 1 168 ? -58.83400 15.70800  14.92300  1.000 40.91000  ? 597  LEU   A C   1 
ATOM   1213 O  O   . LEU   A 1 168 ? -58.68700 16.93200  14.81600  1.000 25.74000  ? 597  LEU   A O   1 
ATOM   1214 C  CB  . LEU   A 1 168 ? -58.12200 15.99700  17.32600  1.000 34.31000  ? 597  LEU   A CB  1 
ATOM   1215 C  CG  . LEU   A 1 168 ? -57.46200 15.47100  18.61200  1.000 39.97000  ? 597  LEU   A CG  1 
ATOM   1216 C  CD1 . LEU   A 1 168 ? -56.78500 16.59200  19.40400  1.000 46.15000  ? 597  LEU   A CD1 1 
ATOM   1217 C  CD2 . LEU   A 1 168 ? -58.56100 14.90200  19.38800  1.000 38.26000  ? 597  LEU   A CD2 1 
ATOM   1218 N  N   . ALA   A 1 169 ? -59.26200 14.95300  13.91100  1.000 37.84000  ? 598  ALA   A N   1 
ATOM   1219 C  CA  . ALA   A 1 169 ? -59.32900 15.48400  12.53500  1.000 29.67000  ? 598  ALA   A CA  1 
ATOM   1220 C  C   . ALA   A 1 169 ? -60.35300 16.60000  12.37300  1.000 32.56000  ? 598  ALA   A C   1 
ATOM   1221 O  O   . ALA   A 1 169 ? -60.05500 17.64700  11.78200  1.000 34.12000  ? 598  ALA   A O   1 
ATOM   1222 C  CB  . ALA   A 1 169 ? -59.66000 14.35800  11.56600  1.000 37.53000  ? 598  ALA   A CB  1 
ATOM   1223 N  N   . THR   A 1 170 ? -61.58500 16.36000  12.80300  1.000 26.61000  ? 599  THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 170 ? -62.63700 17.35400  12.74100  1.000 28.15000  ? 599  THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 170 ? -62.36700 18.48900  13.72200  1.000 30.09000  ? 599  THR   A C   1 
ATOM   1226 O  O   . THR   A 1 170 ? -62.66700 19.65100  13.45300  1.000 25.71000  ? 599  THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 170 ? -63.96600 16.65300  13.06400  1.000 39.57000  ? 599  THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 170 ? -64.37600 15.87100  11.94800  1.000 55.19000  ? 599  THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 170 ? -65.04300 17.61400  13.33800  1.000 31.78000  ? 599  THR   A CG2 1 
ATOM   1230 N  N   . VAL   A 1 171 ? -61.81300 18.17300  14.89000  1.000 20.77000  ? 600  VAL   A N   1 
ATOM   1231 C  CA  . VAL   A 1 171 ? -61.49900 19.22500  15.84600  1.000 19.49000  ? 600  VAL   A CA  1 
ATOM   1232 C  C   . VAL   A 1 171 ? -60.51000 20.19300  15.21200  1.000 24.86000  ? 600  VAL   A C   1 
ATOM   1233 O  O   . VAL   A 1 171 ? -60.71100 21.41600  15.22700  1.000 23.00000  ? 600  VAL   A O   1 
ATOM   1234 C  CB  . VAL   A 1 171 ? -60.93800 18.63000  17.15800  1.000 21.80000  ? 600  VAL   A CB  1 
ATOM   1235 C  CG1 . VAL   A 1 171 ? -60.52800 19.78000  18.09600  1.000 28.30000  ? 600  VAL   A CG1 1 
ATOM   1236 C  CG2 . VAL   A 1 171 ? -61.99900 17.76300  17.81300  1.000 26.45000  ? 600  VAL   A CG2 1 
ATOM   1237 N  N   . LYS   A 1 172 ? -59.45800 19.66200  14.59400  1.000 17.69000  ? 601  LYS   A N   1 
ATOM   1238 C  CA  . LYS   A 1 172 ? -58.41500 20.54500  14.05900  1.000 20.23000  ? 601  LYS   A CA  1 
ATOM   1239 C  C   . LYS   A 1 172 ? -58.89800 21.27500  12.82700  1.000 21.06000  ? 601  LYS   A C   1 
ATOM   1240 O  O   . LYS   A 1 172 ? -58.49100 22.40900  12.57800  1.000 20.66000  ? 601  LYS   A O   1 
ATOM   1241 C  CB  . LYS   A 1 172 ? -57.16400 19.73900  13.68600  1.000 23.67000  ? 601  LYS   A CB  1 
ATOM   1242 C  CG  . LYS   A 1 172 ? -56.30400 19.48600  14.96400  1.000 33.64000  ? 601  LYS   A CG  1 
ATOM   1243 C  CD  . LYS   A 1 172 ? -55.03400 18.70800  14.67000  1.000 42.41000  ? 601  LYS   A CD  1 
ATOM   1244 C  CE  . LYS   A 1 172 ? -54.82400 18.61500  13.21000  1.000 48.92000  ? 601  LYS   A CE  1 
ATOM   1245 N  NZ  . LYS   A 1 172 ? -53.42700 18.22700  12.93900  1.000 58.37000  ? 601  LYS   A NZ  1 
ATOM   1246 N  N   . SER   A 1 173 ? -59.64600 20.59600  11.97500  1.000 18.89000  ? 602  SER   A N   1 
ATOM   1247 C  CA  . SER   A 1 173 ? -59.91400 21.23100  10.67400  1.000 20.76000  ? 602  SER   A CA  1 
ATOM   1248 C  C   . SER   A 1 173 ? -61.20100 22.05200  10.63400  1.000 17.94000  ? 602  SER   A C   1 
ATOM   1249 O  O   . SER   A 1 173 ? -61.27600 22.99200  9.83500   1.000 21.34000  ? 602  SER   A O   1 
ATOM   1250 C  CB  . SER   A 1 173 ? -59.97000 20.17100  9.58200   1.000 22.84000  ? 602  SER   A CB  1 
ATOM   1251 O  OG  . SER   A 1 173 ? -61.08600 19.34700  9.77100   1.000 31.98000  ? 602  SER   A OG  1 
ATOM   1252 N  N   . ARG   A 1 174 ? -62.20600 21.72300  11.45900  1.000 18.15000  ? 603  ARG   A N   1 
ATOM   1253 C  CA  . ARG   A 1 174 ? -63.56200 22.26600  11.32800  1.000 18.67000  ? 603  ARG   A CA  1 
ATOM   1254 C  C   . ARG   A 1 174 ? -63.89600 23.28500  12.40100  1.000 25.26000  ? 603  ARG   A C   1 
ATOM   1255 O  O   . ARG   A 1 174 ? -64.64800 24.21600  12.13000  1.000 23.19000  ? 603  ARG   A O   1 
ATOM   1256 C  CB  . ARG   A 1 174 ? -64.57800 21.12800  11.45400  1.000 22.32000  ? 603  ARG   A CB  1 
ATOM   1257 C  CG  . ARG   A 1 174 ? -64.94200 20.24900  10.29500  1.000 33.96000  ? 603  ARG   A CG  1 
ATOM   1258 C  CD  . ARG   A 1 174 ? -65.10400 20.81000  8.94600   1.000 56.65000  ? 603  ARG   A CD  1 
ATOM   1259 N  NE  . ARG   A 1 174 ? -64.85300 19.71000  8.03100   1.000 69.01000  ? 603  ARG   A NE  1 
ATOM   1260 C  CZ  . ARG   A 1 174 ? -65.26400 19.68600  6.77700   1.000 64.53000  ? 603  ARG   A CZ  1 
ATOM   1261 N  NH1 . ARG   A 1 174 ? -66.17700 20.54300  6.34200   1.000 66.60000  ? 603  ARG   A NH1 1 
ATOM   1262 N  NH2 . ARG   A 1 174 ? -64.84200 18.71200  5.97500   1.000 62.69000  ? 603  ARG   A NH2 1 
ATOM   1263 N  N   . TRP   A 1 175 ? -63.40800 23.12200  13.64600  1.000 19.63000  ? 604  TRP   A N   1 
ATOM   1264 C  CA  . TRP   A 1 175 ? -63.87200 24.02000  14.69500  1.000 19.30000  ? 604  TRP   A CA  1 
ATOM   1265 C  C   . TRP   A 1 175 ? -63.37600 25.43600  14.46000  1.000 20.47000  ? 604  TRP   A C   1 
ATOM   1266 O  O   . TRP   A 1 175 ? -62.21900 25.67100  14.13300  1.000 19.73000  ? 604  TRP   A O   1 
ATOM   1267 C  CB  . TRP   A 1 175 ? -63.38500 23.57900  16.07100  1.000 23.09000  ? 604  TRP   A CB  1 
ATOM   1268 C  CG  . TRP   A 1 175 ? -64.03800 22.31800  16.58900  1.000 20.42000  ? 604  TRP   A CG  1 
ATOM   1269 C  CD1 . TRP   A 1 175 ? -64.88400 21.46500  15.93900  1.000 28.68000  ? 604  TRP   A CD1 1 
ATOM   1270 C  CD2 . TRP   A 1 175 ? -63.82200 21.77800  17.88200  1.000 23.64000  ? 604  TRP   A CD2 1 
ATOM   1271 N  NE1 . TRP   A 1 175 ? -65.21400 20.38600  16.78500  1.000 27.06000  ? 604  TRP   A NE1 1 
ATOM   1272 C  CE2 . TRP   A 1 175 ? -64.56700 20.57900  17.97800  1.000 21.65000  ? 604  TRP   A CE2 1 
ATOM   1273 C  CE3 . TRP   A 1 175 ? -63.06400 22.19800  18.97000  1.000 28.63000  ? 604  TRP   A CE3 1 
ATOM   1274 C  CZ2 . TRP   A 1 175 ? -64.58300 19.80700  19.13800  1.000 25.36000  ? 604  TRP   A CZ2 1 
ATOM   1275 C  CZ3 . TRP   A 1 175 ? -63.06300 21.41600  20.11900  1.000 30.04000  ? 604  TRP   A CZ3 1 
ATOM   1276 C  CH2 . TRP   A 1 175 ? -63.81400 20.23700  20.18100  1.000 24.28000  ? 604  TRP   A CH2 1 
ATOM   1277 N  N   . SER   A 1 176 ? -64.27100 26.39600  14.71200  1.000 21.05000  ? 605  SER   A N   1 
ATOM   1278 C  CA  . SER   A 1 176 ? -63.90300 27.79400  14.66300  1.000 19.62000  ? 605  SER   A CA  1 
ATOM   1279 C  C   . SER   A 1 176 ? -62.77800 28.04200  15.65800  1.000 22.22000  ? 605  SER   A C   1 
ATOM   1280 O  O   . SER   A 1 176 ? -62.84600 27.59100  16.81100  1.000 22.87000  ? 605  SER   A O   1 
ATOM   1281 C  CB  . SER   A 1 176 ? -65.14200 28.65700  15.01700  1.000 23.17000  ? 605  SER   A CB  1 
ATOM   1282 O  OG  . SER   A 1 176 ? -64.73000 29.97300  15.25300  1.000 30.39000  ? 605  SER   A OG  1 
ATOM   1283 N  N   . GLY   A 1 177 ? -61.74900 28.76800  15.22600  1.000 19.45000  ? 606  GLY   A N   1 
ATOM   1284 C  CA  . GLY   A 1 177 ? -60.66100 29.12900  16.13300  1.000 19.17000  ? 606  GLY   A CA  1 
ATOM   1285 C  C   . GLY   A 1 177 ? -59.63100 28.03700  16.37200  1.000 21.83000  ? 606  GLY   A C   1 
ATOM   1286 O  O   . GLY   A 1 177 ? -58.88800 28.10700  17.35600  1.000 20.63000  ? 606  GLY   A O   1 
ATOM   1287 N  N   . SER   A 1 178 ? -59.57900 27.01000  15.52500  1.000 19.30000  ? 607  SER   A N   1 
ATOM   1288 C  CA  . SER   A 1 178 ? -58.59800 25.93400  15.70200  1.000 17.37000  ? 607  SER   A CA  1 
ATOM   1289 C  C   . SER   A 1 178 ? -57.26400 26.20600  15.02000  1.000 16.25000  ? 607  SER   A C   1 
ATOM   1290 O  O   . SER   A 1 178 ? -56.45100 25.26500  14.90200  1.000 18.69000  ? 607  SER   A O   1 
ATOM   1291 C  CB  . SER   A 1 178 ? -59.19400 24.61100  15.22700  1.000 18.69000  ? 607  SER   A CB  1 
ATOM   1292 O  OG  . SER   A 1 178 ? -59.95200 24.00000  16.27100  1.000 20.04000  ? 607  SER   A OG  1 
ATOM   1293 N  N   . HIS   A 1 179 ? -56.95000 27.47900  14.71000  1.000 16.46000  ? 608  HIS   A N   1 
ATOM   1294 C  CA  . HIS   A 1 179 ? -55.64800 27.88800  14.16400  1.000 17.18000  ? 608  HIS   A CA  1 
ATOM   1295 C  C   . HIS   A 1 179 ? -55.35200 27.22800  12.81000  1.000 19.76000  ? 608  HIS   A C   1 
ATOM   1296 O  O   . HIS   A 1 179 ? -54.22700 26.83500  12.52500  1.000 17.34000  ? 608  HIS   A O   1 
ATOM   1297 C  CB  . HIS   A 1 179 ? -54.52400 27.61300  15.20300  1.000 15.89000  ? 608  HIS   A CB  1 
ATOM   1298 C  CG  . HIS   A 1 179 ? -55.01100 27.86900  16.61200  1.000 21.46000  ? 608  HIS   A CG  1 
ATOM   1299 N  ND1 . HIS   A 1 179 ? -55.38000 29.13400  17.03600  1.000 22.73000  ? 608  HIS   A ND1 1 
ATOM   1300 C  CD2 . HIS   A 1 179 ? -55.25700 27.02700  17.66200  1.000 21.64000  ? 608  HIS   A CD2 1 
ATOM   1301 C  CE1 . HIS   A 1 179 ? -55.81900 29.06600  18.28800  1.000 24.41000  ? 608  HIS   A CE1 1 
ATOM   1302 N  NE2 . HIS   A 1 179 ? -55.75000 27.80800  18.69300  1.000 22.54000  ? 608  HIS   A NE2 1 
ATOM   1303 N  N   . GLN   A 1 180 ? -56.36700 27.16700  11.93000  1.000 16.18000  ? 609  GLN   A N   1 
ATOM   1304 C  CA  . GLN   A 1 180 ? -56.21000 26.54600  10.61700  1.000 15.75000  ? 609  GLN   A CA  1 
ATOM   1305 C  C   . GLN   A 1 180 ? -55.18800 27.28500  9.75500   1.000 15.71000  ? 609  GLN   A C   1 
ATOM   1306 O  O   . GLN   A 1 180 ? -54.45700 26.65800  8.96100   1.000 16.09000  ? 609  GLN   A O   1 
ATOM   1307 C  CB  . GLN   A 1 180 ? -57.58500 26.51500  9.91900   1.000 15.41000  ? 609  GLN   A CB  1 
ATOM   1308 C  CG  . GLN   A 1 180 ? -58.53600 25.43700  10.50300  1.000 17.50000  ? 609  GLN   A CG  1 
ATOM   1309 C  CD  . GLN   A 1 180 ? -59.45500 25.95900  11.60500  1.000 18.69000  ? 609  GLN   A CD  1 
ATOM   1310 O  OE1 . GLN   A 1 180 ? -59.07900 26.84100  12.39700  1.000 17.27000  ? 609  GLN   A OE1 1 
ATOM   1311 N  NE2 . GLN   A 1 180 ? -60.64300 25.34400  11.72100  1.000 18.14000  ? 609  GLN   A NE2 1 
ATOM   1312 N  N   . PHE   A 1 181 ? -55.09800 28.60200  9.89500   1.000 15.65000  ? 610  PHE   A N   1 
ATOM   1313 C  CA  . PHE   A 1 181 ? -54.06800 29.33000  9.14600   1.000 15.09000  ? 610  PHE   A CA  1 
ATOM   1314 C  C   . PHE   A 1 181 ? -52.67000 28.89600  9.55400   1.000 19.38000  ? 610  PHE   A C   1 
ATOM   1315 O  O   . PHE   A 1 181 ? -51.81400 28.65400  8.69000   1.000 19.90000  ? 610  PHE   A O   1 
ATOM   1316 C  CB  . PHE   A 1 181 ? -54.26100 30.84100  9.36000   1.000 16.89000  ? 610  PHE   A CB  1 
ATOM   1317 C  CG  . PHE   A 1 181 ? -53.17300 31.67100  8.78800   1.000 24.87000  ? 610  PHE   A CG  1 
ATOM   1318 C  CD1 . PHE   A 1 181 ? -53.04000 31.89400  7.45100   1.000 35.79000  ? 610  PHE   A CD1 1 
ATOM   1319 C  CD2 . PHE   A 1 181 ? -52.21700 32.19900  9.65000   1.000 32.85000  ? 610  PHE   A CD2 1 
ATOM   1320 C  CE1 . PHE   A 1 181 ? -51.96600 32.64100  6.97600   1.000 42.41000  ? 610  PHE   A CE1 1 
ATOM   1321 C  CE2 . PHE   A 1 181 ? -51.18100 32.97500  9.16500   1.000 40.88000  ? 610  PHE   A CE2 1 
ATOM   1322 C  CZ  . PHE   A 1 181 ? -51.07200 33.19300  7.82600   1.000 33.73000  ? 610  PHE   A CZ  1 
ATOM   1323 N  N   . GLU   A 1 182 ? -52.45400 28.73400  10.86500  1.000 16.37000  ? 611  GLU   A N   1 
ATOM   1324 C  CA  . GLU   A 1 182 ? -51.13400 28.32600  11.35300  1.000 17.17000  ? 611  GLU   A CA  1 
ATOM   1325 C  C   . GLU   A 1 182 ? -50.84100 26.87500  11.02300  1.000 22.12000  ? 611  GLU   A C   1 
ATOM   1326 O  O   . GLU   A 1 182 ? -49.68000 26.49000  10.73200  1.000 21.80000  ? 611  GLU   A O   1 
ATOM   1327 C  CB  . GLU   A 1 182 ? -51.07900 28.56900  12.85500  1.000 18.97000  ? 611  GLU   A CB  1 
ATOM   1328 C  CG  . GLU   A 1 182 ? -51.30900 30.01300  13.30100  1.000 20.34000  ? 611  GLU   A CG  1 
ATOM   1329 C  CD  . GLU   A 1 182 ? -52.78400 30.44600  13.42900  1.000 26.88000  ? 611  GLU   A CD  1 
ATOM   1330 O  OE1 . GLU   A 1 182 ? -53.72700 29.90200  12.81700  1.000 21.16000  ? 611  GLU   A OE1 1 
ATOM   1331 O  OE2 . GLU   A 1 182 ? -53.06200 31.22800  14.35900  1.000 36.18000  ? 611  GLU   A OE2 1 
ATOM   1332 N  N   . GLN   A 1 183 ? -51.87000 26.05400  11.03600  1.000 16.90000  ? 612  GLN   A N   1 
ATOM   1333 C  CA  . GLN   A 1 183 ? -51.70800 24.66000  10.64100  1.000 18.16000  ? 612  GLN   A CA  1 
ATOM   1334 C  C   . GLN   A 1 183 ? -51.23600 24.55600  9.20600   1.000 20.34000  ? 612  GLN   A C   1 
ATOM   1335 O  O   . GLN   A 1 183 ? -50.38500 23.71900  8.88700   1.000 20.63000  ? 612  GLN   A O   1 
ATOM   1336 C  CB  . GLN   A 1 183 ? -53.02000 23.90700  10.79900  1.000 15.73000  ? 612  GLN   A CB  1 
ATOM   1337 C  CG  . GLN   A 1 183 ? -53.39600 23.54700  12.23600  1.000 17.53000  ? 612  GLN   A CG  1 
ATOM   1338 C  CD  . GLN   A 1 183 ? -54.76600 22.86400  12.23200  1.000 25.46000  ? 612  GLN   A CD  1 
ATOM   1339 O  OE1 . GLN   A 1 183 ? -54.97400 21.82700  11.57800  1.000 27.15000  ? 612  GLN   A OE1 1 
ATOM   1340 N  NE2 . GLN   A 1 183 ? -55.70600 23.47300  12.87100  1.000 21.02000  ? 612  GLN   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 184 ? -51.82200 25.36600  8.30200   1.000 19.42000  ? 613  LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 184 ? -51.36200 25.35100  6.91000   1.000 17.55000  ? 613  LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 184 ? -49.86400 25.65200  6.82300   1.000 20.13000  ? 613  LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 184 ? -49.10800 24.95300  6.13000   1.000 19.32000  ? 613  LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 184 ? -52.17400 26.34900  6.07300   1.000 18.79000  ? 613  LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 184 ? -51.71700 26.45200  4.60000   1.000 17.73000  ? 613  LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 184 ? -51.81900 25.19100  3.78900   1.000 19.24000  ? 613  LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 184 ? -52.50400 27.55000  3.89200   1.000 17.33000  ? 613  LEU   A CD2 1 
ATOM   1349 N  N   A SER   A 1 185 ? -49.41000 26.69100  7.52200   0.617 18.32000  ? 614  SER   A N   1 
ATOM   1350 N  N   B SER   A 1 185 ? -49.40300 26.69200  7.51300   0.383 18.42000  ? 614  SER   A N   1 
ATOM   1351 C  CA  A SER   A 1 185 ? -47.99700 27.06000  7.43100   0.617 19.02000  ? 614  SER   A CA  1 
ATOM   1352 C  CA  B SER   A 1 185 ? -47.99100 27.04600  7.36700   0.383 19.03000  ? 614  SER   A CA  1 
ATOM   1353 C  C   A SER   A 1 185 ? -47.10300 25.92300  7.90100   0.617 24.98000  ? 614  SER   A C   1 
ATOM   1354 C  C   B SER   A 1 185 ? -47.08300 25.95000  7.91700   0.383 24.91000  ? 614  SER   A C   1 
ATOM   1355 O  O   A SER   A 1 185 ? -46.00800 25.70000  7.35600   0.617 21.47000  ? 614  SER   A O   1 
ATOM   1356 O  O   B SER   A 1 185 ? -45.95000 25.78400  7.44200   0.383 21.51000  ? 614  SER   A O   1 
ATOM   1357 C  CB  A SER   A 1 185 ? -47.72500 28.31500  8.26900   0.617 28.24000  ? 614  SER   A CB  1 
ATOM   1358 C  CB  B SER   A 1 185 ? -47.69000 28.36800  8.07700   0.383 28.68000  ? 614  SER   A CB  1 
ATOM   1359 O  OG  A SER   A 1 185 ? -48.66400 29.30800  7.94000   0.617 28.92000  ? 614  SER   A OG  1 
ATOM   1360 O  OG  B SER   A 1 185 ? -47.84000 28.19500  9.45800   0.383 31.68000  ? 614  SER   A OG  1 
ATOM   1361 N  N   . GLY   A 1 186 ? -47.56000 25.19900  8.91000   1.000 18.65000  ? 615  GLY   A N   1 
ATOM   1362 C  CA  . GLY   A 1 186 ? -46.76100 24.14000  9.49400   1.000 21.56000  ? 615  GLY   A CA  1 
ATOM   1363 C  C   . GLY   A 1 186 ? -46.76600 22.86200  8.71800   1.000 22.85000  ? 615  GLY   A C   1 
ATOM   1364 O  O   . GLY   A 1 186 ? -45.91100 22.00600  8.99000   1.000 24.59000  ? 615  GLY   A O   1 
ATOM   1365 N  N   . SER   A 1 187 ? -47.71200 22.70000  7.77600   1.000 17.26000  ? 616  SER   A N   1 
ATOM   1366 C  CA  . SER   A 1 187 ? -47.90000 21.45800  7.02100   1.000 16.19000  ? 616  SER   A CA  1 
ATOM   1367 C  C   . SER   A 1 187 ? -47.56200 21.58600  5.55400   1.000 19.54000  ? 616  SER   A C   1 
ATOM   1368 O  O   . SER   A 1 187 ? -47.46800 20.57600  4.85900   1.000 17.25000  ? 616  SER   A O   1 
ATOM   1369 C  CB  . SER   A 1 187 ? -49.35100 20.97400  7.17100   1.000 21.62000  ? 616  SER   A CB  1 
ATOM   1370 O  OG  . SER   A 1 187 ? -49.54500 20.55800  8.51900   1.000 25.51000  ? 616  SER   A OG  1 
ATOM   1371 N  N   . ILE   A 1 188 ? -47.39600 22.81500  5.04400   1.000 17.26000  ? 617  ILE   A N   1 
ATOM   1372 C  CA  . ILE   A 1 188 ? -47.33900 23.00700  3.58500   1.000 18.29000  ? 617  ILE   A CA  1 
ATOM   1373 C  C   . ILE   A 1 188 ? -46.28100 22.11500  2.89300   1.000 17.44000  ? 617  ILE   A C   1 
ATOM   1374 O  O   . ILE   A 1 188 ? -46.53700 21.60200  1.79400   1.000 17.92000  ? 617  ILE   A O   1 
ATOM   1375 C  CB  . ILE   A 1 188 ? -47.13900 24.51800  3.27100   1.000 24.06000  ? 617  ILE   A CB  1 
ATOM   1376 C  CG1 . ILE   A 1 188 ? -47.17100 24.78400  1.77000   1.000 23.17000  ? 617  ILE   A CG1 1 
ATOM   1377 C  CG2 . ILE   A 1 188 ? -45.91500 25.08300  3.90800   1.000 23.32000  ? 617  ILE   A CG2 1 
ATOM   1378 C  CD1 . ILE   A 1 188 ? -48.44600 24.23000  1.12100   1.000 31.97000  ? 617  ILE   A CD1 1 
ATOM   1379 N  N   . LEU   A 1 189 ? -45.08800 21.93500  3.49400   1.000 18.83000  ? 618  LEU   A N   1 
ATOM   1380 C  CA  . LEU   A 1 189 ? -44.03600 21.18800  2.79800   1.000 17.90000  ? 618  LEU   A CA  1 
ATOM   1381 C  C   . LEU   A 1 189 ? -44.43400 19.73900  2.48800   1.000 21.18000  ? 618  LEU   A C   1 
ATOM   1382 O  O   . LEU   A 1 189 ? -43.92100 19.13900  1.52200   1.000 19.76000  ? 618  LEU   A O   1 
ATOM   1383 C  CB  . LEU   A 1 189 ? -42.76000 21.20700  3.61700   1.000 19.28000  ? 618  LEU   A CB  1 
ATOM   1384 C  CG  . LEU   A 1 189 ? -42.11500 22.57200  3.79600   1.000 22.18000  ? 618  LEU   A CG  1 
ATOM   1385 C  CD1 . LEU   A 1 189 ? -40.82400 22.41800  4.60400   1.000 22.28000  ? 618  LEU   A CD1 1 
ATOM   1386 C  CD2 . LEU   A 1 189 ? -41.85600 23.33100  2.43200   1.000 20.52000  ? 618  LEU   A CD2 1 
ATOM   1387 N  N   . TRP   A 1 190 ? -45.31200 19.14000  3.30300   1.000 20.12000  ? 619  TRP   A N   1 
