data_9BV8
# 
_entry.id   9BV8 
# 
_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   9BV8         pdb_00009bv8 10.2210/pdb9bv8/pdb 
WWPDB D_1000284181 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-04-23 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
6 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BV8 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              taosheng.chen@stjude.org 
_pdbx_contact_author.name_first         Taosheng 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6420-3809 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Jingheng, W.'      1 0000-0001-5747-6673 
'Nithianantham, S.' 2 0000-0001-6238-647X 
'Miller, D.J.'      3 0000-0003-1202-511X 
'Chen, T.'          4 0000-0001-6420-3809 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3423 
_citation.page_last                 3423 
_citation.title                     'Decoding the selective chemical modulation of CYP3A4.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58749-8 
_citation.pdbx_database_id_PubMed   40210880 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, J.'          1  ? 
primary 'Nithianantham, S.' 2  ? 
primary 'Chai, S.C.'        3  ? 
primary 'Jung, Y.H.'        4  ? 
primary 'Yang, L.'          5  ? 
primary 'Ong, H.W.'         6  ? 
primary 'Li, Y.'            7  ? 
primary 'Zhang, Y.'         8  ? 
primary 'Miller, D.J.'      9  ? 
primary 'Chen, T.'          10 ? 
# 
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 'Cytochrome P450 3A4'                                                           55594.637 1 
1.14.14.1,1.14.14.56,1.14.14.73,1.14.14.55 ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                               616.487   1 ? ? ? ? 
3 non-polymer syn 'N-[(2P)-2-(1H-imidazol-1-yl)-5-(trifluoromethyl)phenyl]cyclobutanecarboxamide' 309.286   1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;1,4-cineole 2-exo-monooxygenase,8-cineole 2-exo-monooxygenase,Albendazole monooxygenase (sulfoxide-forming),Albendazole sulfoxidase,CYPIIIA3,CYPIIIA4,Cholesterol 25-hydroxylase,Cytochrome P450 3A3,Cytochrome P450 HLp,Cytochrome P450 NF-25,Cytochrome P450-PCN1,Nifedipine oxidase,Quinine 3-monooxygenase
;
# 
_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       
;MALYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSV
FTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRL
EDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPN
KAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVS
GAHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MALYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSV
FTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRL
EDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPN
KAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVS
GAHHHH
;
_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 'PROTOPORPHYRIN IX CONTAINING FE'                                               HEM   
3 'N-[(2P)-2-(1H-imidazol-1-yl)-5-(trifluoromethyl)phenyl]cyclobutanecarboxamide' A1ASS 
# 
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   ALA n 
1 3   LEU n 
1 4   TYR n 
1 5   GLY n 
1 6   THR n 
1 7   HIS n 
1 8   SER n 
1 9   HIS n 
1 10  GLY n 
1 11  LEU n 
1 12  PHE n 
1 13  LYS n 
1 14  LYS n 
1 15  LEU n 
1 16  GLY n 
1 17  ILE n 
1 18  PRO n 
1 19  GLY n 
1 20  PRO n 
1 21  THR n 
1 22  PRO n 
1 23  LEU n 
1 24  PRO n 
1 25  PHE n 
1 26  LEU n 
1 27  GLY n 
1 28  ASN n 
1 29  ILE n 
1 30  LEU n 
1 31  SER n 
1 32  TYR n 
1 33  HIS n 
1 34  LYS n 
1 35  GLY n 
1 36  PHE n 
1 37  CYS n 
1 38  MET n 
1 39  PHE n 
1 40  ASP n 
1 41  MET n 
1 42  GLU n 
1 43  CYS n 
1 44  HIS n 
1 45  LYS n 
1 46  LYS n 
1 47  TYR n 
1 48  GLY n 
1 49  LYS n 
1 50  VAL n 
1 51  TRP n 
1 52  GLY n 
1 53  PHE n 
1 54  TYR n 
1 55  ASP n 
1 56  GLY n 
1 57  GLN n 
1 58  GLN n 
1 59  PRO n 
1 60  VAL n 
1 61  LEU n 
1 62  ALA n 
1 63  ILE n 
1 64  THR n 
1 65  ASP n 
1 66  PRO n 
1 67  ASP n 
1 68  MET n 
1 69  ILE n 
1 70  LYS n 
1 71  THR n 
1 72  VAL n 
1 73  LEU n 
1 74  VAL n 
1 75  LYS n 
1 76  GLU n 
1 77  CYS n 
1 78  TYR n 
1 79  SER n 
1 80  VAL n 
1 81  PHE n 
1 82  THR n 
1 83  ASN n 
1 84  ARG n 
1 85  ARG n 
1 86  PRO n 
1 87  PHE n 
1 88  GLY n 
1 89  PRO n 
1 90  VAL n 
1 91  GLY n 
1 92  PHE n 
1 93  MET n 
1 94  LYS n 
1 95  SER n 
1 96  ALA n 
1 97  ILE n 
1 98  SER n 
1 99  ILE n 
1 100 ALA n 
1 101 GLU n 
1 102 ASP n 
1 103 GLU n 
1 104 GLU n 
1 105 TRP n 
1 106 LYS n 
1 107 ARG n 
1 108 LEU n 
1 109 ARG n 
1 110 SER n 
1 111 LEU n 
1 112 LEU n 
1 113 SER n 
1 114 PRO n 
1 115 THR n 
1 116 PHE n 
1 117 THR n 
1 118 SER n 
1 119 GLY n 
1 120 LYS n 
1 121 LEU n 
1 122 LYS n 
1 123 GLU n 
1 124 MET n 
1 125 VAL n 
1 126 PRO n 
1 127 ILE n 
1 128 ILE n 
1 129 ALA n 
1 130 GLN n 
1 131 TYR n 
1 132 GLY n 
1 133 ASP n 
1 134 VAL n 
1 135 LEU n 
1 136 VAL n 
1 137 ARG n 
1 138 ASN n 
1 139 LEU n 
1 140 ARG n 
1 141 ARG n 
1 142 GLU n 
1 143 ALA n 
1 144 GLU n 
1 145 THR n 
1 146 GLY n 
1 147 LYS n 
1 148 PRO n 
1 149 VAL n 
1 150 THR n 
1 151 LEU n 
1 152 LYS n 
1 153 ASP n 
1 154 VAL n 
1 155 PHE n 
1 156 GLY n 
1 157 ALA n 
1 158 TYR n 
1 159 SER n 
1 160 MET n 
1 161 ASP n 
1 162 VAL n 
1 163 ILE n 
1 164 THR n 
1 165 SER n 
1 166 THR n 
1 167 SER n 
1 168 PHE n 
1 169 GLY n 
1 170 VAL n 
1 171 ASN n 
1 172 ILE n 
1 173 ASP n 
1 174 SER n 
1 175 LEU n 
1 176 ASN n 
1 177 ASN n 
1 178 PRO n 
1 179 GLN n 
1 180 ASP n 
1 181 PRO n 
1 182 PHE n 
1 183 VAL n 
1 184 GLU n 
1 185 ASN n 
1 186 THR n 
1 187 LYS n 
1 188 LYS n 
1 189 LEU n 
1 190 LEU n 
1 191 ARG n 
1 192 PHE n 
1 193 ASP n 
1 194 PHE n 
1 195 LEU n 
1 196 ASP n 
1 197 PRO n 
1 198 PHE n 
1 199 PHE n 
1 200 LEU n 
1 201 SER n 
1 202 ILE n 
1 203 THR n 
1 204 VAL n 
1 205 PHE n 
1 206 PRO n 
1 207 PHE n 
1 208 LEU n 
1 209 ILE n 
1 210 PRO n 
1 211 ILE n 
1 212 LEU n 
1 213 GLU n 
1 214 VAL n 
1 215 LEU n 
1 216 ASN n 
1 217 ILE n 
1 218 CYS n 
1 219 VAL n 
1 220 PHE n 
1 221 PRO n 
1 222 ARG n 
1 223 GLU n 
1 224 VAL n 
1 225 THR n 
1 226 ASN n 
1 227 PHE n 
1 228 LEU n 
1 229 ARG n 
1 230 LYS n 
1 231 SER n 
1 232 VAL n 
1 233 LYS n 
1 234 ARG n 
1 235 MET n 
1 236 LYS n 
1 237 GLU n 
1 238 SER n 
1 239 ARG n 
1 240 LEU n 
1 241 GLU n 
1 242 ASP n 
1 243 THR n 
1 244 GLN n 
1 245 LYS n 
1 246 HIS n 
1 247 ARG n 
1 248 VAL n 
1 249 ASP n 
1 250 PHE n 
1 251 LEU n 
1 252 GLN n 
1 253 LEU n 
1 254 MET n 
1 255 ILE n 
1 256 ASP n 
1 257 SER n 
1 258 GLN n 
1 259 ASN n 
1 260 SER n 
1 261 LYS n 
1 262 GLU n 
1 263 THR n 
1 264 GLU n 
1 265 SER n 
1 266 HIS n 
1 267 LYS n 
1 268 ALA n 
1 269 LEU n 
1 270 SER n 
1 271 ASP n 
1 272 LEU n 
1 273 GLU n 
1 274 LEU n 
1 275 VAL n 
1 276 ALA n 
1 277 GLN n 
1 278 SER n 
1 279 ILE n 
1 280 ILE n 
1 281 PHE n 
1 282 ILE n 
1 283 PHE n 
1 284 ALA n 
1 285 GLY n 
1 286 TYR n 
1 287 GLU n 
1 288 THR n 
1 289 THR n 
1 290 SER n 
1 291 SER n 
1 292 VAL n 
1 293 LEU n 
1 294 SER n 
1 295 PHE n 
1 296 ILE n 
1 297 MET n 
1 298 TYR n 
1 299 GLU n 
1 300 LEU n 
1 301 ALA n 
1 302 THR n 
1 303 HIS n 
1 304 PRO n 
1 305 ASP n 
1 306 VAL n 
1 307 GLN n 
1 308 GLN n 
1 309 LYS n 
1 310 LEU n 
1 311 GLN n 
1 312 GLU n 
1 313 GLU n 
1 314 ILE n 
1 315 ASP n 
1 316 ALA n 
1 317 VAL n 
1 318 LEU n 
1 319 PRO n 
1 320 ASN n 
1 321 LYS n 
1 322 ALA n 
1 323 PRO n 
1 324 PRO n 
1 325 THR n 
1 326 TYR n 
1 327 ASP n 
1 328 THR n 
1 329 VAL n 
1 330 LEU n 
1 331 GLN n 
1 332 MET n 
1 333 GLU n 
1 334 TYR n 
1 335 LEU n 
1 336 ASP n 
1 337 MET n 
1 338 VAL n 
1 339 VAL n 
1 340 ASN n 
1 341 GLU n 
1 342 THR n 
1 343 LEU n 
1 344 ARG n 
1 345 LEU n 
1 346 PHE n 
1 347 PRO n 
1 348 ILE n 
1 349 ALA n 
1 350 MET n 
1 351 ARG n 
1 352 LEU n 
1 353 GLU n 
1 354 ARG n 
1 355 VAL n 
1 356 CYS n 
1 357 LYS n 
1 358 LYS n 
1 359 ASP n 
1 360 VAL n 
1 361 GLU n 
1 362 ILE n 
1 363 ASN n 
1 364 GLY n 
1 365 MET n 
1 366 PHE n 
1 367 ILE n 
1 368 PRO n 
1 369 LYS n 
1 370 GLY n 
1 371 VAL n 
1 372 VAL n 
1 373 VAL n 
1 374 MET n 
1 375 ILE n 
1 376 PRO n 
1 377 SER n 
1 378 TYR n 
1 379 ALA n 
1 380 LEU n 
1 381 HIS n 
1 382 ARG n 
1 383 ASP n 
1 384 PRO n 
1 385 LYS n 
1 386 TYR n 
1 387 TRP n 
1 388 THR n 
1 389 GLU n 
1 390 PRO n 
1 391 GLU n 
1 392 LYS n 
1 393 PHE n 
1 394 LEU n 
1 395 PRO n 
1 396 GLU n 
1 397 ARG n 
1 398 PHE n 
1 399 SER n 
1 400 LYS n 
1 401 LYS n 
1 402 ASN n 
1 403 LYS n 
1 404 ASP n 
1 405 ASN n 
1 406 ILE n 
1 407 ASP n 
1 408 PRO n 
1 409 TYR n 
1 410 ILE n 
1 411 TYR n 
1 412 THR n 
1 413 PRO n 
1 414 PHE n 
1 415 GLY n 
1 416 SER n 
1 417 GLY n 
1 418 PRO n 
1 419 ARG n 
1 420 ASN n 
1 421 CYS n 
1 422 ILE n 
1 423 GLY n 
1 424 MET n 
1 425 ARG n 
1 426 PHE n 
1 427 ALA n 
1 428 LEU n 
1 429 MET n 
1 430 ASN n 
1 431 MET n 
1 432 LYS n 
1 433 LEU n 
1 434 ALA n 
1 435 LEU n 
1 436 ILE n 
1 437 ARG n 
1 438 VAL n 
1 439 LEU n 
1 440 GLN n 
1 441 ASN n 
1 442 PHE n 
1 443 SER n 
1 444 PHE n 
1 445 LYS n 
1 446 PRO n 
1 447 CYS n 
1 448 LYS n 
1 449 GLU n 
1 450 THR n 
1 451 GLN n 
1 452 ILE n 
1 453 PRO n 
1 454 LEU n 
1 455 LYS n 
1 456 LEU n 
1 457 SER n 
1 458 LEU n 
1 459 GLY n 
1 460 GLY n 
1 461 LEU n 
1 462 LEU n 
1 463 GLN n 
1 464 PRO n 
1 465 GLU n 
1 466 LYS n 
1 467 PRO n 
1 468 VAL n 
1 469 VAL n 
1 470 LEU n 
1 471 LYS n 
1 472 VAL n 
1 473 GLU n 
1 474 SER n 
1 475 ARG n 
1 476 ASP n 
1 477 GLY n 
1 478 THR n 
1 479 VAL n 
1 480 SER n 
1 481 GLY n 
1 482 ALA n 
1 483 HIS n 
1 484 HIS n 
1 485 HIS n 
1 486 HIS 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                   486 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CYP3A4, CYP3A3' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               DH5alpha 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pCWori 
_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 
A1ASS non-polymer         . 'N-[(2P)-2-(1H-imidazol-1-yl)-5-(trifluoromethyl)phenyl]cyclobutanecarboxamide' ?    'C15 H14 F3 N3 O' 
309.286 
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 
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  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                               HEME 
'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                                                       ?    'C6 H10 N3 O2 1' 
156.162 
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 
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   22  ?   ?   ?   A . n 
A 1 2   ALA 2   23  ?   ?   ?   A . n 
A 1 3   LEU 3   24  ?   ?   ?   A . n 
A 1 4   TYR 4   25  ?   ?   ?   A . n 
A 1 5   GLY 5   26  ?   ?   ?   A . n 
A 1 6   THR 6   27  ?   ?   ?   A . n 
A 1 7   HIS 7   28  28  HIS HIS A . n 
A 1 8   SER 8   29  29  SER SER A . n 
A 1 9   HIS 9   30  30  HIS HIS A . n 
A 1 10  GLY 10  31  31  GLY GLY A . n 
A 1 11  LEU 11  32  32  LEU LEU A . n 
A 1 12  PHE 12  33  33  PHE PHE A . n 
A 1 13  LYS 13  34  34  LYS LYS A . n 
A 1 14  LYS 14  35  35  LYS LYS A . n 
A 1 15  LEU 15  36  36  LEU LEU A . n 
A 1 16  GLY 16  37  37  GLY GLY A . n 
A 1 17  ILE 17  38  38  ILE ILE A . n 
A 1 18  PRO 18  39  39  PRO PRO A . n 
A 1 19  GLY 19  40  40  GLY GLY A . n 
A 1 20  PRO 20  41  41  PRO PRO A . n 
A 1 21  THR 21  42  42  THR THR A . n 
A 1 22  PRO 22  43  43  PRO PRO A . n 
A 1 23  LEU 23  44  44  LEU LEU A . n 
A 1 24  PRO 24  45  45  PRO PRO A . n 
A 1 25  PHE 25  46  46  PHE PHE A . n 
A 1 26  LEU 26  47  47  LEU LEU A . n 
A 1 27  GLY 27  48  48  GLY GLY A . n 
A 1 28  ASN 28  49  49  ASN ASN A . n 
A 1 29  ILE 29  50  50  ILE ILE A . n 
A 1 30  LEU 30  51  51  LEU LEU A . n 
A 1 31  SER 31  52  52  SER SER A . n 
A 1 32  TYR 32  53  53  TYR TYR A . n 
A 1 33  HIS 33  54  54  HIS HIS A . n 
A 1 34  LYS 34  55  55  LYS LYS A . n 
A 1 35  GLY 35  56  56  GLY GLY A . n 
A 1 36  PHE 36  57  57  PHE PHE A . n 
A 1 37  CYS 37  58  58  CYS CYS A . n 
A 1 38  MET 38  59  59  MET MET A . n 
A 1 39  PHE 39  60  60  PHE PHE A . n 
A 1 40  ASP 40  61  61  ASP ASP A . n 
A 1 41  MET 41  62  62  MET MET A . n 
A 1 42  GLU 42  63  63  GLU GLU A . n 
A 1 43  CYS 43  64  64  CYS CYS A . n 
A 1 44  HIS 44  65  65  HIS HIS A . n 
A 1 45  LYS 45  66  66  LYS LYS A . n 
A 1 46  LYS 46  67  67  LYS LYS A . n 
A 1 47  TYR 47  68  68  TYR TYR A . n 
A 1 48  GLY 48  69  69  GLY GLY A . n 
A 1 49  LYS 49  70  70  LYS LYS A . n 
A 1 50  VAL 50  71  71  VAL VAL A . n 
A 1 51  TRP 51  72  72  TRP TRP A . n 
A 1 52  GLY 52  73  73  GLY GLY A . n 
A 1 53  PHE 53  74  74  PHE PHE A . n 
A 1 54  TYR 54  75  75  TYR TYR A . n 
A 1 55  ASP 55  76  76  ASP ASP A . n 
A 1 56  GLY 56  77  77  GLY GLY A . n 
A 1 57  GLN 57  78  78  GLN GLN A . n 
A 1 58  GLN 58  79  79  GLN GLN A . n 
A 1 59  PRO 59  80  80  PRO PRO A . n 
A 1 60  VAL 60  81  81  VAL VAL A . n 
A 1 61  LEU 61  82  82  LEU LEU A . n 
A 1 62  ALA 62  83  83  ALA ALA A . n 
A 1 63  ILE 63  84  84  ILE ILE A . n 
A 1 64  THR 64  85  85  THR THR A . n 
A 1 65  ASP 65  86  86  ASP ASP A . n 
A 1 66  PRO 66  87  87  PRO PRO A . n 
A 1 67  ASP 67  88  88  ASP ASP A . n 
A 1 68  MET 68  89  89  MET MET A . n 
A 1 69  ILE 69  90  90  ILE ILE A . n 
A 1 70  LYS 70  91  91  LYS LYS A . n 
A 1 71  THR 71  92  92  THR THR A . n 
A 1 72  VAL 72  93  93  VAL VAL A . n 
A 1 73  LEU 73  94  94  LEU LEU A . n 
A 1 74  VAL 74  95  95  VAL VAL A . n 
A 1 75  LYS 75  96  96  LYS LYS A . n 
A 1 76  GLU 76  97  97  GLU GLU A . n 
A 1 77  CYS 77  98  98  CYS CYS A . n 
A 1 78  TYR 78  99  99  TYR TYR A . n 
A 1 79  SER 79  100 100 SER SER A . n 
A 1 80  VAL 80  101 101 VAL VAL A . n 
A 1 81  PHE 81  102 102 PHE PHE A . n 
A 1 82  THR 82  103 103 THR THR A . n 
A 1 83  ASN 83  104 104 ASN ASN A . n 
A 1 84  ARG 84  105 105 ARG ARG A . n 
A 1 85  ARG 85  106 106 ARG ARG A . n 
A 1 86  PRO 86  107 107 PRO PRO A . n 
A 1 87  PHE 87  108 108 PHE PHE A . n 
A 1 88  GLY 88  109 109 GLY GLY A . n 
A 1 89  PRO 89  110 110 PRO PRO A . n 
A 1 90  VAL 90  111 111 VAL VAL A . n 
A 1 91  GLY 91  112 112 GLY GLY A . n 
A 1 92  PHE 92  113 113 PHE PHE A . n 
A 1 93  MET 93  114 114 MET MET A . n 
A 1 94  LYS 94  115 115 LYS LYS A . n 
A 1 95  SER 95  116 116 SER SER A . n 
A 1 96  ALA 96  117 117 ALA ALA A . n 
A 1 97  ILE 97  118 118 ILE ILE A . n 
A 1 98  SER 98  119 119 SER SER A . n 
A 1 99  ILE 99  120 120 ILE ILE A . n 
A 1 100 ALA 100 121 121 ALA ALA A . n 
A 1 101 GLU 101 122 122 GLU GLU A . n 
A 1 102 ASP 102 123 123 ASP ASP A . n 
A 1 103 GLU 103 124 124 GLU GLU A . n 
A 1 104 GLU 104 125 125 GLU GLU A . n 
A 1 105 TRP 105 126 126 TRP TRP A . n 
A 1 106 LYS 106 127 127 LYS LYS A . n 
A 1 107 ARG 107 128 128 ARG ARG A . n 
A 1 108 LEU 108 129 129 LEU LEU A . n 
A 1 109 ARG 109 130 130 ARG ARG A . n 
A 1 110 SER 110 131 131 SER SER A . n 
A 1 111 LEU 111 132 132 LEU LEU A . n 
A 1 112 LEU 112 133 133 LEU LEU A . n 
A 1 113 SER 113 134 134 SER SER A . n 
A 1 114 PRO 114 135 135 PRO PRO A . n 
A 1 115 THR 115 136 136 THR THR A . n 
A 1 116 PHE 116 137 137 PHE PHE A . n 
A 1 117 THR 117 138 138 THR THR A . n 
A 1 118 SER 118 139 139 SER SER A . n 
A 1 119 GLY 119 140 140 GLY GLY A . n 
A 1 120 LYS 120 141 141 LYS LYS A . n 
A 1 121 LEU 121 142 142 LEU LEU A . n 
A 1 122 LYS 122 143 143 LYS LYS A . n 
A 1 123 GLU 123 144 144 GLU GLU A . n 
A 1 124 MET 124 145 145 MET MET A . n 
A 1 125 VAL 125 146 146 VAL VAL A . n 
A 1 126 PRO 126 147 147 PRO PRO A . n 
A 1 127 ILE 127 148 148 ILE ILE A . n 
A 1 128 ILE 128 149 149 ILE ILE A . n 
A 1 129 ALA 129 150 150 ALA ALA A . n 
A 1 130 GLN 130 151 151 GLN GLN A . n 
A 1 131 TYR 131 152 152 TYR TYR A . n 
A 1 132 GLY 132 153 153 GLY GLY A . n 
A 1 133 ASP 133 154 154 ASP ASP A . n 
A 1 134 VAL 134 155 155 VAL VAL A . n 
A 1 135 LEU 135 156 156 LEU LEU A . n 
A 1 136 VAL 136 157 157 VAL VAL A . n 
A 1 137 ARG 137 158 158 ARG ARG A . n 
A 1 138 ASN 138 159 159 ASN ASN A . n 
A 1 139 LEU 139 160 160 LEU LEU A . n 
A 1 140 ARG 140 161 161 ARG ARG A . n 
A 1 141 ARG 141 162 162 ARG ARG A . n 
A 1 142 GLU 142 163 163 GLU GLU A . n 
A 1 143 ALA 143 164 164 ALA ALA A . n 
A 1 144 GLU 144 165 165 GLU GLU A . n 
A 1 145 THR 145 166 166 THR THR A . n 
A 1 146 GLY 146 167 167 GLY GLY A . n 
A 1 147 LYS 147 168 168 LYS LYS A . n 
A 1 148 PRO 148 169 169 PRO PRO A . n 
A 1 149 VAL 149 170 170 VAL VAL A . n 
A 1 150 THR 150 171 171 THR THR A . n 
A 1 151 LEU 151 172 172 LEU LEU A . n 
A 1 152 LYS 152 173 173 LYS LYS A . n 
A 1 153 ASP 153 174 174 ASP ASP A . n 
A 1 154 VAL 154 175 175 VAL VAL A . n 
A 1 155 PHE 155 176 176 PHE PHE A . n 
A 1 156 GLY 156 177 177 GLY GLY A . n 
A 1 157 ALA 157 178 178 ALA ALA A . n 
A 1 158 TYR 158 179 179 TYR TYR A . n 
A 1 159 SER 159 180 180 SER SER A . n 
A 1 160 MET 160 181 181 MET MET A . n 
A 1 161 ASP 161 182 182 ASP ASP A . n 
A 1 162 VAL 162 183 183 VAL VAL A . n 
A 1 163 ILE 163 184 184 ILE ILE A . n 
A 1 164 THR 164 185 185 THR THR A . n 
A 1 165 SER 165 186 186 SER SER A . n 
A 1 166 THR 166 187 187 THR THR A . n 
A 1 167 SER 167 188 188 SER SER A . n 
A 1 168 PHE 168 189 189 PHE PHE A . n 
A 1 169 GLY 169 190 190 GLY GLY A . n 
A 1 170 VAL 170 191 191 VAL VAL A . n 
A 1 171 ASN 171 192 192 ASN ASN A . n 
A 1 172 ILE 172 193 193 ILE ILE A . n 
A 1 173 ASP 173 194 194 ASP ASP A . n 
A 1 174 SER 174 195 195 SER SER A . n 
A 1 175 LEU 175 196 196 LEU LEU A . n 
A 1 176 ASN 176 197 197 ASN ASN A . n 
A 1 177 ASN 177 198 198 ASN ASN A . n 
A 1 178 PRO 178 199 199 PRO PRO A . n 
A 1 179 GLN 179 200 200 GLN GLN A . n 
A 1 180 ASP 180 201 201 ASP ASP A . n 
A 1 181 PRO 181 202 202 PRO PRO A . n 
A 1 182 PHE 182 203 203 PHE PHE A . n 
A 1 183 VAL 183 204 204 VAL VAL A . n 
A 1 184 GLU 184 205 205 GLU GLU A . n 
A 1 185 ASN 185 206 206 ASN ASN A . n 
A 1 186 THR 186 207 207 THR THR A . n 
A 1 187 LYS 187 208 208 LYS LYS A . n 
A 1 188 LYS 188 209 209 LYS LYS A . n 
A 1 189 LEU 189 210 210 LEU LEU A . n 
A 1 190 LEU 190 211 211 LEU LEU A . n 
A 1 191 ARG 191 212 212 ARG ARG A . n 
A 1 192 PHE 192 213 213 PHE PHE A . n 
A 1 193 ASP 193 214 214 ASP ASP A . n 
A 1 194 PHE 194 215 215 PHE PHE A . n 
A 1 195 LEU 195 216 216 LEU LEU A . n 
A 1 196 ASP 196 217 217 ASP ASP A . n 
A 1 197 PRO 197 218 218 PRO PRO A . n 
A 1 198 PHE 198 219 219 PHE PHE A . n 
A 1 199 PHE 199 220 220 PHE PHE A . n 
A 1 200 LEU 200 221 221 LEU LEU A . n 
A 1 201 SER 201 222 222 SER SER A . n 
A 1 202 ILE 202 223 223 ILE ILE A . n 
A 1 203 THR 203 224 224 THR THR A . n 
A 1 204 VAL 204 225 225 VAL VAL A . n 
A 1 205 PHE 205 226 226 PHE PHE A . n 
A 1 206 PRO 206 227 227 PRO PRO A . n 
A 1 207 PHE 207 228 228 PHE PHE A . n 
A 1 208 LEU 208 229 229 LEU LEU A . n 
A 1 209 ILE 209 230 230 ILE ILE A . n 
A 1 210 PRO 210 231 231 PRO PRO A . n 
A 1 211 ILE 211 232 232 ILE ILE A . n 
A 1 212 LEU 212 233 233 LEU LEU A . n 
A 1 213 GLU 213 234 234 GLU GLU A . n 
A 1 214 VAL 214 235 235 VAL VAL A . n 
A 1 215 LEU 215 236 236 LEU LEU A . n 
A 1 216 ASN 216 237 237 ASN ASN A . n 
A 1 217 ILE 217 238 238 ILE ILE A . n 
A 1 218 CYS 218 239 239 CYS CYS A . n 
A 1 219 VAL 219 240 240 VAL VAL A . n 
A 1 220 PHE 220 241 241 PHE PHE A . n 
A 1 221 PRO 221 242 242 PRO PRO A . n 
A 1 222 ARG 222 243 243 ARG ARG A . n 
A 1 223 GLU 223 244 244 GLU GLU A . n 
A 1 224 VAL 224 245 245 VAL VAL A . n 
A 1 225 THR 225 246 246 THR THR A . n 
A 1 226 ASN 226 247 247 ASN ASN A . n 
A 1 227 PHE 227 248 248 PHE PHE A . n 
A 1 228 LEU 228 249 249 LEU LEU A . n 
A 1 229 ARG 229 250 250 ARG ARG A . n 
A 1 230 LYS 230 251 251 LYS LYS A . n 
A 1 231 SER 231 252 252 SER SER A . n 
A 1 232 VAL 232 253 253 VAL VAL A . n 
A 1 233 LYS 233 254 254 LYS LYS A . n 
A 1 234 ARG 234 255 255 ARG ARG A . n 
A 1 235 MET 235 256 256 MET MET A . n 
A 1 236 LYS 236 257 257 LYS LYS A . n 
A 1 237 GLU 237 258 258 GLU GLU A . n 
A 1 238 SER 238 259 259 SER SER A . n 
A 1 239 ARG 239 260 260 ARG ARG A . n 
A 1 240 LEU 240 261 261 LEU LEU A . n 
A 1 241 GLU 241 262 262 GLU GLU A . n 
A 1 242 ASP 242 263 263 ASP ASP A . n 
A 1 243 THR 243 264 264 THR THR A . n 
A 1 244 GLN 244 265 265 GLN GLN A . n 
A 1 245 LYS 245 266 266 LYS LYS A . n 
A 1 246 HIS 246 267 267 HIS HIS A . n 
A 1 247 ARG 247 268 268 ARG ARG A . n 
A 1 248 VAL 248 269 269 VAL VAL A . n 
A 1 249 ASP 249 270 270 ASP ASP A . n 
A 1 250 PHE 250 271 271 PHE PHE A . n 
A 1 251 LEU 251 272 272 LEU LEU A . n 
A 1 252 GLN 252 273 273 GLN GLN A . n 
A 1 253 LEU 253 274 274 LEU LEU A . n 
A 1 254 MET 254 275 275 MET MET A . n 
A 1 255 ILE 255 276 276 ILE ILE A . n 
A 1 256 ASP 256 277 277 ASP ASP A . n 
A 1 257 SER 257 278 278 SER SER A . n 
A 1 258 GLN 258 279 279 GLN GLN A . n 
A 1 259 ASN 259 280 280 ASN ASN A . n 
A 1 260 SER 260 281 281 SER SER A . n 
A 1 261 LYS 261 282 ?   ?   ?   A . n 
A 1 262 GLU 262 283 ?   ?   ?   A . n 
A 1 263 THR 263 284 ?   ?   ?   A . n 
A 1 264 GLU 264 285 ?   ?   ?   A . n 
A 1 265 SER 265 286 ?   ?   ?   A . n 
A 1 266 HIS 266 287 287 HIS HIS A . n 
A 1 267 LYS 267 288 288 LYS LYS A . n 
A 1 268 ALA 268 289 289 ALA ALA A . n 
A 1 269 LEU 269 290 290 LEU LEU A . n 
A 1 270 SER 270 291 291 SER SER A . n 
A 1 271 ASP 271 292 292 ASP ASP A . n 
A 1 272 LEU 272 293 293 LEU LEU A . n 
A 1 273 GLU 273 294 294 GLU GLU A . n 
A 1 274 LEU 274 295 295 LEU LEU A . n 
A 1 275 VAL 275 296 296 VAL VAL A . n 
A 1 276 ALA 276 297 297 ALA ALA A . n 
A 1 277 GLN 277 298 298 GLN GLN A . n 
A 1 278 SER 278 299 299 SER SER A . n 
A 1 279 ILE 279 300 300 ILE ILE A . n 
A 1 280 ILE 280 301 301 ILE ILE A . n 
A 1 281 PHE 281 302 302 PHE PHE A . n 
A 1 282 ILE 282 303 303 ILE ILE A . n 
A 1 283 PHE 283 304 304 PHE PHE A . n 
A 1 284 ALA 284 305 305 ALA ALA A . n 
A 1 285 GLY 285 306 306 GLY GLY A . n 
A 1 286 TYR 286 307 307 TYR TYR A . n 
A 1 287 GLU 287 308 308 GLU GLU A . n 
A 1 288 THR 288 309 309 THR THR A . n 
A 1 289 THR 289 310 310 THR THR A . n 
A 1 290 SER 290 311 311 SER SER A . n 
A 1 291 SER 291 312 312 SER SER A . n 
A 1 292 VAL 292 313 313 VAL VAL A . n 
A 1 293 LEU 293 314 314 LEU LEU A . n 
A 1 294 SER 294 315 315 SER SER A . n 
A 1 295 PHE 295 316 316 PHE PHE A . n 
A 1 296 ILE 296 317 317 ILE ILE A . n 
A 1 297 MET 297 318 318 MET MET A . n 
A 1 298 TYR 298 319 319 TYR TYR A . n 
A 1 299 GLU 299 320 320 GLU GLU A . n 
A 1 300 LEU 300 321 321 LEU LEU A . n 
A 1 301 ALA 301 322 322 ALA ALA A . n 
A 1 302 THR 302 323 323 THR THR A . n 
A 1 303 HIS 303 324 324 HIS HIS A . n 
A 1 304 PRO 304 325 325 PRO PRO A . n 
A 1 305 ASP 305 326 326 ASP ASP A . n 
A 1 306 VAL 306 327 327 VAL VAL A . n 
A 1 307 GLN 307 328 328 GLN GLN A . n 
A 1 308 GLN 308 329 329 GLN GLN A . n 
A 1 309 LYS 309 330 330 LYS LYS A . n 
A 1 310 LEU 310 331 331 LEU LEU A . n 
A 1 311 GLN 311 332 332 GLN GLN A . n 
A 1 312 GLU 312 333 333 GLU GLU A . n 
A 1 313 GLU 313 334 334 GLU GLU A . n 
A 1 314 ILE 314 335 335 ILE ILE A . n 
A 1 315 ASP 315 336 336 ASP ASP A . n 
A 1 316 ALA 316 337 337 ALA ALA A . n 
A 1 317 VAL 317 338 338 VAL VAL A . n 
A 1 318 LEU 318 339 339 LEU LEU A . n 
A 1 319 PRO 319 340 340 PRO PRO A . n 
A 1 320 ASN 320 341 341 ASN ASN A . n 
A 1 321 LYS 321 342 342 LYS LYS A . n 
A 1 322 ALA 322 343 343 ALA ALA A . n 
A 1 323 PRO 323 344 344 PRO PRO A . n 
A 1 324 PRO 324 345 345 PRO PRO A . n 
A 1 325 THR 325 346 346 THR THR A . n 
A 1 326 TYR 326 347 347 TYR TYR A . n 
A 1 327 ASP 327 348 348 ASP ASP A . n 
A 1 328 THR 328 349 349 THR THR A . n 
A 1 329 VAL 329 350 350 VAL VAL A . n 
A 1 330 LEU 330 351 351 LEU LEU A . n 
A 1 331 GLN 331 352 352 GLN GLN A . n 
A 1 332 MET 332 353 353 MET MET A . n 
A 1 333 GLU 333 354 354 GLU GLU A . n 
A 1 334 TYR 334 355 355 TYR TYR A . n 
A 1 335 LEU 335 356 356 LEU LEU A . n 
A 1 336 ASP 336 357 357 ASP ASP A . n 
A 1 337 MET 337 358 358 MET MET A . n 
A 1 338 VAL 338 359 359 VAL VAL A . n 
A 1 339 VAL 339 360 360 VAL VAL A . n 
A 1 340 ASN 340 361 361 ASN ASN A . n 
A 1 341 GLU 341 362 362 GLU GLU A . n 
A 1 342 THR 342 363 363 THR THR A . n 
A 1 343 LEU 343 364 364 LEU LEU A . n 
A 1 344 ARG 344 365 365 ARG ARG A . n 
A 1 345 LEU 345 366 366 LEU LEU A . n 
A 1 346 PHE 346 367 367 PHE PHE A . n 
A 1 347 PRO 347 368 368 PRO PRO A . n 
A 1 348 ILE 348 369 369 ILE ILE A . n 
A 1 349 ALA 349 370 370 ALA ALA A . n 
A 1 350 MET 350 371 371 MET MET A . n 
A 1 351 ARG 351 372 372 ARG ARG A . n 
A 1 352 LEU 352 373 373 LEU LEU A . n 
A 1 353 GLU 353 374 374 GLU GLU A . n 
A 1 354 ARG 354 375 375 ARG ARG A . n 
A 1 355 VAL 355 376 376 VAL VAL A . n 
A 1 356 CYS 356 377 377 CYS CYS A . n 
A 1 357 LYS 357 378 378 LYS LYS A . n 
A 1 358 LYS 358 379 379 LYS LYS A . n 
A 1 359 ASP 359 380 380 ASP ASP A . n 
A 1 360 VAL 360 381 381 VAL VAL A . n 
A 1 361 GLU 361 382 382 GLU GLU A . n 
A 1 362 ILE 362 383 383 ILE ILE A . n 
A 1 363 ASN 363 384 384 ASN ASN A . n 
A 1 364 GLY 364 385 385 GLY GLY A . n 
A 1 365 MET 365 386 386 MET MET A . n 
A 1 366 PHE 366 387 387 PHE PHE A . n 
A 1 367 ILE 367 388 388 ILE ILE A . n 
A 1 368 PRO 368 389 389 PRO PRO A . n 
A 1 369 LYS 369 390 390 LYS LYS A . n 
A 1 370 GLY 370 391 391 GLY GLY A . n 
A 1 371 VAL 371 392 392 VAL VAL A . n 
A 1 372 VAL 372 393 393 VAL VAL A . n 
A 1 373 VAL 373 394 394 VAL VAL A . n 
A 1 374 MET 374 395 395 MET MET A . n 
A 1 375 ILE 375 396 396 ILE ILE A . n 
A 1 376 PRO 376 397 397 PRO PRO A . n 
A 1 377 SER 377 398 398 SER SER A . n 
A 1 378 TYR 378 399 399 TYR TYR A . n 
A 1 379 ALA 379 400 400 ALA ALA A . n 
A 1 380 LEU 380 401 401 LEU LEU A . n 
A 1 381 HIS 381 402 402 HIS HIS A . n 
A 1 382 ARG 382 403 403 ARG ARG A . n 
A 1 383 ASP 383 404 404 ASP ASP A . n 
A 1 384 PRO 384 405 405 PRO PRO A . n 
A 1 385 LYS 385 406 406 LYS LYS A . n 
A 1 386 TYR 386 407 407 TYR TYR A . n 
A 1 387 TRP 387 408 408 TRP TRP A . n 
A 1 388 THR 388 409 409 THR THR A . n 
A 1 389 GLU 389 410 410 GLU GLU A . n 
A 1 390 PRO 390 411 411 PRO PRO A . n 
A 1 391 GLU 391 412 412 GLU GLU A . n 
A 1 392 LYS 392 413 413 LYS LYS A . n 
A 1 393 PHE 393 414 414 PHE PHE A . n 
A 1 394 LEU 394 415 415 LEU LEU A . n 
A 1 395 PRO 395 416 416 PRO PRO A . n 
A 1 396 GLU 396 417 417 GLU GLU A . n 
A 1 397 ARG 397 418 418 ARG ARG A . n 
A 1 398 PHE 398 419 419 PHE PHE A . n 
A 1 399 SER 399 420 420 SER SER A . n 
A 1 400 LYS 400 421 421 LYS LYS A . n 
A 1 401 LYS 401 422 422 LYS LYS A . n 
A 1 402 ASN 402 423 423 ASN ASN A . n 
A 1 403 LYS 403 424 424 LYS LYS A . n 
A 1 404 ASP 404 425 425 ASP ASP A . n 
A 1 405 ASN 405 426 426 ASN ASN A . n 
A 1 406 ILE 406 427 427 ILE ILE A . n 
A 1 407 ASP 407 428 428 ASP ASP A . n 
A 1 408 PRO 408 429 429 PRO PRO A . n 
A 1 409 TYR 409 430 430 TYR TYR A . n 
A 1 410 ILE 410 431 431 ILE ILE A . n 
A 1 411 TYR 411 432 432 TYR TYR A . n 
A 1 412 THR 412 433 433 THR THR A . n 
A 1 413 PRO 413 434 434 PRO PRO A . n 
A 1 414 PHE 414 435 435 PHE PHE A . n 
A 1 415 GLY 415 436 436 GLY GLY A . n 
A 1 416 SER 416 437 437 SER SER A . n 
A 1 417 GLY 417 438 438 GLY GLY A . n 
A 1 418 PRO 418 439 439 PRO PRO A . n 
A 1 419 ARG 419 440 440 ARG ARG A . n 
A 1 420 ASN 420 441 441 ASN ASN A . n 
A 1 421 CYS 421 442 442 CYS CYS A . n 
A 1 422 ILE 422 443 443 ILE ILE A . n 
A 1 423 GLY 423 444 444 GLY GLY A . n 
A 1 424 MET 424 445 445 MET MET A . n 
A 1 425 ARG 425 446 446 ARG ARG A . n 
A 1 426 PHE 426 447 447 PHE PHE A . n 
A 1 427 ALA 427 448 448 ALA ALA A . n 
A 1 428 LEU 428 449 449 LEU LEU A . n 
A 1 429 MET 429 450 450 MET MET A . n 
A 1 430 ASN 430 451 451 ASN ASN A . n 
A 1 431 MET 431 452 452 MET MET A . n 
A 1 432 LYS 432 453 453 LYS LYS A . n 
A 1 433 LEU 433 454 454 LEU LEU A . n 
A 1 434 ALA 434 455 455 ALA ALA A . n 
A 1 435 LEU 435 456 456 LEU LEU A . n 
A 1 436 ILE 436 457 457 ILE ILE A . n 
A 1 437 ARG 437 458 458 ARG ARG A . n 
A 1 438 VAL 438 459 459 VAL VAL A . n 
A 1 439 LEU 439 460 460 LEU LEU A . n 
A 1 440 GLN 440 461 461 GLN GLN A . n 
A 1 441 ASN 441 462 462 ASN ASN A . n 
A 1 442 PHE 442 463 463 PHE PHE A . n 
A 1 443 SER 443 464 464 SER SER A . n 
A 1 444 PHE 444 465 465 PHE PHE A . n 
A 1 445 LYS 445 466 466 LYS LYS A . n 
A 1 446 PRO 446 467 467 PRO PRO A . n 
A 1 447 CYS 447 468 468 CYS CYS A . n 
A 1 448 LYS 448 469 469 LYS LYS A . n 
A 1 449 GLU 449 470 470 GLU GLU A . n 
A 1 450 THR 450 471 471 THR THR A . n 
A 1 451 GLN 451 472 472 GLN GLN A . n 
A 1 452 ILE 452 473 473 ILE ILE A . n 
A 1 453 PRO 453 474 474 PRO PRO A . n 
A 1 454 LEU 454 475 475 LEU LEU A . n 
A 1 455 LYS 455 476 476 LYS LYS A . n 
A 1 456 LEU 456 477 477 LEU LEU A . n 
A 1 457 SER 457 478 478 SER SER A . n 
A 1 458 LEU 458 479 479 LEU LEU A . n 
A 1 459 GLY 459 480 480 GLY GLY A . n 
A 1 460 GLY 460 481 481 GLY GLY A . n 
A 1 461 LEU 461 482 482 LEU LEU A . n 
A 1 462 LEU 462 483 483 LEU LEU A . n 
A 1 463 GLN 463 484 484 GLN GLN A . n 
A 1 464 PRO 464 485 485 PRO PRO A . n 
A 1 465 GLU 465 486 486 GLU GLU A . n 
A 1 466 LYS 466 487 487 LYS LYS A . n 
A 1 467 PRO 467 488 488 PRO PRO A . n 
A 1 468 VAL 468 489 489 VAL VAL A . n 
A 1 469 VAL 469 490 490 VAL VAL A . n 
A 1 470 LEU 470 491 491 LEU LEU A . n 
A 1 471 LYS 471 492 492 LYS LYS A . n 
A 1 472 VAL 472 493 493 VAL VAL A . n 
A 1 473 GLU 473 494 494 GLU GLU A . n 
A 1 474 SER 474 495 495 SER SER A . n 
A 1 475 ARG 475 496 496 ARG ARG A . n 
A 1 476 ASP 476 497 ?   ?   ?   A . n 
A 1 477 GLY 477 498 ?   ?   ?   A . n 
A 1 478 THR 478 499 ?   ?   ?   A . n 
A 1 479 VAL 479 500 ?   ?   ?   A . n 
A 1 480 SER 480 501 ?   ?   ?   A . n 
A 1 481 GLY 481 502 ?   ?   ?   A . n 
A 1 482 ALA 482 503 ?   ?   ?   A . n 
A 1 483 HIS 483 504 ?   ?   ?   A . n 
A 1 484 HIS 484 505 ?   ?   ?   A . n 
A 1 485 HIS 485 506 ?   ?   ?   A . n 
A 1 486 HIS 486 507 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ASS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ASS 
_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 HEM   1 601 501 HEM   HEM A . 
C 3 A1ASS 1 602 502 A1ASS LIG A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 34  ? CG  ? A LYS 13  CG  
2   1 Y 1 A LYS 34  ? CD  ? A LYS 13  CD  
3   1 Y 1 A LYS 34  ? CE  ? A LYS 13  CE  
4   1 Y 1 A LYS 34  ? NZ  ? A LYS 13  NZ  
5   1 Y 1 A LYS 35  ? CG  ? A LYS 14  CG  
6   1 Y 1 A LYS 35  ? CD  ? A LYS 14  CD  
7   1 Y 1 A LYS 35  ? CE  ? A LYS 14  CE  
8   1 Y 1 A LYS 35  ? NZ  ? A LYS 14  NZ  
9   1 Y 1 A LYS 70  ? CG  ? A LYS 49  CG  
10  1 Y 1 A LYS 70  ? CD  ? A LYS 49  CD  
11  1 Y 1 A LYS 70  ? CE  ? A LYS 49  CE  
12  1 Y 1 A LYS 70  ? NZ  ? A LYS 49  NZ  
13  1 Y 1 A LYS 96  ? CG  ? A LYS 75  CG  
14  1 Y 1 A LYS 96  ? CD  ? A LYS 75  CD  
15  1 Y 1 A LYS 96  ? CE  ? A LYS 75  CE  
16  1 Y 1 A LYS 96  ? NZ  ? A LYS 75  NZ  
17  1 Y 1 A LYS 115 ? CG  ? A LYS 94  CG  
18  1 Y 1 A LYS 115 ? CD  ? A LYS 94  CD  
19  1 Y 1 A LYS 115 ? CE  ? A LYS 94  CE  
20  1 Y 1 A LYS 115 ? NZ  ? A LYS 94  NZ  
21  1 Y 1 A LYS 127 ? CG  ? A LYS 106 CG  
22  1 Y 1 A LYS 127 ? CD  ? A LYS 106 CD  
23  1 Y 1 A LYS 127 ? CE  ? A LYS 106 CE  
24  1 Y 1 A LYS 127 ? NZ  ? A LYS 106 NZ  
25  1 Y 1 A ARG 158 ? CG  ? A ARG 137 CG  
26  1 Y 1 A ARG 158 ? CD  ? A ARG 137 CD  
27  1 Y 1 A ARG 158 ? NE  ? A ARG 137 NE  
28  1 Y 1 A ARG 158 ? CZ  ? A ARG 137 CZ  
29  1 Y 1 A ARG 158 ? NH1 ? A ARG 137 NH1 
30  1 Y 1 A ARG 158 ? NH2 ? A ARG 137 NH2 
31  1 Y 1 A GLU 163 ? CG  ? A GLU 142 CG  
32  1 Y 1 A GLU 163 ? CD  ? A GLU 142 CD  
33  1 Y 1 A GLU 163 ? OE1 ? A GLU 142 OE1 
34  1 Y 1 A GLU 163 ? OE2 ? A GLU 142 OE2 
35  1 Y 1 A LYS 168 ? CG  ? A LYS 147 CG  
36  1 Y 1 A LYS 168 ? CD  ? A LYS 147 CD  
37  1 Y 1 A LYS 168 ? CE  ? A LYS 147 CE  
38  1 Y 1 A LYS 168 ? NZ  ? A LYS 147 NZ  
39  1 Y 1 A LYS 173 ? CG  ? A LYS 152 CG  
40  1 Y 1 A LYS 173 ? CD  ? A LYS 152 CD  
41  1 Y 1 A LYS 173 ? CE  ? A LYS 152 CE  
42  1 Y 1 A LYS 173 ? NZ  ? A LYS 152 NZ  
43  1 Y 1 A GLN 200 ? CG  ? A GLN 179 CG  
44  1 Y 1 A GLN 200 ? CD  ? A GLN 179 CD  
45  1 Y 1 A GLN 200 ? OE1 ? A GLN 179 OE1 
46  1 Y 1 A GLN 200 ? NE2 ? A GLN 179 NE2 
47  1 Y 1 A GLU 205 ? CG  ? A GLU 184 CG  
48  1 Y 1 A GLU 205 ? CD  ? A GLU 184 CD  
49  1 Y 1 A GLU 205 ? OE1 ? A GLU 184 OE1 
50  1 Y 1 A GLU 205 ? OE2 ? A GLU 184 OE2 
51  1 Y 1 A LYS 208 ? CG  ? A LYS 187 CG  
52  1 Y 1 A LYS 208 ? CD  ? A LYS 187 CD  
53  1 Y 1 A LYS 208 ? CE  ? A LYS 187 CE  
54  1 Y 1 A LYS 208 ? NZ  ? A LYS 187 NZ  
55  1 Y 1 A GLU 244 ? CG  ? A GLU 223 CG  
56  1 Y 1 A GLU 244 ? CD  ? A GLU 223 CD  
57  1 Y 1 A GLU 244 ? OE1 ? A GLU 223 OE1 
58  1 Y 1 A GLU 244 ? OE2 ? A GLU 223 OE2 
59  1 Y 1 A VAL 245 ? CG1 ? A VAL 224 CG1 
60  1 Y 1 A VAL 245 ? CG2 ? A VAL 224 CG2 
61  1 Y 1 A LYS 251 ? CG  ? A LYS 230 CG  
62  1 Y 1 A LYS 251 ? CD  ? A LYS 230 CD  
63  1 Y 1 A LYS 251 ? CE  ? A LYS 230 CE  
64  1 Y 1 A LYS 251 ? NZ  ? A LYS 230 NZ  
65  1 Y 1 A LYS 254 ? CG  ? A LYS 233 CG  
66  1 Y 1 A LYS 254 ? CD  ? A LYS 233 CD  
67  1 Y 1 A LYS 254 ? CE  ? A LYS 233 CE  
68  1 Y 1 A LYS 254 ? NZ  ? A LYS 233 NZ  
69  1 Y 1 A SER 259 ? OG  ? A SER 238 OG  
70  1 Y 1 A GLN 265 ? CG  ? A GLN 244 CG  
71  1 Y 1 A GLN 265 ? CD  ? A GLN 244 CD  
72  1 Y 1 A GLN 265 ? OE1 ? A GLN 244 OE1 
73  1 Y 1 A GLN 265 ? NE2 ? A GLN 244 NE2 
74  1 Y 1 A LYS 266 ? CG  ? A LYS 245 CG  
75  1 Y 1 A LYS 266 ? CD  ? A LYS 245 CD  
76  1 Y 1 A LYS 266 ? CE  ? A LYS 245 CE  
77  1 Y 1 A LYS 266 ? NZ  ? A LYS 245 NZ  
78  1 Y 1 A HIS 267 ? CG  ? A HIS 246 CG  
79  1 Y 1 A HIS 267 ? ND1 ? A HIS 246 ND1 
80  1 Y 1 A HIS 267 ? CD2 ? A HIS 246 CD2 
81  1 Y 1 A HIS 267 ? CE1 ? A HIS 246 CE1 
82  1 Y 1 A HIS 267 ? NE2 ? A HIS 246 NE2 
83  1 Y 1 A SER 281 ? OG  ? A SER 260 OG  
84  1 Y 1 A LYS 288 ? CG  ? A LYS 267 CG  
85  1 Y 1 A LYS 288 ? CD  ? A LYS 267 CD  
86  1 Y 1 A LYS 288 ? CE  ? A LYS 267 CE  
87  1 Y 1 A LYS 288 ? NZ  ? A LYS 267 NZ  
88  1 Y 1 A GLU 382 ? CG  ? A GLU 361 CG  
89  1 Y 1 A GLU 382 ? CD  ? A GLU 361 CD  
90  1 Y 1 A GLU 382 ? OE1 ? A GLU 361 OE1 
91  1 Y 1 A GLU 382 ? OE2 ? A GLU 361 OE2 
92  1 Y 1 A LYS 406 ? CG  ? A LYS 385 CG  
93  1 Y 1 A LYS 406 ? CD  ? A LYS 385 CD  
94  1 Y 1 A LYS 406 ? CE  ? A LYS 385 CE  
95  1 Y 1 A LYS 406 ? NZ  ? A LYS 385 NZ  
96  1 Y 1 A LYS 422 ? CG  ? A LYS 401 CG  
97  1 Y 1 A LYS 422 ? CD  ? A LYS 401 CD  
98  1 Y 1 A LYS 422 ? CE  ? A LYS 401 CE  
99  1 Y 1 A LYS 422 ? NZ  ? A LYS 401 NZ  
100 1 Y 1 A LYS 466 ? CG  ? A LYS 445 CG  
101 1 Y 1 A LYS 466 ? CD  ? A LYS 445 CD  
102 1 Y 1 A LYS 466 ? CE  ? A LYS 445 CE  
103 1 Y 1 A LYS 466 ? NZ  ? A LYS 445 NZ  
104 1 Y 1 A LYS 469 ? CG  ? A LYS 448 CG  
105 1 Y 1 A LYS 469 ? CD  ? A LYS 448 CD  
106 1 Y 1 A LYS 469 ? CE  ? A LYS 448 CE  
107 1 Y 1 A LYS 469 ? NZ  ? A LYS 448 NZ  
108 1 Y 1 A GLU 470 ? CG  ? A GLU 449 CG  
109 1 Y 1 A GLU 470 ? CD  ? A GLU 449 CD  
110 1 Y 1 A GLU 470 ? OE1 ? A GLU 449 OE1 
111 1 Y 1 A GLU 470 ? OE2 ? A GLU 449 OE2 
112 1 Y 1 A LYS 487 ? CG  ? A LYS 466 CG  
113 1 Y 1 A LYS 487 ? CD  ? A LYS 466 CD  
114 1 Y 1 A LYS 487 ? CE  ? A LYS 466 CE  
115 1 Y 1 A LYS 487 ? NZ  ? A LYS 466 NZ  
116 1 Y 1 A LYS 492 ? CG  ? A LYS 471 CG  
117 1 Y 1 A LYS 492 ? CD  ? A LYS 471 CD  
118 1 Y 1 A LYS 492 ? CE  ? A LYS 471 CE  
119 1 Y 1 A LYS 492 ? NZ  ? A LYS 471 NZ  
# 
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  ? ? ? '(1.20.1_4487)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .               2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .               3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .               4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BV8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.241 
_cell.length_a_esd                 ? 
_cell.length_b                     100.808 
_cell.length_b_esd                 ? 
_cell.length_c                     131.560 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BV8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   9BV8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.60 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES, pH 7.0, 10-12% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-24 
_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                    'SI(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BV8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.00 
_reflns.d_resolution_low                               44.85 
_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                                     10614 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.24 
_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                                0.176 
_reflns.pdbx_Rpim_I_all                                0.054 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       110215 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.167 
_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                                    3.00 
_reflns_shell.d_res_low                                     3.18 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           17021 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1698 
_reflns_shell.percent_possible_obs                          99.9 
_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                               10.0 
_reflns_shell.pdbx_chi_squared                              1.46 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.6 
_reflns_shell.pdbx_Rrim_I_all                               1.244 
_reflns_shell.pdbx_Rpim_I_all                               0.387 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.756 
_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                                  1.180 
_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                               ? 
_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                                 9BV8 
_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                            3.00 
_refine.ls_d_res_low                             40.21 
_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                     10603 
_refine.ls_number_reflns_R_free                  530 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.88 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2343 
_refine.ls_R_factor_R_free                       0.2612 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2328 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 30.32 
_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                            0.37 
_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.pdbx_number_atoms_protein        3622 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         65 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3687 
_refine_hist.d_res_high                       3.00 
_refine_hist.d_res_low                        40.21 
# 
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' ? 0.002  ? 3787 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.539  ? 5170 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.229 ? 1365 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.039  ? 579  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 658  ? f_plane_restr      ? ? 
# 
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' 3.00 3.30  . . 126 2473 100.00 . . . . 0.3356 . . . . . . . . . . . 0.3742 
'X-RAY DIFFRACTION' 3.30 3.78  . . 136 2479 100.00 . . . . 0.2754 . . . . . . . . . . . 0.3260 
'X-RAY DIFFRACTION' 3.78 4.76  . . 128 2511 100.00 . . . . 0.2288 . . . . . . . . . . . 0.3064 
'X-RAY DIFFRACTION' 4.76 40.21 . . 140 2610 100.00 . . . . 0.1973 . . . . . . . . . . . 0.1989 
# 
_struct.entry_id                     9BV8 
_struct.title                        'Crystal structure of human CYP3A4 in complex with SJYHJ-114' 
_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        9BV8 
_struct_keywords.text            
;Cytochrome P450 3A4, CYP3A4, CYP3A4-selective inhibitor, drug metabolizing enzyme, OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex
;
_struct_keywords.pdbx_keywords   'OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CP3A4_HUMAN 
_struct_ref.pdbx_db_accession          P08684 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFT
NRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDV
ITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLED
TQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKA
PPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKN
KDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA

;
_struct_ref.pdbx_align_begin           24 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BV8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 482 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P08684 
_struct_ref_seq.db_align_beg                  24 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  503 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       24 
_struct_ref_seq.pdbx_auth_seq_align_end       503 
# 
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 9BV8 MET A 1   ? UNP P08684 ? ? 'initiating methionine' 22  1 
1 9BV8 ALA A 2   ? UNP P08684 ? ? 'expression tag'        23  2 
1 9BV8 HIS A 483 ? UNP P08684 ? ? 'expression tag'        504 3 
1 9BV8 HIS A 484 ? UNP P08684 ? ? 'expression tag'        505 4 
1 9BV8 HIS A 485 ? UNP P08684 ? ? 'expression tag'        506 5 
1 9BV8 HIS A 486 ? UNP P08684 ? ? 'expression tag'        507 6 
# 
_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 
# 
_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 GLY A 10  ? LEU A 15  ? GLY A 31  LEU A 36  1 ? 6  
HELX_P HELX_P2  AA2 ASN A 28  ? HIS A 33  ? ASN A 49  HIS A 54  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 34  ? GLY A 48  ? LYS A 55  GLY A 69  1 ? 15 
HELX_P HELX_P4  AA4 ASP A 65  ? VAL A 74  ? ASP A 86  VAL A 95  1 ? 10 
HELX_P HELX_P5  AA5 VAL A 90  ? ALA A 96  ? VAL A 111 ALA A 117 5 ? 7  
HELX_P HELX_P6  AA6 GLU A 101 ? SER A 113 ? GLU A 122 SER A 134 1 ? 13 
HELX_P HELX_P7  AA7 PRO A 114 ? PHE A 116 ? PRO A 135 PHE A 137 5 ? 3  
HELX_P HELX_P8  AA8 THR A 117 ? THR A 145 ? THR A 138 THR A 166 1 ? 29 
HELX_P HELX_P9  AA9 LEU A 151 ? SER A 167 ? LEU A 172 SER A 188 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 180 ? LYS A 187 ? ASP A 201 LYS A 208 1 ? 8  
HELX_P HELX_P11 AB2 ASP A 196 ? PHE A 205 ? ASP A 217 PHE A 226 1 ? 10 
HELX_P HELX_P12 AB3 LEU A 208 ? LEU A 215 ? LEU A 229 LEU A 236 1 ? 8  
HELX_P HELX_P13 AB4 PRO A 221 ? GLU A 237 ? PRO A 242 GLU A 258 1 ? 17 
HELX_P HELX_P14 AB5 ASP A 249 ? SER A 260 ? ASP A 270 SER A 281 1 ? 12 
HELX_P HELX_P15 AB6 SER A 270 ? HIS A 303 ? SER A 291 HIS A 324 1 ? 34 
HELX_P HELX_P16 AB7 HIS A 303 ? LEU A 318 ? HIS A 324 LEU A 339 1 ? 16 
HELX_P HELX_P17 AB8 THR A 325 ? MET A 332 ? THR A 346 MET A 353 1 ? 8  
HELX_P HELX_P18 AB9 MET A 332 ? PHE A 346 ? MET A 353 PHE A 367 1 ? 15 
HELX_P HELX_P19 AC1 PRO A 376 ? HIS A 381 ? PRO A 397 HIS A 402 1 ? 6  
HELX_P HELX_P20 AC2 LEU A 394 ? SER A 399 ? LEU A 415 SER A 420 5 ? 6  
HELX_P HELX_P21 AC3 GLY A 423 ? ASN A 441 ? GLY A 444 ASN A 462 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 421 SG ? ? ? 1_555 B HEM   . FE  ? ? A CYS 442 A HEM   601 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 C A1ASS . N20 ? ? A HEM 601 A A1ASS 602 1_555 ? ? ? ? ? ? ? 2.223 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NA  ? B HEM   . ? A HEM   601 ? 1_555 99.8  ? 
2  SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 88.5  ? 
3  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 88.3  ? 
4  SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 82.5  ? 
5  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 177.0 ? 
6  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 93.6  ? 
7  SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 93.2  ? 
8  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 90.3  ? 
9  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 178.0 ? 
10 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 87.8  ? 
11 SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N20 ? C A1ASS . ? A A1ASS 602 ? 1_555 169.7 ? 
12 NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N20 ? C A1ASS . ? A A1ASS 602 ? 1_555 90.4  ? 
13 NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N20 ? C A1ASS . ? A A1ASS 602 ? 1_555 90.2  ? 
14 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N20 ? C A1ASS . ? A A1ASS 602 ? 1_555 87.3  ? 