ATOM   1388 C  CA  . TRP   A 1 190 ? -45.70900 17.74700  3.12600   1.000 16.30000  ? 619  TRP   A CA  1 
ATOM   1389 C  C   . TRP   A 1 190 ? -47.01900 17.61300  2.38200   1.000 17.33000  ? 619  TRP   A C   1 
ATOM   1390 O  O   . TRP   A 1 190 ? -47.52200 16.48900  2.21400   1.000 17.53000  ? 619  TRP   A O   1 
ATOM   1391 C  CB  . TRP   A 1 190 ? -45.81100 17.03000  4.51900   1.000 17.99000  ? 619  TRP   A CB  1 
ATOM   1392 C  CG  . TRP   A 1 190 ? -44.49100 16.94800  5.19700   1.000 16.68000  ? 619  TRP   A CG  1 
ATOM   1393 C  CD1 . TRP   A 1 190 ? -43.59900 15.87800  5.16400   1.000 18.50000  ? 619  TRP   A CD1 1 
ATOM   1394 C  CD2 . TRP   A 1 190 ? -43.84600 17.97600  5.99600   1.000 18.90000  ? 619  TRP   A CD2 1 
ATOM   1395 N  NE1 . TRP   A 1 190 ? -42.44400 16.18500  5.89100   1.000 18.27000  ? 619  TRP   A NE1 1 
ATOM   1396 C  CE2 . TRP   A 1 190 ? -42.58400 17.45500  6.41500   1.000 21.00000  ? 619  TRP   A CE2 1 
ATOM   1397 C  CE3 . TRP   A 1 190 ? -44.23400 19.28300  6.41600   1.000 15.39000  ? 619  TRP   A CE3 1 
ATOM   1398 C  CZ2 . TRP   A 1 190 ? -41.67400 18.19000  7.17300   1.000 19.39000  ? 619  TRP   A CZ2 1 
ATOM   1399 C  CZ3 . TRP   A 1 190 ? -43.33000 19.98500  7.23400   1.000 17.59000  ? 619  TRP   A CZ3 1 
ATOM   1400 C  CH2 . TRP   A 1 190 ? -42.06200 19.45700  7.56400   1.000 24.73000  ? 619  TRP   A CH2 1 
ATOM   1401 N  N   . MET   A 1 191 ? -47.60800 18.72400  1.89000   1.000 19.17000  ? 620  MET   A N   1 
ATOM   1402 C  CA  . MET   A 1 191 ? -48.99700 18.70500  1.46800   1.000 16.61000  ? 620  MET   A CA  1 
ATOM   1403 C  C   . MET   A 1 191 ? -49.15700 18.42500  -0.03100  1.000 17.70000  ? 620  MET   A C   1 
ATOM   1404 O  O   . MET   A 1 191 ? -48.60000 19.14700  -0.87000  1.000 19.07000  ? 620  MET   A O   1 
ATOM   1405 C  CB  . MET   A 1 191 ? -49.63000 20.03800  1.92400   1.000 17.76000  ? 620  MET   A CB  1 
ATOM   1406 C  CG  . MET   A 1 191 ? -51.10800 20.03000  1.69700   1.000 22.85000  ? 620  MET   A CG  1 
ATOM   1407 S  SD  . MET   A 1 191 ? -51.82800 21.69200  2.19600   1.000 21.60000  ? 620  MET   A SD  1 
ATOM   1408 C  CE  . MET   A 1 191 ? -51.76800 21.52300  3.96100   1.000 24.57000  ? 620  MET   A CE  1 
ATOM   1409 N  N   . ALA   A 1 192 ? -49.89900 17.36300  -0.36700  1.000 17.98000  ? 621  ALA   A N   1 
ATOM   1410 C  CA  . ALA   A 1 192 ? -50.10200 17.02400  -1.78400  1.000 17.47000  ? 621  ALA   A CA  1 
ATOM   1411 C  C   . ALA   A 1 192 ? -50.78300 18.17900  -2.51900  1.000 18.55000  ? 621  ALA   A C   1 
ATOM   1412 O  O   . ALA   A 1 192 ? -51.55700 18.93000  -1.91100  1.000 17.96000  ? 621  ALA   A O   1 
ATOM   1413 C  CB  . ALA   A 1 192 ? -50.95300 15.77100  -1.92100  1.000 16.55000  ? 621  ALA   A CB  1 
ATOM   1414 N  N   . PRO   A 1 193 ? -50.46000 18.38100  -3.80900  1.000 19.70000  ? 622  PRO   A N   1 
ATOM   1415 C  CA  . PRO   A 1 193 ? -51.07900 19.50100  -4.55400  1.000 18.39000  ? 622  PRO   A CA  1 
ATOM   1416 C  C   . PRO   A 1 193 ? -52.56700 19.53100  -4.44000  1.000 18.31000  ? 622  PRO   A C   1 
ATOM   1417 O  O   . PRO   A 1 193 ? -53.14600 20.64000  -4.33100  1.000 18.76000  ? 622  PRO   A O   1 
ATOM   1418 C  CB  . PRO   A 1 193 ? -50.62200 19.26900  -6.02300  1.000 20.40000  ? 622  PRO   A CB  1 
ATOM   1419 C  CG  . PRO   A 1 193 ? -49.27600 18.53000  -5.85300  1.000 24.56000  ? 622  PRO   A CG  1 
ATOM   1420 C  CD  . PRO   A 1 193 ? -49.49100 17.61400  -4.62000  1.000 21.94000  ? 622  PRO   A CD  1 
ATOM   1421 N  N   . GLU   A 1 194 ? -53.23900 18.35900  -4.40100  1.000 18.08000  ? 623  GLU   A N   1 
ATOM   1422 C  CA  . GLU   A 1 194 ? -54.69400 18.38700  -4.35100  1.000 18.07000  ? 623  GLU   A CA  1 
ATOM   1423 C  C   . GLU   A 1 194 ? -55.23700 18.74600  -2.96200  1.000 20.53000  ? 623  GLU   A C   1 
ATOM   1424 O  O   . GLU   A 1 194 ? -56.38600 19.20500  -2.86600  1.000 21.20000  ? 623  GLU   A O   1 
ATOM   1425 C  CB  . GLU   A 1 194 ? -55.28500 17.05600  -4.84500  1.000 18.22000  ? 623  GLU   A CB  1 
ATOM   1426 C  CG  . GLU   A 1 194 ? -55.14800 15.82400  -3.86700  1.000 18.52000  ? 623  GLU   A CG  1 
ATOM   1427 C  CD  . GLU   A 1 194 ? -53.79700 15.09400  -4.00000  1.000 19.90000  ? 623  GLU   A CD  1 
ATOM   1428 O  OE1 . GLU   A 1 194 ? -52.88900 15.60500  -4.68100  1.000 20.07000  ? 623  GLU   A OE1 1 
ATOM   1429 O  OE2 . GLU   A 1 194 ? -53.62800 13.99800  -3.36700  1.000 19.14000  ? 623  GLU   A OE2 1 
ATOM   1430 N  N   . VAL   A 1 195 ? -54.44900 18.54200  -1.90500  1.000 17.43000  ? 624  VAL   A N   1 
ATOM   1431 C  CA  . VAL   A 1 195 ? -54.82600 19.04500  -0.58800  1.000 19.42000  ? 624  VAL   A CA  1 
ATOM   1432 C  C   . VAL   A 1 195 ? -54.61100 20.55300  -0.50400  1.000 19.69000  ? 624  VAL   A C   1 
ATOM   1433 O  O   . VAL   A 1 195 ? -55.38200 21.26300  0.17600   1.000 18.88000  ? 624  VAL   A O   1 
ATOM   1434 C  CB  . VAL   A 1 195 ? -54.05700 18.30800  0.51900   1.000 19.05000  ? 624  VAL   A CB  1 
ATOM   1435 C  CG1 . VAL   A 1 195 ? -54.36300 18.92300  1.92500   1.000 16.48000  ? 624  VAL   A CG1 1 
ATOM   1436 C  CG2 . VAL   A 1 195 ? -54.47800 16.81200  0.49700   1.000 18.32000  ? 624  VAL   A CG2 1 
ATOM   1437 N  N   . ILE   A 1 196 ? -53.59800 21.08100  -1.17500  1.000 18.33000  ? 625  ILE   A N   1 
ATOM   1438 C  CA  . ILE   A 1 196 ? -53.45800 22.53600  -1.23400  1.000 16.34000  ? 625  ILE   A CA  1 
ATOM   1439 C  C   . ILE   A 1 196 ? -54.70400 23.12000  -1.86800  1.000 15.72000  ? 625  ILE   A C   1 
ATOM   1440 O  O   . ILE   A 1 196 ? -55.37200 23.97900  -1.27700  1.000 20.07000  ? 625  ILE   A O   1 
ATOM   1441 C  CB  . ILE   A 1 196 ? -52.20800 22.93400  -2.02900  1.000 18.57000  ? 625  ILE   A CB  1 
ATOM   1442 C  CG1 . ILE   A 1 196 ? -50.92700 22.53800  -1.29800  1.000 16.80000  ? 625  ILE   A CG1 1 
ATOM   1443 C  CG2 . ILE   A 1 196 ? -52.23800 24.47100  -2.26700  1.000 18.92000  ? 625  ILE   A CG2 1 
ATOM   1444 C  CD1 . ILE   A 1 196 ? -49.64700 22.79200  -2.07900  1.000 19.14000  ? 625  ILE   A CD1 1 
ATOM   1445 N  N   . ARG   A 1 197 ? -55.09700 22.60000  -3.04200  1.000 18.13000  ? 626  ARG   A N   1 
ATOM   1446 C  CA  . ARG   A 1 197 ? -56.21900 23.22100  -3.76700  1.000 19.07000  ? 626  ARG   A CA  1 
ATOM   1447 C  C   . ARG   A 1 197 ? -57.56600 22.92900  -3.11900  1.000 18.56000  ? 626  ARG   A C   1 
ATOM   1448 O  O   . ARG   A 1 197 ? -58.46200 23.79200  -3.18500  1.000 20.90000  ? 626  ARG   A O   1 
ATOM   1449 C  CB  . ARG   A 1 197 ? -56.26100 22.72200  -5.24000  1.000 20.20000  ? 626  ARG   A CB  1 
ATOM   1450 C  CG  . ARG   A 1 197 ? -55.23200 23.40900  -6.15600  1.000 27.38000  ? 626  ARG   A CG  1 
ATOM   1451 C  CD  . ARG   A 1 197 ? -55.88600 24.68200  -6.78800  1.000 58.64000  ? 626  ARG   A CD  1 
ATOM   1452 N  NE  . ARG   A 1 197 ? -55.01400 25.40100  -7.71900  1.000 47.36000  ? 626  ARG   A NE  1 
ATOM   1453 C  CZ  . ARG   A 1 197 ? -53.93800 26.08100  -7.33300  1.000 63.72000  ? 626  ARG   A CZ  1 
ATOM   1454 N  NH1 . ARG   A 1 197 ? -53.58000 26.15300  -6.04000  1.000 35.83000  ? 626  ARG   A NH1 1 
ATOM   1455 N  NH2 . ARG   A 1 197 ? -53.19300 26.70100  -8.25700  1.000 47.46000  ? 626  ARG   A NH2 1 
ATOM   1456 N  N   . MET   A 1 198 ? -57.78900 21.69800  -2.59500  1.000 17.18000  ? 627  MET   A N   1 
ATOM   1457 C  CA  . MET   A 1 198 ? -59.07400 21.29600  -2.00200  1.000 19.07000  ? 627  MET   A CA  1 
ATOM   1458 C  C   . MET   A 1 198 ? -60.22500 21.32500  -3.02600  1.000 23.99000  ? 627  MET   A C   1 
ATOM   1459 O  O   . MET   A 1 198 ? -61.38600 21.49700  -2.66400  1.000 24.64000  ? 627  MET   A O   1 
ATOM   1460 C  CB  . MET   A 1 198 ? -59.40300 22.21500  -0.80900  1.000 20.71000  ? 627  MET   A CB  1 
ATOM   1461 C  CG  . MET   A 1 198 ? -58.71100 22.02100  0.48200   1.000 20.19000  ? 627  MET   A CG  1 
ATOM   1462 S  SD  . MET   A 1 198 ? -58.22700 20.35700  1.05700   1.000 21.62000  ? 627  MET   A SD  1 
ATOM   1463 C  CE  . MET   A 1 198 ? -59.76100 20.12300  1.97700   1.000 24.11000  ? 627  MET   A CE  1 
ATOM   1464 N  N   . GLN   A 1 199 ? -59.91900 21.16700  -4.31300  1.000 20.81000  ? 628  GLN   A N   1 
ATOM   1465 C  CA  . GLN   A 1 199 ? -60.91000 21.27700  -5.36900  1.000 23.24000  ? 628  GLN   A CA  1 
ATOM   1466 C  C   . GLN   A 1 199 ? -61.40400 19.91800  -5.82700  1.000 32.09000  ? 628  GLN   A C   1 
ATOM   1467 O  O   . GLN   A 1 199 ? -62.58700 19.79200  -6.17300  1.000 29.15000  ? 628  GLN   A O   1 
ATOM   1468 C  CB  . GLN   A 1 199 ? -60.31100 22.06700  -6.54700  1.000 29.39000  ? 628  GLN   A CB  1 
ATOM   1469 C  CG  . GLN   A 1 199 ? -61.13400 22.16800  -7.79400  1.000 50.44000  ? 628  GLN   A CG  1 
ATOM   1470 C  CD  . GLN   A 1 199 ? -60.56000 23.21600  -8.76200  1.000 67.91000  ? 628  GLN   A CD  1 
ATOM   1471 O  OE1 . GLN   A 1 199 ? -61.20500 24.21800  -9.07400  1.000 61.29000  ? 628  GLN   A OE1 1 
ATOM   1472 N  NE2 . GLN   A 1 199 ? -59.33800 22.97800  -9.23400  1.000 68.54000  ? 628  GLN   A NE2 1 
ATOM   1473 N  N   . ASP   A 1 200 ? -60.54000 18.89000  -5.78400  1.000 25.24000  ? 629  ASP   A N   1 
ATOM   1474 C  CA  . ASP   A 1 200 ? -60.92400 17.58700  -6.29600  1.000 29.90000  ? 629  ASP   A CA  1 
ATOM   1475 C  C   . ASP   A 1 200 ? -61.77900 16.89100  -5.25900  1.000 28.09000  ? 629  ASP   A C   1 
ATOM   1476 O  O   . ASP   A 1 200 ? -61.91200 17.33900  -4.12800  1.000 28.00000  ? 629  ASP   A O   1 
ATOM   1477 C  CB  . ASP   A 1 200 ? -59.68600 16.72900  -6.65500  1.000 31.07000  ? 629  ASP   A CB  1 
ATOM   1478 C  CG  . ASP   A 1 200 ? -58.93100 17.26400  -7.88000  1.000 38.45000  ? 629  ASP   A CG  1 
ATOM   1479 O  OD1 . ASP   A 1 200 ? -59.56800 17.86900  -8.77200  1.000 40.66000  ? 629  ASP   A OD1 1 
ATOM   1480 O  OD2 . ASP   A 1 200 ? -57.68800 17.09600  -7.96700  1.000 39.56000  ? 629  ASP   A OD2 1 
ATOM   1481 N  N   . LYS   A 1 201 ? -62.43300 15.82200  -5.68900  1.000 26.30000  ? 630  LYS   A N   1 
ATOM   1482 C  CA  . LYS   A 1 201 ? -63.26700 15.04700  -4.78600  1.000 24.40000  ? 630  LYS   A CA  1 
ATOM   1483 C  C   . LYS   A 1 201 ? -62.40100 14.40100  -3.71400  1.000 30.79000  ? 630  LYS   A C   1 
ATOM   1484 O  O   . LYS   A 1 201 ? -61.33300 13.87900  -4.03300  1.000 30.04000  ? 630  LYS   A O   1 
ATOM   1485 C  CB  . LYS   A 1 201 ? -63.99700 13.95900  -5.58000  1.000 34.34000  ? 630  LYS   A CB  1 
ATOM   1486 C  CG  . LYS   A 1 201 ? -65.18600 13.37500  -4.83200  1.000 41.89000  ? 630  LYS   A CG  1 
ATOM   1487 C  CD  . LYS   A 1 201 ? -65.77800 12.25300  -5.68900  1.000 50.67000  ? 630  LYS   A CD  1 
ATOM   1488 C  CE  . LYS   A 1 201 ? -66.96200 12.70800  -6.49800  1.000 59.40000  ? 630  LYS   A CE  1 
ATOM   1489 N  NZ  . LYS   A 1 201 ? -67.67400 11.51700  -7.06000  1.000 74.12000  ? 630  LYS   A NZ  1 
ATOM   1490 N  N   . ASN   A 1 202 ? -62.84900 14.48700  -2.43000  1.000 26.98000  ? 631  ASN   A N   1 
ATOM   1491 C  CA  . ASN   A 1 202 ? -62.15700 13.90500  -1.27500  1.000 27.33000  ? 631  ASN   A CA  1 
ATOM   1492 C  C   . ASN   A 1 202 ? -60.66500 14.18300  -1.33900  1.000 20.41000  ? 631  ASN   A C   1 
ATOM   1493 O  O   . ASN   A 1 202 ? -59.85300 13.26000  -1.57300  1.000 22.87000  ? 631  ASN   A O   1 
ATOM   1494 C  CB  . ASN   A 1 202 ? -62.42200 12.40200  -1.20200  1.000 35.21000  ? 631  ASN   A CB  1 
ATOM   1495 C  CG  . ASN   A 1 202 ? -63.89300 12.08800  -0.95800  1.000 38.85000  ? 631  ASN   A CG  1 
ATOM   1496 O  OD1 . ASN   A 1 202 ? -64.51600 12.65300  -0.07000  1.000 40.27000  ? 631  ASN   A OD1 1 
ATOM   1497 N  ND2 . ASN   A 1 202 ? -64.45700 11.20800  -1.78600  1.000 35.76000  ? 631  ASN   A ND2 1 
ATOM   1498 N  N   . PRO   A 1 203 ? -60.26800 15.43700  -1.07900  1.000 24.94000  ? 632  PRO   A N   1 
ATOM   1499 C  CA  . PRO   A 1 203 ? -58.85100 15.80000  -1.18600  1.000 20.32000  ? 632  PRO   A CA  1 
ATOM   1500 C  C   . PRO   A 1 203 ? -57.95700 15.05900  -0.23400  1.000 17.11000  ? 632  PRO   A C   1 
ATOM   1501 O  O   . PRO   A 1 203 ? -56.80500 14.76000  -0.60400  1.000 17.85000  ? 632  PRO   A O   1 
ATOM   1502 C  CB  . PRO   A 1 203 ? -58.83100 17.32100  -0.90500  1.000 26.76000  ? 632  PRO   A CB  1 
ATOM   1503 C  CG  . PRO   A 1 203 ? -60.27200 17.77600  -0.97800  1.000 32.63000  ? 632  PRO   A CG  1 
ATOM   1504 C  CD  . PRO   A 1 203 ? -61.13300 16.57000  -0.68300  1.000 27.62000  ? 632  PRO   A CD  1 
ATOM   1505 N  N   . TYR   A 1 204 ? -58.42500 14.75100  0.97900   1.000 20.45000  ? 633  TYR   A N   1 
ATOM   1506 C  CA  . TYR   A 1 204 ? -57.65300 13.91900  1.90300   1.000 18.85000  ? 633  TYR   A CA  1 
ATOM   1507 C  C   . TYR   A 1 204 ? -57.95600 12.45900  1.60600   1.000 16.72000  ? 633  TYR   A C   1 
ATOM   1508 O  O   . TYR   A 1 204 ? -59.13400 12.05500  1.55800   1.000 21.57000  ? 633  TYR   A O   1 
ATOM   1509 C  CB  . TYR   A 1 204 ? -57.98300 14.23500  3.37100   1.000 19.82000  ? 633  TYR   A CB  1 
ATOM   1510 C  CG  . TYR   A 1 204 ? -57.33500 15.50300  3.85200   1.000 18.72000  ? 633  TYR   A CG  1 
ATOM   1511 C  CD1 . TYR   A 1 204 ? -56.01500 15.53800  4.23600   1.000 17.13000  ? 633  TYR   A CD1 1 
ATOM   1512 C  CD2 . TYR   A 1 204 ? -58.06000 16.68600  3.91800   1.000 26.15000  ? 633  TYR   A CD2 1 
ATOM   1513 C  CE1 . TYR   A 1 204 ? -55.40200 16.70600  4.69600   1.000 16.63000  ? 633  TYR   A CE1 1 
ATOM   1514 C  CE2 . TYR   A 1 204 ? -57.47400 17.85700  4.34400   1.000 23.70000  ? 633  TYR   A CE2 1 
ATOM   1515 C  CZ  . TYR   A 1 204 ? -56.17000 17.86800  4.76000   1.000 22.53000  ? 633  TYR   A CZ  1 
ATOM   1516 O  OH  . TYR   A 1 204 ? -55.56200 19.02000  5.22000   1.000 26.04000  ? 633  TYR   A OH  1 
ATOM   1517 N  N   . SER   A 1 205 ? -56.89500 11.68000  1.40200   1.000 17.28000  ? 634  SER   A N   1 
ATOM   1518 C  CA  . SER   A 1 205 ? -57.04600 10.28800  0.95000   1.000 18.66000  ? 634  SER   A CA  1 
ATOM   1519 C  C   . SER   A 1 205 ? -55.84600 9.48700   1.42300   1.000 18.06000  ? 634  SER   A C   1 
ATOM   1520 O  O   . SER   A 1 205 ? -54.86300 10.04500  1.87600   1.000 14.78000  ? 634  SER   A O   1 
ATOM   1521 C  CB  . SER   A 1 205 ? -57.13500 10.23500  -0.57900  1.000 18.12000  ? 634  SER   A CB  1 
ATOM   1522 O  OG  . SER   A 1 205 ? -55.90000 10.65800  -1.12300  1.000 16.78000  ? 634  SER   A OG  1 
ATOM   1523 N  N   . PHE   A 1 206 ? -55.92700 8.13800   1.31800   1.000 18.63000  ? 635  PHE   A N   1 
ATOM   1524 C  CA  . PHE   A 1 206 ? -54.69700 7.36400   1.43600   1.000 17.24000  ? 635  PHE   A CA  1 
ATOM   1525 C  C   . PHE   A 1 206 ? -53.61100 7.93100   0.53800   1.000 18.12000  ? 635  PHE   A C   1 
ATOM   1526 O  O   . PHE   A 1 206 ? -52.43200 7.94000   0.92000   1.000 16.24000  ? 635  PHE   A O   1 
ATOM   1527 C  CB  . PHE   A 1 206 ? -54.96300 5.88500   1.06700   1.000 17.70000  ? 635  PHE   A CB  1 
ATOM   1528 C  CG  . PHE   A 1 206 ? -55.87900 5.16900   2.03200   1.000 20.39000  ? 635  PHE   A CG  1 
ATOM   1529 C  CD1 . PHE   A 1 206 ? -56.08300 5.64400   3.29800   1.000 16.13000  ? 635  PHE   A CD1 1 
ATOM   1530 C  CD2 . PHE   A 1 206 ? -56.50300 3.97000   1.66400   1.000 30.77000  ? 635  PHE   A CD2 1 
ATOM   1531 C  CE1 . PHE   A 1 206 ? -56.96400 4.98600   4.21200   1.000 20.41000  ? 635  PHE   A CE1 1 
ATOM   1532 C  CE2 . PHE   A 1 206 ? -57.37200 3.29000   2.55100   1.000 32.10000  ? 635  PHE   A CE2 1 
ATOM   1533 C  CZ  . PHE   A 1 206 ? -57.60200 3.80200   3.82900   1.000 26.71000  ? 635  PHE   A CZ  1 
ATOM   1534 N  N   . GLN   A 1 207 ? -53.96800 8.37400   -0.69100  1.000 15.19000  ? 636  GLN   A N   1 
ATOM   1535 C  CA  . GLN   A 1 207 ? -52.91700 8.82900   -1.59000  1.000 17.65000  ? 636  GLN   A CA  1 
ATOM   1536 C  C   . GLN   A 1 207 ? -52.29800 10.14700  -1.13700  1.000 13.80000  ? 636  GLN   A C   1 
ATOM   1537 O  O   . GLN   A 1 207 ? -51.11900 10.40700  -1.42500  1.000 15.74000  ? 636  GLN   A O   1 
ATOM   1538 C  CB  . GLN   A 1 207 ? -53.51300 9.01300   -3.00600  1.000 23.23000  ? 636  GLN   A CB  1 
ATOM   1539 C  CG  . GLN   A 1 207 ? -53.72900 7.69100   -3.77600  1.000 20.12000  ? 636  GLN   A CG  1 
ATOM   1540 C  CD  . GLN   A 1 207 ? -55.02700 7.04000   -3.49400  1.000 27.82000  ? 636  GLN   A CD  1 
ATOM   1541 O  OE1 . GLN   A 1 207 ? -55.84500 7.47600   -2.63100  1.000 25.98000  ? 636  GLN   A OE1 1 
ATOM   1542 N  NE2 . GLN   A 1 207 ? -55.25600 5.94400   -4.20200  1.000 26.46000  ? 636  GLN   A NE2 1 
ATOM   1543 N  N   . SER   A 1 208 ? -53.07600 11.03900  -0.50300  1.000 16.64000  ? 637  SER   A N   1 
ATOM   1544 C  CA  . SER   A 1 208 ? -52.36400 12.22700  -0.00200  1.000 16.63000  ? 637  SER   A CA  1 
ATOM   1545 C  C   . SER   A 1 208 ? -51.45600 11.89100  1.17800   1.000 15.84000  ? 637  SER   A C   1 
ATOM   1546 O  O   . SER   A 1 208 ? -50.41600 12.53500  1.35600   1.000 15.00000  ? 637  SER   A O   1 
ATOM   1547 C  CB  . SER   A 1 208 ? -53.33700 13.37400  0.36900   1.000 15.29000  ? 637  SER   A CB  1 
ATOM   1548 O  OG  . SER   A 1 208 ? -54.35100 12.96700  1.29900   1.000 17.36000  ? 637  SER   A OG  1 
ATOM   1549 N  N   . ASP   A 1 209 ? -51.77200 10.87000  1.97200   1.000 16.72000  ? 638  ASP   A N   1 
ATOM   1550 C  CA  . ASP   A 1 209 ? -50.81300 10.41900  2.97900   1.000 14.07000  ? 638  ASP   A CA  1 
ATOM   1551 C  C   . ASP   A 1 209 ? -49.56400 9.87000   2.30300   1.000 15.52000  ? 638  ASP   A C   1 
ATOM   1552 O  O   . ASP   A 1 209 ? -48.46400 10.03200  2.79800   1.000 16.41000  ? 638  ASP   A O   1 
ATOM   1553 C  CB  . ASP   A 1 209 ? -51.42100 9.30800   3.83400   1.000 16.70000  ? 638  ASP   A CB  1 
ATOM   1554 C  CG  . ASP   A 1 209 ? -52.32800 9.80300   4.97300   1.000 18.42000  ? 638  ASP   A CG  1 
ATOM   1555 O  OD1 . ASP   A 1 209 ? -52.43900 11.04200  5.28400   1.000 16.71000  ? 638  ASP   A OD1 1 
ATOM   1556 O  OD2 . ASP   A 1 209 ? -52.98700 8.89700   5.58300   1.000 15.54000  ? 638  ASP   A OD2 1 
ATOM   1557 N  N   . VAL   A 1 210 ? -49.74300 9.17000   1.17500   1.000 13.64000  ? 639  VAL   A N   1 
ATOM   1558 C  CA  . VAL   A 1 210 ? -48.57900 8.65500   0.46200   1.000 15.64000  ? 639  VAL   A CA  1 
ATOM   1559 C  C   . VAL   A 1 210 ? -47.66500 9.78200   0.01300   1.000 16.67000  ? 639  VAL   A C   1 
ATOM   1560 O  O   . VAL   A 1 210 ? -46.43600 9.68500   0.07500   1.000 15.30000  ? 639  VAL   A O   1 
ATOM   1561 C  CB  . VAL   A 1 210 ? -49.06200 7.78100   -0.72000  1.000 17.34000  ? 639  VAL   A CB  1 
ATOM   1562 C  CG1 . VAL   A 1 210 ? -47.89400 7.48100   -1.68700  1.000 19.65000  ? 639  VAL   A CG1 1 
ATOM   1563 C  CG2 . VAL   A 1 210 ? -49.67600 6.48000   -0.16400  1.000 14.52000  ? 639  VAL   A CG2 1 
ATOM   1564 N  N   . TYR   A 1 211 ? -48.24700 10.87600  -0.46000  1.000 16.52000  ? 640  TYR   A N   1 
ATOM   1565 C  CA  . TYR   A 1 211 ? -47.42000 11.98900  -0.87800  1.000 16.72000  ? 640  TYR   A CA  1 