15 ND ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N20 ? C A1ASS . ? A A1ASS 602 ? 1_555 88.4  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 50  ? ASP A 55  ? VAL A 71  ASP A 76  
AA1 2 GLN A 58  ? ILE A 63  ? GLN A 79  ILE A 84  
AA1 3 VAL A 372 ? ILE A 375 ? VAL A 393 ILE A 396 
AA1 4 LEU A 352 ? VAL A 355 ? LEU A 373 VAL A 376 
AA2 1 VAL A 149 ? THR A 150 ? VAL A 170 THR A 171 
AA2 2 VAL A 469 ? SER A 474 ? VAL A 490 SER A 495 
AA2 3 PHE A 442 ? PRO A 446 ? PHE A 463 PRO A 467 
AA3 1 VAL A 360 ? ILE A 362 ? VAL A 381 ILE A 383 
AA3 2 MET A 365 ? ILE A 367 ? MET A 386 ILE A 388 
# 
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 PHE A 53  ? N PHE A 74  O VAL A 60  ? O VAL A 81  
AA1 2 3 N LEU A 61  ? N LEU A 82  O MET A 374 ? O MET A 395 
AA1 3 4 O ILE A 375 ? O ILE A 396 N LEU A 352 ? N LEU A 373 
AA2 1 2 N VAL A 149 ? N VAL A 170 O LEU A 470 ? O LEU A 491 
AA2 2 3 O LYS A 471 ? O LYS A 492 N LYS A 445 ? N LYS A 466 
AA3 1 2 N VAL A 360 ? N VAL A 381 O ILE A 367 ? O ILE A 388 
# 
_pdbx_entry_details.entry_id                   9BV8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 HIS A 30  ? ? -82.54  48.74   
2 1 PHE A 46  ? ? 70.99   -10.65  
3 1 VAL A 101 ? ? -124.85 -55.21  
4 1 MET A 114 ? ? -68.34  1.05    
5 1 ASP A 123 ? ? 59.02   -125.19 
6 1 PHE A 226 ? ? -116.65 67.70   
7 1 MET A 371 ? ? 71.70   -12.09  
8 1 ARG A 372 ? ? -170.90 136.57  
# 
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 22  ? A MET 1   
2  1 Y 1 A ALA 23  ? A ALA 2   
3  1 Y 1 A LEU 24  ? A LEU 3   
4  1 Y 1 A TYR 25  ? A TYR 4   
5  1 Y 1 A GLY 26  ? A GLY 5   
6  1 Y 1 A THR 27  ? A THR 6   
7  1 Y 1 A LYS 282 ? A LYS 261 
8  1 Y 1 A GLU 283 ? A GLU 262 
9  1 Y 1 A THR 284 ? A THR 263 
10 1 Y 1 A GLU 285 ? A GLU 264 
11 1 Y 1 A SER 286 ? A SER 265 
12 1 Y 1 A ASP 497 ? A ASP 476 
13 1 Y 1 A GLY 498 ? A GLY 477 
14 1 Y 1 A THR 499 ? A THR 478 
15 1 Y 1 A VAL 500 ? A VAL 479 
16 1 Y 1 A SER 501 ? A SER 480 
17 1 Y 1 A GLY 502 ? A GLY 481 
18 1 Y 1 A ALA 503 ? A ALA 482 
19 1 Y 1 A HIS 504 ? A HIS 483 
20 1 Y 1 A HIS 505 ? A HIS 484 
21 1 Y 1 A HIS 506 ? A HIS 485 
22 1 Y 1 A HIS 507 ? A HIS 486 
# 
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 
A1ASS C10  C  N N 1   
A1ASS C15  C  Y N 2   
A1ASS C21  C  Y N 3   
A1ASS C02  C  N N 4   
A1ASS C04  C  Y N 5   
A1ASS C05  C  Y N 6   
A1ASS C06  C  Y N 7   
A1ASS C08  C  N N 8   
A1ASS C09  C  N N 9   
A1ASS C11  C  N N 10  
A1ASS C12  C  N N 11  
A1ASS C14  C  Y N 12  
A1ASS C16  C  Y N 13  
A1ASS C18  C  Y N 14  
A1ASS C19  C  Y N 15  
A1ASS F01  F  N N 16  
A1ASS F03  F  N N 17  
A1ASS F22  F  N N 18  
A1ASS N07  N  N N 19  
A1ASS N17  N  Y N 20  
A1ASS N20  N  Y N 21  
A1ASS O13  O  N N 22  
A1ASS H1   H  N N 23  
A1ASS H2   H  N N 24  
A1ASS H3   H  N N 25  
A1ASS H4   H  N N 26  
A1ASS H5   H  N N 27  
A1ASS H6   H  N N 28  
A1ASS H7   H  N N 29  
A1ASS H8   H  N N 30  
A1ASS H9   H  N N 31  
A1ASS H10  H  N N 32  
A1ASS H11  H  N N 33  
A1ASS H12  H  N N 34  
A1ASS H13  H  N N 35  
A1ASS H14  H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
GLN   N    N  N N 124 
GLN   CA   C  N S 125 
GLN   C    C  N N 126 
GLN   O    O  N N 127 
GLN   CB   C  N N 128 
GLN   CG   C  N N 129 
GLN   CD   C  N N 130 
GLN   OE1  O  N N 131 
GLN   NE2  N  N N 132 
GLN   OXT  O  N N 133 
GLN   H    H  N N 134 
GLN   H2   H  N N 135 
GLN   HA   H  N N 136 
GLN   HB2  H  N N 137 
GLN   HB3  H  N N 138 
GLN   HG2  H  N N 139 
GLN   HG3  H  N N 140 
GLN   HE21 H  N N 141 
GLN   HE22 H  N N 142 
GLN   HXT  H  N N 143 
GLU   N    N  N N 144 
GLU   CA   C  N S 145 
GLU   C    C  N N 146 
GLU   O    O  N N 147 
GLU   CB   C  N N 148 
GLU   CG   C  N N 149 
GLU   CD   C  N N 150 
GLU   OE1  O  N N 151 
GLU   OE2  O  N N 152 
GLU   OXT  O  N N 153 
GLU   H    H  N N 154 
GLU   H2   H  N N 155 
GLU   HA   H  N N 156 
GLU   HB2  H  N N 157 
GLU   HB3  H  N N 158 
GLU   HG2  H  N N 159 
GLU   HG3  H  N N 160 
GLU   HE2  H  N N 161 
GLU   HXT  H  N N 162 
GLY   N    N  N N 163 
GLY   CA   C  N N 164 
GLY   C    C  N N 165 
GLY   O    O  N N 166 
GLY   OXT  O  N N 167 
GLY   H    H  N N 168 
GLY   H2   H  N N 169 
GLY   HA2  H  N N 170 
GLY   HA3  H  N N 171 
GLY   HXT  H  N N 172 
HEM   CHA  C  N N 173 
HEM   CHB  C  N N 174 
HEM   CHC  C  N N 175 
HEM   CHD  C  N N 176 
HEM   C1A  C  Y N 177 
HEM   C2A  C  Y N 178 
HEM   C3A  C  Y N 179 
HEM   C4A  C  Y N 180 
HEM   CMA  C  N N 181 
HEM   CAA  C  N N 182 
HEM   CBA  C  N N 183 
HEM   CGA  C  N N 184 
HEM   O1A  O  N N 185 
HEM   O2A  O  N N 186 
HEM   C1B  C  N N 187 
HEM   C2B  C  N N 188 
HEM   C3B  C  N N 189 
HEM   C4B  C  N N 190 
HEM   CMB  C  N N 191 
HEM   CAB  C  N N 192 
HEM   CBB  C  N N 193 
HEM   C1C  C  Y N 194 
HEM   C2C  C  Y N 195 
HEM   C3C  C  Y N 196 
HEM   C4C  C  Y N 197 
HEM   CMC  C  N N 198 
HEM   CAC  C  N N 199 
HEM   CBC  C  N N 200 
HEM   C1D  C  N N 201 
HEM   C2D  C  N N 202 
HEM   C3D  C  N N 203 
HEM   C4D  C  N N 204 
HEM   CMD  C  N N 205 
HEM   CAD  C  N N 206 
HEM   CBD  C  N N 207 
HEM   CGD  C  N N 208 
HEM   O1D  O  N N 209 
HEM   O2D  O  N N 210 
HEM   NA   N  Y N 211 
HEM   NB   N  N N 212 
HEM   NC   N  Y N 213 
HEM   ND   N  N N 214 
HEM   FE   FE N N 215 
HEM   HHB  H  N N 216 
HEM   HHC  H  N N 217 
HEM   HHD  H  N N 218 
HEM   HMA  H  N N 219 
HEM   HMAA H  N N 220 
HEM   HMAB H  N N 221 
HEM   HAA  H  N N 222 
HEM   HAAA H  N N 223 
HEM   HBA  H  N N 224 
HEM   HBAA H  N N 225 
HEM   HMB  H  N N 226 
HEM   HMBA H  N N 227 
HEM   HMBB H  N N 228 
HEM   HAB  H  N N 229 
HEM   HBB  H  N N 230 
HEM   HBBA H  N N 231 
HEM   HMC  H  N N 232 
HEM   HMCA H  N N 233 
HEM   HMCB H  N N 234 
HEM   HAC  H  N N 235 
HEM   HBC  H  N N 236 
HEM   HBCA H  N N 237 
HEM   HMD  H  N N 238 
HEM   HMDA H  N N 239 
HEM   HMDB H  N N 240 
HEM   HAD  H  N N 241 
HEM   HADA H  N N 242 
HEM   HBD  H  N N 243 
HEM   HBDA H  N N 244 
HEM   H2A  H  N N 245 
HEM   H2D  H  N N 246 
HEM   HHA  H  N N 247 
HIS   N    N  N N 248 
HIS   CA   C  N S 249 
HIS   C    C  N N 250 
HIS   O    O  N N 251 
HIS   CB   C  N N 252 
HIS   CG   C  Y N 253 
HIS   ND1  N  Y N 254 
HIS   CD2  C  Y N 255 
HIS   CE1  C  Y N 256 
HIS   NE2  N  Y N 257 
HIS   OXT  O  N N 258 
HIS   H    H  N N 259 
HIS   H2   H  N N 260 
HIS   HA   H  N N 261 
HIS   HB2  H  N N 262 
HIS   HB3  H  N N 263 
HIS   HD1  H  N N 264 
HIS   HD2  H  N N 265 
HIS   HE1  H  N N 266 
HIS   HE2  H  N N 267 
HIS   HXT  H  N N 268 
ILE   N    N  N N 269 
ILE   CA   C  N S 270 
ILE   C    C  N N 271 
ILE   O    O  N N 272 
ILE   CB   C  N S 273 
ILE   CG1  C  N N 274 
ILE   CG2  C  N N 275 
ILE   CD1  C  N N 276 
ILE   OXT  O  N N 277 
ILE   H    H  N N 278 
ILE   H2   H  N N 279 
ILE   HA   H  N N 280 
ILE   HB   H  N N 281 
ILE   HG12 H  N N 282 
ILE   HG13 H  N N 283 
ILE   HG21 H  N N 284 
ILE   HG22 H  N N 285 
ILE   HG23 H  N N 286 
ILE   HD11 H  N N 287 
ILE   HD12 H  N N 288 
ILE   HD13 H  N N 289 
ILE   HXT  H  N N 290 
LEU   N    N  N N 291 
LEU   CA   C  N S 292 
LEU   C    C  N N 293 
LEU   O    O  N N 294 
LEU   CB   C  N N 295 
LEU   CG   C  N N 296 
LEU   CD1  C  N N 297 
LEU   CD2  C  N N 298 
LEU   OXT  O  N N 299 
LEU   H    H  N N 300 
LEU   H2   H  N N 301 
LEU   HA   H  N N 302 
LEU   HB2  H  N N 303 
LEU   HB3  H  N N 304 
LEU   HG   H  N N 305 
LEU   HD11 H  N N 306 
LEU   HD12 H  N N 307 
LEU   HD13 H  N N 308 
LEU   HD21 H  N N 309 
LEU   HD22 H  N N 310 
LEU   HD23 H  N N 311 
LEU   HXT  H  N N 312 
LYS   N    N  N N 313 
LYS   CA   C  N S 314 
LYS   C    C  N N 315 
LYS   O    O  N N 316 
LYS   CB   C  N N 317 
LYS   CG   C  N N 318 
LYS   CD   C  N N 319 
LYS   CE   C  N N 320 
LYS   NZ   N  N N 321 
LYS   OXT  O  N N 322 
LYS   H    H  N N 323 
LYS   H2   H  N N 324 
LYS   HA   H  N N 325 
LYS   HB2  H  N N 326 
LYS   HB3  H  N N 327 
LYS   HG2  H  N N 328 
LYS   HG3  H  N N 329 
LYS   HD2  H  N N 330 
LYS   HD3  H  N N 331 
LYS   HE2  H  N N 332 
LYS   HE3  H  N N 333 
LYS   HZ1  H  N N 334 
LYS   HZ2  H  N N 335 
LYS   HZ3  H  N N 336 
LYS   HXT  H  N N 337 
MET   N    N  N N 338 
MET   CA   C  N S 339 
MET   C    C  N N 340 
MET   O    O  N N 341 
MET   CB   C  N N 342 
MET   CG   C  N N 343 
MET   SD   S  N N 344 
MET   CE   C  N N 345 
MET   OXT  O  N N 346 
MET   H    H  N N 347 
MET   H2   H  N N 348 
MET   HA   H  N N 349 
MET   HB2  H  N N 350 
MET   HB3  H  N N 351 
MET   HG2  H  N N 352 
MET   HG3  H  N N 353 
MET   HE1  H  N N 354 
MET   HE2  H  N N 355 
MET   HE3  H  N N 356 
MET   HXT  H  N N 357 
PHE   N    N  N N 358 
PHE   CA   C  N S 359 
PHE   C    C  N N 360 
PHE   O    O  N N 361 
PHE   CB   C  N N 362 
PHE   CG   C  Y N 363 
PHE   CD1  C  Y N 364 
PHE   CD2  C  Y N 365 
PHE   CE1  C  Y N 366 
PHE   CE2  C  Y N 367 
PHE   CZ   C  Y N 368 
PHE   OXT  O  N N 369 
PHE   H    H  N N 370 
PHE   H2   H  N N 371 
PHE   HA   H  N N 372 
PHE   HB2  H  N N 373 
PHE   HB3  H  N N 374 
PHE   HD1  H  N N 375 
PHE   HD2  H  N N 376 
PHE   HE1  H  N N 377 
PHE   HE2  H  N N 378 
PHE   HZ   H  N N 379 
PHE   HXT  H  N N 380 
PRO   N    N  N N 381 
PRO   CA   C  N S 382 
PRO   C    C  N N 383 
PRO   O    O  N N 384 
PRO   CB   C  N N 385 
PRO   CG   C  N N 386 
PRO   CD   C  N N 387 
PRO   OXT  O  N N 388 
PRO   H    H  N N 389 
PRO   HA   H  N N 390 
PRO   HB2  H  N N 391 
PRO   HB3  H  N N 392 
PRO   HG2  H  N N 393 
PRO   HG3  H  N N 394 
PRO   HD2  H  N N 395 
PRO   HD3  H  N N 396 
PRO   HXT  H  N N 397 
SER   N    N  N N 398 
SER   CA   C  N S 399 
SER   C    C  N N 400 
SER   O    O  N N 401 
SER   CB   C  N N 402 
SER   OG   O  N N 403 
SER   OXT  O  N N 404 
SER   H    H  N N 405 
SER   H2   H  N N 406 
SER   HA   H  N N 407 
SER   HB2  H  N N 408 
SER   HB3  H  N N 409 
SER   HG   H  N N 410 
SER   HXT  H  N N 411 
THR   N    N  N N 412 
THR   CA   C  N S 413 
THR   C    C  N N 414 
THR   O    O  N N 415 
THR   CB   C  N R 416 
THR   OG1  O  N N 417 
THR   CG2  C  N N 418 
THR   OXT  O  N N 419 
THR   H    H  N N 420 
THR   H2   H  N N 421 
THR   HA   H  N N 422 
THR   HB   H  N N 423 
THR   HG1  H  N N 424 
THR   HG21 H  N N 425 
THR   HG22 H  N N 426 
THR   HG23 H  N N 427 
THR   HXT  H  N N 428 
TRP   N    N  N N 429 
TRP   CA   C  N S 430 
TRP   C    C  N N 431 
TRP   O    O  N N 432 
TRP   CB   C  N N 433 
TRP   CG   C  Y N 434 
TRP   CD1  C  Y N 435 
TRP   CD2  C  Y N 436 
TRP   NE1  N  Y N 437 
TRP   CE2  C  Y N 438 
TRP   CE3  C  Y N 439 
TRP   CZ2  C  Y N 440 
TRP   CZ3  C  Y N 441 
TRP   CH2  C  Y N 442 
TRP   OXT  O  N N 443 
TRP   H    H  N N 444 
TRP   H2   H  N N 445 
TRP   HA   H  N N 446 
TRP   HB2  H  N N 447 
TRP   HB3  H  N N 448 
TRP   HD1  H  N N 449 
TRP   HE1  H  N N 450 
TRP   HE3  H  N N 451 
TRP   HZ2  H  N N 452 
TRP   HZ3  H  N N 453 
TRP   HH2  H  N N 454 
TRP   HXT  H  N N 455 
TYR   N    N  N N 456 
TYR   CA   C  N S 457 
TYR   C    C  N N 458 
TYR   O    O  N N 459 
TYR   CB   C  N N 460 
TYR   CG   C  Y N 461 
TYR   CD1  C  Y N 462 
TYR   CD2  C  Y N 463 
TYR   CE1  C  Y N 464 
TYR   CE2  C  Y N 465 
TYR   CZ   C  Y N 466 
TYR   OH   O  N N 467 
TYR   OXT  O  N N 468 
TYR   H    H  N N 469 
TYR   H2   H  N N 470 
TYR   HA   H  N N 471 
TYR   HB2  H  N N 472 
TYR   HB3  H  N N 473 
TYR   HD1  H  N N 474 
TYR   HD2  H  N N 475 
TYR   HE1  H  N N 476 
TYR   HE2  H  N N 477 
TYR   HH   H  N N 478 
TYR   HXT  H  N N 479 
VAL   N    N  N N 480 
VAL   CA   C  N S 481 
VAL   C    C  N N 482 
VAL   O    O  N N 483 
VAL   CB   C  N N 484 
VAL   CG1  C  N N 485 
VAL   CG2  C  N N 486 
VAL   OXT  O  N N 487 
VAL   H    H  N N 488 
VAL   H2   H  N N 489 
VAL   HA   H  N N 490 
VAL   HB   H  N N 491 
VAL   HG11 H  N N 492 
VAL   HG12 H  N N 493 
VAL   HG13 H  N N 494 
VAL   HG21 H  N N 495 
VAL   HG22 H  N N 496 
VAL   HG23 H  N N 497 
VAL   HXT  H  N N 498 
# 
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 
A1ASS C11 C10  sing N N 1   
A1ASS C11 C12  sing N N 2   
A1ASS C10 C09  sing N N 3   
A1ASS C12 C09  sing N N 4   
A1ASS C09 C08  sing N N 5   
A1ASS C08 N07  sing N N 6   
A1ASS C08 O13  doub N N 7   
A1ASS N07 C06  sing N N 8   
A1ASS C19 C18  doub Y N 9   
A1ASS C19 N20  sing Y N 10  
A1ASS C18 N17  sing Y N 11  
A1ASS N20 C21  doub Y N 12  
A1ASS C06 C16  doub Y N 13  
A1ASS C06 C05  sing Y N 14  
A1ASS N17 C21  sing Y N 15  
A1ASS N17 C16  sing N N 16  
A1ASS C16 C15  sing Y N 17  
A1ASS C05 C04  doub Y N 18  
A1ASS C15 C14  doub Y N 19  
A1ASS C04 C14  sing Y N 20  
A1ASS C04 C02  sing N N 21  
A1ASS F01 C02  sing N N 22  
A1ASS C02 F22  sing N N 23  
A1ASS C02 F03  sing N N 24  
A1ASS C10 H1   sing N N 25  
A1ASS C10 H2   sing N N 26  
A1ASS C15 H3   sing N N 27  
A1ASS C21 H4   sing N N 28  
A1ASS C05 H5   sing N N 29  
A1ASS C09 H6   sing N N 30  
A1ASS C11 H7   sing N N 31  
A1ASS C11 H8   sing N N 32  
A1ASS C12 H9   sing N N 33  
A1ASS C12 H10  sing N N 34  
A1ASS C14 H11  sing N N 35  
A1ASS C18 H12  sing N N 36  
A1ASS C19 H13  sing N N 37  
A1ASS N07 H14  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HEM   CHA C1A  sing N N 167 
HEM   CHA C4D  doub N N 168 
HEM   CHA HHA  sing N N 169 
HEM   CHB C4A  sing N N 170 
HEM   CHB C1B  doub N N 171 
HEM   CHB HHB  sing N N 172 
HEM   CHC C4B  sing N N 173 
HEM   CHC C1C  doub N N 174 
HEM   CHC HHC  sing N N 175 
HEM   CHD C4C  doub N N 176 
HEM   CHD C1D  sing N N 177 
HEM   CHD HHD  sing N N 178 
HEM   C1A C2A  doub Y N 179 
HEM   C1A NA   sing Y N 180 
HEM   C2A C3A  sing Y N 181 
HEM   C2A CAA  sing N N 182 
HEM   C3A C4A  doub Y N 183 
HEM   C3A CMA  sing N N 184 
HEM   C4A NA   sing Y N 185 
HEM   CMA HMA  sing N N 186 
HEM   CMA HMAA sing N N 187 
HEM   CMA HMAB sing N N 188 
HEM   CAA CBA  sing N N 189 
HEM   CAA HAA  sing N N 190 
HEM   CAA HAAA sing N N 191 
HEM   CBA CGA  sing N N 192 
HEM   CBA HBA  sing N N 193 
HEM   CBA HBAA sing N N 194 
HEM   CGA O1A  doub N N 195 
HEM   CGA O2A  sing N N 196 
HEM   C1B C2B  sing N N 197 
HEM   C1B NB   sing N N 198 
HEM   C2B C3B  doub N N 199 
HEM   C2B CMB  sing N N 200 
HEM   C3B C4B  sing N N 201 
HEM   C3B CAB  sing N N 202 
HEM   C4B NB   doub N N 203 
HEM   CMB HMB  sing N N 204 
HEM   CMB HMBA sing N N 205 
HEM   CMB HMBB sing N N 206 
HEM   CAB CBB  doub N N 207 
HEM   CAB HAB  sing N N 208 
HEM   CBB HBB  sing N N 209 
HEM   CBB HBBA sing N N 210 
HEM   C1C C2C  sing Y N 211 
HEM   C1C NC   sing Y N 212 
HEM   C2C C3C  doub Y N 213 
HEM   C2C CMC  sing N N 214 
HEM   C3C C4C  sing Y N 215 
HEM   C3C CAC  sing N N 216 
HEM   C4C NC   sing Y N 217 
HEM   CMC HMC  sing N N 218 
HEM   CMC HMCA sing N N 219 
HEM   CMC HMCB sing N N 220 
HEM   CAC CBC  doub N N 221 
HEM   CAC HAC  sing N N 222 
HEM   CBC HBC  sing N N 223 
HEM   CBC HBCA sing N N 224 
HEM   C1D C2D  sing N N 225 
HEM   C1D ND   doub N N 226 
HEM   C2D C3D  doub N N 227 
HEM   C2D CMD  sing N N 228 
HEM   C3D C4D  sing N N 229 
HEM   C3D CAD  sing N N 230 
HEM   C4D ND   sing N N 231 
HEM   CMD HMD  sing N N 232 
HEM   CMD HMDA sing N N 233 
HEM   CMD HMDB sing N N 234 
HEM   CAD CBD  sing N N 235 
HEM   CAD HAD  sing N N 236 
HEM   CAD HADA sing N N 237 
HEM   CBD CGD  sing N N 238 
HEM   CBD HBD  sing N N 239 
HEM   CBD HBDA sing N N 240 
HEM   CGD O1D  doub N N 241 
HEM   CGD O2D  sing N N 242 
HEM   O2A H2A  sing N N 243 
HEM   O2D H2D  sing N N 244 
HEM   FE  NA   sing N N 245 
HEM   FE  NB   sing N N 246 
HEM   FE  NC   sing N N 247 
HEM   FE  ND   sing N N 248 
HIS   N   CA   sing N N 249 
HIS   N   H    sing N N 250 
HIS   N   H2   sing N N 251 
HIS   CA  C    sing N N 252 
HIS   CA  CB   sing N N 253 
HIS   CA  HA   sing N N 254 
HIS   C   O    doub N N 255 
HIS   C   OXT  sing N N 256 
HIS   CB  CG   sing N N 257 
HIS   CB  HB2  sing N N 258 
HIS   CB  HB3  sing N N 259 
HIS   CG  ND1  sing Y N 260 
HIS   CG  CD2  doub Y N 261 
HIS   ND1 CE1  doub Y N 262 
HIS   ND1 HD1  sing N N 263 
HIS   CD2 NE2  sing Y N 264 
HIS   CD2 HD2  sing N N 265 
HIS   CE1 NE2  sing Y N 266 
HIS   CE1 HE1  sing N N 267 
HIS   NE2 HE2  sing N N 268 
HIS   OXT HXT  sing N N 269 
ILE   N   CA   sing N N 270 
ILE   N   H    sing N N 271 
ILE   N   H2   sing N N 272 
ILE   CA  C    sing N N 273 
ILE   CA  CB   sing N N 274 
ILE   CA  HA   sing N N 275 
ILE   C   O    doub N N 276 
ILE   C   OXT  sing N N 277 
ILE   CB  CG1  sing N N 278 
ILE   CB  CG2  sing N N 279 
ILE   CB  HB   sing N N 280 
ILE   CG1 CD1  sing N N 281 
ILE   CG1 HG12 sing N N 282 
ILE   CG1 HG13 sing N N 283 
ILE   CG2 HG21 sing N N 284 
ILE   CG2 HG22 sing N N 285 
ILE   CG2 HG23 sing N N 286 
ILE   CD1 HD11 sing N N 287 
ILE   CD1 HD12 sing N N 288 
ILE   CD1 HD13 sing N N 289 
ILE   OXT HXT  sing N N 290 
LEU   N   CA   sing N N 291 
LEU   N   H    sing N N 292 
LEU   N   H2   sing N N 293 
LEU   CA  C    sing N N 294 
LEU   CA  CB   sing N N 295 
LEU   CA  HA   sing N N 296 
LEU   C   O    doub N N 297 
LEU   C   OXT  sing N N 298 
LEU   CB  CG   sing N N 299 
LEU   CB  HB2  sing N N 300 
LEU   CB  HB3  sing N N 301 
LEU   CG  CD1  sing N N 302 
LEU   CG  CD2  sing N N 303 
LEU   CG  HG   sing N N 304 
LEU   CD1 HD11 sing N N 305 
LEU   CD1 HD12 sing N N 306 
LEU   CD1 HD13 sing N N 307 
LEU   CD2 HD21 sing N N 308 
LEU   CD2 HD22 sing N N 309 
LEU   CD2 HD23 sing N N 310 
LEU   OXT HXT  sing N N 311 
LYS   N   CA   sing N N 312 
LYS   N   H    sing N N 313 
LYS   N   H2   sing N N 314 
LYS   CA  C    sing N N 315 
LYS   CA  CB   sing N N 316 
LYS   CA  HA   sing N N 317 
LYS   C   O    doub N N 318 
LYS   C   OXT  sing N N 319 
LYS   CB  CG   sing N N 320 
LYS   CB  HB2  sing N N 321 
LYS   CB  HB3  sing N N 322 
LYS   CG  CD   sing N N 323 
LYS   CG  HG2  sing N N 324 
LYS   CG  HG3  sing N N 325 
LYS   CD  CE   sing N N 326 
LYS   CD  HD2  sing N N 327 
LYS   CD  HD3  sing N N 328 
LYS   CE  NZ   sing N N 329 
LYS   CE  HE2  sing N N 330 
LYS   CE  HE3  sing N N 331 
LYS   NZ  HZ1  sing N N 332 
LYS   NZ  HZ2  sing N N 333 
LYS   NZ  HZ3  sing N N 334 
LYS   OXT HXT  sing N N 335 
MET   N   CA   sing N N 336 
MET   N   H    sing N N 337 
MET   N   H2   sing N N 338 
MET   CA  C    sing N N 339 
MET   CA  CB   sing N N 340 
MET   CA  HA   sing N N 341 
MET   C   O    doub N N 342 
MET   C   OXT  sing N N 343 
MET   CB  CG   sing N N 344 
MET   CB  HB2  sing N N 345 
MET   CB  HB3  sing N N 346 
MET   CG  SD   sing N N 347 
MET   CG  HG2  sing N N 348 
MET   CG  HG3  sing N N 349 
MET   SD  CE   sing N N 350 
MET   CE  HE1  sing N N 351 
MET   CE  HE2  sing N N 352 
MET   CE  HE3  sing N N 353 
MET   OXT HXT  sing N N 354 
PHE   N   CA   sing N N 355 
PHE   N   H    sing N N 356 
PHE   N   H2   sing N N 357 
PHE   CA  C    sing N N 358 
PHE   CA  CB   sing N N 359 
PHE   CA  HA   sing N N 360 
PHE   C   O    doub N N 361 
PHE   C   OXT  sing N N 362 
PHE   CB  CG   sing N N 363 
PHE   CB  HB2  sing N N 364 
PHE   CB  HB3  sing N N 365 
PHE   CG  CD1  doub Y N 366 
PHE   CG  CD2  sing Y N 367 
PHE   CD1 CE1  sing Y N 368 
PHE   CD1 HD1  sing N N 369 
PHE   CD2 CE2  doub Y N 370 
PHE   CD2 HD2  sing N N 371 
PHE   CE1 CZ   doub Y N 372 
PHE   CE1 HE1  sing N N 373 
PHE   CE2 CZ   sing Y N 374 
PHE   CE2 HE2  sing N N 375 
PHE   CZ  HZ   sing N N 376 
PHE   OXT HXT  sing N N 377 
PRO   N   CA   sing N N 378 
PRO   N   CD   sing N N 379 
PRO   N   H    sing N N 380 
PRO   CA  C    sing N N 381 
PRO   CA  CB   sing N N 382 
PRO   CA  HA   sing N N 383 
PRO   C   O    doub N N 384 
PRO   C   OXT  sing N N 385 
PRO   CB  CG   sing N N 386 
PRO   CB  HB2  sing N N 387 
PRO   CB  HB3  sing N N 388 
PRO   CG  CD   sing N N 389 
PRO   CG  HG2  sing N N 390 
PRO   CG  HG3  sing N N 391 
PRO   CD  HD2  sing N N 392 
PRO   CD  HD3  sing N N 393 
PRO   OXT HXT  sing N N 394 
SER   N   CA   sing N N 395 
SER   N   H    sing N N 396 
SER   N   H2   sing N N 397 
SER   CA  C    sing N N 398 
SER   CA  CB   sing N N 399 
SER   CA  HA   sing N N 400 
SER   C   O    doub N N 401 
SER   C   OXT  sing N N 402 
SER   CB  OG   sing N N 403 
SER   CB  HB2  sing N N 404 
SER   CB  HB3  sing N N 405 
SER   OG  HG   sing N N 406 
SER   OXT HXT  sing N N 407 
THR   N   CA   sing N N 408 
THR   N   H    sing N N 409 
THR   N   H2   sing N N 410 
THR   CA  C    sing N N 411 
THR   CA  CB   sing N N 412 
THR   CA  HA   sing N N 413 
THR   C   O    doub N N 414 
THR   C   OXT  sing N N 415 
THR   CB  OG1  sing N N 416 
THR   CB  CG2  sing N N 417 
THR   CB  HB   sing N N 418 
THR   OG1 HG1  sing N N 419 
THR   CG2 HG21 sing N N 420 
THR   CG2 HG22 sing N N 421 
THR   CG2 HG23 sing N N 422 
THR   OXT HXT  sing N N 423 
TRP   N   CA   sing N N 424 
TRP   N   H    sing N N 425 
TRP   N   H2   sing N N 426 
TRP   CA  C    sing N N 427 
TRP   CA  CB   sing N N 428 
TRP   CA  HA   sing N N 429 
TRP   C   O    doub N N 430 
TRP   C   OXT  sing N N 431 
TRP   CB  CG   sing N N 432 
TRP   CB  HB2  sing N N 433 
TRP   CB  HB3  sing N N 434 
TRP   CG  CD1  doub Y N 435 
TRP   CG  CD2  sing Y N 436 
TRP   CD1 NE1  sing Y N 437 
TRP   CD1 HD1  sing N N 438 
TRP   CD2 CE2  doub Y N 439 
TRP   CD2 CE3  sing Y N 440 
TRP   NE1 CE2  sing Y N 441 
TRP   NE1 HE1  sing N N 442 
TRP   CE2 CZ2  sing Y N 443 
TRP   CE3 CZ3  doub Y N 444 
TRP   CE3 HE3  sing N N 445 
TRP   CZ2 CH2  doub Y N 446 
TRP   CZ2 HZ2  sing N N 447 
TRP   CZ3 CH2  sing Y N 448 
TRP   CZ3 HZ3  sing N N 449 
TRP   CH2 HH2  sing N N 450 
TRP   OXT HXT  sing N N 451 
TYR   N   CA   sing N N 452 
TYR   N   H    sing N N 453 
TYR   N   H2   sing N N 454 
TYR   CA  C    sing N N 455 
TYR   CA  CB   sing N N 456 
TYR   CA  HA   sing N N 457 
TYR   C   O    doub N N 458 
TYR   C   OXT  sing N N 459 
TYR   CB  CG   sing N N 460 
TYR   CB  HB2  sing N N 461 
TYR   CB  HB3  sing N N 462 
TYR   CG  CD1  doub Y N 463 
TYR   CG  CD2  sing Y N 464 
TYR   CD1 CE1  sing Y N 465 
TYR   CD1 HD1  sing N N 466 
TYR   CD2 CE2  doub Y N 467 
TYR   CD2 HD2  sing N N 468 
TYR   CE1 CZ   doub Y N 469 
TYR   CE1 HE1  sing N N 470 
TYR   CE2 CZ   sing Y N 471 
TYR   CE2 HE2  sing N N 472 
TYR   CZ  OH   sing N N 473 
TYR   OH  HH   sing N N 474 
TYR   OXT HXT  sing N N 475 
VAL   N   CA   sing N N 476 
VAL   N   H    sing N N 477 
VAL   N   H2   sing N N 478 
VAL   CA  C    sing N N 479 
VAL   CA  CB   sing N N 480 
VAL   CA  HA   sing N N 481 
VAL   C   O    doub N N 482 
VAL   C   OXT  sing N N 483 
VAL   CB  CG1  sing N N 484 
VAL   CB  CG2  sing N N 485 
VAL   CB  HB   sing N N 486 
VAL   CG1 HG11 sing N N 487 
VAL   CG1 HG12 sing N N 488 
VAL   CG1 HG13 sing N N 489 
VAL   CG2 HG21 sing N N 490 
VAL   CG2 HG22 sing N N 491 
VAL   CG2 HG23 sing N N 492 
VAL   OXT HXT  sing N N 493 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM118041 
_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   1TQN 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BV8 
_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]   0.012946 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009920 
_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]   0.007601 
_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 
C  
F  
FE 
N  
O  
S  
# 
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   . HIS   A 1 7   ? -30.643 8.184   -15.960 1.00 76.85  ? 28  HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 7   ? -29.870 8.857   -14.921 1.00 87.36  ? 28  HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 7   ? -28.378 8.752   -15.213 1.00 88.85  ? 28  HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 7   ? -27.767 9.690   -15.727 1.00 84.27  ? 28  HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 7   ? -30.186 8.265   -13.545 1.00 87.37  ? 28  HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 7   ? -29.325 8.804   -12.444 1.00 93.25  ? 28  HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 7   ? -28.551 7.994   -11.640 1.00 93.91  ? 28  HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 7   ? -29.109 10.071  -12.019 1.00 91.62  ? 28  HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 7   ? -27.900 8.739   -10.765 1.00 91.75  ? 28  HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 7   ? -28.221 10.003  -10.973 1.00 94.24  ? 28  HIS   A NE2 1 
ATOM   11   N  N   . SER   A 1 8   ? -27.793 7.604   -14.881 1.00 84.07  ? 29  SER   A N   1 
ATOM   12   C  CA  . SER   A 1 8   ? -26.400 7.328   -15.201 1.00 78.74  ? 29  SER   A CA  1 
ATOM   13   C  C   . SER   A 1 8   ? -26.227 6.775   -16.607 1.00 77.39  ? 29  SER   A C   1 
ATOM   14   O  O   . SER   A 1 8   ? -25.129 6.324   -16.953 1.00 77.01  ? 29  SER   A O   1 
ATOM   15   C  CB  . SER   A 1 8   ? -25.802 6.358   -14.178 1.00 77.83  ? 29  SER   A CB  1 
ATOM   16   O  OG  . SER   A 1 8   ? -26.425 5.089   -14.253 1.00 75.29  ? 29  SER   A OG  1 
ATOM   17   N  N   . HIS   A 1 9   ? -27.286 6.801   -17.419 1.00 74.78  ? 30  HIS   A N   1 
ATOM   18   C  CA  . HIS   A 1 9   ? -27.223 6.321   -18.793 1.00 71.69  ? 30  HIS   A CA  1 
ATOM   19   C  C   . HIS   A 1 9   ? -26.656 7.389   -19.724 1.00 74.16  ? 30  HIS   A C   1 
ATOM   20   O  O   . HIS   A 1 9   ? -27.225 7.661   -20.787 1.00 78.55  ? 30  HIS   A O   1 
ATOM   21   C  CB  . HIS   A 1 9   ? -28.611 5.899   -19.289 1.00 68.44  ? 30  HIS   A CB  1 
ATOM   22   C  CG  . HIS   A 1 9   ? -29.264 4.826   -18.469 1.00 66.08  ? 30  HIS   A CG  1 
ATOM   23   N  ND1 . HIS   A 1 9   ? -30.497 4.299   -18.789 1.00 64.67  ? 30  HIS   A ND1 1 
ATOM   24   C  CD2 . HIS   A 1 9   ? -28.863 4.187   -17.344 1.00 66.63  ? 30  HIS   A CD2 1 
ATOM   25   C  CE1 . HIS   A 1 9   ? -30.826 3.381   -17.897 1.00 64.33  ? 30  HIS   A CE1 1 
ATOM   26   N  NE2 . HIS   A 1 9   ? -29.852 3.294   -17.010 1.00 66.25  ? 30  HIS   A NE2 1 
ATOM   27   N  N   . GLY   A 1 10  ? -25.533 7.990   -19.341 1.00 72.92  ? 31  GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 10  ? -24.864 8.964   -20.180 1.00 72.56  ? 31  GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 10  ? -23.360 8.815   -20.104 1.00 74.30  ? 31  GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 10  ? -22.611 9.650   -20.618 1.00 74.57  ? 31  GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 11  ? -22.910 7.744   -19.448 1.00 76.00  ? 32  LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 11  ? -21.480 7.528   -19.256 1.00 72.70  ? 32  LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 11  ? -20.797 7.073   -20.541 1.00 72.93  ? 32  LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 11  ? -19.738 7.593   -20.906 1.00 74.60  ? 32  LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 11  ? -21.257 6.507   -18.140 1.00 70.99  ? 32  LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 11  ? -19.800 6.134   -17.869 1.00 71.28  ? 32  LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 11  ? -18.980 7.377   -17.562 1.00 76.84  ? 32  LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 11  ? -19.713 5.134   -16.729 1.00 70.54  ? 32  LEU   A CD2 1 
ATOM   39   N  N   . PHE   A 1 12  ? -21.389 6.104   -21.242 1.00 72.90  ? 33  PHE   A N   1 
ATOM   40   C  CA  . PHE   A 1 12  ? -20.750 5.532   -22.420 1.00 73.13  ? 33  PHE   A CA  1 
ATOM   41   C  C   . PHE   A 1 12  ? -20.834 6.438   -23.642 1.00 72.63  ? 33  PHE   A C   1 
ATOM   42   O  O   . PHE   A 1 12  ? -20.078 6.234   -24.598 1.00 73.79  ? 33  PHE   A O   1 
ATOM   43   C  CB  . PHE   A 1 12  ? -21.360 4.162   -22.728 1.00 72.50  ? 33  PHE   A CB  1 
ATOM   44   C  CG  . PHE   A 1 12  ? -20.948 3.090   -21.758 1.00 69.61  ? 33  PHE   A CG  1 
ATOM   45   C  CD1 . PHE   A 1 12  ? -19.659 3.065   -21.249 1.00 68.47  ? 33  PHE   A CD1 1 
ATOM   46   C  CD2 . PHE   A 1 12  ? -21.846 2.121   -21.342 1.00 67.74  ? 33  PHE   A CD2 1 
ATOM   47   C  CE1 . PHE   A 1 12  ? -19.269 2.089   -20.352 1.00 64.05  ? 33  PHE   A CE1 1 
ATOM   48   C  CE2 . PHE   A 1 12  ? -21.462 1.141   -20.442 1.00 66.33  ? 33  PHE   A CE2 1 
ATOM   49   C  CZ  . PHE   A 1 12  ? -20.171 1.126   -19.948 1.00 63.64  ? 33  PHE   A CZ  1 
ATOM   50   N  N   . LYS   A 1 13  ? -21.727 7.428   -23.633 1.00 73.49  ? 34  LYS   A N   1 
ATOM   51   C  CA  . LYS   A 1 13  ? -21.724 8.429   -24.694 1.00 73.34  ? 34  LYS   A CA  1 
ATOM   52   C  C   . LYS   A 1 13  ? -20.661 9.493   -24.447 1.00 73.96  ? 34  LYS   A C   1 
ATOM   53   O  O   . LYS   A 1 13  ? -19.976 9.919   -25.383 1.00 74.51  ? 34  LYS   A O   1 
ATOM   54   C  CB  . LYS   A 1 13  ? -23.106 9.073   -24.817 1.00 69.26  ? 34  LYS   A CB  1 
ATOM   55   N  N   . LYS   A 1 14  ? -20.503 9.922   -23.191 1.00 73.37  ? 35  LYS   A N   1 
ATOM   56   C  CA  . LYS   A 1 14  ? -19.505 10.932  -22.862 1.00 74.37  ? 35  LYS   A CA  1 
ATOM   57   C  C   . LYS   A 1 14  ? -18.081 10.402  -22.968 1.00 77.77  ? 35  LYS   A C   1 
ATOM   58   O  O   . LYS   A 1 14  ? -17.137 11.199  -22.993 1.00 83.35  ? 35  LYS   A O   1 
ATOM   59   C  CB  . LYS   A 1 14  ? -19.753 11.479  -21.455 1.00 69.17  ? 35  LYS   A CB  1 
ATOM   60   N  N   . LEU   A 1 15  ? -17.903 9.083   -23.020 1.00 74.12  ? 36  LEU   A N   1 
ATOM   61   C  CA  . LEU   A 1 15  ? -16.594 8.476   -23.215 1.00 75.38  ? 36  LEU   A CA  1 
ATOM   62   C  C   . LEU   A 1 15  ? -16.362 8.020   -24.649 1.00 75.02  ? 36  LEU   A C   1 
ATOM   63   O  O   . LEU   A 1 15  ? -15.296 7.472   -24.944 1.00 73.96  ? 36  LEU   A O   1 
ATOM   64   C  CB  . LEU   A 1 15  ? -16.412 7.288   -22.266 1.00 77.76  ? 36  LEU   A CB  1 
ATOM   65   C  CG  . LEU   A 1 15  ? -16.416 7.578   -20.766 1.00 76.98  ? 36  LEU   A CG  1 
ATOM   66   C  CD1 . LEU   A 1 15  ? -16.169 6.295   -19.997 1.00 74.59  ? 36  LEU   A CD1 1 
ATOM   67   C  CD2 . LEU   A 1 15  ? -15.376 8.630   -20.412 1.00 80.22  ? 36  LEU   A CD2 1 
ATOM   68   N  N   . GLY   A 1 16  ? -17.327 8.230   -25.541 1.00 74.12  ? 37  GLY   A N   1 
ATOM   69   C  CA  . GLY   A 1 16  ? -17.174 7.798   -26.916 1.00 75.49  ? 37  GLY   A CA  1 
ATOM   70   C  C   . GLY   A 1 16  ? -17.237 6.303   -27.122 1.00 75.00  ? 37  GLY   A C   1 
ATOM   71   O  O   . GLY   A 1 16  ? -16.793 5.812   -28.162 1.00 75.90  ? 37  GLY   A O   1 
ATOM   72   N  N   . ILE   A 1 17  ? -17.778 5.563   -26.159 1.00 73.51  ? 38  ILE   A N   1 
ATOM   73   C  CA  . ILE   A 1 17  ? -17.857 4.106   -26.238 1.00 73.62  ? 38  ILE   A CA  1 
ATOM   74   C  C   . ILE   A 1 17  ? -19.177 3.708   -26.888 1.00 72.11  ? 38  ILE   A C   1 
ATOM   75   O  O   . ILE   A 1 17  ? -20.248 4.120   -26.419 1.00 69.61  ? 38  ILE   A O   1 
ATOM   76   C  CB  . ILE   A 1 17  ? -17.706 3.464   -24.850 1.00 72.31  ? 38  ILE   A CB  1 
ATOM   77   C  CG1 . ILE   A 1 17  ? -16.338 3.802   -24.251 1.00 70.85  ? 38  ILE   A CG1 1 
ATOM   78   C  CG2 . ILE   A 1 17  ? -17.892 1.959   -24.937 1.00 69.88  ? 38  ILE   A CG2 1 
ATOM   79   C  CD1 . ILE   A 1 17  ? -16.114 3.220   -22.870 1.00 70.67  ? 38  ILE   A CD1 1 
ATOM   80   N  N   . PRO   A 1 18  ? -19.155 2.919   -27.959 1.00 72.04  ? 39  PRO   A N   1 
ATOM   81   C  CA  . PRO   A 1 18  ? -20.406 2.528   -28.621 1.00 71.31  ? 39  PRO   A CA  1 
ATOM   82   C  C   . PRO   A 1 18  ? -21.210 1.555   -27.770 1.00 71.84  ? 39  PRO   A C   1 
ATOM   83   O  O   . PRO   A 1 18  ? -20.757 1.051   -26.740 1.00 72.96  ? 39  PRO   A O   1 
ATOM   84   C  CB  . PRO   A 1 18  ? -19.928 1.875   -29.920 1.00 71.20  ? 39  PRO   A CB  1 
ATOM   85   C  CG  . PRO   A 1 18  ? -18.561 1.367   -29.598 1.00 69.42  ? 39  PRO   A CG  1 
ATOM   86   C  CD  . PRO   A 1 18  ? -17.971 2.362   -28.636 1.00 68.93  ? 39  PRO   A CD  1 
ATOM   87   N  N   . GLY   A 1 19  ? -22.437 1.301   -28.219 1.00 75.23  ? 40  GLY   A N   1 
ATOM   88   C  CA  . GLY   A 1 19  ? -23.318 0.376   -27.547 1.00 74.91  ? 40  GLY   A CA  1 
ATOM   89   C  C   . GLY   A 1 19  ? -24.781 0.619   -27.859 1.00 72.24  ? 40  GLY   A C   1 
ATOM   90   O  O   . GLY   A 1 19  ? -25.155 1.635   -28.455 1.00 72.05  ? 40  GLY   A O   1 
ATOM   91   N  N   . PRO   A 1 20  ? -25.640 -0.322  -27.470 1.00 72.33  ? 41  PRO   A N   1 
ATOM   92   C  CA  . PRO   A 1 20  ? -27.081 -0.131  -27.667 1.00 68.50  ? 41  PRO   A CA  1 
ATOM   93   C  C   . PRO   A 1 20  ? -27.620 1.000   -26.804 1.00 66.56  ? 41  PRO   A C   1 
ATOM   94   O  O   . PRO   A 1 20  ? -27.155 1.238   -25.687 1.00 64.99  ? 41  PRO   A O   1 
ATOM   95   C  CB  . PRO   A 1 20  ? -27.678 -1.483  -27.258 1.00 65.40  ? 41  PRO   A CB  1 
ATOM   96   C  CG  . PRO   A 1 20  ? -26.663 -2.080  -26.336 1.00 65.22  ? 41  PRO   A CG  1 
ATOM   97   C  CD  . PRO   A 1 20  ? -25.328 -1.617  -26.843 1.00 69.90  ? 41  PRO   A CD  1 
ATOM   98   N  N   . THR   A 1 21  ? -28.621 1.693   -27.338 1.00 69.54  ? 42  THR   A N   1 
ATOM   99   C  CA  . THR   A 1 21  ? -29.165 2.874   -26.675 1.00 69.23  ? 42  THR   A CA  1 
ATOM   100  C  C   . THR   A 1 21  ? -30.071 2.459   -25.519 1.00 65.63  ? 42  THR   A C   1 
ATOM   101  O  O   . THR   A 1 21  ? -31.010 1.683   -25.721 1.00 60.15  ? 42  THR   A O   1 
ATOM   102  C  CB  . THR   A 1 21  ? -29.937 3.742   -27.661 1.00 66.95  ? 42  THR   A CB  1 
ATOM   103  O  OG1 . THR   A 1 21  ? -29.099 4.039   -28.785 1.00 67.88  ? 42  THR   A OG1 1 
ATOM   104  C  CG2 . THR   A 1 21  ? -30.358 5.047   -27.001 1.00 62.73  ? 42  THR   A CG2 1 
ATOM   105  N  N   . PRO   A 1 22  ? -29.826 2.954   -24.307 1.00 64.46  ? 43  PRO   A N   1 
ATOM   106  C  CA  . PRO   A 1 22  ? -30.562 2.463   -23.136 1.00 62.82  ? 43  PRO   A CA  1 
ATOM   107  C  C   . PRO   A 1 22  ? -31.924 3.115   -22.965 1.00 61.13  ? 43  PRO   A C   1 
ATOM   108  O  O   . PRO   A 1 22  ? -32.099 4.315   -23.176 1.00 60.75  ? 43  PRO   A O   1 
ATOM   109  C  CB  . PRO   A 1 22  ? -29.637 2.827   -21.970 1.00 63.72  ? 43  PRO   A CB  1 
ATOM   110  C  CG  . PRO   A 1 22  ? -28.924 4.040   -22.441 1.00 63.53  ? 43  PRO   A CG  1 
ATOM   111  C  CD  . PRO   A 1 22  ? -28.742 3.881   -23.931 1.00 62.26  ? 43  PRO   A CD  1 
ATOM   112  N  N   . LEU   A 1 23  ? -32.898 2.297   -22.555 1.00 60.66  ? 44  LEU   A N   1 
ATOM   113  C  CA  . LEU   A 1 23  ? -34.224 2.774   -22.202 1.00 57.28  ? 44  LEU   A CA  1 
ATOM   114  C  C   . LEU   A 1 23  ? -34.244 3.243   -20.749 1.00 58.24  ? 44  LEU   A C   1 
ATOM   115  O  O   . LEU   A 1 23  ? -33.513 2.711   -19.910 1.00 57.95  ? 44  LEU   A O   1 
ATOM   116  C  CB  . LEU   A 1 23  ? -35.267 1.674   -22.402 1.00 55.07  ? 44  LEU   A CB  1 
ATOM   117  C  CG  . LEU   A 1 23  ? -35.520 1.173   -23.825 1.00 53.50  ? 44  LEU   A CG  1 
ATOM   118  C  CD1 . LEU   A 1 23  ? -36.717 0.235   -23.838 1.00 42.63  ? 44  LEU   A CD1 1 
ATOM   119  C  CD2 . LEU   A 1 23  ? -35.736 2.342   -24.767 1.00 54.95  ? 44  LEU   A CD2 1 
ATOM   120  N  N   . PRO   A 1 24  ? -35.061 4.248   -20.429 1.00 59.00  ? 45  PRO   A N   1 
ATOM   121  C  CA  . PRO   A 1 24  ? -35.146 4.712   -19.038 1.00 56.39  ? 45  PRO   A CA  1 
ATOM   122  C  C   . PRO   A 1 24  ? -35.591 3.604   -18.090 1.00 59.41  ? 45  PRO   A C   1 
ATOM   123  O  O   . PRO   A 1 24  ? -36.457 2.789   -18.418 1.00 62.30  ? 45  PRO   A O   1 
ATOM   124  C  CB  . PRO   A 1 24  ? -36.179 5.841   -19.106 1.00 52.44  ? 45  PRO   A CB  1 
ATOM   125  C  CG  . PRO   A 1 24  ? -36.114 6.326   -20.510 1.00 54.44  ? 45  PRO   A CG  1 
ATOM   126  C  CD  . PRO   A 1 24  ? -35.846 5.099   -21.341 1.00 56.94  ? 45  PRO   A CD  1 
ATOM   127  N  N   . PHE   A 1 25  ? -34.951 3.569   -16.917 1.00 60.16  ? 46  PHE   A N   1 
ATOM   128  C  CA  . PHE   A 1 25  ? -35.266 2.683   -15.796 1.00 60.50  ? 46  PHE   A CA  1 
ATOM   129  C  C   . PHE   A 1 25  ? -34.898 1.229   -16.067 1.00 60.96  ? 46  PHE   A C   1 
ATOM   130  O  O   . PHE   A 1 25  ? -34.888 0.410   -15.141 1.00 66.02  ? 46  PHE   A O   1 
ATOM   131  C  CB  . PHE   A 1 25  ? -36.754 2.739   -15.433 1.00 59.81  ? 46  PHE   A CB  1 
ATOM   132  C  CG  . PHE   A 1 25  ? -37.170 3.987   -14.715 1.00 64.19  ? 46  PHE   A CG  1 
ATOM   133  C  CD1 . PHE   A 1 25  ? -36.599 4.333   -13.501 1.00 67.05  ? 46  PHE   A CD1 1 
ATOM   134  C  CD2 . PHE   A 1 25  ? -38.165 4.794   -15.237 1.00 62.89  ? 46  PHE   A CD2 1 
ATOM   135  C  CE1 . PHE   A 1 25  ? -36.997 5.477   -12.836 1.00 66.85  ? 46  PHE   A CE1 1 
ATOM   136  C  CE2 . PHE   A 1 25  ? -38.569 5.937   -14.578 1.00 63.18  ? 46  PHE   A CE2 1 
ATOM   137  C  CZ  . PHE   A 1 25  ? -37.984 6.280   -13.375 1.00 67.22  ? 46  PHE   A CZ  1 
ATOM   138  N  N   . LEU   A 1 26  ? -34.558 0.901   -17.313 1.00 58.61  ? 47  LEU   A N   1 
ATOM   139  C  CA  . LEU   A 1 26  ? -34.355 -0.482  -17.715 1.00 59.65  ? 47  LEU   A CA  1 
ATOM   140  C  C   . LEU   A 1 26  ? -33.002 -0.751  -18.347 1.00 61.36  ? 47  LEU   A C   1 
ATOM   141  O  O   . LEU   A 1 26  ? -32.534 -1.894  -18.288 1.00 60.30  ? 47  LEU   A O   1 
ATOM   142  C  CB  . LEU   A 1 26  ? -35.444 -0.927  -18.710 1.00 56.11  ? 47  LEU   A CB  1 
ATOM   143  C  CG  . LEU   A 1 26  ? -36.885 -1.108  -18.226 1.00 56.49  ? 47  LEU   A CG  1 
ATOM   144  C  CD1 . LEU   A 1 26  ? -37.756 -1.677  -19.341 1.00 55.42  ? 47  LEU   A CD1 1 
ATOM   145  C  CD2 . LEU   A 1 26  ? -36.936 -2.001  -16.998 1.00 56.67  ? 47  LEU   A CD2 1 
ATOM   146  N  N   . GLY   A 1 27  ? -32.361 0.252   -18.938 1.00 61.69  ? 48  GLY   A N   1 
ATOM   147  C  CA  . GLY   A 1 27  ? -31.163 -0.036  -19.692 1.00 59.51  ? 48  GLY   A CA  1 
ATOM   148  C  C   . GLY   A 1 27  ? -31.487 -0.893  -20.900 1.00 62.12  ? 48  GLY   A C   1 
ATOM   149  O  O   . GLY   A 1 27  ? -32.573 -0.818  -21.486 1.00 63.10  ? 48  GLY   A O   1 
ATOM   150  N  N   . ASN   A 1 28  ? -30.527 -1.736  -21.274 1.00 59.23  ? 49  ASN   A N   1 
ATOM   151  C  CA  . ASN   A 1 28  ? -30.674 -2.648  -22.401 1.00 58.97  ? 49  ASN   A CA  1 
ATOM   152  C  C   . ASN   A 1 28  ? -31.130 -4.033  -21.957 1.00 62.61  ? 49  ASN   A C   1 
ATOM   153  O  O   . ASN   A 1 28  ? -30.842 -5.031  -22.627 1.00 64.53  ? 49  ASN   A O   1 
ATOM   154  C  CB  . ASN   A 1 28  ? -29.360 -2.726  -23.175 1.00 62.49  ? 49  ASN   A CB  1 
ATOM   155  C  CG  . ASN   A 1 28  ? -28.660 -1.382  -23.255 1.00 64.28  ? 49  ASN   A CG  1 
ATOM   156  O  OD1 . ASN   A 1 28  ? -27.916 -1.003  -22.351 1.00 62.19  ? 49  ASN   A OD1 1 
ATOM   157  N  ND2 . ASN   A 1 28  ? -28.907 -0.648  -24.333 1.00 67.81  ? 49  ASN   A ND2 1 
ATOM   158  N  N   . ILE   A 1 29  ? -31.844 -4.102  -20.830 1.00 59.37  ? 50  ILE   A N   1 
ATOM   159  C  CA  . ILE   A 1 29  ? -32.289 -5.381  -20.281 1.00 57.30  ? 50  ILE   A CA  1 
ATOM   160  C  C   . ILE   A 1 29  ? -33.206 -6.102  -21.261 1.00 58.53  ? 50  ILE   A C   1 
ATOM   161  O  O   . ILE   A 1 29  ? -33.138 -7.329  -21.410 1.00 60.74  ? 50  ILE   A O   1 
ATOM   162  C  CB  . ILE   A 1 29  ? -32.970 -5.157  -18.915 1.00 59.29  ? 50  ILE   A CB  1 
ATOM   163  C  CG1 . ILE   A 1 29  ? -31.932 -5.182  -17.789 1.00 63.37  ? 50  ILE   A CG1 1 
ATOM   164  C  CG2 . ILE   A 1 29  ? -34.074 -6.181  -18.674 1.00 59.15  ? 50  ILE   A CG2 1 
ATOM   165  C  CD1 . ILE   A 1 29  ? -32.530 -5.037  -16.404 1.00 67.03  ? 50  ILE   A CD1 1 
ATOM   166  N  N   . LEU   A 1 30  ? -34.070 -5.354  -21.954 1.00 60.55  ? 51  LEU   A N   1 
ATOM   167  C  CA  . LEU   A 1 30  ? -34.999 -5.968  -22.895 1.00 60.33  ? 51  LEU   A CA  1 
ATOM   168  C  C   . LEU   A 1 30  ? -34.287 -6.677  -24.040 1.00 62.54  ? 51  LEU   A C   1 
ATOM   169  O  O   . LEU   A 1 30  ? -34.893 -7.533  -24.693 1.00 64.71  ? 51  LEU   A O   1 
ATOM   170  C  CB  . LEU   A 1 30  ? -35.960 -4.915  -23.450 1.00 54.96  ? 51  LEU   A CB  1 
ATOM   171  C  CG  . LEU   A 1 30  ? -36.920 -4.286  -22.439 1.00 55.95  ? 51  LEU   A CG  1 
ATOM   172  C  CD1 . LEU   A 1 30  ? -37.900 -3.351  -23.133 1.00 50.64  ? 51  LEU   A CD1 1 
ATOM   173  C  CD2 . LEU   A 1 30  ? -37.658 -5.366  -21.663 1.00 54.50  ? 51  LEU   A CD2 1 
ATOM   174  N  N   . SER   A 1 31  ? -33.020 -6.348  -24.299 1.00 56.54  ? 52  SER   A N   1 
ATOM   175  C  CA  . SER   A 1 31  ? -32.252 -7.066  -25.310 1.00 60.82  ? 52  SER   A CA  1 
ATOM   176  C  C   . SER   A 1 31  ? -31.816 -8.452  -24.852 1.00 62.42  ? 52  SER   A C   1 
ATOM   177  O  O   . SER   A 1 31  ? -31.111 -9.135  -25.603 1.00 63.15  ? 52  SER   A O   1 
ATOM   178  C  CB  . SER   A 1 31  ? -31.025 -6.251  -25.722 1.00 61.69  ? 52  SER   A CB  1 
ATOM   179  O  OG  . SER   A 1 31  ? -31.382 -5.177  -26.576 1.00 65.19  ? 52  SER   A OG  1 
ATOM   180  N  N   . TYR   A 1 32  ? -32.205 -8.881  -23.652 1.00 61.28  ? 53  TYR   A N   1 
ATOM   181  C  CA  . TYR   A 1 32  ? -31.918 -10.223 -23.167 1.00 61.03  ? 53  TYR   A CA  1 
ATOM   182  C  C   . TYR   A 1 32  ? -32.998 -11.229 -23.542 1.00 65.24  ? 53  TYR   A C   1 
ATOM   183  O  O   . TYR   A 1 32  ? -33.029 -12.324 -22.970 1.00 63.92  ? 53  TYR   A O   1 
ATOM   184  C  CB  . TYR   A 1 32  ? -31.738 -10.218 -21.644 1.00 60.02  ? 53  TYR   A CB  1 
ATOM   185  C  CG  . TYR   A 1 32  ? -30.422 -9.647  -21.165 1.00 58.64  ? 53  TYR   A CG  1 
ATOM   186  C  CD1 . TYR   A 1 32  ? -29.214 -10.158 -21.620 1.00 60.57  ? 53  TYR   A CD1 1 
ATOM   187  C  CD2 . TYR   A 1 32  ? -30.388 -8.615  -20.237 1.00 57.85  ? 53  TYR   A CD2 1 
ATOM   188  C  CE1 . TYR   A 1 32  ? -28.010 -9.643  -21.181 1.00 62.23  ? 53  TYR   A CE1 1 
ATOM   189  C  CE2 . TYR   A 1 32  ? -29.187 -8.095  -19.789 1.00 59.24  ? 53  TYR   A CE2 1 
ATOM   190  C  CZ  . TYR   A 1 32  ? -28.001 -8.613  -20.264 1.00 59.61  ? 53  TYR   A CZ  1 
ATOM   191  O  OH  . TYR   A 1 32  ? -26.803 -8.099  -19.821 1.00 54.49  ? 53  TYR   A OH  1 
ATOM   192  N  N   . HIS   A 1 33  ? -33.886 -10.886 -24.480 1.00 66.68  ? 54  HIS   A N   1 
ATOM   193  C  CA  . HIS   A 1 33  ? -34.948 -11.809 -24.866 1.00 66.08  ? 54  HIS   A CA  1 
ATOM   194  C  C   . HIS   A 1 33  ? -34.408 -13.059 -25.548 1.00 67.69  ? 54  HIS   A C   1 
ATOM   195  O  O   . HIS   A 1 33  ? -35.122 -14.065 -25.626 1.00 68.89  ? 54  HIS   A O   1 
ATOM   196  C  CB  . HIS   A 1 33  ? -35.959 -11.109 -25.779 1.00 66.48  ? 54  HIS   A CB  1 
ATOM   197  C  CG  . HIS   A 1 33  ? -35.441 -10.823 -27.155 1.00 68.70  ? 54  HIS   A CG  1 
ATOM   198  N  ND1 . HIS   A 1 33  ? -34.364 -9.996  -27.389 1.00 69.73  ? 54  HIS   A ND1 1 
ATOM   199  C  CD2 . HIS   A 1 33  ? -35.861 -11.247 -28.371 1.00 70.20  ? 54  HIS   A CD2 1 
ATOM   200  C  CE1 . HIS   A 1 33  ? -34.139 -9.927  -28.689 1.00 69.72  ? 54  HIS   A CE1 1 
ATOM   201  N  NE2 . HIS   A 1 33  ? -35.034 -10.677 -29.308 1.00 73.92  ? 54  HIS   A NE2 1 
ATOM   202  N  N   . LYS   A 1 34  ? -33.172 -13.019 -26.044 1.00 67.35  ? 55  LYS   A N   1 