ATOM   1566 C  C   . TYR   A 1 211 ? -46.62300 12.55500  0.30400   1.000 15.73000  ? 640  TYR   A C   1 
ATOM   1567 O  O   . TYR   A 1 211 ? -45.41600 12.83000  0.19300   1.000 15.58000  ? 640  TYR   A O   1 
ATOM   1568 C  CB  . TYR   A 1 211 ? -48.35900 13.05000  -1.52400  1.000 13.27000  ? 640  TYR   A CB  1 
ATOM   1569 C  CG  . TYR   A 1 211 ? -47.53000 14.26300  -1.95500  1.000 14.83000  ? 640  TYR   A CG  1 
ATOM   1570 C  CD1 . TYR   A 1 211 ? -47.17800 15.25200  -1.05700  1.000 15.88000  ? 640  TYR   A CD1 1 
ATOM   1571 C  CD2 . TYR   A 1 211 ? -47.15500 14.44000  -3.31000  1.000 17.37000  ? 640  TYR   A CD2 1 
ATOM   1572 C  CE1 . TYR   A 1 211 ? -46.38100 16.35300  -1.43900  1.000 16.72000  ? 640  TYR   A CE1 1 
ATOM   1573 C  CE2 . TYR   A 1 211 ? -46.36500 15.53700  -3.69800  1.000 17.39000  ? 640  TYR   A CE2 1 
ATOM   1574 C  CZ  . TYR   A 1 211 ? -46.00400 16.50000  -2.76200  1.000 19.32000  ? 640  TYR   A CZ  1 
ATOM   1575 O  OH  . TYR   A 1 211 ? -45.21700 17.56900  -3.11700  1.000 20.39000  ? 640  TYR   A OH  1 
ATOM   1576 N  N   . ALA   A 1 212 ? -47.27800 12.73500  1.46800   1.000 13.61000  ? 641  ALA   A N   1 
ATOM   1577 C  CA  . ALA   A 1 212 ? -46.54600 13.22200  2.62400   1.000 16.69000  ? 641  ALA   A CA  1 
ATOM   1578 C  C   . ALA   A 1 212 ? -45.41100 12.28000  2.99000   1.000 16.46000  ? 641  ALA   A C   1 
ATOM   1579 O  O   . ALA   A 1 212 ? -44.31900 12.70600  3.38100   1.000 16.73000  ? 641  ALA   A O   1 
ATOM   1580 C  CB  . ALA   A 1 212 ? -47.51400 13.33400  3.81400   1.000 16.40000  ? 641  ALA   A CB  1 
ATOM   1581 N  N   . PHE   A 1 213 ? -45.68700 10.98000  2.91300   1.000 12.85000  ? 642  PHE   A N   1 
ATOM   1582 C  CA  . PHE   A 1 213 ? -44.64100 9.98800   3.14600   1.000 14.21000  ? 642  PHE   A CA  1 
ATOM   1583 C  C   . PHE   A 1 213 ? -43.50500 10.12600  2.12400   1.000 14.93000  ? 642  PHE   A C   1 
ATOM   1584 O  O   . PHE   A 1 213 ? -42.34200 9.99600   2.48700   1.000 17.00000  ? 642  PHE   A O   1 
ATOM   1585 C  CB  . PHE   A 1 213 ? -45.26400 8.59800   3.08800   1.000 15.77000  ? 642  PHE   A CB  1 
ATOM   1586 C  CG  . PHE   A 1 213 ? -44.24400 7.46500   3.26100   1.000 14.80000  ? 642  PHE   A CG  1 
ATOM   1587 C  CD1 . PHE   A 1 213 ? -43.80100 7.09300   4.53300   1.000 18.73000  ? 642  PHE   A CD1 1 
ATOM   1588 C  CD2 . PHE   A 1 213 ? -43.77800 6.75200   2.14200   1.000 16.83000  ? 642  PHE   A CD2 1 
ATOM   1589 C  CE1 . PHE   A 1 213 ? -42.86400 6.05100   4.70400   1.000 20.38000  ? 642  PHE   A CE1 1 
ATOM   1590 C  CE2 . PHE   A 1 213 ? -42.83000 5.73300   2.28600   1.000 17.80000  ? 642  PHE   A CE2 1 
ATOM   1591 C  CZ  . PHE   A 1 213 ? -42.36200 5.36600   3.58500   1.000 19.38000  ? 642  PHE   A CZ  1 
ATOM   1592 N  N   . GLY   A 1 214 ? -43.82200 10.41000  0.85300   1.000 16.27000  ? 643  GLY   A N   1 
ATOM   1593 C  CA  . GLY   A 1 214 ? -42.74300 10.68800  -0.10300  1.000 18.76000  ? 643  GLY   A CA  1 
ATOM   1594 C  C   . GLY   A 1 214 ? -41.87300 11.85600  0.29800   1.000 18.22000  ? 643  GLY   A C   1 
ATOM   1595 O  O   . GLY   A 1 214 ? -40.66900 11.84900  0.05700   1.000 17.87000  ? 643  GLY   A O   1 
ATOM   1596 N  N   . ILE   A 1 215 ? -42.45600 12.88300  0.94400   1.000 16.72000  ? 644  ILE   A N   1 
ATOM   1597 C  CA  . ILE   A 1 215 ? -41.64800 14.01800  1.40000   1.000 14.67000  ? 644  ILE   A CA  1 
ATOM   1598 C  C   . ILE   A 1 215 ? -40.79100 13.59300  2.59500   1.000 17.63000  ? 644  ILE   A C   1 
ATOM   1599 O  O   . ILE   A 1 215 ? -39.64200 13.99900  2.72400   1.000 19.29000  ? 644  ILE   A O   1 
ATOM   1600 C  CB  . ILE   A 1 215 ? -42.55900 15.22900  1.75700   1.000 15.44000  ? 644  ILE   A CB  1 
ATOM   1601 C  CG1 . ILE   A 1 215 ? -43.35700 15.69700  0.53700   1.000 15.85000  ? 644  ILE   A CG1 1 
ATOM   1602 C  CG2 . ILE   A 1 215 ? -41.74400 16.32700  2.46500   1.000 17.04000  ? 644  ILE   A CG2 1 
ATOM   1603 C  CD1 . ILE   A 1 215 ? -42.45800 16.35000  -0.62100  1.000 18.83000  ? 644  ILE   A CD1 1 
ATOM   1604 N  N   . VAL   A 1 216 ? -41.32100 12.72600  3.47400   1.000 16.83000  ? 645  VAL   A N   1 
ATOM   1605 C  CA  . VAL   A 1 216 ? -40.48400 12.15300  4.53000   1.000 15.21000  ? 645  VAL   A CA  1 
ATOM   1606 C  C   . VAL   A 1 216 ? -39.33200 11.33100  3.92900   1.000 13.80000  ? 645  VAL   A C   1 
ATOM   1607 O  O   . VAL   A 1 216 ? -38.18800 11.43000  4.40100   1.000 18.62000  ? 645  VAL   A O   1 
ATOM   1608 C  CB  . VAL   A 1 216 ? -41.35300 11.30700  5.48400   1.000 16.12000  ? 645  VAL   A CB  1 
ATOM   1609 C  CG1 . VAL   A 1 216 ? -40.43500 10.65100  6.57400   1.000 19.33000  ? 645  VAL   A CG1 1 
ATOM   1610 C  CG2 . VAL   A 1 216 ? -42.36100 12.24500  6.18300   1.000 18.31000  ? 645  VAL   A CG2 1 
ATOM   1611 N  N   . LEU   A 1 217 ? -39.60300 10.56600  2.86000   1.000 19.34000  ? 646  LEU   A N   1 
ATOM   1612 C  CA  . LEU   A 1 217 ? -38.51100 9.86500   2.17500   1.000 19.90000  ? 646  LEU   A CA  1 
ATOM   1613 C  C   . LEU   A 1 217 ? -37.47800 10.84300  1.65200   1.000 18.05000  ? 646  LEU   A C   1 
ATOM   1614 O  O   . LEU   A 1 217 ? -36.26600 10.63600  1.81700   1.000 20.33000  ? 646  LEU   A O   1 
ATOM   1615 C  CB  . LEU   A 1 217 ? -39.05800 9.01500   1.03900   1.000 19.35000  ? 646  LEU   A CB  1 
ATOM   1616 C  CG  . LEU   A 1 217 ? -39.87700 7.78300   1.39300   1.000 17.28000  ? 646  LEU   A CG  1 
ATOM   1617 C  CD1 . LEU   A 1 217 ? -40.21400 7.10200   0.07600   1.000 19.72000  ? 646  LEU   A CD1 1 
ATOM   1618 C  CD2 . LEU   A 1 217 ? -39.18000 6.81700   2.36200   1.000 21.40000  ? 646  LEU   A CD2 1 
ATOM   1619 N  N   . TYR   A 1 218 ? -37.93500 11.95400  1.05600   1.000 17.09000  ? 647  TYR   A N   1 
ATOM   1620 C  CA  . TYR   A 1 218 ? -37.00700 12.99000  0.61600   1.000 19.24000  ? 647  TYR   A CA  1 
ATOM   1621 C  C   . TYR   A 1 218 ? -36.15000 13.51700  1.76400   1.000 20.16000  ? 647  TYR   A C   1 
ATOM   1622 O  O   . TYR   A 1 218 ? -34.92500 13.64000  1.63400   1.000 23.55000  ? 647  TYR   A O   1 
ATOM   1623 C  CB  . TYR   A 1 218 ? -37.82100 14.11300  -0.05300  1.000 17.59000  ? 647  TYR   A CB  1 
ATOM   1624 C  CG  . TYR   A 1 218 ? -36.96400 15.22300  -0.59000  1.000 20.80000  ? 647  TYR   A CG  1 
ATOM   1625 C  CD1 . TYR   A 1 218 ? -36.57800 16.28400  0.23400   1.000 20.75000  ? 647  TYR   A CD1 1 
ATOM   1626 C  CD2 . TYR   A 1 218 ? -36.54900 15.22600  -1.94100  1.000 26.81000  ? 647  TYR   A CD2 1 
ATOM   1627 C  CE1 . TYR   A 1 218 ? -35.77900 17.34000  -0.27400  1.000 22.58000  ? 647  TYR   A CE1 1 
ATOM   1628 C  CE2 . TYR   A 1 218 ? -35.71700 16.31300  -2.45000  1.000 21.35000  ? 647  TYR   A CE2 1 
ATOM   1629 C  CZ  . TYR   A 1 218 ? -35.36400 17.31600  -1.59600  1.000 29.97000  ? 647  TYR   A CZ  1 
ATOM   1630 O  OH  . TYR   A 1 218 ? -34.56900 18.34300  -2.08000  1.000 30.06000  ? 647  TYR   A OH  1 
ATOM   1631 N  N   . GLU   A 1 219 ? -36.76200 13.78800  2.93300   1.000 18.70000  ? 648  GLU   A N   1 
ATOM   1632 C  CA  . GLU   A 1 219 ? -35.99700 14.24200  4.07900   1.000 20.01000  ? 648  GLU   A CA  1 
ATOM   1633 C  C   . GLU   A 1 219 ? -34.95000 13.21500  4.49700   1.000 21.24000  ? 648  GLU   A C   1 
ATOM   1634 O  O   . GLU   A 1 219 ? -33.80900 13.57100  4.82700   1.000 22.50000  ? 648  GLU   A O   1 
ATOM   1635 C  CB  . GLU   A 1 219 ? -36.94100 14.52700  5.25300   1.000 20.24000  ? 648  GLU   A CB  1 
ATOM   1636 C  CG  . GLU   A 1 219 ? -37.97600 15.63500  4.99800   1.000 16.32000  ? 648  GLU   A CG  1 
ATOM   1637 C  CD  . GLU   A 1 219 ? -38.78200 15.79500  6.27800   1.000 18.58000  ? 648  GLU   A CD  1 
ATOM   1638 O  OE1 . GLU   A 1 219 ? -38.26500 16.37900  7.22900   1.000 19.25000  ? 648  GLU   A OE1 1 
ATOM   1639 O  OE2 . GLU   A 1 219 ? -39.88800 15.24700  6.34300   1.000 17.62000  ? 648  GLU   A OE2 1 
ATOM   1640 N  N   . LEU   A 1 220 ? -35.35400 11.94100  4.59200   1.000 21.41000  ? 649  LEU   A N   1 
ATOM   1641 C  CA  . LEU   A 1 220 ? -34.38600 10.92300  4.99200   1.000 20.94000  ? 649  LEU   A CA  1 
ATOM   1642 C  C   . LEU   A 1 220 ? -33.24000 10.80700  3.99300   1.000 21.17000  ? 649  LEU   A C   1 
ATOM   1643 O  O   . LEU   A 1 220 ? -32.07900 10.61600  4.39800   1.000 21.61000  ? 649  LEU   A O   1 
ATOM   1644 C  CB  . LEU   A 1 220 ? -35.07700 9.57300   5.12400   1.000 21.78000  ? 649  LEU   A CB  1 
ATOM   1645 C  CG  . LEU   A 1 220 ? -36.02500 9.50700   6.34300   1.000 19.64000  ? 649  LEU   A CG  1 
ATOM   1646 C  CD1 . LEU   A 1 220 ? -36.98600 8.32000   6.07900   1.000 20.09000  ? 649  LEU   A CD1 1 
ATOM   1647 C  CD2 . LEU   A 1 220 ? -35.29300 9.30900   7.68000   1.000 20.82000  ? 649  LEU   A CD2 1 
ATOM   1648 N  N   . MET   A 1 221 ? -33.55100 10.85100  2.69100   1.000 22.39000  ? 650  MET   A N   1 
ATOM   1649 C  CA  . MET   A 1 221 ? -32.57600 10.46300  1.66600   1.000 25.71000  ? 650  MET   A CA  1 
ATOM   1650 C  C   . MET   A 1 221 ? -31.71800 11.64200  1.21200   1.000 38.14000  ? 650  MET   A C   1 
ATOM   1651 O  O   . MET   A 1 221 ? -30.68600 11.42400  0.55700   1.000 27.89000  ? 650  MET   A O   1 
ATOM   1652 C  CB  . MET   A 1 221 ? -33.30600 9.88400   0.44300   1.000 26.79000  ? 650  MET   A CB  1 
ATOM   1653 C  CG  . MET   A 1 221 ? -33.99700 8.58800   0.78100   1.000 24.47000  ? 650  MET   A CG  1 
ATOM   1654 S  SD  . MET   A 1 221 ? -32.80500 7.30800   1.32400   1.000 32.88000  ? 650  MET   A SD  1 
ATOM   1655 C  CE  . MET   A 1 221 ? -33.78300 6.55900   2.63100   1.000 31.98000  ? 650  MET   A CE  1 
ATOM   1656 N  N   . THR   A 1 222 ? -32.15600 12.88600  1.48400   1.000 25.73000  ? 651  THR   A N   1 
ATOM   1657 C  CA  . THR   A 1 222 ? -31.36600 14.10400  1.24100   1.000 29.87000  ? 651  THR   A CA  1 
ATOM   1658 C  C   . THR   A 1 222 ? -30.83100 14.73900  2.50700   1.000 30.03000  ? 651  THR   A C   1 
ATOM   1659 O  O   . THR   A 1 222 ? -29.89500 15.55200  2.44400   1.000 28.72000  ? 651  THR   A O   1 
ATOM   1660 C  CB  . THR   A 1 222 ? -32.19900 15.20100  0.54300   1.000 24.25000  ? 651  THR   A CB  1 
ATOM   1661 O  OG1 . THR   A 1 222 ? -33.16700 15.74300  1.48000   1.000 22.75000  ? 651  THR   A OG1 1 
ATOM   1662 C  CG2 . THR   A 1 222 ? -32.90100 14.70900  -0.72000  1.000 25.92000  ? 651  THR   A CG2 1 
ATOM   1663 N  N   . GLY   A 1 223 ? -31.43600 14.45700  3.65000   1.000 23.67000  ? 652  GLY   A N   1 
ATOM   1664 C  CA  . GLY   A 1 223 ? -31.11900 15.22200  4.82600   1.000 23.16000  ? 652  GLY   A CA  1 
ATOM   1665 C  C   . GLY   A 1 223 ? -31.74000 16.61600  4.88400   1.000 28.56000  ? 652  GLY   A C   1 
ATOM   1666 O  O   . GLY   A 1 223 ? -31.54000 17.30200  5.88300   1.000 28.35000  ? 652  GLY   A O   1 
ATOM   1667 N  N   . GLN   A 1 224 ? -32.51600 17.03200  3.87400   1.000 25.59000  ? 653  GLN   A N   1 
ATOM   1668 C  CA  . GLN   A 1 224 ? -33.03300 18.39700  3.76700   1.000 25.38000  ? 653  GLN   A CA  1 
ATOM   1669 C  C   . GLN   A 1 224 ? -34.56100 18.42000  3.74100   1.000 22.19000  ? 653  GLN   A C   1 
ATOM   1670 O  O   . GLN   A 1 224 ? -35.20400 17.44400  3.38200   1.000 22.50000  ? 653  GLN   A O   1 
ATOM   1671 C  CB  . GLN   A 1 224 ? -32.52300 19.04300  2.45300   1.000 24.09000  ? 653  GLN   A CB  1 
ATOM   1672 C  CG  . GLN   A 1 224 ? -31.04600 19.21400  2.48900   1.000 31.21000  ? 653  GLN   A CG  1 
ATOM   1673 C  CD  . GLN   A 1 224 ? -30.51500 20.08800  1.35800   1.000 53.14000  ? 653  GLN   A CD  1 
ATOM   1674 O  OE1 . GLN   A 1 224 ? -30.90700 19.93400  0.19900   1.000 54.48000  ? 653  GLN   A OE1 1 
ATOM   1675 N  NE2 . GLN   A 1 224 ? -29.60900 20.99900  1.69300   1.000 67.03000  ? 653  GLN   A NE2 1 
ATOM   1676 N  N   . LEU   A 1 225 ? -35.11300 19.58700  3.99300   1.000 19.96000  ? 654  LEU   A N   1 
ATOM   1677 C  CA  . LEU   A 1 225 ? -36.50200 19.85900  3.66900   1.000 22.95000  ? 654  LEU   A CA  1 
ATOM   1678 C  C   . LEU   A 1 225 ? -36.62100 20.17800  2.17700   1.000 21.92000  ? 654  LEU   A C   1 
ATOM   1679 O  O   . LEU   A 1 225 ? -35.67800 20.69900  1.58000   1.000 27.52000  ? 654  LEU   A O   1 
ATOM   1680 C  CB  . LEU   A 1 225 ? -36.99400 21.03600  4.49000   1.000 24.36000  ? 654  LEU   A CB  1 
ATOM   1681 C  CG  . LEU   A 1 225 ? -37.14600 20.76400  5.99500   1.000 23.53000  ? 654  LEU   A CG  1 
ATOM   1682 C  CD1 . LEU   A 1 225 ? -37.26300 22.07400  6.77700   1.000 21.88000  ? 654  LEU   A CD1 1 
ATOM   1683 C  CD2 . LEU   A 1 225 ? -38.37000 19.82300  6.24800   1.000 21.84000  ? 654  LEU   A CD2 1 
ATOM   1684 N  N   . PRO   A 1 226 ? -37.71600 19.83600  1.53900   1.000 21.42000  ? 655  PRO   A N   1 
ATOM   1685 C  CA  . PRO   A 1 226 ? -37.86000 20.16900  0.11800   1.000 20.36000  ? 655  PRO   A CA  1 
ATOM   1686 C  C   . PRO   A 1 226 ? -37.94300 21.68200  -0.02300  1.000 26.59000  ? 655  PRO   A C   1 
ATOM   1687 O  O   . PRO   A 1 226 ? -38.34000 22.38800  0.91100   1.000 22.09000  ? 655  PRO   A O   1 
ATOM   1688 C  CB  . PRO   A 1 226 ? -39.17600 19.51300  -0.27900  1.000 22.83000  ? 655  PRO   A CB  1 
ATOM   1689 C  CG  . PRO   A 1 226 ? -39.99900 19.55200  1.02000   1.000 21.14000  ? 655  PRO   A CG  1 
ATOM   1690 C  CD  . PRO   A 1 226 ? -38.95200 19.26600  2.11200   1.000 23.29000  ? 655  PRO   A CD  1 
ATOM   1691 N  N   . TYR   A 1 227 ? -37.52500 22.17800  -1.19200  1.000 25.32000  ? 656  TYR   A N   1 
ATOM   1692 C  CA  . TYR   A 1 227 ? -37.67000 23.59600  -1.56600  1.000 26.73000  ? 656  TYR   A CA  1 
ATOM   1693 C  C   . TYR   A 1 227 ? -36.82400 24.53500  -0.72200  1.000 28.61000  ? 656  TYR   A C   1 
ATOM   1694 O  O   . TYR   A 1 227 ? -37.17500 25.72200  -0.54800  1.000 26.78000  ? 656  TYR   A O   1 
ATOM   1695 C  CB  . TYR   A 1 227 ? -39.13500 24.04900  -1.52600  1.000 21.35000  ? 656  TYR   A CB  1 
ATOM   1696 C  CG  . TYR   A 1 227 ? -40.12600 22.99800  -1.97300  1.000 20.41000  ? 656  TYR   A CG  1 
ATOM   1697 C  CD1 . TYR   A 1 227 ? -40.00300 22.39800  -3.21700  1.000 21.80000  ? 656  TYR   A CD1 1 
ATOM   1698 C  CD2 . TYR   A 1 227 ? -41.19400 22.60900  -1.14700  1.000 18.96000  ? 656  TYR   A CD2 1 
ATOM   1699 C  CE1 . TYR   A 1 227 ? -40.90200 21.41700  -3.65600  1.000 24.22000  ? 656  TYR   A CE1 1 
ATOM   1700 C  CE2 . TYR   A 1 227 ? -42.14400 21.66100  -1.58700  1.000 17.54000  ? 656  TYR   A CE2 1 
ATOM   1701 C  CZ  . TYR   A 1 227 ? -41.96100 21.03100  -2.81000  1.000 22.74000  ? 656  TYR   A CZ  1 
ATOM   1702 O  OH  . TYR   A 1 227 ? -42.86200 20.07800  -3.26200  1.000 22.73000  ? 656  TYR   A OH  1 
ATOM   1703 N  N   . SER   A 1 228 ? -35.69300 24.05800  -0.20300  1.000 27.05000  ? 657  SER   A N   1 
ATOM   1704 C  CA  . SER   A 1 228 ? -34.95500 24.88000  0.74700   1.000 28.89000  ? 657  SER   A CA  1 
ATOM   1705 C  C   . SER   A 1 228 ? -34.25500 26.04600  0.04500   1.000 34.14000  ? 657  SER   A C   1 
ATOM   1706 O  O   . SER   A 1 228 ? -33.75300 26.94300  0.71500   1.000 32.62000  ? 657  SER   A O   1 
ATOM   1707 C  CB  . SER   A 1 228 ? -33.93200 24.03600  1.50900   1.000 36.50000  ? 657  SER   A CB  1 
ATOM   1708 O  OG  . SER   A 1 228 ? -33.02800 23.41900  0.60900   1.000 41.20000  ? 657  SER   A OG  1 
ATOM   1709 N  N   . ASN   A 1 229 ? -34.23200 26.05100  -1.28100  1.000 28.63000  ? 658  ASN   A N   1 
ATOM   1710 C  CA  . ASN   A 1 229 ? -33.73800 27.19300  -2.06800  1.000 38.69000  ? 658  ASN   A CA  1 
ATOM   1711 C  C   . ASN   A 1 229 ? -34.80200 28.23700  -2.38000  1.000 42.58000  ? 658  ASN   A C   1 
ATOM   1712 O  O   . ASN   A 1 229 ? -34.48400 29.29300  -2.93800  1.000 40.66000  ? 658  ASN   A O   1 
ATOM   1713 C  CB  . ASN   A 1 229 ? -33.10400 26.65600  -3.35400  1.000 45.30000  ? 658  ASN   A CB  1 
ATOM   1714 C  CG  . ASN   A 1 229 ? -34.10100 25.85000  -4.20600  1.000 56.11000  ? 658  ASN   A CG  1 
ATOM   1715 O  OD1 . ASN   A 1 229 ? -35.02300 25.18700  -3.67300  1.000 36.44000  ? 658  ASN   A OD1 1 
ATOM   1716 N  ND2 . ASN   A 1 229 ? -33.91100 25.87900  -5.51800  1.000 58.13000  ? 658  ASN   A ND2 1 
ATOM   1717 N  N   . ILE   A 1 230 ? -36.04400 27.97800  -2.03900  1.000 33.40000  ? 659  ILE   A N   1 
ATOM   1718 C  CA  . ILE   A 1 230 ? -37.14900 28.90900  -2.20000  1.000 40.30000  ? 659  ILE   A CA  1 
ATOM   1719 C  C   . ILE   A 1 230 ? -37.46500 29.44100  -0.80700  1.000 49.21000  ? 659  ILE   A C   1 
ATOM   1720 O  O   . ILE   A 1 230 ? -38.09300 28.76000  0.01300   1.000 63.43000  ? 659  ILE   A O   1 
ATOM   1721 C  CB  . ILE   A 1 230 ? -38.36000 28.22700  -2.83400  1.000 37.15000  ? 659  ILE   A CB  1 
ATOM   1722 C  CG1 . ILE   A 1 230 ? -38.01200 27.80100  -4.25600  1.000 43.46000  ? 659  ILE   A CG1 1 
ATOM   1723 C  CG2 . ILE   A 1 230 ? -39.57100 29.13000  -2.78600  1.000 34.98000  ? 659  ILE   A CG2 1 
ATOM   1724 C  CD1 . ILE   A 1 230 ? -38.84700 26.65400  -4.71600  1.000 46.07000  ? 659  ILE   A CD1 1 
ATOM   1725 N  N   . ASN   A 1 231 ? -37.04000 30.66700  -0.53400  1.000 55.11000  ? 660  ASN   A N   1 
ATOM   1726 C  CA  . ASN   A 1 231 ? -37.21200 31.25200  0.79900   1.000 83.26000  ? 660  ASN   A CA  1 
ATOM   1727 C  C   . ASN   A 1 231 ? -38.67800 31.47600  1.19700   1.000 78.00000  ? 660  ASN   A C   1 
ATOM   1728 O  O   . ASN   A 1 231 ? -38.99200 31.56100  2.39100   1.000 65.22000  ? 660  ASN   A O   1 
ATOM   1729 C  CB  . ASN   A 1 231 ? -36.47300 32.58100  0.83200   1.000 76.27000  ? 660  ASN   A CB  1 
ATOM   1730 C  CG  . ASN   A 1 231 ? -37.18900 33.63100  0.02400   1.000 87.27000  ? 660  ASN   A CG  1 
ATOM   1731 O  OD1 . ASN   A 1 231 ? -37.56400 33.38300  -1.14000  1.000 61.90000  ? 660  ASN   A OD1 1 
ATOM   1732 N  ND2 . ASN   A 1 231 ? -37.39100 34.80800  0.61900   1.000 88.89000  ? 660  ASN   A ND2 1 
ATOM   1733 N  N   . ASN   A 1 232 ? -39.57900 31.54800  0.23700   1.000 83.16000  ? 661  ASN   A N   1 
ATOM   1734 C  CA  . ASN   A 1 232 ? -40.86500 32.21000  0.39500   1.000 48.79000  ? 661  ASN   A CA  1 
ATOM   1735 C  C   . ASN   A 1 232 ? -41.99900 31.17400  0.40300   1.000 51.35000  ? 661  ASN   A C   1 
ATOM   1736 O  O   . ASN   A 1 232 ? -42.40400 30.66800  -0.64600  1.000 52.19000  ? 661  ASN   A O   1 
ATOM   1737 C  CB  . ASN   A 1 232 ? -40.97900 33.21400  -0.74700  1.000 43.01000  ? 661  ASN   A CB  1 
ATOM   1738 C  CG  . ASN   A 1 232 ? -42.30800 33.96200  -0.76600  1.000 74.92000  ? 661  ASN   A CG  1 
ATOM   1739 O  OD1 . ASN   A 1 232 ? -43.37500 33.37900  -0.57800  1.000 59.10000  ? 661  ASN   A OD1 1 
ATOM   1740 N  ND2 . ASN   A 1 232 ? -42.23900 35.27900  -0.97400  1.000 67.60000  ? 661  ASN   A ND2 1 
ATOM   1741 N  N   . ARG   A 1 233 ? -42.54700 30.86900  1.57600   1.000 63.43000  ? 662  ARG   A N   1 
ATOM   1742 C  CA  . ARG   A 1 233 ? -43.60300 29.84800  1.62800   1.000 60.77000  ? 662  ARG   A CA  1 
ATOM   1743 C  C   . ARG   A 1 233 ? -44.79800 30.21000  0.74300   1.000 61.27000  ? 662  ARG   A C   1 
ATOM   1744 O  O   . ARG   A 1 233 ? -45.66400 29.36200  0.43300   1.000 31.26000  ? 662  ARG   A O   1 
ATOM   1745 C  CB  . ARG   A 1 233 ? -44.07700 29.67300  3.06800   1.000 60.59000  ? 662  ARG   A CB  1 
ATOM   1746 C  CG  . ARG   A 1 233 ? -43.05300 29.04300  4.01200   1.000 64.21000  ? 662  ARG   A CG  1 
ATOM   1747 C  CD  . ARG   A 1 233 ? -42.79800 27.55800  3.76800   1.000 57.65000  ? 662  ARG   A CD  1 
ATOM   1748 N  NE  . ARG   A 1 233 ? -41.58000 27.12200  4.44900   1.000 69.69000  ? 662  ARG   A NE  1 
ATOM   1749 C  CZ  . ARG   A 1 233 ? -41.57100 26.39100  5.56000   1.000 59.08000  ? 662  ARG   A CZ  1 
ATOM   1750 N  NH1 . ARG   A 1 233 ? -42.69700 26.01200  6.14800   1.000 57.05000  ? 662  ARG   A NH1 1 
ATOM   1751 N  NH2 . ARG   A 1 233 ? -40.40300 26.03900  6.10300   1.000 63.17000  ? 662  ARG   A NH2 1 
ATOM   1752 N  N   . ASP   A 1 234 ? -44.86500 31.44900  0.31100   1.000 50.50000  ? 663  ASP   A N   1 
ATOM   1753 C  CA  . ASP   A 1 234 ? -46.08500 31.85500  -0.32000  1.000 44.41000  ? 663  ASP   A CA  1 
ATOM   1754 C  C   . ASP   A 1 234 ? -45.94300 31.45900  -1.79900  1.000 28.91000  ? 663  ASP   A C   1 
ATOM   1755 O  O   . ASP   A 1 234 ? -46.90500 31.03700  -2.45400  1.000 39.99000  ? 663  ASP   A O   1 
ATOM   1756 C  CB  . ASP   A 1 234 ? -46.23700 33.36300  -0.05900  1.000 64.02000  ? 663  ASP   A CB  1 
ATOM   1757 C  CG  . ASP   A 1 234 ? -46.57100 33.70300  1.40300   1.000 74.98000  ? 663  ASP   A CG  1 
ATOM   1758 O  OD1 . ASP   A 1 234 ? -46.96400 32.84300  2.19800   1.000 60.89000  ? 663  ASP   A OD1 1 
ATOM   1759 O  OD2 . ASP   A 1 234 ? -46.43400 34.89900  1.76600   1.000 80.61000  ? 663  ASP   A OD2 1 
ATOM   1760 N  N   . GLN   A 1 235 ? -44.70400 31.42800  -2.27600  1.000 32.67000  ? 664  GLN   A N   1 
ATOM   1761 C  CA  . GLN   A 1 235 ? -44.42100 30.90800  -3.61000  1.000 35.84000  ? 664  GLN   A CA  1 
ATOM   1762 C  C   . GLN   A 1 235 ? -44.52600 29.37400  -3.63200  1.000 33.87000  ? 664  GLN   A C   1 
ATOM   1763 O  O   . GLN   A 1 235 ? -44.99500 28.77500  -4.62400  1.000 28.03000  ? 664  GLN   A O   1 
ATOM   1764 C  CB  . GLN   A 1 235 ? -43.03600 31.41100  -4.01500  1.000 36.69000  ? 664  GLN   A CB  1 
ATOM   1765 C  CG  . GLN   A 1 235 ? -42.43000 30.80300  -5.21400  1.000 37.49000  ? 664  GLN   A CG  1 
ATOM   1766 C  CD  . GLN   A 1 235 ? -41.15600 31.55300  -5.63500  1.000 52.15000  ? 664  GLN   A CD  1 
ATOM   1767 O  OE1 . GLN   A 1 235 ? -40.19100 30.95900  -6.10800  1.000 41.46000  ? 664  GLN   A OE1 1 
ATOM   1768 N  NE2 . GLN   A 1 235 ? -41.12600 32.84900  -5.35900  1.000 55.16000  ? 664  GLN   A NE2 1 
ATOM   1769 N  N   . ILE   A 1 236 ? -44.10600 28.72300  -2.54200  1.000 26.85000  ? 665  ILE   A N   1 
ATOM   1770 C  CA  . ILE   A 1 236 ? -44.25000 27.25900  -2.43700  1.000 25.15000  ? 665  ILE   A CA  1 
ATOM   1771 C  C   . ILE   A 1 236 ? -45.70700 26.84400  -2.55000  1.000 25.62000  ? 665  ILE   A C   1 
ATOM   1772 O  O   . ILE   A 1 236 ? -46.05000 25.94500  -3.33100  1.000 24.59000  ? 665  ILE   A O   1 
ATOM   1773 C  CB  . ILE   A 1 236 ? -43.62200 26.74000  -1.13700  1.000 26.21000  ? 665  ILE   A CB  1 
ATOM   1774 C  CG1 . ILE   A 1 236 ? -42.11900 27.00100  -1.18100  1.000 29.20000  ? 665  ILE   A CG1 1 
ATOM   1775 C  CG2 . ILE   A 1 236 ? -43.90400 25.23200  -1.00700  1.000 27.85000  ? 665  ILE   A CG2 1 
ATOM   1776 C  CD1 . ILE   A 1 236 ? -41.39300 26.75900  0.18700   1.000 31.45000  ? 665  ILE   A CD1 1 
ATOM   1777 N  N   . ILE   A 1 237 ? -46.59900 27.47000  -1.76700  1.000 25.30000  ? 666  ILE   A N   1 
ATOM   1778 C  CA  . ILE   A 1 237 ? -47.99600 27.03200  -1.82300  1.000 24.36000  ? 666  ILE   A CA  1 
ATOM   1779 C  C   . ILE   A 1 237 ? -48.60200 27.24600  -3.21500  1.000 26.84000  ? 666  ILE   A C   1 
ATOM   1780 O  O   . ILE   A 1 237 ? -49.34600 26.40600  -3.72100  1.000 21.47000  ? 666  ILE   A O   1 
ATOM   1781 C  CB  . ILE   A 1 237 ? -48.82800 27.72300  -0.72000  1.000 25.70000  ? 666  ILE   A CB  1 
ATOM   1782 C  CG1 . ILE   A 1 237 ? -50.30400 27.37900  -0.88800  1.000 34.02000  ? 666  ILE   A CG1 1 
ATOM   1783 C  CG2 . ILE   A 1 237 ? -48.70000 29.22000  -0.75100  1.000 31.34000  ? 666  ILE   A CG2 1 
ATOM   1784 C  CD1 . ILE   A 1 237 ? -51.00700 27.22400  0.46300   1.000 39.09000  ? 666  ILE   A CD1 1 
ATOM   1785 N  N   . ALA   A 1 238 ? -48.32400 28.38200  -3.85200  1.000 23.79000  ? 667  ALA   A N   1 
ATOM   1786 C  CA  . ALA   A 1 238 ? -48.90100 28.63900  -5.16400  1.000 21.59000  ? 667  ALA   A CA  1 
ATOM   1787 C  C   . ALA   A 1 238 ? -48.32100 27.70600  -6.20800  1.000 18.13000  ? 667  ALA   A C   1 
ATOM   1788 O  O   . ALA   A 1 238 ? -49.05200 27.16200  -7.04500  1.000 22.33000  ? 667  ALA   A O   1 
ATOM   1789 C  CB  . ALA   A 1 238 ? -48.64900 30.11600  -5.56200  1.000 29.56000  ? 667  ALA   A CB  1 
ATOM   1790 N  N   A MET   A 1 239 ? -46.99800 27.49700  -6.16900  0.504 20.93000  ? 668  MET   A N   1 
ATOM   1791 N  N   B MET   A 1 239 ? -47.00100 27.52000  -6.18400  0.496 20.95000  ? 668  MET   A N   1 
ATOM   1792 C  CA  A MET   A 1 239 ? -46.34100 26.73500  -7.23200  0.504 22.27000  ? 668  MET   A CA  1 
ATOM   1793 C  CA  B MET   A 1 239 ? -46.37800 26.71800  -7.23000  0.496 22.26000  ? 668  MET   A CA  1 
ATOM   1794 C  C   A MET   A 1 239 ? -46.60300 25.23300  -7.08500  0.504 23.69000  ? 668  MET   A C   1 
ATOM   1795 C  C   B MET   A 1 239 ? -46.75200 25.25100  -7.07100  0.496 23.75000  ? 668  MET   A C   1 
ATOM   1796 O  O   A MET   A 1 239 ? -46.79500 24.52700  -8.08300  0.504 22.89000  ? 668  MET   A O   1 
ATOM   1797 O  O   B MET   A 1 239 ? -47.18200 24.59700  -8.03200  0.496 20.85000  ? 668  MET   A O   1 
ATOM   1798 C  CB  A MET   A 1 239 ? -44.83100 27.02300  -7.23200  0.504 26.10000  ? 668  MET   A CB  1 
ATOM   1799 C  CB  B MET   A 1 239 ? -44.86000 26.89600  -7.19800  0.496 25.93000  ? 668  MET   A CB  1 
ATOM   1800 C  CG  A MET   A 1 239 ? -44.39900 28.31700  -8.02400  0.504 28.33000  ? 668  MET   A CG  1 
ATOM   1801 C  CG  B MET   A 1 239 ? -44.42200 28.28700  -7.64800  0.496 29.53000  ? 668  MET   A CG  1 
ATOM   1802 S  SD  A MET   A 1 239 ? -44.81100 28.36800  -9.79700  0.504 24.77000  ? 668  MET   A SD  1 
ATOM   1803 S  SD  B MET   A 1 239 ? -42.64100 28.42700  -7.59900  0.496 36.91000  ? 668  MET   A SD  1 
ATOM   1804 C  CE  A MET   A 1 239 ? -43.36800 27.55000  -10.47000 0.504 30.79000  ? 668  MET   A CE  1 
ATOM   1805 C  CE  B MET   A 1 239 ? -42.14400 27.45900  -9.02000  0.496 31.27000  ? 668  MET   A CE  1 
ATOM   1806 N  N   . VAL   A 1 240 ? -46.63500 24.72300  -5.85000  1.000 22.40000  ? 669  VAL   A N   1 
ATOM   1807 C  CA  . VAL   A 1 240 ? -46.97800 23.31100  -5.70200  1.000 18.91000  ? 669  VAL   A CA  1 
ATOM   1808 C  C   . VAL   A 1 240 ? -48.44900 23.09100  -6.03400  1.000 18.45000  ? 669  VAL   A C   1 
ATOM   1809 O  O   . VAL   A 1 240 ? -48.80900 22.12400  -6.72700  1.000 20.51000  ? 669  VAL   A O   1 
ATOM   1810 C  CB  . VAL   A 1 240 ? -46.62100 22.79900  -4.29300  1.000 21.26000  ? 669  VAL   A CB  1 
ATOM   1811 C  CG1 . VAL   A 1 240 ? -47.10600 21.32200  -4.18800  1.000 21.40000  ? 669  VAL   A CG1 1 
ATOM   1812 C  CG2 . VAL   A 1 240 ? -45.13500 22.93400  -4.06500  1.000 20.32000  ? 669  VAL   A CG2 1 
ATOM   1813 N  N   . GLY   A 1 241 ? -49.34000 23.98600  -5.56200  1.000 20.41000  ? 670  GLY   A N   1 
ATOM   1814 C  CA  . GLY   A 1 241 ? -50.76600 23.81000  -5.86900  1.000 18.05000  ? 670  GLY   A CA  1 
ATOM   1815 C  C   . GLY   A 1 241 ? -51.10600 23.87900  -7.35000  1.000 24.57000  ? 670  GLY   A C   1 
ATOM   1816 O  O   . GLY   A 1 241 ? -52.08700 23.25600  -7.81500  1.000 24.67000  ? 670  GLY   A O   1 
ATOM   1817 N  N   . ALA   A 1 242 ? -50.31100 24.61900  -8.12600  1.000 21.59000  ? 671  ALA   A N   1 
ATOM   1818 C  CA  . ALA   A 1 242 ? -50.55100 24.75500  -9.56600  1.000 23.16000  ? 671  ALA   A CA  1 
ATOM   1819 C  C   . ALA   A 1 242 ? -49.93500 23.61900  -10.35700 1.000 27.59000  ? 671  ALA   A C   1 
ATOM   1820 O  O   . ALA   A 1 242 ? -50.06200 23.59300  -11.59800 1.000 27.06000  ? 671  ALA   A O   1 
ATOM   1821 C  CB  . ALA   A 1 242 ? -49.97800 26.07400  -10.11000 1.000 24.25000  ? 671  ALA   A CB  1 
ATOM   1822 N  N   . GLY   A 1 243 ? -49.25300 22.71100  -9.67400  1.000 23.54000  ? 672  GLY   A N   1 
ATOM   1823 C  CA  . GLY   A 1 243 ? -48.56100 21.63500  -10.34200 1.000 29.24000  ? 672  GLY   A CA  1 
ATOM   1824 C  C   . GLY   A 1 243 ? -47.22500 21.99500  -10.94100 1.000 27.01000  ? 672  GLY   A C   1 
ATOM   1825 O  O   . GLY   A 1 243 ? -46.73700 21.23300  -11.78300 1.000 36.50000  ? 672  GLY   A O   1 
ATOM   1826 N  N   . ALA   A 1 244 ? -46.62200 23.12800  -10.55600 1.000 24.89000  ? 673  ALA   A N   1 
ATOM   1827 C  CA  . ALA   A 1 244 ? -45.41200 23.65800  -11.18600 1.000 30.50000  ? 673  ALA   A CA  1 
ATOM   1828 C  C   . ALA   A 1 244 ? -44.16600 23.53900  -10.32500 1.000 30.07000  ? 673  ALA   A C   1 
ATOM   1829 O  O   . ALA   A 1 244 ? -43.14200 24.17800  -10.62500 1.000 34.39000  ? 673  ALA   A O   1 
ATOM   1830 C  CB  . ALA   A 1 244 ? -45.59200 25.14200  -11.56500 1.000 28.19000  ? 673  ALA   A CB  1 
ATOM   1831 N  N   . LEU   A 1 245 ? -44.22300 22.79500  -9.23000  1.000 29.96000  ? 674  LEU   A N   1 
ATOM   1832 C  CA  . LEU   A 1 245 ? -43.07400 22.67500  -8.36100  1.000 26.63000  ? 674  LEU   A CA  1 
ATOM   1833 C  C   . LEU   A 1 245 ? -43.17900 21.34200  -7.66000  1.000 32.82000  ? 674  LEU   A C   1 
ATOM   1834 O  O   . LEU   A 1 245 ? -44.26300 20.95900  -7.20200  1.000 28.99000  ? 674  LEU   A O   1 
ATOM   1835 C  CB  . LEU   A 1 245 ? -43.00800 23.78800  -7.32000  1.000 24.82000  ? 674  LEU   A CB  1 
ATOM   1836 C  CG  . LEU   A 1 245 ? -41.88400 23.73600  -6.29500  1.000 22.28000  ? 674  LEU   A CG  1 
ATOM   1837 C  CD1 . LEU   A 1 245 ? -40.47700 23.78100  -6.99300  1.000 32.56000  ? 674  LEU   A CD1 1 
ATOM   1838 C  CD2 . LEU   A 1 245 ? -42.01600 24.89000  -5.33200  1.000 24.87000  ? 674  LEU   A CD2 1 
ATOM   1839 N  N   . SER   A 1 246 ? -42.05600 20.64600  -7.59200  1.000 26.21000  ? 675  SER   A N   1 
ATOM   1840 C  CA  . SER   A 1 246 ? -41.99200 19.35500  -6.92700  1.000 27.95000  ? 675  SER   A CA  1 
ATOM   1841 C  C   . SER   A 1 246 ? -40.57500 19.20100  -6.41000  1.000 33.12000  ? 675  SER   A C   1 
ATOM   1842 O  O   . SER   A 1 246 ? -39.67700 19.95000  -6.81800  1.000 24.43000  ? 675  SER   A O   1 
ATOM   1843 C  CB  . SER   A 1 246 ? -42.37200 18.20700  -7.87100  1.000 31.82000  ? 675  SER   A CB  1 
ATOM   1844 O  OG  . SER   A 1 246 ? -41.48900 18.14500  -8.97700  1.000 39.52000  ? 675  SER   A OG  1 
ATOM   1845 N  N   . PRO   A 1 247 ? -40.34300 18.29700  -5.47400  1.000 24.46000  ? 676  PRO   A N   1 
ATOM   1846 C  CA  . PRO   A 1 247 ? -39.01900 18.24700  -4.86900  1.000 22.63000  ? 676  PRO   A CA  1 
ATOM   1847 C  C   . PRO   A 1 247 ? -37.97600 17.85600  -5.89900  1.000 24.40000  ? 676  PRO   A C   1 
ATOM   1848 O  O   . PRO   A 1 247 ? -38.24400 17.07700  -6.82500  1.000 28.35000  ? 676  PRO   A O   1 
ATOM   1849 C  CB  . PRO   A 1 247 ? -39.14900 17.17500  -3.77900  1.000 25.06000  ? 676  PRO   A CB  1 
ATOM   1850 C  CG  . PRO   A 1 247 ? -40.64200 17.21300  -3.44700  1.000 21.93000  ? 676  PRO   A CG  1 
ATOM   1851 C  CD  . PRO   A 1 247 ? -41.33600 17.47200  -4.76100  1.000 22.43000  ? 676  PRO   A CD  1 
ATOM   1852 N  N   . ASP   A 1 248 ? -36.79100 18.40600  -5.70100  1.000 24.03000  ? 677  ASP   A N   1 
ATOM   1853 C  CA  . ASP   A 1 248 ? -35.65400 18.18400  -6.61000  1.000 27.08000  ? 677  ASP   A CA  1 
ATOM   1854 C  C   . ASP   A 1 248 ? -34.93400 16.88900  -6.24100  1.000 24.56000  ? 677  ASP   A C   1 
ATOM   1855 O  O   . ASP   A 1 248 ? -34.06200 16.87800  -5.36900  1.000 27.18000  ? 677  ASP   A O   1 
ATOM   1856 C  CB  . ASP   A 1 248 ? -34.70200 19.37100  -6.54600  1.000 29.74000  ? 677  ASP   A CB  1 
ATOM   1857 C  CG  . ASP   A 1 248 ? -33.55900 19.24500  -7.54100  1.000 42.47000  ? 677  ASP   A CG  1 
ATOM   1858 O  OD1 . ASP   A 1 248 ? -33.48000 18.20100  -8.23100  1.000 31.40000  ? 677  ASP   A OD1 1 
ATOM   1859 O  OD2 . ASP   A 1 248 ? -32.74400 20.17400  -7.59500  1.000 41.80000  ? 677  ASP   A OD2 1 
ATOM   1860 N  N   . LEU   A 1 249 ? -35.28200 15.79900  -6.94000  1.000 25.26000  ? 678  LEU   A N   1 
ATOM   1861 C  CA  . LEU   A 1 249 ? -34.72700 14.49900  -6.57000  1.000 30.17000  ? 678  LEU   A CA  1 
ATOM   1862 C  C   . LEU   A 1 249 ? -33.24800 14.38500  -6.89500  1.000 38.18000  ? 678  LEU   A C   1 
ATOM   1863 O  O   . LEU   A 1 249 ? -32.59400 13.45900  -6.40800  1.000 30.99000  ? 678  LEU   A O   1 
ATOM   1864 C  CB  . LEU   A 1 249 ? -35.49400 13.36900  -7.24200  1.000 35.67000  ? 678  LEU   A CB  1 
ATOM   1865 C  CG  . LEU   A 1 249 ? -36.98000 13.29800  -6.89700  1.000 36.12000  ? 678  LEU   A CG  1 
ATOM   1866 C  CD1 . LEU   A 1 249 ? -37.56700 11.93100  -7.28700  1.000 38.71000  ? 678  LEU   A CD1 1 
ATOM   1867 C  CD2 . LEU   A 1 249 ? -37.18400 13.57100  -5.42300  1.000 36.31000  ? 678  LEU   A CD2 1 
ATOM   1868 N  N   . SER   A 1 250 ? -32.69100 15.32800  -7.65700  1.000 32.49000  ? 679  SER   A N   1 
ATOM   1869 C  CA  . SER   A 1 250 ? -31.24400 15.32100  -7.83400  1.000 36.79000  ? 679  SER   A CA  1 
ATOM   1870 C  C   . SER   A 1 250 ? -30.49400 15.57400  -6.52100  1.000 37.77000  ? 679  SER   A C   1 
ATOM   1871 O  O   . SER   A 1 250 ? -29.28100 15.36000  -6.46200  1.000 34.91000  ? 679  SER   A O   1 
ATOM   1872 C  CB  . SER   A 1 250 ? -30.89400 16.33300  -8.95200  1.000 32.23000  ? 679  SER   A CB  1 
ATOM   1873 O  OG  . SER   A 1 250 ? -30.71400 17.66300  -8.45200  1.000 35.41000  ? 679  SER   A OG  1 
ATOM   1874 N  N   . LYS   A 1 251 ? -31.17800 15.95700  -5.43500  1.000 29.13000  ? 680  LYS   A N   1 
ATOM   1875 C  CA  . LYS   A 1 251 ? -30.50000 16.14400  -4.15700  1.000 29.06000  ? 680  LYS   A CA  1 
ATOM   1876 C  C   . LYS   A 1 251 ? -30.32600 14.83700  -3.37700  1.000 26.83000  ? 680  LYS   A C   1 
ATOM   1877 O  O   . LYS   A 1 251 ? -29.70400 14.83100  -2.31200  1.000 31.81000  ? 680  LYS   A O   1 
ATOM   1878 C  CB  . LYS   A 1 251 ? -31.29200 17.12900  -3.29700  1.000 35.67000  ? 680  LYS   A CB  1 
ATOM   1879 C  CG  . LYS   A 1 251 ? -31.54100 18.49700  -3.88600  1.000 41.54000  ? 680  LYS   A CG  1 
ATOM   1880 C  CD  . LYS   A 1 251 ? -30.57100 19.54700  -3.40800  1.000 57.57000  ? 680  LYS   A CD  1 
ATOM   1881 C  CE  . LYS   A 1 251 ? -30.77000 20.87200  -4.19600  1.000 68.48000  ? 680  LYS   A CE  1 
ATOM   1882 N  NZ  . LYS   A 1 251 ? -29.68400 21.16700  -5.18600  1.000 68.20000  ? 680  LYS   A NZ  1 
ATOM   1883 N  N   . VAL   A 1 252 ? -30.93500 13.75300  -3.83600  1.000 27.34000  ? 681  VAL   A N   1 
ATOM   1884 C  CA  . VAL   A 1 252 ? -30.79900 12.49600  -3.11300  1.000 31.01000  ? 681  VAL   A CA  1 
ATOM   1885 C  C   . VAL   A 1 252 ? -29.32400 12.11800  -2.99800  1.000 46.88000  ? 681  VAL   A C   1 
ATOM   1886 O  O   . VAL   A 1 252 ? -28.54000 12.31900  -3.92800  1.000 44.16000  ? 681  VAL   A O   1 
ATOM   1887 C  CB  . VAL   A 1 252 ? -31.65000 11.43800  -3.83100  1.000 42.54000  ? 681  VAL   A CB  1 
ATOM   1888 C  CG1 . VAL   A 1 252 ? -31.63500 10.22900  -3.07300  1.000 40.55000  ? 681  VAL   A CG1 1 
ATOM   1889 C  CG2 . VAL   A 1 252 ? -33.11500 11.90400  -3.83000  1.000 32.98000  ? 681  VAL   A CG2 1 
ATOM   1890 N  N   . ARG   A 1 253 ? -28.92900 11.63500  -1.82400  1.000 32.59000  ? 682  ARG   A N   1 
ATOM   1891 C  CA  . ARG   A 1 253 ? -27.54200 11.26500  -1.56400  1.000 46.65000  ? 682  ARG   A CA  1 
ATOM   1892 C  C   . ARG   A 1 253 ? -27.05800 10.22800  -2.57100  1.000 50.01000  ? 682  ARG   A C   1 
ATOM   1893 O  O   . ARG   A 1 253 ? -27.84700 9.46300   -3.14100  1.000 40.17000  ? 682  ARG   A O   1 
ATOM   1894 C  CB  . ARG   A 1 253 ? -27.40500 10.65000  -0.18600  1.000 45.14000  ? 682  ARG   A CB  1 
ATOM   1895 C  CG  . ARG   A 1 253 ? -26.84200 11.56800  0.84000   1.000 55.12000  ? 682  ARG   A CG  1 
ATOM   1896 C  CD  . ARG   A 1 253 ? -27.52300 11.21200  2.10500   1.000 61.45000  ? 682  ARG   A CD  1 
ATOM   1897 N  NE  . ARG   A 1 253 ? -27.47100 12.29400  3.07000   1.000 77.71000  ? 682  ARG   A NE  1 
ATOM   1898 C  CZ  . ARG   A 1 253 ? -28.31700 12.37400  4.08200   1.000 62.69000  ? 682  ARG   A CZ  1 
ATOM   1899 N  NH1 . ARG   A 1 253 ? -29.25900 11.45300  4.25700   1.000 48.02000  ? 682  ARG   A NH1 1 
ATOM   1900 N  NH2 . ARG   A 1 253 ? -28.23600 13.40600  4.91900   1.000 46.12000  ? 682  ARG   A NH2 1 
ATOM   1901 N  N   . SER   A 1 254 ? -25.73200 10.18000  -2.76600  1.000 49.74000  ? 683  SER   A N   1 
ATOM   1902 C  CA  . SER   A 1 254 ? -25.17900 9.27400   -3.77600  1.000 53.37000  ? 683  SER   A CA  1 
ATOM   1903 C  C   . SER   A 1 254 ? -25.43100 7.80900   -3.41100  1.000 38.72000  ? 683  SER   A C   1 
ATOM   1904 O  O   . SER   A 1 254 ? -25.70200 6.98700   -4.29800  1.000 43.17000  ? 683  SER   A O   1 
ATOM   1905 C  CB  . SER   A 1 254 ? -23.68200 9.56200   -3.97500  1.000 42.48000  ? 683  SER   A CB  1 
ATOM   1906 O  OG  . SER   A 1 254 ? -22.97400 9.53500   -2.73900  1.000 53.04000  ? 683  SER   A OG  1 
ATOM   1907 N  N   . ASN   A 1 255 ? -25.45200 7.48900   -2.11300  1.000 36.39000  ? 684  ASN   A N   1 
ATOM   1908 C  CA  . ASN   A 1 255 ? -25.67000 6.12900   -1.64600  1.000 41.06000  ? 684  ASN   A CA  1 
ATOM   1909 C  C   . ASN   A 1 255 ? -27.14200 5.75000   -1.49600  1.000 33.91000  ? 684  ASN   A C   1 
ATOM   1910 O  O   . ASN   A 1 255 ? -27.43400 4.66800   -0.97900  1.000 32.94000  ? 684  ASN   A O   1 
ATOM   1911 C  CB  . ASN   A 1 255 ? -24.95200 5.89000   -0.30700  1.000 47.79000  ? 684  ASN   A CB  1 
ATOM   1912 C  CG  . ASN   A 1 255 ? -25.43200 6.83000   0.82100   1.000 50.91000  ? 684  ASN   A CG  1 
ATOM   1913 O  OD1 . ASN   A 1 255 ? -26.17300 7.78500   0.59300   1.000 52.86000  ? 684  ASN   A OD1 1 
ATOM   1914 N  ND2 . ASN   A 1 255 ? -25.07500 6.48800   2.05800   1.000 62.31000  ? 684  ASN   A ND2 1 
ATOM   1915 N  N   . CYS   A 1 256 ? -28.07600 6.58700   -1.92600  1.000 36.12000  ? 685  CYS   A N   1 
ATOM   1916 C  CA  . CYS   A 1 256 ? -29.46300 6.17800   -1.87500  1.000 29.11000  ? 685  CYS   A CA  1 
ATOM   1917 C  C   . CYS   A 1 256 ? -29.71400 5.14300   -2.96100  1.000 32.70000  ? 685  CYS   A C   1 
ATOM   1918 O  O   . CYS   A 1 256 ? -29.37900 5.39000   -4.12300  1.000 31.40000  ? 685  CYS   A O   1 
ATOM   1919 C  CB  . CYS   A 1 256 ? -30.37400 7.37900   -2.06100  1.000 31.57000  ? 685  CYS   A CB  1 