ATOM   203  C  CA  . LYS   A 1 34  ? -32.526 -14.182 -26.636 1.00 70.78  ? 55  LYS   A CA  1 
ATOM   204  C  C   . LYS   A 1 34  ? -31.356 -14.689 -25.801 1.00 70.83  ? 55  LYS   A C   1 
ATOM   205  O  O   . LYS   A 1 34  ? -30.557 -15.492 -26.295 1.00 73.69  ? 55  LYS   A O   1 
ATOM   206  C  CB  . LYS   A 1 34  ? -32.069 -13.862 -28.061 1.00 73.20  ? 55  LYS   A CB  1 
ATOM   207  C  CG  . LYS   A 1 34  ? -33.218 -13.576 -29.016 1.00 73.30  ? 55  LYS   A CG  1 
ATOM   208  C  CD  . LYS   A 1 34  ? -32.736 -13.348 -30.439 1.00 76.26  ? 55  LYS   A CD  1 
ATOM   209  C  CE  . LYS   A 1 34  ? -33.914 -13.181 -31.388 1.00 79.45  ? 55  LYS   A CE  1 
ATOM   210  N  NZ  . LYS   A 1 34  ? -33.482 -13.036 -32.805 1.00 83.49  ? 55  LYS   A NZ  1 
ATOM   211  N  N   . GLY   A 1 35  ? -31.237 -14.244 -24.554 1.00 64.67  ? 56  GLY   A N   1 
ATOM   212  C  CA  . GLY   A 1 35  ? -30.240 -14.755 -23.637 1.00 62.27  ? 56  GLY   A CA  1 
ATOM   213  C  C   . GLY   A 1 35  ? -29.019 -13.856 -23.536 1.00 62.20  ? 56  GLY   A C   1 
ATOM   214  O  O   . GLY   A 1 35  ? -28.841 -12.890 -24.283 1.00 65.04  ? 56  GLY   A O   1 
ATOM   215  N  N   . PHE   A 1 36  ? -28.165 -14.195 -22.566 1.00 61.75  ? 57  PHE   A N   1 
ATOM   216  C  CA  . PHE   A 1 36  ? -26.923 -13.453 -22.365 1.00 61.13  ? 57  PHE   A CA  1 
ATOM   217  C  C   . PHE   A 1 36  ? -25.989 -13.604 -23.557 1.00 62.92  ? 57  PHE   A C   1 
ATOM   218  O  O   . PHE   A 1 36  ? -25.424 -12.622 -24.050 1.00 65.28  ? 57  PHE   A O   1 
ATOM   219  C  CB  . PHE   A 1 36  ? -26.220 -13.934 -21.094 1.00 61.35  ? 57  PHE   A CB  1 
ATOM   220  C  CG  . PHE   A 1 36  ? -26.867 -13.475 -19.824 1.00 62.53  ? 57  PHE   A CG  1 
ATOM   221  C  CD1 . PHE   A 1 36  ? -26.706 -12.174 -19.384 1.00 62.53  ? 57  PHE   A CD1 1 
ATOM   222  C  CD2 . PHE   A 1 36  ? -27.613 -14.351 -19.056 1.00 63.03  ? 57  PHE   A CD2 1 
ATOM   223  C  CE1 . PHE   A 1 36  ? -27.293 -11.748 -18.210 1.00 64.13  ? 57  PHE   A CE1 1 
ATOM   224  C  CE2 . PHE   A 1 36  ? -28.198 -13.932 -17.880 1.00 63.16  ? 57  PHE   A CE2 1 
ATOM   225  C  CZ  . PHE   A 1 36  ? -28.041 -12.629 -17.457 1.00 62.82  ? 57  PHE   A CZ  1 
ATOM   226  N  N   . CYS   A 1 37  ? -25.813 -14.837 -24.029 1.00 65.31  ? 58  CYS   A N   1 
ATOM   227  C  CA  . CYS   A 1 37  ? -24.764 -15.133 -24.998 1.00 65.75  ? 58  CYS   A CA  1 
ATOM   228  C  C   . CYS   A 1 37  ? -25.098 -14.600 -26.383 1.00 68.51  ? 58  CYS   A C   1 
ATOM   229  O  O   . CYS   A 1 37  ? -24.218 -14.083 -27.079 1.00 69.13  ? 58  CYS   A O   1 
ATOM   230  C  CB  . CYS   A 1 37  ? -24.527 -16.639 -25.045 1.00 67.55  ? 58  CYS   A CB  1 
ATOM   231  S  SG  . CYS   A 1 37  ? -24.194 -17.361 -23.429 1.00 72.49  ? 58  CYS   A SG  1 
ATOM   232  N  N   . MET   A 1 38  ? -26.357 -14.726 -26.805 1.00 69.04  ? 59  MET   A N   1 
ATOM   233  C  CA  . MET   A 1 38  ? -26.750 -14.186 -28.102 1.00 68.52  ? 59  MET   A CA  1 
ATOM   234  C  C   . MET   A 1 38  ? -26.636 -12.666 -28.116 1.00 66.91  ? 59  MET   A C   1 
ATOM   235  O  O   . MET   A 1 38  ? -26.285 -12.070 -29.141 1.00 69.14  ? 59  MET   A O   1 
ATOM   236  C  CB  . MET   A 1 38  ? -28.172 -14.632 -28.446 1.00 73.56  ? 59  MET   A CB  1 
ATOM   237  C  CG  . MET   A 1 38  ? -28.296 -15.296 -29.812 1.00 82.28  ? 59  MET   A CG  1 
ATOM   238  S  SD  . MET   A 1 38  ? -27.257 -16.760 -29.995 1.00 88.64  ? 59  MET   A SD  1 
ATOM   239  C  CE  . MET   A 1 38  ? -28.134 -17.945 -28.977 1.00 84.14  ? 59  MET   A CE  1 
ATOM   240  N  N   . PHE   A 1 39  ? -26.935 -12.021 -26.984 1.00 67.38  ? 60  PHE   A N   1 
ATOM   241  C  CA  . PHE   A 1 39  ? -26.798 -10.571 -26.894 1.00 66.02  ? 60  PHE   A CA  1 
ATOM   242  C  C   . PHE   A 1 39  ? -25.343 -10.139 -27.043 1.00 67.57  ? 60  PHE   A C   1 
ATOM   243  O  O   . PHE   A 1 39  ? -25.053 -9.137  -27.707 1.00 68.80  ? 60  PHE   A O   1 
ATOM   244  C  CB  . PHE   A 1 39  ? -27.380 -10.076 -25.570 1.00 63.99  ? 60  PHE   A CB  1 
ATOM   245  C  CG  . PHE   A 1 39  ? -27.078 -8.635  -25.271 1.00 65.98  ? 60  PHE   A CG  1 
ATOM   246  C  CD1 . PHE   A 1 39  ? -27.735 -7.619  -25.945 1.00 65.44  ? 60  PHE   A CD1 1 
ATOM   247  C  CD2 . PHE   A 1 39  ? -26.143 -8.296  -24.307 1.00 63.82  ? 60  PHE   A CD2 1 
ATOM   248  C  CE1 . PHE   A 1 39  ? -27.459 -6.293  -25.668 1.00 62.58  ? 60  PHE   A CE1 1 
ATOM   249  C  CE2 . PHE   A 1 39  ? -25.863 -6.973  -24.024 1.00 60.52  ? 60  PHE   A CE2 1 
ATOM   250  C  CZ  . PHE   A 1 39  ? -26.522 -5.970  -24.705 1.00 62.32  ? 60  PHE   A CZ  1 
ATOM   251  N  N   . ASP   A 1 40  ? -24.413 -10.876 -26.431 1.00 68.39  ? 61  ASP   A N   1 
ATOM   252  C  CA  . ASP   A 1 40  ? -23.002 -10.520 -26.546 1.00 71.18  ? 61  ASP   A CA  1 
ATOM   253  C  C   . ASP   A 1 40  ? -22.462 -10.829 -27.936 1.00 70.88  ? 61  ASP   A C   1 
ATOM   254  O  O   . ASP   A 1 40  ? -21.605 -10.100 -28.450 1.00 71.59  ? 61  ASP   A O   1 
ATOM   255  C  CB  . ASP   A 1 40  ? -22.191 -11.248 -25.476 1.00 70.23  ? 61  ASP   A CB  1 
ATOM   256  C  CG  . ASP   A 1 40  ? -22.536 -10.785 -24.077 1.00 67.28  ? 61  ASP   A CG  1 
ATOM   257  O  OD1 . ASP   A 1 40  ? -22.865 -9.591  -23.916 1.00 67.47  ? 61  ASP   A OD1 1 
ATOM   258  O  OD2 . ASP   A 1 40  ? -22.488 -11.614 -23.144 1.00 64.91  ? 61  ASP   A OD2 1 
ATOM   259  N  N   . MET   A 1 41  ? -22.944 -11.910 -28.555 1.00 71.44  ? 62  MET   A N   1 
ATOM   260  C  CA  . MET   A 1 41  ? -22.539 -12.230 -29.920 1.00 73.30  ? 62  MET   A CA  1 
ATOM   261  C  C   . MET   A 1 41  ? -22.943 -11.123 -30.887 1.00 75.04  ? 62  MET   A C   1 
ATOM   262  O  O   . MET   A 1 41  ? -22.132 -10.666 -31.701 1.00 77.27  ? 62  MET   A O   1 
ATOM   263  C  CB  . MET   A 1 41  ? -23.150 -13.566 -30.347 1.00 72.92  ? 62  MET   A CB  1 
ATOM   264  C  CG  . MET   A 1 41  ? -22.497 -14.791 -29.727 1.00 74.88  ? 62  MET   A CG  1 
ATOM   265  S  SD  . MET   A 1 41  ? -21.166 -15.462 -30.742 1.00 83.28  ? 62  MET   A SD  1 
ATOM   266  C  CE  . MET   A 1 41  ? -22.073 -15.951 -32.207 1.00 75.97  ? 62  MET   A CE  1 
ATOM   267  N  N   . GLU   A 1 42  ? -24.201 -10.678 -30.809 1.00 73.36  ? 63  GLU   A N   1 
ATOM   268  C  CA  . GLU   A 1 42  ? -24.676 -9.637  -31.717 1.00 74.81  ? 63  GLU   A CA  1 
ATOM   269  C  C   . GLU   A 1 42  ? -23.968 -8.311  -31.468 1.00 74.96  ? 63  GLU   A C   1 
ATOM   270  O  O   . GLU   A 1 42  ? -23.598 -7.611  -32.418 1.00 77.89  ? 63  GLU   A O   1 
ATOM   271  C  CB  . GLU   A 1 42  ? -26.190 -9.465  -31.579 1.00 74.76  ? 63  GLU   A CB  1 
ATOM   272  C  CG  . GLU   A 1 42  ? -27.002 -10.599 -32.177 1.00 79.71  ? 63  GLU   A CG  1 
ATOM   273  C  CD  . GLU   A 1 42  ? -28.441 -10.202 -32.449 1.00 90.30  ? 63  GLU   A CD  1 
ATOM   274  O  OE1 . GLU   A 1 42  ? -28.810 -9.047  -32.147 1.00 90.48  ? 63  GLU   A OE1 1 
ATOM   275  O  OE2 . GLU   A 1 42  ? -29.203 -11.046 -32.969 1.00 92.79  ? 63  GLU   A OE2 1 
ATOM   276  N  N   . CYS   A 1 43  ? -23.777 -7.947  -30.198 1.00 73.07  ? 64  CYS   A N   1 
ATOM   277  C  CA  . CYS   A 1 43  ? -23.065 -6.714  -29.880 1.00 76.14  ? 64  CYS   A CA  1 
ATOM   278  C  C   . CYS   A 1 43  ? -21.646 -6.742  -30.428 1.00 76.41  ? 64  CYS   A C   1 
ATOM   279  O  O   . CYS   A 1 43  ? -21.144 -5.729  -30.930 1.00 76.38  ? 64  CYS   A O   1 
ATOM   280  C  CB  . CYS   A 1 43  ? -23.047 -6.493  -28.368 1.00 76.93  ? 64  CYS   A CB  1 
ATOM   281  S  SG  . CYS   A 1 43  ? -24.520 -5.699  -27.699 1.00 71.28  ? 64  CYS   A SG  1 
ATOM   282  N  N   . HIS   A 1 44  ? -20.986 -7.899  -30.343 1.00 77.01  ? 65  HIS   A N   1 
ATOM   283  C  CA  . HIS   A 1 44  ? -19.624 -8.025  -30.849 1.00 77.03  ? 65  HIS   A CA  1 
ATOM   284  C  C   . HIS   A 1 44  ? -19.565 -7.758  -32.348 1.00 77.56  ? 65  HIS   A C   1 
ATOM   285  O  O   . HIS   A 1 44  ? -18.588 -7.188  -32.847 1.00 78.45  ? 65  HIS   A O   1 
ATOM   286  C  CB  . HIS   A 1 44  ? -19.088 -9.421  -30.525 1.00 73.90  ? 65  HIS   A CB  1 
ATOM   287  C  CG  . HIS   A 1 44  ? -17.616 -9.573  -30.742 1.00 76.68  ? 65  HIS   A CG  1 
ATOM   288  N  ND1 . HIS   A 1 44  ? -16.691 -8.701  -30.208 1.00 78.22  ? 65  HIS   A ND1 1 
ATOM   289  C  CD2 . HIS   A 1 44  ? -16.907 -10.503 -31.424 1.00 77.95  ? 65  HIS   A CD2 1 
ATOM   290  C  CE1 . HIS   A 1 44  ? -15.476 -9.086  -30.557 1.00 78.99  ? 65  HIS   A CE1 1 
ATOM   291  N  NE2 . HIS   A 1 44  ? -15.579 -10.177 -31.294 1.00 78.48  ? 65  HIS   A NE2 1 
ATOM   292  N  N   . LYS   A 1 45  ? -20.607 -8.161  -33.080 1.00 75.31  ? 66  LYS   A N   1 
ATOM   293  C  CA  . LYS   A 1 45  ? -20.623 -7.969  -34.527 1.00 75.23  ? 66  LYS   A CA  1 
ATOM   294  C  C   . LYS   A 1 45  ? -20.765 -6.499  -34.904 1.00 78.37  ? 66  LYS   A C   1 
ATOM   295  O  O   . LYS   A 1 45  ? -20.068 -6.017  -35.805 1.00 79.48  ? 66  LYS   A O   1 
ATOM   296  C  CB  . LYS   A 1 45  ? -21.753 -8.797  -35.144 1.00 75.17  ? 66  LYS   A CB  1 
ATOM   297  C  CG  . LYS   A 1 45  ? -21.610 -10.292 -34.912 1.00 80.10  ? 66  LYS   A CG  1 
ATOM   298  C  CD  . LYS   A 1 45  ? -22.953 -11.003 -34.934 1.00 80.57  ? 66  LYS   A CD  1 
ATOM   299  C  CE  . LYS   A 1 45  ? -22.807 -12.456 -34.505 1.00 79.26  ? 66  LYS   A CE  1 
ATOM   300  N  NZ  . LYS   A 1 45  ? -24.122 -13.140 -34.358 1.00 79.42  ? 66  LYS   A NZ  1 
ATOM   301  N  N   . LYS   A 1 46  ? -21.648 -5.766  -34.226 1.00 79.36  ? 67  LYS   A N   1 
ATOM   302  C  CA  . LYS   A 1 46  ? -22.043 -4.433  -34.666 1.00 77.34  ? 67  LYS   A CA  1 
ATOM   303  C  C   . LYS   A 1 46  ? -21.445 -3.298  -33.844 1.00 77.85  ? 67  LYS   A C   1 
ATOM   304  O  O   . LYS   A 1 46  ? -21.798 -2.138  -34.080 1.00 80.27  ? 67  LYS   A O   1 
ATOM   305  C  CB  . LYS   A 1 46  ? -23.572 -4.308  -34.663 1.00 76.82  ? 67  LYS   A CB  1 
ATOM   306  C  CG  . LYS   A 1 46  ? -24.207 -4.428  -33.290 1.00 77.69  ? 67  LYS   A CG  1 
ATOM   307  C  CD  . LYS   A 1 46  ? -25.589 -3.797  -33.266 1.00 80.91  ? 67  LYS   A CD  1 
ATOM   308  C  CE  . LYS   A 1 46  ? -26.523 -4.448  -34.272 1.00 83.70  ? 67  LYS   A CE  1 
ATOM   309  N  NZ  . LYS   A 1 46  ? -27.858 -3.787  -34.284 1.00 82.52  ? 67  LYS   A NZ  1 
ATOM   310  N  N   . TYR   A 1 47  ? -20.556 -3.584  -32.894 1.00 76.31  ? 68  TYR   A N   1 
ATOM   311  C  CA  . TYR   A 1 47  ? -19.944 -2.523  -32.104 1.00 75.30  ? 68  TYR   A CA  1 
ATOM   312  C  C   . TYR   A 1 47  ? -18.430 -2.614  -31.998 1.00 77.71  ? 68  TYR   A C   1 
ATOM   313  O  O   . TYR   A 1 47  ? -17.815 -1.673  -31.482 1.00 79.26  ? 68  TYR   A O   1 
ATOM   314  C  CB  . TYR   A 1 47  ? -20.544 -2.482  -30.690 1.00 74.68  ? 68  TYR   A CB  1 
ATOM   315  C  CG  . TYR   A 1 47  ? -21.986 -2.026  -30.668 1.00 75.89  ? 68  TYR   A CG  1 
ATOM   316  C  CD1 . TYR   A 1 47  ? -22.332 -0.739  -31.064 1.00 74.92  ? 68  TYR   A CD1 1 
ATOM   317  C  CD2 . TYR   A 1 47  ? -23.000 -2.880  -30.255 1.00 76.43  ? 68  TYR   A CD2 1 
ATOM   318  C  CE1 . TYR   A 1 47  ? -23.649 -0.319  -31.053 1.00 75.14  ? 68  TYR   A CE1 1 
ATOM   319  C  CE2 . TYR   A 1 47  ? -24.319 -2.467  -30.238 1.00 75.81  ? 68  TYR   A CE2 1 
ATOM   320  C  CZ  . TYR   A 1 47  ? -24.637 -1.187  -30.639 1.00 75.00  ? 68  TYR   A CZ  1 
ATOM   321  O  OH  . TYR   A 1 47  ? -25.949 -0.774  -30.624 1.00 75.91  ? 68  TYR   A OH  1 
ATOM   322  N  N   . GLY   A 1 48  ? -17.810 -3.697  -32.458 1.00 78.28  ? 69  GLY   A N   1 
ATOM   323  C  CA  . GLY   A 1 48  ? -16.364 -3.760  -32.513 1.00 78.67  ? 69  GLY   A CA  1 
ATOM   324  C  C   . GLY   A 1 48  ? -15.716 -4.507  -31.366 1.00 79.79  ? 69  GLY   A C   1 
ATOM   325  O  O   . GLY   A 1 48  ? -16.246 -5.513  -30.887 1.00 80.13  ? 69  GLY   A O   1 
ATOM   326  N  N   . LYS   A 1 49  ? -14.559 -4.015  -30.918 1.00 77.02  ? 70  LYS   A N   1 
ATOM   327  C  CA  . LYS   A 1 49  ? -13.776 -4.700  -29.898 1.00 74.49  ? 70  LYS   A CA  1 
ATOM   328  C  C   . LYS   A 1 49  ? -14.174 -4.319  -28.479 1.00 75.51  ? 70  LYS   A C   1 
ATOM   329  O  O   . LYS   A 1 49  ? -14.011 -5.132  -27.561 1.00 77.57  ? 70  LYS   A O   1 
ATOM   330  C  CB  . LYS   A 1 49  ? -12.286 -4.414  -30.103 1.00 74.67  ? 70  LYS   A CB  1 
ATOM   331  N  N   . VAL   A 1 50  ? -14.676 -3.104  -28.271 1.00 73.21  ? 71  VAL   A N   1 
ATOM   332  C  CA  . VAL   A 1 50  ? -15.094 -2.631  -26.956 1.00 71.14  ? 71  VAL   A CA  1 
ATOM   333  C  C   . VAL   A 1 50  ? -16.440 -1.934  -27.100 1.00 73.90  ? 71  VAL   A C   1 
ATOM   334  O  O   . VAL   A 1 50  ? -16.607 -1.074  -27.973 1.00 75.56  ? 71  VAL   A O   1 
ATOM   335  C  CB  . VAL   A 1 50  ? -14.053 -1.682  -26.332 1.00 71.41  ? 71  VAL   A CB  1 
ATOM   336  C  CG1 . VAL   A 1 50  ? -14.656 -0.914  -25.168 1.00 69.86  ? 71  VAL   A CG1 1 
ATOM   337  C  CG2 . VAL   A 1 50  ? -12.830 -2.464  -25.874 1.00 75.73  ? 71  VAL   A CG2 1 
ATOM   338  N  N   . TRP   A 1 51  ? -17.395 -2.302  -26.248 1.00 71.95  ? 72  TRP   A N   1 
ATOM   339  C  CA  . TRP   A 1 51  ? -18.714 -1.685  -26.258 1.00 69.77  ? 72  TRP   A CA  1 
ATOM   340  C  C   . TRP   A 1 51  ? -19.280 -1.716  -24.846 1.00 70.05  ? 72  TRP   A C   1 
ATOM   341  O  O   . TRP   A 1 51  ? -18.785 -2.431  -23.970 1.00 67.26  ? 72  TRP   A O   1 
ATOM   342  C  CB  . TRP   A 1 51  ? -19.657 -2.383  -27.242 1.00 71.96  ? 72  TRP   A CB  1 
ATOM   343  C  CG  . TRP   A 1 51  ? -20.095 -3.748  -26.804 1.00 74.01  ? 72  TRP   A CG  1 
ATOM   344  C  CD1 . TRP   A 1 51  ? -21.213 -4.058  -26.085 1.00 72.46  ? 72  TRP   A CD1 1 
ATOM   345  C  CD2 . TRP   A 1 51  ? -19.426 -4.988  -27.061 1.00 75.76  ? 72  TRP   A CD2 1 
ATOM   346  N  NE1 . TRP   A 1 51  ? -21.279 -5.414  -25.876 1.00 74.82  ? 72  TRP   A NE1 1 
ATOM   347  C  CE2 . TRP   A 1 51  ? -20.195 -6.007  -26.466 1.00 75.35  ? 72  TRP   A CE2 1 
ATOM   348  C  CE3 . TRP   A 1 51  ? -18.251 -5.335  -27.736 1.00 75.55  ? 72  TRP   A CE3 1 
ATOM   349  C  CZ2 . TRP   A 1 51  ? -19.828 -7.350  -26.525 1.00 74.60  ? 72  TRP   A CZ2 1 
ATOM   350  C  CZ3 . TRP   A 1 51  ? -17.888 -6.669  -27.793 1.00 75.12  ? 72  TRP   A CZ3 1 
ATOM   351  C  CH2 . TRP   A 1 51  ? -18.674 -7.660  -27.192 1.00 74.92  ? 72  TRP   A CH2 1 
ATOM   352  N  N   . GLY   A 1 52  ? -20.335 -0.928  -24.632 1.00 72.58  ? 73  GLY   A N   1 
ATOM   353  C  CA  . GLY   A 1 52  ? -20.936 -0.810  -23.325 1.00 67.43  ? 73  GLY   A CA  1 
ATOM   354  C  C   . GLY   A 1 52  ? -22.446 -0.943  -23.384 1.00 67.25  ? 73  GLY   A C   1 
ATOM   355  O  O   . GLY   A 1 52  ? -23.070 -0.811  -24.437 1.00 67.62  ? 73  GLY   A O   1 
ATOM   356  N  N   . PHE   A 1 53  ? -23.023 -1.215  -22.215 1.00 63.22  ? 74  PHE   A N   1 
ATOM   357  C  CA  . PHE   A 1 53  ? -24.467 -1.331  -22.057 1.00 59.76  ? 74  PHE   A CA  1 
ATOM   358  C  C   . PHE   A 1 53  ? -24.793 -1.169  -20.580 1.00 58.89  ? 74  PHE   A C   1 
ATOM   359  O  O   . PHE   A 1 53  ? -23.901 -1.083  -19.733 1.00 59.67  ? 74  PHE   A O   1 
ATOM   360  C  CB  . PHE   A 1 53  ? -24.994 -2.661  -22.610 1.00 62.09  ? 74  PHE   A CB  1 
ATOM   361  C  CG  . PHE   A 1 53  ? -24.440 -3.876  -21.917 1.00 65.03  ? 74  PHE   A CG  1 
ATOM   362  C  CD1 . PHE   A 1 53  ? -23.167 -4.337  -22.209 1.00 62.17  ? 74  PHE   A CD1 1 
ATOM   363  C  CD2 . PHE   A 1 53  ? -25.201 -4.565  -20.987 1.00 61.25  ? 74  PHE   A CD2 1 
ATOM   364  C  CE1 . PHE   A 1 53  ? -22.659 -5.454  -21.576 1.00 61.29  ? 74  PHE   A CE1 1 
ATOM   365  C  CE2 . PHE   A 1 53  ? -24.697 -5.683  -20.353 1.00 59.40  ? 74  PHE   A CE2 1 
ATOM   366  C  CZ  . PHE   A 1 53  ? -23.426 -6.129  -20.651 1.00 60.48  ? 74  PHE   A CZ  1 
ATOM   367  N  N   . TYR   A 1 54  ? -26.089 -1.125  -20.277 1.00 60.40  ? 75  TYR   A N   1 
ATOM   368  C  CA  . TYR   A 1 54  ? -26.559 -0.848  -18.926 1.00 58.71  ? 75  TYR   A CA  1 
ATOM   369  C  C   . TYR   A 1 54  ? -27.524 -1.934  -18.470 1.00 57.02  ? 75  TYR   A C   1 
ATOM   370  O  O   . TYR   A 1 54  ? -28.502 -2.232  -19.165 1.00 60.66  ? 75  TYR   A O   1 
ATOM   371  C  CB  . TYR   A 1 54  ? -27.233 0.528   -18.855 1.00 59.69  ? 75  TYR   A CB  1 
ATOM   372  C  CG  . TYR   A 1 54  ? -26.322 1.682   -19.224 1.00 61.76  ? 75  TYR   A CG  1 
ATOM   373  C  CD1 . TYR   A 1 54  ? -26.178 2.085   -20.546 1.00 61.50  ? 75  TYR   A CD1 1 
ATOM   374  C  CD2 . TYR   A 1 54  ? -25.612 2.371   -18.249 1.00 63.64  ? 75  TYR   A CD2 1 
ATOM   375  C  CE1 . TYR   A 1 54  ? -25.348 3.142   -20.886 1.00 65.52  ? 75  TYR   A CE1 1 
ATOM   376  C  CE2 . TYR   A 1 54  ? -24.779 3.429   -18.579 1.00 66.56  ? 75  TYR   A CE2 1 
ATOM   377  C  CZ  . TYR   A 1 54  ? -24.652 3.810   -19.899 1.00 68.98  ? 75  TYR   A CZ  1 
ATOM   378  O  OH  . TYR   A 1 54  ? -23.826 4.860   -20.231 1.00 71.51  ? 75  TYR   A OH  1 
ATOM   379  N  N   . ASP   A 1 55  ? -27.246 -2.519  -17.303 1.00 57.13  ? 76  ASP   A N   1 
ATOM   380  C  CA  . ASP   A 1 55  ? -28.148 -3.468  -16.646 1.00 57.34  ? 76  ASP   A CA  1 
ATOM   381  C  C   . ASP   A 1 55  ? -28.965 -2.671  -15.635 1.00 57.86  ? 76  ASP   A C   1 
ATOM   382  O  O   . ASP   A 1 55  ? -28.574 -2.511  -14.478 1.00 58.34  ? 76  ASP   A O   1 
ATOM   383  C  CB  . ASP   A 1 55  ? -27.372 -4.597  -15.977 1.00 56.19  ? 76  ASP   A CB  1 
ATOM   384  C  CG  . ASP   A 1 55  ? -26.803 -5.586  -16.972 1.00 56.76  ? 76  ASP   A CG  1 
ATOM   385  O  OD1 . ASP   A 1 55  ? -27.402 -5.746  -18.056 1.00 55.58  ? 76  ASP   A OD1 1 
ATOM   386  O  OD2 . ASP   A 1 55  ? -25.762 -6.206  -16.670 1.00 57.64  ? 76  ASP   A OD2 1 
ATOM   387  N  N   . GLY   A 1 56  ? -30.119 -2.180  -16.076 1.00 57.79  ? 77  GLY   A N   1 
ATOM   388  C  CA  . GLY   A 1 56  ? -30.840 -1.197  -15.296 1.00 62.38  ? 77  GLY   A CA  1 
ATOM   389  C  C   . GLY   A 1 56  ? -30.087 0.116   -15.320 1.00 60.07  ? 77  GLY   A C   1 
ATOM   390  O  O   . GLY   A 1 56  ? -29.957 0.738   -16.378 1.00 57.40  ? 77  GLY   A O   1 
ATOM   391  N  N   . GLN   A 1 57  ? -29.575 0.546   -14.169 1.00 59.97  ? 78  GLN   A N   1 
ATOM   392  C  CA  . GLN   A 1 57  ? -28.710 1.714   -14.093 1.00 61.27  ? 78  GLN   A CA  1 
ATOM   393  C  C   . GLN   A 1 57  ? -27.237 1.340   -13.975 1.00 60.20  ? 78  GLN   A C   1 
ATOM   394  O  O   . GLN   A 1 57  ? -26.397 2.223   -13.772 1.00 60.36  ? 78  GLN   A O   1 
ATOM   395  C  CB  . GLN   A 1 57  ? -29.119 2.597   -12.912 1.00 64.25  ? 78  GLN   A CB  1 
ATOM   396  C  CG  . GLN   A 1 57  ? -30.586 3.000   -12.906 1.00 65.12  ? 78  GLN   A CG  1 
ATOM   397  C  CD  . GLN   A 1 57  ? -30.886 4.148   -13.849 1.00 68.49  ? 78  GLN   A CD  1 
ATOM   398  O  OE1 . GLN   A 1 57  ? -30.045 5.018   -14.072 1.00 75.54  ? 78  GLN   A OE1 1 
ATOM   399  N  NE2 . GLN   A 1 57  ? -32.090 4.155   -14.408 1.00 65.49  ? 78  GLN   A NE2 1 
ATOM   400  N  N   . GLN   A 1 58  ? -26.905 0.054   -14.103 1.00 59.64  ? 79  GLN   A N   1 
ATOM   401  C  CA  . GLN   A 1 58  ? -25.546 -0.419  -13.871 1.00 58.60  ? 79  GLN   A CA  1 
ATOM   402  C  C   . GLN   A 1 58  ? -24.753 -0.387  -15.172 1.00 61.24  ? 79  GLN   A C   1 
ATOM   403  O  O   . GLN   A 1 58  ? -25.076 -1.146  -16.099 1.00 59.13  ? 79  GLN   A O   1 
ATOM   404  C  CB  . GLN   A 1 58  ? -25.566 -1.830  -13.301 1.00 57.25  ? 79  GLN   A CB  1 
ATOM   405  C  CG  . GLN   A 1 58  ? -24.195 -2.476  -13.195 1.00 60.05  ? 79  GLN   A CG  1 
ATOM   406  C  CD  . GLN   A 1 58  ? -23.286 -1.752  -12.224 1.00 59.10  ? 79  GLN   A CD  1 
ATOM   407  O  OE1 . GLN   A 1 58  ? -22.288 -1.152  -12.620 1.00 58.55  ? 79  GLN   A OE1 1 
ATOM   408  N  NE2 . GLN   A 1 58  ? -23.626 -1.809  -10.941 1.00 56.80  ? 79  GLN   A NE2 1 
ATOM   409  N  N   . PRO   A 1 59  ? -23.717 0.442   -15.287 1.00 61.87  ? 80  PRO   A N   1 
ATOM   410  C  CA  . PRO   A 1 59  ? -22.905 0.435   -16.510 1.00 61.65  ? 80  PRO   A CA  1 
ATOM   411  C  C   . PRO   A 1 59  ? -22.043 -0.816  -16.580 1.00 61.00  ? 80  PRO   A C   1 
ATOM   412  O  O   . PRO   A 1 59  ? -21.410 -1.210  -15.597 1.00 62.25  ? 80  PRO   A O   1 
ATOM   413  C  CB  . PRO   A 1 59  ? -22.042 1.699   -16.378 1.00 60.63  ? 80  PRO   A CB  1 
ATOM   414  C  CG  . PRO   A 1 59  ? -22.618 2.472   -15.220 1.00 61.39  ? 80  PRO   A CG  1 
ATOM   415  C  CD  . PRO   A 1 59  ? -23.262 1.462   -14.331 1.00 59.54  ? 80  PRO   A CD  1 
ATOM   416  N  N   . VAL   A 1 60  ? -22.028 -1.447  -17.751 1.00 60.01  ? 81  VAL   A N   1 
ATOM   417  C  CA  . VAL   A 1 60  ? -21.204 -2.624  -17.997 1.00 63.23  ? 81  VAL   A CA  1 
ATOM   418  C  C   . VAL   A 1 60  ? -20.371 -2.375  -19.245 1.00 64.49  ? 81  VAL   A C   1 
ATOM   419  O  O   . VAL   A 1 60  ? -20.912 -2.014  -20.296 1.00 64.61  ? 81  VAL   A O   1 
ATOM   420  C  CB  . VAL   A 1 60  ? -22.047 -3.904  -18.163 1.00 62.14  ? 81  VAL   A CB  1 
ATOM   421  C  CG1 . VAL   A 1 60  ? -21.138 -5.118  -18.267 1.00 60.12  ? 81  VAL   A CG1 1 
ATOM   422  C  CG2 . VAL   A 1 60  ? -23.019 -4.060  -17.005 1.00 61.69  ? 81  VAL   A CG2 1 
ATOM   423  N  N   . LEU   A 1 61  ? -19.060 -2.567  -19.130 1.00 66.06  ? 82  LEU   A N   1 
ATOM   424  C  CA  . LEU   A 1 61  ? -18.140 -2.435  -20.249 1.00 63.08  ? 82  LEU   A CA  1 
ATOM   425  C  C   . LEU   A 1 61  ? -17.642 -3.815  -20.654 1.00 63.67  ? 82  LEU   A C   1 
ATOM   426  O  O   . LEU   A 1 61  ? -17.130 -4.565  -19.817 1.00 63.68  ? 82  LEU   A O   1 
ATOM   427  C  CB  . LEU   A 1 61  ? -16.959 -1.532  -19.887 1.00 62.66  ? 82  LEU   A CB  1 
ATOM   428  C  CG  . LEU   A 1 61  ? -15.968 -1.283  -21.025 1.00 64.37  ? 82  LEU   A CG  1 
ATOM   429  C  CD1 . LEU   A 1 61  ? -16.678 -0.641  -22.204 1.00 66.94  ? 82  LEU   A CD1 1 
ATOM   430  C  CD2 . LEU   A 1 61  ? -14.805 -0.423  -20.565 1.00 66.81  ? 82  LEU   A CD2 1 
ATOM   431  N  N   . ALA   A 1 62  ? -17.797 -4.145  -21.931 1.00 63.53  ? 83  ALA   A N   1 
ATOM   432  C  CA  . ALA   A 1 62  ? -17.324 -5.408  -22.481 1.00 65.66  ? 83  ALA   A CA  1 
ATOM   433  C  C   . ALA   A 1 62  ? -16.004 -5.183  -23.204 1.00 69.29  ? 83  ALA   A C   1 
ATOM   434  O  O   . ALA   A 1 62  ? -15.852 -4.211  -23.950 1.00 71.79  ? 83  ALA   A O   1 
ATOM   435  C  CB  . ALA   A 1 62  ? -18.353 -6.013  -23.436 1.00 65.12  ? 83  ALA   A CB  1 
ATOM   436  N  N   . ILE   A 1 63  ? -15.044 -6.075  -22.964 1.00 68.46  ? 84  ILE   A N   1 
ATOM   437  C  CA  . ILE   A 1 63  ? -13.713 -5.980  -23.551 1.00 71.02  ? 84  ILE   A CA  1 
ATOM   438  C  C   . ILE   A 1 63  ? -13.372 -7.309  -24.214 1.00 73.20  ? 84  ILE   A C   1 
ATOM   439  O  O   . ILE   A 1 63  ? -13.728 -8.379  -23.706 1.00 71.14  ? 84  ILE   A O   1 
ATOM   440  C  CB  . ILE   A 1 63  ? -12.644 -5.595  -22.502 1.00 69.85  ? 84  ILE   A CB  1 
ATOM   441  C  CG1 . ILE   A 1 63  ? -12.436 -6.718  -21.483 1.00 70.09  ? 84  ILE   A CG1 1 
ATOM   442  C  CG2 . ILE   A 1 63  ? -13.036 -4.307  -21.786 1.00 69.38  ? 84  ILE   A CG2 1 
ATOM   443  C  CD1 . ILE   A 1 63  ? -11.364 -6.416  -20.456 1.00 72.31  ? 84  ILE   A CD1 1 
ATOM   444  N  N   . THR   A 1 64  ? -12.703 -7.239  -25.367 1.00 77.12  ? 85  THR   A N   1 
ATOM   445  C  CA  . THR   A 1 64  ? -12.309 -8.431  -26.104 1.00 75.31  ? 85  THR   A CA  1 
ATOM   446  C  C   . THR   A 1 64  ? -10.819 -8.492  -26.414 1.00 76.29  ? 85  THR   A C   1 
ATOM   447  O  O   . THR   A 1 64  ? -10.359 -9.506  -26.953 1.00 75.79  ? 85  THR   A O   1 
ATOM   448  C  CB  . THR   A 1 64  ? -13.094 -8.539  -27.422 1.00 74.11  ? 85  THR   A CB  1 
ATOM   449  O  OG1 . THR   A 1 64  ? -12.697 -7.487  -28.308 1.00 74.68  ? 85  THR   A OG1 1 
ATOM   450  C  CG2 . THR   A 1 64  ? -14.592 -8.450  -27.168 1.00 72.39  ? 85  THR   A CG2 1 
ATOM   451  N  N   . ASP   A 1 65  ? -10.055 -7.452  -26.106 1.00 77.16  ? 86  ASP   A N   1 
ATOM   452  C  CA  . ASP   A 1 65  ? -8.619  -7.496  -26.358 1.00 80.75  ? 86  ASP   A CA  1 
ATOM   453  C  C   . ASP   A 1 65  ? -7.957  -8.424  -25.346 1.00 81.49  ? 86  ASP   A C   1 
ATOM   454  O  O   . ASP   A 1 65  ? -8.134  -8.239  -24.136 1.00 80.58  ? 86  ASP   A O   1 
ATOM   455  C  CB  . ASP   A 1 65  ? -8.007  -6.097  -26.284 1.00 83.30  ? 86  ASP   A CB  1 
ATOM   456  C  CG  . ASP   A 1 65  ? -6.574  -6.054  -26.795 1.00 84.35  ? 86  ASP   A CG  1 
ATOM   457  O  OD1 . ASP   A 1 65  ? -5.733  -6.839  -26.308 1.00 82.29  ? 86  ASP   A OD1 1 
ATOM   458  O  OD2 . ASP   A 1 65  ? -6.289  -5.235  -27.693 1.00 86.25  ? 86  ASP   A OD2 1 
ATOM   459  N  N   . PRO   A 1 66  ? -7.201  -9.430  -25.795 1.00 80.92  ? 87  PRO   A N   1 
ATOM   460  C  CA  . PRO   A 1 66  ? -6.561  -10.348 -24.837 1.00 77.15  ? 87  PRO   A CA  1 
ATOM   461  C  C   . PRO   A 1 66  ? -5.645  -9.649  -23.848 1.00 78.79  ? 87  PRO   A C   1 
ATOM   462  O  O   . PRO   A 1 66  ? -5.592  -10.041 -22.675 1.00 78.46  ? 87  PRO   A O   1 
ATOM   463  C  CB  . PRO   A 1 66  ? -5.787  -11.314 -25.746 1.00 77.52  ? 87  PRO   A CB  1 
ATOM   464  C  CG  . PRO   A 1 66  ? -6.480  -11.230 -27.071 1.00 80.10  ? 87  PRO   A CG  1 
ATOM   465  C  CD  . PRO   A 1 66  ? -6.953  -9.817  -27.194 1.00 79.46  ? 87  PRO   A CD  1 
ATOM   466  N  N   . ASP   A 1 67  ? -4.920  -8.618  -24.289 1.00 80.31  ? 88  ASP   A N   1 
ATOM   467  C  CA  . ASP   A 1 67  ? -4.056  -7.878  -23.375 1.00 80.76  ? 88  ASP   A CA  1 
ATOM   468  C  C   . ASP   A 1 67  ? -4.870  -7.137  -22.321 1.00 79.96  ? 88  ASP   A C   1 
ATOM   469  O  O   . ASP   A 1 67  ? -4.493  -7.109  -21.143 1.00 79.18  ? 88  ASP   A O   1 
ATOM   470  C  CB  . ASP   A 1 67  ? -3.177  -6.905  -24.160 1.00 84.67  ? 88  ASP   A CB  1 
ATOM   471  C  CG  . ASP   A 1 67  ? -2.279  -7.609  -25.158 1.00 86.48  ? 88  ASP   A CG  1 
ATOM   472  O  OD1 . ASP   A 1 67  ? -1.801  -8.720  -24.847 1.00 84.95  ? 88  ASP   A OD1 1 
ATOM   473  O  OD2 . ASP   A 1 67  ? -2.055  -7.053  -26.254 1.00 90.79  ? 88  ASP   A OD2 1 
ATOM   474  N  N   . MET   A 1 68  ? -5.985  -6.527  -22.728 1.00 81.07  ? 89  MET   A N   1 
ATOM   475  C  CA  . MET   A 1 68  ? -6.858  -5.859  -21.768 1.00 80.81  ? 89  MET   A CA  1 
ATOM   476  C  C   . MET   A 1 68  ? -7.460  -6.859  -20.790 1.00 76.72  ? 89  MET   A C   1 
ATOM   477  O  O   . MET   A 1 68  ? -7.585  -6.573  -19.594 1.00 73.49  ? 89  MET   A O   1 
ATOM   478  C  CB  . MET   A 1 68  ? -7.957  -5.097  -22.509 1.00 80.16  ? 89  MET   A CB  1 
ATOM   479  C  CG  . MET   A 1 68  ? -8.225  -3.700  -21.977 1.00 82.48  ? 89  MET   A CG  1 
ATOM   480  S  SD  . MET   A 1 68  ? -9.366  -2.785  -23.031 1.00 86.96  ? 89  MET   A SD  1 
ATOM   481  C  CE  . MET   A 1 68  ? -8.503  -2.851  -24.600 1.00 84.18  ? 89  MET   A CE  1 
ATOM   482  N  N   . ILE   A 1 69  ? -7.839  -8.039  -21.287 1.00 76.95  ? 90  ILE   A N   1 
ATOM   483  C  CA  . ILE   A 1 69  ? -8.391  -9.082  -20.426 1.00 74.55  ? 90  ILE   A CA  1 
ATOM   484  C  C   . ILE   A 1 69  ? -7.366  -9.505  -19.380 1.00 75.82  ? 90  ILE   A C   1 
ATOM   485  O  O   . ILE   A 1 69  ? -7.679  -9.626  -18.189 1.00 75.34  ? 90  ILE   A O   1 
ATOM   486  C  CB  . ILE   A 1 69  ? -8.860  -10.279 -21.272 1.00 73.01  ? 90  ILE   A CB  1 
ATOM   487  C  CG1 . ILE   A 1 69  ? -10.041 -9.881  -22.160 1.00 73.72  ? 90  ILE   A CG1 1 
ATOM   488  C  CG2 . ILE   A 1 69  ? -9.231  -11.453 -20.381 1.00 72.50  ? 90  ILE   A CG2 1 
ATOM   489  C  CD1 . ILE   A 1 69  ? -10.456 -10.960 -23.135 1.00 71.44  ? 90  ILE   A CD1 1 
ATOM   490  N  N   . LYS   A 1 70  ? -6.121  -9.728  -19.811 1.00 76.16  ? 91  LYS   A N   1 
ATOM   491  C  CA  . LYS   A 1 70  ? -5.074  -10.128 -18.875 1.00 76.25  ? 91  LYS   A CA  1 
ATOM   492  C  C   . LYS   A 1 70  ? -4.788  -9.035  -17.856 1.00 74.91  ? 91  LYS   A C   1 
ATOM   493  O  O   . LYS   A 1 70  ? -4.461  -9.333  -16.701 1.00 73.21  ? 91  LYS   A O   1 
ATOM   494  C  CB  . LYS   A 1 70  ? -3.798  -10.492 -19.634 1.00 78.88  ? 91  LYS   A CB  1 
ATOM   495  C  CG  . LYS   A 1 70  ? -2.666  -10.977 -18.738 1.00 80.47  ? 91  LYS   A CG  1 
ATOM   496  C  CD  . LYS   A 1 70  ? -1.359  -11.113 -19.501 1.00 79.71  ? 91  LYS   A CD  1 
ATOM   497  C  CE  . LYS   A 1 70  ? -0.210  -11.438 -18.559 1.00 83.64  ? 91  LYS   A CE  1 
ATOM   498  N  NZ  . LYS   A 1 70  ? 1.098   -11.499 -19.267 1.00 86.45  ? 91  LYS   A NZ  1 
ATOM   499  N  N   . THR   A 1 71  ? -4.899  -7.768  -18.261 1.00 73.89  ? 92  THR   A N   1 
ATOM   500  C  CA  . THR   A 1 71  ? -4.726  -6.675  -17.310 1.00 75.14  ? 92  THR   A CA  1 
ATOM   501  C  C   . THR   A 1 71  ? -5.802  -6.714  -16.232 1.00 76.13  ? 92  THR   A C   1 
ATOM   502  O  O   . THR   A 1 71  ? -5.522  -6.470  -15.052 1.00 77.36  ? 92  THR   A O   1 
ATOM   503  C  CB  . THR   A 1 71  ? -4.748  -5.332  -18.040 1.00 76.10  ? 92  THR   A CB  1 
ATOM   504  O  OG1 . THR   A 1 71  ? -3.902  -5.400  -19.195 1.00 75.49  ? 92  THR   A OG1 1 
ATOM   505  C  CG2 . THR   A 1 71  ? -4.249  -4.226  -17.125 1.00 72.65  ? 92  THR   A CG2 1 
ATOM   506  N  N   . VAL   A 1 72  ? -7.040  -7.021  -16.620 1.00 74.21  ? 93  VAL   A N   1 
ATOM   507  C  CA  . VAL   A 1 72  ? -8.143  -7.052  -15.666 1.00 72.88  ? 93  VAL   A CA  1 
ATOM   508  C  C   . VAL   A 1 72  ? -8.099  -8.316  -14.815 1.00 74.03  ? 93  VAL   A C   1 
ATOM   509  O  O   . VAL   A 1 72  ? -8.271  -8.259  -13.592 1.00 74.32  ? 93  VAL   A O   1 
ATOM   510  C  CB  . VAL   A 1 72  ? -9.483  -6.916  -16.412 1.00 71.89  ? 93  VAL   A CB  1 
ATOM   511  C  CG1 . VAL   A 1 72  ? -10.647 -7.058  -15.447 1.00 70.80  ? 93  VAL   A CG1 1 
ATOM   512  C  CG2 . VAL   A 1 72  ? -9.550  -5.583  -17.139 1.00 75.09  ? 93  VAL   A CG2 1 
ATOM   513  N  N   . LEU   A 1 73  ? -7.870  -9.472  -15.439 1.00 72.81  ? 94  LEU   A N   1 
ATOM   514  C  CA  . LEU   A 1 73  ? -7.963  -10.733 -14.712 1.00 72.55  ? 94  LEU   A CA  1 
ATOM   515  C  C   . LEU   A 1 73  ? -6.680  -11.080 -13.967 1.00 73.79  ? 94  LEU   A C   1 
ATOM   516  O  O   . LEU   A 1 73  ? -6.743  -11.710 -12.906 1.00 76.54  ? 94  LEU   A O   1 
ATOM   517  C  CB  . LEU   A 1 73  ? -8.326  -11.869 -15.671 1.00 72.35  ? 94  LEU   A CB  1 
ATOM   518  C  CG  . LEU   A 1 73  ? -9.669  -11.754 -16.396 1.00 72.62  ? 94  LEU   A CG  1 
ATOM   519  C  CD1 . LEU   A 1 73  ? -9.968  -13.020 -17.182 1.00 69.30  ? 94  LEU   A CD1 1 
ATOM   520  C  CD2 . LEU   A 1 73  ? -10.788 -11.458 -15.411 1.00 69.79  ? 94  LEU   A CD2 1 
ATOM   521  N  N   . VAL   A 1 74  ? -5.519  -10.681 -14.486 1.00 76.83  ? 95  VAL   A N   1 
ATOM   522  C  CA  . VAL   A 1 74  ? -4.248  -11.120 -13.916 1.00 78.69  ? 95  VAL   A CA  1 
ATOM   523  C  C   . VAL   A 1 74  ? -3.459  -9.941  -13.361 1.00 74.98  ? 95  VAL   A C   1 
ATOM   524  O  O   . VAL   A 1 74  ? -3.098  -9.925  -12.179 1.00 72.88  ? 95  VAL   A O   1 
ATOM   525  C  CB  . VAL   A 1 74  ? -3.413  -11.888 -14.957 1.00 79.52  ? 95  VAL   A CB  1 
ATOM   526  C  CG1 . VAL   A 1 74  ? -2.072  -12.294 -14.364 1.00 78.61  ? 95  VAL   A CG1 1 
ATOM   527  C  CG2 . VAL   A 1 74  ? -4.173  -13.109 -15.454 1.00 75.93  ? 95  VAL   A CG2 1 
ATOM   528  N  N   . LYS   A 1 75  ? -3.184  -8.949  -14.211 1.00 74.55  ? 96  LYS   A N   1 
ATOM   529  C  CA  . LYS   A 1 75  ? -2.262  -7.879  -13.837 1.00 76.84  ? 96  LYS   A CA  1 
ATOM   530  C  C   . LYS   A 1 75  ? -2.808  -7.048  -12.681 1.00 76.67  ? 96  LYS   A C   1 
ATOM   531  O  O   . LYS   A 1 75  ? -2.205  -6.984  -11.604 1.00 75.94  ? 96  LYS   A O   1 
ATOM   532  C  CB  . LYS   A 1 75  ? -1.972  -6.992  -15.049 1.00 73.03  ? 96  LYS   A CB  1 
ATOM   533  N  N   . GLU   A 1 76  ? -3.961  -6.414  -12.882 1.00 77.47  ? 97  GLU   A N   1 
ATOM   534  C  CA  . GLU   A 1 76  ? -4.523  -5.477  -11.910 1.00 79.47  ? 97  GLU   A CA  1 
ATOM   535  C  C   . GLU   A 1 76  ? -5.652  -6.101  -11.100 1.00 78.20  ? 97  GLU   A C   1 
ATOM   536  O  O   . GLU   A 1 76  ? -6.654  -5.444  -10.806 1.00 79.14  ? 97  GLU   A O   1 
ATOM   537  C  CB  . GLU   A 1 76  ? -5.004  -4.214  -12.617 1.00 78.99  ? 97  GLU   A CB  1 
ATOM   538  C  CG  . GLU   A 1 76  ? -3.918  -3.463  -13.378 1.00 80.32  ? 97  GLU   A CG  1 
ATOM   539  C  CD  . GLU   A 1 76  ? -3.005  -2.656  -12.472 1.00 85.33  ? 97  GLU   A CD  1 
ATOM   540  O  OE1 . GLU   A 1 76  ? -3.265  -2.602  -11.250 1.00 82.64  ? 97  GLU   A OE1 1 
ATOM   541  O  OE2 . GLU   A 1 76  ? -2.028  -2.069  -12.983 1.00 86.60  ? 97  GLU   A OE2 1 
ATOM   542  N  N   . CYS   A 1 77  ? -5.515  -7.378  -10.735 1.00 78.00  ? 98  CYS   A N   1 
ATOM   543  C  CA  . CYS   A 1 77  ? -6.572  -8.058  -9.992  1.00 75.44  ? 98  CYS   A CA  1 
ATOM   544  C  C   . CYS   A 1 77  ? -6.665  -7.541  -8.560  1.00 77.10  ? 98  CYS   A C   1 
ATOM   545  O  O   . CYS   A 1 77  ? -7.736  -7.117  -8.111  1.00 78.07  ? 98  CYS   A O   1 
ATOM   546  C  CB  . CYS   A 1 77  ? -6.329  -9.567  -10.007 1.00 74.92  ? 98  CYS   A CB  1 
ATOM   547  S  SG  . CYS   A 1 77  ? -7.566  -10.539 -9.118  1.00 74.45  ? 98  CYS   A SG  1 
ATOM   548  N  N   . TYR   A 1 78  ? -5.552  -7.566  -7.824  1.00 80.08  ? 99  TYR   A N   1 
ATOM   549  C  CA  . TYR   A 1 78  ? -5.587  -7.149  -6.426  1.00 79.59  ? 99  TYR   A CA  1 
ATOM   550  C  C   . TYR   A 1 78  ? -5.787  -5.645  -6.281  1.00 77.94  ? 99  TYR   A C   1 
ATOM   551  O  O   . TYR   A 1 78  ? -6.408  -5.196  -5.311  1.00 75.31  ? 99  TYR   A O   1 
ATOM   552  C  CB  . TYR   A 1 78  ? -4.303  -7.577  -5.713  1.00 78.65  ? 99  TYR   A CB  1 
ATOM   553  C  CG  . TYR   A 1 78  ? -4.125  -9.074  -5.584  1.00 78.53  ? 99  TYR   A CG  1 
ATOM   554  C  CD1 . TYR   A 1 78  ? -3.483  -9.803  -6.577  1.00 78.03  ? 99  TYR   A CD1 1 
ATOM   555  C  CD2 . TYR   A 1 78  ? -4.590  -9.756  -4.466  1.00 77.49  ? 99  TYR   A CD2 1 
ATOM   556  C  CE1 . TYR   A 1 78  ? -3.314  -11.168 -6.465  1.00 80.45  ? 99  TYR   A CE1 1 
ATOM   557  C  CE2 . TYR   A 1 78  ? -4.424  -11.125 -4.343  1.00 79.10  ? 99  TYR   A CE2 1 
ATOM   558  C  CZ  . TYR   A 1 78  ? -3.786  -11.825 -5.347  1.00 81.85  ? 99  TYR   A CZ  1 
ATOM   559  O  OH  . TYR   A 1 78  ? -3.617  -13.186 -5.235  1.00 76.27  ? 99  TYR   A OH  1 
ATOM   560  N  N   . SER   A 1 79  ? -5.271  -4.853  -7.223  1.00 79.24  ? 100 SER   A N   1 
ATOM   561  C  CA  . SER   A 1 79  ? -5.319  -3.402  -7.075  1.00 79.91  ? 100 SER   A CA  1 
ATOM   562  C  C   . SER   A 1 79  ? -6.727  -2.863  -7.303  1.00 81.09  ? 100 SER   A C   1 
ATOM   563  O  O   . SER   A 1 79  ? -7.279  -2.164  -6.446  1.00 81.65  ? 100 SER   A O   1 
ATOM   564  C  CB  . SER   A 1 79  ? -4.324  -2.744  -8.033  1.00 80.03  ? 100 SER   A CB  1 
ATOM   565  O  OG  . SER   A 1 79  ? -4.651  -3.034  -9.379  1.00 82.71  ? 100 SER   A OG  1 
ATOM   566  N  N   . VAL   A 1 80  ? -7.333  -3.188  -8.442  1.00 81.26  ? 101 VAL   A N   1 
ATOM   567  C  CA  . VAL   A 1 80  ? -8.607  -2.574  -8.797  1.00 80.82  ? 101 VAL   A CA  1 
ATOM   568  C  C   . VAL   A 1 80  ? -9.678  -3.620  -9.076  1.00 78.63  ? 101 VAL   A C   1 
ATOM   569  O  O   . VAL   A 1 80  ? -10.748 -3.601  -8.458  1.00 80.20  ? 101 VAL   A O   1 
ATOM   570  C  CB  . VAL   A 1 80  ? -8.444  -1.615  -9.996  1.00 81.30  ? 101 VAL   A CB  1 
ATOM   571  C  CG1 . VAL   A 1 80  ? -7.606  -2.256  -11.087 1.00 80.52  ? 101 VAL   A CG1 1 
ATOM   572  C  CG2 . VAL   A 1 80  ? -9.804  -1.195  -10.540 1.00 79.00  ? 101 VAL   A CG2 1 
ATOM   573  N  N   . PHE   A 1 81  ? -9.406  -4.542  -9.998  1.00 76.66  ? 102 PHE   A N   1 
ATOM   574  C  CA  . PHE   A 1 81  ? -10.418 -5.502  -10.450 1.00 74.79  ? 102 PHE   A CA  1 
ATOM   575  C  C   . PHE   A 1 81  ? -10.430 -6.716  -9.520  1.00 75.72  ? 102 PHE   A C   1 
ATOM   576  O  O   . PHE   A 1 81  ? -10.095 -7.840  -9.896  1.00 78.41  ? 102 PHE   A O   1 
ATOM   577  C  CB  . PHE   A 1 81  ? -10.161 -5.909  -11.897 1.00 74.66  ? 102 PHE   A CB  1 
ATOM   578  C  CG  . PHE   A 1 81  ? -10.182 -4.762  -12.866 1.00 75.76  ? 102 PHE   A CG  1 
ATOM   579  C  CD1 . PHE   A 1 81  ? -11.380 -4.174  -13.238 1.00 73.65  ? 102 PHE   A CD1 1 
ATOM   580  C  CD2 . PHE   A 1 81  ? -9.007  -4.280  -13.418 1.00 78.44  ? 102 PHE   A CD2 1 
ATOM   581  C  CE1 . PHE   A 1 81  ? -11.402 -3.119  -14.132 1.00 74.66  ? 102 PHE   A CE1 1 
ATOM   582  C  CE2 . PHE   A 1 81  ? -9.023  -3.226  -14.314 1.00 78.22  ? 102 PHE   A CE2 1 
ATOM   583  C  CZ  . PHE   A 1 81  ? -10.224 -2.645  -14.672 1.00 76.99  ? 102 PHE   A CZ  1 
ATOM   584  N  N   . THR   A 1 82  ? -10.852 -6.468  -8.280  1.00 74.93  ? 103 THR   A N   1 
ATOM   585  C  CA  . THR   A 1 82  ? -10.778 -7.489  -7.242  1.00 76.41  ? 103 THR   A CA  1 
ATOM   586  C  C   . THR   A 1 82  ? -12.079 -8.259  -7.053  1.00 73.98  ? 103 THR   A C   1 
ATOM   587  O  O   . THR   A 1 82  ? -12.038 -9.459  -6.756  1.00 72.90  ? 103 THR   A O   1 
ATOM   588  C  CB  . THR   A 1 82  ? -10.371 -6.851  -5.908  1.00 76.71  ? 103 THR   A CB  1 
ATOM   589  O  OG1 . THR   A 1 82  ? -9.236  -6.001  -6.118  1.00 79.49  ? 103 THR   A OG1 1 
ATOM   590  C  CG2 . THR   A 1 82  ? -10.002 -7.921  -4.890  1.00 75.76  ? 103 THR   A CG2 1 
ATOM   591  N  N   . ASN   A 1 83  ? -13.228 -7.615  -7.233  1.00 72.02  ? 104 ASN   A N   1 
ATOM   592  C  CA  . ASN   A 1 83  ? -14.506 -8.195  -6.856  1.00 71.17  ? 104 ASN   A CA  1 
ATOM   593  C  C   . ASN   A 1 83  ? -15.417 -8.346  -8.066  1.00 68.13  ? 104 ASN   A C   1 
ATOM   594  O  O   . ASN   A 1 83  ? -15.222 -7.710  -9.105  1.00 66.16  ? 104 ASN   A O   1 
ATOM   595  C  CB  . ASN   A 1 83  ? -15.197 -7.339  -5.791  1.00 73.71  ? 104 ASN   A CB  1 
ATOM   596  C  CG  . ASN   A 1 83  ? -14.286 -7.022  -4.626  1.00 75.08  ? 104 ASN   A CG  1 
ATOM   597  O  OD1 . ASN   A 1 83  ? -13.457 -7.842  -4.233  1.00 74.50  ? 104 ASN   A OD1 1 
ATOM   598  N  ND2 . ASN   A 1 83  ? -14.428 -5.825  -4.072  1.00 78.73  ? 104 ASN   A ND2 1 
ATOM   599  N  N   . ARG   A 1 84  ? -16.418 -9.208  -7.911  1.00 67.72  ? 105 ARG   A N   1 
ATOM   600  C  CA  . ARG   A 1 84  ? -17.434 -9.413  -8.928  1.00 63.62  ? 105 ARG   A CA  1 
ATOM   601  C  C   . ARG   A 1 84  ? -18.642 -8.521  -8.650  1.00 67.31  ? 105 ARG   A C   1 
ATOM   602  O  O   . ARG   A 1 84  ? -18.711 -7.812  -7.643  1.00 67.78  ? 105 ARG   A O   1 
ATOM   603  C  CB  . ARG   A 1 84  ? -17.849 -10.883 -8.986  1.00 62.20  ? 105 ARG   A CB  1 
ATOM   604  C  CG  . ARG   A 1 84  ? -16.764 -11.822 -9.478  1.00 63.92  ? 105 ARG   A CG  1 
ATOM   605  C  CD  . ARG   A 1 84  ? -17.295 -13.237 -9.632  1.00 62.91  ? 105 ARG   A CD  1 
ATOM   606  N  NE  . ARG   A 1 84  ? -16.268 -14.147 -10.123 1.00 64.98  ? 105 ARG   A NE  1 
ATOM   607  C  CZ  . ARG   A 1 84  ? -15.468 -14.862 -9.344  1.00 64.46  ? 105 ARG   A CZ  1 
ATOM   608  N  NH1 . ARG   A 1 84  ? -15.554 -14.802 -8.025  1.00 65.34  ? 105 ARG   A NH1 1 
ATOM   609  N  NH2 . ARG   A 1 84  ? -14.559 -15.656 -9.902  1.00 62.67  ? 105 ARG   A NH2 1 
ATOM   610  N  N   . ARG   A 1 85  ? -19.605 -8.558  -9.558  1.00 66.57  ? 106 ARG   A N   1 
ATOM   611  C  CA  . ARG   A 1 85  ? -20.828 -7.788  -9.381  1.00 65.09  ? 106 ARG   A CA  1 
ATOM   612  C  C   . ARG   A 1 85  ? -21.698 -8.429  -8.305  1.00 67.82  ? 106 ARG   A C   1 
ATOM   613  O  O   . ARG   A 1 85  ? -21.963 -9.634  -8.369  1.00 66.53  ? 106 ARG   A O   1 
ATOM   614  C  CB  . ARG   A 1 85  ? -21.592 -7.696  -10.701 1.00 64.30  ? 106 ARG   A CB  1 
ATOM   615  C  CG  . ARG   A 1 85  ? -23.064 -7.344  -10.548 1.00 63.56  ? 106 ARG   A CG  1 
ATOM   616  C  CD  . ARG   A 1 85  ? -23.658 -6.811  -11.844 1.00 64.68  ? 106 ARG   A CD  1 
ATOM   617  N  NE  . ARG   A 1 85  ? -23.405 -7.689  -12.980 1.00 64.54  ? 106 ARG   A NE  1 
ATOM   618  C  CZ  . ARG   A 1 85  ? -23.949 -7.535  -14.180 1.00 65.57  ? 106 ARG   A CZ  1 
ATOM   619  N  NH1 . ARG   A 1 85  ? -24.797 -6.551  -14.433 1.00 62.49  ? 106 ARG   A NH1 1 
ATOM   620  N  NH2 . ARG   A 1 85  ? -23.639 -8.392  -15.149 1.00 66.22  ? 106 ARG   A NH2 1 
ATOM   621  N  N   . PRO   A 1 86  ? -22.138 -7.675  -7.298  1.00 65.47  ? 107 PRO   A N   1 
ATOM   622  C  CA  . PRO   A 1 86  ? -23.111 -8.223  -6.346  1.00 63.58  ? 107 PRO   A CA  1 
ATOM   623  C  C   . PRO   A 1 86  ? -24.404 -8.563  -7.071  1.00 66.72  ? 107 PRO   A C   1 
ATOM   624  O  O   . PRO   A 1 86  ? -24.863 -7.812  -7.934  1.00 69.73  ? 107 PRO   A O   1 
ATOM   625  C  CB  . PRO   A 1 86  ? -23.310 -7.084  -5.336  1.00 65.64  ? 107 PRO   A CB  1 
ATOM   626  C  CG  . PRO   A 1 86  ? -22.210 -6.091  -5.617  1.00 68.64  ? 107 PRO   A CG  1 
ATOM   627  C  CD  . PRO   A 1 86  ? -21.871 -6.248  -7.059  1.00 61.41  ? 107 PRO   A CD  1 
ATOM   628  N  N   . PHE   A 1 87  ? -24.999 -9.705  -6.720  1.00 66.64  ? 108 PHE   A N   1 
ATOM   629  C  CA  . PHE   A 1 87  ? -26.123 -10.204 -7.498  1.00 67.56  ? 108 PHE   A CA  1 
ATOM   630  C  C   . PHE   A 1 87  ? -27.455 -10.225 -6.759  1.00 70.65  ? 108 PHE   A C   1 
ATOM   631  O  O   . PHE   A 1 87  ? -28.498 -10.219 -7.420  1.00 71.56  ? 108 PHE   A O   1 
ATOM   632  C  CB  . PHE   A 1 87  ? -25.819 -11.611 -8.045  1.00 67.68  ? 108 PHE   A CB  1 
ATOM   633  C  CG  . PHE   A 1 87  ? -25.634 -12.666 -6.989  1.00 63.46  ? 108 PHE   A CG  1 
ATOM   634  C  CD1 . PHE   A 1 87  ? -24.416 -12.818 -6.344  1.00 60.11  ? 108 PHE   A CD1 1 
ATOM   635  C  CD2 . PHE   A 1 87  ? -26.664 -13.535 -6.673  1.00 63.19  ? 108 PHE   A CD2 1 
ATOM   636  C  CE1 . PHE   A 1 87  ? -24.241 -13.800 -5.385  1.00 59.59  ? 108 PHE   A CE1 1 
ATOM   637  C  CE2 . PHE   A 1 87  ? -26.494 -14.519 -5.716  1.00 62.76  ? 108 PHE   A CE2 1 
ATOM   638  C  CZ  . PHE   A 1 87  ? -25.281 -14.651 -5.072  1.00 58.96  ? 108 PHE   A CZ  1 
ATOM   639  N  N   . GLY   A 1 88  ? -27.461 -10.228 -5.428  1.00 68.38  ? 109 GLY   A N   1 
ATOM   640  C  CA  . GLY   A 1 88  ? -28.707 -10.193 -4.700  1.00 66.18  ? 109 GLY   A CA  1 
ATOM   641  C  C   . GLY   A 1 88  ? -28.554 -10.417 -3.210  1.00 64.79  ? 109 GLY   A C   1 
ATOM   642  O  O   . GLY   A 1 88  ? -27.443 -10.440 -2.671  1.00 67.79  ? 109 GLY   A O   1 
ATOM   643  N  N   . PRO   A 1 89  ? -29.680 -10.582 -2.512  1.00 63.28  ? 110 PRO   A N   1 
ATOM   644  C  CA  . PRO   A 1 89  ? -29.634 -10.827 -1.061  1.00 63.71  ? 110 PRO   A CA  1 
ATOM   645  C  C   . PRO   A 1 89  ? -29.002 -12.180 -0.769  1.00 66.18  ? 110 PRO   A C   1 
ATOM   646  O  O   . PRO   A 1 89  ? -29.491 -13.219 -1.219  1.00 63.24  ? 110 PRO   A O   1 
ATOM   647  C  CB  . PRO   A 1 89  ? -31.109 -10.784 -0.647  1.00 60.25  ? 110 PRO   A CB  1 
ATOM   648  C  CG  . PRO   A 1 89  ? -31.864 -11.111 -1.897  1.00 60.69  ? 110 PRO   A CG  1 
ATOM   649  C  CD  . PRO   A 1 89  ? -31.059 -10.540 -3.028  1.00 62.27  ? 110 PRO   A CD  1 
ATOM   650  N  N   . VAL   A 1 90  ? -27.910 -12.163 -0.002  1.00 67.30  ? 111 VAL   A N   1 