ATOM   1920 S  SG  . CYS   A 1 256 ? -32.17800 6.98500   -2.18400  1.000 34.01000  ? 685  CYS   A SG  1 
ATOM   1921 N  N   . PRO   A 1 257 ? -30.25400 3.97100   -2.63500  1.000 28.93000  ? 686  PRO   A N   1 
ATOM   1922 C  CA  . PRO   A 1 257 ? -30.53800 2.98000   -3.68700  1.000 24.90000  ? 686  PRO   A CA  1 
ATOM   1923 C  C   . PRO   A 1 257 ? -31.44100 3.52800   -4.79100  1.000 34.50000  ? 686  PRO   A C   1 
ATOM   1924 O  O   . PRO   A 1 257 ? -32.43800 4.21400   -4.54100  1.000 28.77000  ? 686  PRO   A O   1 
ATOM   1925 C  CB  . PRO   A 1 257 ? -31.22300 1.83000   -2.93600  1.000 28.89000  ? 686  PRO   A CB  1 
ATOM   1926 C  CG  . PRO   A 1 257 ? -30.76800 1.99200   -1.42600  1.000 29.96000  ? 686  PRO   A CG  1 
ATOM   1927 C  CD  . PRO   A 1 257 ? -30.57300 3.48900   -1.26900  1.000 33.39000  ? 686  PRO   A CD  1 
ATOM   1928 N  N   . LYS   A 1 258 ? -31.09600 3.20200   -6.03900  1.000 29.51000  ? 687  LYS   A N   1 
ATOM   1929 C  CA  . LYS   A 1 258 ? -31.94200 3.60400   -7.16500  1.000 28.13000  ? 687  LYS   A CA  1 
ATOM   1930 C  C   . LYS   A 1 258 ? -33.40900 3.23600   -6.96100  1.000 27.59000  ? 687  LYS   A C   1 
ATOM   1931 O  O   . LYS   A 1 258 ? -34.32500 3.99400   -7.35400  1.000 28.55000  ? 687  LYS   A O   1 
ATOM   1932 C  CB  . LYS   A 1 258 ? -31.43600 2.95900   -8.46600  1.000 34.09000  ? 687  LYS   A CB  1 
ATOM   1933 C  CG  . LYS   A 1 258 ? -30.00400 3.26100   -8.81700  1.000 39.04000  ? 687  LYS   A CG  1 
ATOM   1934 C  CD  . LYS   A 1 258 ? -29.89600 3.21800   -10.37800 1.000 59.79000  ? 687  LYS   A CD  1 
ATOM   1935 C  CE  . LYS   A 1 258 ? -28.49400 2.91100   -10.90900 1.000 64.87000  ? 687  LYS   A CE  1 
ATOM   1936 N  NZ  . LYS   A 1 258 ? -27.63900 2.16800   -9.93300  1.000 72.14000  ? 687  LYS   A NZ  1 
ATOM   1937 N  N   . ALA   A 1 259 ? -33.65700 2.04400   -6.41100  1.000 24.86000  ? 688  ALA   A N   1 
ATOM   1938 C  CA  . ALA   A 1 259 ? -35.02000 1.61000   -6.20200  1.000 26.13000  ? 688  ALA   A CA  1 
ATOM   1939 C  C   . ALA   A 1 259 ? -35.74200 2.51400   -5.18700  1.000 22.22000  ? 688  ALA   A C   1 
ATOM   1940 O  O   . ALA   A 1 259 ? -36.95500 2.73200   -5.31200  1.000 25.01000  ? 688  ALA   A O   1 
ATOM   1941 C  CB  . ALA   A 1 259 ? -35.06800 0.15100   -5.74600  1.000 26.61000  ? 688  ALA   A CB  1 
ATOM   1942 N  N   . MET   A 1 260 ? -35.00200 3.06900   -4.22900  1.000 22.91000  ? 689  MET   A N   1 
ATOM   1943 C  CA  . MET   A 1 260 ? -35.63200 3.99700   -3.29200  1.000 25.28000  ? 689  MET   A CA  1 
ATOM   1944 C  C   . MET   A 1 260 ? -35.91900 5.32000   -4.00400  1.000 25.28000  ? 689  MET   A C   1 
ATOM   1945 O  O   . MET   A 1 260 ? -36.94400 5.95900   -3.74300  1.000 24.46000  ? 689  MET   A O   1 
ATOM   1946 C  CB  . MET   A 1 260 ? -34.74100 4.23700   -2.07600  1.000 24.68000  ? 689  MET   A CB  1 
ATOM   1947 C  CG  . MET   A 1 260 ? -35.22800 5.31900   -1.06300  1.000 24.90000  ? 689  MET   A CG  1 
ATOM   1948 S  SD  . MET   A 1 260 ? -36.88000 4.95200   -0.38700  1.000 29.08000  ? 689  MET   A SD  1 
ATOM   1949 C  CE  . MET   A 1 260 ? -36.49700 3.73100   0.81100   1.000 27.28000  ? 689  MET   A CE  1 
ATOM   1950 N  N   . LYS   A 1 261 ? -35.00800 5.78000   -4.87400  1.000 24.03000  ? 690  LYS   A N   1 
ATOM   1951 C  CA  . LYS   A 1 261 ? -35.29500 7.00800   -5.62100  1.000 20.92000  ? 690  LYS   A CA  1 
ATOM   1952 C  C   . LYS   A 1 261 ? -36.49800 6.82100   -6.51200  1.000 24.92000  ? 690  LYS   A C   1 
ATOM   1953 O  O   . LYS   A 1 261 ? -37.35000 7.72100   -6.63500  1.000 23.04000  ? 690  LYS   A O   1 
ATOM   1954 C  CB  . LYS   A 1 261 ? -34.07600 7.43500   -6.44700  1.000 25.84000  ? 690  LYS   A CB  1 
ATOM   1955 C  CG  . LYS   A 1 261 ? -34.15200 8.82500   -6.99600  1.000 31.79000  ? 690  LYS   A CG  1 
ATOM   1956 C  CD  . LYS   A 1 261 ? -32.78700 9.27100   -7.54300  1.000 39.41000  ? 690  LYS   A CD  1 
ATOM   1957 C  CE  . LYS   A 1 261 ? -32.93300 10.53500  -8.37500  1.000 49.00000  ? 690  LYS   A CE  1 
ATOM   1958 N  NZ  . LYS   A 1 261 ? -31.60800 11.07900  -8.81400  1.000 46.94000  ? 690  LYS   A NZ  1 
ATOM   1959 N  N   . ARG   A 1 262 ? -36.60100 5.66300   -7.14900  1.000 23.87000  ? 691  ARG   A N   1 
ATOM   1960 C  CA  . ARG   A 1 262 ? -37.76200 5.40000   -7.98700  1.000 20.48000  ? 691  ARG   A CA  1 
ATOM   1961 C  C   . ARG   A 1 262 ? -39.04000 5.40500   -7.14800  1.000 24.06000  ? 691  ARG   A C   1 
ATOM   1962 O  O   . ARG   A 1 262 ? -40.07200 5.93800   -7.56700  1.000 24.65000  ? 691  ARG   A O   1 
ATOM   1963 C  CB  . ARG   A 1 262 ? -37.62400 4.05700   -8.71000  1.000 26.05000  ? 691  ARG   A CB  1 
ATOM   1964 C  CG  . ARG   A 1 262 ? -36.55700 4.10500   -9.83500  1.000 29.15000  ? 691  ARG   A CG  1 
ATOM   1965 C  CD  . ARG   A 1 262 ? -36.78100 2.96500   -10.83100 1.000 33.61000  ? 691  ARG   A CD  1 
ATOM   1966 N  NE  . ARG   A 1 262 ? -36.62900 1.64900   -10.21700 1.000 31.16000  ? 691  ARG   A NE  1 
ATOM   1967 C  CZ  . ARG   A 1 262 ? -35.46400 1.04000   -10.02700 1.000 39.89000  ? 691  ARG   A CZ  1 
ATOM   1968 N  NH1 . ARG   A 1 262 ? -34.32600 1.57800   -10.43900 1.000 35.10000  ? 691  ARG   A NH1 1 
ATOM   1969 N  NH2 . ARG   A 1 262 ? -35.43800 -0.11600  -9.36900  1.000 38.31000  ? 691  ARG   A NH2 1 
ATOM   1970 N  N   . LEU   A 1 263 ? -38.98900 4.78700   -5.97700  1.000 21.60000  ? 692  LEU   A N   1 
ATOM   1971 C  CA  . LEU   A 1 263 ? -40.17300 4.73000   -5.10600  1.000 24.07000  ? 692  LEU   A CA  1 
ATOM   1972 C  C   . LEU   A 1 263 ? -40.60300 6.13300   -4.66100  1.000 18.57000  ? 692  LEU   A C   1 
ATOM   1973 O  O   . LEU   A 1 263 ? -41.79200 6.46900   -4.68800  1.000 21.43000  ? 692  LEU   A O   1 
ATOM   1974 C  CB  . LEU   A 1 263 ? -39.85100 3.87000   -3.87600  1.000 22.42000  ? 692  LEU   A CB  1 
ATOM   1975 C  CG  . LEU   A 1 263 ? -40.91600 3.83700   -2.74700  1.000 22.44000  ? 692  LEU   A CG  1 
ATOM   1976 C  CD1 . LEU   A 1 263 ? -42.22900 3.17900   -3.19400  1.000 20.95000  ? 692  LEU   A CD1 1 
ATOM   1977 C  CD2 . LEU   A 1 263 ? -40.26300 3.11700   -1.51600  1.000 22.25000  ? 692  LEU   A CD2 1 
ATOM   1978 N  N   A MET   A 1 264 ? -39.64300 6.94500   -4.20800  0.646 23.08000  ? 693  MET   A N   1 
ATOM   1979 N  N   B MET   A 1 264 ? -39.63300 6.94800   -4.22600  0.354 23.06000  ? 693  MET   A N   1 
ATOM   1980 C  CA  A MET   A 1 264 ? -39.90800 8.34000   -3.84400  0.646 22.97000  ? 693  MET   A CA  1 
ATOM   1981 C  CA  B MET   A 1 264 ? -39.87200 8.35000   -3.87700  0.354 22.91000  ? 693  MET   A CA  1 
ATOM   1982 C  C   A MET   A 1 264 ? -40.60000 9.13000   -4.96300  0.646 24.75000  ? 693  MET   A C   1 
ATOM   1983 C  C   B MET   A 1 264 ? -40.63100 9.07700   -4.98000  0.354 24.68000  ? 693  MET   A C   1 
ATOM   1984 O  O   A MET   A 1 264 ? -41.59400 9.83000   -4.71700  0.646 20.83000  ? 693  MET   A O   1 
ATOM   1985 O  O   B MET   A 1 264 ? -41.67800 9.69500   -4.73900  0.354 20.90000  ? 693  MET   A O   1 
ATOM   1986 C  CB  A MET   A 1 264 ? -38.59300 8.99100   -3.43600  0.646 23.51000  ? 693  MET   A CB  1 
ATOM   1987 C  CB  B MET   A 1 264 ? -38.53200 9.04000   -3.63800  0.354 23.32000  ? 693  MET   A CB  1 
ATOM   1988 C  CG  A MET   A 1 264 ? -38.70400 10.46700  -3.08500  0.646 24.75000  ? 693  MET   A CG  1 
ATOM   1989 C  CG  B MET   A 1 264 ? -37.77900 8.58700   -2.41000  0.354 15.60000  ? 693  MET   A CG  1 
ATOM   1990 S  SD  A MET   A 1 264 ? -37.13800 11.20200  -2.66200  0.646 26.28000  ? 693  MET   A SD  1 
ATOM   1991 S  SD  B MET   A 1 264 ? -36.05400 9.20000   -2.41400  0.354 27.78000  ? 693  MET   A SD  1 
ATOM   1992 C  CE  A MET   A 1 264 ? -36.25300 9.82700   -1.94200  0.646 27.44000  ? 693  MET   A CE  1 
ATOM   1993 C  CE  B MET   A 1 264 ? -36.26500 10.95900  -2.11200  0.354 22.51000  ? 693  MET   A CE  1 
ATOM   1994 N  N   . ALA   A 1 265 ? -40.10800 9.01000   -6.20800  1.000 22.73000  ? 694  ALA   A N   1 
ATOM   1995 C  CA  . ALA   A 1 265 ? -40.76100 9.67000   -7.33900  1.000 25.97000  ? 694  ALA   A CA  1 
ATOM   1996 C  C   . ALA   A 1 265 ? -42.19600 9.19800   -7.51400  1.000 24.33000  ? 694  ALA   A C   1 
ATOM   1997 O  O   . ALA   A 1 265 ? -43.08100 9.98400   -7.87400  1.000 21.90000  ? 694  ALA   A O   1 
ATOM   1998 C  CB  . ALA   A 1 265 ? -39.95400 9.40200   -8.63600  1.000 20.89000  ? 694  ALA   A CB  1 
ATOM   1999 N  N   . GLU   A 1 266 ? -42.46100 7.89900   -7.27500  1.000 19.79000  ? 695  GLU   A N   1 
ATOM   2000 C  CA  . GLU   A 1 266 ? -43.81600 7.39900   -7.42800  1.000 20.92000  ? 695  GLU   A CA  1 
ATOM   2001 C  C   . GLU   A 1 266 ? -44.74100 8.00000   -6.35000  1.000 17.84000  ? 695  GLU   A C   1 
ATOM   2002 O  O   . GLU   A 1 266 ? -45.91200 8.30500   -6.60800  1.000 18.19000  ? 695  GLU   A O   1 
ATOM   2003 C  CB  . GLU   A 1 266 ? -43.82900 5.88200   -7.30500  1.000 28.27000  ? 695  GLU   A CB  1 
ATOM   2004 C  CG  . GLU   A 1 266 ? -43.46300 5.11000   -8.59000  1.000 36.47000  ? 695  GLU   A CG  1 
ATOM   2005 C  CD  . GLU   A 1 266 ? -44.70400 4.77000   -9.43500  1.000 69.68000  ? 695  GLU   A CD  1 
ATOM   2006 O  OE1 . GLU   A 1 266 ? -45.35400 5.68300   -10.00700 1.000 57.66000  ? 695  GLU   A OE1 1 
ATOM   2007 O  OE2 . GLU   A 1 266 ? -45.10200 3.58300   -9.41900  1.000 72.96000  ? 695  GLU   A OE2 1 
ATOM   2008 N  N   . CYS   A 1 267 ? -44.24600 8.06700   -5.12900  1.000 19.87000  ? 696  CYS   A N   1 
ATOM   2009 C  CA  . CYS   A 1 267 ? -45.10800 8.56900   -4.03300  1.000 20.18000  ? 696  CYS   A CA  1 
ATOM   2010 C  C   . CYS   A 1 267 ? -45.41600 10.03800  -4.23600  1.000 21.21000  ? 696  CYS   A C   1 
ATOM   2011 O  O   . CYS   A 1 267 ? -46.44900 10.52000  -3.76700  1.000 19.21000  ? 696  CYS   A O   1 
ATOM   2012 C  CB  . CYS   A 1 267 ? -44.41100 8.44200   -2.68400  1.000 16.34000  ? 696  CYS   A CB  1 
ATOM   2013 S  SG  . CYS   A 1 267 ? -44.15400 6.68800   -2.11400  1.000 21.71000  ? 696  CYS   A SG  1 
ATOM   2014 N  N   . LEU   A 1 268 ? -44.51700 10.74200  -4.90600  1.000 19.88000  ? 697  LEU   A N   1 
ATOM   2015 C  CA  . LEU   A 1 268 ? -44.62500 12.18900  -5.12500  1.000 21.10000  ? 697  LEU   A CA  1 
ATOM   2016 C  C   . LEU   A 1 268 ? -45.37200 12.57200  -6.38600  1.000 21.62000  ? 697  LEU   A C   1 
ATOM   2017 O  O   . LEU   A 1 268 ? -45.46300 13.77700  -6.66900  1.000 24.85000  ? 697  LEU   A O   1 
ATOM   2018 C  CB  . LEU   A 1 268 ? -43.24900 12.81900  -5.15500  1.000 19.98000  ? 697  LEU   A CB  1 
ATOM   2019 C  CG  . LEU   A 1 268 ? -42.49800 12.77300  -3.81000  1.000 19.06000  ? 697  LEU   A CG  1 
ATOM   2020 C  CD1 . LEU   A 1 268 ? -41.01400 13.20700  -3.87900  1.000 23.06000  ? 697  LEU   A CD1 1 
ATOM   2021 C  CD2 . LEU   A 1 268 ? -43.27900 13.62600  -2.70900  1.000 18.73000  ? 697  LEU   A CD2 1 
ATOM   2022 N  N   . LYS   A 1 269 ? -45.94600 11.61600  -7.11800  1.000 19.05000  ? 698  LYS   A N   1 
ATOM   2023 C  CA  . LYS   A 1 269 ? -46.61100 11.93300  -8.38400  1.000 23.70000  ? 698  LYS   A CA  1 
ATOM   2024 C  C   . LYS   A 1 269 ? -47.68800 12.99100  -8.18500  1.000 26.12000  ? 698  LYS   A C   1 
ATOM   2025 O  O   . LYS   A 1 269 ? -48.48400 12.92700  -7.24400  1.000 22.82000  ? 698  LYS   A O   1 
ATOM   2026 C  CB  . LYS   A 1 269 ? -47.25800 10.68000  -8.95900  1.000 23.39000  ? 698  LYS   A CB  1 
ATOM   2027 C  CG  . LYS   A 1 269 ? -46.20700 9.68200   -9.56300  1.000 27.59000  ? 698  LYS   A CG  1 
ATOM   2028 C  CD  . LYS   A 1 269 ? -45.97300 9.96500   -11.00100 1.000 43.01000  ? 698  LYS   A CD  1 
ATOM   2029 C  CE  . LYS   A 1 269 ? -45.19900 8.82300   -11.67400 1.000 44.22000  ? 698  LYS   A CE  1 
ATOM   2030 N  NZ  . LYS   A 1 269 ? -43.91000 9.32300   -12.19900 1.000 55.25000  ? 698  LYS   A NZ  1 
ATOM   2031 N  N   . LYS   A 1 270 ? -47.74600 13.95800  -9.10000  1.000 23.92000  ? 699  LYS   A N   1 
ATOM   2032 C  CA  . LYS   A 1 270 ? -48.77600 14.99000  -8.97500  1.000 23.95000  ? 699  LYS   A CA  1 
ATOM   2033 C  C   . LYS   A 1 270 ? -50.16800 14.39300  -9.07300  1.000 24.00000  ? 699  LYS   A C   1 
ATOM   2034 O  O   . LYS   A 1 270 ? -51.09400 14.80400  -8.34600  1.000 28.42000  ? 699  LYS   A O   1 
ATOM   2035 C  CB  . LYS   A 1 270 ? -48.56400 16.05700  -10.06000 1.000 27.29000  ? 699  LYS   A CB  1 
ATOM   2036 C  CG  . LYS   A 1 270 ? -47.43800 17.00400  -9.67000  1.000 33.85000  ? 699  LYS   A CG  1 
ATOM   2037 C  CD  . LYS   A 1 270 ? -46.80100 17.72900  -10.87500 1.000 50.78000  ? 699  LYS   A CD  1 
ATOM   2038 C  CE  . LYS   A 1 270 ? -45.53100 18.44400  -10.44600 1.000 49.88000  ? 699  LYS   A CE  1 
ATOM   2039 N  NZ  . LYS   A 1 270 ? -44.65000 18.87600  -11.59400 1.000 50.74000  ? 699  LYS   A NZ  1 
ATOM   2040 N  N   . LYS   A 1 271 ? -50.36900 13.47600  -10.00600 1.000 26.87000  ? 700  LYS   A N   1 
ATOM   2041 C  CA  . LYS   A 1 271 ? -51.64500 12.81000  -10.16200 1.000 31.63000  ? 700  LYS   A CA  1 
ATOM   2042 C  C   . LYS   A 1 271 ? -51.77000 11.72700  -9.09300  1.000 25.46000  ? 700  LYS   A C   1 
ATOM   2043 O  O   . LYS   A 1 271 ? -51.04700 10.72500  -9.14900  1.000 26.62000  ? 700  LYS   A O   1 
ATOM   2044 C  CB  . LYS   A 1 271 ? -51.71300 12.19200  -11.54900 1.000 36.53000  ? 700  LYS   A CB  1 
ATOM   2045 C  CG  . LYS   A 1 271 ? -51.85300 13.24800  -12.64600 1.000 47.64000  ? 700  LYS   A CG  1 
ATOM   2046 C  CD  . LYS   A 1 271 ? -51.96200 12.62300  -14.05400 1.000 57.88000  ? 700  LYS   A CD  1 
ATOM   2047 C  CE  . LYS   A 1 271 ? -52.57100 11.22600  -14.06100 1.000 58.86000  ? 700  LYS   A CE  1 
ATOM   2048 N  NZ  . LYS   A 1 271 ? -54.03200 11.19100  -13.81400 1.000 66.40000  ? 700  LYS   A NZ  1 
ATOM   2049 N  N   . ARG   A 1 272 ? -52.70900 11.91100  -8.16200  1.000 26.49000  ? 701  ARG   A N   1 
ATOM   2050 C  CA  . ARG   A 1 272 ? -52.78700 11.03200  -7.00100  1.000 22.37000  ? 701  ARG   A CA  1 
ATOM   2051 C  C   . ARG   A 1 272 ? -53.07200 9.58000   -7.38500  1.000 25.10000  ? 701  ARG   A C   1 
ATOM   2052 O  O   . ARG   A 1 272 ? -52.58500 8.66300   -6.70800  1.000 23.78000  ? 701  ARG   A O   1 
ATOM   2053 C  CB  . ARG   A 1 272 ? -53.82500 11.56700  -6.03800  1.000 22.57000  ? 701  ARG   A CB  1 
ATOM   2054 C  CG  . ARG   A 1 272 ? -55.23100 11.58900  -6.56200  1.000 23.14000  ? 701  ARG   A CG  1 
ATOM   2055 C  CD  . ARG   A 1 272 ? -56.20200 12.06500  -5.48100  1.000 25.91000  ? 701  ARG   A CD  1 
ATOM   2056 N  NE  . ARG   A 1 272 ? -57.55000 12.17400  -6.00400  1.000 31.55000  ? 701  ARG   A NE  1 
ATOM   2057 C  CZ  . ARG   A 1 272 ? -58.57700 12.59700  -5.29500  1.000 31.08000  ? 701  ARG   A CZ  1 
ATOM   2058 N  NH1 . ARG   A 1 272 ? -58.42400 12.98900  -4.04300  1.000 23.79000  ? 701  ARG   A NH1 1 
ATOM   2059 N  NH2 . ARG   A 1 272 ? -59.78700 12.63800  -5.86200  1.000 30.71000  ? 701  ARG   A NH2 1 
ATOM   2060 N  N   A ASP   A 1 273 ? -53.83500 9.34800   -8.46000  0.601 25.60000  ? 702  ASP   A N   1 
ATOM   2061 N  N   B ASP   A 1 273 ? -53.82200 9.32900   -8.46300  0.399 25.66000  ? 702  ASP   A N   1 
ATOM   2062 C  CA  A ASP   A 1 273 ? -54.16600 7.98400   -8.86300  0.601 29.15000  ? 702  ASP   A CA  1 
ATOM   2063 C  CA  B ASP   A 1 273 ? -54.13100 7.93500   -8.77700  0.399 29.16000  ? 702  ASP   A CA  1 
ATOM   2064 C  C   A ASP   A 1 273 ? -52.94000 7.18800   -9.29800  0.601 31.13000  ? 702  ASP   A C   1 
ATOM   2065 C  C   B ASP   A 1 273 ? -52.89600 7.16100   -9.22500  0.399 31.13000  ? 702  ASP   A C   1 
ATOM   2066 O  O   A ASP   A 1 273 ? -53.02900 5.96000   -9.38000  0.601 32.68000  ? 702  ASP   A O   1 
ATOM   2067 O  O   B ASP   A 1 273 ? -52.93200 5.92700   -9.24000  0.399 32.90000  ? 702  ASP   A O   1 
ATOM   2068 C  CB  A ASP   A 1 273 ? -55.19700 8.00000   -10.00100 0.601 30.97000  ? 702  ASP   A CB  1 
ATOM   2069 C  CB  B ASP   A 1 273 ? -55.22500 7.83600   -9.84700  0.399 31.10000  ? 702  ASP   A CB  1 
ATOM   2070 C  CG  A ASP   A 1 273 ? -56.59000 8.38800   -9.53200  0.601 38.08000  ? 702  ASP   A CG  1 
ATOM   2071 C  CG  B ASP   A 1 273 ? -54.80500 8.42700   -11.18200 0.399 27.28000  ? 702  ASP   A CG  1 
ATOM   2072 O  OD1 A ASP   A 1 273 ? -56.70400 9.08000   -8.50500  0.601 49.97000  ? 702  ASP   A OD1 1 
ATOM   2073 O  OD1 B ASP   A 1 273 ? -53.70300 8.99600   -11.28400 0.399 39.69000  ? 702  ASP   A OD1 1 
ATOM   2074 O  OD2 A ASP   A 1 273 ? -57.57900 8.02800   -10.21100 0.601 53.25000  ? 702  ASP   A OD2 1 
ATOM   2075 O  OD2 B ASP   A 1 273 ? -55.60400 8.34000   -12.14300 0.399 43.33000  ? 702  ASP   A OD2 1 
ATOM   2076 N  N   . GLU   A 1 274 ? -51.80900 7.85300   -9.58100  1.000 22.47000  ? 703  GLU   A N   1 
ATOM   2077 C  CA  . GLU   A 1 274 ? -50.56800 7.20800   -9.97400  1.000 31.71000  ? 703  GLU   A CA  1 
ATOM   2078 C  C   . GLU   A 1 274 ? -49.68800 6.83900   -8.79100  1.000 30.94000  ? 703  GLU   A C   1 
ATOM   2079 O  O   . GLU   A 1 274 ? -48.62200 6.25300   -8.98700  1.000 26.81000  ? 703  GLU   A O   1 
ATOM   2080 C  CB  . GLU   A 1 274 ? -49.78100 8.13700   -10.89900 1.000 33.42000  ? 703  GLU   A CB  1 
ATOM   2081 C  CG  . GLU   A 1 274 ? -50.50700 8.39600   -12.22700 1.000 37.21000  ? 703  GLU   A CG  1 
ATOM   2082 C  CD  . GLU   A 1 274 ? -49.71100 9.28300   -13.17700 1.000 42.10000  ? 703  GLU   A CD  1 
ATOM   2083 O  OE1 . GLU   A 1 274 ? -48.59700 9.74200   -12.84300 1.000 46.18000  ? 703  GLU   A OE1 1 
ATOM   2084 O  OE2 . GLU   A 1 274 ? -50.21700 9.50800   -14.28700 1.000 57.00000  ? 703  GLU   A OE2 1 
ATOM   2085 N  N   . ARG   A 1 275 ? -50.06000 7.25900   -7.55100  1.000 24.60000  ? 704  ARG   A N   1 
ATOM   2086 C  CA  . ARG   A 1 275 ? -49.17900 6.93600   -6.43100  1.000 17.25000  ? 704  ARG   A CA  1 
ATOM   2087 C  C   . ARG   A 1 275 ? -49.47700 5.51600   -5.94600  1.000 16.06000  ? 704  ARG   A C   1 
ATOM   2088 O  O   . ARG   A 1 275 ? -50.63600 5.09600   -5.92300  1.000 22.99000  ? 704  ARG   A O   1 
ATOM   2089 C  CB  . ARG   A 1 275 ? -49.44700 7.93600   -5.26400  1.000 17.58000  ? 704  ARG   A CB  1 
ATOM   2090 C  CG  . ARG   A 1 275 ? -49.06000 9.38400   -5.59700  1.000 17.31000  ? 704  ARG   A CG  1 
ATOM   2091 C  CD  . ARG   A 1 275 ? -49.54400 10.37400  -4.46900  1.000 17.93000  ? 704  ARG   A CD  1 
ATOM   2092 N  NE  . ARG   A 1 275 ? -49.58800 11.75300  -5.01000  1.000 17.31000  ? 704  ARG   A NE  1 
ATOM   2093 C  CZ  . ARG   A 1 275 ? -50.51100 12.63700  -4.69100  1.000 19.18000  ? 704  ARG   A CZ  1 
ATOM   2094 N  NH1 . ARG   A 1 275 ? -51.36800 12.40700  -3.68500  1.000 16.59000  ? 704  ARG   A NH1 1 
ATOM   2095 N  NH2 . ARG   A 1 275 ? -50.60800 13.76800  -5.43300  1.000 19.98000  ? 704  ARG   A NH2 1 
ATOM   2096 N  N   . PRO   A 1 276 ? -48.46000 4.78400   -5.50800  1.000 17.73000  ? 705  PRO   A N   1 