ATOM   651  C  CA  . VAL   A 1 90  ? -27.092 -13.345 0.225   1.00 67.57  ? 111 VAL   A CA  1 
ATOM   652  C  C   . VAL   A 1 90  ? -27.102 -13.777 1.686   1.00 69.82  ? 111 VAL   A C   1 
ATOM   653  O  O   . VAL   A 1 90  ? -27.102 -14.978 1.982   1.00 70.97  ? 111 VAL   A O   1 
ATOM   654  C  CB  . VAL   A 1 90  ? -25.645 -13.122 -0.263  1.00 65.24  ? 111 VAL   A CB  1 
ATOM   655  C  CG1 . VAL   A 1 90  ? -25.579 -13.222 -1.776  1.00 60.94  ? 111 VAL   A CG1 1 
ATOM   656  C  CG2 . VAL   A 1 90  ? -25.130 -11.765 0.201   1.00 68.89  ? 111 VAL   A CG2 1 
ATOM   657  N  N   . GLY   A 1 91  ? -27.094 -12.825 2.616   1.00 68.22  ? 112 GLY   A N   1 
ATOM   658  C  CA  . GLY   A 1 91  ? -27.077 -13.187 4.028   1.00 68.71  ? 112 GLY   A CA  1 
ATOM   659  C  C   . GLY   A 1 91  ? -25.715 -13.701 4.455   1.00 70.48  ? 112 GLY   A C   1 
ATOM   660  O  O   . GLY   A 1 91  ? -24.675 -13.143 4.092   1.00 70.64  ? 112 GLY   A O   1 
ATOM   661  N  N   . PHE   A 1 92  ? -25.716 -14.788 5.235   1.00 75.92  ? 113 PHE   A N   1 
ATOM   662  C  CA  . PHE   A 1 92  ? -24.459 -15.346 5.726   1.00 76.04  ? 113 PHE   A CA  1 
ATOM   663  C  C   . PHE   A 1 92  ? -23.576 -15.864 4.597   1.00 73.94  ? 113 PHE   A C   1 
ATOM   664  O  O   . PHE   A 1 92  ? -22.356 -15.977 4.776   1.00 73.90  ? 113 PHE   A O   1 
ATOM   665  C  CB  . PHE   A 1 92  ? -24.729 -16.463 6.742   1.00 76.69  ? 113 PHE   A CB  1 
ATOM   666  C  CG  . PHE   A 1 92  ? -24.895 -17.829 6.128   1.00 74.37  ? 113 PHE   A CG  1 
ATOM   667  C  CD1 . PHE   A 1 92  ? -26.130 -18.254 5.664   1.00 76.68  ? 113 PHE   A CD1 1 
ATOM   668  C  CD2 . PHE   A 1 92  ? -23.820 -18.700 6.042   1.00 77.12  ? 113 PHE   A CD2 1 
ATOM   669  C  CE1 . PHE   A 1 92  ? -26.284 -19.514 5.108   1.00 80.41  ? 113 PHE   A CE1 1 
ATOM   670  C  CE2 . PHE   A 1 92  ? -23.965 -19.957 5.487   1.00 76.57  ? 113 PHE   A CE2 1 
ATOM   671  C  CZ  . PHE   A 1 92  ? -25.198 -20.366 5.020   1.00 78.53  ? 113 PHE   A CZ  1 
ATOM   672  N  N   . MET   A 1 93  ? -24.160 -16.168 3.436   1.00 72.26  ? 114 MET   A N   1 
ATOM   673  C  CA  . MET   A 1 93  ? -23.405 -16.657 2.286   1.00 69.99  ? 114 MET   A CA  1 
ATOM   674  C  C   . MET   A 1 93  ? -22.498 -15.577 1.709   1.00 69.50  ? 114 MET   A C   1 
ATOM   675  O  O   . MET   A 1 93  ? -21.799 -15.810 0.718   1.00 67.05  ? 114 MET   A O   1 
ATOM   676  C  CB  . MET   A 1 93  ? -24.349 -17.182 1.205   1.00 67.78  ? 114 MET   A CB  1 
ATOM   677  C  CG  . MET   A 1 93  ? -24.969 -18.531 1.529   1.00 69.26  ? 114 MET   A CG  1 
ATOM   678  S  SD  . MET   A 1 93  ? -23.740 -19.850 1.639   1.00 68.30  ? 114 MET   A SD  1 
ATOM   679  C  CE  . MET   A 1 93  ? -23.141 -19.893 -0.049  1.00 65.78  ? 114 MET   A CE  1 
ATOM   680  N  N   . LYS   A 1 94  ? -22.502 -14.391 2.322   1.00 70.00  ? 115 LYS   A N   1 
ATOM   681  C  CA  . LYS   A 1 94  ? -21.544 -13.358 1.959   1.00 70.75  ? 115 LYS   A CA  1 
ATOM   682  C  C   . LYS   A 1 94  ? -20.111 -13.767 2.274   1.00 72.12  ? 115 LYS   A C   1 
ATOM   683  O  O   . LYS   A 1 94  ? -19.175 -13.106 1.809   1.00 72.68  ? 115 LYS   A O   1 
ATOM   684  C  CB  . LYS   A 1 94  ? -21.885 -12.052 2.682   1.00 65.69  ? 115 LYS   A CB  1 
ATOM   685  N  N   . SER   A 1 95  ? -19.920 -14.831 3.052   1.00 72.75  ? 116 SER   A N   1 
ATOM   686  C  CA  . SER   A 1 95  ? -18.600 -15.343 3.392   1.00 74.27  ? 116 SER   A CA  1 
ATOM   687  C  C   . SER   A 1 95  ? -18.090 -16.386 2.404   1.00 70.28  ? 116 SER   A C   1 
ATOM   688  O  O   . SER   A 1 95  ? -16.973 -16.884 2.577   1.00 68.28  ? 116 SER   A O   1 
ATOM   689  C  CB  . SER   A 1 95  ? -18.616 -15.938 4.803   1.00 75.55  ? 116 SER   A CB  1 
ATOM   690  O  OG  . SER   A 1 95  ? -19.086 -14.992 5.748   1.00 78.32  ? 116 SER   A OG  1 
ATOM   691  N  N   . ALA   A 1 96  ? -18.876 -16.740 1.391   1.00 69.78  ? 117 ALA   A N   1 
ATOM   692  C  CA  . ALA   A 1 96  ? -18.402 -17.659 0.368   1.00 65.30  ? 117 ALA   A CA  1 
ATOM   693  C  C   . ALA   A 1 96  ? -17.306 -17.002 -0.463  1.00 65.38  ? 117 ALA   A C   1 
ATOM   694  O  O   . ALA   A 1 96  ? -17.328 -15.794 -0.711  1.00 68.02  ? 117 ALA   A O   1 
ATOM   695  C  CB  . ALA   A 1 96  ? -19.555 -18.103 -0.532  1.00 64.22  ? 117 ALA   A CB  1 
ATOM   696  N  N   . ILE   A 1 97  ? -16.335 -17.815 -0.889  1.00 66.65  ? 118 ILE   A N   1 
ATOM   697  C  CA  . ILE   A 1 97  ? -15.169 -17.279 -1.587  1.00 64.72  ? 118 ILE   A CA  1 
ATOM   698  C  C   . ILE   A 1 97  ? -15.570 -16.665 -2.925  1.00 63.74  ? 118 ILE   A C   1 
ATOM   699  O  O   . ILE   A 1 97  ? -15.021 -15.637 -3.339  1.00 66.76  ? 118 ILE   A O   1 
ATOM   700  C  CB  . ILE   A 1 97  ? -14.099 -18.374 -1.753  1.00 69.20  ? 118 ILE   A CB  1 
ATOM   701  C  CG1 . ILE   A 1 97  ? -12.949 -17.879 -2.634  1.00 69.87  ? 118 ILE   A CG1 1 
ATOM   702  C  CG2 . ILE   A 1 97  ? -14.706 -19.647 -2.325  1.00 66.92  ? 118 ILE   A CG2 1 
ATOM   703  C  CD1 . ILE   A 1 97  ? -11.882 -18.921 -2.881  1.00 68.99  ? 118 ILE   A CD1 1 
ATOM   704  N  N   . SER   A 1 98  ? -16.537 -17.272 -3.617  1.00 61.98  ? 119 SER   A N   1 
ATOM   705  C  CA  . SER   A 1 98  ? -17.008 -16.727 -4.885  1.00 62.68  ? 119 SER   A CA  1 
ATOM   706  C  C   . SER   A 1 98  ? -17.798 -15.436 -4.713  1.00 64.02  ? 119 SER   A C   1 
ATOM   707  O  O   . SER   A 1 98  ? -18.025 -14.732 -5.703  1.00 63.71  ? 119 SER   A O   1 
ATOM   708  C  CB  . SER   A 1 98  ? -17.860 -17.766 -5.616  1.00 61.23  ? 119 SER   A CB  1 
ATOM   709  O  OG  . SER   A 1 98  ? -18.829 -18.329 -4.750  1.00 63.21  ? 119 SER   A OG  1 
ATOM   710  N  N   . ILE   A 1 99  ? -18.216 -15.112 -3.492  1.00 63.60  ? 120 ILE   A N   1 
ATOM   711  C  CA  . ILE   A 1 99  ? -18.962 -13.891 -3.224  1.00 60.81  ? 120 ILE   A CA  1 
ATOM   712  C  C   . ILE   A 1 99  ? -18.178 -12.907 -2.361  1.00 65.32  ? 120 ILE   A C   1 
ATOM   713  O  O   . ILE   A 1 99  ? -18.502 -11.709 -2.369  1.00 68.00  ? 120 ILE   A O   1 
ATOM   714  C  CB  . ILE   A 1 99  ? -20.326 -14.209 -2.574  1.00 62.98  ? 120 ILE   A CB  1 
ATOM   715  C  CG1 . ILE   A 1 99  ? -21.003 -15.367 -3.309  1.00 64.64  ? 120 ILE   A CG1 1 
ATOM   716  C  CG2 . ILE   A 1 99  ? -21.246 -12.996 -2.593  1.00 61.11  ? 120 ILE   A CG2 1 
ATOM   717  C  CD1 . ILE   A 1 99  ? -22.365 -15.729 -2.759  1.00 62.94  ? 120 ILE   A CD1 1 
ATOM   718  N  N   . ALA   A 1 100 ? -17.150 -13.360 -1.645  1.00 65.81  ? 121 ALA   A N   1 
ATOM   719  C  CA  . ALA   A 1 100 ? -16.376 -12.481 -0.780  1.00 68.66  ? 121 ALA   A CA  1 
ATOM   720  C  C   . ALA   A 1 100 ? -15.681 -11.395 -1.596  1.00 68.99  ? 121 ALA   A C   1 
ATOM   721  O  O   . ALA   A 1 100 ? -15.477 -11.519 -2.806  1.00 67.82  ? 121 ALA   A O   1 
ATOM   722  C  CB  . ALA   A 1 100 ? -15.344 -13.281 0.013   1.00 67.81  ? 121 ALA   A CB  1 
ATOM   723  N  N   . GLU   A 1 101 ? -15.323 -10.308 -0.914  1.00 71.51  ? 122 GLU   A N   1 
ATOM   724  C  CA  . GLU   A 1 101 ? -14.753 -9.141  -1.566  1.00 75.34  ? 122 GLU   A CA  1 
ATOM   725  C  C   . GLU   A 1 101 ? -13.532 -8.638  -0.810  1.00 76.92  ? 122 GLU   A C   1 
ATOM   726  O  O   . GLU   A 1 101 ? -13.430 -8.785  0.411   1.00 76.71  ? 122 GLU   A O   1 
ATOM   727  C  CB  . GLU   A 1 101 ? -15.781 -8.008  -1.680  1.00 75.16  ? 122 GLU   A CB  1 
ATOM   728  C  CG  . GLU   A 1 101 ? -16.934 -8.310  -2.619  1.00 74.83  ? 122 GLU   A CG  1 
ATOM   729  C  CD  . GLU   A 1 101 ? -17.926 -7.170  -2.705  1.00 77.64  ? 122 GLU   A CD  1 
ATOM   730  O  OE1 . GLU   A 1 101 ? -17.735 -6.157  -1.998  1.00 79.42  ? 122 GLU   A OE1 1 
ATOM   731  O  OE2 . GLU   A 1 101 ? -18.898 -7.285  -3.481  1.00 79.02  ? 122 GLU   A OE2 1 
ATOM   732  N  N   . ASP   A 1 102 ? -12.609 -8.047  -1.566  1.00 74.13  ? 123 ASP   A N   1 
ATOM   733  C  CA  . ASP   A 1 102 ? -11.469 -7.280  -1.043  1.00 75.73  ? 123 ASP   A CA  1 
ATOM   734  C  C   . ASP   A 1 102 ? -10.629 -8.187  -0.145  1.00 76.85  ? 123 ASP   A C   1 
ATOM   735  O  O   . ASP   A 1 102 ? -10.207 -9.263  -0.598  1.00 75.64  ? 123 ASP   A O   1 
ATOM   736  C  CB  . ASP   A 1 102 ? -12.002 -6.009  -0.393  1.00 78.06  ? 123 ASP   A CB  1 
ATOM   737  C  CG  . ASP   A 1 102 ? -12.591 -5.047  -1.405  1.00 81.22  ? 123 ASP   A CG  1 
ATOM   738  O  OD1 . ASP   A 1 102 ? -12.047 -4.963  -2.527  1.00 83.29  ? 123 ASP   A OD1 1 
ATOM   739  O  OD2 . ASP   A 1 102 ? -13.596 -4.379  -1.085  1.00 81.44  ? 123 ASP   A OD2 1 
ATOM   740  N  N   . GLU   A 1 103 ? -10.365 -7.810  1.108   1.00 76.20  ? 124 GLU   A N   1 
ATOM   741  C  CA  . GLU   A 1 103 ? -9.387  -8.537  1.911   1.00 77.50  ? 124 GLU   A CA  1 
ATOM   742  C  C   . GLU   A 1 103 ? -9.918  -9.876  2.402   1.00 78.84  ? 124 GLU   A C   1 
ATOM   743  O  O   . GLU   A 1 103 ? -9.139  -10.824 2.553   1.00 78.14  ? 124 GLU   A O   1 
ATOM   744  C  CB  . GLU   A 1 103 ? -8.936  -7.679  3.092   1.00 79.41  ? 124 GLU   A CB  1 
ATOM   745  C  CG  . GLU   A 1 103 ? -8.086  -6.478  2.699   1.00 80.39  ? 124 GLU   A CG  1 
ATOM   746  C  CD  . GLU   A 1 103 ? -6.768  -6.873  2.052   1.00 84.99  ? 124 GLU   A CD  1 
ATOM   747  O  OE1 . GLU   A 1 103 ? -6.311  -8.017  2.264   1.00 85.56  ? 124 GLU   A OE1 1 
ATOM   748  O  OE2 . GLU   A 1 103 ? -6.189  -6.038  1.326   1.00 84.25  ? 124 GLU   A OE2 1 
ATOM   749  N  N   . GLU   A 1 104 ? -11.223 -9.980  2.668   1.00 77.36  ? 125 GLU   A N   1 
ATOM   750  C  CA  . GLU   A 1 104 ? -11.757 -11.251 3.147   1.00 75.70  ? 125 GLU   A CA  1 
ATOM   751  C  C   . GLU   A 1 104 ? -11.585 -12.344 2.101   1.00 75.43  ? 125 GLU   A C   1 
ATOM   752  O  O   . GLU   A 1 104 ? -11.345 -13.507 2.444   1.00 77.05  ? 125 GLU   A O   1 
ATOM   753  C  CB  . GLU   A 1 104 ? -13.229 -11.114 3.538   1.00 77.46  ? 125 GLU   A CB  1 
ATOM   754  C  CG  . GLU   A 1 104 ? -13.735 -12.306 4.347   1.00 80.14  ? 125 GLU   A CG  1 
ATOM   755  C  CD  . GLU   A 1 104 ? -15.230 -12.271 4.601   1.00 84.97  ? 125 GLU   A CD  1 
ATOM   756  O  OE1 . GLU   A 1 104 ? -15.957 -11.627 3.816   1.00 86.75  ? 125 GLU   A OE1 1 
ATOM   757  O  OE2 . GLU   A 1 104 ? -15.678 -12.891 5.590   1.00 84.43  ? 125 GLU   A OE2 1 
ATOM   758  N  N   . TRP   A 1 105 ? -11.705 -11.994 0.817   1.00 73.76  ? 126 TRP   A N   1 
ATOM   759  C  CA  . TRP   A 1 105 ? -11.461 -12.973 -0.237  1.00 74.80  ? 126 TRP   A CA  1 
ATOM   760  C  C   . TRP   A 1 105 ? -10.025 -13.477 -0.195  1.00 76.02  ? 126 TRP   A C   1 
ATOM   761  O  O   . TRP   A 1 105 ? -9.776  -14.685 -0.279  1.00 75.49  ? 126 TRP   A O   1 
ATOM   762  C  CB  . TRP   A 1 105 ? -11.769 -12.373 -1.609  1.00 70.01  ? 126 TRP   A CB  1 
ATOM   763  C  CG  . TRP   A 1 105 ? -11.248 -13.225 -2.728  1.00 71.15  ? 126 TRP   A CG  1 
ATOM   764  C  CD1 . TRP   A 1 105 ? -11.704 -14.459 -3.094  1.00 72.09  ? 126 TRP   A CD1 1 
ATOM   765  C  CD2 . TRP   A 1 105 ? -10.165 -12.918 -3.616  1.00 73.80  ? 126 TRP   A CD2 1 
ATOM   766  N  NE1 . TRP   A 1 105 ? -10.975 -14.937 -4.156  1.00 70.95  ? 126 TRP   A NE1 1 
ATOM   767  C  CE2 . TRP   A 1 105 ? -10.026 -14.011 -4.496  1.00 73.30  ? 126 TRP   A CE2 1 
ATOM   768  C  CE3 . TRP   A 1 105 ? -9.302  -11.826 -3.755  1.00 74.33  ? 126 TRP   A CE3 1 
ATOM   769  C  CZ2 . TRP   A 1 105 ? -9.060  -14.043 -5.502  1.00 71.41  ? 126 TRP   A CZ2 1 
ATOM   770  C  CZ3 . TRP   A 1 105 ? -8.343  -11.860 -4.754  1.00 75.71  ? 126 TRP   A CZ3 1 
ATOM   771  C  CH2 . TRP   A 1 105 ? -8.231  -12.961 -5.614  1.00 73.30  ? 126 TRP   A CH2 1 
ATOM   772  N  N   . LYS   A 1 106 ? -9.066  -12.557 -0.062  1.00 75.34  ? 127 LYS   A N   1 
ATOM   773  C  CA  . LYS   A 1 106 ? -7.662  -12.952 -0.005  1.00 75.67  ? 127 LYS   A CA  1 
ATOM   774  C  C   . LYS   A 1 106 ? -7.401  -13.870 1.180   1.00 74.70  ? 127 LYS   A C   1 
ATOM   775  O  O   . LYS   A 1 106 ? -6.652  -14.848 1.067   1.00 75.55  ? 127 LYS   A O   1 
ATOM   776  C  CB  . LYS   A 1 106 ? -6.771  -11.711 0.068   1.00 77.24  ? 127 LYS   A CB  1 
ATOM   777  N  N   . ARG   A 1 107 ? -8.007  -13.567 2.329   1.00 73.92  ? 128 ARG   A N   1 
ATOM   778  C  CA  . ARG   A 1 107 ? -7.903  -14.459 3.478   1.00 75.70  ? 128 ARG   A CA  1 
ATOM   779  C  C   . ARG   A 1 107 ? -8.542  -15.812 3.187   1.00 78.02  ? 128 ARG   A C   1 
ATOM   780  O  O   . ARG   A 1 107 ? -7.982  -16.858 3.534   1.00 77.72  ? 128 ARG   A O   1 
ATOM   781  C  CB  . ARG   A 1 107 ? -8.544  -13.808 4.703   1.00 75.52  ? 128 ARG   A CB  1 
ATOM   782  C  CG  . ARG   A 1 107 ? -8.808  -14.771 5.845   1.00 77.19  ? 128 ARG   A CG  1 
ATOM   783  C  CD  . ARG   A 1 107 ? -9.468  -14.076 7.022   1.00 79.95  ? 128 ARG   A CD  1 
ATOM   784  N  NE  . ARG   A 1 107 ? -10.029 -15.040 7.960   1.00 84.67  ? 128 ARG   A NE  1 
ATOM   785  C  CZ  . ARG   A 1 107 ? -11.283 -15.471 7.927   1.00 86.19  ? 128 ARG   A CZ  1 
ATOM   786  N  NH1 . ARG   A 1 107 ? -12.143 -15.024 7.027   1.00 85.25  ? 128 ARG   A NH1 1 
ATOM   787  N  NH2 . ARG   A 1 107 ? -11.683 -16.371 8.821   1.00 85.97  ? 128 ARG   A NH2 1 
ATOM   788  N  N   . LEU   A 1 108 ? -9.711  -15.812 2.541   1.00 78.14  ? 129 LEU   A N   1 
ATOM   789  C  CA  . LEU   A 1 108 ? -10.393 -17.070 2.247   1.00 74.85  ? 129 LEU   A CA  1 
ATOM   790  C  C   . LEU   A 1 108 ? -9.717  -17.835 1.117   1.00 74.05  ? 129 LEU   A C   1 
ATOM   791  O  O   . LEU   A 1 108 ? -9.689  -19.071 1.142   1.00 74.18  ? 129 LEU   A O   1 
ATOM   792  C  CB  . LEU   A 1 108 ? -11.860 -16.802 1.910   1.00 75.22  ? 129 LEU   A CB  1 
ATOM   793  C  CG  . LEU   A 1 108 ? -12.721 -16.309 3.073   1.00 76.17  ? 129 LEU   A CG  1 
ATOM   794  C  CD1 . LEU   A 1 108 ? -14.020 -15.712 2.564   1.00 74.43  ? 129 LEU   A CD1 1 
ATOM   795  C  CD2 . LEU   A 1 108 ? -12.998 -17.438 4.057   1.00 76.82  ? 129 LEU   A CD2 1 
ATOM   796  N  N   . ARG   A 1 109 ? -9.177  -17.130 0.122   1.00 74.44  ? 130 ARG   A N   1 
ATOM   797  C  CA  . ARG   A 1 109 ? -8.450  -17.806 -0.949  1.00 72.92  ? 130 ARG   A CA  1 
ATOM   798  C  C   . ARG   A 1 109 ? -7.205  -18.500 -0.410  1.00 75.73  ? 130 ARG   A C   1 
ATOM   799  O  O   . ARG   A 1 109 ? -6.848  -19.593 -0.863  1.00 76.55  ? 130 ARG   A O   1 
ATOM   800  C  CB  . ARG   A 1 109 ? -8.076  -16.807 -2.046  1.00 71.39  ? 130 ARG   A CB  1 
ATOM   801  C  CG  . ARG   A 1 109 ? -7.395  -17.428 -3.258  1.00 69.63  ? 130 ARG   A CG  1 
ATOM   802  C  CD  . ARG   A 1 109 ? -8.402  -18.041 -4.221  1.00 67.26  ? 130 ARG   A CD  1 
ATOM   803  N  NE  . ARG   A 1 109 ? -7.744  -18.679 -5.355  1.00 63.03  ? 130 ARG   A NE  1 
ATOM   804  C  CZ  . ARG   A 1 109 ? -8.352  -19.017 -6.484  1.00 63.63  ? 130 ARG   A CZ  1 
ATOM   805  N  NH1 . ARG   A 1 109 ? -9.639  -18.776 -6.676  1.00 66.12  ? 130 ARG   A NH1 1 
ATOM   806  N  NH2 . ARG   A 1 109 ? -7.650  -19.604 -7.448  1.00 60.95  ? 130 ARG   A NH2 1 
ATOM   807  N  N   . SER   A 1 110 ? -6.528  -17.872 0.555   1.00 77.54  ? 131 SER   A N   1 
ATOM   808  C  CA  . SER   A 1 110 ? -5.339  -18.477 1.143   1.00 74.73  ? 131 SER   A CA  1 
ATOM   809  C  C   . SER   A 1 110 ? -5.683  -19.731 1.938   1.00 76.26  ? 131 SER   A C   1 
ATOM   810  O  O   . SER   A 1 110 ? -5.001  -20.755 1.817   1.00 77.14  ? 131 SER   A O   1 
ATOM   811  C  CB  . SER   A 1 110 ? -4.619  -17.462 2.032   1.00 74.21  ? 131 SER   A CB  1 
ATOM   812  O  OG  . SER   A 1 110 ? -4.204  -16.333 1.283   1.00 79.69  ? 131 SER   A OG  1 
ATOM   813  N  N   . LEU   A 1 111 ? -6.739  -19.675 2.754   1.00 76.31  ? 132 LEU   A N   1 
ATOM   814  C  CA  . LEU   A 1 111 ? -7.072  -20.802 3.619   1.00 76.87  ? 132 LEU   A CA  1 
ATOM   815  C  C   . LEU   A 1 111 ? -7.663  -21.978 2.852   1.00 79.12  ? 132 LEU   A C   1 
ATOM   816  O  O   . LEU   A 1 111 ? -7.662  -23.100 3.371   1.00 83.97  ? 132 LEU   A O   1 
ATOM   817  C  CB  . LEU   A 1 111 ? -8.046  -20.357 4.712   1.00 78.42  ? 132 LEU   A CB  1 
ATOM   818  C  CG  . LEU   A 1 111 ? -7.551  -19.265 5.663   1.00 80.62  ? 132 LEU   A CG  1 
ATOM   819  C  CD1 . LEU   A 1 111 ? -8.641  -18.880 6.651   1.00 81.76  ? 132 LEU   A CD1 1 
ATOM   820  C  CD2 . LEU   A 1 111 ? -6.292  -19.710 6.393   1.00 81.54  ? 132 LEU   A CD2 1 
ATOM   821  N  N   . LEU   A 1 112 ? -8.160  -21.754 1.633   1.00 77.85  ? 133 LEU   A N   1 
ATOM   822  C  CA  . LEU   A 1 112 ? -8.810  -22.803 0.860   1.00 79.54  ? 133 LEU   A CA  1 
ATOM   823  C  C   . LEU   A 1 112 ? -7.966  -23.358 -0.278  1.00 80.13  ? 133 LEU   A C   1 
ATOM   824  O  O   . LEU   A 1 112 ? -8.259  -24.459 -0.754  1.00 79.65  ? 133 LEU   A O   1 
ATOM   825  C  CB  . LEU   A 1 112 ? -10.141 -22.297 0.284   1.00 76.32  ? 133 LEU   A CB  1 
ATOM   826  C  CG  . LEU   A 1 112 ? -11.322 -22.263 1.256   1.00 75.59  ? 133 LEU   A CG  1 
ATOM   827  C  CD1 . LEU   A 1 112 ? -12.555 -21.670 0.592   1.00 74.24  ? 133 LEU   A CD1 1 
ATOM   828  C  CD2 . LEU   A 1 112 ? -11.612 -23.661 1.777   1.00 75.87  ? 133 LEU   A CD2 1 
ATOM   829  N  N   . SER   A 1 113 ? -6.942  -22.633 -0.730  1.00 79.17  ? 134 SER   A N   1 
ATOM   830  C  CA  . SER   A 1 113 ? -6.103  -23.138 -1.817  1.00 79.13  ? 134 SER   A CA  1 
ATOM   831  C  C   . SER   A 1 113 ? -5.446  -24.476 -1.495  1.00 81.25  ? 134 SER   A C   1 
ATOM   832  O  O   . SER   A 1 113 ? -5.477  -25.372 -2.357  1.00 80.96  ? 134 SER   A O   1 
ATOM   833  C  CB  . SER   A 1 113 ? -5.061  -22.081 -2.202  1.00 78.23  ? 134 SER   A CB  1 
ATOM   834  O  OG  . SER   A 1 113 ? -5.679  -20.919 -2.726  1.00 78.32  ? 134 SER   A OG  1 
ATOM   835  N  N   . PRO   A 1 114 ? -4.844  -24.691 -0.318  1.00 82.76  ? 135 PRO   A N   1 
ATOM   836  C  CA  . PRO   A 1 114 ? -4.254  -26.012 -0.038  1.00 81.69  ? 135 PRO   A CA  1 
ATOM   837  C  C   . PRO   A 1 114 ? -5.258  -27.151 -0.070  1.00 81.96  ? 135 PRO   A C   1 
ATOM   838  O  O   . PRO   A 1 114 ? -4.861  -28.301 -0.294  1.00 83.41  ? 135 PRO   A O   1 
ATOM   839  C  CB  . PRO   A 1 114 ? -3.648  -25.839 1.362   1.00 83.12  ? 135 PRO   A CB  1 
ATOM   840  C  CG  . PRO   A 1 114 ? -3.404  -24.381 1.485   1.00 81.34  ? 135 PRO   A CG  1 
ATOM   841  C  CD  . PRO   A 1 114 ? -4.545  -23.734 0.764   1.00 82.50  ? 135 PRO   A CD  1 
ATOM   842  N  N   . THR   A 1 115 ? -6.544  -26.872 0.157   1.00 81.97  ? 136 THR   A N   1 
ATOM   843  C  CA  . THR   A 1 115 ? -7.571  -27.901 0.046   1.00 79.71  ? 136 THR   A CA  1 
ATOM   844  C  C   . THR   A 1 115 ? -7.734  -28.398 -1.386  1.00 78.38  ? 136 THR   A C   1 
ATOM   845  O  O   . THR   A 1 115 ? -8.198  -29.525 -1.592  1.00 77.67  ? 136 THR   A O   1 
ATOM   846  C  CB  . THR   A 1 115 ? -8.900  -27.358 0.577   1.00 79.81  ? 136 THR   A CB  1 
ATOM   847  O  OG1 . THR   A 1 115 ? -8.693  -26.776 1.870   1.00 85.74  ? 136 THR   A OG1 1 
ATOM   848  C  CG2 . THR   A 1 115 ? -9.939  -28.461 0.696   1.00 80.48  ? 136 THR   A CG2 1 
ATOM   849  N  N   . PHE   A 1 116 ? -7.339  -27.597 -2.377  1.00 78.21  ? 137 PHE   A N   1 
ATOM   850  C  CA  . PHE   A 1 116 ? -7.471  -27.961 -3.782  1.00 77.20  ? 137 PHE   A CA  1 
ATOM   851  C  C   . PHE   A 1 116 ? -6.129  -28.315 -4.415  1.00 78.67  ? 137 PHE   A C   1 
ATOM   852  O  O   . PHE   A 1 116 ? -5.972  -28.205 -5.635  1.00 78.75  ? 137 PHE   A O   1 
ATOM   853  C  CB  . PHE   A 1 116 ? -8.160  -26.833 -4.550  1.00 73.76  ? 137 PHE   A CB  1 
ATOM   854  C  CG  . PHE   A 1 116 ? -9.576  -26.581 -4.106  1.00 70.72  ? 137 PHE   A CG  1 
ATOM   855  C  CD1 . PHE   A 1 116 ? -10.626 -27.288 -4.668  1.00 69.01  ? 137 PHE   A CD1 1 
ATOM   856  C  CD2 . PHE   A 1 116 ? -9.854  -25.653 -3.118  1.00 71.64  ? 137 PHE   A CD2 1 
ATOM   857  C  CE1 . PHE   A 1 116 ? -11.929 -27.066 -4.259  1.00 64.15  ? 137 PHE   A CE1 1 
ATOM   858  C  CE2 . PHE   A 1 116 ? -11.154 -25.426 -2.704  1.00 69.08  ? 137 PHE   A CE2 1 
ATOM   859  C  CZ  . PHE   A 1 116 ? -12.192 -26.135 -3.276  1.00 63.60  ? 137 PHE   A CZ  1 
ATOM   860  N  N   . THR   A 1 117 ? -5.163  -28.738 -3.605  1.00 80.80  ? 138 THR   A N   1 
ATOM   861  C  CA  . THR   A 1 117 ? -3.875  -29.191 -4.110  1.00 79.97  ? 138 THR   A CA  1 
ATOM   862  C  C   . THR   A 1 117 ? -4.041  -30.463 -4.937  1.00 81.73  ? 138 THR   A C   1 
ATOM   863  O  O   . THR   A 1 117 ? -4.906  -31.299 -4.662  1.00 84.91  ? 138 THR   A O   1 
ATOM   864  C  CB  . THR   A 1 117 ? -2.913  -29.442 -2.944  1.00 82.45  ? 138 THR   A CB  1 
ATOM   865  O  OG1 . THR   A 1 117 ? -2.898  -28.296 -2.083  1.00 82.74  ? 138 THR   A OG1 1 
ATOM   866  C  CG2 . THR   A 1 117 ? -1.498  -29.707 -3.442  1.00 85.80  ? 138 THR   A CG2 1 
ATOM   867  N  N   . SER   A 1 118 ? -3.199  -30.601 -5.968  1.00 79.72  ? 139 SER   A N   1 
ATOM   868  C  CA  . SER   A 1 118 ? -3.219  -31.812 -6.785  1.00 80.31  ? 139 SER   A CA  1 
ATOM   869  C  C   . SER   A 1 118 ? -2.946  -33.054 -5.947  1.00 82.77  ? 139 SER   A C   1 
ATOM   870  O  O   . SER   A 1 118 ? -3.419  -34.146 -6.284  1.00 82.66  ? 139 SER   A O   1 
ATOM   871  C  CB  . SER   A 1 118 ? -2.199  -31.706 -7.920  1.00 77.92  ? 139 SER   A CB  1 
ATOM   872  O  OG  . SER   A 1 118 ? -0.872  -31.757 -7.426  1.00 84.15  ? 139 SER   A OG  1 
ATOM   873  N  N   . GLY   A 1 119 ? -2.187  -32.911 -4.858  1.00 83.34  ? 140 GLY   A N   1 
ATOM   874  C  CA  . GLY   A 1 119 ? -2.016  -34.024 -3.939  1.00 84.56  ? 140 GLY   A CA  1 
ATOM   875  C  C   . GLY   A 1 119 ? -3.318  -34.436 -3.281  1.00 84.89  ? 140 GLY   A C   1 
ATOM   876  O  O   . GLY   A 1 119 ? -3.597  -35.628 -3.125  1.00 85.64  ? 140 GLY   A O   1 
ATOM   877  N  N   . LYS   A 1 120 ? -4.133  -33.455 -2.881  1.00 84.62  ? 141 LYS   A N   1 
ATOM   878  C  CA  . LYS   A 1 120 ? -5.449  -33.762 -2.329  1.00 83.71  ? 141 LYS   A CA  1 
ATOM   879  C  C   . LYS   A 1 120 ? -6.353  -34.399 -3.376  1.00 85.00  ? 141 LYS   A C   1 
ATOM   880  O  O   . LYS   A 1 120 ? -7.112  -35.326 -3.068  1.00 85.40  ? 141 LYS   A O   1 
ATOM   881  C  CB  . LYS   A 1 120 ? -6.096  -32.496 -1.767  1.00 80.49  ? 141 LYS   A CB  1 
ATOM   882  C  CG  . LYS   A 1 120 ? -5.755  -32.201 -0.315  1.00 81.23  ? 141 LYS   A CG  1 
ATOM   883  C  CD  . LYS   A 1 120 ? -4.327  -31.720 -0.148  1.00 82.79  ? 141 LYS   A CD  1 
ATOM   884  C  CE  . LYS   A 1 120 ? -3.997  -31.493 1.318   1.00 86.83  ? 141 LYS   A CE  1 
ATOM   885  N  NZ  . LYS   A 1 120 ? -2.617  -30.963 1.496   1.00 93.31  ? 141 LYS   A NZ  1 
ATOM   886  N  N   . LEU   A 1 121 ? -6.288  -33.913 -4.619  1.00 83.37  ? 142 LEU   A N   1 
ATOM   887  C  CA  . LEU   A 1 121 ? -7.134  -34.458 -5.676  1.00 82.82  ? 142 LEU   A CA  1 
ATOM   888  C  C   . LEU   A 1 121 ? -6.817  -35.925 -5.936  1.00 85.77  ? 142 LEU   A C   1 
ATOM   889  O  O   . LEU   A 1 121 ? -7.728  -36.738 -6.135  1.00 85.75  ? 142 LEU   A O   1 
ATOM   890  C  CB  . LEU   A 1 121 ? -6.969  -33.636 -6.954  1.00 78.46  ? 142 LEU   A CB  1 
ATOM   891  C  CG  . LEU   A 1 121 ? -7.859  -34.026 -8.134  1.00 77.17  ? 142 LEU   A CG  1 
ATOM   892  C  CD1 . LEU   A 1 121 ? -9.325  -33.950 -7.740  1.00 72.97  ? 142 LEU   A CD1 1 
ATOM   893  C  CD2 . LEU   A 1 121 ? -7.575  -33.137 -9.333  1.00 74.14  ? 142 LEU   A CD2 1 
ATOM   894  N  N   . LYS   A 1 122 ? -5.531  -36.282 -5.934  1.00 86.75  ? 143 LYS   A N   1 
ATOM   895  C  CA  . LYS   A 1 122 ? -5.149  -37.677 -6.127  1.00 83.65  ? 143 LYS   A CA  1 
ATOM   896  C  C   . LYS   A 1 122 ? -5.697  -38.555 -5.009  1.00 85.53  ? 143 LYS   A C   1 
ATOM   897  O  O   . LYS   A 1 122 ? -6.118  -39.693 -5.250  1.00 87.58  ? 143 LYS   A O   1 
ATOM   898  C  CB  . LYS   A 1 122 ? -3.626  -37.797 -6.215  1.00 83.67  ? 143 LYS   A CB  1 
ATOM   899  C  CG  . LYS   A 1 122 ? -3.129  -39.158 -6.678  1.00 87.31  ? 143 LYS   A CG  1 
ATOM   900  C  CD  . LYS   A 1 122 ? -1.632  -39.135 -6.949  1.00 89.99  ? 143 LYS   A CD  1 
ATOM   901  C  CE  . LYS   A 1 122 ? -1.140  -40.468 -7.493  1.00 90.01  ? 143 LYS   A CE  1 
ATOM   902  N  NZ  . LYS   A 1 122 ? 0.303   -40.418 -7.866  1.00 95.16  ? 143 LYS   A NZ  1 
ATOM   903  N  N   . GLU   A 1 123 ? -5.702  -38.042 -3.776  1.00 83.27  ? 144 GLU   A N   1 
ATOM   904  C  CA  . GLU   A 1 123 ? -6.246  -38.797 -2.655  1.00 83.72  ? 144 GLU   A CA  1 
ATOM   905  C  C   . GLU   A 1 123 ? -7.763  -38.926 -2.720  1.00 83.98  ? 144 GLU   A C   1 
ATOM   906  O  O   . GLU   A 1 123 ? -8.328  -39.778 -2.026  1.00 82.88  ? 144 GLU   A O   1 
ATOM   907  C  CB  . GLU   A 1 123 ? -5.831  -38.152 -1.332  1.00 83.50  ? 144 GLU   A CB  1 
ATOM   908  C  CG  . GLU   A 1 123 ? -4.326  -38.117 -1.105  1.00 87.84  ? 144 GLU   A CG  1 
ATOM   909  C  CD  . GLU   A 1 123 ? -3.960  -37.887 0.350   1.00 92.59  ? 144 GLU   A CD  1 
ATOM   910  O  OE1 . GLU   A 1 123 ? -4.817  -38.129 1.225   1.00 93.24  ? 144 GLU   A OE1 1 
ATOM   911  O  OE2 . GLU   A 1 123 ? -2.814  -37.467 0.618   1.00 92.85  ? 144 GLU   A OE2 1 
ATOM   912  N  N   . MET   A 1 124 ? -8.434  -38.104 -3.528  1.00 85.95  ? 145 MET   A N   1 
ATOM   913  C  CA  . MET   A 1 124 ? -9.874  -38.213 -3.724  1.00 85.73  ? 145 MET   A CA  1 
ATOM   914  C  C   . MET   A 1 124 ? -10.249 -39.021 -4.959  1.00 84.58  ? 145 MET   A C   1 
ATOM   915  O  O   . MET   A 1 124 ? -11.439 -39.284 -5.167  1.00 82.50  ? 145 MET   A O   1 
ATOM   916  C  CB  . MET   A 1 124 ? -10.506 -36.819 -3.825  1.00 84.17  ? 145 MET   A CB  1 
ATOM   917  C  CG  . MET   A 1 124 ? -10.276 -35.932 -2.613  1.00 84.00  ? 145 MET   A CG  1 
ATOM   918  S  SD  . MET   A 1 124 ? -11.176 -34.374 -2.730  1.00 82.86  ? 145 MET   A SD  1 
ATOM   919  C  CE  . MET   A 1 124 ? -10.625 -33.548 -1.241  1.00 82.43  ? 145 MET   A CE  1 
ATOM   920  N  N   . VAL   A 1 125 ? -9.270  -39.416 -5.778  1.00 84.97  ? 146 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 125 ? -9.575  -40.172 -6.997  1.00 84.25  ? 146 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 125 ? -10.272 -41.497 -6.704  1.00 84.99  ? 146 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 125 ? -11.267 -41.807 -7.380  1.00 82.74  ? 146 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 125 ? -8.304  -40.346 -7.843  1.00 85.36  ? 146 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 125 ? -8.545  -41.340 -8.969  1.00 85.13  ? 146 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 125 ? -7.858  -39.007 -8.407  1.00 85.26  ? 146 VAL   A CG2 1 
ATOM   927  N  N   . PRO   A 1 126 ? -9.823  -42.319 -5.744  1.00 84.74  ? 147 PRO   A N   1 
ATOM   928  C  CA  . PRO   A 1 126 ? -10.540 -43.583 -5.493  1.00 82.30  ? 147 PRO   A CA  1 
ATOM   929  C  C   . PRO   A 1 126 ? -11.998 -43.387 -5.125  1.00 83.73  ? 147 PRO   A C   1 
ATOM   930  O  O   . PRO   A 1 126 ? -12.826 -44.257 -5.423  1.00 83.02  ? 147 PRO   A O   1 
ATOM   931  C  CB  . PRO   A 1 126 ? -9.748  -44.213 -4.339  1.00 80.71  ? 147 PRO   A CB  1 
ATOM   932  C  CG  . PRO   A 1 126 ? -8.398  -43.625 -4.445  1.00 81.91  ? 147 PRO   A CG  1 
ATOM   933  C  CD  . PRO   A 1 126 ? -8.609  -42.220 -4.911  1.00 82.68  ? 147 PRO   A CD  1 
ATOM   934  N  N   . ILE   A 1 127 ? -12.338 -42.267 -4.487  1.00 84.40  ? 148 ILE   A N   1 
ATOM   935  C  CA  . ILE   A 1 127 ? -13.722 -42.016 -4.095  1.00 82.44  ? 148 ILE   A CA  1 
ATOM   936  C  C   . ILE   A 1 127 ? -14.595 -41.818 -5.328  1.00 82.48  ? 148 ILE   A C   1 
ATOM   937  O  O   . ILE   A 1 127 ? -15.580 -42.534 -5.538  1.00 80.46  ? 148 ILE   A O   1 
ATOM   938  C  CB  . ILE   A 1 127 ? -13.807 -40.803 -3.152  1.00 79.13  ? 148 ILE   A CB  1 
ATOM   939  C  CG1 . ILE   A 1 127 ? -13.129 -41.103 -1.811  1.00 80.81  ? 148 ILE   A CG1 1 
ATOM   940  C  CG2 . ILE   A 1 127 ? -15.252 -40.397 -2.946  1.00 80.62  ? 148 ILE   A CG2 1 
ATOM   941  C  CD1 . ILE   A 1 127 ? -11.644 -40.808 -1.786  1.00 83.76  ? 148 ILE   A CD1 1 
ATOM   942  N  N   . ILE   A 1 128 ? -14.243 -40.840 -6.166  1.00 80.16  ? 149 ILE   A N   1 
ATOM   943  C  CA  . ILE   A 1 128 ? -15.066 -40.531 -7.328  1.00 79.39  ? 149 ILE   A CA  1 
ATOM   944  C  C   . ILE   A 1 128 ? -14.996 -41.627 -8.382  1.00 81.51  ? 149 ILE   A C   1 
ATOM   945  O  O   . ILE   A 1 128 ? -15.883 -41.711 -9.240  1.00 79.32  ? 149 ILE   A O   1 
ATOM   946  C  CB  . ILE   A 1 128 ? -14.662 -39.162 -7.905  1.00 75.21  ? 149 ILE   A CB  1 
ATOM   947  C  CG1 . ILE   A 1 128 ? -13.189 -39.161 -8.306  1.00 79.86  ? 149 ILE   A CG1 1 
ATOM   948  C  CG2 . ILE   A 1 128 ? -14.903 -38.078 -6.880  1.00 76.61  ? 149 ILE   A CG2 1 
ATOM   949  C  CD1 . ILE   A 1 128 ? -12.624 -37.768 -8.526  1.00 78.23  ? 149 ILE   A CD1 1 
ATOM   950  N  N   . ALA   A 1 129 ? -13.965 -42.475 -8.343  1.00 80.32  ? 150 ALA   A N   1 
ATOM   951  C  CA  . ALA   A 1 129 ? -13.945 -43.642 -9.217  1.00 79.16  ? 150 ALA   A CA  1 
ATOM   952  C  C   . ALA   A 1 129 ? -14.912 -44.715 -8.735  1.00 81.15  ? 150 ALA   A C   1 
ATOM   953  O  O   . ALA   A 1 129 ? -15.406 -45.512 -9.542  1.00 80.91  ? 150 ALA   A O   1 
ATOM   954  C  CB  . ALA   A 1 129 ? -12.529 -44.208 -9.314  1.00 82.05  ? 150 ALA   A CB  1 
ATOM   955  N  N   . GLN   A 1 130 ? -15.185 -44.754 -7.429  1.00 80.55  ? 151 GLN   A N   1 
ATOM   956  C  CA  . GLN   A 1 130 ? -16.152 -45.710 -6.898  1.00 78.69  ? 151 GLN   A CA  1 
ATOM   957  C  C   . GLN   A 1 130 ? -17.537 -45.472 -7.483  1.00 78.14  ? 151 GLN   A C   1 
ATOM   958  O  O   . GLN   A 1 130 ? -18.249 -46.424 -7.823  1.00 77.61  ? 151 GLN   A O   1 
ATOM   959  C  CB  . GLN   A 1 130 ? -16.190 -45.622 -5.371  1.00 81.71  ? 151 GLN   A CB  1 
ATOM   960  C  CG  . GLN   A 1 130 ? -17.333 -46.388 -4.724  1.00 81.05  ? 151 GLN   A CG  1 
ATOM   961  C  CD  . GLN   A 1 130 ? -17.469 -46.088 -3.242  1.00 81.33  ? 151 GLN   A CD  1 
ATOM   962  O  OE1 . GLN   A 1 130 ? -16.654 -45.368 -2.664  1.00 78.90  ? 151 GLN   A OE1 1 
ATOM   963  N  NE2 . GLN   A 1 130 ? -18.506 -46.638 -2.619  1.00 80.47  ? 151 GLN   A NE2 1 
ATOM   964  N  N   . TYR   A 1 131 ? -17.932 -44.208 -7.614  1.00 79.47  ? 152 TYR   A N   1 
ATOM   965  C  CA  . TYR   A 1 131 ? -19.231 -43.866 -8.173  1.00 77.75  ? 152 TYR   A CA  1 
ATOM   966  C  C   . TYR   A 1 131 ? -19.226 -43.810 -9.692  1.00 76.74  ? 152 TYR   A C   1 
ATOM   967  O  O   . TYR   A 1 131 ? -20.297 -43.678 -10.295 1.00 76.95  ? 152 TYR   A O   1 
ATOM   968  C  CB  . TYR   A 1 131 ? -19.712 -42.540 -7.587  1.00 76.12  ? 152 TYR   A CB  1 
ATOM   969  C  CG  . TYR   A 1 131 ? -19.763 -42.602 -6.085  1.00 77.48  ? 152 TYR   A CG  1 
ATOM   970  C  CD1 . TYR   A 1 131 ? -20.833 -43.204 -5.436  1.00 76.31  ? 152 TYR   A CD1 1 
ATOM   971  C  CD2 . TYR   A 1 131 ? -18.721 -42.104 -5.317  1.00 77.37  ? 152 TYR   A CD2 1 
ATOM   972  C  CE1 . TYR   A 1 131 ? -20.879 -43.279 -4.063  1.00 76.52  ? 152 TYR   A CE1 1 
ATOM   973  C  CE2 . TYR   A 1 131 ? -18.755 -42.178 -3.945  1.00 78.80  ? 152 TYR   A CE2 1 
ATOM   974  C  CZ  . TYR   A 1 131 ? -19.836 -42.765 -3.324  1.00 79.75  ? 152 TYR   A CZ  1 
ATOM   975  O  OH  . TYR   A 1 131 ? -19.868 -42.837 -1.957  1.00 80.53  ? 152 TYR   A OH  1 
ATOM   976  N  N   . GLY   A 1 132 ? -18.055 -43.897 -10.322 1.00 75.06  ? 153 GLY   A N   1 
ATOM   977  C  CA  . GLY   A 1 132 ? -18.021 -44.238 -11.732 1.00 75.23  ? 153 GLY   A CA  1 
ATOM   978  C  C   . GLY   A 1 132 ? -18.543 -45.640 -11.978 1.00 77.46  ? 153 GLY   A C   1 
ATOM   979  O  O   . GLY   A 1 132 ? -19.304 -45.876 -12.920 1.00 78.83  ? 153 GLY   A O   1 
ATOM   980  N  N   . ASP   A 1 133 ? -18.144 -46.590 -11.126 1.00 77.39  ? 154 ASP   A N   1 
ATOM   981  C  CA  . ASP   A 1 133 ? -18.685 -47.944 -11.208 1.00 77.41  ? 154 ASP   A CA  1 
ATOM   982  C  C   . ASP   A 1 133 ? -20.174 -47.965 -10.887 1.00 77.88  ? 154 ASP   A C   1 
ATOM   983  O  O   . ASP   A 1 133 ? -20.944 -48.687 -11.530 1.00 80.03  ? 154 ASP   A O   1 
ATOM   984  C  CB  . ASP   A 1 133 ? -17.921 -48.874 -10.264 1.00 77.02  ? 154 ASP   A CB  1 
ATOM   985  C  CG  . ASP   A 1 133 ? -16.498 -49.122 -10.718 1.00 80.99  ? 154 ASP   A CG  1 
ATOM   986  O  OD1 . ASP   A 1 133 ? -16.266 -49.171 -11.944 1.00 83.33  ? 154 ASP   A OD1 1 
ATOM   987  O  OD2 . ASP   A 1 133 ? -15.613 -49.264 -9.848  1.00 77.53  ? 154 ASP   A OD2 1 
ATOM   988  N  N   . VAL   A 1 134 ? -20.596 -47.189 -9.884  1.00 77.29  ? 155 VAL   A N   1 
ATOM   989  C  CA  . VAL   A 1 134 ? -22.020 -47.081 -9.577  1.00 75.00  ? 155 VAL   A CA  1 
ATOM   990  C  C   . VAL   A 1 134 ? -22.778 -46.528 -10.773 1.00 75.85  ? 155 VAL   A C   1 
ATOM   991  O  O   . VAL   A 1 134 ? -23.930 -46.905 -11.022 1.00 76.19  ? 155 VAL   A O   1 
ATOM   992  C  CB  . VAL   A 1 134 ? -22.234 -46.207 -8.325  1.00 71.97  ? 155 VAL   A CB  1 
ATOM   993  C  CG1 . VAL   A 1 134 ? -23.710 -46.147 -7.959  1.00 72.33  ? 155 VAL   A CG1 1 
ATOM   994  C  CG2 . VAL   A 1 134 ? -21.412 -46.731 -7.159  1.00 72.82  ? 155 VAL   A CG2 1 
ATOM   995  N  N   . LEU   A 1 135 ? -22.144 -45.636 -11.537 1.00 74.40  ? 156 LEU   A N   1 
ATOM   996  C  CA  . LEU   A 1 135 ? -22.806 -45.010 -12.674 1.00 75.26  ? 156 LEU   A CA  1 
ATOM   997  C  C   . LEU   A 1 135 ? -23.133 -46.029 -13.759 1.00 77.59  ? 156 LEU   A C   1 
ATOM   998  O  O   . LEU   A 1 135 ? -24.259 -46.066 -14.267 1.00 76.04  ? 156 LEU   A O   1 
ATOM   999  C  CB  . LEU   A 1 135 ? -21.926 -43.888 -13.226 1.00 72.77  ? 156 LEU   A CB  1 
ATOM   1000 C  CG  . LEU   A 1 135 ? -22.460 -43.061 -14.393 1.00 71.18  ? 156 LEU   A CG  1 
ATOM   1001 C  CD1 . LEU   A 1 135 ? -23.872 -42.586 -14.104 1.00 69.53  ? 156 LEU   A CD1 1 
ATOM   1002 C  CD2 . LEU   A 1 135 ? -21.542 -41.878 -14.642 1.00 69.74  ? 156 LEU   A CD2 1 
ATOM   1003 N  N   . VAL   A 1 136 ? -22.164 -46.876 -14.119 1.00 79.23  ? 157 VAL   A N   1 
ATOM   1004 C  CA  . VAL   A 1 136 ? -22.395 -47.830 -15.201 1.00 81.19  ? 157 VAL   A CA  1 
ATOM   1005 C  C   . VAL   A 1 136 ? -23.433 -48.871 -14.799 1.00 81.52  ? 157 VAL   A C   1 
ATOM   1006 O  O   . VAL   A 1 136 ? -24.183 -49.365 -15.650 1.00 79.56  ? 157 VAL   A O   1 
ATOM   1007 C  CB  . VAL   A 1 136 ? -21.069 -48.484 -15.646 1.00 80.81  ? 157 VAL   A CB  1 
ATOM   1008 C  CG1 . VAL   A 1 136 ? -20.046 -47.416 -16.009 1.00 79.39  ? 157 VAL   A CG1 1 
ATOM   1009 C  CG2 . VAL   A 1 136 ? -20.523 -49.414 -14.574 1.00 77.82  ? 157 VAL   A CG2 1 
ATOM   1010 N  N   . ARG   A 1 137 ? -23.497 -49.225 -13.513 1.00 79.82  ? 158 ARG   A N   1 
ATOM   1011 C  CA  . ARG   A 1 137 ? -24.501 -50.182 -13.057 1.00 81.22  ? 158 ARG   A CA  1 
ATOM   1012 C  C   . ARG   A 1 137 ? -25.908 -49.639 -13.275 1.00 82.07  ? 158 ARG   A C   1 
ATOM   1013 O  O   . ARG   A 1 137 ? -26.756 -50.301 -13.884 1.00 85.17  ? 158 ARG   A O   1 
ATOM   1014 C  CB  . ARG   A 1 137 ? -24.273 -50.519 -11.583 1.00 77.70  ? 158 ARG   A CB  1 
ATOM   1015 N  N   . ASN   A 1 138 ? -26.169 -48.423 -12.792 1.00 83.80  ? 159 ASN   A N   1 
ATOM   1016 C  CA  . ASN   A 1 138 ? -27.466 -47.798 -13.023 1.00 87.79  ? 159 ASN   A CA  1 
ATOM   1017 C  C   . ASN   A 1 138 ? -27.663 -47.443 -14.490 1.00 88.00  ? 159 ASN   A C   1 
ATOM   1018 O  O   . ASN   A 1 138 ? -28.803 -47.400 -14.969 1.00 88.33  ? 159 ASN   A O   1 
ATOM   1019 C  CB  . ASN   A 1 138 ? -27.609 -46.553 -12.146 1.00 86.16  ? 159 ASN   A CB  1 
ATOM   1020 C  CG  . ASN   A 1 138 ? -27.614 -46.880 -10.665 1.00 87.08  ? 159 ASN   A CG  1 
ATOM   1021 O  OD1 . ASN   A 1 138 ? -27.461 -48.037 -10.272 1.00 88.31  ? 159 ASN   A OD1 1 
ATOM   1022 N  ND2 . ASN   A 1 138 ? -27.784 -45.858 -9.833  1.00 85.56  ? 159 ASN   A ND2 1 
ATOM   1023 N  N   . LEU   A 1 139 ? -26.572 -47.185 -15.215 1.00 86.53  ? 160 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 139 ? -26.664 -46.918 -16.646 1.00 86.54  ? 160 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 139 ? -26.945 -48.183 -17.445 1.00 86.89  ? 160 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 139 ? -27.614 -48.118 -18.482 1.00 86.17  ? 160 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 139 ? -25.375 -46.257 -17.141 1.00 83.47  ? 160 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 139 ? -25.358 -45.711 -18.568 1.00 83.40  ? 160 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 139 ? -26.557 -44.809 -18.804 1.00 83.63  ? 160 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 139 ? -24.062 -44.959 -18.831 1.00 81.27  ? 160 LEU   A CD2 1 
ATOM   1031 N  N   . ARG   A 1 140 ? -26.444 -49.332 -16.983 1.00 86.98  ? 161 ARG   A N   1 
ATOM   1032 C  CA  . ARG   A 1 140 ? -26.769 -50.596 -17.635 1.00 89.04  ? 161 ARG   A CA  1 
ATOM   1033 C  C   . ARG   A 1 140 ? -28.259 -50.891 -17.534 1.00 89.64  ? 161 ARG   A C   1 
ATOM   1034 O  O   . ARG   A 1 140 ? -28.866 -51.403 -18.481 1.00 91.74  ? 161 ARG   A O   1 
ATOM   1035 C  CB  . ARG   A 1 140 ? -25.953 -51.732 -17.015 1.00 85.83  ? 161 ARG   A CB  1 
ATOM   1036 C  CG  . ARG   A 1 140 ? -25.879 -52.992 -17.865 1.00 84.27  ? 161 ARG   A CG  1 
ATOM   1037 C  CD  . ARG   A 1 140 ? -24.486 -53.173 -18.446 1.00 79.03  ? 161 ARG   A CD  1 
ATOM   1038 N  NE  . ARG   A 1 140 ? -23.469 -53.216 -17.401 1.00 76.06  ? 161 ARG   A NE  1 
ATOM   1039 C  CZ  . ARG   A 1 140 ? -22.163 -53.256 -17.626 1.00 78.44  ? 161 ARG   A CZ  1 
ATOM   1040 N  NH1 . ARG   A 1 140 ? -21.673 -53.258 -18.855 1.00 77.04  ? 161 ARG   A NH1 1 
ATOM   1041 N  NH2 . ARG   A 1 140 ? -21.328 -53.294 -16.592 1.00 76.09  ? 161 ARG   A NH2 1 
ATOM   1042 N  N   . ARG   A 1 141 ? -28.863 -50.570 -16.386 1.00 88.25  ? 162 ARG   A N   1 
ATOM   1043 C  CA  . ARG   A 1 141 ? -30.302 -50.745 -16.223 1.00 90.01  ? 162 ARG   A CA  1 
ATOM   1044 C  C   . ARG   A 1 141 ? -31.073 -49.914 -17.240 1.00 93.32  ? 162 ARG   A C   1 
ATOM   1045 O  O   . ARG   A 1 141 ? -32.032 -50.398 -17.852 1.00 94.21  ? 162 ARG   A O   1 
ATOM   1046 C  CB  . ARG   A 1 141 ? -30.710 -50.366 -14.799 1.00 90.48  ? 162 ARG   A CB  1 
ATOM   1047 C  CG  . ARG   A 1 141 ? -31.922 -51.107 -14.266 1.00 91.28  ? 162 ARG   A CG  1 
ATOM   1048 C  CD  . ARG   A 1 141 ? -32.315 -50.591 -12.889 1.00 90.94  ? 162 ARG   A CD  1 
ATOM   1049 N  NE  . ARG   A 1 141 ? -31.154 -50.314 -12.050 1.00 91.82  ? 162 ARG   A NE  1 
ATOM   1050 C  CZ  . ARG   A 1 141 ? -30.562 -51.205 -11.266 1.00 89.50  ? 162 ARG   A CZ  1 
ATOM   1051 N  NH1 . ARG   A 1 141 ? -30.992 -52.454 -11.190 1.00 88.59  ? 162 ARG   A NH1 1 
ATOM   1052 N  NH2 . ARG   A 1 141 ? -29.511 -50.834 -10.541 1.00 88.33  ? 162 ARG   A NH2 1 
ATOM   1053 N  N   . GLU   A 1 142 ? -30.662 -48.659 -17.438 1.00 95.58  ? 163 GLU   A N   1 
ATOM   1054 C  CA  . GLU   A 1 142 ? -31.318 -47.798 -18.414 1.00 93.35  ? 163 GLU   A CA  1 
ATOM   1055 C  C   . GLU   A 1 142 ? -31.051 -48.237 -19.848 1.00 93.88  ? 163 GLU   A C   1 
ATOM   1056 O  O   . GLU   A 1 142 ? -31.809 -47.862 -20.748 1.00 91.88  ? 163 GLU   A O   1 
ATOM   1057 C  CB  . GLU   A 1 142 ? -30.869 -46.349 -18.219 1.00 89.58  ? 163 GLU   A CB  1 
ATOM   1058 N  N   . ALA   A 1 143 ? -29.991 -49.014 -20.082 1.00 93.94  ? 164 ALA   A N   1 
ATOM   1059 C  CA  . ALA   A 1 143 ? -29.724 -49.521 -21.424 1.00 93.36  ? 164 ALA   A CA  1 
ATOM   1060 C  C   . ALA   A 1 143 ? -30.511 -50.797 -21.697 1.00 94.11  ? 164 ALA   A C   1 
ATOM   1061 O  O   . ALA   A 1 143 ? -31.101 -50.955 -22.773 1.00 95.25  ? 164 ALA   A O   1 
ATOM   1062 C  CB  . ALA   A 1 143 ? -28.225 -49.762 -21.608 1.00 91.38  ? 164 ALA   A CB  1 
ATOM   1063 N  N   . GLU   A 1 144 ? -30.529 -51.721 -20.732 1.00 96.45  ? 165 GLU   A N   1 
ATOM   1064 C  CA  . GLU   A 1 144 ? -31.294 -52.953 -20.898 1.00 97.36  ? 165 GLU   A CA  1 
ATOM   1065 C  C   . GLU   A 1 144 ? -32.789 -52.676 -20.987 1.00 97.39  ? 165 GLU   A C   1 
ATOM   1066 O  O   . GLU   A 1 144 ? -33.533 -53.466 -21.580 1.00 96.75  ? 165 GLU   A O   1 
ATOM   1067 C  CB  . GLU   A 1 144 ? -30.990 -53.916 -19.750 1.00 93.90  ? 165 GLU   A CB  1 
ATOM   1068 C  CG  . GLU   A 1 144 ? -29.559 -54.433 -19.746 1.00 94.19  ? 165 GLU   A CG  1 
ATOM   1069 C  CD  . GLU   A 1 144 ? -29.239 -55.271 -18.523 1.00 97.46  ? 165 GLU   A CD  1 
ATOM   1070 O  OE1 . GLU   A 1 144 ? -29.920 -55.103 -17.490 1.00 98.11  ? 165 GLU   A OE1 1 
ATOM   1071 O  OE2 . GLU   A 1 144 ? -28.307 -56.100 -18.596 1.00 96.98  ? 165 GLU   A OE2 1 
ATOM   1072 N  N   . THR   A 1 145 ? -33.246 -51.563 -20.407 1.00 96.19  ? 166 THR   A N   1 
ATOM   1073 C  CA  . THR   A 1 145 ? -34.636 -51.153 -20.568 1.00 97.70  ? 166 THR   A CA  1 
ATOM   1074 C  C   . THR   A 1 145 ? -34.956 -50.795 -22.015 1.00 97.64  ? 166 THR   A C   1 
ATOM   1075 O  O   . THR   A 1 145 ? -36.130 -50.803 -22.403 1.00 95.48  ? 166 THR   A O   1 
ATOM   1076 C  CB  . THR   A 1 145 ? -34.938 -49.967 -19.645 1.00 98.26  ? 166 THR   A CB  1 
ATOM   1077 O  OG1 . THR   A 1 145 ? -34.417 -50.235 -18.337 1.00 95.82  ? 166 THR   A OG1 1 
ATOM   1078 C  CG2 . THR   A 1 145 ? -36.439 -49.732 -19.534 1.00 99.32  ? 166 THR   A CG2 1 
ATOM   1079 N  N   . GLY   A 1 146 ? -33.939 -50.506 -22.824 1.00 96.98  ? 167 GLY   A N   1 
ATOM   1080 C  CA  . GLY   A 1 146 ? -34.163 -50.154 -24.215 1.00 97.72  ? 167 GLY   A CA  1 
ATOM   1081 C  C   . GLY   A 1 146 ? -34.911 -48.855 -24.403 1.00 97.80  ? 167 GLY   A C   1 
ATOM   1082 O  O   . GLY   A 1 146 ? -35.680 -48.720 -25.361 1.00 97.26  ? 167 GLY   A O   1 
ATOM   1083 N  N   . LYS   A 1 147 ? -34.703 -47.889 -23.512 1.00 96.47  ? 168 LYS   A N   1 
ATOM   1084 C  CA  . LYS   A 1 147 ? -35.374 -46.607 -23.590 1.00 96.58  ? 168 LYS   A CA  1 
ATOM   1085 C  C   . LYS   A 1 147 ? -34.353 -45.485 -23.723 1.00 94.51  ? 168 LYS   A C   1 
ATOM   1086 O  O   . LYS   A 1 147 ? -33.247 -45.579 -23.179 1.00 93.91  ? 168 LYS   A O   1 
ATOM   1087 C  CB  . LYS   A 1 147 ? -36.243 -46.356 -22.349 1.00 95.22  ? 168 LYS   A CB  1 
ATOM   1088 N  N   . PRO   A 1 148 ? -34.687 -44.425 -24.457 1.00 94.76  ? 169 PRO   A N   1 
ATOM   1089 C  CA  . PRO   A 1 148 ? -33.795 -43.261 -24.525 1.00 92.43  ? 169 PRO   A CA  1 
ATOM   1090 C  C   . PRO   A 1 148 ? -33.517 -42.710 -23.133 1.00 91.09  ? 169 PRO   A C   1 
ATOM   1091 O  O   . PRO   A 1 148 ? -34.425 -42.556 -22.314 1.00 93.63  ? 169 PRO   A O   1 
ATOM   1092 C  CB  . PRO   A 1 148 ? -34.581 -42.266 -25.387 1.00 89.93  ? 169 PRO   A CB  1 
ATOM   1093 C  CG  . PRO   A 1 148 ? -35.472 -43.129 -26.227 1.00 94.23  ? 169 PRO   A CG  1 
ATOM   1094 C  CD  . PRO   A 1 148 ? -35.844 -44.295 -25.358 1.00 95.95  ? 169 PRO   A CD  1 
ATOM   1095 N  N   . VAL   A 1 149 ? -32.248 -42.412 -22.875 1.00 88.26  ? 170 VAL   A N   1 
ATOM   1096 C  CA  . VAL   A 1 149 ? -31.777 -42.032 -21.549 1.00 86.87  ? 170 VAL   A CA  1 
ATOM   1097 C  C   . VAL   A 1 149 ? -31.563 -40.528 -21.513 1.00 84.73  ? 170 VAL   A C   1 
ATOM   1098 O  O   . VAL   A 1 149 ? -30.935 -39.960 -22.414 1.00 85.47  ? 170 VAL   A O   1 
ATOM   1099 C  CB  . VAL   A 1 149 ? -30.482 -42.778 -21.186 1.00 83.68  ? 170 VAL   A CB  1 
ATOM   1100 C  CG1 . VAL   A 1 149 ? -29.964 -42.321 -19.832 1.00 79.36  ? 170 VAL   A CG1 1 
ATOM   1101 C  CG2 . VAL   A 1 149 ? -30.715 -44.280 -21.197 1.00 88.27  ? 170 VAL   A CG2 1 
ATOM   1102 N  N   . THR   A 1 150 ? -32.084 -39.882 -20.473 1.00 81.64  ? 171 THR   A N   1 
ATOM   1103 C  CA  . THR   A 1 150 ? -31.831 -38.464 -20.257 1.00 80.59  ? 171 THR   A CA  1 
ATOM   1104 C  C   . THR   A 1 150 ? -30.483 -38.288 -19.569 1.00 77.78  ? 171 THR   A C   1 
ATOM   1105 O  O   . THR   A 1 150 ? -30.238 -38.869 -18.507 1.00 76.12  ? 171 THR   A O   1 
ATOM   1106 C  CB  . THR   A 1 150 ? -32.942 -37.838 -19.419 1.00 80.58  ? 171 THR   A CB  1 
ATOM   1107 O  OG1 . THR   A 1 150 ? -34.191 -37.948 -20.115 1.00 80.50  ? 171 THR   A OG1 1 
ATOM   1108 C  CG2 . THR   A 1 150 ? -32.643 -36.370 -19.155 1.00 79.54  ? 171 THR   A CG2 1 
ATOM   1109 N  N   . LEU   A 1 151 ? -29.609 -37.486 -20.181 1.00 77.58  ? 172 LEU   A N   1 
ATOM   1110 C  CA  . LEU   A 1 151 ? -28.242 -37.359 -19.684 1.00 75.42  ? 172 LEU   A CA  1 
ATOM   1111 C  C   . LEU   A 1 151 ? -28.190 -36.601 -18.363 1.00 73.92  ? 172 LEU   A C   1 
ATOM   1112 O  O   . LEU   A 1 151 ? -27.389 -36.937 -17.482 1.00 73.78  ? 172 LEU   A O   1 
ATOM   1113 C  CB  . LEU   A 1 151 ? -27.369 -36.673 -20.733 1.00 75.91  ? 172 LEU   A CB  1 
ATOM   1114 C  CG  . LEU   A 1 151 ? -27.311 -37.373 -22.091 1.00 77.93  ? 172 LEU   A CG  1 
ATOM   1115 C  CD1 . LEU   A 1 151 ? -26.334 -36.668 -23.016 1.00 77.03  ? 172 LEU   A CD1 1 
ATOM   1116 C  CD2 . LEU   A 1 151 ? -26.936 -38.837 -21.918 1.00 73.91  ? 172 LEU   A CD2 1 
ATOM   1117 N  N   . LYS   A 1 152 ? -29.028 -35.573 -18.208 1.00 71.98  ? 173 LYS   A N   1 
ATOM   1118 C  CA  . LYS   A 1 152 ? -28.998 -34.761 -16.997 1.00 70.83  ? 173 LYS   A CA  1 
ATOM   1119 C  C   . LYS   A 1 152 ? -29.307 -35.571 -15.744 1.00 70.63  ? 173 LYS   A C   1 
ATOM   1120 O  O   . LYS   A 1 152 ? -28.899 -35.173 -14.646 1.00 68.42  ? 173 LYS   A O   1 
ATOM   1121 C  CB  . LYS   A 1 152 ? -29.987 -33.600 -17.119 1.00 71.44  ? 173 LYS   A CB  1 
ATOM   1122 N  N   . ASP   A 1 153 ? -30.005 -36.699 -15.881 1.00 73.38  ? 174 ASP   A N   1 
ATOM   1123 C  CA  . ASP   A 1 153 ? -30.401 -37.475 -14.711 1.00 71.71  ? 174 ASP   A CA  1 
ATOM   1124 C  C   . ASP   A 1 153 ? -29.292 -38.414 -14.248 1.00 70.18  ? 174 ASP   A C   1 
ATOM   1125 O  O   . ASP   A 1 153 ? -29.020 -38.508 -13.046 1.00 69.35  ? 174 ASP   A O   1 
ATOM   1126 C  CB  . ASP   A 1 153 ? -31.676 -38.261 -15.020 1.00 72.42  ? 174 ASP   A CB  1 
ATOM   1127 C  CG  . ASP   A 1 153 ? -32.804 -37.367 -15.502 1.00 79.48  ? 174 ASP   A CG  1 
ATOM   1128 O  OD1 . ASP   A 1 153 ? -32.807 -36.169 -15.145 1.00 80.76  ? 174 ASP   A OD1 1 
ATOM   1129 O  OD2 . ASP   A 1 153 ? -33.685 -37.861 -16.236 1.00 82.40  ? 174 ASP   A OD2 1 
ATOM   1130 N  N   . VAL   A 1 154 ? -28.650 -39.123 -15.179 1.00 69.97  ? 175 VAL   A N   1 
ATOM   1131 C  CA  . VAL   A 1 154 ? -27.558 -40.017 -14.802 1.00 71.87  ? 175 VAL   A CA  1 
ATOM   1132 C  C   . VAL   A 1 154 ? -26.334 -39.219 -14.369 1.00 68.97  ? 175 VAL   A C   1 
ATOM   1133 O  O   . VAL   A 1 154 ? -25.662 -39.570 -13.392 1.00 67.30  ? 175 VAL   A O   1 
ATOM   1134 C  CB  . VAL   A 1 154 ? -27.233 -40.983 -15.955 1.00 73.79  ? 175 VAL   A CB  1 
ATOM   1135 C  CG1 . VAL   A 1 154 ? -28.203 -42.154 -15.951 1.00 72.82  ? 175 VAL   A CG1 1 
ATOM   1136 C  CG2 . VAL   A 1 154 ? -27.286 -40.253 -17.289 1.00 73.63  ? 175 VAL   A CG2 1 
ATOM   1137 N  N   . PHE   A 1 155 ? -26.021 -38.137 -15.086 1.00 69.44  ? 176 PHE   A N   1 
ATOM   1138 C  CA  . PHE   A 1 155 ? -24.884 -37.306 -14.705 1.00 67.76  ? 176 PHE   A CA  1 
ATOM   1139 C  C   . PHE   A 1 155 ? -25.193 -36.455 -13.481 1.00 67.49  ? 176 PHE   A C   1 
ATOM   1140 O  O   . PHE   A 1 155 ? -24.282 -36.121 -12.715 1.00 66.01  ? 176 PHE   A O   1 
ATOM   1141 C  CB  . PHE   A 1 155 ? -24.462 -36.425 -15.877 1.00 68.25  ? 176 PHE   A CB  1 
ATOM   1142 C  CG  . PHE   A 1 155 ? -23.874 -37.192 -17.021 1.00 67.98  ? 176 PHE   A CG  1 
ATOM   1143 C  CD1 . PHE   A 1 155 ? -22.985 -38.227 -16.789 1.00 66.94  ? 176 PHE   A CD1 1 
ATOM   1144 C  CD2 . PHE   A 1 155 ? -24.223 -36.892 -18.326 1.00 68.76  ? 176 PHE   A CD2 1 
ATOM   1145 C  CE1 . PHE   A 1 155 ? -22.444 -38.940 -17.838 1.00 66.99  ? 176 PHE   A CE1 1 
ATOM   1146 C  CE2 . PHE   A 1 155 ? -23.686 -37.604 -19.380 1.00 68.46  ? 176 PHE   A CE2 1 
ATOM   1147 C  CZ  . PHE   A 1 155 ? -22.796 -38.629 -19.134 1.00 68.49  ? 176 PHE   A CZ  1 
ATOM   1148 N  N   . GLY   A 1 156 ? -26.459 -36.081 -13.290 1.00 66.61  ? 177 GLY   A N   1 
ATOM   1149 C  CA  . GLY   A 1 156 ? -26.836 -35.409 -12.058 1.00 65.80  ? 177 GLY   A CA  1 
ATOM   1150 C  C   . GLY   A 1 156 ? -26.630 -36.289 -10.841 1.00 68.77  ? 177 GLY   A C   1 
ATOM   1151 O  O   . GLY   A 1 156 ? -26.082 -35.852 -9.826  1.00 68.30  ? 177 GLY   A O   1 
ATOM   1152 N  N   . ALA   A 1 157 ? -27.053 -37.553 -10.936 1.00 71.13  ? 178 ALA   A N   1 
ATOM   1153 C  CA  . ALA   A 1 157 ? -26.877 -38.482 -9.825  1.00 68.70  ? 178 ALA   A CA  1 
ATOM   1154 C  C   . ALA   A 1 157 ? -25.407 -38.804 -9.589  1.00 67.56  ? 178 ALA   A C   1 
ATOM   1155 O  O   . ALA   A 1 157 ? -24.994 -38.989 -8.439  1.00 68.37  ? 178 ALA   A O   1 
ATOM   1156 C  CB  . ALA   A 1 157 ? -27.673 -39.760 -10.078 1.00 72.36  ? 178 ALA   A CB  1 
ATOM   1157 N  N   . TYR   A 1 158 ? -24.605 -38.885 -10.654 1.00 66.47  ? 179 TYR   A N   1 
ATOM   1158 C  CA  . TYR   A 1 158 ? -23.171 -39.085 -10.475 1.00 67.25  ? 179 TYR   A CA  1 
ATOM   1159 C  C   . TYR   A 1 158 ? -22.545 -37.903 -9.745  1.00 69.90  ? 179 TYR   A C   1 
ATOM   1160 O  O   . TYR   A 1 158 ? -21.747 -38.081 -8.818  1.00 68.65  ? 179 TYR   A O   1 
ATOM   1161 C  CB  . TYR   A 1 158 ? -22.488 -39.302 -11.824 1.00 64.98  ? 179 TYR   A CB  1 
ATOM   1162 C  CG  . TYR   A 1 158 ? -20.976 -39.264 -11.739 1.00 67.88  ? 179 TYR   A CG  1 
ATOM   1163 C  CD1 . TYR   A 1 158 ? -20.263 -40.341 -11.226 1.00 70.66  ? 179 TYR   A CD1 1 
ATOM   1164 C  CD2 . TYR   A 1 158 ? -20.262 -38.148 -12.165 1.00 67.60  ? 179 TYR   A CD2 1 
ATOM   1165 C  CE1 . TYR   A 1 158 ? -18.883 -40.310 -11.141 1.00 70.46  ? 179 TYR   A CE1 1 
ATOM   1166 C  CE2 . TYR   A 1 158 ? -18.882 -38.108 -12.083 1.00 66.47  ? 179 TYR   A CE2 1 
ATOM   1167 C  CZ  . TYR   A 1 158 ? -18.199 -39.193 -11.572 1.00 67.11  ? 179 TYR   A CZ  1 
ATOM   1168 O  OH  . TYR   A 1 158 ? -16.826 -39.160 -11.490 1.00 68.87  ? 179 TYR   A OH  1 
ATOM   1169 N  N   . SER   A 1 159 ? -22.907 -36.683 -10.150 1.00 69.31  ? 180 SER   A N   1 
ATOM   1170 C  CA  . SER   A 1 159 ? -22.396 -35.493 -9.480  1.00 67.59  ? 180 SER   A CA  1 
ATOM   1171 C  C   . SER   A 1 159 ? -22.841 -35.454 -8.026  1.00 68.66  ? 180 SER   A C   1 
ATOM   1172 O  O   . SER   A 1 159 ? -22.068 -35.069 -7.141  1.00 68.37  ? 180 SER   A O   1 
ATOM   1173 C  CB  . SER   A 1 159 ? -22.857 -34.238 -10.220 1.00 66.45  ? 180 SER   A CB  1 
ATOM   1174 O  OG  . SER   A 1 159 ? -22.395 -33.068 -9.571  1.00 68.49  ? 180 SER   A OG  1 
ATOM   1175 N  N   . MET   A 1 160 ? -24.088 -35.849 -7.764  1.00 68.80  ? 181 MET   A N   1 
ATOM   1176 C  CA  . MET   A 1 160 ? -24.575 -35.935 -6.392  1.00 68.88  ? 181 MET   A CA  1 
ATOM   1177 C  C   . MET   A 1 160 ? -23.703 -36.865 -5.561  1.00 73.03  ? 181 MET   A C   1 
ATOM   1178 O  O   . MET   A 1 160 ? -23.297 -36.525 -4.444  1.00 74.56  ? 181 MET   A O   1 
ATOM   1179 C  CB  . MET   A 1 160 ? -26.023 -36.422 -6.386  1.00 72.09  ? 181 MET   A CB  1 
ATOM   1180 C  CG  . MET   A 1 160 ? -26.662 -36.439 -5.011  1.00 78.10  ? 181 MET   A CG  1 
ATOM   1181 S  SD  . MET   A 1 160 ? -27.380 -34.841 -4.594  1.00 82.88  ? 181 MET   A SD  1 
ATOM   1182 C  CE  . MET   A 1 160 ? -28.644 -34.719 -5.856  1.00 79.39  ? 181 MET   A CE  1 
ATOM   1183 N  N   . ASP   A 1 161 ? -23.402 -38.049 -6.097  1.00 73.67  ? 182 ASP   A N   1 
ATOM   1184 C  CA  . ASP   A 1 161 ? -22.589 -39.011 -5.361  1.00 71.30  ? 182 ASP   A CA  1 
ATOM   1185 C  C   . ASP   A 1 161 ? -21.186 -38.474 -5.115  1.00 72.23  ? 182 ASP   A C   1 
ATOM   1186 O  O   . ASP   A 1 161 ? -20.606 -38.694 -4.045  1.00 71.47  ? 182 ASP   A O   1 
ATOM   1187 C  CB  . ASP   A 1 161 ? -22.529 -40.335 -6.122  1.00 75.05  ? 182 ASP   A CB  1 
ATOM   1188 C  CG  . ASP   A 1 161 ? -23.898 -40.934 -6.357  1.00 77.08  ? 182 ASP   A CG  1 
ATOM   1189 O  OD1 . ASP   A 1 161 ? -24.895 -40.283 -5.985  1.00 76.55  ? 182 ASP   A OD1 1 
ATOM   1190 O  OD2 . ASP   A 1 161 ? -23.975 -42.052 -6.911  1.00 76.09  ? 182 ASP   A OD2 1 
ATOM   1191 N  N   . VAL   A 1 162 ? -20.622 -37.775 -6.100  1.00 70.13  ? 183 VAL   A N   1 
ATOM   1192 C  CA  . VAL   A 1 162 ? -19.258 -37.273 -5.978  1.00 70.02  ? 183 VAL   A CA  1 
ATOM   1193 C  C   . VAL   A 1 162 ? -19.170 -36.215 -4.883  1.00 72.50  ? 183 VAL   A C   1 
ATOM   1194 O  O   . VAL   A 1 162 ? -18.274 -36.256 -4.030  1.00 73.79  ? 183 VAL   A O   1 
ATOM   1195 C  CB  . VAL   A 1 162 ? -18.770 -36.736 -7.335  1.00 66.88  ? 183 VAL   A CB  1 
ATOM   1196 C  CG1 . VAL   A 1 162 ? -17.565 -35.829 -7.155  1.00 66.88  ? 183 VAL   A CG1 1 
ATOM   1197 C  CG2 . VAL   A 1 162 ? -18.441 -37.895 -8.265  1.00 69.21  ? 183 VAL   A CG2 1 
ATOM   1198 N  N   . ILE   A 1 163 ? -20.101 -35.258 -4.881  1.00 69.32  ? 184 ILE   A N   1 
ATOM   1199 C  CA  . ILE   A 1 163 ? -20.038 -34.168 -3.910  1.00 73.25  ? 184 ILE   A CA  1 
ATOM   1200 C  C   . ILE   A 1 163 ? -20.285 -34.688 -2.499  1.00 74.42  ? 184 ILE   A C   1 
ATOM   1201 O  O   . ILE   A 1 163 ? -19.517 -34.401 -1.575  1.00 74.87  ? 184 ILE   A O   1 
ATOM   1202 C  CB  . ILE   A 1 163 ? -21.038 -33.056 -4.274  1.00 71.57  ? 184 ILE   A CB  1 
ATOM   1203 C  CG1 . ILE   A 1 163 ? -20.761 -32.519 -5.677  1.00 69.23  ? 184 ILE   A CG1 1 
ATOM   1204 C  CG2 . ILE   A 1 163 ? -20.963 -31.934 -3.256  1.00 67.48  ? 184 ILE   A CG2 1 
ATOM   1205 C  CD1 . ILE   A 1 163 ? -21.712 -31.425 -6.100  1.00 64.90  ? 184 ILE   A CD1 1 
ATOM   1206 N  N   . THR   A 1 164 ? -21.352 -35.473 -2.315  1.00 71.64  ? 185 THR   A N   1 
ATOM   1207 C  CA  . THR   A 1 164 ? -21.700 -35.942 -0.976  1.00 74.26  ? 185 THR   A CA  1 
ATOM   1208 C  C   . THR   A 1 164 ? -20.568 -36.745 -0.349  1.00 78.48  ? 185 THR   A C   1 
ATOM   1209 O  O   . THR   A 1 164 ? -20.450 -36.796 0.881   1.00 81.46  ? 185 THR   A O   1 
ATOM   1210 C  CB  . THR   A 1 164 ? -22.975 -36.787 -1.023  1.00 76.17  ? 185 THR   A CB  1 
ATOM   1211 O  OG1 . THR   A 1 164 ? -22.819 -37.844 -1.978  1.00 77.81  ? 185 THR   A OG1 1 
ATOM   1212 C  CG2 . THR   A 1 164 ? -24.173 -35.930 -1.397  1.00 79.69  ? 185 THR   A CG2 1 
ATOM   1213 N  N   . SER   A 1 165 ? -19.720 -37.362 -1.171  1.00 79.87  ? 186 SER   A N   1 
ATOM   1214 C  CA  . SER   A 1 165 ? -18.607 -38.162 -0.677  1.00 79.04  ? 186 SER   A CA  1 
ATOM   1215 C  C   . SER   A 1 165 ? -17.335 -37.334 -0.521  1.00 80.65  ? 186 SER   A C   1 
ATOM   1216 O  O   . SER   A 1 165 ? -16.674 -37.396 0.521   1.00 82.41  ? 186 SER   A O   1 
ATOM   1217 C  CB  . SER   A 1 165 ? -18.364 -39.344 -1.619  1.00 77.36  ? 186 SER   A CB  1 
ATOM   1218 O  OG  . SER   A 1 165 ? -19.591 -39.892 -2.068  1.00 80.35  ? 186 SER   A OG  1 
ATOM   1219 N  N   . THR   A 1 166 ? -16.983 -36.553 -1.546  1.00 79.43  ? 187 THR   A N   1 
ATOM   1220 C  CA  . THR   A 1 166 ? -15.760 -35.760 -1.503  1.00 77.10  ? 187 THR   A CA  1 
ATOM   1221 C  C   . THR   A 1 166 ? -15.877 -34.540 -0.601  1.00 78.53  ? 187 THR   A C   1 
ATOM   1222 O  O   . THR   A 1 166 ? -14.849 -33.967 -0.228  1.00 83.27  ? 187 THR   A O   1 
ATOM   1223 C  CB  . THR   A 1 166 ? -15.365 -35.304 -2.909  1.00 74.60  ? 187 THR   A CB  1 
ATOM   1224 O  OG1 . THR   A 1 166 ? -16.505 -34.740 -3.570  1.00 74.72  ? 187 THR   A OG1 1 
ATOM   1225 C  CG2 . THR   A 1 166 ? -14.830 -36.469 -3.720  1.00 73.46  ? 187 THR   A CG2 1 
ATOM   1226 N  N   . SER   A 1 167 ? -17.092 -34.121 -0.253  1.00 79.18  ? 188 SER   A N   1 
ATOM   1227 C  CA  . SER   A 1 167 ? -17.289 -32.944 0.584   1.00 80.95  ? 188 SER   A CA  1 
ATOM   1228 C  C   . SER   A 1 167 ? -17.599 -33.286 2.034   1.00 83.39  ? 188 SER   A C   1 
ATOM   1229 O  O   . SER   A 1 167 ? -17.050 -32.655 2.940   1.00 83.02  ? 188 SER   A O   1 
ATOM   1230 C  CB  . SER   A 1 167 ? -18.415 -32.070 0.020   1.00 80.18  ? 188 SER   A CB  1 
ATOM   1231 O  OG  . SER   A 1 167 ? -18.534 -30.855 0.738   1.00 83.19  ? 188 SER   A OG  1 
ATOM   1232 N  N   . PHE   A 1 168 ? -18.462 -34.270 2.279   1.00 85.20  ? 189 PHE   A N   1 
ATOM   1233 C  CA  . PHE   A 1 168 ? -18.878 -34.615 3.632   1.00 85.55  ? 189 PHE   A CA  1 
ATOM   1234 C  C   . PHE   A 1 168 ? -18.569 -36.049 4.028   1.00 85.47  ? 189 PHE   A C   1 
ATOM   1235 O  O   . PHE   A 1 168 ? -18.359 -36.312 5.214   1.00 86.44  ? 189 PHE   A O   1 
ATOM   1236 C  CB  . PHE   A 1 168 ? -20.385 -34.372 3.802   1.00 84.18  ? 189 PHE   A CB  1 
ATOM   1237 C  CG  . PHE   A 1 168 ? -20.827 -33.000 3.382   1.00 83.07  ? 189 PHE   A CG  1 
ATOM   1238 C  CD1 . PHE   A 1 168 ? -20.090 -31.881 3.733   1.00 82.30  ? 189 PHE   A CD1 1 
ATOM   1239 C  CD2 . PHE   A 1 168 ? -21.974 -32.832 2.626   1.00 81.93  ? 189 PHE   A CD2 1 
ATOM   1240 C  CE1 . PHE   A 1 168 ? -20.493 -30.620 3.343   1.00 82.83  ? 189 PHE   A CE1 1 
ATOM   1241 C  CE2 . PHE   A 1 168 ? -22.381 -31.575 2.234   1.00 82.24  ? 189 PHE   A CE2 1 
ATOM   1242 C  CZ  . PHE   A 1 168 ? -21.640 -30.467 2.593   1.00 83.26  ? 189 PHE   A CZ  1 
ATOM   1243 N  N   . GLY   A 1 169 ? -18.537 -36.979 3.078   1.00 84.38  ? 190 GLY   A N   1 
ATOM   1244 C  CA  . GLY   A 1 169 ? -18.280 -38.370 3.375   1.00 80.88  ? 190 GLY   A CA  1 
ATOM   1245 C  C   . GLY   A 1 169 ? -19.507 -39.251 3.438   1.00 80.04  ? 190 GLY   A C   1 
ATOM   1246 O  O   . GLY   A 1 169 ? -19.370 -40.450 3.710   1.00 85.33  ? 190 GLY   A O   1 
ATOM   1247 N  N   . VAL   A 1 170 ? -20.699 -38.704 3.200   1.00 80.00  ? 191 VAL   A N   1 
ATOM   1248 C  CA  . VAL   A 1 170 ? -21.924 -39.502 3.209   1.00 82.08  ? 191 VAL   A CA  1 
ATOM   1249 C  C   . VAL   A 1 170 ? -21.963 -40.287 1.900   1.00 81.13  ? 191 VAL   A C   1 
ATOM   1250 O  O   . VAL   A 1 170 ? -22.354 -39.769 0.852   1.00 81.21  ? 191 VAL   A O   1 
ATOM   1251 C  CB  . VAL   A 1 170 ? -23.174 -38.640 3.404   1.00 81.45  ? 191 VAL   A CB  1 
ATOM   1252 C  CG1 . VAL   A 1 170 ? -23.369 -38.329 4.879   1.00 85.74  ? 191 VAL   A CG1 1 
ATOM   1253 C  CG2 . VAL   A 1 170 ? -23.078 -37.345 2.611   1.00 84.53  ? 191 VAL   A CG2 1 
ATOM   1254 N  N   . ASN   A 1 171 ? -21.550 -41.551 1.961   1.00 80.76  ? 192 ASN   A N   1 
ATOM   1255 C  CA  . ASN   A 1 171 ? -21.458 -42.410 0.786   1.00 79.88  ? 192 ASN   A CA  1 
ATOM   1256 C  C   . ASN   A 1 171 ? -22.823 -43.034 0.522   1.00 78.62  ? 192 ASN   A C   1 
ATOM   1257 O  O   . ASN   A 1 171 ? -23.235 -43.964 1.223   1.00 83.29  ? 192 ASN   A O   1 
ATOM   1258 C  CB  . ASN   A 1 171 ? -20.390 -43.480 0.992   1.00 80.60  ? 192 ASN   A CB  1 
ATOM   1259 C  CG  . ASN   A 1 171 ? -18.985 -42.909 0.980   1.00 84.29  ? 192 ASN   A CG  1 
ATOM   1260 O  OD1 . ASN   A 1 171 ? -18.786 -41.711 1.181   1.00 84.91  ? 192 ASN   A OD1 1 
ATOM   1261 N  ND2 . ASN   A 1 171 ? -18.001 -43.766 0.736   1.00 87.17  ? 192 ASN   A ND2 1 
ATOM   1262 N  N   . ILE   A 1 172 ? -23.519 -42.531 -0.494  1.00 77.52  ? 193 ILE   A N   1 
ATOM   1263 C  CA  . ILE   A 1 172 ? -24.884 -42.951 -0.786  1.00 79.77  ? 193 ILE   A CA  1 
ATOM   1264 C  C   . ILE   A 1 172 ? -25.097 -42.962 -2.293  1.00 79.62  ? 193 ILE   A C   1 
ATOM   1265 O  O   . ILE   A 1 172 ? -24.719 -42.013 -2.988  1.00 78.71  ? 193 ILE   A O   1 
ATOM   1266 C  CB  . ILE   A 1 172 ? -25.918 -42.027 -0.112  1.00 83.09  ? 193 ILE   A CB  1 
ATOM   1267 C  CG1 . ILE   A 1 172 ? -25.457 -40.570 -0.194  1.00 82.62  ? 193 ILE   A CG1 1 
ATOM   1268 C  CG2 . ILE   A 1 172 ? -26.154 -42.443 1.331   1.00 85.10  ? 193 ILE   A CG2 1 
ATOM   1269 C  CD1 . ILE   A 1 172 ? -26.365 -39.597 0.526   1.00 83.25  ? 193 ILE   A CD1 1 
ATOM   1270 N  N   . ASP   A 1 173 ? -25.699 -44.037 -2.796  1.00 82.00  ? 194 ASP   A N   1 
ATOM   1271 C  CA  . ASP   A 1 173 ? -26.262 -44.019 -4.137  1.00 80.45  ? 194 ASP   A CA  1 
ATOM   1272 C  C   . ASP   A 1 173 ? -27.431 -43.040 -4.173  1.00 83.66  ? 194 ASP   A C   1 
ATOM   1273 O  O   . ASP   A 1 173 ? -28.137 -42.848 -3.180  1.00 87.10  ? 194 ASP   A O   1 
ATOM   1274 C  CB  . ASP   A 1 173 ? -26.723 -45.422 -4.541  1.00 81.08  ? 194 ASP   A CB  1 
ATOM   1275 C  CG  . ASP   A 1 173 ? -27.102 -45.521 -6.010  1.00 86.36  ? 194 ASP   A CG  1 
ATOM   1276 O  OD1 . ASP   A 1 173 ? -26.985 -44.508 -6.733  1.00 88.97  ? 194 ASP   A OD1 1 
ATOM   1277 O  OD2 . ASP   A 1 173 ? -27.514 -46.618 -6.443  1.00 84.01  ? 194 ASP   A OD2 1 
ATOM   1278 N  N   . SER   A 1 174 ? -27.623 -42.401 -5.321  1.00 83.41  ? 195 SER   A N   1 
ATOM   1279 C  CA  . SER   A 1 174 ? -28.638 -41.359 -5.425  1.00 83.55  ? 195 SER   A CA  1 
ATOM   1280 C  C   . SER   A 1 174 ? -29.746 -41.674 -6.414  1.00 86.11  ? 195 SER   A C   1 
ATOM   1281 O  O   . SER   A 1 174 ? -30.915 -41.418 -6.114  1.00 89.03  ? 195 SER   A O   1 
ATOM   1282 C  CB  . SER   A 1 174 ? -27.985 -40.022 -5.801  1.00 81.99  ? 195 SER   A CB  1 
ATOM   1283 O  OG  . SER   A 1 174 ? -27.127 -39.575 -4.765  1.00 80.52  ? 195 SER   A OG  1 
ATOM   1284 N  N   . LEU   A 1 175 ? -29.418 -42.226 -7.585  1.00 86.12  ? 196 LEU   A N   1 
ATOM   1285 C  CA  . LEU   A 1 175 ? -30.447 -42.481 -8.588  1.00 87.26  ? 196 LEU   A CA  1 
ATOM   1286 C  C   . LEU   A 1 175 ? -31.481 -43.480 -8.081  1.00 87.88  ? 196 LEU   A C   1 
ATOM   1287 O  O   . LEU   A 1 175 ? -32.687 -43.287 -8.274  1.00 89.98  ? 196 LEU   A O   1 
ATOM   1288 C  CB  . LEU   A 1 175 ? -29.810 -42.983 -9.884  1.00 86.86  ? 196 LEU   A CB  1 
ATOM   1289 C  CG  . LEU   A 1 175 ? -30.787 -43.235 -11.034 1.00 88.30  ? 196 LEU   A CG  1 
ATOM   1290 C  CD1 . LEU   A 1 175 ? -31.521 -41.954 -11.403 1.00 86.12  ? 196 LEU   A CD1 1 
ATOM   1291 C  CD2 . LEU   A 1 175 ? -30.063 -43.807 -12.241 1.00 90.18  ? 196 LEU   A CD2 1 
ATOM   1292 N  N   . ASN   A 1 176 ? -31.032 -44.548 -7.426  1.00 90.82  ? 197 ASN   A N   1 
ATOM   1293 C  CA  . ASN   A 1 176 ? -31.927 -45.560 -6.884  1.00 94.10  ? 197 ASN   A CA  1 
ATOM   1294 C  C   . ASN   A 1 176 ? -32.231 -45.358 -5.408  1.00 96.30  ? 197 ASN   A C   1 
ATOM   1295 O  O   . ASN   A 1 176 ? -32.939 -46.181 -4.819  1.00 97.88  ? 197 ASN   A O   1 
ATOM   1296 C  CB  . ASN   A 1 176 ? -31.338 -46.956 -7.105  1.00 89.12  ? 197 ASN   A CB  1 
ATOM   1297 C  CG  . ASN   A 1 176 ? -31.291 -47.341 -8.569  1.00 89.53  ? 197 ASN   A CG  1 
ATOM   1298 O  OD1 . ASN   A 1 176 ? -32.167 -46.966 -9.349  1.00 89.05  ? 197 ASN   A OD1 1 
ATOM   1299 N  ND2 . ASN   A 1 176 ? -30.263 -48.089 -8.953  1.00 87.40  ? 197 ASN   A ND2 1 
ATOM   1300 N  N   . ASN   A 1 177 ? -31.715 -44.295 -4.797  1.00 91.67  ? 198 ASN   A N   1 
ATOM   1301 C  CA  . ASN   A 1 177 ? -31.987 -43.982 -3.393  1.00 93.53  ? 198 ASN   A CA  1 
ATOM   1302 C  C   . ASN   A 1 177 ? -32.334 -42.503 -3.242  1.00 92.82  ? 198 ASN   A C   1 
ATOM   1303 O  O   . ASN   A 1 177 ? -31.609 -41.743 -2.593  1.00 91.16  ? 198 ASN   A O   1 
ATOM   1304 C  CB  . ASN   A 1 177 ? -30.786 -44.365 -2.528  1.00 92.70  ? 198 ASN   A CB  1 
ATOM   1305 C  CG  . ASN   A 1 177 ? -31.069 -44.252 -1.040  1.00 95.34  ? 198 ASN   A CG  1 
ATOM   1306 O  OD1 . ASN   A 1 177 ? -32.217 -44.123 -0.620  1.00 98.53  ? 198 ASN   A OD1 1 
ATOM   1307 N  ND2 . ASN   A 1 177 ? -30.014 -44.306 -0.235  1.00 91.32  ? 198 ASN   A ND2 1 
ATOM   1308 N  N   . PRO   A 1 178 ? -33.443 -42.058 -3.826  1.00 93.60  ? 199 PRO   A N   1 
ATOM   1309 C  CA  . PRO   A 1 178 ? -33.851 -40.660 -3.683  1.00 90.86  ? 199 PRO   A CA  1 
ATOM   1310 C  C   . PRO   A 1 178 ? -34.562 -40.461 -2.349  1.00 92.69  ? 199 PRO   A C   1 
ATOM   1311 O  O   . PRO   A 1 178 ? -34.722 -41.390 -1.559  1.00 96.74  ? 199 PRO   A O   1 
ATOM   1312 C  CB  . PRO   A 1 178 ? -34.794 -40.456 -4.866  1.00 87.42  ? 199 PRO   A CB  1 
ATOM   1313 C  CG  . PRO   A 1 178 ? -35.450 -41.778 -5.021  1.00 93.89  ? 199 PRO   A CG  1 
ATOM   1314 C  CD  . PRO   A 1 178 ? -34.426 -42.824 -4.616  1.00 93.15  ? 199 PRO   A CD  1 
ATOM   1315 N  N   . GLN   A 1 179 ? -34.977 -39.219 -2.106  1.00 91.48  ? 200 GLN   A N   1 
ATOM   1316 C  CA  . GLN   A 1 179 ? -35.618 -38.794 -0.864  1.00 93.21  ? 200 GLN   A CA  1 
ATOM   1317 C  C   . GLN   A 1 179 ? -34.714 -38.966 0.350   1.00 92.82  ? 200 GLN   A C   1 
ATOM   1318 O  O   . GLN   A 1 179 ? -35.176 -38.816 1.488   1.00 92.50  ? 200 GLN   A O   1 
ATOM   1319 C  CB  . GLN   A 1 179 ? -36.948 -39.524 -0.634  1.00 88.89  ? 200 GLN   A CB  1 
ATOM   1320 N  N   . ASP   A 1 180 ? -33.441 -39.287 0.138   1.00 91.31  ? 201 ASP   A N   1 
ATOM   1321 C  CA  . ASP   A 1 180 ? -32.478 -39.280 1.226   1.00 89.80  ? 201 ASP   A CA  1 
ATOM   1322 C  C   . ASP   A 1 180 ? -32.278 -37.846 1.711   1.00 92.49  ? 201 ASP   A C   1 
ATOM   1323 O  O   . ASP   A 1 180 ? -32.328 -36.911 0.907   1.00 90.10  ? 201 ASP   A O   1 
ATOM   1324 C  CB  . ASP   A 1 180 ? -31.153 -39.892 0.756   1.00 89.25  ? 201 ASP   A CB  1 
ATOM   1325 C  CG  . ASP   A 1 180 ? -30.109 -39.970 1.857   1.00 91.02  ? 201 ASP   A CG  1 
ATOM   1326 O  OD1 . ASP   A 1 180 ? -29.575 -38.914 2.259   1.00 88.06  ? 201 ASP   A OD1 1 
ATOM   1327 O  OD2 . ASP   A 1 180 ? -29.822 -41.093 2.323   1.00 93.11  ? 201 ASP   A OD2 1 
ATOM   1328 N  N   . PRO   A 1 181 ? -32.081 -37.639 3.019   1.00 93.64  ? 202 PRO   A N   1 
ATOM   1329 C  CA  . PRO   A 1 181 ? -31.950 -36.261 3.532   1.00 92.91  ? 202 PRO   A CA  1 
ATOM   1330 C  C   . PRO   A 1 181 ? -30.934 -35.401 2.794   1.00 89.84  ? 202 PRO   A C   1 
ATOM   1331 O  O   . PRO   A 1 181 ? -31.272 -34.293 2.358   1.00 88.56  ? 202 PRO   A O   1 
ATOM   1332 C  CB  . PRO   A 1 181 ? -31.559 -36.490 4.997   1.00 92.51  ? 202 PRO   A CB  1 
ATOM   1333 C  CG  . PRO   A 1 181 ? -32.229 -37.772 5.351   1.00 90.73  ? 202 PRO   A CG  1 
ATOM   1334 C  CD  . PRO   A 1 181 ? -32.176 -38.627 4.110   1.00 92.02  ? 202 PRO   A CD  1 
ATOM   1335 N  N   . PHE   A 1 182 ? -29.696 -35.877 2.641   1.00 87.54  ? 203 PHE   A N   1 
ATOM   1336 C  CA  . PHE   A 1 182 ? -28.696 -35.096 1.917   1.00 84.86  ? 203 PHE   A CA  1 
ATOM   1337 C  C   . PHE   A 1 182 ? -29.088 -34.909 0.457   1.00 83.80  ? 203 PHE   A C   1 
ATOM   1338 O  O   . PHE   A 1 182 ? -28.961 -33.808 -0.092  1.00 84.56  ? 203 PHE   A O   1 
ATOM   1339 C  CB  . PHE   A 1 182 ? -27.324 -35.764 2.015   1.00 85.08  ? 203 PHE   A CB  1 
ATOM   1340 C  CG  . PHE   A 1 182 ? -26.699 -35.676 3.376   1.00 87.09  ? 203 PHE   A CG  1 
ATOM   1341 C  CD1 . PHE   A 1 182 ? -26.999 -36.612 4.351   1.00 90.94  ? 203 PHE   A CD1 1 
ATOM   1342 C  CD2 . PHE   A 1 182 ? -25.803 -34.664 3.678   1.00 86.76  ? 203 PHE   A CD2 1 
ATOM   1343 C  CE1 . PHE   A 1 182 ? -26.422 -36.538 5.605   1.00 91.68  ? 203 PHE   A CE1 1 
ATOM   1344 C  CE2 . PHE   A 1 182 ? -25.222 -34.584 4.929   1.00 90.71  ? 203 PHE   A CE2 1 
ATOM   1345 C  CZ  . PHE   A 1 182 ? -25.533 -35.523 5.894   1.00 91.33  ? 203 PHE   A CZ  1 
ATOM   1346 N  N   . VAL   A 1 183 ? -29.576 -35.972 -0.185  1.00 83.03  ? 204 VAL   A N   1 
ATOM   1347 C  CA  . VAL   A 1 183 ? -29.857 -35.916 -1.617  1.00 80.95  ? 204 VAL   A CA  1 
ATOM   1348 C  C   . VAL   A 1 183 ? -31.019 -34.975 -1.909  1.00 81.21  ? 204 VAL   A C   1 
ATOM   1349 O  O   . VAL   A 1 183 ? -30.954 -34.158 -2.836  1.00 79.70  ? 204 VAL   A O   1 
ATOM   1350 C  CB  . VAL   A 1 183 ? -30.121 -37.332 -2.159  1.00 82.32  ? 204 VAL   A CB  1 
ATOM   1351 C  CG1 . VAL   A 1 183 ? -30.519 -37.277 -3.624  1.00 80.49  ? 204 VAL   A CG1 1 
ATOM   1352 C  CG2 . VAL   A 1 183 ? -28.894 -38.210 -1.967  1.00 80.80  ? 204 VAL   A CG2 1 
ATOM   1353 N  N   . GLU   A 1 184 ? -32.096 -35.066 -1.124  1.00 84.10  ? 205 GLU   A N   1 
ATOM   1354 C  CA  . GLU   A 1 184 ? -33.287 -34.271 -1.408  1.00 84.20  ? 205 GLU   A CA  1 
ATOM   1355 C  C   . GLU   A 1 184 ? -33.035 -32.780 -1.227  1.00 82.12  ? 205 GLU   A C   1 
ATOM   1356 O  O   . GLU   A 1 184 ? -33.620 -31.965 -1.949  1.00 79.96  ? 205 GLU   A O   1 
ATOM   1357 C  CB  . GLU   A 1 184 ? -34.445 -34.721 -0.518  1.00 87.34  ? 205 GLU   A CB  1 
ATOM   1358 N  N   . ASN   A 1 185 ? -32.180 -32.403 -0.274  1.00 80.65  ? 206 ASN   A N   1 
ATOM   1359 C  CA  . ASN   A 1 185 ? -31.911 -30.988 -0.046  1.00 80.68  ? 206 ASN   A CA  1 
ATOM   1360 C  C   . ASN   A 1 185 ? -30.847 -30.455 -1.000  1.00 80.52  ? 206 ASN   A C   1 
ATOM   1361 O  O   . ASN   A 1 185 ? -30.999 -29.362 -1.558  1.00 80.63  ? 206 ASN   A O   1 
ATOM   1362 C  CB  . ASN   A 1 185 ? -31.496 -30.757 1.408   1.00 83.99  ? 206 ASN   A CB  1 
ATOM   1363 C  CG  . ASN   A 1 185 ? -32.686 -30.623 2.334   1.00 88.58  ? 206 ASN   A CG  1 
ATOM   1364 O  OD1 . ASN   A 1 185 ? -33.747 -30.143 1.937   1.00 86.96  ? 206 ASN   A OD1 1 
ATOM   1365 N  ND2 . ASN   A 1 185 ? -32.516 -31.049 3.578   1.00 90.71  ? 206 ASN   A ND2 1 
ATOM   1366 N  N   . THR   A 1 186 ? -29.759 -31.205 -1.196  1.00 80.14  ? 207 THR   A N   1 
ATOM   1367 C  CA  . THR   A 1 186 ? -28.716 -30.760 -2.115  1.00 78.22  ? 207 THR   A CA  1 
ATOM   1368 C  C   . THR   A 1 186 ? -29.197 -30.726 -3.559  1.00 77.98  ? 207 THR   A C   1 
ATOM   1369 O  O   . THR   A 1 186 ? -28.636 -29.978 -4.367  1.00 77.81  ? 207 THR   A O   1 
ATOM   1370 C  CB  . THR   A 1 186 ? -27.479 -31.652 -2.002  1.00 75.04  ? 207 THR   A CB  1 
ATOM   1371 O  OG1 . THR   A 1 186 ? -27.853 -33.021 -2.195  1.00 84.40  ? 207 THR   A OG1 1 
ATOM   1372 C  CG2 . THR   A 1 186 ? -26.829 -31.491 -0.634  1.00 74.82  ? 207 THR   A CG2 1 
ATOM   1373 N  N   . LYS   A 1 187 ? -30.220 -31.512 -3.902  1.00 75.71  ? 208 LYS   A N   1 
ATOM   1374 C  CA  . LYS   A 1 187 ? -30.832 -31.404 -5.219  1.00 75.56  ? 208 LYS   A CA  1 
ATOM   1375 C  C   . LYS   A 1 187 ? -31.560 -30.081 -5.413  1.00 76.01  ? 208 LYS   A C   1 
ATOM   1376 O  O   . LYS   A 1 187 ? -31.928 -29.756 -6.547  1.00 74.09  ? 208 LYS   A O   1 
ATOM   1377 C  CB  . LYS   A 1 187 ? -31.802 -32.564 -5.452  1.00 74.33  ? 208 LYS   A CB  1 
ATOM   1378 N  N   . LYS   A 1 188 ? -31.779 -29.321 -4.341  1.00 78.11  ? 209 LYS   A N   1 
ATOM   1379 C  CA  . LYS   A 1 188 ? -32.400 -28.008 -4.424  1.00 77.89  ? 209 LYS   A CA  1 
ATOM   1380 C  C   . LYS   A 1 188 ? -31.395 -26.884 -4.648  1.00 75.57  ? 209 LYS   A C   1 
ATOM   1381 O  O   . LYS   A 1 188 ? -31.810 -25.739 -4.857  1.00 74.19  ? 209 LYS   A O   1 
ATOM   1382 C  CB  . LYS   A 1 188 ? -33.209 -27.725 -3.152  1.00 78.40  ? 209 LYS   A CB  1 
ATOM   1383 C  CG  . LYS   A 1 188 ? -34.341 -28.713 -2.906  1.00 80.51  ? 209 LYS   A CG  1 
ATOM   1384 C  CD  . LYS   A 1 188 ? -34.963 -28.528 -1.530  1.00 81.53  ? 209 LYS   A CD  1 
ATOM   1385 C  CE  . LYS   A 1 188 ? -36.058 -29.555 -1.281  1.00 81.02  ? 209 LYS   A CE  1 
ATOM   1386 N  NZ  . LYS   A 1 188 ? -36.547 -29.533 0.126   1.00 81.71  ? 209 LYS   A NZ  1 
ATOM   1387 N  N   . LEU   A 1 189 ? -30.093 -27.177 -4.613  1.00 74.43  ? 210 LEU   A N   1 
ATOM   1388 C  CA  . LEU   A 1 189 ? -29.057 -26.171 -4.860  1.00 71.33  ? 210 LEU   A CA  1 
ATOM   1389 C  C   . LEU   A 1 189 ? -28.839 -26.031 -6.368  1.00 72.04  ? 210 LEU   A C   1 
ATOM   1390 O  O   . LEU   A 1 189 ? -27.839 -26.469 -6.938  1.00 70.57  ? 210 LEU   A O   1 
ATOM   1391 C  CB  . LEU   A 1 189 ? -27.768 -26.537 -4.137  1.00 69.56  ? 210 LEU   A CB  1 
ATOM   1392 C  CG  . LEU   A 1 189 ? -27.615 -26.092 -2.680  1.00 67.79  ? 210 LEU   A CG  1 
ATOM   1393 C  CD1 . LEU   A 1 189 ? -26.403 -26.753 -2.039  1.00 66.97  ? 210 LEU   A CD1 1 
ATOM   1394 C  CD2 . LEU   A 1 189 ? -27.504 -24.578 -2.587  1.00 63.57  ? 210 LEU   A CD2 1 
ATOM   1395 N  N   . LEU   A 1 190 ? -29.810 -25.397 -7.016  1.00 73.21  ? 211 LEU   A N   1 
ATOM   1396 C  CA  . LEU   A 1 190 ? -29.798 -25.219 -8.460  1.00 73.00  ? 211 LEU   A CA  1 
ATOM   1397 C  C   . LEU   A 1 190 ? -29.305 -23.823 -8.823  1.00 69.45  ? 211 LEU   A C   1 
ATOM   1398 O  O   . LEU   A 1 190 ? -29.420 -22.879 -8.038  1.00 66.61  ? 211 LEU   A O   1 
ATOM   1399 C  CB  . LEU   A 1 190 ? -31.192 -25.459 -9.043  1.00 75.01  ? 211 LEU   A CB  1 
ATOM   1400 C  CG  . LEU   A 1 190 ? -31.824 -26.808 -8.684  1.00 77.27  ? 211 LEU   A CG  1 
ATOM   1401 C  CD1 . LEU   A 1 190 ? -33.199 -26.947 -9.318  1.00 77.83  ? 211 LEU   A CD1 1 
ATOM   1402 C  CD2 . LEU   A 1 190 ? -30.919 -27.962 -9.096  1.00 73.63  ? 211 LEU   A CD2 1 
ATOM   1403 N  N   . ARG   A 1 191 ? -28.761 -23.705 -10.031 1.00 71.08  ? 212 ARG   A N   1 
ATOM   1404 C  CA  . ARG   A 1 191 ? -28.104 -22.481 -10.465 1.00 71.16  ? 212 ARG   A CA  1 
ATOM   1405 C  C   . ARG   A 1 191 ? -29.096 -21.324 -10.568 1.00 64.89  ? 212 ARG   A C   1 
ATOM   1406 O  O   . ARG   A 1 191 ? -30.316 -21.511 -10.620 1.00 65.14  ? 212 ARG   A O   1 
ATOM   1407 C  CB  . ARG   A 1 191 ? -27.414 -22.696 -11.812 1.00 71.42  ? 212 ARG   A CB  1 
ATOM   1408 C  CG  . ARG   A 1 191 ? -26.282 -23.708 -11.776 1.00 73.73  ? 212 ARG   A CG  1 
ATOM   1409 C  CD  . ARG   A 1 191 ? -25.845 -24.092 -13.180 1.00 77.84  ? 212 ARG   A CD  1 
ATOM   1410 N  NE  . ARG   A 1 191 ? -26.930 -24.715 -13.928 1.00 79.07  ? 212 ARG   A NE  1 
ATOM   1411 C  CZ  . ARG   A 1 191 ? -26.833 -25.138 -15.181 1.00 77.00  ? 212 ARG   A CZ  1 
ATOM   1412 N  NH1 . ARG   A 1 191 ? -25.707 -25.019 -15.866 1.00 73.58  ? 212 ARG   A NH1 1 
ATOM   1413 N  NH2 . ARG   A 1 191 ? -27.893 -25.696 -15.761 1.00 73.24  ? 212 ARG   A NH2 1 
ATOM   1414 N  N   . PHE   A 1 192 ? -28.549 -20.112 -10.600 1.00 60.34  ? 213 PHE   A N   1 
ATOM   1415 C  CA  . PHE   A 1 192 ? -29.346 -18.892 -10.626 1.00 60.23  ? 213 PHE   A CA  1 
ATOM   1416 C  C   . PHE   A 1 192 ? -29.564 -18.446 -12.067 1.00 62.77  ? 213 PHE   A C   1 
ATOM   1417 O  O   . PHE   A 1 192 ? -28.600 -18.200 -12.801 1.00 65.61  ? 213 PHE   A O   1 
ATOM   1418 C  CB  . PHE   A 1 192 ? -28.662 -17.783 -9.826  1.00 61.22  ? 213 PHE   A CB  1 
ATOM   1419 C  CG  . PHE   A 1 192 ? -28.524 -18.083 -8.361  1.00 60.96  ? 213 PHE   A CG  1 
ATOM   1420 C  CD1 . PHE   A 1 192 ? -29.537 -18.728 -7.671  1.00 59.85  ? 213 PHE   A CD1 1 
ATOM   1421 C  CD2 . PHE   A 1 192 ? -27.377 -17.721 -7.673  1.00 60.64  ? 213 PHE   A CD2 1 
ATOM   1422 C  CE1 . PHE   A 1 192 ? -29.410 -19.004 -6.322  1.00 58.51  ? 213 PHE   A CE1 1 
ATOM   1423 C  CE2 . PHE   A 1 192 ? -27.244 -17.996 -6.325  1.00 59.20  ? 213 PHE   A CE2 1 
ATOM   1424 C  CZ  . PHE   A 1 192 ? -28.262 -18.638 -5.649  1.00 61.61  ? 213 PHE   A CZ  1 
ATOM   1425 N  N   . ASP   A 1 193 ? -30.830 -18.341 -12.465 1.00 62.75  ? 214 ASP   A N   1 
ATOM   1426 C  CA  . ASP   A 1 193 ? -31.207 -17.803 -13.770 1.00 62.02  ? 214 ASP   A CA  1 
ATOM   1427 C  C   . ASP   A 1 193 ? -31.372 -16.299 -13.601 1.00 60.52  ? 214 ASP   A C   1 
ATOM   1428 O  O   . ASP   A 1 193 ? -32.433 -15.812 -13.208 1.00 61.70  ? 214 ASP   A O   1 
ATOM   1429 C  CB  . ASP   A 1 193 ? -32.484 -18.467 -14.274 1.00 60.88  ? 214 ASP   A CB  1 
ATOM   1430 C  CG  . ASP   A 1 193 ? -32.917 -17.954 -15.638 1.00 60.17  ? 214 ASP   A CG  1 
ATOM   1431 O  OD1 . ASP   A 1 193 ? -32.186 -17.150 -16.248 1.00 61.57  ? 214 ASP   A OD1 1 
ATOM   1432 O  OD2 . ASP   A 1 193 ? -34.002 -18.365 -16.103 1.00 60.11  ? 214 ASP   A OD2 1 
ATOM   1433 N  N   . PHE   A 1 194 ? -30.315 -15.553 -13.901 1.00 61.31  ? 215 PHE   A N   1 
ATOM   1434 C  CA  . PHE   A 1 194 ? -30.370 -14.111 -13.674 1.00 62.26  ? 215 PHE   A CA  1 
ATOM   1435 C  C   . PHE   A 1 194 ? -31.251 -13.375 -14.679 1.00 58.95  ? 215 PHE   A C   1 
ATOM   1436 O  O   . PHE   A 1 194 ? -31.288 -12.141 -14.622 1.00 62.31  ? 215 PHE   A O   1 
ATOM   1437 C  CB  . PHE   A 1 194 ? -28.957 -13.528 -13.680 1.00 63.14  ? 215 PHE   A CB  1 
ATOM   1438 C  CG  . PHE   A 1 194 ? -28.100 -14.011 -12.542 1.00 62.41  ? 215 PHE   A CG  1 
ATOM   1439 C  CD1 . PHE   A 1 194 ? -28.170 -13.405 -11.298 1.00 61.10  ? 215 PHE   A CD1 1 
ATOM   1440 C  CD2 . PHE   A 1 194 ? -27.224 -15.069 -12.716 1.00 66.11  ? 215 PHE   A CD2 1 
ATOM   1441 C  CE1 . PHE   A 1 194 ? -27.383 -13.846 -10.250 1.00 61.54  ? 215 PHE   A CE1 1 
ATOM   1442 C  CE2 . PHE   A 1 194 ? -26.434 -15.514 -11.672 1.00 67.37  ? 215 PHE   A CE2 1 
ATOM   1443 C  CZ  . PHE   A 1 194 ? -26.514 -14.901 -10.438 1.00 64.55  ? 215 PHE   A CZ  1 
ATOM   1444 N  N   . LEU   A 1 195 ? -31.947 -14.061 -15.584 1.00 58.73  ? 216 LEU   A N   1 
ATOM   1445 C  CA  . LEU   A 1 195 ? -32.961 -13.441 -16.427 1.00 60.71  ? 216 LEU   A CA  1 
ATOM   1446 C  C   . LEU   A 1 195 ? -34.376 -13.810 -15.996 1.00 60.37  ? 216 LEU   A C   1 
ATOM   1447 O  O   . LEU   A 1 195 ? -35.337 -13.465 -16.692 1.00 61.26  ? 216 LEU   A O   1 
ATOM   1448 C  CB  . LEU   A 1 195 ? -32.743 -13.816 -17.894 1.00 61.54  ? 216 LEU   A CB  1 
ATOM   1449 C  CG  . LEU   A 1 195 ? -31.500 -13.215 -18.549 1.00 61.28  ? 216 LEU   A CG  1 
ATOM   1450 C  CD1 . LEU   A 1 195 ? -31.464 -13.527 -20.038 1.00 61.90  ? 216 LEU   A CD1 1 
ATOM   1451 C  CD2 . LEU   A 1 195 ? -31.434 -11.715 -18.305 1.00 59.54  ? 216 LEU   A CD2 1 
ATOM   1452 N  N   . ASP   A 1 196 ? -34.525 -14.500 -14.866 1.00 59.86  ? 217 ASP   A N   1 
ATOM   1453 C  CA  . ASP   A 1 196 ? -35.835 -14.838 -14.335 1.00 58.82  ? 217 ASP   A CA  1 
ATOM   1454 C  C   . ASP   A 1 196 ? -36.483 -13.581 -13.757 1.00 61.31  ? 217 ASP   A C   1 
ATOM   1455 O  O   . ASP   A 1 196 ? -35.816 -12.560 -13.575 1.00 60.98  ? 217 ASP   A O   1 
ATOM   1456 C  CB  . ASP   A 1 196 ? -35.708 -15.949 -13.288 1.00 58.84  ? 217 ASP   A CB  1 
ATOM   1457 C  CG  . ASP   A 1 196 ? -35.370 -15.423 -11.905 1.00 62.27  ? 217 ASP   A CG  1 
ATOM   1458 O  OD1 . ASP   A 1 196 ? -34.576 -14.465 -11.797 1.00 63.58  ? 217 ASP   A OD1 1 
ATOM   1459 O  OD2 . ASP   A 1 196 ? -35.900 -15.979 -10.920 1.00 64.20  ? 217 ASP   A OD2 1 
ATOM   1460 N  N   . PRO   A 1 197 ? -37.795 -13.610 -13.487 1.00 61.48  ? 218 PRO   A N   1 
ATOM   1461 C  CA  . PRO   A 1 197 ? -38.454 -12.396 -12.970 1.00 59.42  ? 218 PRO   A CA  1 
ATOM   1462 C  C   . PRO   A 1 197 ? -37.825 -11.818 -11.711 1.00 59.00  ? 218 PRO   A C   1 
ATOM   1463 O  O   . PRO   A 1 197 ? -37.716 -10.591 -11.600 1.00 60.58  ? 218 PRO   A O   1 
ATOM   1464 C  CB  . PRO   A 1 197 ? -39.889 -12.871 -12.710 1.00 56.75  ? 218 PRO   A CB  1 
ATOM   1465 C  CG  . PRO   A 1 197 ? -40.100 -13.956 -13.690 1.00 57.99  ? 218 PRO   A CG  1 
ATOM   1466 C  CD  . PRO   A 1 197 ? -38.777 -14.661 -13.819 1.00 59.51  ? 218 PRO   A CD  1 
ATOM   1467 N  N   . PHE   A 1 198 ? -37.402 -12.659 -10.763 1.00 60.11  ? 219 PHE   A N   1 
ATOM   1468 C  CA  . PHE   A 1 198 ? -36.857 -12.135 -9.512  1.00 58.27  ? 219 PHE   A CA  1 
ATOM   1469 C  C   . PHE   A 1 198 ? -35.578 -11.344 -9.753  1.00 60.21  ? 219 PHE   A C   1 
ATOM   1470 O  O   . PHE   A 1 198 ? -35.461 -10.189 -9.329  1.00 59.70  ? 219 PHE   A O   1 
ATOM   1471 C  CB  . PHE   A 1 198 ? -36.601 -13.269 -8.520  1.00 54.57  ? 219 PHE   A CB  1 
ATOM   1472 C  CG  . PHE   A 1 198 ? -35.955 -12.813 -7.238  1.00 54.23  ? 219 PHE   A CG  1 
ATOM   1473 C  CD1 . PHE   A 1 198 ? -36.696 -12.155 -6.271  1.00 56.33  ? 219 PHE   A CD1 1 
ATOM   1474 C  CD2 . PHE   A 1 198 ? -34.607 -13.037 -7.004  1.00 54.36  ? 219 PHE   A CD2 1 
ATOM   1475 C  CE1 . PHE   A 1 198 ? -36.106 -11.729 -5.094  1.00 55.01  ? 219 PHE   A CE1 1 
ATOM   1476 C  CE2 . PHE   A 1 198 ? -34.012 -12.614 -5.828  1.00 55.13  ? 219 PHE   A CE2 1 
ATOM   1477 C  CZ  . PHE   A 1 198 ? -34.764 -11.960 -4.873  1.00 54.42  ? 219 PHE   A CZ  1 
ATOM   1478 N  N   . PHE   A 1 199 ? -34.608 -11.944 -10.447 1.00 60.44  ? 220 PHE   A N   1 
ATOM   1479 C  CA  . PHE   A 1 199 ? -33.327 -11.271 -10.636 1.00 60.21  ? 220 PHE   A CA  1 
ATOM   1480 C  C   . PHE   A 1 199 ? -33.433 -10.118 -11.624 1.00 59.38  ? 220 PHE   A C   1 
ATOM   1481 O  O   . PHE   A 1 199 ? -32.692 -9.137  -11.503 1.00 59.97  ? 220 PHE   A O   1 
ATOM   1482 C  CB  . PHE   A 1 199 ? -32.262 -12.269 -11.085 1.00 58.13  ? 220 PHE   A CB  1 
ATOM   1483 C  CG  . PHE   A 1 199 ? -31.767 -13.160 -9.980  1.00 56.40  ? 220 PHE   A CG  1 
ATOM   1484 C  CD1 . PHE   A 1 199 ? -30.969 -12.652 -8.968  1.00 57.48  ? 220 PHE   A CD1 1 
ATOM   1485 C  CD2 . PHE   A 1 199 ? -32.095 -14.503 -9.955  1.00 57.15  ? 220 PHE   A CD2 1 
ATOM   1486 C  CE1 . PHE   A 1 199 ? -30.513 -13.469 -7.950  1.00 56.80  ? 220 PHE   A CE1 1 
ATOM   1487 C  CE2 . PHE   A 1 199 ? -31.642 -15.324 -8.942  1.00 54.24  ? 220 PHE   A CE2 1 
ATOM   1488 C  CZ  . PHE   A 1 199 ? -30.850 -14.806 -7.939  1.00 52.48  ? 220 PHE   A CZ  1 
ATOM   1489 N  N   . LEU   A 1 200 ? -34.331 -10.216 -12.608 1.00 56.58  ? 221 LEU   A N   1 
ATOM   1490 C  CA  . LEU   A 1 200 ? -34.596 -9.065  -13.465 1.00 58.16  ? 221 LEU   A CA  1 
ATOM   1491 C  C   . LEU   A 1 200 ? -35.183 -7.913  -12.661 1.00 61.27  ? 221 LEU   A C   1 
ATOM   1492 O  O   . LEU   A 1 200 ? -34.809 -6.752  -12.863 1.00 65.90  ? 221 LEU   A O   1 
ATOM   1493 C  CB  . LEU   A 1 200 ? -35.532 -9.451  -14.612 1.00 59.52  ? 221 LEU   A CB  1 
ATOM   1494 C  CG  . LEU   A 1 200 ? -34.862 -9.868  -15.924 1.00 62.44  ? 221 LEU   A CG  1 
ATOM   1495 C  CD1 . LEU   A 1 200 ? -35.847 -9.799  -17.085 1.00 61.64  ? 221 LEU   A CD1 1 
ATOM   1496 C  CD2 . LEU   A 1 200 ? -33.641 -9.005  -16.198 1.00 56.00  ? 221 LEU   A CD2 1 
ATOM   1497 N  N   . SER   A 1 201 ? -36.104 -8.214  -11.743 1.00 59.99  ? 222 SER   A N   1 
ATOM   1498 C  CA  . SER   A 1 201 ? -36.633 -7.182  -10.858 1.00 59.12  ? 222 SER   A CA  1 
ATOM   1499 C  C   . SER   A 1 201 ? -35.546 -6.644  -9.936  1.00 60.89  ? 222 SER   A C   1 
ATOM   1500 O  O   . SER   A 1 201 ? -35.503 -5.442  -9.648  1.00 61.87  ? 222 SER   A O   1 
ATOM   1501 C  CB  . SER   A 1 201 ? -37.802 -7.735  -10.043 1.00 57.54  ? 222 SER   A CB  1 
ATOM   1502 O  OG  . SER   A 1 201 ? -38.794 -8.297  -10.884 1.00 58.98  ? 222 SER   A OG  1 
ATOM   1503 N  N   . ILE   A 1 202 ? -34.661 -7.524  -9.459  1.00 62.24  ? 223 ILE   A N   1 
ATOM   1504 C  CA  . ILE   A 1 202 ? -33.562 -7.093  -8.599  1.00 61.04  ? 223 ILE   A CA  1 
ATOM   1505 C  C   . ILE   A 1 202 ? -32.627 -6.157  -9.355  1.00 61.06  ? 223 ILE   A C   1 
ATOM   1506 O  O   . ILE   A 1 202 ? -32.122 -5.174  -8.798  1.00 62.52  ? 223 ILE   A O   1 
ATOM   1507 C  CB  . ILE   A 1 202 ? -32.815 -8.318  -8.039  1.00 62.00  ? 223 ILE   A CB  1 
ATOM   1508 C  CG1 . ILE   A 1 202 ? -33.677 -9.045  -7.005  1.00 60.67  ? 223 ILE   A CG1 1 
ATOM   1509 C  CG2 . ILE   A 1 202 ? -31.486 -7.912  -7.425  1.00 64.80  ? 223 ILE   A CG2 1 
ATOM   1510 C  CD1 . ILE   A 1 202 ? -34.147 -8.161  -5.877  1.00 61.29  ? 223 ILE   A CD1 1 
ATOM   1511 N  N   . THR   A 1 203 ? -32.383 -6.445  -10.636 1.00 61.65  ? 224 THR   A N   1 
ATOM   1512 C  CA  . THR   A 1 203 ? -31.523 -5.582  -11.439 1.00 62.54  ? 224 THR   A CA  1 
ATOM   1513 C  C   . THR   A 1 203 ? -32.146 -4.204  -11.638 1.00 62.58  ? 224 THR   A C   1 
ATOM   1514 O  O   . THR   A 1 203 ? -31.447 -3.186  -11.578 1.00 62.45  ? 224 THR   A O   1 
ATOM   1515 C  CB  . THR   A 1 203 ? -31.233 -6.239  -12.789 1.00 61.41  ? 224 THR   A CB  1 
ATOM   1516 O  OG1 . THR   A 1 203 ? -30.753 -7.572  -12.579 1.00 66.35  ? 224 THR   A OG1 1 
ATOM   1517 C  CG2 . THR   A 1 203 ? -30.183 -5.448  -13.553 1.00 62.27  ? 224 THR   A CG2 1 
ATOM   1518 N  N   . VAL   A 1 204 ? -33.458 -4.151  -11.883 1.00 62.49  ? 225 VAL   A N   1 
ATOM   1519 C  CA  . VAL   A 1 204 ? -34.127 -2.867  -12.076 1.00 62.65  ? 225 VAL   A CA  1 
ATOM   1520 C  C   . VAL   A 1 204 ? -34.261 -2.121  -10.751 1.00 62.75  ? 225 VAL   A C   1 
ATOM   1521 O  O   . VAL   A 1 204 ? -34.177 -0.888  -10.710 1.00 62.61  ? 225 VAL   A O   1 
ATOM   1522 C  CB  . VAL   A 1 204 ? -35.493 -3.071  -12.757 1.00 63.96  ? 225 VAL   A CB  1 
ATOM   1523 C  CG1 . VAL   A 1 204 ? -36.168 -1.730  -13.010 1.00 62.70  ? 225 VAL   A CG1 1 
ATOM   1524 C  CG2 . VAL   A 1 204 ? -35.325 -3.828  -14.064 1.00 65.54  ? 225 VAL   A CG2 1 
ATOM   1525 N  N   . PHE   A 1 205 ? -34.473 -2.848  -9.649  1.00 62.88  ? 226 PHE   A N   1 
ATOM   1526 C  CA  . PHE   A 1 205 ? -34.599 -2.258  -8.316  1.00 60.85  ? 226 PHE   A CA  1 
ATOM   1527 C  C   . PHE   A 1 205 ? -33.463 -2.746  -7.418  1.00 59.61  ? 226 PHE   A C   1 
ATOM   1528 O  O   . PHE   A 1 205 ? -33.704 -3.490  -6.457  1.00 62.49  ? 226 PHE   A O   1 
ATOM   1529 C  CB  . PHE   A 1 205 ? -35.932 -2.600  -7.648  1.00 62.91  ? 226 PHE   A CB  1 
ATOM   1530 C  CG  . PHE   A 1 205 ? -37.118 -2.638  -8.572  1.00 65.78  ? 226 PHE   A CG  1 
ATOM   1531 C  CD1 . PHE   A 1 205 ? -37.341 -1.642  -9.507  1.00 66.69  ? 226 PHE   A CD1 1 
ATOM   1532 C  CD2 . PHE   A 1 205 ? -38.033 -3.676  -8.476  1.00 63.44  ? 226 PHE   A CD2 1 
ATOM   1533 C  CE1 . PHE   A 1 205 ? -38.447 -1.692  -10.339 1.00 67.38  ? 226 PHE   A CE1 1 
ATOM   1534 C  CE2 . PHE   A 1 205 ? -39.138 -3.732  -9.302  1.00 63.06  ? 226 PHE   A CE2 1 
ATOM   1535 C  CZ  . PHE   A 1 205 ? -39.347 -2.739  -10.235 1.00 66.78  ? 226 PHE   A CZ  1 
ATOM   1536 N  N   . PRO   A 1 206 ? -32.215 -2.352  -7.693  1.00 56.13  ? 227 PRO   A N   1 
ATOM   1537 C  CA  . PRO   A 1 206 ? -31.124 -2.744  -6.785  1.00 56.19  ? 227 PRO   A CA  1 
ATOM   1538 C  C   . PRO   A 1 206 ? -31.267 -2.161  -5.392  1.00 58.17  ? 227 PRO   A C   1 
ATOM   1539 O  O   . PRO   A 1 206 ? -30.687 -2.705  -4.446  1.00 57.20  ? 227 PRO   A O   1 
ATOM   1540 C  CB  . PRO   A 1 206 ? -29.868 -2.218  -7.492  1.00 55.31  ? 227 PRO   A CB  1 
ATOM   1541 C  CG  . PRO   A 1 206 ? -30.355 -1.086  -8.313  1.00 59.27  ? 227 PRO   A CG  1 
ATOM   1542 C  CD  . PRO   A 1 206 ? -31.735 -1.465  -8.766  1.00 57.73  ? 227 PRO   A CD  1 
ATOM   1543 N  N   . PHE   A 1 207 ? -32.027 -1.075  -5.235  1.00 59.55  ? 228 PHE   A N   1 
ATOM   1544 C  CA  . PHE   A 1 207 ? -32.253 -0.481  -3.925  1.00 58.86  ? 228 PHE   A CA  1 