ATOM   2097 C  CA  . PRO   A 1 276 ? -48.69600 3.45800   -4.90500  1.000 20.87000  ? 705  PRO   A CA  1 
ATOM   2098 C  C   . PRO   A 1 276 ? -49.33400 3.59500   -3.53500  1.000 27.19000  ? 705  PRO   A C   1 
ATOM   2099 O  O   . PRO   A 1 276 ? -49.18400 4.61400   -2.88400  1.000 24.88000  ? 705  PRO   A O   1 
ATOM   2100 C  CB  . PRO   A 1 276 ? -47.29000 2.88900   -4.75800  1.000 20.16000  ? 705  PRO   A CB  1 
ATOM   2101 C  CG  . PRO   A 1 276 ? -46.40700 4.09300   -4.50100  1.000 19.84000  ? 705  PRO   A CG  1 
ATOM   2102 C  CD  . PRO   A 1 276 ? -47.06100 5.23800   -5.37500  1.000 17.93000  ? 705  PRO   A CD  1 
ATOM   2103 N  N   . LEU   A 1 277 ? -49.96400 2.53000   -3.06200  1.000 20.52000  ? 706  LEU   A N   1 
ATOM   2104 C  CA  . LEU   A 1 277 ? -50.52000 2.51800   -1.70500  1.000 22.58000  ? 706  LEU   A CA  1 
ATOM   2105 C  C   . LEU   A 1 277 ? -49.58300 1.74100   -0.78000  1.000 20.02000  ? 706  LEU   A C   1 
ATOM   2106 O  O   . LEU   A 1 277 ? -48.57800 1.19700   -1.21500  1.000 20.11000  ? 706  LEU   A O   1 
ATOM   2107 C  CB  . LEU   A 1 277 ? -51.92300 1.92900   -1.71200  1.000 22.75000  ? 706  LEU   A CB  1 
ATOM   2108 C  CG  . LEU   A 1 277 ? -52.98600 2.82800   -2.39100  1.000 27.11000  ? 706  LEU   A CG  1 
ATOM   2109 C  CD1 . LEU   A 1 277 ? -54.32900 2.15500   -2.44700  1.000 33.61000  ? 706  LEU   A CD1 1 
ATOM   2110 C  CD2 . LEU   A 1 277 ? -53.14600 4.11100   -1.59900  1.000 29.47000  ? 706  LEU   A CD2 1 
ATOM   2111 N  N   . PHE   A 1 278 ? -49.86600 1.76800   0.56100   1.000 18.35000  ? 707  PHE   A N   1 
ATOM   2112 C  CA  . PHE   A 1 278 ? -48.77300 1.34900   1.44400   1.000 17.93000  ? 707  PHE   A CA  1 
ATOM   2113 C  C   . PHE   A 1 278 ? -48.41100 -0.15000  1.42600   1.000 16.13000  ? 707  PHE   A C   1 
ATOM   2114 O  O   . PHE   A 1 278 ? -47.25400 -0.46800  1.64800   1.000 19.07000  ? 707  PHE   A O   1 
ATOM   2115 C  CB  . PHE   A 1 278 ? -49.08200 1.79600   2.89500   1.000 22.51000  ? 707  PHE   A CB  1 
ATOM   2116 C  CG  . PHE   A 1 278 ? -48.56200 3.18400   3.17000   1.000 14.17000  ? 707  PHE   A CG  1 
ATOM   2117 C  CD1 . PHE   A 1 278 ? -47.17000 3.40500   3.37800   1.000 15.31000  ? 707  PHE   A CD1 1 
ATOM   2118 C  CD2 . PHE   A 1 278 ? -49.40800 4.29000   3.07200   1.000 17.71000  ? 707  PHE   A CD2 1 
ATOM   2119 C  CE1 . PHE   A 1 278 ? -46.62100 4.69000   3.52000   1.000 18.56000  ? 707  PHE   A CE1 1 
ATOM   2120 C  CE2 . PHE   A 1 278 ? -48.89300 5.57500   3.25500   1.000 17.70000  ? 707  PHE   A CE2 1 
ATOM   2121 C  CZ  . PHE   A 1 278 ? -47.49700 5.79800   3.47200   1.000 16.63000  ? 707  PHE   A CZ  1 
ATOM   2122 N  N   . PRO   A 1 279 ? -49.31500 -1.07500  1.11700   1.000 18.63000  ? 708  PRO   A N   1 
ATOM   2123 C  CA  . PRO   A 1 279 ? -48.81900 -2.47400  0.97000   1.000 19.64000  ? 708  PRO   A CA  1 
ATOM   2124 C  C   . PRO   A 1 279 ? -47.74100 -2.57300  -0.07500  1.000 20.05000  ? 708  PRO   A C   1 
ATOM   2125 O  O   . PRO   A 1 279 ? -46.69700 -3.20400  0.15400   1.000 21.17000  ? 708  PRO   A O   1 
ATOM   2126 C  CB  . PRO   A 1 279 ? -50.08300 -3.24100  0.59500   1.000 21.18000  ? 708  PRO   A CB  1 
ATOM   2127 C  CG  . PRO   A 1 279 ? -51.20800 -2.45400  1.18600   1.000 24.37000  ? 708  PRO   A CG  1 
ATOM   2128 C  CD  . PRO   A 1 279 ? -50.77000 -1.01100  0.94700   1.000 17.47000  ? 708  PRO   A CD  1 
ATOM   2129 N  N   . GLN   A 1 280 ? -47.93500 -1.89200  -1.22700  1.000 20.07000  ? 709  GLN   A N   1 
ATOM   2130 C  CA  . GLN   A 1 280 ? -46.90000 -1.88000  -2.25600  1.000 21.18000  ? 709  GLN   A CA  1 
ATOM   2131 C  C   . GLN   A 1 280 ? -45.64600 -1.16000  -1.79500  1.000 21.06000  ? 709  GLN   A C   1 
ATOM   2132 O  O   . GLN   A 1 280 ? -44.53000 -1.62600  -2.05200  1.000 21.01000  ? 709  GLN   A O   1 
ATOM   2133 C  CB  . GLN   A 1 280 ? -47.45600 -1.22300  -3.52800  1.000 18.60000  ? 709  GLN   A CB  1 
ATOM   2134 C  CG  . GLN   A 1 280 ? -46.42800 -1.17400  -4.68100  1.000 29.07000  ? 709  GLN   A CG  1 
ATOM   2135 C  CD  . GLN   A 1 280 ? -46.96500 -0.48300  -5.94400  1.000 39.21000  ? 709  GLN   A CD  1 
ATOM   2136 O  OE1 . GLN   A 1 280 ? -48.18800 -0.43500  -6.18500  1.000 31.90000  ? 709  GLN   A OE1 1 
ATOM   2137 N  NE2 . GLN   A 1 280 ? -46.05000 0.04500   -6.76000  1.000 33.69000  ? 709  GLN   A NE2 1 
ATOM   2138 N  N   . ILE   A 1 281 ? -45.79700 0.01200   -1.13100  1.000 17.85000  ? 710  ILE   A N   1 
ATOM   2139 C  CA  . ILE   A 1 281 ? -44.64300 0.77300   -0.66100  1.000 16.46000  ? 710  ILE   A CA  1 
ATOM   2140 C  C   . ILE   A 1 281 ? -43.81400 -0.07000  0.29600   1.000 15.95000  ? 710  ILE   A C   1 
ATOM   2141 O  O   . ILE   A 1 281 ? -42.57600 -0.13200  0.21200   1.000 19.27000  ? 710  ILE   A O   1 
ATOM   2142 C  CB  . ILE   A 1 281 ? -45.12300 2.07100   0.02600   1.000 18.16000  ? 710  ILE   A CB  1 
ATOM   2143 C  CG1 . ILE   A 1 281 ? -45.72700 3.01800   -1.06600  1.000 18.82000  ? 710  ILE   A CG1 1 
ATOM   2144 C  CG2 . ILE   A 1 281 ? -43.96500 2.71200   0.79900   1.000 20.28000  ? 710  ILE   A CG2 1 
ATOM   2145 C  CD1 . ILE   A 1 281 ? -46.62600 4.15400   -0.42100  1.000 16.53000  ? 710  ILE   A CD1 1 
ATOM   2146 N  N   . LEU   A 1 282 ? -44.49700 -0.66800  1.26800   1.000 20.08000  ? 711  LEU   A N   1 
ATOM   2147 C  CA  . LEU   A 1 282 ? -43.83200 -1.48100  2.26900   1.000 22.93000  ? 711  LEU   A CA  1 
ATOM   2148 C  C   . LEU   A 1 282 ? -43.08100 -2.62000  1.60400   1.000 22.71000  ? 711  LEU   A C   1 
ATOM   2149 O  O   . LEU   A 1 282 ? -41.89300 -2.85500  1.87700   1.000 21.50000  ? 711  LEU   A O   1 
ATOM   2150 C  CB  . LEU   A 1 282 ? -44.88200 -1.97700  3.25400   1.000 21.21000  ? 711  LEU   A CB  1 
ATOM   2151 C  CG  . LEU   A 1 282 ? -44.51000 -2.71600  4.50900   1.000 25.48000  ? 711  LEU   A CG  1 
ATOM   2152 C  CD1 . LEU   A 1 282 ? -43.45400 -1.94400  5.27100   1.000 22.37000  ? 711  LEU   A CD1 1 
ATOM   2153 C  CD2 . LEU   A 1 282 ? -45.81600 -2.92100  5.28700   1.000 23.00000  ? 711  LEU   A CD2 1 
ATOM   2154 N  N   . ALA   A 1 283 ? -43.72600 -3.28500  0.66100   1.000 21.91000  ? 712  ALA   A N   1 
ATOM   2155 C  CA  . ALA   A 1 283 ? -43.03800 -4.40200  -0.00800  1.000 25.48000  ? 712  ALA   A CA  1 
ATOM   2156 C  C   . ALA   A 1 283 ? -41.79500 -3.93700  -0.77200  1.000 28.17000  ? 712  ALA   A C   1 
ATOM   2157 O  O   . ALA   A 1 283 ? -40.75600 -4.61600  -0.74900  1.000 27.08000  ? 712  ALA   A O   1 
ATOM   2158 C  CB  . ALA   A 1 283 ? -44.03200 -5.12600  -0.91500  1.000 25.89000  ? 712  ALA   A CB  1 
ATOM   2159 N  N   . SER   A 1 284 ? -41.85600 -2.76200  -1.44100  1.000 22.34000  ? 713  SER   A N   1 
ATOM   2160 C  CA  . SER   A 1 284 ? -40.69000 -2.25400  -2.15600  1.000 24.09000  ? 713  SER   A CA  1 
ATOM   2161 C  C   . SER   A 1 284 ? -39.56500 -1.93700  -1.19600  1.000 24.45000  ? 713  SER   A C   1 
ATOM   2162 O  O   . SER   A 1 284 ? -38.39200 -2.14400  -1.50100  1.000 24.20000  ? 713  SER   A O   1 
ATOM   2163 C  CB  . SER   A 1 284 ? -41.04500 -0.97000  -2.96400  1.000 22.21000  ? 713  SER   A CB  1 
ATOM   2164 O  OG  . SER   A 1 284 ? -42.00700 -1.25000  -3.99000  1.000 24.43000  ? 713  SER   A OG  1 
ATOM   2165 N  N   . ILE   A 1 285 ? -39.89400 -1.35000  -0.04100  1.000 20.27000  ? 714  ILE   A N   1 
ATOM   2166 C  CA  . ILE   A 1 285 ? -38.84800 -1.02600  0.89900   1.000 16.62000  ? 714  ILE   A CA  1 
ATOM   2167 C  C   . ILE   A 1 285 ? -38.25100 -2.30500  1.50400   1.000 23.38000  ? 714  ILE   A C   1 
ATOM   2168 O  O   . ILE   A 1 285 ? -37.01800 -2.41500  1.67800   1.000 26.99000  ? 714  ILE   A O   1 
ATOM   2169 C  CB  . ILE   A 1 285 ? -39.40500 -0.09900  2.00400   1.000 18.63000  ? 714  ILE   A CB  1 
ATOM   2170 C  CG1 . ILE   A 1 285 ? -39.88600 1.21900   1.34600   1.000 18.15000  ? 714  ILE   A CG1 1 
ATOM   2171 C  CG2 . ILE   A 1 285 ? -38.29100 0.18100   3.04900   1.000 22.54000  ? 714  ILE   A CG2 1 
ATOM   2172 C  CD1 . ILE   A 1 285 ? -40.60000 2.21000   2.36400   1.000 21.63000  ? 714  ILE   A CD1 1 
ATOM   2173 N  N   . GLU   A 1 286 ? -39.10400 -3.25900  1.86700   1.000 22.47000  ? 715  GLU   A N   1 
ATOM   2174 C  CA  . GLU   A 1 286 ? -38.55900 -4.50600  2.41300   1.000 26.52000  ? 715  GLU   A CA  1 
ATOM   2175 C  C   . GLU   A 1 286 ? -37.58500 -5.13300  1.41500   1.000 26.72000  ? 715  GLU   A C   1 
ATOM   2176 O  O   . GLU   A 1 286 ? -36.47600 -5.54300  1.78400   1.000 30.16000  ? 715  GLU   A O   1 
ATOM   2177 C  CB  . GLU   A 1 286 ? -39.70600 -5.45000  2.78000   1.000 30.27000  ? 715  GLU   A CB  1 
ATOM   2178 C  CG  . GLU   A 1 286 ? -40.52900 -4.97400  4.05700   1.000 29.17000  ? 715  GLU   A CG  1 
ATOM   2179 C  CD  . GLU   A 1 286 ? -41.84600 -5.68800  4.22800   1.000 32.46000  ? 715  GLU   A CD  1 
ATOM   2180 O  OE1 . GLU   A 1 286 ? -42.32300 -6.30800  3.25200   1.000 43.33000  ? 715  GLU   A OE1 1 
ATOM   2181 O  OE2 . GLU   A 1 286 ? -42.41100 -5.65800  5.36100   1.000 39.55000  ? 715  GLU   A OE2 1 
ATOM   2182 N  N   . LEU   A 1 287 ? -37.94200 -5.12800  0.12800   1.000 27.19000  ? 716  LEU   A N   1 
ATOM   2183 C  CA  . LEU   A 1 287 ? -37.08300 -5.71900  -0.89800  1.000 28.01000  ? 716  LEU   A CA  1 
ATOM   2184 C  C   . LEU   A 1 287 ? -35.76500 -4.97100  -1.01700  1.000 37.21000  ? 716  LEU   A C   1 
ATOM   2185 O  O   . LEU   A 1 287 ? -34.68600 -5.58100  -1.02700  1.000 34.26000  ? 716  LEU   A O   1 
ATOM   2186 C  CB  . LEU   A 1 287 ? -37.82200 -5.75000  -2.24300  1.000 26.62000  ? 716  LEU   A CB  1 
ATOM   2187 C  CG  . LEU   A 1 287 ? -37.02000 -6.18200  -3.47100  1.000 33.47000  ? 716  LEU   A CG  1 
ATOM   2188 C  CD1 . LEU   A 1 287 ? -36.49700 -7.57600  -3.17700  1.000 34.70000  ? 716  LEU   A CD1 1 
ATOM   2189 C  CD2 . LEU   A 1 287 ? -37.88800 -6.19200  -4.72600  1.000 29.76000  ? 716  LEU   A CD2 1 
ATOM   2190 N  N   . LEU   A 1 288 ? -35.81000 -3.63800  -1.12100  1.000 30.53000  ? 717  LEU   A N   1 
ATOM   2191 C  CA  . LEU   A 1 288 ? -34.54700 -2.95500  -1.30800  1.000 32.71000  ? 717  LEU   A CA  1 
ATOM   2192 C  C   . LEU   A 1 288 ? -33.69000 -3.02700  -0.04300  1.000 29.00000  ? 717  LEU   A C   1 
ATOM   2193 O  O   . LEU   A 1 288 ? -32.46400 -2.94400  -0.14400  1.000 39.04000  ? 717  LEU   A O   1 
ATOM   2194 C  CB  . LEU   A 1 288 ? -34.77700 -1.50700  -1.80400  1.000 31.33000  ? 717  LEU   A CB  1 
ATOM   2195 C  CG  . LEU   A 1 288 ? -35.33000 -0.43500  -0.86500  1.000 31.49000  ? 717  LEU   A CG  1 
ATOM   2196 C  CD1 . LEU   A 1 288 ? -34.16100 0.27300   -0.27600  1.000 30.23000  ? 717  LEU   A CD1 1 
ATOM   2197 C  CD2 . LEU   A 1 288 ? -36.19400 0.59700   -1.65200  1.000 27.93000  ? 717  LEU   A CD2 1 
ATOM   2198 N  N   . ALA   A 1 289 ? -34.30500 -3.25100  1.13000   1.000 31.10000  ? 718  ALA   A N   1 
ATOM   2199 C  CA  . ALA   A 1 289 ? -33.54400 -3.38800  2.37500   1.000 33.54000  ? 718  ALA   A CA  1 
ATOM   2200 C  C   . ALA   A 1 289 ? -32.73500 -4.68900  2.41000   1.000 42.25000  ? 718  ALA   A C   1 
ATOM   2201 O  O   . ALA   A 1 289 ? -31.60900 -4.70600  2.91800   1.000 38.01000  ? 718  ALA   A O   1 
ATOM   2202 C  CB  . ALA   A 1 289 ? -34.48200 -3.34900  3.58000   1.000 31.06000  ? 718  ALA   A CB  1 
ATOM   2203 N  N   . ARG   A 1 290 ? -33.31700 -5.79300  1.92900   1.000 45.51000  ? 719  ARG   A N   1 
ATOM   2204 C  CA  . ARG   A 1 290 ? -32.56900 -7.04500  1.75300   1.000 47.63000  ? 719  ARG   A CA  1 
ATOM   2205 C  C   . ARG   A 1 290 ? -31.45400 -6.91800  0.73300   1.000 51.11000  ? 719  ARG   A C   1 
ATOM   2206 O  O   . ARG   A 1 290 ? -30.40100 -7.54300  0.89000   1.000 51.50000  ? 719  ARG   A O   1 
ATOM   2207 C  CB  . ARG   A 1 290 ? -33.50600 -8.17600  1.32400   1.000 39.28000  ? 719  ARG   A CB  1 
ATOM   2208 C  CG  . ARG   A 1 290 ? -34.70600 -8.31000  2.21500   1.000 42.57000  ? 719  ARG   A CG  1 
ATOM   2209 C  CD  . ARG   A 1 290 ? -35.48700 -9.59300  1.93600   1.000 50.17000  ? 719  ARG   A CD  1 
ATOM   2210 N  NE  . ARG   A 1 290 ? -36.34000 -9.47700  0.75700   1.000 44.55000  ? 719  ARG   A NE  1 
ATOM   2211 C  CZ  . ARG   A 1 290 ? -37.62700 -9.16000  0.82900   1.000 48.25000  ? 719  ARG   A CZ  1 
ATOM   2212 N  NH1 . ARG   A 1 290 ? -38.18400 -8.81400  1.97500   1.000 37.83000  ? 719  ARG   A NH1 1 
ATOM   2213 N  NH2 . ARG   A 1 290 ? -38.36800 -9.17100  -0.27400  1.000 41.89000  ? 719  ARG   A NH2 1 
ATOM   2214 N  N   . SER   A 1 291 ? -31.66000 -6.13300  -0.31700  1.000 48.46000  ? 720  SER   A N   1 
ATOM   2215 C  CA  . SER   A 1 291 ? -30.69300 -6.03200  -1.40400  1.000 44.37000  ? 720  SER   A CA  1 
ATOM   2216 C  C   . SER   A 1 291 ? -29.54300 -5.07600  -1.10700  1.000 54.26000  ? 720  SER   A C   1 
ATOM   2217 O  O   . SER   A 1 291 ? -28.76700 -4.77500  -2.02200  1.000 61.55000  ? 720  SER   A O   1 
ATOM   2218 C  CB  . SER   A 1 291 ? -31.40400 -5.59900  -2.69500  1.000 49.62000  ? 720  SER   A CB  1 
ATOM   2219 O  OG  . SER   A 1 291 ? -32.60800 -6.35400  -2.89300  1.000 44.12000  ? 720  SER   A OG  1 
ATOM   2220 N  N   . LEU   A 1 292 ? -29.40800 -4.58900  0.12800   1.000 62.14000  ? 721  LEU   A N   1 
ATOM   2221 C  CA  . LEU   A 1 292 ? -28.36800 -3.60400  0.44300   1.000 53.35000  ? 721  LEU   A CA  1 
ATOM   2222 C  C   . LEU   A 1 292 ? -26.96200 -4.23500  0.39400   1.000 63.83000  ? 721  LEU   A C   1 
ATOM   2223 O  O   . LEU   A 1 292 ? -26.25500 -4.30600  1.40200   1.000 68.69000  ? 721  LEU   A O   1 
ATOM   2224 C  CB  . LEU   A 1 292 ? -28.62400 -2.97800  1.81600   1.000 47.53000  ? 721  LEU   A CB  1 
ATOM   2225 C  CG  . LEU   A 1 292 ? -29.50000 -1.72800  1.83600   1.000 46.13000  ? 721  LEU   A CG  1 
ATOM   2226 C  CD1 . LEU   A 1 292 ? -29.60700 -1.20900  3.27300   1.000 52.11000  ? 721  LEU   A CD1 1 
ATOM   2227 C  CD2 . LEU   A 1 292 ? -28.96800 -0.63200  0.90700   1.000 43.98000  ? 721  LEU   A CD2 1 
HETATM 2228 C  C18 . A1AQY B 2 .   ? -50.25000 13.61900  22.30000  1.000 14.57000  ? 801  A1AQY A C18 1 
HETATM 2229 C  C14 . A1AQY B 2 .   ? -48.18900 14.09700  21.02000  1.000 11.39000  ? 801  A1AQY A C14 1 
HETATM 2230 C  C13 . A1AQY B 2 .   ? -39.71900 14.24600  22.87200  1.000 18.78000  ? 801  A1AQY A C13 1 
HETATM 2231 C  C17 . A1AQY B 2 .   ? -50.90800 13.11600  21.13600  1.000 13.39000  ? 801  A1AQY A C17 1 
HETATM 2232 C  C16 . A1AQY B 2 .   ? -50.15500 13.09700  19.94800  1.000 12.18000  ? 801  A1AQY A C16 1 
HETATM 2233 C  C15 . A1AQY B 2 .   ? -48.83200 13.56900  19.88300  1.000 13.77000  ? 801  A1AQY A C15 1 
HETATM 2234 C  C10 . A1AQY B 2 .   ? -42.06200 14.49200  22.17800  1.000 17.40000  ? 801  A1AQY A C10 1 
HETATM 2235 C  C8  . A1AQY B 2 .   ? -41.37900 12.53500  23.43300  1.000 18.54000  ? 801  A1AQY A C8  1 
HETATM 2236 C  C5  . A1AQY B 2 .   ? -45.99000 12.68000  22.22900  1.000 14.16000  ? 801  A1AQY A C5  1 
HETATM 2237 C  C6  . A1AQY B 2 .   ? -44.90600 12.04200  22.83700  1.000 16.87000  ? 801  A1AQY A C6  1 
HETATM 2238 C  C1  . A1AQY B 2 .   ? -43.63300 12.64100  22.81100  1.000 15.42000  ? 801  A1AQY A C1  1 
HETATM 2239 C  C4  . A1AQY B 2 .   ? -45.78300 13.93200  21.58300  1.000 12.33000  ? 801  A1AQY A C4  1 
HETATM 2240 C  C19 . A1AQY B 2 .   ? -48.92700 14.10500  22.21400  1.000 15.90000  ? 801  A1AQY A C19 1 
HETATM 2241 C  C2  . A1AQY B 2 .   ? -43.41200 13.89600  22.17300  1.000 12.24000  ? 801  A1AQY A C2  1 
HETATM 2242 C  C3  . A1AQY B 2 .   ? -44.51900 14.50200  21.57000  1.000 13.19000  ? 801  A1AQY A C3  1 
HETATM 2243 C  C24 . A1AQY B 2 .   ? -51.22600 9.26300   18.86200  1.000 16.43000  ? 801  A1AQY A C24 1 
HETATM 2244 C  C25 . A1AQY B 2 .   ? -52.13700 8.40300   19.81700  1.000 20.05000  ? 801  A1AQY A C25 1 
HETATM 2245 C  C26 . A1AQY B 2 .   ? -52.97500 9.68700   20.03700  1.000 16.80000  ? 801  A1AQY A C26 1 
HETATM 2246 F  F20 . A1AQY B 2 .   ? -48.30000 14.55800  23.32800  1.000 17.01000  ? 801  A1AQY A F20 1 
HETATM 2247 F  F29 . A1AQY B 2 .   ? -52.84000 7.43300   19.17200  1.000 17.66000  ? 801  A1AQY A F29 1 
HETATM 2248 N  N12 . A1AQY B 2 .   ? -46.86100 14.54900  20.96700  1.000 12.47000  ? 801  A1AQY A N12 1 
HETATM 2249 N  N21 . A1AQY B 2 .   ? -50.72900 12.61400  18.77900  1.000 13.68000  ? 801  A1AQY A N21 1 
HETATM 2250 N  N23 . A1AQY B 2 .   ? -51.77900 10.45000  19.56000  1.000 16.65000  ? 801  A1AQY A N23 1 
HETATM 2251 N  N7  . A1AQY B 2 .   ? -42.58100 12.00900  23.43800  1.000 17.20000  ? 801  A1AQY A N7  1 
HETATM 2252 N  N9  . A1AQY B 2 .   ? -41.10600 13.74500  22.82700  1.000 17.61000  ? 801  A1AQY A N9  1 
HETATM 2253 O  O11 . A1AQY B 2 .   ? -41.82900 15.58200  21.60900  1.000 16.39000  ? 801  A1AQY A O11 1 
HETATM 2254 O  O27 . A1AQY B 2 .   ? -53.19100 12.52500  19.33300  1.000 16.90000  ? 801  A1AQY A O27 1 
HETATM 2255 O  O28 . A1AQY B 2 .   ? -52.40700 11.47800  17.30700  1.000 17.88000  ? 801  A1AQY A O28 1 
HETATM 2256 S  S22 . A1AQY B 2 .   ? -52.09300 11.86300  18.69000  1.000 15.74000  ? 801  A1AQY A S22 1 
HETATM 2257 CL CL1 . A1AQY B 2 .   ? -44.38300 16.04500  20.73300  1.000 21.69000  ? 801  A1AQY A CL1 1 
HETATM 2258 CL CL2 . A1AQY B 2 .   ? -47.97300 13.56300  18.39200  1.000 15.54000  ? 801  A1AQY A CL2 1 
HETATM 2259 S  S   . DMS   C 3 .   ? -46.85100 22.58200  13.27100  1.000 58.78000  ? 802  DMS   A S   1 
HETATM 2260 O  O   . DMS   C 3 .   ? -48.14100 23.24300  12.83700  1.000 45.94000  ? 802  DMS   A O   1 
HETATM 2261 C  C1  . DMS   C 3 .   ? -45.38200 23.60100  12.93500  1.000 54.64000  ? 802  DMS   A C1  1 
HETATM 2262 C  C2  . DMS   C 3 .   ? -46.93900 22.54700  15.05600  1.000 37.05000  ? 802  DMS   A C2  1 
HETATM 2263 S  S   . DMS   D 3 .   ? -54.43700 19.25900  -7.81600  1.000 76.39000  ? 803  DMS   A S   1 
HETATM 2264 O  O   . DMS   D 3 .   ? -55.80900 19.79800  -7.44000  1.000 37.10000  ? 803  DMS   A O   1 
HETATM 2265 C  C1  . DMS   D 3 .   ? -54.41800 18.35100  -9.39800  1.000 75.17000  ? 803  DMS   A C1  1 
HETATM 2266 C  C2  . DMS   D 3 .   ? -53.33900 20.66000  -8.15900  1.000 37.26000  ? 803  DMS   A C2  1 
HETATM 2267 S  S   . DMS   E 3 .   ? -50.18400 20.70000  15.50400  1.000 91.22000  ? 804  DMS   A S   1 
HETATM 2268 O  O   . DMS   E 3 .   ? -49.19200 20.38400  14.39400  1.000 51.97000  ? 804  DMS   A O   1 
HETATM 2269 C  C1  . DMS   E 3 .   ? -49.65100 21.02100  17.24700  1.000 26.07000  ? 804  DMS   A C1  1 
HETATM 2270 C  C2  . DMS   E 3 .   ? -51.14400 19.18500  15.78900  1.000 38.47000  ? 804  DMS   A C2  1 
HETATM 2271 S  S   . DMS   F 3 .   ? -45.24600 20.11600  18.96100  1.000 94.65000  ? 805  DMS   A S   1 
HETATM 2272 O  O   . DMS   F 3 .   ? -44.72900 18.98100  18.12700  1.000 64.77000  ? 805  DMS   A O   1 
HETATM 2273 C  C1  . DMS   F 3 .   ? -44.27000 20.17100  20.51900  1.000 34.36000  ? 805  DMS   A C1  1 
HETATM 2274 C  C2  . DMS   F 3 .   ? -47.02900 19.80100  19.26900  1.000 35.09000  ? 805  DMS   A C2  1 