ATOM   1545 C  C   . PHE   A 1 207 ? -33.114 -1.352  -3.017  1.00 60.91  ? 228 PHE   A C   1 
ATOM   1546 O  O   . PHE   A 1 207 ? -33.194 -1.069  -1.817  1.00 61.05  ? 228 PHE   A O   1 
ATOM   1547 C  CB  . PHE   A 1 207 ? -32.895 0.900   -4.085  1.00 59.72  ? 228 PHE   A CB  1 
ATOM   1548 C  CG  . PHE   A 1 207 ? -34.099 0.909   -4.985  1.00 60.54  ? 228 PHE   A CG  1 
ATOM   1549 C  CD1 . PHE   A 1 207 ? -35.356 0.612   -4.486  1.00 62.29  ? 228 PHE   A CD1 1 
ATOM   1550 C  CD2 . PHE   A 1 207 ? -33.976 1.220   -6.330  1.00 58.85  ? 228 PHE   A CD2 1 
ATOM   1551 C  CE1 . PHE   A 1 207 ? -36.466 0.620   -5.309  1.00 64.75  ? 228 PHE   A CE1 1 
ATOM   1552 C  CE2 . PHE   A 1 207 ? -35.085 1.230   -7.160  1.00 60.90  ? 228 PHE   A CE2 1 
ATOM   1553 C  CZ  . PHE   A 1 207 ? -36.331 0.929   -6.647  1.00 62.52  ? 228 PHE   A CZ  1 
ATOM   1554 N  N   . LEU   A 1 208 ? -33.762 -2.387  -3.553  1.00 61.95  ? 229 LEU   A N   1 
ATOM   1555 C  CA  . LEU   A 1 208 ? -34.568 -3.285  -2.737  1.00 62.03  ? 229 LEU   A CA  1 
ATOM   1556 C  C   . LEU   A 1 208 ? -33.760 -4.414  -2.110  1.00 61.85  ? 229 LEU   A C   1 
ATOM   1557 O  O   . LEU   A 1 208 ? -34.276 -5.096  -1.217  1.00 62.15  ? 229 LEU   A O   1 
ATOM   1558 C  CB  . LEU   A 1 208 ? -35.709 -3.878  -3.568  1.00 62.87  ? 229 LEU   A CB  1 
ATOM   1559 C  CG  . LEU   A 1 208 ? -36.743 -2.884  -4.102  1.00 66.05  ? 229 LEU   A CG  1 
ATOM   1560 C  CD1 . LEU   A 1 208 ? -37.891 -3.612  -4.789  1.00 66.89  ? 229 LEU   A CD1 1 
ATOM   1561 C  CD2 . LEU   A 1 208 ? -37.257 -1.990  -2.986  1.00 64.48  ? 229 LEU   A CD2 1 
ATOM   1562 N  N   . ILE   A 1 209 ? -32.519 -4.633  -2.559  1.00 59.23  ? 230 ILE   A N   1 
ATOM   1563 C  CA  . ILE   A 1 209 ? -31.681 -5.667  -1.944  1.00 58.14  ? 230 ILE   A CA  1 
ATOM   1564 C  C   . ILE   A 1 209 ? -31.484 -5.425  -0.455  1.00 59.26  ? 230 ILE   A C   1 
ATOM   1565 O  O   . ILE   A 1 209 ? -31.602 -6.383  0.324   1.00 58.03  ? 230 ILE   A O   1 
ATOM   1566 C  CB  . ILE   A 1 209 ? -30.358 -5.804  -2.711  1.00 60.48  ? 230 ILE   A CB  1 
ATOM   1567 C  CG1 . ILE   A 1 209 ? -30.611 -6.199  -4.165  1.00 60.65  ? 230 ILE   A CG1 1 
ATOM   1568 C  CG2 . ILE   A 1 209 ? -29.459 -6.833  -2.042  1.00 58.91  ? 230 ILE   A CG2 1 
ATOM   1569 C  CD1 . ILE   A 1 209 ? -29.338 -6.475  -4.937  1.00 59.37  ? 230 ILE   A CD1 1 
ATOM   1570 N  N   . PRO   A 1 210 ? -31.177 -4.209  0.021   1.00 62.77  ? 231 PRO   A N   1 
ATOM   1571 C  CA  . PRO   A 1 210 ? -31.092 -4.011  1.479   1.00 59.67  ? 231 PRO   A CA  1 
ATOM   1572 C  C   . PRO   A 1 210 ? -32.386 -4.329  2.204   1.00 59.41  ? 231 PRO   A C   1 
ATOM   1573 O  O   . PRO   A 1 210 ? -32.345 -4.793  3.350   1.00 60.38  ? 231 PRO   A O   1 
ATOM   1574 C  CB  . PRO   A 1 210 ? -30.719 -2.528  1.611   1.00 60.71  ? 231 PRO   A CB  1 
ATOM   1575 C  CG  . PRO   A 1 210 ? -30.068 -2.182  0.326   1.00 58.11  ? 231 PRO   A CG  1 
ATOM   1576 C  CD  . PRO   A 1 210 ? -30.791 -2.986  -0.710  1.00 59.23  ? 231 PRO   A CD  1 
ATOM   1577 N  N   . ILE   A 1 211 ? -33.534 -4.087  1.573   1.00 60.04  ? 232 ILE   A N   1 
ATOM   1578 C  CA  . ILE   A 1 211 ? -34.817 -4.402  2.195   1.00 59.14  ? 232 ILE   A CA  1 
ATOM   1579 C  C   . ILE   A 1 211 ? -34.981 -5.908  2.351   1.00 60.24  ? 232 ILE   A C   1 
ATOM   1580 O  O   . ILE   A 1 211 ? -35.418 -6.399  3.399   1.00 61.15  ? 232 ILE   A O   1 
ATOM   1581 C  CB  . ILE   A 1 211 ? -35.967 -3.792  1.376   1.00 60.81  ? 232 ILE   A CB  1 
ATOM   1582 C  CG1 . ILE   A 1 211 ? -35.893 -2.270  1.433   1.00 62.55  ? 232 ILE   A CG1 1 
ATOM   1583 C  CG2 . ILE   A 1 211 ? -37.308 -4.295  1.874   1.00 61.93  ? 232 ILE   A CG2 1 
ATOM   1584 C  CD1 . ILE   A 1 211 ? -36.993 -1.600  0.684   1.00 60.06  ? 232 ILE   A CD1 1 
ATOM   1585 N  N   . LEU   A 1 212 ? -34.641 -6.664  1.305   1.00 60.10  ? 233 LEU   A N   1 
ATOM   1586 C  CA  . LEU   A 1 212 ? -34.751 -8.116  1.375   1.00 57.49  ? 233 LEU   A CA  1 
ATOM   1587 C  C   . LEU   A 1 212 ? -33.780 -8.703  2.391   1.00 58.94  ? 233 LEU   A C   1 
ATOM   1588 O  O   . LEU   A 1 212 ? -34.088 -9.716  3.029   1.00 60.17  ? 233 LEU   A O   1 
ATOM   1589 C  CB  . LEU   A 1 212 ? -34.514 -8.723  -0.008  1.00 55.34  ? 233 LEU   A CB  1 
ATOM   1590 C  CG  . LEU   A 1 212 ? -35.513 -8.290  -1.082  1.00 55.72  ? 233 LEU   A CG  1 
ATOM   1591 C  CD1 . LEU   A 1 212 ? -35.099 -8.824  -2.440  1.00 56.14  ? 233 LEU   A CD1 1 
ATOM   1592 C  CD2 . LEU   A 1 212 ? -36.911 -8.761  -0.720  1.00 55.38  ? 233 LEU   A CD2 1 
ATOM   1593 N  N   . GLU   A 1 213 ? -32.606 -8.088  2.552   1.00 59.51  ? 234 GLU   A N   1 
ATOM   1594 C  CA  . GLU   A 1 213 ? -31.619 -8.607  3.493   1.00 62.23  ? 234 GLU   A CA  1 
ATOM   1595 C  C   . GLU   A 1 213 ? -32.103 -8.485  4.934   1.00 62.08  ? 234 GLU   A C   1 
ATOM   1596 O  O   . GLU   A 1 213 ? -32.019 -9.445  5.709   1.00 60.48  ? 234 GLU   A O   1 
ATOM   1597 C  CB  . GLU   A 1 213 ? -30.285 -7.881  3.310   1.00 63.53  ? 234 GLU   A CB  1 
ATOM   1598 C  CG  . GLU   A 1 213 ? -29.525 -8.266  2.046   1.00 63.71  ? 234 GLU   A CG  1 
ATOM   1599 C  CD  . GLU   A 1 213 ? -28.795 -9.595  2.168   1.00 70.02  ? 234 GLU   A CD  1 
ATOM   1600 O  OE1 . GLU   A 1 213 ? -29.163 -10.416 3.036   1.00 71.32  ? 234 GLU   A OE1 1 
ATOM   1601 O  OE2 . GLU   A 1 213 ? -27.840 -9.816  1.393   1.00 69.96  ? 234 GLU   A OE2 1 
ATOM   1602 N  N   . VAL   A 1 214 ? -32.613 -7.309  5.313   1.00 60.93  ? 235 VAL   A N   1 
ATOM   1603 C  CA  . VAL   A 1 214 ? -33.044 -7.104  6.694   1.00 61.14  ? 235 VAL   A CA  1 
ATOM   1604 C  C   . VAL   A 1 214 ? -34.229 -8.001  7.027   1.00 59.73  ? 235 VAL   A C   1 
ATOM   1605 O  O   . VAL   A 1 214 ? -34.418 -8.390  8.187   1.00 60.15  ? 235 VAL   A O   1 
ATOM   1606 C  CB  . VAL   A 1 214 ? -33.358 -5.614  6.948   1.00 57.61  ? 235 VAL   A CB  1 
ATOM   1607 C  CG1 . VAL   A 1 214 ? -34.621 -5.187  6.218   1.00 58.92  ? 235 VAL   A CG1 1 
ATOM   1608 C  CG2 . VAL   A 1 214 ? -33.474 -5.339  8.442   1.00 54.81  ? 235 VAL   A CG2 1 
ATOM   1609 N  N   . LEU   A 1 215 ? -35.035 -8.354  6.026   1.00 59.24  ? 236 LEU   A N   1 
ATOM   1610 C  CA  . LEU   A 1 215 ? -36.123 -9.307  6.200   1.00 58.42  ? 236 LEU   A CA  1 
ATOM   1611 C  C   . LEU   A 1 215 ? -35.637 -10.748 6.267   1.00 58.96  ? 236 LEU   A C   1 
ATOM   1612 O  O   . LEU   A 1 215 ? -36.467 -11.657 6.388   1.00 57.33  ? 236 LEU   A O   1 
ATOM   1613 C  CB  . LEU   A 1 215 ? -37.141 -9.156  5.066   1.00 54.34  ? 236 LEU   A CB  1 
ATOM   1614 C  CG  . LEU   A 1 215 ? -37.968 -7.872  5.096   1.00 53.69  ? 236 LEU   A CG  1 
ATOM   1615 C  CD1 . LEU   A 1 215 ? -38.916 -7.816  3.912   1.00 56.30  ? 236 LEU   A CD1 1 
ATOM   1616 C  CD2 . LEU   A 1 215 ? -38.735 -7.769  6.402   1.00 55.98  ? 236 LEU   A CD2 1 
ATOM   1617 N  N   . ASN   A 1 216 ? -34.323 -10.969 6.188   1.00 61.20  ? 237 ASN   A N   1 
ATOM   1618 C  CA  . ASN   A 1 216 ? -33.731 -12.306 6.213   1.00 62.79  ? 237 ASN   A CA  1 
ATOM   1619 C  C   . ASN   A 1 216 ? -34.232 -13.151 5.044   1.00 61.72  ? 237 ASN   A C   1 
ATOM   1620 O  O   . ASN   A 1 216 ? -34.450 -14.357 5.170   1.00 65.25  ? 237 ASN   A O   1 
ATOM   1621 C  CB  . ASN   A 1 216 ? -33.989 -13.002 7.553   1.00 64.54  ? 237 ASN   A CB  1 
ATOM   1622 C  CG  . ASN   A 1 216 ? -32.809 -13.834 8.016   1.00 72.01  ? 237 ASN   A CG  1 
ATOM   1623 O  OD1 . ASN   A 1 216 ? -32.213 -14.577 7.236   1.00 75.50  ? 237 ASN   A OD1 1 
ATOM   1624 N  ND2 . ASN   A 1 216 ? -32.459 -13.707 9.291   1.00 75.08  ? 237 ASN   A ND2 1 
ATOM   1625 N  N   . ILE   A 1 217 ? -34.415 -12.508 3.893   1.00 58.14  ? 238 ILE   A N   1 
ATOM   1626 C  CA  . ILE   A 1 217 ? -34.787 -13.180 2.653   1.00 56.14  ? 238 ILE   A CA  1 
ATOM   1627 C  C   . ILE   A 1 217 ? -33.516 -13.391 1.843   1.00 58.82  ? 238 ILE   A C   1 
ATOM   1628 O  O   . ILE   A 1 217 ? -32.799 -12.430 1.537   1.00 60.14  ? 238 ILE   A O   1 
ATOM   1629 C  CB  . ILE   A 1 217 ? -35.827 -12.368 1.863   1.00 58.20  ? 238 ILE   A CB  1 
ATOM   1630 C  CG1 . ILE   A 1 217 ? -37.162 -12.337 2.613   1.00 53.10  ? 238 ILE   A CG1 1 
ATOM   1631 C  CG2 . ILE   A 1 217 ? -36.008 -12.942 0.466   1.00 59.73  ? 238 ILE   A CG2 1 
ATOM   1632 C  CD1 . ILE   A 1 217 ? -38.276 -11.634 1.861   1.00 51.89  ? 238 ILE   A CD1 1 
ATOM   1633 N  N   . CYS   A 1 218 ? -33.233 -14.645 1.496   1.00 64.21  ? 239 CYS   A N   1 
ATOM   1634 C  CA  . CYS   A 1 218 ? -31.966 -15.027 0.888   1.00 64.53  ? 239 CYS   A CA  1 
ATOM   1635 C  C   . CYS   A 1 218 ? -32.210 -15.791 -0.405  1.00 63.91  ? 239 CYS   A C   1 
ATOM   1636 O  O   . CYS   A 1 218 ? -33.152 -16.583 -0.501  1.00 66.42  ? 239 CYS   A O   1 
ATOM   1637 C  CB  . CYS   A 1 218 ? -31.137 -15.883 1.855   1.00 66.10  ? 239 CYS   A CB  1 
ATOM   1638 S  SG  . CYS   A 1 218 ? -29.634 -16.588 1.143   1.00 71.56  ? 239 CYS   A SG  1 
ATOM   1639 N  N   . VAL   A 1 219 ? -31.345 -15.556 -1.398  1.00 65.53  ? 240 VAL   A N   1 
ATOM   1640 C  CA  . VAL   A 1 219 ? -31.478 -16.241 -2.682  1.00 66.90  ? 240 VAL   A CA  1 
ATOM   1641 C  C   . VAL   A 1 219 ? -31.258 -17.739 -2.524  1.00 66.74  ? 240 VAL   A C   1 
ATOM   1642 O  O   . VAL   A 1 219 ? -31.842 -18.542 -3.263  1.00 67.67  ? 240 VAL   A O   1 
ATOM   1643 C  CB  . VAL   A 1 219 ? -30.518 -15.632 -3.725  1.00 62.34  ? 240 VAL   A CB  1 
ATOM   1644 C  CG1 . VAL   A 1 219 ? -30.915 -14.197 -4.038  1.00 62.66  ? 240 VAL   A CG1 1 
ATOM   1645 C  CG2 . VAL   A 1 219 ? -29.076 -15.699 -3.243  1.00 61.17  ? 240 VAL   A CG2 1 
ATOM   1646 N  N   . PHE   A 1 220 ? -30.414 -18.140 -1.582  1.00 67.05  ? 241 PHE   A N   1 
ATOM   1647 C  CA  . PHE   A 1 220 ? -30.256 -19.555 -1.269  1.00 70.21  ? 241 PHE   A CA  1 
ATOM   1648 C  C   . PHE   A 1 220 ? -31.434 -20.028 -0.424  1.00 73.47  ? 241 PHE   A C   1 
ATOM   1649 O  O   . PHE   A 1 220 ? -31.773 -19.380 0.571   1.00 72.94  ? 241 PHE   A O   1 
ATOM   1650 C  CB  . PHE   A 1 220 ? -28.946 -19.801 -0.526  1.00 69.16  ? 241 PHE   A CB  1 
ATOM   1651 C  CG  . PHE   A 1 220 ? -27.719 -19.430 -1.313  1.00 68.62  ? 241 PHE   A CG  1 
ATOM   1652 C  CD1 . PHE   A 1 220 ? -27.227 -18.136 -1.290  1.00 68.36  ? 241 PHE   A CD1 1 
ATOM   1653 C  CD2 . PHE   A 1 220 ? -27.050 -20.380 -2.067  1.00 69.96  ? 241 PHE   A CD2 1 
ATOM   1654 C  CE1 . PHE   A 1 220 ? -26.096 -17.794 -2.010  1.00 65.41  ? 241 PHE   A CE1 1 
ATOM   1655 C  CE2 . PHE   A 1 220 ? -25.918 -20.045 -2.788  1.00 66.77  ? 241 PHE   A CE2 1 
ATOM   1656 C  CZ  . PHE   A 1 220 ? -25.442 -18.751 -2.759  1.00 64.31  ? 241 PHE   A CZ  1 
ATOM   1657 N  N   . PRO   A 1 221 ? -32.089 -21.129 -0.792  1.00 74.07  ? 242 PRO   A N   1 
ATOM   1658 C  CA  . PRO   A 1 221 ? -33.229 -21.617 0.002   1.00 77.48  ? 242 PRO   A CA  1 
ATOM   1659 C  C   . PRO   A 1 221 ? -32.822 -21.914 1.437   1.00 82.36  ? 242 PRO   A C   1 
ATOM   1660 O  O   . PRO   A 1 221 ? -31.889 -22.679 1.692   1.00 80.66  ? 242 PRO   A O   1 
ATOM   1661 C  CB  . PRO   A 1 221 ? -33.656 -22.888 -0.743  1.00 78.16  ? 242 PRO   A CB  1 
ATOM   1662 C  CG  . PRO   A 1 221 ? -33.155 -22.699 -2.138  1.00 74.47  ? 242 PRO   A CG  1 
ATOM   1663 C  CD  . PRO   A 1 221 ? -31.869 -21.937 -2.005  1.00 71.90  ? 242 PRO   A CD  1 
ATOM   1664 N  N   . ARG   A 1 222 ? -33.547 -21.306 2.383   1.00 84.97  ? 243 ARG   A N   1 
ATOM   1665 C  CA  . ARG   A 1 222 ? -33.189 -21.439 3.793   1.00 84.86  ? 243 ARG   A CA  1 
ATOM   1666 C  C   . ARG   A 1 222 ? -33.329 -22.875 4.281   1.00 85.82  ? 243 ARG   A C   1 
ATOM   1667 O  O   . ARG   A 1 222 ? -32.629 -23.283 5.215   1.00 87.81  ? 243 ARG   A O   1 
ATOM   1668 C  CB  . ARG   A 1 222 ? -34.047 -20.504 4.649   1.00 88.22  ? 243 ARG   A CB  1 
ATOM   1669 C  CG  . ARG   A 1 222 ? -33.629 -20.462 6.115   1.00 88.60  ? 243 ARG   A CG  1 
ATOM   1670 C  CD  . ARG   A 1 222 ? -34.639 -19.734 6.985   1.00 91.08  ? 243 ARG   A CD  1 
ATOM   1671 N  NE  . ARG   A 1 222 ? -34.686 -18.303 6.710   1.00 92.04  ? 243 ARG   A NE  1 
ATOM   1672 C  CZ  . ARG   A 1 222 ? -35.413 -17.434 7.400   1.00 86.69  ? 243 ARG   A CZ  1 
ATOM   1673 N  NH1 . ARG   A 1 222 ? -36.162 -17.817 8.421   1.00 86.77  ? 243 ARG   A NH1 1 
ATOM   1674 N  NH2 . ARG   A 1 222 ? -35.387 -16.150 7.057   1.00 80.37  ? 243 ARG   A NH2 1 
ATOM   1675 N  N   . GLU   A 1 223 ? -34.223 -23.653 3.667   1.00 86.59  ? 244 GLU   A N   1 
ATOM   1676 C  CA  . GLU   A 1 223 ? -34.377 -25.052 4.056   1.00 86.18  ? 244 GLU   A CA  1 
ATOM   1677 C  C   . GLU   A 1 223 ? -33.086 -25.827 3.827   1.00 86.21  ? 244 GLU   A C   1 
ATOM   1678 O  O   . GLU   A 1 223 ? -32.650 -26.602 4.685   1.00 87.61  ? 244 GLU   A O   1 
ATOM   1679 C  CB  . GLU   A 1 223 ? -35.534 -25.685 3.282   1.00 81.06  ? 244 GLU   A CB  1 
ATOM   1680 N  N   . VAL   A 1 224 ? -32.453 -25.620 2.671   1.00 85.21  ? 245 VAL   A N   1 
ATOM   1681 C  CA  . VAL   A 1 224 ? -31.210 -26.320 2.364   1.00 83.45  ? 245 VAL   A CA  1 
ATOM   1682 C  C   . VAL   A 1 224 ? -30.065 -25.797 3.226   1.00 85.08  ? 245 VAL   A C   1 
ATOM   1683 O  O   . VAL   A 1 224 ? -29.213 -26.569 3.680   1.00 86.15  ? 245 VAL   A O   1 
ATOM   1684 C  CB  . VAL   A 1 224 ? -30.889 -26.201 0.862   1.00 75.73  ? 245 VAL   A CB  1 
ATOM   1685 N  N   . THR   A 1 225 ? -30.018 -24.481 3.456   1.00 83.68  ? 246 THR   A N   1 
ATOM   1686 C  CA  . THR   A 1 225 ? -28.888 -23.898 4.174   1.00 84.08  ? 246 THR   A CA  1 
ATOM   1687 C  C   . THR   A 1 225 ? -28.904 -24.276 5.650   1.00 85.86  ? 246 THR   A C   1 
ATOM   1688 O  O   . THR   A 1 225 ? -27.864 -24.636 6.214   1.00 86.24  ? 246 THR   A O   1 
ATOM   1689 C  CB  . THR   A 1 225 ? -28.884 -22.377 4.015   1.00 84.51  ? 246 THR   A CB  1 
ATOM   1690 O  OG1 . THR   A 1 225 ? -30.042 -21.822 4.654   1.00 87.10  ? 246 THR   A OG1 1 
ATOM   1691 C  CG2 . THR   A 1 225 ? -28.890 -21.993 2.542   1.00 79.54  ? 246 THR   A CG2 1 
ATOM   1692 N  N   . ASN   A 1 226 ? -30.068 -24.191 6.296   1.00 86.60  ? 247 ASN   A N   1 
ATOM   1693 C  CA  . ASN   A 1 226 ? -30.144 -24.528 7.714   1.00 88.22  ? 247 ASN   A CA  1 
ATOM   1694 C  C   . ASN   A 1 226 ? -29.933 -26.019 7.940   1.00 88.34  ? 247 ASN   A C   1 
ATOM   1695 O  O   . ASN   A 1 226 ? -29.342 -26.421 8.950   1.00 87.84  ? 247 ASN   A O   1 
ATOM   1696 C  CB  . ASN   A 1 226 ? -31.484 -24.075 8.291   1.00 89.08  ? 247 ASN   A CB  1 
ATOM   1697 C  CG  . ASN   A 1 226 ? -31.615 -22.566 8.338   1.00 92.48  ? 247 ASN   A CG  1 
ATOM   1698 O  OD1 . ASN   A 1 226 ? -30.790 -21.845 7.775   1.00 91.01  ? 247 ASN   A OD1 1 
ATOM   1699 N  ND2 . ASN   A 1 226 ? -32.655 -22.079 9.006   1.00 96.06  ? 247 ASN   A ND2 1 
ATOM   1700 N  N   . PHE   A 1 227 ? -30.419 -26.854 7.019   1.00 87.23  ? 248 PHE   A N   1 
ATOM   1701 C  CA  . PHE   A 1 227 ? -30.183 -28.290 7.120   1.00 87.41  ? 248 PHE   A CA  1 
ATOM   1702 C  C   . PHE   A 1 227 ? -28.694 -28.606 7.067   1.00 88.90  ? 248 PHE   A C   1 
ATOM   1703 O  O   . PHE   A 1 227 ? -28.182 -29.381 7.882   1.00 90.79  ? 248 PHE   A O   1 
ATOM   1704 C  CB  . PHE   A 1 227 ? -30.932 -29.024 6.005   1.00 86.79  ? 248 PHE   A CB  1 
ATOM   1705 C  CG  . PHE   A 1 227 ? -30.476 -30.444 5.794   1.00 90.08  ? 248 PHE   A CG  1 
ATOM   1706 C  CD1 . PHE   A 1 227 ? -30.957 -31.467 6.593   1.00 90.20  ? 248 PHE   A CD1 1 
ATOM   1707 C  CD2 . PHE   A 1 227 ? -29.579 -30.759 4.782   1.00 90.94  ? 248 PHE   A CD2 1 
ATOM   1708 C  CE1 . PHE   A 1 227 ? -30.545 -32.773 6.398   1.00 91.52  ? 248 PHE   A CE1 1 
ATOM   1709 C  CE2 . PHE   A 1 227 ? -29.164 -32.062 4.582   1.00 90.11  ? 248 PHE   A CE2 1 
ATOM   1710 C  CZ  . PHE   A 1 227 ? -29.648 -33.071 5.391   1.00 90.93  ? 248 PHE   A CZ  1 
ATOM   1711 N  N   . LEU   A 1 228 ? -27.980 -28.004 6.113   1.00 87.60  ? 249 LEU   A N   1 
ATOM   1712 C  CA  . LEU   A 1 228 ? -26.565 -28.315 5.941   1.00 88.76  ? 249 LEU   A CA  1 
ATOM   1713 C  C   . LEU   A 1 228 ? -25.718 -27.763 7.081   1.00 90.44  ? 249 LEU   A C   1 
ATOM   1714 O  O   . LEU   A 1 228 ? -24.742 -28.403 7.486   1.00 91.48  ? 249 LEU   A O   1 
ATOM   1715 C  CB  . LEU   A 1 228 ? -26.072 -27.787 4.594   1.00 87.28  ? 249 LEU   A CB  1 
ATOM   1716 C  CG  . LEU   A 1 228 ? -26.546 -28.563 3.363   1.00 88.56  ? 249 LEU   A CG  1 
ATOM   1717 C  CD1 . LEU   A 1 228 ? -26.005 -27.931 2.090   1.00 83.79  ? 249 LEU   A CD1 1 
ATOM   1718 C  CD2 . LEU   A 1 228 ? -26.131 -30.026 3.456   1.00 85.97  ? 249 LEU   A CD2 1 
ATOM   1719 N  N   . ARG   A 1 229 ? -26.067 -26.587 7.611   1.00 90.84  ? 250 ARG   A N   1 
ATOM   1720 C  CA  . ARG   A 1 229 ? -25.328 -26.063 8.756   1.00 91.08  ? 250 ARG   A CA  1 
ATOM   1721 C  C   . ARG   A 1 229 ? -25.497 -26.966 9.970   1.00 91.06  ? 250 ARG   A C   1 
ATOM   1722 O  O   . ARG   A 1 229 ? -24.537 -27.206 10.711  1.00 91.40  ? 250 ARG   A O   1 
ATOM   1723 C  CB  . ARG   A 1 229 ? -25.773 -24.633 9.072   1.00 90.11  ? 250 ARG   A CB  1 
ATOM   1724 C  CG  . ARG   A 1 229 ? -24.840 -23.895 10.031  1.00 89.50  ? 250 ARG   A CG  1 
ATOM   1725 C  CD  . ARG   A 1 229 ? -25.037 -22.383 9.973   1.00 91.26  ? 250 ARG   A CD  1 
ATOM   1726 N  NE  . ARG   A 1 229 ? -26.261 -21.953 10.639  1.00 96.65  ? 250 ARG   A NE  1 
ATOM   1727 C  CZ  . ARG   A 1 229 ? -26.674 -20.695 10.712  1.00 92.72  ? 250 ARG   A CZ  1 
ATOM   1728 N  NH1 . ARG   A 1 229 ? -25.988 -19.708 10.157  1.00 85.77  ? 250 ARG   A NH1 1 
ATOM   1729 N  NH2 . ARG   A 1 229 ? -27.803 -20.419 11.357  1.00 90.38  ? 250 ARG   A NH2 1 
ATOM   1730 N  N   . LYS   A 1 230 ? -26.711 -27.478 10.186  1.00 89.61  ? 251 LYS   A N   1 
ATOM   1731 C  CA  . LYS   A 1 230 ? -26.924 -28.457 11.247  1.00 90.31  ? 251 LYS   A CA  1 
ATOM   1732 C  C   . LYS   A 1 230 ? -26.288 -29.796 10.898  1.00 93.58  ? 251 LYS   A C   1 
ATOM   1733 O  O   . LYS   A 1 230 ? -25.699 -30.454 11.763  1.00 97.46  ? 251 LYS   A O   1 
ATOM   1734 C  CB  . LYS   A 1 230 ? -28.420 -28.627 11.514  1.00 89.64  ? 251 LYS   A CB  1 
ATOM   1735 N  N   . SER   A 1 231 ? -26.404 -30.219 9.635   1.00 92.27  ? 252 SER   A N   1 
ATOM   1736 C  CA  . SER   A 1 231 ? -25.804 -31.483 9.218   1.00 92.65  ? 252 SER   A CA  1 
ATOM   1737 C  C   . SER   A 1 231 ? -24.291 -31.447 9.370   1.00 92.39  ? 252 SER   A C   1 
ATOM   1738 O  O   . SER   A 1 231 ? -23.682 -32.421 9.828   1.00 95.29  ? 252 SER   A O   1 
ATOM   1739 C  CB  . SER   A 1 231 ? -26.190 -31.804 7.775   1.00 91.88  ? 252 SER   A CB  1 
ATOM   1740 O  OG  . SER   A 1 231 ? -27.575 -32.085 7.670   1.00 94.60  ? 252 SER   A OG  1 
ATOM   1741 N  N   . VAL   A 1 232 ? -23.665 -30.332 8.988   1.00 91.55  ? 253 VAL   A N   1 
ATOM   1742 C  CA  . VAL   A 1 232 ? -22.237 -30.171 9.240   1.00 92.97  ? 253 VAL   A CA  1 
ATOM   1743 C  C   . VAL   A 1 232 ? -21.960 -30.228 10.735  1.00 96.17  ? 253 VAL   A C   1 
ATOM   1744 O  O   . VAL   A 1 232 ? -21.016 -30.888 11.180  1.00 99.23  ? 253 VAL   A O   1 
ATOM   1745 C  CB  . VAL   A 1 232 ? -21.723 -28.861 8.612   1.00 90.53  ? 253 VAL   A CB  1 
ATOM   1746 C  CG1 . VAL   A 1 232 ? -20.364 -28.491 9.183   1.00 87.91  ? 253 VAL   A CG1 1 
ATOM   1747 C  CG2 . VAL   A 1 232 ? -21.639 -28.998 7.099   1.00 88.08  ? 253 VAL   A CG2 1 
ATOM   1748 N  N   . LYS   A 1 233 ? -22.809 -29.577 11.536  1.00 96.12  ? 254 LYS   A N   1 
ATOM   1749 C  CA  . LYS   A 1 233 ? -22.590 -29.527 12.979  1.00 97.85  ? 254 LYS   A CA  1 
ATOM   1750 C  C   . LYS   A 1 233 ? -22.592 -30.920 13.598  1.00 100.41 ? 254 LYS   A C   1 
ATOM   1751 O  O   . LYS   A 1 233 ? -21.772 -31.216 14.475  1.00 102.48 ? 254 LYS   A O   1 
ATOM   1752 C  CB  . LYS   A 1 233 ? -23.652 -28.648 13.640  1.00 92.70  ? 254 LYS   A CB  1 
ATOM   1753 N  N   . ARG   A 1 234 ? -23.507 -31.791 13.160  1.00 99.38  ? 255 ARG   A N   1 
ATOM   1754 C  CA  . ARG   A 1 234 ? -23.578 -33.126 13.746  1.00 100.23 ? 255 ARG   A CA  1 
ATOM   1755 C  C   . ARG   A 1 234 ? -22.333 -33.944 13.418  1.00 102.43 ? 255 ARG   A C   1 
ATOM   1756 O  O   . ARG   A 1 234 ? -21.867 -34.732 14.248  1.00 104.28 ? 255 ARG   A O   1 
ATOM   1757 C  CB  . ARG   A 1 234 ? -24.847 -33.850 13.282  1.00 98.53  ? 255 ARG   A CB  1 
ATOM   1758 C  CG  . ARG   A 1 234 ? -24.720 -34.605 11.965  1.00 98.85  ? 255 ARG   A CG  1 
ATOM   1759 C  CD  . ARG   A 1 234 ? -25.780 -35.686 11.827  1.00 98.45  ? 255 ARG   A CD  1 
ATOM   1760 N  NE  . ARG   A 1 234 ? -25.461 -36.622 10.755  1.00 101.04 ? 255 ARG   A NE  1 
ATOM   1761 C  CZ  . ARG   A 1 234 ? -25.884 -36.504 9.504   1.00 100.91 ? 255 ARG   A CZ  1 
ATOM   1762 N  NH1 . ARG   A 1 234 ? -26.657 -35.498 9.128   1.00 95.15  ? 255 ARG   A NH1 1 
ATOM   1763 N  NH2 . ARG   A 1 234 ? -25.525 -37.419 8.609   1.00 101.25 ? 255 ARG   A NH2 1 
ATOM   1764 N  N   . MET   A 1 235 ? -21.771 -33.763 12.221  1.00 100.74 ? 256 MET   A N   1 
ATOM   1765 C  CA  . MET   A 1 235 ? -20.607 -34.532 11.802  1.00 101.99 ? 256 MET   A CA  1 
ATOM   1766 C  C   . MET   A 1 235 ? -19.291 -33.793 11.998  1.00 103.32 ? 256 MET   A C   1 
ATOM   1767 O  O   . MET   A 1 235 ? -18.233 -34.432 11.964  1.00 105.63 ? 256 MET   A O   1 
ATOM   1768 C  CB  . MET   A 1 235 ? -20.740 -34.937 10.328  1.00 101.25 ? 256 MET   A CB  1 
ATOM   1769 C  CG  . MET   A 1 235 ? -20.818 -33.765 9.364   1.00 99.57  ? 256 MET   A CG  1 
ATOM   1770 S  SD  . MET   A 1 235 ? -21.127 -34.293 7.670   1.00 97.12  ? 256 MET   A SD  1 
ATOM   1771 C  CE  . MET   A 1 235 ? -22.630 -35.241 7.887   1.00 95.96  ? 256 MET   A CE  1 
ATOM   1772 N  N   . LYS   A 1 236 ? -19.328 -32.473 12.195  1.00 102.46 ? 257 LYS   A N   1 
ATOM   1773 C  CA  . LYS   A 1 236 ? -18.098 -31.719 12.416  1.00 105.38 ? 257 LYS   A CA  1 
ATOM   1774 C  C   . LYS   A 1 236 ? -17.409 -32.162 13.700  1.00 108.73 ? 257 LYS   A C   1 
ATOM   1775 O  O   . LYS   A 1 236 ? -16.209 -32.456 13.705  1.00 108.67 ? 257 LYS   A O   1 
ATOM   1776 C  CB  . LYS   A 1 236 ? -18.407 -30.221 12.452  1.00 100.86 ? 257 LYS   A CB  1 
ATOM   1777 C  CG  . LYS   A 1 236 ? -17.208 -29.294 12.536  1.00 99.88  ? 257 LYS   A CG  1 
ATOM   1778 C  CD  . LYS   A 1 236 ? -17.671 -27.849 12.400  1.00 98.83  ? 257 LYS   A CD  1 
ATOM   1779 C  CE  . LYS   A 1 236 ? -16.792 -26.886 13.183  1.00 96.21  ? 257 LYS   A CE  1 
ATOM   1780 N  NZ  . LYS   A 1 236 ? -15.649 -26.367 12.383  1.00 91.82  ? 257 LYS   A NZ  1 
ATOM   1781 N  N   . GLU   A 1 237 ? -18.158 -32.227 14.798  1.00 108.56 ? 258 GLU   A N   1 
ATOM   1782 C  CA  . GLU   A 1 237 ? -17.608 -32.605 16.096  1.00 109.83 ? 258 GLU   A CA  1 
ATOM   1783 C  C   . GLU   A 1 237 ? -18.313 -33.792 16.732  1.00 108.51 ? 258 GLU   A C   1 
ATOM   1784 O  O   . GLU   A 1 237 ? -17.649 -34.661 17.302  1.00 109.08 ? 258 GLU   A O   1 
ATOM   1785 C  CB  . GLU   A 1 237 ? -17.667 -31.411 17.059  1.00 110.44 ? 258 GLU   A CB  1 
ATOM   1786 C  CG  . GLU   A 1 237 ? -17.230 -30.079 16.457  1.00 108.74 ? 258 GLU   A CG  1 
ATOM   1787 C  CD  . GLU   A 1 237 ? -15.726 -29.964 16.287  1.00 111.97 ? 258 GLU   A CD  1 
ATOM   1788 O  OE1 . GLU   A 1 237 ? -15.166 -30.618 15.383  1.00 110.87 ? 258 GLU   A OE1 1 
ATOM   1789 O  OE2 . GLU   A 1 237 ? -15.099 -29.215 17.066  1.00 115.09 ? 258 GLU   A OE2 1 
ATOM   1790 N  N   . SER   A 1 238 ? -19.645 -33.858 16.649  1.00 107.06 ? 259 SER   A N   1 
ATOM   1791 C  CA  . SER   A 1 238 ? -20.395 -34.906 17.334  1.00 109.22 ? 259 SER   A CA  1 
ATOM   1792 C  C   . SER   A 1 238 ? -20.224 -36.280 16.698  1.00 111.27 ? 259 SER   A C   1 
ATOM   1793 O  O   . SER   A 1 238 ? -20.637 -37.275 17.304  1.00 111.46 ? 259 SER   A O   1 
ATOM   1794 C  CB  . SER   A 1 238 ? -21.881 -34.541 17.385  1.00 106.83 ? 259 SER   A CB  1 
ATOM   1795 N  N   . ARG   A 1 239 ? -19.641 -36.364 15.500  1.00 110.32 ? 260 ARG   A N   1 
ATOM   1796 C  CA  . ARG   A 1 239 ? -19.342 -37.645 14.877  1.00 108.93 ? 260 ARG   A CA  1 
ATOM   1797 C  C   . ARG   A 1 239 ? -17.910 -37.746 14.371  1.00 110.82 ? 260 ARG   A C   1 
ATOM   1798 O  O   . ARG   A 1 239 ? -17.529 -38.800 13.851  1.00 114.81 ? 260 ARG   A O   1 
ATOM   1799 C  CB  . ARG   A 1 239 ? -20.302 -37.922 13.709  1.00 109.24 ? 260 ARG   A CB  1 
ATOM   1800 C  CG  . ARG   A 1 239 ? -21.775 -37.897 14.078  1.00 107.67 ? 260 ARG   A CG  1 
ATOM   1801 C  CD  . ARG   A 1 239 ? -22.651 -38.397 12.935  1.00 107.52 ? 260 ARG   A CD  1 
ATOM   1802 N  NE  . ARG   A 1 239 ? -22.173 -37.961 11.627  1.00 107.53 ? 260 ARG   A NE  1 
ATOM   1803 C  CZ  . ARG   A 1 239 ? -21.579 -38.754 10.746  1.00 107.03 ? 260 ARG   A CZ  1 
ATOM   1804 N  NH1 . ARG   A 1 239 ? -21.386 -40.039 10.993  1.00 106.62 ? 260 ARG   A NH1 1 
ATOM   1805 N  NH2 . ARG   A 1 239 ? -21.167 -38.244 9.588   1.00 104.55 ? 260 ARG   A NH2 1 
ATOM   1806 N  N   . LEU   A 1 240 ? -17.113 -36.689 14.502  1.00 109.96 ? 261 LEU   A N   1 
ATOM   1807 C  CA  . LEU   A 1 240 ? -15.727 -36.672 14.046  1.00 111.77 ? 261 LEU   A CA  1 
ATOM   1808 C  C   . LEU   A 1 240 ? -14.723 -36.683 15.186  1.00 112.61 ? 261 LEU   A C   1 
ATOM   1809 O  O   . LEU   A 1 240 ? -13.729 -37.409 15.118  1.00 112.04 ? 261 LEU   A O   1 
ATOM   1810 C  CB  . LEU   A 1 240 ? -15.486 -35.442 13.156  1.00 109.19 ? 261 LEU   A CB  1 
ATOM   1811 C  CG  . LEU   A 1 240 ? -14.127 -35.125 12.515  1.00 106.91 ? 261 LEU   A CG  1 
ATOM   1812 C  CD1 . LEU   A 1 240 ? -13.257 -34.254 13.419  1.00 107.50 ? 261 LEU   A CD1 1 
ATOM   1813 C  CD2 . LEU   A 1 240 ? -13.383 -36.390 12.106  1.00 108.03 ? 261 LEU   A CD2 1 
ATOM   1814 N  N   . GLU   A 1 241 ? -14.953 -35.892 16.236  1.00 112.91 ? 262 GLU   A N   1 
ATOM   1815 C  CA  . GLU   A 1 241 ? -14.044 -35.904 17.377  1.00 113.16 ? 262 GLU   A CA  1 
ATOM   1816 C  C   . GLU   A 1 241 ? -14.085 -37.243 18.101  1.00 114.47 ? 262 GLU   A C   1 
ATOM   1817 O  O   . GLU   A 1 241 ? -13.050 -37.735 18.570  1.00 114.52 ? 262 GLU   A O   1 
ATOM   1818 C  CB  . GLU   A 1 241 ? -14.379 -34.759 18.330  1.00 115.13 ? 262 GLU   A CB  1 
ATOM   1819 C  CG  . GLU   A 1 241 ? -14.196 -33.385 17.714  1.00 113.99 ? 262 GLU   A CG  1 
ATOM   1820 C  CD  . GLU   A 1 241 ? -12.781 -33.153 17.217  1.00 116.48 ? 262 GLU   A CD  1 
ATOM   1821 O  OE1 . GLU   A 1 241 ? -11.830 -33.640 17.867  1.00 115.57 ? 262 GLU   A OE1 1 
ATOM   1822 O  OE2 . GLU   A 1 241 ? -12.619 -32.487 16.173  1.00 118.89 ? 262 GLU   A OE2 1 
ATOM   1823 N  N   . ASP   A 1 242 ? -15.267 -37.847 18.206  1.00 113.92 ? 263 ASP   A N   1 
ATOM   1824 C  CA  . ASP   A 1 242 ? -15.384 -39.172 18.802  1.00 114.12 ? 263 ASP   A CA  1 
ATOM   1825 C  C   . ASP   A 1 242 ? -15.136 -40.244 17.747  1.00 112.89 ? 263 ASP   A C   1 
ATOM   1826 O  O   . ASP   A 1 242 ? -15.949 -41.159 17.580  1.00 111.77 ? 263 ASP   A O   1 
ATOM   1827 C  CB  . ASP   A 1 242 ? -16.762 -39.351 19.438  1.00 112.91 ? 263 ASP   A CB  1 
ATOM   1828 C  CG  . ASP   A 1 242 ? -17.112 -38.226 20.397  1.00 116.91 ? 263 ASP   A CG  1 
ATOM   1829 O  OD1 . ASP   A 1 242 ? -16.257 -37.338 20.614  1.00 116.86 ? 263 ASP   A OD1 1 
ATOM   1830 O  OD2 . ASP   A 1 242 ? -18.238 -38.225 20.931  1.00 120.01 ? 263 ASP   A OD2 1 
ATOM   1831 N  N   . THR   A 1 243 ? -14.008 -40.139 17.043  1.00 111.51 ? 264 THR   A N   1 
ATOM   1832 C  CA  . THR   A 1 243 ? -13.633 -41.048 15.969  1.00 113.59 ? 264 THR   A CA  1 
ATOM   1833 C  C   . THR   A 1 243 ? -12.181 -40.776 15.604  1.00 112.26 ? 264 THR   A C   1 
ATOM   1834 O  O   . THR   A 1 243 ? -11.756 -39.618 15.570  1.00 110.81 ? 264 THR   A O   1 
ATOM   1835 C  CB  . THR   A 1 243 ? -14.536 -40.867 14.736  1.00 113.40 ? 264 THR   A CB  1 
ATOM   1836 O  OG1 . THR   A 1 243 ? -15.869 -41.291 15.046  1.00 110.56 ? 264 THR   A OG1 1 
ATOM   1837 C  CG2 . THR   A 1 243 ? -14.018 -41.677 13.553  1.00 113.06 ? 264 THR   A CG2 1 
ATOM   1838 N  N   . GLN   A 1 244 ? -11.424 -41.845 15.341  1.00 110.57 ? 265 GLN   A N   1 
ATOM   1839 C  CA  . GLN   A 1 244 ? -10.019 -41.732 14.961  1.00 109.79 ? 265 GLN   A CA  1 
ATOM   1840 C  C   . GLN   A 1 244 ? -9.751  -42.280 13.564  1.00 110.82 ? 265 GLN   A C   1 
ATOM   1841 O  O   . GLN   A 1 244 ? -8.599  -42.567 13.226  1.00 109.19 ? 265 GLN   A O   1 
ATOM   1842 C  CB  . GLN   A 1 244 ? -9.128  -42.439 15.984  1.00 107.20 ? 265 GLN   A CB  1 
ATOM   1843 N  N   . LYS   A 1 245 ? -10.788 -42.443 12.749  1.00 111.50 ? 266 LYS   A N   1 
ATOM   1844 C  CA  . LYS   A 1 245 ? -10.591 -42.882 11.378  1.00 110.76 ? 266 LYS   A CA  1 
ATOM   1845 C  C   . LYS   A 1 245 ? -9.990  -41.757 10.540  1.00 113.93 ? 266 LYS   A C   1 
ATOM   1846 O  O   . LYS   A 1 245 ? -9.993  -40.585 10.926  1.00 114.65 ? 266 LYS   A O   1 
ATOM   1847 C  CB  . LYS   A 1 245 ? -11.912 -43.345 10.765  1.00 107.57 ? 266 LYS   A CB  1 
ATOM   1848 N  N   . HIS   A 1 246 ? -9.456  -42.132 9.383   1.00 110.60 ? 267 HIS   A N   1 
ATOM   1849 C  CA  . HIS   A 1 246 ? -8.954  -41.148 8.439   1.00 109.54 ? 267 HIS   A CA  1 
ATOM   1850 C  C   . HIS   A 1 246 ? -10.091 -40.629 7.568   1.00 108.86 ? 267 HIS   A C   1 
ATOM   1851 O  O   . HIS   A 1 246 ? -11.018 -41.363 7.213   1.00 105.79 ? 267 HIS   A O   1 
ATOM   1852 C  CB  . HIS   A 1 246 ? -7.856  -41.748 7.562   1.00 110.39 ? 267 HIS   A CB  1 
ATOM   1853 N  N   . ARG   A 1 247 ? -10.019 -39.343 7.236   1.00 107.29 ? 268 ARG   A N   1 
ATOM   1854 C  CA  . ARG   A 1 247 ? -11.003 -38.696 6.382   1.00 102.97 ? 268 ARG   A CA  1 
ATOM   1855 C  C   . ARG   A 1 247 ? -10.289 -37.885 5.313   1.00 97.01  ? 268 ARG   A C   1 
ATOM   1856 O  O   . ARG   A 1 247 ? -9.228  -37.306 5.563   1.00 93.99  ? 268 ARG   A O   1 
ATOM   1857 C  CB  . ARG   A 1 247 ? -11.950 -37.803 7.195   1.00 102.41 ? 268 ARG   A CB  1 
ATOM   1858 C  CG  . ARG   A 1 247 ? -13.115 -38.554 7.822   1.00 101.30 ? 268 ARG   A CG  1 
ATOM   1859 C  CD  . ARG   A 1 247 ? -13.836 -37.701 8.852   1.00 103.07 ? 268 ARG   A CD  1 
ATOM   1860 N  NE  . ARG   A 1 247 ? -14.414 -36.492 8.279   1.00 103.59 ? 268 ARG   A NE  1 
ATOM   1861 C  CZ  . ARG   A 1 247 ? -15.716 -36.264 8.162   1.00 98.40  ? 268 ARG   A CZ  1 
ATOM   1862 N  NH1 . ARG   A 1 247 ? -16.612 -37.145 8.574   1.00 100.60 ? 268 ARG   A NH1 1 
ATOM   1863 N  NH2 . ARG   A 1 247 ? -16.129 -35.118 7.627   1.00 91.07  ? 268 ARG   A NH2 1 
ATOM   1864 N  N   . VAL   A 1 248 ? -10.880 -37.849 4.119   1.00 94.99  ? 269 VAL   A N   1 
ATOM   1865 C  CA  . VAL   A 1 248 ? -10.280 -37.209 2.956   1.00 94.27  ? 269 VAL   A CA  1 
ATOM   1866 C  C   . VAL   A 1 248 ? -11.193 -36.166 2.329   1.00 92.61  ? 269 VAL   A C   1 
ATOM   1867 O  O   . VAL   A 1 248 ? -10.805 -35.529 1.345   1.00 87.90  ? 269 VAL   A O   1 
ATOM   1868 C  CB  . VAL   A 1 248 ? -9.863  -38.260 1.905   1.00 91.24  ? 269 VAL   A CB  1 
ATOM   1869 C  CG1 . VAL   A 1 248 ? -11.073 -38.732 1.111   1.00 89.55  ? 269 VAL   A CG1 1 
ATOM   1870 C  CG2 . VAL   A 1 248 ? -8.756  -37.730 0.993   1.00 91.73  ? 269 VAL   A CG2 1 
ATOM   1871 N  N   . ASP   A 1 249 ? -12.390 -35.961 2.874   1.00 90.69  ? 270 ASP   A N   1 
ATOM   1872 C  CA  . ASP   A 1 249 ? -13.340 -35.051 2.256   1.00 86.82  ? 270 ASP   A CA  1 
ATOM   1873 C  C   . ASP   A 1 249 ? -12.908 -33.596 2.448   1.00 86.45  ? 270 ASP   A C   1 
ATOM   1874 O  O   . ASP   A 1 249 ? -12.015 -33.277 3.238   1.00 86.51  ? 270 ASP   A O   1 
ATOM   1875 C  CB  . ASP   A 1 249 ? -14.744 -35.272 2.822   1.00 86.89  ? 270 ASP   A CB  1 
ATOM   1876 C  CG  . ASP   A 1 249 ? -14.772 -35.282 4.340   1.00 91.49  ? 270 ASP   A CG  1 
ATOM   1877 O  OD1 . ASP   A 1 249 ? -14.271 -34.318 4.958   1.00 92.57  ? 270 ASP   A OD1 1 
ATOM   1878 O  OD2 . ASP   A 1 249 ? -15.312 -36.251 4.916   1.00 92.69  ? 270 ASP   A OD2 1 
ATOM   1879 N  N   . PHE   A 1 250 ? -13.561 -32.705 1.693   1.00 84.41  ? 271 PHE   A N   1 
ATOM   1880 C  CA  . PHE   A 1 250 ? -13.271 -31.278 1.805   1.00 82.93  ? 271 PHE   A CA  1 
ATOM   1881 C  C   . PHE   A 1 250 ? -13.515 -30.774 3.221   1.00 85.43  ? 271 PHE   A C   1 
ATOM   1882 O  O   . PHE   A 1 250 ? -12.782 -29.911 3.715   1.00 85.71  ? 271 PHE   A O   1 
ATOM   1883 C  CB  . PHE   A 1 250 ? -14.120 -30.482 0.812   1.00 77.41  ? 271 PHE   A CB  1 
ATOM   1884 C  CG  . PHE   A 1 250 ? -13.697 -30.641 -0.621  1.00 74.44  ? 271 PHE   A CG  1 
ATOM   1885 C  CD1 . PHE   A 1 250 ? -12.476 -30.154 -1.057  1.00 74.06  ? 271 PHE   A CD1 1 
ATOM   1886 C  CD2 . PHE   A 1 250 ? -14.534 -31.252 -1.539  1.00 72.98  ? 271 PHE   A CD2 1 
ATOM   1887 C  CE1 . PHE   A 1 250 ? -12.089 -30.291 -2.377  1.00 70.51  ? 271 PHE   A CE1 1 
ATOM   1888 C  CE2 . PHE   A 1 250 ? -14.153 -31.393 -2.860  1.00 69.85  ? 271 PHE   A CE2 1 
ATOM   1889 C  CZ  . PHE   A 1 250 ? -12.930 -30.911 -3.280  1.00 66.07  ? 271 PHE   A CZ  1 
ATOM   1890 N  N   . LEU   A 1 251 ? -14.546 -31.301 3.886   1.00 85.56  ? 272 LEU   A N   1 
ATOM   1891 C  CA  . LEU   A 1 251 ? -14.862 -30.865 5.243   1.00 86.96  ? 272 LEU   A CA  1 
ATOM   1892 C  C   . LEU   A 1 251 ? -13.699 -31.130 6.191   1.00 89.31  ? 272 LEU   A C   1 
ATOM   1893 O  O   . LEU   A 1 251 ? -13.328 -30.264 6.993   1.00 88.69  ? 272 LEU   A O   1 
ATOM   1894 C  CB  . LEU   A 1 251 ? -16.131 -31.566 5.729   1.00 86.65  ? 272 LEU   A CB  1 
ATOM   1895 C  CG  . LEU   A 1 251 ? -16.520 -31.441 7.203   1.00 86.71  ? 272 LEU   A CG  1 
ATOM   1896 C  CD1 . LEU   A 1 251 ? -16.610 -29.985 7.619   1.00 85.68  ? 272 LEU   A CD1 1 
ATOM   1897 C  CD2 . LEU   A 1 251 ? -17.841 -32.152 7.456   1.00 87.92  ? 272 LEU   A CD2 1 
ATOM   1898 N  N   . GLN   A 1 252 ? -13.105 -32.323 6.109   1.00 90.47  ? 273 GLN   A N   1 
ATOM   1899 C  CA  . GLN   A 1 252 ? -11.985 -32.651 6.985   1.00 93.03  ? 273 GLN   A CA  1 
ATOM   1900 C  C   . GLN   A 1 252 ? -10.793 -31.743 6.721   1.00 93.30  ? 273 GLN   A C   1 
ATOM   1901 O  O   . GLN   A 1 252 ? -10.120 -31.301 7.660   1.00 95.44  ? 273 GLN   A O   1 
ATOM   1902 C  CB  . GLN   A 1 252 ? -11.588 -34.116 6.807   1.00 95.07  ? 273 GLN   A CB  1 
ATOM   1903 C  CG  . GLN   A 1 252 ? -10.494 -34.579 7.756   1.00 97.54  ? 273 GLN   A CG  1 
ATOM   1904 C  CD  . GLN   A 1 252 ? -10.975 -34.697 9.190   1.00 98.64  ? 273 GLN   A CD  1 
ATOM   1905 O  OE1 . GLN   A 1 252 ? -12.177 -34.727 9.454   1.00 97.85  ? 273 GLN   A OE1 1 
ATOM   1906 N  NE2 . GLN   A 1 252 ? -10.035 -34.764 10.126  1.00 100.00 ? 273 GLN   A NE2 1 
ATOM   1907 N  N   . LEU   A 1 253 ? -10.513 -31.458 5.447   1.00 91.00  ? 274 LEU   A N   1 
ATOM   1908 C  CA  . LEU   A 1 253 ? -9.398  -30.577 5.116   1.00 91.91  ? 274 LEU   A CA  1 
ATOM   1909 C  C   . LEU   A 1 253 ? -9.628  -29.171 5.655   1.00 92.38  ? 274 LEU   A C   1 
ATOM   1910 O  O   . LEU   A 1 253 ? -8.682  -28.498 6.079   1.00 93.04  ? 274 LEU   A O   1 
ATOM   1911 C  CB  . LEU   A 1 253 ? -9.189  -30.550 3.601   1.00 88.88  ? 274 LEU   A CB  1 
ATOM   1912 C  CG  . LEU   A 1 253 ? -8.933  -31.919 2.966   1.00 86.87  ? 274 LEU   A CG  1 
ATOM   1913 C  CD1 . LEU   A 1 253 ? -8.852  -31.814 1.454   1.00 82.53  ? 274 LEU   A CD1 1 
ATOM   1914 C  CD2 . LEU   A 1 253 ? -7.666  -32.542 3.531   1.00 88.90  ? 274 LEU   A CD2 1 
ATOM   1915 N  N   . MET   A 1 254 ? -10.881 -28.710 5.645   1.00 93.62  ? 275 MET   A N   1 
ATOM   1916 C  CA  . MET   A 1 254 ? -11.203 -27.421 6.247   1.00 92.19  ? 275 MET   A CA  1 
ATOM   1917 C  C   . MET   A 1 254 ? -11.238 -27.495 7.769   1.00 91.75  ? 275 MET   A C   1 
ATOM   1918 O  O   . MET   A 1 254 ? -10.891 -26.516 8.439   1.00 90.27  ? 275 MET   A O   1 
ATOM   1919 C  CB  . MET   A 1 254 ? -12.541 -26.914 5.709   1.00 90.72  ? 275 MET   A CB  1 
ATOM   1920 C  CG  . MET   A 1 254 ? -12.565 -26.756 4.198   1.00 88.21  ? 275 MET   A CG  1 
ATOM   1921 S  SD  . MET   A 1 254 ? -14.176 -26.239 3.590   1.00 75.77  ? 275 MET   A SD  1 
ATOM   1922 C  CE  . MET   A 1 254 ? -14.352 -24.678 4.441   1.00 81.71  ? 275 MET   A CE  1 
ATOM   1923 N  N   . ILE   A 1 255 ? -11.660 -28.631 8.329   1.00 92.65  ? 276 ILE   A N   1 
ATOM   1924 C  CA  . ILE   A 1 255 ? -11.591 -28.817 9.776   1.00 93.22  ? 276 ILE   A CA  1 
ATOM   1925 C  C   . ILE   A 1 255 ? -10.141 -28.787 10.241  1.00 95.05  ? 276 ILE   A C   1 
ATOM   1926 O  O   . ILE   A 1 255 ? -9.796  -28.118 11.223  1.00 95.02  ? 276 ILE   A O   1 
ATOM   1927 C  CB  . ILE   A 1 255 ? -12.289 -30.126 10.187  1.00 90.61  ? 276 ILE   A CB  1 
ATOM   1928 C  CG1 . ILE   A 1 255 ? -13.809 -29.983 10.099  1.00 93.80  ? 276 ILE   A CG1 1 
ATOM   1929 C  CG2 . ILE   A 1 255 ? -11.876 -30.534 11.594  1.00 92.26  ? 276 ILE   A CG2 1 
ATOM   1930 C  CD1 . ILE   A 1 255 ? -14.557 -31.238 10.502  1.00 94.01  ? 276 ILE   A CD1 1 
ATOM   1931 N  N   . ASP   A 1 256 ? -9.268  -29.505 9.530   1.00 95.10  ? 277 ASP   A N   1 
ATOM   1932 C  CA  . ASP   A 1 256 ? -7.851  -29.515 9.874   1.00 96.22  ? 277 ASP   A CA  1 
ATOM   1933 C  C   . ASP   A 1 256 ? -7.198  -28.156 9.672   1.00 97.43  ? 277 ASP   A C   1 
ATOM   1934 O  O   . ASP   A 1 256 ? -6.180  -27.871 10.310  1.00 99.75  ? 277 ASP   A O   1 
ATOM   1935 C  CB  . ASP   A 1 256 ? -7.117  -30.575 9.053   1.00 99.26  ? 277 ASP   A CB  1 
ATOM   1936 C  CG  . ASP   A 1 256 ? -7.543  -31.984 9.409   1.00 100.90 ? 277 ASP   A CG  1 
ATOM   1937 O  OD1 . ASP   A 1 256 ? -8.581  -32.136 10.089  1.00 99.52  ? 277 ASP   A OD1 1 
ATOM   1938 O  OD2 . ASP   A 1 256 ? -6.837  -32.939 9.020   1.00 102.61 ? 277 ASP   A OD2 1 
ATOM   1939 N  N   . SER   A 1 257 ? -7.753  -27.318 8.796   1.00 96.15  ? 278 SER   A N   1 
ATOM   1940 C  CA  . SER   A 1 257 ? -7.251  -25.955 8.668   1.00 95.08  ? 278 SER   A CA  1 
ATOM   1941 C  C   . SER   A 1 257 ? -7.494  -25.166 9.947   1.00 96.16  ? 278 SER   A C   1 
ATOM   1942 O  O   . SER   A 1 257 ? -6.660  -24.346 10.350  1.00 95.94  ? 278 SER   A O   1 
ATOM   1943 C  CB  . SER   A 1 257 ? -7.902  -25.259 7.475   1.00 94.07  ? 278 SER   A CB  1 
ATOM   1944 O  OG  . SER   A 1 257 ? -9.300  -25.121 7.662   1.00 93.08  ? 278 SER   A OG  1 
ATOM   1945 N  N   . GLN   A 1 258 ? -8.638  -25.395 10.596  1.00 96.37  ? 279 GLN   A N   1 
ATOM   1946 C  CA  . GLN   A 1 258 ? -8.916  -24.750 11.874  1.00 97.21  ? 279 GLN   A CA  1 
ATOM   1947 C  C   . GLN   A 1 258 ? -7.957  -25.202 12.968  1.00 101.32 ? 279 GLN   A C   1 
ATOM   1948 O  O   . GLN   A 1 258 ? -7.817  -24.505 13.979  1.00 102.58 ? 279 GLN   A O   1 
ATOM   1949 C  CB  . GLN   A 1 258 ? -10.359 -25.033 12.302  1.00 93.98  ? 279 GLN   A CB  1 
ATOM   1950 C  CG  . GLN   A 1 258 ? -11.408 -24.648 11.268  1.00 91.30  ? 279 GLN   A CG  1 
ATOM   1951 C  CD  . GLN   A 1 258 ? -12.825 -24.908 11.747  1.00 90.99  ? 279 GLN   A CD  1 
ATOM   1952 O  OE1 . GLN   A 1 258 ? -13.335 -26.023 11.641  1.00 92.96  ? 279 GLN   A OE1 1 
ATOM   1953 N  NE2 . GLN   A 1 258 ? -13.468 -23.874 12.278  1.00 90.65  ? 279 GLN   A NE2 1 
ATOM   1954 N  N   . ASN   A 1 259 ? -7.300  -26.350 12.792  1.00 100.07 ? 280 ASN   A N   1 
ATOM   1955 C  CA  . ASN   A 1 259 ? -6.434  -26.884 13.840  1.00 97.18  ? 280 ASN   A CA  1 
ATOM   1956 C  C   . ASN   A 1 259 ? -5.203  -26.007 14.049  1.00 97.82  ? 280 ASN   A C   1 
ATOM   1957 O  O   . ASN   A 1 259 ? -4.873  -25.644 15.184  1.00 99.75  ? 280 ASN   A O   1 
ATOM   1958 C  CB  . ASN   A 1 259 ? -6.029  -28.318 13.499  1.00 97.62  ? 280 ASN   A CB  1 
ATOM   1959 C  CG  . ASN   A 1 259 ? -7.213  -29.265 13.471  1.00 100.76 ? 280 ASN   A CG  1 
ATOM   1960 O  OD1 . ASN   A 1 259 ? -8.354  -28.854 13.682  1.00 100.55 ? 280 ASN   A OD1 1 
ATOM   1961 N  ND2 . ASN   A 1 259 ? -6.948  -30.539 13.204  1.00 101.45 ? 280 ASN   A ND2 1 
ATOM   1962 N  N   . SER   A 1 260 ? -4.512  -25.654 12.969  1.00 97.22  ? 281 SER   A N   1 
ATOM   1963 C  CA  . SER   A 1 260 ? -3.311  -24.831 13.072  1.00 94.19  ? 281 SER   A CA  1 
ATOM   1964 C  C   . SER   A 1 260 ? -3.022  -24.097 11.767  1.00 91.76  ? 281 SER   A C   1 
ATOM   1965 O  O   . SER   A 1 260 ? -1.877  -23.742 11.484  1.00 88.71  ? 281 SER   A O   1 
ATOM   1966 C  CB  . SER   A 1 260 ? -2.106  -25.688 13.468  1.00 88.14  ? 281 SER   A CB  1 
ATOM   1967 N  N   . HIS   A 1 266 ? -3.073  -15.692 8.135   1.00 85.76  ? 287 HIS   A N   1 
ATOM   1968 C  CA  . HIS   A 1 266 ? -4.241  -14.822 8.199   1.00 90.07  ? 287 HIS   A CA  1 
ATOM   1969 C  C   . HIS   A 1 266 ? -4.999  -15.010 9.509   1.00 94.08  ? 287 HIS   A C   1 
ATOM   1970 O  O   . HIS   A 1 266 ? -4.537  -14.594 10.570  1.00 97.07  ? 287 HIS   A O   1 
ATOM   1971 C  CB  . HIS   A 1 266 ? -5.173  -15.080 7.013   1.00 84.72  ? 287 HIS   A CB  1 
ATOM   1972 C  CG  . HIS   A 1 266 ? -4.692  -14.482 5.727   1.00 80.56  ? 287 HIS   A CG  1 
ATOM   1973 N  ND1 . HIS   A 1 266 ? -3.861  -15.154 4.857   1.00 82.89  ? 287 HIS   A ND1 1 
ATOM   1974 C  CD2 . HIS   A 1 266 ? -4.923  -13.271 5.166   1.00 78.86  ? 287 HIS   A CD2 1 
ATOM   1975 C  CE1 . HIS   A 1 266 ? -3.603  -14.384 3.815   1.00 80.23  ? 287 HIS   A CE1 1 
ATOM   1976 N  NE2 . HIS   A 1 266 ? -4.235  -13.236 3.978   1.00 78.71  ? 287 HIS   A NE2 1 
ATOM   1977 N  N   . LYS   A 1 267 ? -6.167  -15.640 9.423   1.00 90.55  ? 288 LYS   A N   1 
ATOM   1978 C  CA  . LYS   A 1 267 ? -7.013  -15.877 10.584  1.00 89.89  ? 288 LYS   A CA  1 
ATOM   1979 C  C   . LYS   A 1 267 ? -7.617  -17.272 10.460  1.00 90.62  ? 288 LYS   A C   1 
ATOM   1980 O  O   . LYS   A 1 267 ? -7.280  -18.039 9.552   1.00 91.50  ? 288 LYS   A O   1 
ATOM   1981 C  CB  . LYS   A 1 267 ? -8.083  -14.784 10.707  1.00 88.35  ? 288 LYS   A CB  1 
ATOM   1982 N  N   . ALA   A 1 268 ? -8.521  -17.600 11.376  1.00 89.20  ? 289 ALA   A N   1 
ATOM   1983 C  CA  . ALA   A 1 268 ? -9.114  -18.926 11.453  1.00 90.34  ? 289 ALA   A CA  1 
ATOM   1984 C  C   . ALA   A 1 268 ? -10.453 -18.957 10.729  1.00 89.64  ? 289 ALA   A C   1 
ATOM   1985 O  O   . ALA   A 1 268 ? -11.214 -17.986 10.765  1.00 89.56  ? 289 ALA   A O   1 
ATOM   1986 C  CB  . ALA   A 1 268 ? -9.304  -19.353 12.910  1.00 90.81  ? 289 ALA   A CB  1 
ATOM   1987 N  N   . LEU   A 1 269 ? -10.733 -20.080 10.072  1.00 88.35  ? 290 LEU   A N   1 
ATOM   1988 C  CA  . LEU   A 1 269 ? -12.018 -20.280 9.413   1.00 86.66  ? 290 LEU   A CA  1 
ATOM   1989 C  C   . LEU   A 1 269 ? -13.110 -20.392 10.467  1.00 87.20  ? 290 LEU   A C   1 
ATOM   1990 O  O   . LEU   A 1 269 ? -13.133 -21.348 11.249  1.00 88.01  ? 290 LEU   A O   1 
ATOM   1991 C  CB  . LEU   A 1 269 ? -11.985 -21.531 8.539   1.00 89.03  ? 290 LEU   A CB  1 
ATOM   1992 C  CG  . LEU   A 1 269 ? -11.703 -21.348 7.047   1.00 86.94  ? 290 LEU   A CG  1 