HETATM 2275 S  S   . SO4   G 4 .   ? -61.65900 0.06100   22.81600  0.377 25.34000  ? 806  SO4   A S   1 
HETATM 2276 O  O1  . SO4   G 4 .   ? -61.08900 -0.05000  21.47000  0.377 25.27000  ? 806  SO4   A O1  1 
HETATM 2277 O  O2  . SO4   G 4 .   ? -63.12700 0.12700   22.67800  0.377 22.63000  ? 806  SO4   A O2  1 
HETATM 2278 O  O3  . SO4   G 4 .   ? -61.28400 -1.12700  23.58000  0.377 32.21000  ? 806  SO4   A O3  1 
HETATM 2279 O  O4  . SO4   G 4 .   ? -61.12800 1.24100   23.52600  0.377 20.92000  ? 806  SO4   A O4  1 
HETATM 2280 O  O   . HOH   H 5 .   ? -51.67200 27.96300  -7.23000  1.000 30.63000  ? 901  HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? -30.28300 12.07200  6.14800   1.000 40.71000  ? 902  HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? -54.44700 25.43800  26.86900  1.000 49.50000  ? 903  HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? -61.68000 0.64900   19.39800  1.000 33.99000  ? 904  HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? -56.00500 10.44000  -12.93700 1.000 47.39000  ? 905  HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? -42.40400 18.47700  10.43700  1.000 30.54000  ? 906  HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? -42.47500 11.14100  -11.87000 1.000 47.68000  ? 907  HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? -56.93900 8.10800   -6.37600  1.000 47.07000  ? 908  HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? -41.96200 21.36600  10.98400  1.000 43.91000  ? 909  HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? -53.77700 15.51500  16.29400  1.000 41.80000  ? 910  HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? -51.14100 20.26500  12.00300  1.000 36.23000  ? 911  HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? -44.69400 -6.50900  3.15000   1.000 44.03000  ? 912  HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? -24.84200 11.77200  13.71300  1.000 50.06000  ? 913  HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? -56.64600 15.01100  -7.46200  1.000 36.77000  ? 914  HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? -52.66900 16.35900  -7.45700  1.000 34.00000  ? 915  HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? -31.05900 22.39800  3.02100   1.000 44.83000  ? 916  HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? -60.74900 1.78400   4.40200   1.000 49.06000  ? 917  HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? -42.51500 20.04200  -11.23200 1.000 47.85000  ? 918  HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? -61.40700 27.04200  20.13700  1.000 54.32000  ? 919  HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? -56.66800 11.36500  11.41100  1.000 33.82000  ? 920  HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? -46.74900 1.76000   -9.02900  1.000 51.90000  ? 921  HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? -42.66200 17.34800  17.46800  1.000 36.62000  ? 922  HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? -24.16300 4.16700   2.12000   1.000 52.59000  ? 923  HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? -38.10600 4.21900   27.90700  1.000 43.37000  ? 924  HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? -29.68400 17.03500  7.57500   1.000 42.31000  ? 925  HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? -27.49900 12.92600  16.80300  1.000 43.71000  ? 926  HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? -44.17200 21.60100  10.75000  1.000 39.80000  ? 927  HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? -36.68800 20.09200  17.01200  1.000 31.04000  ? 928  HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? -38.08400 16.92500  31.95100  1.000 26.04000  ? 929  HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? -53.51600 17.20100  37.95100  1.000 37.34000  ? 930  HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? -32.35300 12.42900  20.45700  1.000 39.95000  ? 931  HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? -37.82100 0.90100   20.94700  1.000 35.82000  ? 932  HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? -63.58100 6.79300   27.07100  1.000 33.06000  ? 933  HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? -41.47100 -4.95500  7.60100   1.000 40.62000  ? 934  HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? -44.47500 16.03500  -7.26100  1.000 34.58000  ? 935  HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? -57.38600 14.68300  33.69300  1.000 35.66000  ? 936  HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? -42.45900 23.99400  7.68400   1.000 43.14000  ? 937  HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? -53.92300 15.96600  14.01400  1.000 44.04000  ? 938  HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? -53.19000 5.18400   -5.97600  1.000 35.46000  ? 939  HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? -58.47700 10.92200  -8.49200  1.000 41.38000  ? 940  HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? -55.17700 31.52300  15.76700  1.000 28.25000  ? 941  HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? -56.63300 20.78200  9.93300   1.000 32.26000  ? 942  HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? -65.86700 31.19500  17.19700  1.000 43.09000  ? 943  HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? -28.92300 15.02600  8.44800   1.000 51.87000  ? 944  HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? -40.68600 7.14400   28.29800  1.000 40.72000  ? 945  HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? -47.92600 15.84100  12.21900  1.000 31.72000  ? 946  HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? -52.86600 15.29200  18.45400  1.000 35.03000  ? 947  HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? -49.51500 21.99400  11.04900  1.000 29.10000  ? 948  HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? -53.68800 -3.89500  16.36300  1.000 14.97000  ? 949  HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? -56.08800 30.61500  12.04500  1.000 20.89000  ? 950  HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? -41.23200 17.29400  19.76100  1.000 36.46000  ? 951  HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? -58.609   1.329     22.933    1.000 24.69000  ? 952  HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? -52.51400 -0.66200  4.13100   1.000 29.27000  ? 953  HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? -35.15700 -10.35500 -1.38300  1.000 42.72000  ? 954  HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? -62.82100 2.87300   18.72700  1.000 28.69000  ? 955  HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? -37.93900 10.06300  30.81600  1.000 32.98000  ? 956  HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? -64.81500 3.91500   27.02900  1.000 45.84000  ? 957  HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? -33.97700 20.73100  -0.41300  1.000 32.05000  ? 958  HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? -44.71700 27.67700  5.97500   1.000 39.84000  ? 959  HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? -59.25100 -1.48200  15.58800  1.000 32.88000  ? 960  HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? -60.92300 19.81900  38.31800  1.000 39.16000  ? 961  HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? -55.96500 12.96400  -2.38200  1.000 19.91000  ? 962  HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? -50.09100 26.11300  20.71000  1.000 39.07000  ? 963  HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? -33.11300 22.50900  -6.43400  1.000 40.69000  ? 964  HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? -39.495   18.313    16.163    1.000 39.23000  ? 965  HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? -58.99500 11.14000  16.25100  1.000 29.82000  ? 966  HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? -42.58600 12.22800  -9.18100  1.000 29.63000  ? 967  HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? -58.76000 11.06300  9.19400   1.000 45.68000  ? 968  HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? -44.51000 19.33000  -1.26400  1.000 20.58000  ? 969  HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? -37.88000 -0.86500  -8.65400  1.000 48.69000  ? 970  HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? -46.78900 20.44200  -7.83900  1.000 33.68000  ? 971  HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? -53.19200 19.99300  10.82600  1.000 36.77000  ? 972  HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? -61.18700 12.45600  3.21600   1.000 46.32000  ? 973  HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? -71.34000 16.53300  25.68700  1.000 41.86000  ? 974  HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? -50.34500 0.20700   -4.74500  1.000 25.10000  ? 975  HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? -60.98500 14.84500  32.75300  1.000 29.03000  ? 976  HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? -63.89700 7.65300   23.04100  1.000 30.10000  ? 977  HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? -57.94400 12.86700  41.19800  1.000 44.43000  ? 978  HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? -67.72400 23.29600  15.98500  1.000 45.36000  ? 979  HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? -51.43600 25.58700  23.29900  1.000 46.36000  ? 980  HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? -39.35100 27.36300  2.97300   1.000 50.67000  ? 981  HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? -43.58100 0.37200   -5.72200  1.000 50.65000  ? 982  HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? -65.45200 7.23900   16.59300  1.000 50.48000  ? 983  HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? -47.96400 -2.67100  8.73200   1.000 24.25000  ? 984  HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? -56.43100 21.57600  5.29600   1.000 26.40000  ? 985  HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? -60.44600 9.92600   0.53800   1.000 34.22000  ? 986  HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? -46.14900 5.68100   31.60400  1.000 21.81000  ? 987  HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? -41.98400 -2.45000  13.11300  1.000 25.96000  ? 988  HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? -49.35600 12.32000  38.95300  1.000 28.77000  ? 989  HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? -42.69300 5.08800   26.10800  1.000 19.01000  ? 990  HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? -40.23700 6.01400   -10.27300 1.000 33.23000  ? 991  HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? -50.58600 25.07300  27.25100  1.000 28.93000  ? 992  HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? -60.46000 -1.05800  8.24000   1.000 43.00000  ? 993  HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? -46.58500 20.98300  -0.84900  1.000 16.89000  ? 994  HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? -34.31100 9.45700   19.04400  1.000 22.75000  ? 995  HOH   A O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? -47.12400 19.44300  15.88500  1.000 50.53000  ? 996  HOH   A O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? -71.14000 23.61300  19.08300  1.000 46.37000  ? 997  HOH   A O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? -42.35300 12.79800  33.19400  1.000 27.25000  ? 998  HOH   A O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? -48.29600 16.94300  6.73700   1.000 24.30000  ? 999  HOH   A O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? -60.12700 12.55600  6.61000   1.000 47.41000  ? 1000 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? -46.68600 -5.35700  1.84400   1.000 29.52000  ? 1001 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? -41.82000 6.30500   33.68500  1.000 30.32000  ? 1002 HOH   A O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? -46.98600 21.52200  36.88400  1.000 18.83000  ? 1003 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? -59.47400 23.30900  7.79400   1.000 19.84000  ? 1004 HOH   A O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? -47.209   27.148    11.912    1.000 38.30000  ? 1005 HOH   A O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? -61.16800 12.24000  -8.20000  1.000 52.45000  ? 1006 HOH   A O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? -53.42100 13.20600  3.87100   1.000 16.28000  ? 1007 HOH   A O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? -37.53300 -2.18100  -4.11000  1.000 29.35000  ? 1008 HOH   A O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? -64.86200 16.25800  -1.80800  1.000 35.13000  ? 1009 HOH   A O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? -63.74900 19.01400  -2.94500  1.000 43.67000  ? 1010 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? -40.82700 -7.36700  -0.65500  1.000 32.96000  ? 1011 HOH   A O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? -34.15600 1.83700   13.61400  1.000 38.72000  ? 1012 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? -52.99100 18.66300  6.48200   1.000 28.20000  ? 1013 HOH   A O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? -62.71600 5.38600   8.61700   1.000 47.18000  ? 1014 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? -69.94100 14.04900  25.92600  1.000 44.27000  ? 1015 HOH   A O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? -32.44800 13.24500  -10.31300 1.000 47.57000  ? 1016 HOH   A O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? -37.36100 12.07900  25.15100  1.000 28.31000  ? 1017 HOH   A O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? -57.73100 19.46500  -5.27100  1.000 25.29000  ? 1018 HOH   A O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? -49.33300 8.11500   38.63400  1.000 25.38000  ? 1019 HOH   A O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? -52.43500 2.43500   1.74300   1.000 21.38000  ? 1020 HOH   A O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? -38.78800 10.66700  37.53100  1.000 54.82000  ? 1021 HOH   A O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? -61.77500 15.88900  36.16600  1.000 46.08000  ? 1022 HOH   A O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? -55.32000 5.90700   37.41800  1.000 25.15000  ? 1023 HOH   A O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? -31.89700 20.13200  7.15900   1.000 31.82000  ? 1024 HOH   A O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? -58.56400 26.21200  -4.56300  1.000 36.99000  ? 1025 HOH   A O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? -49.97400 15.27100  1.64900   1.000 17.23000  ? 1026 HOH   A O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? -32.47900 -1.30300  6.35500   1.000 27.70000  ? 1027 HOH   A O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? -44.80000 -6.16500  6.72100   1.000 38.03000  ? 1028 HOH   A O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? -65.08900 26.46000  10.51200  1.000 20.04000  ? 1029 HOH   A O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? -40.32700 15.25300  -7.26600  1.000 42.17000  ? 1030 HOH   A O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? -56.03900 18.82700  30.91000  1.000 44.63000  ? 1031 HOH   A O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? -46.37100 2.39600   20.64300  1.000 17.20000  ? 1032 HOH   A O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? -64.33800 30.55800  12.53700  1.000 26.11000  ? 1033 HOH   A O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? -38.23600 22.02000  26.59400  1.000 29.71000  ? 1034 HOH   A O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? -59.77300 8.66200   8.39400   1.000 29.54000  ? 1035 HOH   A O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? -52.03600 4.18300   19.86000  1.000 13.92000  ? 1036 HOH   A O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? -50.76300 29.97400  6.18700   1.000 35.40000  ? 1037 HOH   A O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? -65.76800 18.00900  30.93300  1.000 40.65000  ? 1038 HOH   A O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? -59.83400 28.68000  19.94700  1.000 46.10000  ? 1039 HOH   A O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? -39.67000 24.38400  28.39500  1.000 28.58000  ? 1040 HOH   A O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? -44.56800 6.25900   28.49100  1.000 18.79000  ? 1041 HOH   A O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? -61.32000 25.55300  18.19000  1.000 29.06000  ? 1042 HOH   A O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? -33.36200 21.71100  4.61900   1.000 30.49000  ? 1043 HOH   A O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? -26.62700 1.97400   -0.69400  1.000 51.72000  ? 1044 HOH   A O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? -53.61500 14.82400  11.42900  1.000 24.73000  ? 1045 HOH   A O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? -59.11200 12.12900  13.85200  1.000 47.73000  ? 1046 HOH   A O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? -50.25100 19.03200  37.11000  1.000 26.67000  ? 1047 HOH   A O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? -36.69300 11.70300  27.53600  1.000 32.47000  ? 1048 HOH   A O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? -40.50300 1.69500   26.15400  1.000 33.49000  ? 1049 HOH   A O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? -62.27200 14.87700  -8.35600  1.000 35.78000  ? 1050 HOH   A O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? -54.51100 16.93200  31.65700  1.000 40.50000  ? 1051 HOH   A O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? -26.90400 4.90500   11.79900  1.000 36.86000  ? 1052 HOH   A O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? -56.78800 -5.63200  15.37000  1.000 23.86000  ? 1053 HOH   A O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? -50.42600 13.01200  5.70100   1.000 16.39000  ? 1054 HOH   A O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? -30.38800 8.92300   -10.21900 1.000 51.23000  ? 1055 HOH   A O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? -59.89000 10.60700  -2.60800  1.000 35.76000  ? 1056 HOH   A O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? -34.67500 22.37300  -3.96500  1.000 49.68000  ? 1057 HOH   A O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? -26.92400 4.33000   -5.11100  1.000 53.35000  ? 1058 HOH   A O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? -58.23500 6.28300   -1.63300  1.000 40.48000  ? 1059 HOH   A O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? -55.37300 14.80200  35.76900  1.000 30.30000  ? 1060 HOH   A O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? -46.16300 13.95800  -11.48400 1.000 32.09000  ? 