ATOM   1993 C  CD1 . LEU   A 1 269 ? -11.861 -22.670 6.314   1.00 85.74  ? 290 LEU   A CD1 1 
ATOM   1994 C  CD2 . LEU   A 1 269 ? -12.620 -20.293 6.453   1.00 86.11  ? 290 LEU   A CD2 1 
ATOM   1995 N  N   . SER   A 1 270 ? -14.012 -19.415 10.495  1.00 87.30  ? 291 SER   A N   1 
ATOM   1996 C  CA  . SER   A 1 270 ? -15.162 -19.500 11.381  1.00 87.37  ? 291 SER   A CA  1 
ATOM   1997 C  C   . SER   A 1 270 ? -16.006 -20.712 11.014  1.00 85.50  ? 291 SER   A C   1 
ATOM   1998 O  O   . SER   A 1 270 ? -16.077 -21.117 9.850   1.00 84.67  ? 291 SER   A O   1 
ATOM   1999 C  CB  . SER   A 1 270 ? -16.006 -18.228 11.291  1.00 85.64  ? 291 SER   A CB  1 
ATOM   2000 O  OG  . SER   A 1 270 ? -15.218 -17.070 11.501  1.00 87.78  ? 291 SER   A OG  1 
ATOM   2001 N  N   . ASP   A 1 271 ? -16.632 -21.313 12.028  1.00 85.32  ? 292 ASP   A N   1 
ATOM   2002 C  CA  . ASP   A 1 271 ? -17.544 -22.418 11.760  1.00 87.63  ? 292 ASP   A CA  1 
ATOM   2003 C  C   . ASP   A 1 271 ? -18.643 -21.997 10.794  1.00 86.06  ? 292 ASP   A C   1 
ATOM   2004 O  O   . ASP   A 1 271 ? -19.105 -22.809 9.985   1.00 83.51  ? 292 ASP   A O   1 
ATOM   2005 C  CB  . ASP   A 1 271 ? -18.143 -22.939 13.066  1.00 91.35  ? 292 ASP   A CB  1 
ATOM   2006 C  CG  . ASP   A 1 271 ? -17.084 -23.408 14.046  1.00 93.34  ? 292 ASP   A CG  1 
ATOM   2007 O  OD1 . ASP   A 1 271 ? -15.884 -23.187 13.777  1.00 92.36  ? 292 ASP   A OD1 1 
ATOM   2008 O  OD2 . ASP   A 1 271 ? -17.451 -24.000 15.084  1.00 94.70  ? 292 ASP   A OD2 1 
ATOM   2009 N  N   . LEU   A 1 272 ? -19.065 -20.733 10.860  1.00 86.41  ? 293 LEU   A N   1 
ATOM   2010 C  CA  . LEU   A 1 272 ? -19.990 -20.209 9.860   1.00 85.12  ? 293 LEU   A CA  1 
ATOM   2011 C  C   . LEU   A 1 272 ? -19.329 -20.116 8.490   1.00 82.48  ? 293 LEU   A C   1 
ATOM   2012 O  O   . LEU   A 1 272 ? -19.949 -20.446 7.473   1.00 81.32  ? 293 LEU   A O   1 
ATOM   2013 C  CB  . LEU   A 1 272 ? -20.517 -18.844 10.298  1.00 85.71  ? 293 LEU   A CB  1 
ATOM   2014 C  CG  . LEU   A 1 272 ? -21.670 -18.291 9.463   1.00 86.25  ? 293 LEU   A CG  1 
ATOM   2015 C  CD1 . LEU   A 1 272 ? -22.804 -19.300 9.420   1.00 84.16  ? 293 LEU   A CD1 1 
ATOM   2016 C  CD2 . LEU   A 1 272 ? -22.148 -16.965 10.028  1.00 84.77  ? 293 LEU   A CD2 1 
ATOM   2017 N  N   . GLU   A 1 273 ? -18.072 -19.664 8.442   1.00 82.33  ? 294 GLU   A N   1 
ATOM   2018 C  CA  . GLU   A 1 273 ? -17.368 -19.586 7.166   1.00 80.26  ? 294 GLU   A CA  1 
ATOM   2019 C  C   . GLU   A 1 273 ? -17.186 -20.969 6.553   1.00 80.46  ? 294 GLU   A C   1 
ATOM   2020 O  O   . GLU   A 1 273 ? -17.307 -21.136 5.334   1.00 78.69  ? 294 GLU   A O   1 
ATOM   2021 C  CB  . GLU   A 1 273 ? -16.015 -18.893 7.344   1.00 80.18  ? 294 GLU   A CB  1 
ATOM   2022 C  CG  . GLU   A 1 273 ? -16.111 -17.392 7.581   1.00 83.23  ? 294 GLU   A CG  1 
ATOM   2023 C  CD  . GLU   A 1 273 ? -14.775 -16.685 7.437   1.00 85.31  ? 294 GLU   A CD  1 
ATOM   2024 O  OE1 . GLU   A 1 273 ? -13.739 -17.376 7.340   1.00 85.17  ? 294 GLU   A OE1 1 
ATOM   2025 O  OE2 . GLU   A 1 273 ? -14.759 -15.436 7.415   1.00 84.19  ? 294 GLU   A OE2 1 
ATOM   2026 N  N   . LEU   A 1 274 ? -16.900 -21.974 7.385   1.00 81.28  ? 295 LEU   A N   1 
ATOM   2027 C  CA  . LEU   A 1 274 ? -16.723 -23.332 6.879   1.00 77.76  ? 295 LEU   A CA  1 
ATOM   2028 C  C   . LEU   A 1 274 ? -17.993 -23.843 6.209   1.00 76.07  ? 295 LEU   A C   1 
ATOM   2029 O  O   . LEU   A 1 274 ? -17.934 -24.467 5.142   1.00 75.28  ? 295 LEU   A O   1 
ATOM   2030 C  CB  . LEU   A 1 274 ? -16.295 -24.259 8.020   1.00 80.72  ? 295 LEU   A CB  1 
ATOM   2031 C  CG  . LEU   A 1 274 ? -16.136 -25.757 7.753   1.00 80.32  ? 295 LEU   A CG  1 
ATOM   2032 C  CD1 . LEU   A 1 274 ? -14.984 -26.313 8.572   1.00 86.52  ? 295 LEU   A CD1 1 
ATOM   2033 C  CD2 . LEU   A 1 274 ? -17.418 -26.506 8.083   1.00 79.83  ? 295 LEU   A CD2 1 
ATOM   2034 N  N   . VAL   A 1 275 ? -19.153 -23.597 6.824   1.00 77.69  ? 296 VAL   A N   1 
ATOM   2035 C  CA  . VAL   A 1 275 ? -20.413 -24.005 6.211   1.00 74.35  ? 296 VAL   A CA  1 
ATOM   2036 C  C   . VAL   A 1 275 ? -20.661 -23.226 4.926   1.00 72.96  ? 296 VAL   A C   1 
ATOM   2037 O  O   . VAL   A 1 275 ? -21.254 -23.752 3.977   1.00 71.60  ? 296 VAL   A O   1 
ATOM   2038 C  CB  . VAL   A 1 275 ? -21.572 -23.839 7.212   1.00 75.70  ? 296 VAL   A CB  1 
ATOM   2039 C  CG1 . VAL   A 1 275 ? -22.872 -24.353 6.615   1.00 76.74  ? 296 VAL   A CG1 1 
ATOM   2040 C  CG2 . VAL   A 1 275 ? -21.259 -24.570 8.506   1.00 78.01  ? 296 VAL   A CG2 1 
ATOM   2041 N  N   . ALA   A 1 276 ? -20.219 -21.967 4.871   1.00 73.80  ? 297 ALA   A N   1 
ATOM   2042 C  CA  . ALA   A 1 276 ? -20.402 -21.166 3.664   1.00 72.32  ? 297 ALA   A CA  1 
ATOM   2043 C  C   . ALA   A 1 276 ? -19.639 -21.760 2.484   1.00 70.97  ? 297 ALA   A C   1 
ATOM   2044 O  O   . ALA   A 1 276 ? -20.173 -21.861 1.373   1.00 70.00  ? 297 ALA   A O   1 
ATOM   2045 C  CB  . ALA   A 1 276 ? -19.962 -19.725 3.919   1.00 74.78  ? 297 ALA   A CB  1 
ATOM   2046 N  N   . GLN   A 1 277 ? -18.384 -22.160 2.706   1.00 72.03  ? 298 GLN   A N   1 
ATOM   2047 C  CA  . GLN   A 1 277 ? -17.582 -22.709 1.617   1.00 69.04  ? 298 GLN   A CA  1 
ATOM   2048 C  C   . GLN   A 1 277 ? -18.070 -24.093 1.209   1.00 69.16  ? 298 GLN   A C   1 
ATOM   2049 O  O   . GLN   A 1 277 ? -18.065 -24.433 0.020   1.00 69.23  ? 298 GLN   A O   1 
ATOM   2050 C  CB  . GLN   A 1 277 ? -16.109 -22.765 2.017   1.00 69.53  ? 298 GLN   A CB  1 
ATOM   2051 C  CG  . GLN   A 1 277 ? -15.595 -21.517 2.713   1.00 73.16  ? 298 GLN   A CG  1 
ATOM   2052 C  CD  . GLN   A 1 277 ? -15.818 -20.256 1.903   1.00 72.01  ? 298 GLN   A CD  1 
ATOM   2053 O  OE1 . GLN   A 1 277 ? -15.782 -20.277 0.674   1.00 70.79  ? 298 GLN   A OE1 1 
ATOM   2054 N  NE2 . GLN   A 1 277 ? -16.054 -19.147 2.594   1.00 73.72  ? 298 GLN   A NE2 1 
ATOM   2055 N  N   . SER   A 1 278 ? -18.488 -24.909 2.180   1.00 69.24  ? 299 SER   A N   1 
ATOM   2056 C  CA  . SER   A 1 278 ? -18.949 -26.257 1.865   1.00 68.26  ? 299 SER   A CA  1 
ATOM   2057 C  C   . SER   A 1 278 ? -20.189 -26.222 0.981   1.00 69.44  ? 299 SER   A C   1 
ATOM   2058 O  O   . SER   A 1 278 ? -20.340 -27.053 0.078   1.00 73.56  ? 299 SER   A O   1 
ATOM   2059 C  CB  . SER   A 1 278 ? -19.229 -27.032 3.154   1.00 70.99  ? 299 SER   A CB  1 
ATOM   2060 O  OG  . SER   A 1 278 ? -20.298 -26.450 3.878   1.00 74.24  ? 299 SER   A OG  1 
ATOM   2061 N  N   . ILE   A 1 279 ? -21.089 -25.270 1.228   1.00 66.36  ? 300 ILE   A N   1 
ATOM   2062 C  CA  . ILE   A 1 279 ? -22.287 -25.149 0.405   1.00 67.89  ? 300 ILE   A CA  1 
ATOM   2063 C  C   . ILE   A 1 279 ? -21.931 -24.672 -0.999  1.00 64.67  ? 300 ILE   A C   1 
ATOM   2064 O  O   . ILE   A 1 279 ? -22.483 -25.160 -1.992  1.00 63.11  ? 300 ILE   A O   1 
ATOM   2065 C  CB  . ILE   A 1 279 ? -23.307 -24.217 1.084   1.00 71.61  ? 300 ILE   A CB  1 
ATOM   2066 C  CG1 . ILE   A 1 279 ? -23.797 -24.831 2.396   1.00 71.68  ? 300 ILE   A CG1 1 
ATOM   2067 C  CG2 . ILE   A 1 279 ? -24.479 -23.939 0.160   1.00 69.67  ? 300 ILE   A CG2 1 
ATOM   2068 C  CD1 . ILE   A 1 279 ? -24.724 -23.932 3.181   1.00 73.26  ? 300 ILE   A CD1 1 
ATOM   2069 N  N   . ILE   A 1 280 ? -21.003 -23.716 -1.107  1.00 62.72  ? 301 ILE   A N   1 
ATOM   2070 C  CA  . ILE   A 1 280 ? -20.681 -23.153 -2.415  1.00 63.09  ? 301 ILE   A CA  1 
ATOM   2071 C  C   . ILE   A 1 280 ? -20.010 -24.193 -3.306  1.00 61.36  ? 301 ILE   A C   1 
ATOM   2072 O  O   . ILE   A 1 280 ? -20.203 -24.186 -4.528  1.00 60.77  ? 301 ILE   A O   1 
ATOM   2073 C  CB  . ILE   A 1 280 ? -19.827 -21.877 -2.263  1.00 64.39  ? 301 ILE   A CB  1 
ATOM   2074 C  CG1 . ILE   A 1 280 ? -20.154 -20.891 -3.385  1.00 60.41  ? 301 ILE   A CG1 1 
ATOM   2075 C  CG2 . ILE   A 1 280 ? -18.335 -22.187 -2.260  1.00 64.55  ? 301 ILE   A CG2 1 
ATOM   2076 C  CD1 . ILE   A 1 280 ? -21.573 -20.370 -3.337  1.00 58.77  ? 301 ILE   A CD1 1 
ATOM   2077 N  N   . PHE   A 1 281 ? -19.219 -25.099 -2.722  1.00 60.32  ? 302 PHE   A N   1 
ATOM   2078 C  CA  . PHE   A 1 281 ? -18.616 -26.168 -3.512  1.00 61.35  ? 302 PHE   A CA  1 
ATOM   2079 C  C   . PHE   A 1 281 ? -19.684 -27.087 -4.088  1.00 61.53  ? 302 PHE   A C   1 
ATOM   2080 O  O   . PHE   A 1 281 ? -19.557 -27.568 -5.220  1.00 58.97  ? 302 PHE   A O   1 
ATOM   2081 C  CB  . PHE   A 1 281 ? -17.624 -26.962 -2.660  1.00 61.52  ? 302 PHE   A CB  1 
ATOM   2082 C  CG  . PHE   A 1 281 ? -16.481 -26.141 -2.131  1.00 61.12  ? 302 PHE   A CG  1 
ATOM   2083 C  CD1 . PHE   A 1 281 ? -16.092 -24.971 -2.764  1.00 63.35  ? 302 PHE   A CD1 1 
ATOM   2084 C  CD2 . PHE   A 1 281 ? -15.793 -26.543 -0.998  1.00 63.12  ? 302 PHE   A CD2 1 
ATOM   2085 C  CE1 . PHE   A 1 281 ? -15.042 -24.216 -2.275  1.00 63.67  ? 302 PHE   A CE1 1 
ATOM   2086 C  CE2 . PHE   A 1 281 ? -14.741 -25.794 -0.505  1.00 64.92  ? 302 PHE   A CE2 1 
ATOM   2087 C  CZ  . PHE   A 1 281 ? -14.367 -24.629 -1.143  1.00 65.35  ? 302 PHE   A CZ  1 
ATOM   2088 N  N   . ILE   A 1 282 ? -20.740 -27.353 -3.315  1.00 63.67  ? 303 ILE   A N   1 
ATOM   2089 C  CA  . ILE   A 1 282 ? -21.887 -28.085 -3.844  1.00 60.00  ? 303 ILE   A CA  1 
ATOM   2090 C  C   . ILE   A 1 282 ? -22.560 -27.280 -4.947  1.00 62.32  ? 303 ILE   A C   1 
ATOM   2091 O  O   . ILE   A 1 282 ? -22.845 -27.794 -6.035  1.00 63.82  ? 303 ILE   A O   1 
ATOM   2092 C  CB  . ILE   A 1 282 ? -22.882 -28.415 -2.718  1.00 61.43  ? 303 ILE   A CB  1 
ATOM   2093 C  CG1 . ILE   A 1 282 ? -22.177 -29.083 -1.539  1.00 64.71  ? 303 ILE   A CG1 1 
ATOM   2094 C  CG2 . ILE   A 1 282 ? -23.999 -29.303 -3.241  1.00 63.10  ? 303 ILE   A CG2 1 
ATOM   2095 C  CD1 . ILE   A 1 282 ? -23.095 -29.338 -0.368  1.00 68.80  ? 303 ILE   A CD1 1 
ATOM   2096 N  N   . PHE   A 1 283 ? -22.817 -25.997 -4.679  1.00 62.80  ? 304 PHE   A N   1 
ATOM   2097 C  CA  . PHE   A 1 283 ? -23.495 -25.151 -5.654  1.00 61.86  ? 304 PHE   A CA  1 
ATOM   2098 C  C   . PHE   A 1 283 ? -22.662 -24.973 -6.914  1.00 61.74  ? 304 PHE   A C   1 
ATOM   2099 O  O   . PHE   A 1 283 ? -23.214 -24.888 -8.017  1.00 63.82  ? 304 PHE   A O   1 
ATOM   2100 C  CB  . PHE   A 1 283 ? -23.820 -23.793 -5.032  1.00 61.66  ? 304 PHE   A CB  1 
ATOM   2101 C  CG  . PHE   A 1 283 ? -24.532 -22.861 -5.964  1.00 63.58  ? 304 PHE   A CG  1 
ATOM   2102 C  CD1 . PHE   A 1 283 ? -25.901 -22.959 -6.147  1.00 65.68  ? 304 PHE   A CD1 1 
ATOM   2103 C  CD2 . PHE   A 1 283 ? -23.834 -21.888 -6.660  1.00 63.31  ? 304 PHE   A CD2 1 
ATOM   2104 C  CE1 . PHE   A 1 283 ? -26.561 -22.104 -7.007  1.00 65.92  ? 304 PHE   A CE1 1 
ATOM   2105 C  CE2 . PHE   A 1 283 ? -24.488 -21.029 -7.522  1.00 65.25  ? 304 PHE   A CE2 1 
ATOM   2106 C  CZ  . PHE   A 1 283 ? -25.854 -21.137 -7.696  1.00 66.10  ? 304 PHE   A CZ  1 
ATOM   2107 N  N   . ALA   A 1 284 ? -21.338 -24.907 -6.773  1.00 61.31  ? 305 ALA   A N   1 
ATOM   2108 C  CA  . ALA   A 1 284 ? -20.475 -24.795 -7.939  1.00 61.07  ? 305 ALA   A CA  1 
ATOM   2109 C  C   . ALA   A 1 284 ? -20.345 -26.114 -8.688  1.00 60.71  ? 305 ALA   A C   1 
ATOM   2110 O  O   . ALA   A 1 284 ? -20.177 -26.108 -9.911  1.00 62.40  ? 305 ALA   A O   1 
ATOM   2111 C  CB  . ALA   A 1 284 ? -19.091 -24.290 -7.527  1.00 58.19  ? 305 ALA   A CB  1 
ATOM   2112 N  N   . GLY   A 1 285 ? -20.420 -27.245 -7.993  1.00 59.54  ? 306 GLY   A N   1 
ATOM   2113 C  CA  . GLY   A 1 285 ? -20.093 -28.511 -8.621  1.00 60.09  ? 306 GLY   A CA  1 
ATOM   2114 C  C   . GLY   A 1 285 ? -21.239 -29.399 -9.063  1.00 65.42  ? 306 GLY   A C   1 
ATOM   2115 O  O   . GLY   A 1 285 ? -21.009 -30.374 -9.786  1.00 65.48  ? 306 GLY   A O   1 
ATOM   2116 N  N   . TYR   A 1 286 ? -22.474 -29.088 -8.660  1.00 64.70  ? 307 TYR   A N   1 
ATOM   2117 C  CA  . TYR   A 1 286 ? -23.562 -30.039 -8.874  1.00 64.71  ? 307 TYR   A CA  1 
ATOM   2118 C  C   . TYR   A 1 286 ? -24.046 -30.046 -10.322 1.00 66.60  ? 307 TYR   A C   1 
ATOM   2119 O  O   . TYR   A 1 286 ? -23.911 -31.054 -11.024 1.00 67.35  ? 307 TYR   A O   1 
ATOM   2120 C  CB  . TYR   A 1 286 ? -24.722 -29.748 -7.920  1.00 68.27  ? 307 TYR   A CB  1 
ATOM   2121 C  CG  . TYR   A 1 286 ? -25.903 -30.656 -8.159  1.00 71.17  ? 307 TYR   A CG  1 
ATOM   2122 C  CD1 . TYR   A 1 286 ? -25.784 -32.030 -8.005  1.00 71.18  ? 307 TYR   A CD1 1 
ATOM   2123 C  CD2 . TYR   A 1 286 ? -27.131 -30.144 -8.555  1.00 69.68  ? 307 TYR   A CD2 1 
ATOM   2124 C  CE1 . TYR   A 1 286 ? -26.856 -32.870 -8.232  1.00 70.40  ? 307 TYR   A CE1 1 
ATOM   2125 C  CE2 . TYR   A 1 286 ? -28.211 -30.976 -8.782  1.00 71.32  ? 307 TYR   A CE2 1 
ATOM   2126 C  CZ  . TYR   A 1 286 ? -28.067 -32.338 -8.619  1.00 70.96  ? 307 TYR   A CZ  1 
ATOM   2127 O  OH  . TYR   A 1 286 ? -29.138 -33.170 -8.844  1.00 75.45  ? 307 TYR   A OH  1 
ATOM   2128 N  N   . GLU   A 1 287 ? -24.611 -28.932 -10.791 1.00 66.95  ? 308 GLU   A N   1 
ATOM   2129 C  CA  . GLU   A 1 287 ? -25.164 -28.883 -12.139 1.00 67.90  ? 308 GLU   A CA  1 
ATOM   2130 C  C   . GLU   A 1 287 ? -24.123 -28.526 -13.186 1.00 67.43  ? 308 GLU   A C   1 
ATOM   2131 O  O   . GLU   A 1 287 ? -24.345 -28.789 -14.376 1.00 69.58  ? 308 GLU   A O   1 
ATOM   2132 C  CB  . GLU   A 1 287 ? -26.332 -27.887 -12.200 1.00 72.66  ? 308 GLU   A CB  1 
ATOM   2133 C  CG  . GLU   A 1 287 ? -27.646 -28.439 -11.690 1.00 73.42  ? 308 GLU   A CG  1 
ATOM   2134 C  CD  . GLU   A 1 287 ? -28.831 -27.756 -12.329 1.00 79.73  ? 308 GLU   A CD  1 
ATOM   2135 O  OE1 . GLU   A 1 287 ? -28.630 -26.717 -12.994 1.00 80.79  ? 308 GLU   A OE1 1 
ATOM   2136 O  OE2 . GLU   A 1 287 ? -29.961 -28.266 -12.177 1.00 79.34  ? 308 GLU   A OE2 1 
ATOM   2137 N  N   . THR   A 1 288 ? -22.990 -28.001 -12.750 1.00 65.16  ? 309 THR   A N   1 
ATOM   2138 C  CA  . THR   A 1 288 ? -21.927 -27.694 -13.713 1.00 65.93  ? 309 THR   A CA  1 
ATOM   2139 C  C   . THR   A 1 288 ? -21.476 -28.982 -14.350 1.00 65.21  ? 309 THR   A C   1 
ATOM   2140 O  O   . THR   A 1 288 ? -21.635 -29.124 -15.573 1.00 65.84  ? 309 THR   A O   1 
ATOM   2141 C  CB  . THR   A 1 288 ? -20.807 -26.973 -12.974 1.00 63.68  ? 309 THR   A CB  1 
ATOM   2142 O  OG1 . THR   A 1 288 ? -20.688 -27.667 -11.739 1.00 63.05  ? 309 THR   A OG1 1 
ATOM   2143 C  CG2 . THR   A 1 288 ? -21.133 -25.509 -12.748 1.00 62.96  ? 309 THR   A CG2 1 
ATOM   2144 N  N   . THR   A 1 289 ? -20.948 -29.899 -13.548 1.00 64.08  ? 310 THR   A N   1 
ATOM   2145 C  CA  . THR   A 1 289 ? -20.455 -31.181 -14.069 1.00 62.57  ? 310 THR   A CA  1 
ATOM   2146 C  C   . THR   A 1 289 ? -21.538 -31.815 -14.890 1.00 63.84  ? 310 THR   A C   1 
ATOM   2147 O  O   . THR   A 1 289 ? -21.251 -32.235 -16.017 1.00 65.27  ? 310 THR   A O   1 
ATOM   2148 C  CB  . THR   A 1 289 ? -20.058 -32.052 -12.886 1.00 63.65  ? 310 THR   A CB  1 
ATOM   2149 O  OG1 . THR   A 1 289 ? -21.153 -31.947 -11.985 1.00 69.91  ? 310 THR   A OG1 1 
ATOM   2150 C  CG2 . THR   A 1 289 ? -18.794 -31.564 -12.204 1.00 61.33  ? 310 THR   A CG2 1 
ATOM   2151 N  N   . SER   A 1 290 ? -22.754 -31.864 -14.357 1.00 65.04  ? 311 SER   A N   1 
ATOM   2152 C  CA  . SER   A 1 290 ? -23.842 -32.538 -15.057 1.00 64.04  ? 311 SER   A CA  1 
ATOM   2153 C  C   . SER   A 1 290 ? -24.099 -31.906 -16.417 1.00 64.18  ? 311 SER   A C   1 
ATOM   2154 O  O   . SER   A 1 290 ? -24.252 -32.611 -17.417 1.00 65.79  ? 311 SER   A O   1 
ATOM   2155 C  CB  . SER   A 1 290 ? -25.107 -32.510 -14.199 1.00 65.33  ? 311 SER   A CB  1 
ATOM   2156 O  OG  . SER   A 1 290 ? -24.803 -32.825 -12.857 1.00 68.67  ? 311 SER   A OG  1 
ATOM   2157 N  N   . SER   A 1 291 ? -24.138 -30.572 -16.473 1.00 64.36  ? 312 SER   A N   1 
ATOM   2158 C  CA  . SER   A 1 291 ? -24.362 -29.885 -17.739 1.00 64.61  ? 312 SER   A CA  1 
ATOM   2159 C  C   . SER   A 1 291 ? -23.231 -30.167 -18.720 1.00 65.57  ? 312 SER   A C   1 
ATOM   2160 O  O   . SER   A 1 291 ? -23.474 -30.498 -19.886 1.00 66.96  ? 312 SER   A O   1 
ATOM   2161 C  CB  . SER   A 1 291 ? -24.511 -28.384 -17.502 1.00 65.98  ? 312 SER   A CB  1 
ATOM   2162 O  OG  . SER   A 1 291 ? -25.677 -28.093 -16.749 1.00 69.21  ? 312 SER   A OG  1 
ATOM   2163 N  N   . VAL   A 1 292 ? -21.983 -30.053 -18.260 1.00 65.29  ? 313 VAL   A N   1 
ATOM   2164 C  CA  . VAL   A 1 292 ? -20.840 -30.247 -19.152 1.00 64.70  ? 313 VAL   A CA  1 
ATOM   2165 C  C   . VAL   A 1 292 ? -20.783 -31.689 -19.641 1.00 66.51  ? 313 VAL   A C   1 
ATOM   2166 O  O   . VAL   A 1 292 ? -20.607 -31.950 -20.837 1.00 68.73  ? 313 VAL   A O   1 
ATOM   2167 C  CB  . VAL   A 1 292 ? -19.532 -29.838 -18.452 1.00 61.47  ? 313 VAL   A CB  1 
ATOM   2168 C  CG1 . VAL   A 1 292 ? -18.341 -30.129 -19.356 1.00 62.72  ? 313 VAL   A CG1 1 
ATOM   2169 C  CG2 . VAL   A 1 292 ? -19.569 -28.366 -18.078 1.00 61.03  ? 313 VAL   A CG2 1 
ATOM   2170 N  N   . LEU   A 1 293 ? -20.931 -32.648 -18.721 1.00 64.54  ? 314 LEU   A N   1 
ATOM   2171 C  CA  . LEU   A 1 293 ? -20.907 -34.056 -19.108 1.00 64.58  ? 314 LEU   A CA  1 
ATOM   2172 C  C   . LEU   A 1 293 ? -22.021 -34.370 -20.098 1.00 66.96  ? 314 LEU   A C   1 
ATOM   2173 O  O   . LEU   A 1 293 ? -21.817 -35.127 -21.055 1.00 68.35  ? 314 LEU   A O   1 
ATOM   2174 C  CB  . LEU   A 1 293 ? -21.017 -34.946 -17.869 1.00 63.16  ? 314 LEU   A CB  1 
ATOM   2175 C  CG  . LEU   A 1 293 ? -19.751 -35.082 -17.021 1.00 62.85  ? 314 LEU   A CG  1 
ATOM   2176 C  CD1 . LEU   A 1 293 ? -20.001 -35.951 -15.797 1.00 62.63  ? 314 LEU   A CD1 1 
ATOM   2177 C  CD2 . LEU   A 1 293 ? -18.618 -35.651 -17.860 1.00 64.20  ? 314 LEU   A CD2 1 
ATOM   2178 N  N   . SER   A 1 294 ? -23.207 -33.798 -19.881 1.00 65.77  ? 315 SER   A N   1 
ATOM   2179 C  CA  . SER   A 1 294 ? -24.291 -33.954 -20.844 1.00 67.63  ? 315 SER   A CA  1 
ATOM   2180 C  C   . SER   A 1 294 ? -23.914 -33.365 -22.196 1.00 68.34  ? 315 SER   A C   1 
ATOM   2181 O  O   . SER   A 1 294 ? -24.186 -33.967 -23.241 1.00 72.76  ? 315 SER   A O   1 
ATOM   2182 C  CB  . SER   A 1 294 ? -25.566 -33.299 -20.310 1.00 70.05  ? 315 SER   A CB  1 
ATOM   2183 O  OG  . SER   A 1 294 ? -25.972 -33.892 -19.088 1.00 70.24  ? 315 SER   A OG  1 
ATOM   2184 N  N   . PHE   A 1 295 ? -23.285 -32.187 -22.197 1.00 65.08  ? 316 PHE   A N   1 
ATOM   2185 C  CA  . PHE   A 1 295 ? -22.846 -31.583 -23.452 1.00 66.17  ? 316 PHE   A CA  1 
ATOM   2186 C  C   . PHE   A 1 295 ? -21.785 -32.435 -24.138 1.00 68.24  ? 316 PHE   A C   1 
ATOM   2187 O  O   . PHE   A 1 295 ? -21.792 -32.576 -25.366 1.00 69.75  ? 316 PHE   A O   1 
ATOM   2188 C  CB  . PHE   A 1 295 ? -22.317 -30.169 -23.205 1.00 67.47  ? 316 PHE   A CB  1 
ATOM   2189 C  CG  . PHE   A 1 295 ? -23.390 -29.117 -23.142 1.00 66.70  ? 316 PHE   A CG  1 
ATOM   2190 C  CD1 . PHE   A 1 295 ? -24.215 -28.883 -24.230 1.00 66.36  ? 316 PHE   A CD1 1 
ATOM   2191 C  CD2 . PHE   A 1 295 ? -23.561 -28.347 -22.004 1.00 67.08  ? 316 PHE   A CD2 1 
ATOM   2192 C  CE1 . PHE   A 1 295 ? -25.197 -27.914 -24.177 1.00 67.36  ? 316 PHE   A CE1 1 
ATOM   2193 C  CE2 . PHE   A 1 295 ? -24.542 -27.376 -21.945 1.00 65.78  ? 316 PHE   A CE2 1 
ATOM   2194 C  CZ  . PHE   A 1 295 ? -25.360 -27.159 -23.033 1.00 66.54  ? 316 PHE   A CZ  1 
ATOM   2195 N  N   . ILE   A 1 296 ? -20.857 -33.004 -23.363 1.00 67.97  ? 317 ILE   A N   1 
ATOM   2196 C  CA  . ILE   A 1 296 ? -19.786 -33.806 -23.953 1.00 66.85  ? 317 ILE   A CA  1 
ATOM   2197 C  C   . ILE   A 1 296 ? -20.360 -35.040 -24.637 1.00 69.24  ? 317 ILE   A C   1 
ATOM   2198 O  O   . ILE   A 1 296 ? -19.994 -35.368 -25.772 1.00 72.28  ? 317 ILE   A O   1 
ATOM   2199 C  CB  . ILE   A 1 296 ? -18.744 -34.187 -22.886 1.00 66.85  ? 317 ILE   A CB  1 
ATOM   2200 C  CG1 . ILE   A 1 296 ? -18.017 -32.941 -22.383 1.00 68.30  ? 317 ILE   A CG1 1 
ATOM   2201 C  CG2 . ILE   A 1 296 ? -17.749 -35.188 -23.450 1.00 68.26  ? 317 ILE   A CG2 1 
ATOM   2202 C  CD1 . ILE   A 1 296 ? -16.934 -33.229 -21.373 1.00 70.09  ? 317 ILE   A CD1 1 
ATOM   2203 N  N   . MET   A 1 297 ? -21.272 -35.740 -23.958 1.00 68.96  ? 318 MET   A N   1 
ATOM   2204 C  CA  . MET   A 1 297 ? -21.866 -36.932 -24.553 1.00 72.23  ? 318 MET   A CA  1 
ATOM   2205 C  C   . MET   A 1 297 ? -22.696 -36.593 -25.782 1.00 74.14  ? 318 MET   A C   1 
ATOM   2206 O  O   . MET   A 1 297 ? -22.865 -37.440 -26.667 1.00 75.53  ? 318 MET   A O   1 
ATOM   2207 C  CB  . MET   A 1 297 ? -22.717 -37.678 -23.524 1.00 70.94  ? 318 MET   A CB  1 
ATOM   2208 C  CG  . MET   A 1 297 ? -21.902 -38.421 -22.479 1.00 70.13  ? 318 MET   A CG  1 
ATOM   2209 S  SD  . MET   A 1 297 ? -20.378 -39.128 -23.141 1.00 81.91  ? 318 MET   A SD  1 
ATOM   2210 C  CE  . MET   A 1 297 ? -21.008 -40.348 -24.292 1.00 73.39  ? 318 MET   A CE  1 
ATOM   2211 N  N   . TYR   A 1 298 ? -23.221 -35.369 -25.859 1.00 72.64  ? 319 TYR   A N   1 
ATOM   2212 C  CA  . TYR   A 1 298 ? -23.942 -34.959 -27.058 1.00 73.90  ? 319 TYR   A CA  1 
ATOM   2213 C  C   . TYR   A 1 298 ? -23.006 -34.874 -28.257 1.00 75.99  ? 319 TYR   A C   1 
ATOM   2214 O  O   . TYR   A 1 298 ? -23.316 -35.391 -29.338 1.00 77.32  ? 319 TYR   A O   1 
ATOM   2215 C  CB  . TYR   A 1 298 ? -24.639 -33.617 -26.828 1.00 73.10  ? 319 TYR   A CB  1 
ATOM   2216 C  CG  . TYR   A 1 298 ? -25.390 -33.142 -28.047 1.00 76.26  ? 319 TYR   A CG  1 
ATOM   2217 C  CD1 . TYR   A 1 298 ? -26.668 -33.610 -28.322 1.00 77.32  ? 319 TYR   A CD1 1 
ATOM   2218 C  CD2 . TYR   A 1 298 ? -24.815 -32.241 -28.936 1.00 75.85  ? 319 TYR   A CD2 1 
ATOM   2219 C  CE1 . TYR   A 1 298 ? -27.357 -33.188 -29.440 1.00 78.61  ? 319 TYR   A CE1 1 
ATOM   2220 C  CE2 . TYR   A 1 298 ? -25.496 -31.814 -30.057 1.00 75.61  ? 319 TYR   A CE2 1 
ATOM   2221 C  CZ  . TYR   A 1 298 ? -26.765 -32.292 -30.304 1.00 78.41  ? 319 TYR   A CZ  1 
ATOM   2222 O  OH  . TYR   A 1 298 ? -27.449 -31.868 -31.420 1.00 83.00  ? 319 TYR   A OH  1 
ATOM   2223 N  N   . GLU   A 1 299 ? -21.852 -34.225 -28.085 1.00 73.95  ? 320 GLU   A N   1 
ATOM   2224 C  CA  . GLU   A 1 299 ? -20.910 -34.094 -29.191 1.00 75.06  ? 320 GLU   A CA  1 
ATOM   2225 C  C   . GLU   A 1 299 ? -20.340 -35.447 -29.595 1.00 79.18  ? 320 GLU   A C   1 
ATOM   2226 O  O   . GLU   A 1 299 ? -20.103 -35.696 -30.783 1.00 82.02  ? 320 GLU   A O   1 
ATOM   2227 C  CB  . GLU   A 1 299 ? -19.789 -33.124 -28.812 1.00 75.13  ? 320 GLU   A CB  1 
ATOM   2228 C  CG  . GLU   A 1 299 ? -20.267 -31.728 -28.431 1.00 78.04  ? 320 GLU   A CG  1 
ATOM   2229 C  CD  . GLU   A 1 299 ? -20.875 -30.971 -29.598 1.00 81.09  ? 320 GLU   A CD  1 
ATOM   2230 O  OE1 . GLU   A 1 299 ? -20.548 -31.294 -30.758 1.00 83.01  ? 320 GLU   A OE1 1 
ATOM   2231 O  OE2 . GLU   A 1 299 ? -21.685 -30.052 -29.354 1.00 79.04  ? 320 GLU   A OE2 1 
ATOM   2232 N  N   . LEU   A 1 300 ? -20.104 -36.330 -28.620 1.00 76.39  ? 321 LEU   A N   1 
ATOM   2233 C  CA  . LEU   A 1 300 ? -19.592 -37.660 -28.934 1.00 74.01  ? 321 LEU   A CA  1 
ATOM   2234 C  C   . LEU   A 1 300 ? -20.592 -38.461 -29.759 1.00 80.43  ? 321 LEU   A C   1 
ATOM   2235 O  O   . LEU   A 1 300 ? -20.210 -39.151 -30.712 1.00 84.21  ? 321 LEU   A O   1 
ATOM   2236 C  CB  . LEU   A 1 300 ? -19.240 -38.408 -27.647 1.00 72.40  ? 321 LEU   A CB  1 
ATOM   2237 C  CG  . LEU   A 1 300 ? -18.090 -37.842 -26.814 1.00 72.83  ? 321 LEU   A CG  1 
ATOM   2238 C  CD1 . LEU   A 1 300 ? -17.709 -38.795 -25.687 1.00 71.90  ? 321 LEU   A CD1 1 
ATOM   2239 C  CD2 . LEU   A 1 300 ? -16.892 -37.543 -27.697 1.00 74.81  ? 321 LEU   A CD2 1 
ATOM   2240 N  N   . ALA   A 1 301 ? -21.877 -38.386 -29.406 1.00 80.65  ? 322 ALA   A N   1 
ATOM   2241 C  CA  . ALA   A 1 301 ? -22.885 -39.168 -30.116 1.00 80.92  ? 322 ALA   A CA  1 
ATOM   2242 C  C   . ALA   A 1 301 ? -23.107 -38.644 -31.530 1.00 81.98  ? 322 ALA   A C   1 
ATOM   2243 O  O   . ALA   A 1 301 ? -23.242 -39.431 -32.474 1.00 83.61  ? 322 ALA   A O   1 
ATOM   2244 C  CB  . ALA   A 1 301 ? -24.197 -39.168 -29.331 1.00 80.69  ? 322 ALA   A CB  1 
ATOM   2245 N  N   . THR   A 1 302 ? -23.149 -37.322 -31.697 1.00 82.77  ? 323 THR   A N   1 
ATOM   2246 C  CA  . THR   A 1 302 ? -23.365 -36.731 -33.012 1.00 82.61  ? 323 THR   A CA  1 
ATOM   2247 C  C   . THR   A 1 302 ? -22.124 -36.775 -33.894 1.00 83.70  ? 323 THR   A C   1 
ATOM   2248 O  O   . THR   A 1 302 ? -22.233 -36.530 -35.100 1.00 86.90  ? 323 THR   A O   1 
ATOM   2249 C  CB  . THR   A 1 302 ? -23.844 -35.283 -32.872 1.00 79.88  ? 323 THR   A CB  1 
ATOM   2250 O  OG1 . THR   A 1 302 ? -22.900 -34.536 -32.093 1.00 79.98  ? 323 THR   A OG1 1 
ATOM   2251 C  CG2 . THR   A 1 302 ? -25.206 -35.238 -32.195 1.00 78.18  ? 323 THR   A CG2 1 
ATOM   2252 N  N   . HIS   A 1 303 ? -20.958 -37.076 -33.326 1.00 79.71  ? 324 HIS   A N   1 
ATOM   2253 C  CA  . HIS   A 1 303 ? -19.722 -37.268 -34.084 1.00 79.92  ? 324 HIS   A CA  1 
ATOM   2254 C  C   . HIS   A 1 303 ? -19.123 -38.600 -33.654 1.00 82.10  ? 324 HIS   A C   1 
ATOM   2255 O  O   . HIS   A 1 303 ? -18.162 -38.639 -32.875 1.00 82.19  ? 324 HIS   A O   1 
ATOM   2256 C  CB  . HIS   A 1 303 ? -18.738 -36.118 -33.858 1.00 80.88  ? 324 HIS   A CB  1 
ATOM   2257 C  CG  . HIS   A 1 303 ? -19.282 -34.771 -34.223 1.00 81.52  ? 324 HIS   A CG  1 
ATOM   2258 N  ND1 . HIS   A 1 303 ? -20.257 -34.137 -33.483 1.00 80.35  ? 324 HIS   A ND1 1 
ATOM   2259 C  CD2 . HIS   A 1 303 ? -18.984 -33.936 -35.246 1.00 83.25  ? 324 HIS   A CD2 1 
ATOM   2260 C  CE1 . HIS   A 1 303 ? -20.538 -32.970 -34.036 1.00 83.14  ? 324 HIS   A CE1 1 
ATOM   2261 N  NE2 . HIS   A 1 303 ? -19.780 -32.824 -35.107 1.00 82.08  ? 324 HIS   A NE2 1 
ATOM   2262 N  N   . PRO   A 1 304 ? -19.671 -39.717 -34.142 1.00 84.21  ? 325 PRO   A N   1 
ATOM   2263 C  CA  . PRO   A 1 304 ? -19.185 -41.031 -33.688 1.00 80.97  ? 325 PRO   A CA  1 
ATOM   2264 C  C   . PRO   A 1 304 ? -17.730 -41.293 -34.024 1.00 80.70  ? 325 PRO   A C   1 
ATOM   2265 O  O   . PRO   A 1 304 ? -17.116 -42.170 -33.403 1.00 82.99  ? 325 PRO   A O   1 
ATOM   2266 C  CB  . PRO   A 1 304 ? -20.110 -42.020 -34.414 1.00 79.81  ? 325 PRO   A CB  1 
ATOM   2267 C  CG  . PRO   A 1 304 ? -21.308 -41.215 -34.809 1.00 82.12  ? 325 PRO   A CG  1 
ATOM   2268 C  CD  . PRO   A 1 304 ? -20.788 -39.841 -35.092 1.00 82.47  ? 325 PRO   A CD  1 
ATOM   2269 N  N   . ASP   A 1 305 ? -17.160 -40.566 -34.987 1.00 80.84  ? 326 ASP   A N   1 
ATOM   2270 C  CA  . ASP   A 1 305 ? -15.750 -40.748 -35.314 1.00 82.18  ? 326 ASP   A CA  1 
ATOM   2271 C  C   . ASP   A 1 305 ? -14.861 -40.436 -34.117 1.00 83.38  ? 326 ASP   A C   1 
ATOM   2272 O  O   . ASP   A 1 305 ? -13.886 -41.150 -33.856 1.00 82.20  ? 326 ASP   A O   1 
ATOM   2273 C  CB  . ASP   A 1 305 ? -15.376 -39.878 -36.514 1.00 82.50  ? 326 ASP   A CB  1 
ATOM   2274 C  CG  . ASP   A 1 305 ? -15.951 -38.477 -36.422 1.00 85.18  ? 326 ASP   A CG  1 
ATOM   2275 O  OD1 . ASP   A 1 305 ? -16.523 -38.132 -35.366 1.00 87.19  ? 326 ASP   A OD1 1 
ATOM   2276 O  OD2 . ASP   A 1 305 ? -15.838 -37.722 -37.410 1.00 88.44  ? 326 ASP   A OD2 1 
ATOM   2277 N  N   . VAL   A 1 306 ? -15.186 -39.378 -33.373 1.00 82.55  ? 327 VAL   A N   1 
ATOM   2278 C  CA  . VAL   A 1 306 ? -14.375 -39.029 -32.211 1.00 80.56  ? 327 VAL   A CA  1 
ATOM   2279 C  C   . VAL   A 1 306 ? -14.710 -39.919 -31.016 1.00 77.80  ? 327 VAL   A C   1 
ATOM   2280 O  O   . VAL   A 1 306 ? -13.850 -40.155 -30.159 1.00 76.21  ? 327 VAL   A O   1 
ATOM   2281 C  CB  . VAL   A 1 306 ? -14.536 -37.535 -31.872 1.00 80.91  ? 327 VAL   A CB  1 
ATOM   2282 C  CG1 . VAL   A 1 306 ? -14.365 -36.687 -33.125 1.00 81.90  ? 327 VAL   A CG1 1 
ATOM   2283 C  CG2 . VAL   A 1 306 ? -15.875 -37.258 -31.213 1.00 82.75  ? 327 VAL   A CG2 1 
ATOM   2284 N  N   . GLN   A 1 307 ? -15.945 -40.423 -30.929 1.00 77.83  ? 328 GLN   A N   1 
ATOM   2285 C  CA  . GLN   A 1 307 ? -16.290 -41.325 -29.835 1.00 79.32  ? 328 GLN   A CA  1 
ATOM   2286 C  C   . GLN   A 1 307 ? -15.501 -42.625 -29.931 1.00 80.22  ? 328 GLN   A C   1 
ATOM   2287 O  O   . GLN   A 1 307 ? -15.044 -43.159 -28.914 1.00 78.77  ? 328 GLN   A O   1 
ATOM   2288 C  CB  . GLN   A 1 307 ? -17.794 -41.606 -29.826 1.00 77.19  ? 328 GLN   A CB  1 
ATOM   2289 C  CG  . GLN   A 1 307 ? -18.253 -42.449 -28.640 1.00 77.06  ? 328 GLN   A CG  1 
ATOM   2290 C  CD  . GLN   A 1 307 ? -19.749 -42.712 -28.645 1.00 80.76  ? 328 GLN   A CD  1 
ATOM   2291 O  OE1 . GLN   A 1 307 ? -20.243 -43.563 -27.904 1.00 78.23  ? 328 GLN   A OE1 1 
ATOM   2292 N  NE2 . GLN   A 1 307 ? -20.476 -41.981 -29.480 1.00 80.47  ? 328 GLN   A NE2 1 
ATOM   2293 N  N   . GLN   A 1 308 ? -15.336 -43.150 -31.147 1.00 81.13  ? 329 GLN   A N   1 
ATOM   2294 C  CA  . GLN   A 1 308 ? -14.541 -44.360 -31.331 1.00 80.88  ? 329 GLN   A CA  1 
ATOM   2295 C  C   . GLN   A 1 308 ? -13.070 -44.106 -31.028 1.00 81.14  ? 329 GLN   A C   1 
ATOM   2296 O  O   . GLN   A 1 308 ? -12.429 -44.891 -30.319 1.00 79.83  ? 329 GLN   A O   1 
ATOM   2297 C  CB  . GLN   A 1 308 ? -14.711 -44.892 -32.754 1.00 82.47  ? 329 GLN   A CB  1 
ATOM   2298 C  CG  . GLN   A 1 308 ? -13.743 -46.012 -33.103 1.00 81.40  ? 329 GLN   A CG  1 
ATOM   2299 C  CD  . GLN   A 1 308 ? -13.957 -46.557 -34.500 1.00 83.16  ? 329 GLN   A CD  1 
ATOM   2300 O  OE1 . GLN   A 1 308 ? -14.955 -46.253 -35.152 1.00 84.50  ? 329 GLN   A OE1 1 
ATOM   2301 N  NE2 . GLN   A 1 308 ? -13.014 -47.368 -34.968 1.00 81.95  ? 329 GLN   A NE2 1 
ATOM   2302 N  N   . LYS   A 1 309 ? -12.516 -43.010 -31.556 1.00 78.87  ? 330 LYS   A N   1 
ATOM   2303 C  CA  . LYS   A 1 309 ? -11.109 -42.706 -31.310 1.00 76.85  ? 330 LYS   A CA  1 
ATOM   2304 C  C   . LYS   A 1 309 ? -10.848 -42.509 -29.823 1.00 78.81  ? 330 LYS   A C   1 
ATOM   2305 O  O   . LYS   A 1 309 ? -9.814  -42.943 -29.302 1.00 79.95  ? 330 LYS   A O   1 
ATOM   2306 C  CB  . LYS   A 1 309 ? -10.683 -41.469 -32.103 1.00 75.60  ? 330 LYS   A CB  1 
ATOM   2307 C  CG  . LYS   A 1 309 ? -9.206  -41.125 -31.955 1.00 73.68  ? 330 LYS   A CG  1 
ATOM   2308 C  CD  . LYS   A 1 309 ? -8.803  -39.936 -32.815 1.00 74.25  ? 330 LYS   A CD  1 
ATOM   2309 C  CE  . LYS   A 1 309 ? -7.368  -39.514 -32.523 1.00 75.27  ? 330 LYS   A CE  1 
ATOM   2310 N  NZ  . LYS   A 1 309 ? -6.978  -38.274 -33.253 1.00 73.67  ? 330 LYS   A NZ  1 
ATOM   2311 N  N   . LEU   A 1 310 ? -11.778 -41.856 -29.122 1.00 79.89  ? 331 LEU   A N   1 
ATOM   2312 C  CA  . LEU   A 1 310 ? -11.668 -41.747 -27.671 1.00 80.19  ? 331 LEU   A CA  1 
ATOM   2313 C  C   . LEU   A 1 310 ? -11.771 -43.115 -27.008 1.00 79.64  ? 331 LEU   A C   1 
ATOM   2314 O  O   . LEU   A 1 310 ? -11.032 -43.412 -26.063 1.00 78.78  ? 331 LEU   A O   1 
ATOM   2315 C  CB  . LEU   A 1 310 ? -12.744 -40.801 -27.137 1.00 78.18  ? 331 LEU   A CB  1 
ATOM   2316 C  CG  . LEU   A 1 310 ? -12.682 -40.459 -25.649 1.00 76.56  ? 331 LEU   A CG  1 
ATOM   2317 C  CD1 . LEU   A 1 310 ? -11.257 -40.129 -25.249 1.00 75.40  ? 331 LEU   A CD1 1 
ATOM   2318 C  CD2 . LEU   A 1 310 ? -13.606 -39.294 -25.338 1.00 72.70  ? 331 LEU   A CD2 1 
ATOM   2319 N  N   . GLN   A 1 311 ? -12.682 -43.964 -27.492 1.00 79.15  ? 332 GLN   A N   1 
ATOM   2320 C  CA  . GLN   A 1 311 ? -12.807 -45.307 -26.934 1.00 80.52  ? 332 GLN   A CA  1 
ATOM   2321 C  C   . GLN   A 1 311 ? -11.581 -46.159 -27.235 1.00 82.30  ? 332 GLN   A C   1 
ATOM   2322 O  O   . GLN   A 1 311 ? -11.231 -47.041 -26.443 1.00 81.48  ? 332 GLN   A O   1 
ATOM   2323 C  CB  . GLN   A 1 311 ? -14.076 -45.980 -27.460 1.00 77.14  ? 332 GLN   A CB  1 
ATOM   2324 C  CG  . GLN   A 1 311 ? -15.340 -45.569 -26.716 1.00 75.01  ? 332 GLN   A CG  1 
ATOM   2325 C  CD  . GLN   A 1 311 ? -16.607 -46.013 -27.420 1.00 77.46  ? 332 GLN   A CD  1 
ATOM   2326 O  OE1 . GLN   A 1 311 ? -16.667 -46.051 -28.650 1.00 77.93  ? 332 GLN   A OE1 1 
ATOM   2327 N  NE2 . GLN   A 1 311 ? -17.630 -46.351 -26.643 1.00 76.62  ? 332 GLN   A NE2 1 
ATOM   2328 N  N   . GLU   A 1 312 ? -10.922 -45.921 -28.372 1.00 82.52  ? 333 GLU   A N   1 
ATOM   2329 C  CA  . GLU   A 1 312 ? -9.661  -46.602 -28.648 1.00 81.37  ? 333 GLU   A CA  1 
ATOM   2330 C  C   . GLU   A 1 312 ? -8.567  -46.144 -27.692 1.00 81.72  ? 333 GLU   A C   1 
ATOM   2331 O  O   . GLU   A 1 312 ? -7.812  -46.969 -27.162 1.00 83.82  ? 333 GLU   A O   1 
ATOM   2332 C  CB  . GLU   A 1 312 ? -9.238  -46.360 -30.097 1.00 81.54  ? 333 GLU   A CB  1 
ATOM   2333 C  CG  . GLU   A 1 312 ? -10.147 -46.994 -31.134 1.00 82.47  ? 333 GLU   A CG  1 
ATOM   2334 C  CD  . GLU   A 1 312 ? -9.857  -46.499 -32.539 1.00 86.00  ? 333 GLU   A CD  1 
ATOM   2335 O  OE1 . GLU   A 1 312 ? -8.969  -45.635 -32.692 1.00 82.39  ? 333 GLU   A OE1 1 
ATOM   2336 O  OE2 . GLU   A 1 312 ? -10.519 -46.972 -33.488 1.00 86.54  ? 333 GLU   A OE2 1 
ATOM   2337 N  N   . GLU   A 1 313 ? -8.465  -44.832 -27.462 1.00 79.21  ? 334 GLU   A N   1 
ATOM   2338 C  CA  . GLU   A 1 313 ? -7.440  -44.310 -26.564 1.00 79.90  ? 334 GLU   A CA  1 
ATOM   2339 C  C   . GLU   A 1 313 ? -7.665  -44.774 -25.130 1.00 81.10  ? 334 GLU   A C   1 
ATOM   2340 O  O   . GLU   A 1 313 ? -6.709  -45.132 -24.431 1.00 79.47  ? 334 GLU   A O   1 
ATOM   2341 C  CB  . GLU   A 1 313 ? -7.414  -42.784 -26.629 1.00 81.58  ? 334 GLU   A CB  1 
ATOM   2342 C  CG  . GLU   A 1 313 ? -6.308  -42.150 -25.803 1.00 82.08  ? 334 GLU   A CG  1 
ATOM   2343 C  CD  . GLU   A 1 313 ? -6.534  -40.672 -25.563 1.00 81.56  ? 334 GLU   A CD  1 
ATOM   2344 O  OE1 . GLU   A 1 313 ? -7.695  -40.279 -25.323 1.00 82.66  ? 334 GLU   A OE1 1 
ATOM   2345 O  OE2 . GLU   A 1 313 ? -5.553  -39.901 -25.617 1.00 83.75  ? 334 GLU   A OE2 1 
ATOM   2346 N  N   . ILE   A 1 314 ? -8.919  -44.769 -24.674 1.00 82.76  ? 335 ILE   A N   1 
ATOM   2347 C  CA  . ILE   A 1 314 ? -9.220  -45.192 -23.309 1.00 82.30  ? 335 ILE   A CA  1 
ATOM   2348 C  C   . ILE   A 1 314 ? -8.877  -46.665 -23.121 1.00 81.92  ? 335 ILE   A C   1 
ATOM   2349 O  O   . ILE   A 1 314 ? -8.254  -47.055 -22.126 1.00 81.97  ? 335 ILE   A O   1 
ATOM   2350 C  CB  . ILE   A 1 314 ? -10.695 -44.907 -22.972 1.00 83.27  ? 335 ILE   A CB  1 
ATOM   2351 C  CG1 . ILE   A 1 314 ? -10.943 -43.401 -22.881 1.00 78.95  ? 335 ILE   A CG1 1 
ATOM   2352 C  CG2 . ILE   A 1 314 ? -11.085 -45.585 -21.675 1.00 81.90  ? 335 ILE   A CG2 1 
ATOM   2353 C  CD1 . ILE   A 1 314 ? -12.398 -43.036 -22.683 1.00 78.62  ? 335 ILE   A CD1 1 
ATOM   2354 N  N   . ASP   A 1 315 ? -9.273  -47.505 -24.081 1.00 82.56  ? 336 ASP   A N   1 
ATOM   2355 C  CA  . ASP   A 1 315 ? -8.987  -48.933 -23.987 1.00 81.55  ? 336 ASP   A CA  1 
ATOM   2356 C  C   . ASP   A 1 315 ? -7.503  -49.240 -24.143 1.00 82.10  ? 336 ASP   A C   1 
ATOM   2357 O  O   . ASP   A 1 315 ? -7.057  -50.309 -23.714 1.00 86.01  ? 336 ASP   A O   1 
ATOM   2358 C  CB  . ASP   A 1 315 ? -9.795  -49.700 -25.034 1.00 79.16  ? 336 ASP   A CB  1 
ATOM   2359 C  CG  . ASP   A 1 315 ? -11.281 -49.711 -24.729 1.00 81.38  ? 336 ASP   A CG  1 
ATOM   2360 O  OD1 . ASP   A 1 315 ? -11.644 -49.757 -23.535 1.00 81.20  ? 336 ASP   A OD1 1 
ATOM   2361 O  OD2 . ASP   A 1 315 ? -12.086 -49.674 -25.684 1.00 82.21  ? 336 ASP   A OD2 1 
ATOM   2362 N  N   . ALA   A 1 316 ? -6.733  -48.333 -24.748 1.00 81.72  ? 337 ALA   A N   1 
ATOM   2363 C  CA  . ALA   A 1 316 ? -5.299  -48.561 -24.890 1.00 81.03  ? 337 ALA   A CA  1 
ATOM   2364 C  C   . ALA   A 1 316 ? -4.576  -48.355 -23.565 1.00 83.31  ? 337 ALA   A C   1 
ATOM   2365 O  O   . ALA   A 1 316 ? -3.787  -49.206 -23.139 1.00 84.23  ? 337 ALA   A O   1 
ATOM   2366 C  CB  . ALA   A 1 316 ? -4.725  -47.640 -25.967 1.00 80.05  ? 337 ALA   A CB  1 
ATOM   2367 N  N   . VAL   A 1 317 ? -4.828  -47.225 -22.902 1.00 84.44  ? 338 VAL   A N   1 
ATOM   2368 C  CA  . VAL   A 1 317 ? -4.174  -46.953 -21.626 1.00 81.81  ? 338 VAL   A CA  1 
ATOM   2369 C  C   . VAL   A 1 317 ? -4.700  -47.888 -20.545 1.00 81.81  ? 338 VAL   A C   1 
ATOM   2370 O  O   . VAL   A 1 317 ? -3.946  -48.343 -19.676 1.00 82.29  ? 338 VAL   A O   1 
ATOM   2371 C  CB  . VAL   A 1 317 ? -4.353  -45.475 -21.237 1.00 81.13  ? 338 VAL   A CB  1 
ATOM   2372 C  CG1 . VAL   A 1 317 ? -3.389  -45.107 -20.125 1.00 80.99  ? 338 VAL   A CG1 1 
ATOM   2373 C  CG2 . VAL   A 1 317 ? -4.149  -44.578 -22.448 1.00 79.27  ? 338 VAL   A CG2 1 
ATOM   2374 N  N   . LEU   A 1 318 ? -5.998  -48.194 -20.578 1.00 80.68  ? 339 LEU   A N   1 
ATOM   2375 C  CA  . LEU   A 1 318 ? -6.644  -49.060 -19.593 1.00 82.67  ? 339 LEU   A CA  1 
ATOM   2376 C  C   . LEU   A 1 318 ? -7.178  -50.292 -20.311 1.00 84.31  ? 339 LEU   A C   1 
ATOM   2377 O  O   . LEU   A 1 318 ? -8.337  -50.311 -20.756 1.00 83.83  ? 339 LEU   A O   1 
ATOM   2378 C  CB  . LEU   A 1 318 ? -7.763  -48.320 -18.864 1.00 82.55  ? 339 LEU   A CB  1 
ATOM   2379 C  CG  . LEU   A 1 318 ? -7.321  -47.158 -17.976 1.00 81.95  ? 339 LEU   A CG  1 
ATOM   2380 C  CD1 . LEU   A 1 318 ? -8.523  -46.368 -17.495 1.00 81.11  ? 339 LEU   A CD1 1 
ATOM   2381 C  CD2 . LEU   A 1 318 ? -6.501  -47.669 -16.800 1.00 81.15  ? 339 LEU   A CD2 1 
ATOM   2382 N  N   . PRO   A 1 319 ? -6.370  -51.341 -20.448 1.00 85.56  ? 340 PRO   A N   1 
ATOM   2383 C  CA  . PRO   A 1 319 ? -6.829  -52.534 -21.168 1.00 85.81  ? 340 PRO   A CA  1 
ATOM   2384 C  C   . PRO   A 1 319 ? -7.856  -53.310 -20.360 1.00 89.14  ? 340 PRO   A C   1 
ATOM   2385 O  O   . PRO   A 1 319 ? -7.753  -53.426 -19.136 1.00 89.15  ? 340 PRO   A O   1 
ATOM   2386 C  CB  . PRO   A 1 319 ? -5.543  -53.349 -21.368 1.00 85.39  ? 340 PRO   A CB  1 
ATOM   2387 C  CG  . PRO   A 1 319 ? -4.410  -52.402 -21.051 1.00 83.54  ? 340 PRO   A CG  1 
ATOM   2388 C  CD  . PRO   A 1 319 ? -4.961  -51.451 -20.041 1.00 83.36  ? 340 PRO   A CD  1 
ATOM   2389 N  N   . ASN   A 1 320 ? -8.850  -53.851 -21.069 1.00 89.39  ? 341 ASN   A N   1 
ATOM   2390 C  CA  . ASN   A 1 320 ? -9.898  -54.683 -20.474 1.00 89.73  ? 341 ASN   A CA  1 
ATOM   2391 C  C   . ASN   A 1 320 ? -10.601 -53.960 -19.325 1.00 86.91  ? 341 ASN   A C   1 
ATOM   2392 O  O   . ASN   A 1 320 ? -10.766 -54.498 -18.228 1.00 87.69  ? 341 ASN   A O   1 
ATOM   2393 C  CB  . ASN   A 1 320 ? -9.332  -56.031 -20.016 1.00 93.02  ? 341 ASN   A CB  1 
ATOM   2394 C  CG  . ASN   A 1 320 ? -10.419 -57.035 -19.681 1.00 97.42  ? 341 ASN   A CG  1 
ATOM   2395 O  OD1 . ASN   A 1 320 ? -11.592 -56.822 -19.986 1.00 96.56  ? 341 ASN   A OD1 1 
ATOM   2396 N  ND2 . ASN   A 1 320 ? -10.033 -58.138 -19.054 1.00 97.80  ? 341 ASN   A ND2 1 
ATOM   2397 N  N   . LYS   A 1 321 ? -11.013 -52.718 -19.590 1.00 87.34  ? 342 LYS   A N   1 
ATOM   2398 C  CA  . LYS   A 1 321 ? -11.784 -51.916 -18.639 1.00 87.02  ? 342 LYS   A CA  1 
ATOM   2399 C  C   . LYS   A 1 321 ? -11.048 -51.782 -17.305 1.00 84.15  ? 342 LYS   A C   1 
ATOM   2400 O  O   . LYS   A 1 321 ? -11.624 -51.943 -16.227 1.00 83.96  ? 342 LYS   A O   1 
ATOM   2401 C  CB  . LYS   A 1 321 ? -13.186 -52.502 -18.448 1.00 80.69  ? 342 LYS   A CB  1 
ATOM   2402 C  CG  . LYS   A 1 321 ? -13.895 -52.792 -19.765 1.00 78.16  ? 342 LYS   A CG  1 
ATOM   2403 C  CD  . LYS   A 1 321 ? -15.312 -53.301 -19.562 1.00 74.11  ? 342 LYS   A CD  1 
ATOM   2404 C  CE  . LYS   A 1 321 ? -16.007 -53.493 -20.904 1.00 74.48  ? 342 LYS   A CE  1 
ATOM   2405 N  NZ  . LYS   A 1 321 ? -17.459 -53.797 -20.759 1.00 76.07  ? 342 LYS   A NZ  1 
ATOM   2406 N  N   . ALA   A 1 322 ? -9.753  -51.487 -17.391 1.00 81.88  ? 343 ALA   A N   1 
ATOM   2407 C  CA  . ALA   A 1 322 ? -8.933  -51.331 -16.202 1.00 83.39  ? 343 ALA   A CA  1 
ATOM   2408 C  C   . ALA   A 1 322 ? -9.372  -50.101 -15.408 1.00 84.79  ? 343 ALA   A C   1 
ATOM   2409 O  O   . ALA   A 1 322 ? -9.855  -49.122 -15.983 1.00 83.89  ? 343 ALA   A O   1 
ATOM   2410 C  CB  . ALA   A 1 322 ? -7.460  -51.211 -16.585 1.00 82.65  ? 343 ALA   A CB  1 
ATOM   2411 N  N   . PRO   A 1 323 ? -9.223  -50.131 -14.086 1.00 84.70  ? 344 PRO   A N   1 
ATOM   2412 C  CA  . PRO   A 1 323 ? -9.677  -49.006 -13.258 1.00 82.40  ? 344 PRO   A CA  1 
ATOM   2413 C  C   . PRO   A 1 323 ? -8.916  -47.737 -13.589 1.00 83.83  ? 344 PRO   A C   1 
ATOM   2414 O  O   . PRO   A 1 323 ? -7.676  -47.729 -13.603 1.00 85.47  ? 344 PRO   A O   1 
ATOM   2415 C  CB  . PRO   A 1 323 ? -9.377  -49.474 -11.825 1.00 82.77  ? 344 PRO   A CB  1 
ATOM   2416 C  CG  . PRO   A 1 323 ? -9.273  -50.959 -11.918 1.00 87.42  ? 344 PRO   A CG  1 
ATOM   2417 C  CD  . PRO   A 1 323 ? -8.694  -51.236 -13.270 1.00 85.13  ? 344 PRO   A CD  1 
ATOM   2418 N  N   . PRO   A 1 324 ? -9.623  -46.644 -13.868 1.00 83.70  ? 345 PRO   A N   1 
ATOM   2419 C  CA  . PRO   A 1 324 ? -8.940  -45.368 -14.098 1.00 81.34  ? 345 PRO   A CA  1 
ATOM   2420 C  C   . PRO   A 1 324 ? -8.269  -44.872 -12.829 1.00 81.32  ? 345 PRO   A C   1 
ATOM   2421 O  O   . PRO   A 1 324 ? -8.760  -45.077 -11.716 1.00 83.93  ? 345 PRO   A O   1 
ATOM   2422 C  CB  . PRO   A 1 324 ? -10.072 -44.427 -14.534 1.00 78.59  ? 345 PRO   A CB  1 
ATOM   2423 C  CG  . PRO   A 1 324 ? -11.233 -45.320 -14.866 1.00 81.15  ? 345 PRO   A CG  1 
ATOM   2424 C  CD  . PRO   A 1 324 ? -11.083 -46.526 -14.004 1.00 84.70  ? 345 PRO   A CD  1 
ATOM   2425 N  N   . THR   A 1 325 ? -7.130  -44.209 -13.007 1.00 80.35  ? 346 THR   A N   1 
ATOM   2426 C  CA  . THR   A 1 325 ? -6.350  -43.674 -11.902 1.00 82.46  ? 346 THR   A CA  1 
ATOM   2427 C  C   . THR   A 1 325 ? -5.975  -42.230 -12.205 1.00 83.36  ? 346 THR   A C   1 
ATOM   2428 O  O   . THR   A 1 325 ? -6.147  -41.743 -13.325 1.00 82.81  ? 346 THR   A O   1 
ATOM   2429 C  CB  . THR   A 1 325 ? -5.085  -44.509 -11.638 1.00 85.48  ? 346 THR   A CB  1 
ATOM   2430 O  OG1 . THR   A 1 325 ? -4.227  -44.462 -12.784 1.00 86.41  ? 346 THR   A OG1 1 
ATOM   2431 C  CG2 . THR   A 1 325 ? -5.445  -45.959 -11.339 1.00 80.62  ? 346 THR   A CG2 1 
ATOM   2432 N  N   . TYR   A 1 326 ? -5.457  -41.546 -11.181 1.00 84.55  ? 347 TYR   A N   1 
ATOM   2433 C  CA  . TYR   A 1 326 ? -5.086  -40.141 -11.328 1.00 82.55  ? 347 TYR   A CA  1 
ATOM   2434 C  C   . TYR   A 1 326 ? -4.063  -39.954 -12.440 1.00 83.91  ? 347 TYR   A C   1 
ATOM   2435 O  O   . TYR   A 1 326 ? -4.231  -39.101 -13.320 1.00 82.66  ? 347 TYR   A O   1 
ATOM   2436 C  CB  . TYR   A 1 326 ? -4.543  -39.608 -10.000 1.00 81.92  ? 347 TYR   A CB  1 
ATOM   2437 C  CG  . TYR   A 1 326 ? -3.968  -38.210 -10.073 1.00 85.39  ? 347 TYR   A CG  1 
ATOM   2438 C  CD1 . TYR   A 1 326 ? -4.780  -37.096 -9.903  1.00 86.38  ? 347 TYR   A CD1 1 
ATOM   2439 C  CD2 . TYR   A 1 326 ? -2.611  -38.004 -10.296 1.00 84.98  ? 347 TYR   A CD2 1 
ATOM   2440 C  CE1 . TYR   A 1 326 ? -4.261  -35.817 -9.964  1.00 84.50  ? 347 TYR   A CE1 1 