1061 HOH   A O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? -47.49000 16.75300  18.74900  1.000 23.57000  ? 1062 HOH   A O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? -51.05000 15.82900  40.06900  1.000 41.14000  ? 1063 HOH   A O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? -45.25800 18.28000  -5.89200  1.000 24.78000  ? 1064 HOH   A O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? -44.89800 34.56200  -2.70100  1.000 50.05000  ? 1065 HOH   A O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? -67.70000 19.14300  16.03400  1.000 49.41000  ? 1066 HOH   A O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? -31.19400 -1.79400  -2.46300  1.000 44.36000  ? 1067 HOH   A O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? -38.91900 0.83600   -6.24500  1.000 42.92000  ? 1068 HOH   A O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? -55.23700 24.46000  7.25800   1.000 21.60000  ? 1069 HOH   A O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? -44.06400 1.54300   23.04100  1.000 18.30000  ? 1070 HOH   A O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? -37.84700 16.07100  19.23800  1.000 27.75000  ? 1071 HOH   A O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? -38.03900 -1.53500  16.43500  1.000 34.83000  ? 1072 HOH   A O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? -49.15200 18.22700  4.78200   1.000 28.48000  ? 1073 HOH   A O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? -39.93800 6.72200   30.37500  1.000 43.59000  ? 1074 HOH   A O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? -31.65800 -0.04200  -6.14200  1.000 34.54000  ? 1075 HOH   A O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? -58.63500 7.32100   0.66300   1.000 27.93000  ? 1076 HOH   A O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? -37.83200 24.53300  2.80700   1.000 28.99000  ? 1077 HOH   A O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? -37.05700 14.01500  28.93600  1.000 33.72000  ? 1078 HOH   A O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? -31.21400 17.35400  21.20000  1.000 44.29000  ? 1079 HOH   A O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? -58.91400 10.37300  41.01300  1.000 42.96000  ? 1080 HOH   A O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? -46.24000 8.52600   37.87400  1.000 23.49000  ? 1081 HOH   A O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? -74.01600 21.79000  22.37000  1.000 40.80000  ? 1082 HOH   A O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? -61.62300 15.63800  4.36600   1.000 51.36000  ? 1083 HOH   A O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? -50.31300 1.86300   19.30600  1.000 14.80000  ? 1084 HOH   A O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? -57.55200 9.46800   -3.91900  1.000 32.66000  ? 1085 HOH   A O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? -38.15100 21.06200  24.07900  1.000 29.24000  ? 1086 HOH   A O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? -29.15600 11.47400  8.49300   1.000 38.34000  ? 1087 HOH   A O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? -39.59100 23.76600  8.52900   1.000 43.59000  ? 1088 HOH   A O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? -38.88500 -3.05000  13.43000  1.000 50.30000  ? 1089 HOH   A O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? -38.63700 18.69400  -9.40800  1.000 40.90000  ? 1090 HOH   A O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? -54.25500 14.40900  -8.01800  1.000 31.55000  ? 1091 HOH   A O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? -58.61500 6.39100   32.38100  1.000 34.36000  ? 1092 HOH   A O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? -35.93900 15.87200  21.55200  1.000 38.46000  ? 1093 HOH   A O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? -25.52300 1.69200   5.66200   1.000 32.36000  ? 1094 HOH   A O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? -67.06100 25.77400  15.44800  1.000 31.38000  ? 1095 HOH   A O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? -30.93800 -3.22600  5.38600   1.000 44.26000  ? 1096 HOH   A O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? -57.17600 -0.24900  3.60100   1.000 45.47000  ? 1097 HOH   A O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? -46.85100 -4.06100  16.63800  1.000 16.00000  ? 1098 HOH   A O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? -34.99400 -2.33700  7.38000   1.000 35.70000  ? 1099 HOH   A O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? -24.09100 12.37100  -1.61200  1.000 49.04000  ? 1100 HOH   A O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? -64.99300 26.52200  18.56500  1.000 39.09000  ? 1101 HOH   A O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? -33.99500 -5.86200  -5.48400  1.000 52.22000  ? 1102 HOH   A O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? -37.61000 21.48300  -8.32200  1.000 50.26000  ? 1103 HOH   A O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? -44.11600 -3.54200  -4.29800  1.000 32.47000  ? 1104 HOH   A O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? -52.28200 -4.04700  4.88500   1.000 29.49000  ? 1105 HOH   A O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? -26.29300 8.15700   4.99400   1.000 51.35000  ? 1106 HOH   A O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? -40.219   24.764    -10.272   1.000 42.31000  ? 1107 HOH   A O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? -28.86800 16.72800  -0.12400  1.000 52.03000  ? 1108 HOH   A O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? -24.20600 4.75700   5.12800   1.000 42.36000  ? 1109 HOH   A O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? -39.96100 21.43900  -9.62100  1.000 35.26000  ? 1110 HOH   A O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? -50.97000 3.13900   -8.20200  1.000 46.66000  ? 1111 HOH   A O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? -37.71000 14.09200  33.45100  1.000 49.76000  ? 1112 HOH   A O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? -55.39900 11.28400  -10.18600 1.000 36.56000  ? 1113 HOH   A O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? -36.36700 14.54900  24.05600  1.000 32.23000  ? 1114 HOH   A O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? -48.53200 -5.69900  6.10800   1.000 36.85000  ? 1115 HOH   A O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? -36.35200 20.41800  -3.41800  1.000 23.78000  ? 1116 HOH   A O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? -36.64300 15.94600  -9.66200  1.000 38.19000  ? 1117 HOH   A O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? -50.65700 -1.52100  -2.56400  1.000 22.49000  ? 1118 HOH   A O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? -48.25600 12.75400  -12.09400 1.000 30.29000  ? 1119 HOH   A O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? -35.92500 -2.57700  12.99400  1.000 39.45000  ? 1120 HOH   A O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? -37.13800 16.20100  27.96800  1.000 34.77000  ? 1121 HOH   A O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? -52.59100 24.85900  25.28100  1.000 39.58000  ? 1122 HOH   A O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? -52.61000 20.61500  8.21300   1.000 27.98000  ? 1123 HOH   A O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? -41.75100 -0.36500  21.35500  1.000 24.36000  ? 1124 HOH   A O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? -60.35900 22.92100  26.30100  1.000 47.24000  ? 1125 HOH   A O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? -62.36300 4.68900   33.55300  1.000 46.14000  ? 1126 HOH   A O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? -44.40700 23.14000  6.26400   1.000 23.43000  ? 1127 HOH   A O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? -65.692   0.245     20.944    1.000 53.15000  ? 1128 HOH   A O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? -61.27700 15.20500  2.14200   1.000 30.44000  ? 1129 HOH   A O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? -59.10600 6.05700   38.83700  1.000 48.91000  ? 1130 HOH   A O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? -57.01000 17.54900  10.25500  1.000 41.37000  ? 1131 HOH   A O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? -32.59600 -1.30100  -8.74300  1.000 39.24000  ? 1132 HOH   A O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? -60.63400 19.53100  5.67400   1.000 40.66000  ? 1133 HOH   A O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? -62.94000 20.04500  -0.32100  1.000 38.35000  ? 1134 HOH   A O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? -51.48700 17.62800  4.79200   1.000 32.82000  ? 1135 HOH   A O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? -46.74500 12.99900  11.82300  1.000 29.81000  ? 1136 HOH   A O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? -61.442   1.091     28.664    1.000 37.60000  ? 1137 HOH   A O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? -56.30100 18.57200  8.33100   1.000 48.80000  ? 1138 HOH   A O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? -62.42800 10.10900  -4.07100  1.000 51.40000  ? 1139 HOH   A O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? -61.54500 24.83000  -3.13300  1.000 46.83000  ? 1140 HOH   A O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? -28.83300 0.88100   -6.31700  1.000 46.03000  ? 1141 HOH   A O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? -59.158   -4.379    11.591    1.000 41.67000  ? 1142 HOH   A O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? -45.083   27.404    11.009    1.000 42.80000  ? 1143 HOH   A O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? -34.304   23.738    -7.956    1.000 44.05000  ? 1144 HOH   A O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? -30.12500 1.06200   15.45200  1.000 48.30000  ? 1145 HOH   A O   1 
HETATM 2525 O  O   . HOH   H 5 .   ? -61.34800 5.98400   11.05000  1.000 46.71000  ? 1146 HOH   A O   1 
HETATM 2526 O  O   . HOH   H 5 .   ? -54.80300 17.41100  10.02900  1.000 38.18000  ? 1147 HOH   A O   1 
HETATM 2527 O  O   . HOH   H 5 .   ? -49.20500 -4.85700  3.50700   1.000 39.90000  ? 1148 HOH   A O   1 
HETATM 2528 O  O   . HOH   H 5 .   ? -61.83700 17.81000  4.75900   1.000 47.68000  ? 1149 HOH   A O   1 
HETATM 2529 O  O   . HOH   H 5 .   ? -43.18400 14.67900  -8.98400  1.000 40.97000  ? 1150 HOH   A O   1 
HETATM 2530 O  O   . HOH   H 5 .   ? -57.434   -4.447    9.994     1.000 45.88000  ? 1151 HOH   A O   1 
HETATM 2531 O  O   . HOH   H 5 .   ? -47.72900 0.74300   21.20700  1.000 32.97000  ? 1152 HOH   A O   1 
HETATM 2532 O  O   . HOH   H 5 .   ? -39.08300 -2.00200  -5.67400  1.000 52.47000  ? 1153 HOH   A O   1 
HETATM 2533 O  O   . HOH   H 5 .   ? -42.93500 2.65700   -6.88700  1.000 49.94000  ? 1154 HOH   A O   1 
HETATM 2534 O  O   . HOH   H 5 .   ? -51.43100 15.15500  4.04700   1.000 16.64000  ? 1155 HOH   A O   1 
HETATM 2535 O  O   . HOH   H 5 .   ? -60.96200 6.03800   4.92300   1.000 54.31000  ? 1156 HOH   A O   1 
HETATM 2536 O  O   . HOH   H 5 .   ? -62.24300 10.25300  -6.56800  1.000 55.71000  ? 1157 HOH   A O   1 
HETATM 2537 O  O   . HOH   H 5 .   ? -43.598   34.294    -7.381    1.000 30.91000  ? 1158 HOH   A O   1 
HETATM 2538 O  O   . HOH   H 5 .   ? -67.52300 3.65900   23.99400  1.000 56.49000  ? 1159 HOH   A O   1 
HETATM 2539 O  O   . HOH   H 5 .   ? -28.59100 -1.30800  -2.85200  1.000 52.28000  ? 1160 HOH   A O   1 
HETATM 2540 O  O   . HOH   H 5 .   ? -31.46600 -0.56900  -10.55500 1.000 50.47000  ? 1161 HOH   A O   1 
HETATM 2541 O  O   . HOH   H 5 .   ? -40.13000 -2.23100  15.20500  1.000 40.05000  ? 1162 HOH   A O   1 
HETATM 2542 O  O   . HOH   H 5 .   ? -51.82800 6.60200   40.01100  1.000 51.34000  ? 1163 HOH   A O   1 
HETATM 2543 O  O   . HOH   H 5 .   ? -58.05600 13.19600  -9.43300  1.000 50.94000  ? 1164 HOH   A O   1 
HETATM 2544 O  O   . HOH   H 5 .   ? -43.17300 4.78500   31.92400  1.000 31.09000  ? 1165 HOH   A O   1 
HETATM 2545 O  O   . HOH   H 5 .   ? -56.99300 22.77500  8.70300   1.000 30.11000  ? 1166 HOH   A O   1 
HETATM 2546 O  O   . HOH   H 5 .   ? -29.64100 2.36800   18.40600  1.000 49.92000  ? 1167 HOH   A O   1 
HETATM 2547 O  O   . HOH   H 5 .   ? -32.09900 8.80400   -11.63900 1.000 53.52000  ? 1168 HOH   A O   1 
HETATM 2548 O  O   . HOH   H 5 .   ? -68.243   22.031    8.973     1.000 53.25000  ? 1169 HOH   A O   1 
HETATM 2549 O  O   . HOH   H 5 .   ? -63.86100 1.59000   26.51300  1.000 45.85000  ? 1170 HOH   A O   1 
HETATM 2550 O  O   . HOH   H 5 .   ? -41.75100 -4.90900  -4.42100  1.000 33.66000  ? 1171 HOH   A O   1 
HETATM 2551 O  O   . HOH   H 5 .   ? -53.50500 22.41800  6.88800   1.000 28.34000  ? 1172 HOH   A O   1 
HETATM 2552 O  O   . HOH   H 5 .   ? -53.40900 8.15300   40.18000  1.000 44.10000  ? 1173 HOH   A O   1 
HETATM 2553 O  O   . HOH   H 5 .   ? -40.27900 0.00000   23.00500  0.50  44.46000  ? 1174 HOH   A O   1 
HETATM 2554 O  O   . HOH   H 5 .   ? -48.85100 2.43800   -8.47300  1.000 45.24000  ? 1175 HOH   A O   1 
HETATM 2555 O  O   . HOH   H 5 .   ? -37.004   0.977     23.836    1.000 45.16000  ? 1176 HOH   A O   1 
HETATM 2556 O  O   . HOH   H 5 .   ? -48.00200 -5.42600  -2.57100  1.000 44.09000  ? 1177 HOH   A O   1 
HETATM 2557 O  O   . HOH   H 5 .   ? -50.18200 -4.10600  -3.25900  1.000 35.26000  ? 1178 HOH   A O   1 
HETATM 2558 O  O   . HOH   H 5 .   ? -51.597   8.458     38.819    1.000 42.57000  ? 1179 HOH   A O   1 
HETATM 2559 O  O   . HOH   H 5 .   ? -30.80000 -0.11300  11.25200  1.000 36.01000  ? 1180 HOH   A O   1 
HETATM 2560 O  O   . HOH   H 5 .   ? -63.946   24.347    -2.936    1.000 53.90000  ? 1181 HOH   A O   1 
HETATM 2561 O  O   . HOH   H 5 .   ? -48.12900 -6.75300  -0.20600  1.000 45.47000  ? 1182 HOH   A O   1 
HETATM 2562 O  O   . HOH   H 5 .   ? -39.13200 -6.42300  7.57300   1.000 49.11000  ? 1183 HOH   A O   1 
HETATM 2563 O  O   . HOH   H 5 .   ? -55.38300 33.27900  11.97700  1.000 29.49000  ? 1184 HOH   A O   1 
HETATM 2564 O  O   . HOH   H 5 .   ? -63.45500 11.28100  34.97400  1.000 48.00000  ? 1185 HOH   A O   1 
HETATM 2565 O  O   . HOH   H 5 .   ? -50.283   30.912    2.795     1.000 49.30000  ? 1186 HOH   A O   1 
HETATM 2566 O  O   . HOH   H 5 .   ? -28.48000 -4.52600  5.23500   1.000 54.38000  ? 1187 HOH   A O   1 
HETATM 2567 O  O   . HOH   H 5 .   ? -35.07700 -3.24100  -4.95200  1.000 39.11000  ? 1188 HOH   A O   1 
HETATM 2568 O  O   . HOH   H 5 .   ? -27.33100 2.16000   -5.02900  1.000 52.21000  ? 1189 HOH   A O   1 
HETATM 2569 O  O   . HOH   H 5 .   ? -41.48200 -7.64800  -3.15100  1.000 40.69000  ? 1190 HOH   A O   1 
HETATM 2570 O  O   . HOH   H 5 .   ? -40.66500 3.75600   27.94100  1.000 34.77000  ? 1191 HOH   A O   1 
HETATM 2571 O  O   . HOH   H 5 .   ? -47.84800 10.12900  39.19000  1.000 35.36000  ? 1192 HOH   A O   1 
HETATM 2572 O  O   . HOH   H 5 .   ? -67.67100 20.93800  13.68100  1.000 51.47000  ? 1193 HOH   A O   1 
HETATM 2573 O  O   . HOH   H 5 .   ? -54.68900 -0.81200  3.19000   1.000 45.47000  ? 1194 HOH   A O   1 
HETATM 2574 O  O   . HOH   H 5 .   ? -41.01600 1.46100   -7.01000  1.000 49.41000  ? 1195 HOH   A O   1 
HETATM 2575 O  O   . HOH   H 5 .   ? -53.62100 21.69200  -11.25100 1.000 53.21000  ? 1196 HOH   A O   1 
HETATM 2576 O  O   . HOH   H 5 .   ? -68.34200 30.40500  17.12900  1.000 52.46000  ? 1197 HOH   A O   1 
HETATM 2577 O  O   . HOH   H 5 .   ? -60.88400 8.24500   10.63700  1.000 37.42000  ? 1198 HOH   A O   1 
HETATM 2578 O  O   . HOH   H 5 .   ? -31.64900 -2.57300  10.12400  1.000 48.38000  ? 1199 HOH   A O   1 
HETATM 2579 O  O   . HOH   H 5 .   ? -42.06500 5.35900   29.62000  1.000 34.67000  ? 1200 HOH   A O   1 
HETATM 2580 O  O   . HOH   H 5 .   ? -53.48400 17.74500  33.72800  1.000 47.14000  ? 1201 HOH   A O   1 
HETATM 2581 O  O   . HOH   H 5 .   ? -32.74400 -2.61700  -4.74800  1.000 41.57000  ? 1202 HOH   A O   1 
HETATM 2582 O  O   . HOH   H 5 .   ? -46.08000 0.00000   23.00500  0.50  28.36000  ? 1203 HOH   A O   1 
HETATM 2583 O  O   . HOH   H 5 .   ? -66.12800 28.86000  11.42800  1.000 25.08000  ? 1204 HOH   A O   1 
HETATM 2584 O  O   . HOH   H 5 .   ? -59.29700 10.46300  11.76800  1.000 39.21000  ? 1205 HOH   A O   1 
HETATM 2585 O  O   . HOH   H 5 .   ? -55.623   5.211     40.334    1.000 37.82000  ? 1206 HOH   A O   1 
HETATM 2586 O  O   . HOH   H 5 .   ? -39.419   14.276    35.798    1.000 47.10000  ? 1207 HOH   A O   1 
HETATM 2587 O  O   . HOH   H 5 .   ? -52.57700 19.98100  35.42200  1.000 43.72000  ? 1208 HOH   A O   1 
HETATM 2588 O  O   . HOH   H 5 .   ? -40.50000 3.39800   -11.31900 1.000 52.86000  ? 1209 HOH   A O   1 
HETATM 2589 O  O   . HOH   H 5 .   ? -37.36700 18.73500  24.17300  1.000 35.13000  ? 1210 HOH   A O   1 
HETATM 2590 O  O   . HOH   H 5 .   ? -54.23900 2.24700   -6.35900  1.000 49.57000  ? 1211 HOH   A O   1 
HETATM 2591 O  O   . HOH   H 5 .   ? -26.45000 2.29300   11.50300  1.000 57.66000  ? 1212 HOH   A O   1 
HETATM 2592 O  O   . HOH   H 5 .   ? -28.20400 0.40900   11.97100  1.000 47.51000  ? 1213 HOH   A O   1 
HETATM 2593 O  O   . HOH   H 5 .   ? -52.66900 0.34600   -5.85900  1.000 44.80000  ? 1214 HOH   A O   1 
HETATM 2594 O  O   . HOH   H 5 .   ? -51.39700 -5.95900  2.98600   1.000 42.85000  ? 1215 HOH   A O   1 
HETATM 2595 O  O   . HOH   H 5 .   ? -54.54700 -3.32000  4.11400   1.000 39.76000  ? 1216 HOH   A O   1 
HETATM 2596 O  O   . HOH   H 5 .   ? -63.28300 18.25000  1.71100   1.000 44.81000  ? 1217 HOH   A O   1 
HETATM 2597 O  O   . HOH   H 5 .   ? -35.83900 24.78800  4.30300   1.000 44.09000  ? 1218 HOH   A O   1 
HETATM 2598 O  O   . HOH   H 5 .   ? -58.00300 3.20300   -1.77400  1.000 49.31000  ? 1219 HOH   A O   1 
HETATM 2599 O  O   . HOH   H 5 .   ? -46.01400 -5.43300  -4.12200  1.000 36.01000  ? 1220 HOH   A O   1 
HETATM 2600 O  O   . HOH   H 5 .   ? -38.30100 7.46600   -11.53100 1.000 40.58000  ? 1221 HOH   A O   1 
HETATM 2601 O  O   . HOH   H 5 .   ? -54.30900 0.60300   0.96300   1.000 40.27000  ? 1222 HOH   A O   1 
HETATM 2602 O  O   . HOH   H 5 .   ? -48.63500 14.66500  -14.11200 1.000 49.22000  ? 1223 HOH   A O   1 
HETATM 2603 O  O   . HOH   H 5 .   ? -71.39300 17.68500  28.06300  1.000 45.11000  ? 1224 HOH   A O   1 
HETATM 2604 O  O   . HOH   H 5 .   ? -37.80500 16.35600  25.29500  1.000 30.62000  ? 1225 HOH   A O   1 
HETATM 2605 O  O   . HOH   H 5 .   ? -34.09100 24.01000  5.51200   1.000 39.60000  ? 1226 HOH   A O   1 
HETATM 2606 O  O   . HOH   H 5 .   ? -53.27200 -1.54900  -1.68500  1.000 36.96000  ? 1227 HOH   A O   1 
HETATM 2607 O  O   . HOH   H 5 .   ? -60.33000 5.87500   2.58300   1.000 36.69000  ? 1228 HOH   A O   1 
HETATM 2608 O  O   . HOH   H 5 .   ? -47.109   -8.912    4.315     1.000 48.26000  ? 1229 HOH   A O   1 
# 