ATOM   2441 C  CE2 . TYR   A 1 326 ? -2.083  -36.728 -10.360 1.00 87.63  ? 347 TYR   A CE2 1 
ATOM   2442 C  CZ  . TYR   A 1 326 ? -2.913  -35.638 -10.192 1.00 86.48  ? 347 TYR   A CZ  1 
ATOM   2443 O  OH  . TYR   A 1 326 ? -2.393  -34.365 -10.252 1.00 84.06  ? 347 TYR   A OH  1 
ATOM   2444 N  N   . ASP   A 1 327 ? -2.992  -40.750 -12.421 1.00 86.83  ? 348 ASP   A N   1 
ATOM   2445 C  CA  . ASP   A 1 327 ? -1.958  -40.618 -13.440 1.00 85.28  ? 348 ASP   A CA  1 
ATOM   2446 C  C   . ASP   A 1 327 ? -2.450  -41.084 -14.803 1.00 83.87  ? 348 ASP   A C   1 
ATOM   2447 O  O   . ASP   A 1 327 ? -1.974  -40.596 -15.834 1.00 84.50  ? 348 ASP   A O   1 
ATOM   2448 C  CB  . ASP   A 1 327 ? -0.714  -41.399 -13.019 1.00 86.43  ? 348 ASP   A CB  1 
ATOM   2449 C  CG  . ASP   A 1 327 ? -0.181  -40.954 -11.673 1.00 92.60  ? 348 ASP   A CG  1 
ATOM   2450 O  OD1 . ASP   A 1 327 ? -0.039  -39.730 -11.467 1.00 91.65  ? 348 ASP   A OD1 1 
ATOM   2451 O  OD2 . ASP   A 1 327 ? 0.078   -41.826 -10.817 1.00 93.50  ? 348 ASP   A OD2 1 
ATOM   2452 N  N   . THR   A 1 328 ? -3.389  -42.032 -14.829 1.00 82.77  ? 349 THR   A N   1 
ATOM   2453 C  CA  . THR   A 1 328 ? -3.944  -42.488 -16.098 1.00 82.85  ? 349 THR   A CA  1 
ATOM   2454 C  C   . THR   A 1 328 ? -4.717  -41.377 -16.798 1.00 83.09  ? 349 THR   A C   1 
ATOM   2455 O  O   . THR   A 1 328 ? -4.585  -41.189 -18.013 1.00 85.02  ? 349 THR   A O   1 
ATOM   2456 C  CB  . THR   A 1 328 ? -4.847  -43.700 -15.870 1.00 83.56  ? 349 THR   A CB  1 
ATOM   2457 O  OG1 . THR   A 1 328 ? -4.118  -44.718 -15.171 1.00 82.59  ? 349 THR   A OG1 1 
ATOM   2458 C  CG2 . THR   A 1 328 ? -5.327  -44.255 -17.192 1.00 81.04  ? 349 THR   A CG2 1 
ATOM   2459 N  N   . VAL   A 1 329 ? -5.524  -40.626 -16.044 1.00 82.69  ? 350 VAL   A N   1 
ATOM   2460 C  CA  . VAL   A 1 329 ? -6.373  -39.599 -16.643 1.00 83.03  ? 350 VAL   A CA  1 
ATOM   2461 C  C   . VAL   A 1 329 ? -5.529  -38.496 -17.269 1.00 82.37  ? 350 VAL   A C   1 
ATOM   2462 O  O   . VAL   A 1 329 ? -5.835  -38.008 -18.363 1.00 81.62  ? 350 VAL   A O   1 
ATOM   2463 C  CB  . VAL   A 1 329 ? -7.352  -39.040 -15.595 1.00 83.43  ? 350 VAL   A CB  1 
ATOM   2464 C  CG1 . VAL   A 1 329 ? -8.188  -37.923 -16.193 1.00 78.41  ? 350 VAL   A CG1 1 
ATOM   2465 C  CG2 . VAL   A 1 329 ? -8.245  -40.145 -15.063 1.00 80.55  ? 350 VAL   A CG2 1 
ATOM   2466 N  N   . LEU   A 1 330 ? -4.459  -38.082 -16.589 1.00 82.57  ? 351 LEU   A N   1 
ATOM   2467 C  CA  . LEU   A 1 330 ? -3.588  -37.054 -17.143 1.00 82.00  ? 351 LEU   A CA  1 
ATOM   2468 C  C   . LEU   A 1 330 ? -2.890  -37.516 -18.416 1.00 82.30  ? 351 LEU   A C   1 
ATOM   2469 O  O   . LEU   A 1 330 ? -2.454  -36.675 -19.209 1.00 83.69  ? 351 LEU   A O   1 
ATOM   2470 C  CB  . LEU   A 1 330 ? -2.553  -36.625 -16.103 1.00 81.90  ? 351 LEU   A CB  1 
ATOM   2471 C  CG  . LEU   A 1 330 ? -3.117  -35.960 -14.847 1.00 82.60  ? 351 LEU   A CG  1 
ATOM   2472 C  CD1 . LEU   A 1 330 ? -1.999  -35.467 -13.939 1.00 84.49  ? 351 LEU   A CD1 1 
ATOM   2473 C  CD2 . LEU   A 1 330 ? -4.051  -34.820 -15.221 1.00 78.59  ? 351 LEU   A CD2 1 
ATOM   2474 N  N   . GLN   A 1 331 ? -2.770  -38.829 -18.625 1.00 82.37  ? 352 GLN   A N   1 
ATOM   2475 C  CA  . GLN   A 1 331 ? -2.094  -39.332 -19.817 1.00 82.83  ? 352 GLN   A CA  1 
ATOM   2476 C  C   . GLN   A 1 331 ? -2.957  -39.184 -21.066 1.00 83.34  ? 352 GLN   A C   1 
ATOM   2477 O  O   . GLN   A 1 331 ? -2.458  -38.789 -22.126 1.00 84.33  ? 352 GLN   A O   1 
ATOM   2478 C  CB  . GLN   A 1 331 ? -1.702  -40.796 -19.611 1.00 83.25  ? 352 GLN   A CB  1 
ATOM   2479 C  CG  . GLN   A 1 331 ? -1.098  -41.458 -20.836 1.00 88.47  ? 352 GLN   A CG  1 
ATOM   2480 C  CD  . GLN   A 1 331 ? -0.719  -42.905 -20.583 1.00 90.66  ? 352 GLN   A CD  1 
ATOM   2481 O  OE1 . GLN   A 1 331 ? -0.650  -43.349 -19.437 1.00 89.76  ? 352 GLN   A OE1 1 
ATOM   2482 N  NE2 . GLN   A 1 331 ? -0.474  -43.650 -21.655 1.00 90.51  ? 352 GLN   A NE2 1 
ATOM   2483 N  N   . MET   A 1 332 ? -4.247  -39.501 -20.966 1.00 82.39  ? 353 MET   A N   1 
ATOM   2484 C  CA  . MET   A 1 332 ? -5.131  -39.508 -22.130 1.00 81.52  ? 353 MET   A CA  1 
ATOM   2485 C  C   . MET   A 1 332 ? -5.310  -38.092 -22.664 1.00 81.89  ? 353 MET   A C   1 
ATOM   2486 O  O   . MET   A 1 332 ? -5.942  -37.250 -22.021 1.00 83.75  ? 353 MET   A O   1 
ATOM   2487 C  CB  . MET   A 1 332 ? -6.473  -40.134 -21.765 1.00 79.34  ? 353 MET   A CB  1 
ATOM   2488 C  CG  . MET   A 1 332 ? -6.533  -41.642 -21.969 1.00 84.67  ? 353 MET   A CG  1 
ATOM   2489 S  SD  . MET   A 1 332 ? -7.888  -42.425 -21.075 1.00 85.56  ? 353 MET   A SD  1 
ATOM   2490 C  CE  . MET   A 1 332 ? -7.311  -42.246 -19.393 1.00 82.15  ? 353 MET   A CE  1 
ATOM   2491 N  N   . GLU   A 1 333 ? -4.766  -37.833 -23.853 1.00 82.42  ? 354 GLU   A N   1 
ATOM   2492 C  CA  . GLU   A 1 333 ? -4.796  -36.493 -24.421 1.00 81.35  ? 354 GLU   A CA  1 
ATOM   2493 C  C   . GLU   A 1 333 ? -5.978  -36.261 -25.352 1.00 78.70  ? 354 GLU   A C   1 
ATOM   2494 O  O   . GLU   A 1 333 ? -6.447  -35.122 -25.461 1.00 78.27  ? 354 GLU   A O   1 
ATOM   2495 C  CB  . GLU   A 1 333 ? -3.489  -36.203 -25.165 1.00 86.41  ? 354 GLU   A CB  1 
ATOM   2496 C  CG  . GLU   A 1 333 ? -2.281  -36.091 -24.250 1.00 90.45  ? 354 GLU   A CG  1 
ATOM   2497 C  CD  . GLU   A 1 333 ? -1.201  -35.194 -24.818 1.00 94.29  ? 354 GLU   A CD  1 
ATOM   2498 O  OE1 . GLU   A 1 333 ? -1.362  -34.724 -25.964 1.00 95.83  ? 354 GLU   A OE1 1 
ATOM   2499 O  OE2 . GLU   A 1 333 ? -0.196  -34.955 -24.114 1.00 90.27  ? 354 GLU   A OE2 1 
ATOM   2500 N  N   . TYR   A 1 334 ? -6.472  -37.299 -26.033 1.00 77.15  ? 355 TYR   A N   1 
ATOM   2501 C  CA  . TYR   A 1 334 ? -7.684  -37.122 -26.826 1.00 76.42  ? 355 TYR   A CA  1 
ATOM   2502 C  C   . TYR   A 1 334 ? -8.898  -36.915 -25.933 1.00 77.35  ? 355 TYR   A C   1 
ATOM   2503 O  O   . TYR   A 1 334 ? -9.853  -36.239 -26.332 1.00 76.17  ? 355 TYR   A O   1 
ATOM   2504 C  CB  . TYR   A 1 334 ? -7.901  -38.316 -27.756 1.00 74.44  ? 355 TYR   A CB  1 
ATOM   2505 C  CG  . TYR   A 1 334 ? -8.851  -38.033 -28.897 1.00 72.32  ? 355 TYR   A CG  1 
ATOM   2506 C  CD1 . TYR   A 1 334 ? -8.510  -37.126 -29.890 1.00 71.78  ? 355 TYR   A CD1 1 
ATOM   2507 C  CD2 . TYR   A 1 334 ? -10.078 -38.677 -28.990 1.00 73.01  ? 355 TYR   A CD2 1 
ATOM   2508 C  CE1 . TYR   A 1 334 ? -9.364  -36.861 -30.939 1.00 74.79  ? 355 TYR   A CE1 1 
ATOM   2509 C  CE2 . TYR   A 1 334 ? -10.943 -38.419 -30.041 1.00 74.16  ? 355 TYR   A CE2 1 
ATOM   2510 C  CZ  . TYR   A 1 334 ? -10.577 -37.508 -31.012 1.00 75.21  ? 355 TYR   A CZ  1 
ATOM   2511 O  OH  . TYR   A 1 334 ? -11.415 -37.234 -32.066 1.00 73.66  ? 355 TYR   A OH  1 
ATOM   2512 N  N   . LEU   A 1 335 ? -8.882  -37.493 -24.730 1.00 77.01  ? 356 LEU   A N   1 
ATOM   2513 C  CA  . LEU   A 1 335 ? -9.910  -37.187 -23.742 1.00 76.08  ? 356 LEU   A CA  1 
ATOM   2514 C  C   . LEU   A 1 335 ? -9.853  -35.720 -23.337 1.00 74.10  ? 356 LEU   A C   1 
ATOM   2515 O  O   . LEU   A 1 335 ? -10.886 -35.049 -23.235 1.00 74.73  ? 356 LEU   A O   1 
ATOM   2516 C  CB  . LEU   A 1 335 ? -9.744  -38.090 -22.519 1.00 75.32  ? 356 LEU   A CB  1 
ATOM   2517 C  CG  . LEU   A 1 335 ? -10.650 -37.796 -21.324 1.00 70.21  ? 356 LEU   A CG  1 
ATOM   2518 C  CD1 . LEU   A 1 335 ? -12.111 -37.989 -21.697 1.00 69.74  ? 356 LEU   A CD1 1 
ATOM   2519 C  CD2 . LEU   A 1 335 ? -10.268 -38.679 -20.148 1.00 71.22  ? 356 LEU   A CD2 1 
ATOM   2520 N  N   . ASP   A 1 336 ? -8.643  -35.204 -23.101 1.00 74.32  ? 357 ASP   A N   1 
ATOM   2521 C  CA  . ASP   A 1 336 ? -8.490  -33.791 -22.778 1.00 74.02  ? 357 ASP   A CA  1 
ATOM   2522 C  C   . ASP   A 1 336 ? -8.925  -32.908 -23.940 1.00 74.50  ? 357 ASP   A C   1 
ATOM   2523 O  O   . ASP   A 1 336 ? -9.472  -31.821 -23.726 1.00 75.28  ? 357 ASP   A O   1 
ATOM   2524 C  CB  . ASP   A 1 336 ? -7.037  -33.499 -22.395 1.00 74.34  ? 357 ASP   A CB  1 
ATOM   2525 C  CG  . ASP   A 1 336 ? -6.882  -32.195 -21.639 1.00 75.64  ? 357 ASP   A CG  1 
ATOM   2526 O  OD1 . ASP   A 1 336 ? -7.910  -31.543 -21.357 1.00 76.18  ? 357 ASP   A OD1 1 
ATOM   2527 O  OD2 . ASP   A 1 336 ? -5.732  -31.825 -21.322 1.00 76.64  ? 357 ASP   A OD2 1 
ATOM   2528 N  N   . MET   A 1 337 ? -8.684  -33.356 -25.175 1.00 75.13  ? 358 MET   A N   1 
ATOM   2529 C  CA  . MET   A 1 337 ? -9.115  -32.594 -26.343 1.00 74.69  ? 358 MET   A CA  1 
ATOM   2530 C  C   . MET   A 1 337 ? -10.636 -32.531 -26.441 1.00 75.08  ? 358 MET   A C   1 
ATOM   2531 O  O   . MET   A 1 337 ? -11.197 -31.478 -26.764 1.00 73.25  ? 358 MET   A O   1 
ATOM   2532 C  CB  . MET   A 1 337 ? -8.513  -33.202 -27.610 1.00 75.94  ? 358 MET   A CB  1 
ATOM   2533 C  CG  . MET   A 1 337 ? -7.026  -32.922 -27.772 1.00 79.98  ? 358 MET   A CG  1 
ATOM   2534 S  SD  . MET   A 1 337 ? -6.203  -34.012 -28.949 1.00 82.88  ? 358 MET   A SD  1 
ATOM   2535 C  CE  . MET   A 1 337 ? -7.197  -33.757 -30.415 1.00 80.66  ? 358 MET   A CE  1 
ATOM   2536 N  N   . VAL   A 1 338 ? -11.320 -33.646 -26.175 1.00 74.48  ? 359 VAL   A N   1 
ATOM   2537 C  CA  . VAL   A 1 338 ? -12.780 -33.658 -26.242 1.00 73.90  ? 359 VAL   A CA  1 
ATOM   2538 C  C   . VAL   A 1 338 ? -13.373 -32.761 -25.161 1.00 74.10  ? 359 VAL   A C   1 
ATOM   2539 O  O   . VAL   A 1 338 ? -14.304 -31.988 -25.415 1.00 73.38  ? 359 VAL   A O   1 
ATOM   2540 C  CB  . VAL   A 1 338 ? -13.316 -35.098 -26.136 1.00 72.57  ? 359 VAL   A CB  1 
ATOM   2541 C  CG1 . VAL   A 1 338 ? -14.820 -35.086 -25.916 1.00 68.27  ? 359 VAL   A CG1 1 
ATOM   2542 C  CG2 . VAL   A 1 338 ? -12.970 -35.883 -27.392 1.00 73.97  ? 359 VAL   A CG2 1 
ATOM   2543 N  N   . VAL   A 1 339 ? -12.847 -32.858 -23.938 1.00 73.96  ? 360 VAL   A N   1 
ATOM   2544 C  CA  . VAL   A 1 339 ? -13.340 -32.025 -22.843 1.00 70.38  ? 360 VAL   A CA  1 
ATOM   2545 C  C   . VAL   A 1 339 ? -13.149 -30.550 -23.172 1.00 68.32  ? 360 VAL   A C   1 
ATOM   2546 O  O   . VAL   A 1 339 ? -14.073 -29.739 -23.037 1.00 68.37  ? 360 VAL   A O   1 
ATOM   2547 C  CB  . VAL   A 1 339 ? -12.636 -32.399 -21.526 1.00 70.94  ? 360 VAL   A CB  1 
ATOM   2548 C  CG1 . VAL   A 1 339 ? -12.950 -31.371 -20.453 1.00 69.75  ? 360 VAL   A CG1 1 
ATOM   2549 C  CG2 . VAL   A 1 339 ? -13.050 -33.791 -21.075 1.00 71.11  ? 360 VAL   A CG2 1 
ATOM   2550 N  N   . ASN   A 1 340 ? -11.943 -30.185 -23.617 1.00 70.38  ? 361 ASN   A N   1 
ATOM   2551 C  CA  . ASN   A 1 340 ? -11.645 -28.785 -23.899 1.00 69.82  ? 361 ASN   A CA  1 
ATOM   2552 C  C   . ASN   A 1 340 ? -12.527 -28.240 -25.015 1.00 70.98  ? 361 ASN   A C   1 
ATOM   2553 O  O   . ASN   A 1 340 ? -13.053 -27.126 -24.910 1.00 68.29  ? 361 ASN   A O   1 
ATOM   2554 C  CB  . ASN   A 1 340 ? -10.168 -28.626 -24.261 1.00 69.04  ? 361 ASN   A CB  1 
ATOM   2555 C  CG  . ASN   A 1 340 ? -9.247  -28.837 -23.074 1.00 73.07  ? 361 ASN   A CG  1 
ATOM   2556 O  OD1 . ASN   A 1 340 ? -9.697  -29.149 -21.971 1.00 74.47  ? 361 ASN   A OD1 1 
ATOM   2557 N  ND2 . ASN   A 1 340 ? -7.948  -28.677 -23.298 1.00 74.79  ? 361 ASN   A ND2 1 
ATOM   2558 N  N   . GLU   A 1 341 ? -12.705 -29.012 -26.091 1.00 72.51  ? 362 GLU   A N   1 
ATOM   2559 C  CA  . GLU   A 1 341 ? -13.482 -28.519 -27.223 1.00 72.76  ? 362 GLU   A CA  1 
ATOM   2560 C  C   . GLU   A 1 341 ? -14.955 -28.357 -26.871 1.00 70.59  ? 362 GLU   A C   1 
ATOM   2561 O  O   . GLU   A 1 341 ? -15.618 -27.454 -27.395 1.00 69.85  ? 362 GLU   A O   1 
ATOM   2562 C  CB  . GLU   A 1 341 ? -13.314 -29.449 -28.425 1.00 73.67  ? 362 GLU   A CB  1 
ATOM   2563 C  CG  . GLU   A 1 341 ? -14.104 -29.036 -29.666 1.00 75.50  ? 362 GLU   A CG  1 
ATOM   2564 C  CD  . GLU   A 1 341 ? -13.626 -27.729 -30.284 1.00 75.20  ? 362 GLU   A CD  1 
ATOM   2565 O  OE1 . GLU   A 1 341 ? -12.560 -27.219 -29.879 1.00 74.45  ? 362 GLU   A OE1 1 
ATOM   2566 O  OE2 . GLU   A 1 341 ? -14.320 -27.211 -31.185 1.00 76.64  ? 362 GLU   A OE2 1 
ATOM   2567 N  N   . THR   A 1 342 ? -15.487 -29.213 -25.995 1.00 69.81  ? 363 THR   A N   1 
ATOM   2568 C  CA  . THR   A 1 342 ? -16.844 -29.000 -25.503 1.00 68.90  ? 363 THR   A CA  1 
ATOM   2569 C  C   . THR   A 1 342 ? -16.935 -27.706 -24.705 1.00 65.26  ? 363 THR   A C   1 
ATOM   2570 O  O   . THR   A 1 342 ? -17.893 -26.938 -24.856 1.00 64.87  ? 363 THR   A O   1 
ATOM   2571 C  CB  . THR   A 1 342 ? -17.295 -30.178 -24.642 1.00 66.78  ? 363 THR   A CB  1 
ATOM   2572 O  OG1 . THR   A 1 342 ? -17.094 -31.405 -25.355 1.00 67.44  ? 363 THR   A OG1 1 
ATOM   2573 C  CG2 . THR   A 1 342 ? -18.769 -30.037 -24.294 1.00 66.08  ? 363 THR   A CG2 1 
ATOM   2574 N  N   . LEU   A 1 343 ? -15.940 -27.446 -23.852 1.00 64.24  ? 364 LEU   A N   1 
ATOM   2575 C  CA  . LEU   A 1 343 ? -15.966 -26.244 -23.028 1.00 62.69  ? 364 LEU   A CA  1 
ATOM   2576 C  C   . LEU   A 1 343 ? -15.814 -24.980 -23.863 1.00 65.71  ? 364 LEU   A C   1 
ATOM   2577 O  O   . LEU   A 1 343 ? -16.263 -23.908 -23.443 1.00 67.82  ? 364 LEU   A O   1 
ATOM   2578 C  CB  . LEU   A 1 343 ? -14.879 -26.319 -21.956 1.00 62.15  ? 364 LEU   A CB  1 
ATOM   2579 C  CG  . LEU   A 1 343 ? -15.183 -27.301 -20.823 1.00 62.62  ? 364 LEU   A CG  1 
ATOM   2580 C  CD1 . LEU   A 1 343 ? -14.040 -27.364 -19.821 1.00 64.86  ? 364 LEU   A CD1 1 
ATOM   2581 C  CD2 . LEU   A 1 343 ? -16.484 -26.917 -20.133 1.00 58.58  ? 364 LEU   A CD2 1 
ATOM   2582 N  N   . ARG   A 1 344 ? -15.186 -25.076 -25.036 1.00 66.54  ? 365 ARG   A N   1 
ATOM   2583 C  CA  . ARG   A 1 344 ? -15.147 -23.925 -25.931 1.00 63.85  ? 365 ARG   A CA  1 
ATOM   2584 C  C   . ARG   A 1 344 ? -16.536 -23.613 -26.471 1.00 64.28  ? 365 ARG   A C   1 
ATOM   2585 O  O   . ARG   A 1 344 ? -16.985 -22.462 -26.436 1.00 67.52  ? 365 ARG   A O   1 
ATOM   2586 C  CB  . ARG   A 1 344 ? -14.175 -24.172 -27.083 1.00 68.40  ? 365 ARG   A CB  1 
ATOM   2587 C  CG  . ARG   A 1 344 ? -13.995 -22.958 -27.978 1.00 71.38  ? 365 ARG   A CG  1 
ATOM   2588 C  CD  . ARG   A 1 344 ? -13.296 -23.314 -29.274 1.00 71.03  ? 365 ARG   A CD  1 
ATOM   2589 N  NE  . ARG   A 1 344 ? -14.083 -24.236 -30.082 1.00 72.75  ? 365 ARG   A NE  1 
ATOM   2590 C  CZ  . ARG   A 1 344 ? -14.999 -23.863 -30.965 1.00 74.42  ? 365 ARG   A CZ  1 
ATOM   2591 N  NH1 . ARG   A 1 344 ? -15.278 -22.587 -31.174 1.00 75.56  ? 365 ARG   A NH1 1 
ATOM   2592 N  NH2 . ARG   A 1 344 ? -15.652 -24.794 -31.655 1.00 74.89  ? 365 ARG   A NH2 1 
ATOM   2593 N  N   . LEU   A 1 345 ? -17.239 -24.634 -26.964 1.00 64.01  ? 366 LEU   A N   1 
ATOM   2594 C  CA  . LEU   A 1 345 ? -18.575 -24.418 -27.505 1.00 65.02  ? 366 LEU   A CA  1 
ATOM   2595 C  C   . LEU   A 1 345 ? -19.571 -24.038 -26.418 1.00 64.85  ? 366 LEU   A C   1 
ATOM   2596 O  O   . LEU   A 1 345 ? -20.486 -23.246 -26.671 1.00 67.27  ? 366 LEU   A O   1 
ATOM   2597 C  CB  . LEU   A 1 345 ? -19.050 -25.666 -28.249 1.00 67.40  ? 366 LEU   A CB  1 
ATOM   2598 C  CG  . LEU   A 1 345 ? -18.438 -25.903 -29.632 1.00 68.52  ? 366 LEU   A CG  1 
ATOM   2599 C  CD1 . LEU   A 1 345 ? -18.864 -27.253 -30.185 1.00 71.34  ? 366 LEU   A CD1 1 
ATOM   2600 C  CD2 . LEU   A 1 345 ? -18.836 -24.788 -30.583 1.00 69.77  ? 366 LEU   A CD2 1 
ATOM   2601 N  N   . PHE   A 1 346 ? -19.417 -24.579 -25.209 1.00 63.32  ? 367 PHE   A N   1 
ATOM   2602 C  CA  . PHE   A 1 346 ? -20.349 -24.324 -24.110 1.00 61.62  ? 367 PHE   A CA  1 
ATOM   2603 C  C   . PHE   A 1 346 ? -19.604 -23.933 -22.840 1.00 59.70  ? 367 PHE   A C   1 
ATOM   2604 O  O   . PHE   A 1 346 ? -19.476 -24.741 -21.910 1.00 59.20  ? 367 PHE   A O   1 
ATOM   2605 C  CB  . PHE   A 1 346 ? -21.238 -25.540 -23.853 1.00 63.06  ? 367 PHE   A CB  1 
ATOM   2606 C  CG  . PHE   A 1 346 ? -21.948 -26.040 -25.076 1.00 65.58  ? 367 PHE   A CG  1 
ATOM   2607 C  CD1 . PHE   A 1 346 ? -23.020 -25.342 -25.606 1.00 65.63  ? 367 PHE   A CD1 1 
ATOM   2608 C  CD2 . PHE   A 1 346 ? -21.543 -27.210 -25.696 1.00 66.47  ? 367 PHE   A CD2 1 
ATOM   2609 C  CE1 . PHE   A 1 346 ? -23.673 -25.800 -26.733 1.00 66.67  ? 367 PHE   A CE1 1 
ATOM   2610 C  CE2 . PHE   A 1 346 ? -22.193 -27.674 -26.823 1.00 65.54  ? 367 PHE   A CE2 1 
ATOM   2611 C  CZ  . PHE   A 1 346 ? -23.259 -26.969 -27.342 1.00 66.99  ? 367 PHE   A CZ  1 
ATOM   2612 N  N   . PRO   A 1 347 ? -19.103 -22.693 -22.757 1.00 60.50  ? 368 PRO   A N   1 
ATOM   2613 C  CA  . PRO   A 1 347 ? -18.640 -22.186 -21.459 1.00 58.10  ? 368 PRO   A CA  1 
ATOM   2614 C  C   . PRO   A 1 347 ? -19.822 -21.747 -20.607 1.00 60.55  ? 368 PRO   A C   1 
ATOM   2615 O  O   . PRO   A 1 347 ? -20.398 -20.678 -20.832 1.00 59.32  ? 368 PRO   A O   1 
ATOM   2616 C  CB  . PRO   A 1 347 ? -17.735 -21.011 -21.842 1.00 57.46  ? 368 PRO   A CB  1 
ATOM   2617 C  CG  . PRO   A 1 347 ? -18.307 -20.519 -23.132 1.00 59.90  ? 368 PRO   A CG  1 
ATOM   2618 C  CD  . PRO   A 1 347 ? -18.891 -21.717 -23.841 1.00 61.56  ? 368 PRO   A CD  1 
ATOM   2619 N  N   . ILE   A 1 348 ? -20.178 -22.558 -19.607 1.00 61.26  ? 369 ILE   A N   1 
ATOM   2620 C  CA  . ILE   A 1 348 ? -21.448 -22.374 -18.912 1.00 61.80  ? 369 ILE   A CA  1 
ATOM   2621 C  C   . ILE   A 1 348 ? -21.480 -21.105 -18.070 1.00 58.22  ? 369 ILE   A C   1 
ATOM   2622 O  O   . ILE   A 1 348 ? -22.567 -20.634 -17.714 1.00 57.59  ? 369 ILE   A O   1 
ATOM   2623 C  CB  . ILE   A 1 348 ? -21.766 -23.608 -18.047 1.00 58.73  ? 369 ILE   A CB  1 
ATOM   2624 C  CG1 . ILE   A 1 348 ? -20.578 -23.964 -17.154 1.00 55.67  ? 369 ILE   A CG1 1 
ATOM   2625 C  CG2 . ILE   A 1 348 ? -22.148 -24.788 -18.929 1.00 55.78  ? 369 ILE   A CG2 1 
ATOM   2626 C  CD1 . ILE   A 1 348 ? -20.801 -25.205 -16.325 1.00 61.55  ? 369 ILE   A CD1 1 
ATOM   2627 N  N   . ALA   A 1 349 ? -20.323 -20.532 -17.737 1.00 56.62  ? 370 ALA   A N   1 
ATOM   2628 C  CA  . ALA   A 1 349 ? -20.327 -19.242 -17.055 1.00 59.77  ? 370 ALA   A CA  1 
ATOM   2629 C  C   . ALA   A 1 349 ? -20.781 -18.125 -17.986 1.00 57.36  ? 370 ALA   A C   1 
ATOM   2630 O  O   . ALA   A 1 349 ? -21.378 -17.144 -17.528 1.00 54.13  ? 370 ALA   A O   1 
ATOM   2631 C  CB  . ALA   A 1 349 ? -18.941 -18.940 -16.490 1.00 60.31  ? 370 ALA   A CB  1 
ATOM   2632 N  N   . MET   A 1 350 ? -20.462 -18.239 -19.278 1.00 59.76  ? 371 MET   A N   1 
ATOM   2633 C  CA  . MET   A 1 350 ? -20.911 -17.362 -20.358 1.00 57.99  ? 371 MET   A CA  1 
ATOM   2634 C  C   . MET   A 1 350 ? -20.255 -15.991 -20.302 1.00 61.23  ? 371 MET   A C   1 
ATOM   2635 O  O   . MET   A 1 350 ? -20.296 -15.243 -21.284 1.00 66.70  ? 371 MET   A O   1 
ATOM   2636 C  CB  . MET   A 1 350 ? -22.432 -17.169 -20.324 1.00 56.25  ? 371 MET   A CB  1 
ATOM   2637 C  CG  . MET   A 1 350 ? -23.255 -18.437 -20.263 1.00 60.89  ? 371 MET   A CG  1 
ATOM   2638 S  SD  . MET   A 1 350 ? -24.977 -18.078 -19.865 1.00 65.21  ? 371 MET   A SD  1 
ATOM   2639 C  CE  . MET   A 1 350 ? -24.828 -17.580 -18.151 1.00 59.09  ? 371 MET   A CE  1 
ATOM   2640 N  N   . ARG   A 1 351 ? -19.588 -15.684 -19.193 1.00 59.00  ? 372 ARG   A N   1 
ATOM   2641 C  CA  . ARG   A 1 351 ? -19.202 -14.314 -18.890 1.00 57.05  ? 372 ARG   A CA  1 
ATOM   2642 C  C   . ARG   A 1 351 ? -18.271 -14.313 -17.691 1.00 56.84  ? 372 ARG   A C   1 
ATOM   2643 O  O   . ARG   A 1 351 ? -18.524 -15.009 -16.704 1.00 58.22  ? 372 ARG   A O   1 
ATOM   2644 C  CB  . ARG   A 1 351 ? -20.427 -13.440 -18.580 1.00 57.33  ? 372 ARG   A CB  1 
ATOM   2645 C  CG  . ARG   A 1 351 ? -21.091 -12.764 -19.769 1.00 56.73  ? 372 ARG   A CG  1 
ATOM   2646 C  CD  . ARG   A 1 351 ? -22.268 -11.930 -19.302 1.00 61.80  ? 372 ARG   A CD  1 
ATOM   2647 N  NE  . ARG   A 1 351 ? -22.987 -11.303 -20.403 1.00 62.68  ? 372 ARG   A NE  1 
ATOM   2648 C  CZ  . ARG   A 1 351 ? -23.915 -10.369 -20.249 1.00 62.18  ? 372 ARG   A CZ  1 
ATOM   2649 N  NH1 . ARG   A 1 351 ? -24.247 -9.915  -19.051 1.00 62.04  ? 372 ARG   A NH1 1 
ATOM   2650 N  NH2 . ARG   A 1 351 ? -24.524 -9.875  -21.324 1.00 61.65  ? 372 ARG   A NH2 1 
ATOM   2651 N  N   . LEU   A 1 352 ? -17.210 -13.520 -17.780 1.00 56.20  ? 373 LEU   A N   1 
ATOM   2652 C  CA  . LEU   A 1 352 ? -16.348 -13.218 -16.649 1.00 56.68  ? 373 LEU   A CA  1 
ATOM   2653 C  C   . LEU   A 1 352 ? -16.461 -11.728 -16.369 1.00 59.74  ? 373 LEU   A C   1 
ATOM   2654 O  O   . LEU   A 1 352 ? -16.309 -10.911 -17.283 1.00 62.04  ? 373 LEU   A O   1 
ATOM   2655 C  CB  . LEU   A 1 352 ? -14.900 -13.617 -16.939 1.00 60.71  ? 373 LEU   A CB  1 
ATOM   2656 C  CG  . LEU   A 1 352 ? -14.741 -15.031 -17.507 1.00 64.34  ? 373 LEU   A CG  1 
ATOM   2657 C  CD1 . LEU   A 1 352 ? -13.294 -15.320 -17.869 1.00 67.20  ? 373 LEU   A CD1 1 
ATOM   2658 C  CD2 . LEU   A 1 352 ? -15.272 -16.068 -16.525 1.00 59.72  ? 373 LEU   A CD2 1 
ATOM   2659 N  N   . GLU   A 1 353 ? -16.740 -11.377 -15.115 1.00 59.92  ? 374 GLU   A N   1 
ATOM   2660 C  CA  . GLU   A 1 353 ? -17.035 -9.999  -14.747 1.00 60.20  ? 374 GLU   A CA  1 
ATOM   2661 C  C   . GLU   A 1 353 ? -16.184 -9.571  -13.560 1.00 60.75  ? 374 GLU   A C   1 
ATOM   2662 O  O   . GLU   A 1 353 ? -15.978 -10.343 -12.618 1.00 63.25  ? 374 GLU   A O   1 
ATOM   2663 C  CB  . GLU   A 1 353 ? -18.524 -9.824  -14.412 1.00 65.13  ? 374 GLU   A CB  1 
ATOM   2664 C  CG  . GLU   A 1 353 ? -19.463 -10.091 -15.580 1.00 65.63  ? 374 GLU   A CG  1 
ATOM   2665 C  CD  . GLU   A 1 353 ? -20.918 -9.845  -15.231 1.00 68.99  ? 374 GLU   A CD  1 
ATOM   2666 O  OE1 . GLU   A 1 353 ? -21.214 -9.596  -14.043 1.00 71.17  ? 374 GLU   A OE1 1 
ATOM   2667 O  OE2 . GLU   A 1 353 ? -21.768 -9.897  -16.147 1.00 67.82  ? 374 GLU   A OE2 1 
ATOM   2668 N  N   . ARG   A 1 354 ? -15.689 -8.335  -13.619 1.00 61.54  ? 375 ARG   A N   1 
ATOM   2669 C  CA  . ARG   A 1 354 ? -14.945 -7.718  -12.531 1.00 64.38  ? 375 ARG   A CA  1 
ATOM   2670 C  C   . ARG   A 1 354 ? -15.475 -6.309  -12.300 1.00 64.71  ? 375 ARG   A C   1 
ATOM   2671 O  O   . ARG   A 1 354 ? -15.899 -5.628  -13.237 1.00 65.17  ? 375 ARG   A O   1 
ATOM   2672 C  CB  . ARG   A 1 354 ? -13.438 -7.663  -12.831 1.00 67.47  ? 375 ARG   A CB  1 
ATOM   2673 C  CG  . ARG   A 1 354 ? -12.760 -9.021  -12.946 1.00 65.45  ? 375 ARG   A CG  1 
ATOM   2674 C  CD  . ARG   A 1 354 ? -12.654 -9.710  -11.596 1.00 66.25  ? 375 ARG   A CD  1 
ATOM   2675 N  NE  . ARG   A 1 354 ? -11.944 -10.979 -11.693 1.00 67.89  ? 375 ARG   A NE  1 
ATOM   2676 C  CZ  . ARG   A 1 354 ? -12.528 -12.150 -11.908 1.00 63.09  ? 375 ARG   A CZ  1 
ATOM   2677 N  NH1 . ARG   A 1 354 ? -13.840 -12.254 -12.042 1.00 65.84  ? 375 ARG   A NH1 1 
ATOM   2678 N  NH2 . ARG   A 1 354 ? -11.777 -13.244 -11.991 1.00 63.12  ? 375 ARG   A NH2 1 
ATOM   2679 N  N   . VAL   A 1 355 ? -15.445 -5.876  -11.042 1.00 64.06  ? 376 VAL   A N   1 
ATOM   2680 C  CA  . VAL   A 1 355 ? -15.930 -4.557  -10.650 1.00 68.56  ? 376 VAL   A CA  1 
ATOM   2681 C  C   . VAL   A 1 355 ? -14.738 -3.629  -10.472 1.00 70.78  ? 376 VAL   A C   1 
ATOM   2682 O  O   . VAL   A 1 355 ? -13.769 -3.970  -9.780  1.00 70.91  ? 376 VAL   A O   1 
ATOM   2683 C  CB  . VAL   A 1 355 ? -16.776 -4.629  -9.368  1.00 68.38  ? 376 VAL   A CB  1 
ATOM   2684 C  CG1 . VAL   A 1 355 ? -16.950 -3.243  -8.764  1.00 68.81  ? 376 VAL   A CG1 1 
ATOM   2685 C  CG2 . VAL   A 1 355 ? -18.131 -5.240  -9.673  1.00 64.23  ? 376 VAL   A CG2 1 
ATOM   2686 N  N   . CYS   A 1 356 ? -14.807 -2.457  -11.101 1.00 72.40  ? 377 CYS   A N   1 
ATOM   2687 C  CA  . CYS   A 1 356 ? -13.712 -1.492  -11.101 1.00 73.07  ? 377 CYS   A CA  1 
ATOM   2688 C  C   . CYS   A 1 356 ? -13.785 -0.654  -9.829  1.00 73.58  ? 377 CYS   A C   1 
ATOM   2689 O  O   . CYS   A 1 356 ? -14.738 0.109   -9.633  1.00 73.52  ? 377 CYS   A O   1 
ATOM   2690 C  CB  . CYS   A 1 356 ? -13.795 -0.623  -12.351 1.00 73.75  ? 377 CYS   A CB  1 
ATOM   2691 S  SG  . CYS   A 1 356 ? -12.337 0.373   -12.688 1.00 83.71  ? 377 CYS   A SG  1 
ATOM   2692 N  N   . LYS   A 1 357 ? -12.776 -0.785  -8.962  1.00 75.46  ? 378 LYS   A N   1 
ATOM   2693 C  CA  . LYS   A 1 357 ? -12.803 -0.140  -7.653  1.00 76.30  ? 378 LYS   A CA  1 
ATOM   2694 C  C   . LYS   A 1 357 ? -12.362 1.320   -7.675  1.00 80.07  ? 378 LYS   A C   1 
ATOM   2695 O  O   . LYS   A 1 357 ? -12.590 2.025   -6.686  1.00 79.36  ? 378 LYS   A O   1 
ATOM   2696 C  CB  . LYS   A 1 357 ? -11.929 -0.916  -6.662  1.00 75.46  ? 378 LYS   A CB  1 
ATOM   2697 C  CG  . LYS   A 1 357 ? -12.541 -2.225  -6.179  1.00 81.13  ? 378 LYS   A CG  1 
ATOM   2698 C  CD  . LYS   A 1 357 ? -11.775 -2.802  -4.995  1.00 81.90  ? 378 LYS   A CD  1 
ATOM   2699 C  CE  . LYS   A 1 357 ? -10.330 -3.107  -5.350  1.00 81.71  ? 378 LYS   A CE  1 
ATOM   2700 N  NZ  . LYS   A 1 357 ? -9.648  -3.890  -4.281  1.00 80.64  ? 378 LYS   A NZ  1 
ATOM   2701 N  N   . LYS   A 1 358 ? -11.741 1.790   -8.755  1.00 79.26  ? 379 LYS   A N   1 
ATOM   2702 C  CA  . LYS   A 1 358 ? -11.302 3.178   -8.835  1.00 78.74  ? 379 LYS   A CA  1 
ATOM   2703 C  C   . LYS   A 1 358 ? -11.086 3.538   -10.298 1.00 80.67  ? 379 LYS   A C   1 
ATOM   2704 O  O   . LYS   A 1 358 ? -11.075 2.673   -11.174 1.00 80.49  ? 379 LYS   A O   1 
ATOM   2705 C  CB  . LYS   A 1 358 ? -10.024 3.414   -8.020  1.00 82.67  ? 379 LYS   A CB  1 
ATOM   2706 C  CG  . LYS   A 1 358 ? -8.794  2.701   -8.563  1.00 82.70  ? 379 LYS   A CG  1 
ATOM   2707 C  CD  . LYS   A 1 358 ? -7.556  3.031   -7.743  1.00 83.65  ? 379 LYS   A CD  1 
ATOM   2708 C  CE  . LYS   A 1 358 ? -6.312  2.371   -8.318  1.00 83.98  ? 379 LYS   A CE  1 
ATOM   2709 N  NZ  . LYS   A 1 358 ? -5.101  2.660   -7.499  1.00 81.39  ? 379 LYS   A NZ  1 
ATOM   2710 N  N   . ASP   A 1 359 ? -10.915 4.835   -10.552 1.00 79.68  ? 380 ASP   A N   1 
ATOM   2711 C  CA  . ASP   A 1 359 ? -10.607 5.295   -11.901 1.00 80.67  ? 380 ASP   A CA  1 
ATOM   2712 C  C   . ASP   A 1 359 ? -9.246  4.759   -12.327 1.00 82.75  ? 380 ASP   A C   1 
ATOM   2713 O  O   . ASP   A 1 359 ? -8.235  5.008   -11.661 1.00 82.76  ? 380 ASP   A O   1 
ATOM   2714 C  CB  . ASP   A 1 359 ? -10.628 6.820   -11.970 1.00 83.37  ? 380 ASP   A CB  1 
ATOM   2715 C  CG  . ASP   A 1 359 ? -12.014 7.371   -12.240 1.00 85.06  ? 380 ASP   A CG  1 
ATOM   2716 O  OD1 . ASP   A 1 359 ? -12.997 6.621   -12.068 1.00 86.03  ? 380 ASP   A OD1 1 
ATOM   2717 O  OD2 . ASP   A 1 359 ? -12.119 8.551   -12.636 1.00 86.62  ? 380 ASP   A OD2 1 
ATOM   2718 N  N   . VAL   A 1 360 ? -9.224  4.018   -13.433 1.00 82.84  ? 381 VAL   A N   1 
ATOM   2719 C  CA  . VAL   A 1 360 ? -8.015  3.371   -13.930 1.00 81.98  ? 381 VAL   A CA  1 
ATOM   2720 C  C   . VAL   A 1 360 ? -7.967  3.522   -15.445 1.00 85.81  ? 381 VAL   A C   1 
ATOM   2721 O  O   . VAL   A 1 360 ? -9.004  3.500   -16.117 1.00 85.63  ? 381 VAL   A O   1 
ATOM   2722 C  CB  . VAL   A 1 360 ? -7.961  1.874   -13.536 1.00 84.37  ? 381 VAL   A CB  1 
ATOM   2723 C  CG1 . VAL   A 1 360 ? -6.665  1.237   -14.013 1.00 88.00  ? 381 VAL   A CG1 1 
ATOM   2724 C  CG2 . VAL   A 1 360 ? -8.105  1.696   -12.031 1.00 85.83  ? 381 VAL   A CG2 1 
ATOM   2725 N  N   . GLU   A 1 361 ? -6.760  3.691   -15.979 1.00 86.52  ? 382 GLU   A N   1 
ATOM   2726 C  CA  . GLU   A 1 361 ? -6.512  3.638   -17.414 1.00 87.06  ? 382 GLU   A CA  1 
ATOM   2727 C  C   . GLU   A 1 361 ? -5.665  2.407   -17.707 1.00 88.25  ? 382 GLU   A C   1 
ATOM   2728 O  O   . GLU   A 1 361 ? -4.553  2.277   -17.182 1.00 90.49  ? 382 GLU   A O   1 
ATOM   2729 C  CB  . GLU   A 1 361 ? -5.812  4.907   -17.901 1.00 84.24  ? 382 GLU   A CB  1 
ATOM   2730 N  N   . ILE   A 1 362 ? -6.188  1.509   -18.539 1.00 85.28  ? 383 ILE   A N   1 
ATOM   2731 C  CA  . ILE   A 1 362 ? -5.504  0.270   -18.891 1.00 83.67  ? 383 ILE   A CA  1 
ATOM   2732 C  C   . ILE   A 1 362 ? -5.504  0.120   -20.406 1.00 86.67  ? 383 ILE   A C   1 
ATOM   2733 O  O   . ILE   A 1 362 ? -6.555  0.238   -21.047 1.00 86.91  ? 383 ILE   A O   1 
ATOM   2734 C  CB  . ILE   A 1 362 ? -6.156  -0.958  -18.226 1.00 85.70  ? 383 ILE   A CB  1 
ATOM   2735 C  CG1 . ILE   A 1 362 ? -7.669  -0.962  -18.458 1.00 84.45  ? 383 ILE   A CG1 1 
ATOM   2736 C  CG2 . ILE   A 1 362 ? -5.846  -0.985  -16.739 1.00 85.01  ? 383 ILE   A CG2 1 
ATOM   2737 C  CD1 . ILE   A 1 362 ? -8.325  -2.290  -18.160 1.00 83.64  ? 383 ILE   A CD1 1 
ATOM   2738 N  N   . ASN   A 1 363 ? -4.324  -0.137  -20.973 1.00 86.43  ? 384 ASN   A N   1 
ATOM   2739 C  CA  . ASN   A 1 363 ? -4.168  -0.399  -22.405 1.00 85.59  ? 384 ASN   A CA  1 
ATOM   2740 C  C   . ASN   A 1 363 ? -4.797  0.707   -23.250 1.00 86.59  ? 384 ASN   A C   1 
ATOM   2741 O  O   . ASN   A 1 363 ? -5.497  0.450   -24.232 1.00 86.92  ? 384 ASN   A O   1 
ATOM   2742 C  CB  . ASN   A 1 363 ? -4.742  -1.766  -22.774 1.00 86.85  ? 384 ASN   A CB  1 
ATOM   2743 C  CG  . ASN   A 1 363 ? -4.048  -2.902  -22.048 1.00 83.70  ? 384 ASN   A CG  1 
ATOM   2744 O  OD1 . ASN   A 1 363 ? -3.472  -2.709  -20.977 1.00 83.27  ? 384 ASN   A OD1 1 
ATOM   2745 N  ND2 . ASN   A 1 363 ? -4.093  -4.092  -22.632 1.00 82.10  ? 384 ASN   A ND2 1 
ATOM   2746 N  N   . GLY   A 1 364 ? -4.550  1.954   -22.855 1.00 84.85  ? 385 GLY   A N   1 
ATOM   2747 C  CA  . GLY   A 1 364 ? -5.022  3.097   -23.608 1.00 85.33  ? 385 GLY   A CA  1 
ATOM   2748 C  C   . GLY   A 1 364 ? -6.495  3.405   -23.480 1.00 87.86  ? 385 GLY   A C   1 
ATOM   2749 O  O   . GLY   A 1 364 ? -7.011  4.209   -24.264 1.00 85.81  ? 385 GLY   A O   1 
ATOM   2750 N  N   . MET   A 1 365 ? -7.194  2.796   -22.523 1.00 89.90  ? 386 MET   A N   1 
ATOM   2751 C  CA  . MET   A 1 365 ? -8.619  3.029   -22.328 1.00 87.50  ? 386 MET   A CA  1 
ATOM   2752 C  C   . MET   A 1 365 ? -8.878  3.414   -20.881 1.00 86.85  ? 386 MET   A C   1 
ATOM   2753 O  O   . MET   A 1 365 ? -8.386  2.754   -19.961 1.00 87.64  ? 386 MET   A O   1 
ATOM   2754 C  CB  . MET   A 1 365 ? -9.441  1.791   -22.703 1.00 83.82  ? 386 MET   A CB  1 
ATOM   2755 C  CG  . MET   A 1 365 ? -10.942 1.970   -22.533 1.00 85.78  ? 386 MET   A CG  1 
ATOM   2756 S  SD  . MET   A 1 365 ? -11.877 0.648   -23.323 1.00 86.63  ? 386 MET   A SD  1 
ATOM   2757 C  CE  . MET   A 1 365 ? -11.264 0.771   -25.000 1.00 85.52  ? 386 MET   A CE  1 
ATOM   2758 N  N   . PHE   A 1 366 ? -9.653  4.478   -20.687 1.00 84.67  ? 387 PHE   A N   1 
ATOM   2759 C  CA  . PHE   A 1 366 ? -10.006 4.956   -19.357 1.00 84.30  ? 387 PHE   A CA  1 
ATOM   2760 C  C   . PHE   A 1 366 ? -11.284 4.276   -18.882 1.00 85.29  ? 387 PHE   A C   1 
ATOM   2761 O  O   . PHE   A 1 366 ? -12.311 4.322   -19.565 1.00 83.99  ? 387 PHE   A O   1 
ATOM   2762 C  CB  . PHE   A 1 366 ? -10.184 6.474   -19.361 1.00 80.45  ? 387 PHE   A CB  1 
ATOM   2763 C  CG  . PHE   A 1 366 ? -10.881 7.006   -18.142 1.00 79.63  ? 387 PHE   A CG  1 
ATOM   2764 C  CD1 . PHE   A 1 366 ? -10.249 7.002   -16.910 1.00 83.17  ? 387 PHE   A CD1 1 
ATOM   2765 C  CD2 . PHE   A 1 366 ? -12.166 7.517   -18.230 1.00 78.12  ? 387 PHE   A CD2 1 
ATOM   2766 C  CE1 . PHE   A 1 366 ? -10.888 7.492   -15.786 1.00 83.15  ? 387 PHE   A CE1 1 
ATOM   2767 C  CE2 . PHE   A 1 366 ? -12.809 8.009   -17.109 1.00 79.53  ? 387 PHE   A CE2 1 
ATOM   2768 C  CZ  . PHE   A 1 366 ? -12.169 7.997   -15.886 1.00 79.68  ? 387 PHE   A CZ  1 
ATOM   2769 N  N   . ILE   A 1 367 ? -11.212 3.648   -17.717 1.00 82.29  ? 388 ILE   A N   1 
ATOM   2770 C  CA  . ILE   A 1 367 ? -12.329 2.928   -17.112 1.00 79.12  ? 388 ILE   A CA  1 
ATOM   2771 C  C   . ILE   A 1 367 ? -12.799 3.724   -15.900 1.00 79.90  ? 388 ILE   A C   1 
ATOM   2772 O  O   . ILE   A 1 367 ? -12.000 3.978   -14.989 1.00 80.22  ? 388 ILE   A O   1 
ATOM   2773 C  CB  . ILE   A 1 367 ? -11.933 1.499   -16.706 1.00 84.47  ? 388 ILE   A CB  1 
ATOM   2774 C  CG1 . ILE   A 1 367 ? -11.017 0.874   -17.761 1.00 84.04  ? 388 ILE   A CG1 1 
ATOM   2775 C  CG2 . ILE   A 1 367 ? -13.174 0.643   -16.499 1.00 81.24  ? 388 ILE   A CG2 1 
ATOM   2776 C  CD1 . ILE   A 1 367 ? -11.676 0.670   -19.101 1.00 82.51  ? 388 ILE   A CD1 1 
ATOM   2777 N  N   . PRO   A 1 368 ? -14.061 4.140   -15.842 1.00 79.57  ? 389 PRO   A N   1 
ATOM   2778 C  CA  . PRO   A 1 368 ? -14.549 4.861   -14.661 1.00 77.37  ? 389 PRO   A CA  1 
ATOM   2779 C  C   . PRO   A 1 368 ? -14.722 3.926   -13.474 1.00 75.52  ? 389 PRO   A C   1 
ATOM   2780 O  O   . PRO   A 1 368 ? -14.727 2.699   -13.594 1.00 78.20  ? 389 PRO   A O   1 
ATOM   2781 C  CB  . PRO   A 1 368 ? -15.897 5.435   -15.111 1.00 73.92  ? 389 PRO   A CB  1 
ATOM   2782 C  CG  . PRO   A 1 368 ? -15.911 5.296   -16.603 1.00 75.54  ? 389 PRO   A CG  1 
ATOM   2783 C  CD  . PRO   A 1 368 ? -15.070 4.099   -16.910 1.00 77.06  ? 389 PRO   A CD  1 
ATOM   2784 N  N   . LYS   A 1 369 ? -14.864 4.539   -12.302 1.00 73.29  ? 390 LYS   A N   1 
ATOM   2785 C  CA  . LYS   A 1 369 ? -15.112 3.785   -11.081 1.00 73.08  ? 390 LYS   A CA  1 
ATOM   2786 C  C   . LYS   A 1 369 ? -16.547 3.272   -11.053 1.00 74.85  ? 390 LYS   A C   1 
ATOM   2787 O  O   . LYS   A 1 369 ? -17.485 3.982   -11.426 1.00 74.49  ? 390 LYS   A O   1 
ATOM   2788 C  CB  . LYS   A 1 369 ? -14.837 4.662   -9.857  1.00 71.70  ? 390 LYS   A CB  1 
ATOM   2789 C  CG  . LYS   A 1 369 ? -15.218 4.037   -8.524  1.00 71.90  ? 390 LYS   A CG  1 
ATOM   2790 C  CD  . LYS   A 1 369 ? -14.752 4.903   -7.363  1.00 73.43  ? 390 LYS   A CD  1 
ATOM   2791 C  CE  . LYS   A 1 369 ? -15.238 4.360   -6.029  1.00 74.96  ? 390 LYS   A CE  1 
ATOM   2792 N  NZ  . LYS   A 1 369 ? -16.717 4.465   -5.895  1.00 77.30  ? 390 LYS   A NZ  1 
ATOM   2793 N  N   . GLY   A 1 370 ? -16.713 2.025   -10.614 1.00 73.02  ? 391 GLY   A N   1 
ATOM   2794 C  CA  . GLY   A 1 370 ? -18.022 1.429   -10.457 1.00 71.21  ? 391 GLY   A CA  1 
ATOM   2795 C  C   . GLY   A 1 370 ? -18.551 0.689   -11.667 1.00 73.37  ? 391 GLY   A C   1 
ATOM   2796 O  O   . GLY   A 1 370 ? -19.618 0.067   -11.572 1.00 73.74  ? 391 GLY   A O   1 
ATOM   2797 N  N   . VAL   A 1 371 ? -17.851 0.735   -12.795 1.00 68.93  ? 392 VAL   A N   1 
ATOM   2798 C  CA  . VAL   A 1 371 ? -18.285 0.032   -13.996 1.00 67.15  ? 392 VAL   A CA  1 
ATOM   2799 C  C   . VAL   A 1 371 ? -17.915 -1.439  -13.880 1.00 67.01  ? 392 VAL   A C   1 
ATOM   2800 O  O   . VAL   A 1 371 ? -16.834 -1.788  -13.388 1.00 70.63  ? 392 VAL   A O   1 
ATOM   2801 C  CB  . VAL   A 1 371 ? -17.659 0.668   -15.251 1.00 68.49  ? 392 VAL   A CB  1 
ATOM   2802 C  CG1 . VAL   A 1 371 ? -18.140 -0.042  -16.509 1.00 67.69  ? 392 VAL   A CG1 1 
ATOM   2803 C  CG2 . VAL   A 1 371 ? -17.986 2.151   -15.312 1.00 68.21  ? 392 VAL   A CG2 1 
ATOM   2804 N  N   . VAL   A 1 372 ? -18.816 -2.308  -14.325 1.00 64.53  ? 393 VAL   A N   1 
ATOM   2805 C  CA  . VAL   A 1 372 ? -18.562 -3.743  -14.361 1.00 65.87  ? 393 VAL   A CA  1 
ATOM   2806 C  C   . VAL   A 1 372 ? -17.896 -4.080  -15.688 1.00 65.99  ? 393 VAL   A C   1 
ATOM   2807 O  O   . VAL   A 1 372 ? -18.484 -3.881  -16.757 1.00 66.84  ? 393 VAL   A O   1 
ATOM   2808 C  CB  . VAL   A 1 372 ? -19.860 -4.543  -14.176 1.00 64.07  ? 393 VAL   A CB  1 
ATOM   2809 C  CG1 . VAL   A 1 372 ? -19.617 -6.019  -14.455 1.00 65.21  ? 393 VAL   A CG1 1 
ATOM   2810 C  CG2 . VAL   A 1 372 ? -20.405 -4.348  -12.771 1.00 62.47  ? 393 VAL   A CG2 1 
ATOM   2811 N  N   . VAL   A 1 373 ? -16.672 -4.591  -15.622 1.00 65.48  ? 394 VAL   A N   1 
ATOM   2812 C  CA  . VAL   A 1 373 ? -15.930 -4.989  -16.812 1.00 64.78  ? 394 VAL   A CA  1 
ATOM   2813 C  C   . VAL   A 1 373 ? -16.231 -6.456  -17.089 1.00 64.90  ? 394 VAL   A C   1 
ATOM   2814 O  O   . VAL   A 1 373 ? -16.013 -7.316  -16.229 1.00 66.01  ? 394 VAL   A O   1 
ATOM   2815 C  CB  . VAL   A 1 373 ? -14.424 -4.754  -16.633 1.00 65.17  ? 394 VAL   A CB  1 
ATOM   2816 C  CG1 . VAL   A 1 373 ? -13.671 -5.184  -17.879 1.00 67.53  ? 394 VAL   A CG1 1 
ATOM   2817 C  CG2 . VAL   A 1 373 ? -14.157 -3.290  -16.324 1.00 66.53  ? 394 VAL   A CG2 1 
ATOM   2818 N  N   . MET   A 1 374 ? -16.726 -6.743  -18.289 1.00 63.05  ? 395 MET   A N   1 
ATOM   2819 C  CA  . MET   A 1 374 ? -17.236 -8.063  -18.631 1.00 63.53  ? 395 MET   A CA  1 
ATOM   2820 C  C   . MET   A 1 374 ? -16.468 -8.646  -19.809 1.00 65.03  ? 395 MET   A C   1 
ATOM   2821 O  O   . MET   A 1 374 ? -16.187 -7.948  -20.789 1.00 64.11  ? 395 MET   A O   1 
ATOM   2822 C  CB  . MET   A 1 374 ? -18.734 -8.000  -18.955 1.00 60.17  ? 395 MET   A CB  1 
ATOM   2823 C  CG  . MET   A 1 374 ? -19.368 -9.351  -19.242 1.00 62.37  ? 395 MET   A CG  1 
ATOM   2824 S  SD  . MET   A 1 374 ? -19.512 -9.710  -21.003 1.00 60.76  ? 395 MET   A SD  1 
ATOM   2825 C  CE  . MET   A 1 374 ? -20.893 -8.662  -21.447 1.00 63.89  ? 395 MET   A CE  1 
ATOM   2826 N  N   . ILE   A 1 375 ? -16.133 -9.927  -19.704 1.00 64.33  ? 396 ILE   A N   1 
ATOM   2827 C  CA  . ILE   A 1 375 ? -15.447 -10.680 -20.746 1.00 62.52  ? 396 ILE   A CA  1 
ATOM   2828 C  C   . ILE   A 1 375 ? -16.451 -11.666 -21.341 1.00 63.37  ? 396 ILE   A C   1 
ATOM   2829 O  O   . ILE   A 1 375 ? -16.878 -12.604 -20.652 1.00 62.30  ? 396 ILE   A O   1 
ATOM   2830 C  CB  . ILE   A 1 375 ? -14.206 -11.405 -20.205 1.00 64.28  ? 396 ILE   A CB  1 
ATOM   2831 C  CG1 . ILE   A 1 375 ? -13.084 -10.408 -19.890 1.00 66.30  ? 396 ILE   A CG1 1 
ATOM   2832 C  CG2 . ILE   A 1 375 ? -13.716 -12.443 -21.202 1.00 67.10  ? 396 ILE   A CG2 1 
ATOM   2833 C  CD1 . ILE   A 1 375 ? -13.181 -9.754  -18.525 1.00 66.01  ? 396 ILE   A CD1 1 
ATOM   2834 N  N   . PRO   A 1 376 ? -16.864 -11.494 -22.599 1.00 66.85  ? 397 PRO   A N   1 
ATOM   2835 C  CA  . PRO   A 1 376 ? -17.860 -12.394 -23.225 1.00 64.96  ? 397 PRO   A CA  1 
ATOM   2836 C  C   . PRO   A 1 376 ? -17.254 -13.727 -23.660 1.00 65.39  ? 397 PRO   A C   1 
ATOM   2837 O  O   . PRO   A 1 376 ? -16.906 -13.953 -24.819 1.00 68.66  ? 397 PRO   A O   1 
ATOM   2838 C  CB  . PRO   A 1 376 ? -18.352 -11.575 -24.423 1.00 68.14  ? 397 PRO   A CB  1 
ATOM   2839 C  CG  . PRO   A 1 376 ? -17.746 -10.187 -24.270 1.00 65.85  ? 397 PRO   A CG  1 
ATOM   2840 C  CD  . PRO   A 1 376 ? -16.498 -10.382 -23.487 1.00 66.65  ? 397 PRO   A CD  1 
ATOM   2841 N  N   . SER   A 1 377 ? -17.136 -14.644 -22.695 1.00 65.84  ? 398 SER   A N   1 
ATOM   2842 C  CA  . SER   A 1 377 ? -16.469 -15.918 -22.954 1.00 63.45  ? 398 SER   A CA  1 
ATOM   2843 C  C   . SER   A 1 377 ? -17.154 -16.692 -24.074 1.00 64.04  ? 398 SER   A C   1 
ATOM   2844 O  O   . SER   A 1 377 ? -16.482 -17.258 -24.945 1.00 66.93  ? 398 SER   A O   1 
ATOM   2845 C  CB  . SER   A 1 377 ? -16.423 -16.758 -21.677 1.00 62.33  ? 398 SER   A CB  1 
ATOM   2846 O  OG  . SER   A 1 377 ? -15.465 -16.255 -20.761 1.00 64.04  ? 398 SER   A OG  1 
ATOM   2847 N  N   . TYR   A 1 378 ? -18.489 -16.728 -24.071 1.00 65.13  ? 399 TYR   A N   1 
ATOM   2848 C  CA  . TYR   A 1 378 ? -19.210 -17.418 -25.135 1.00 65.83  ? 399 TYR   A CA  1 
ATOM   2849 C  C   . TYR   A 1 378 ? -18.916 -16.792 -26.493 1.00 67.77  ? 399 TYR   A C   1 
ATOM   2850 O  O   . TYR   A 1 378 ? -18.698 -17.505 -27.480 1.00 69.54  ? 399 TYR   A O   1 
ATOM   2851 C  CB  . TYR   A 1 378 ? -20.712 -17.397 -24.847 1.00 66.37  ? 399 TYR   A CB  1 
ATOM   2852 C  CG  . TYR   A 1 378 ? -21.558 -18.169 -25.839 1.00 65.12  ? 399 TYR   A CG  1 
ATOM   2853 C  CD1 . TYR   A 1 378 ? -21.956 -17.594 -27.042 1.00 66.46  ? 399 TYR   A CD1 1 
ATOM   2854 C  CD2 . TYR   A 1 378 ? -21.976 -19.465 -25.564 1.00 63.85  ? 399 TYR   A CD2 1 
ATOM   2855 C  CE1 . TYR   A 1 378 ? -22.735 -18.291 -27.946 1.00 67.66  ? 399 TYR   A CE1 1 
ATOM   2856 C  CE2 . TYR   A 1 378 ? -22.756 -20.171 -26.464 1.00 66.38  ? 399 TYR   A CE2 1 
ATOM   2857 C  CZ  . TYR   A 1 378 ? -23.132 -19.578 -27.653 1.00 68.10  ? 399 TYR   A CZ  1 
ATOM   2858 O  OH  . TYR   A 1 378 ? -23.907 -20.272 -28.554 1.00 68.27  ? 399 TYR   A OH  1 
ATOM   2859 N  N   . ALA   A 1 379 ? -18.908 -15.458 -26.563 1.00 69.77  ? 400 ALA   A N   1 
ATOM   2860 C  CA  . ALA   A 1 379 ? -18.655 -14.784 -27.833 1.00 71.23  ? 400 ALA   A CA  1 
ATOM   2861 C  C   . ALA   A 1 379 ? -17.213 -14.968 -28.286 1.00 71.93  ? 400 ALA   A C   1 
ATOM   2862 O  O   . ALA   A 1 379 ? -16.958 -15.230 -29.467 1.00 75.61  ? 400 ALA   A O   1 
ATOM   2863 C  CB  . ALA   A 1 379 ? -18.993 -13.298 -27.712 1.00 70.94  ? 400 ALA   A CB  1 
ATOM   2864 N  N   . LEU   A 1 380 ? -16.257 -14.832 -27.364 1.00 69.21  ? 401 LEU   A N   1 
ATOM   2865 C  CA  . LEU   A 1 380 ? -14.851 -14.981 -27.729 1.00 70.62  ? 401 LEU   A CA  1 
ATOM   2866 C  C   . LEU   A 1 380 ? -14.532 -16.405 -28.165 1.00 71.42  ? 401 LEU   A C   1 
ATOM   2867 O  O   . LEU   A 1 380 ? -13.663 -16.609 -29.020 1.00 74.89  ? 401 LEU   A O   1 
ATOM   2868 C  CB  . LEU   A 1 380 ? -13.958 -14.565 -26.559 1.00 67.64  ? 401 LEU   A CB  1 
ATOM   2869 C  CG  . LEU   A 1 380 ? -14.082 -13.105 -26.112 1.00 65.47  ? 401 LEU   A CG  1 
ATOM   2870 C  CD1 . LEU   A 1 380 ? -13.156 -12.817 -24.942 1.00 63.20  ? 401 LEU   A CD1 1 
ATOM   2871 C  CD2 . LEU   A 1 380 ? -13.800 -12.161 -27.270 1.00 69.29  ? 401 LEU   A CD2 1 
ATOM   2872 N  N   . HIS   A 1 381 ? -15.221 -17.397 -27.597 1.00 70.99  ? 402 HIS   A N   1 
ATOM   2873 C  CA  . HIS   A 1 381 ? -15.023 -18.784 -27.993 1.00 71.22  ? 402 HIS   A CA  1 
ATOM   2874 C  C   . HIS   A 1 381 ? -15.591 -19.098 -29.370 1.00 74.78  ? 402 HIS   A C   1 
ATOM   2875 O  O   . HIS   A 1 381 ? -15.284 -20.162 -29.918 1.00 77.54  ? 402 HIS   A O   1 
ATOM   2876 C  CB  . HIS   A 1 381 ? -15.657 -19.723 -26.966 1.00 66.27  ? 402 HIS   A CB  1 
ATOM   2877 C  CG  . HIS   A 1 381 ? -14.926 -19.781 -25.663 1.00 64.46  ? 402 HIS   A CG  1 
ATOM   2878 N  ND1 . HIS   A 1 381 ? -15.203 -20.725 -24.698 1.00 62.99  ? 402 HIS   A ND1 1 
ATOM   2879 C  CD2 . HIS   A 1 381 ? -13.928 -19.014 -25.164 1.00 65.72  ? 402 HIS   A CD2 1 
ATOM   2880 C  CE1 . HIS   A 1 381 ? -14.407 -20.538 -23.661 1.00 64.33  ? 402 HIS   A CE1 1 
ATOM   2881 N  NE2 . HIS   A 1 381 ? -13.625 -19.504 -23.917 1.00 64.40  ? 402 HIS   A NE2 1 
ATOM   2882 N  N   . ARG   A 1 382 ? -16.418 -18.217 -29.931 1.00 74.35  ? 403 ARG   A N   1 
ATOM   2883 C  CA  . ARG   A 1 382 ? -17.016 -18.430 -31.244 1.00 76.17  ? 403 ARG   A CA  1 
ATOM   2884 C  C   . ARG   A 1 382 ? -16.728 -17.268 -32.189 1.00 80.54  ? 403 ARG   A C   1 
ATOM   2885 O  O   . ARG   A 1 382 ? -17.454 -17.069 -33.169 1.00 78.70  ? 403 ARG   A O   1 
ATOM   2886 C  CB  . ARG   A 1 382 ? -18.522 -18.668 -31.107 1.00 73.56  ? 403 ARG   A CB  1 
ATOM   2887 C  CG  . ARG   A 1 382 ? -18.875 -19.925 -30.311 1.00 74.07  ? 403 ARG   A CG  1 
ATOM   2888 C  CD  . ARG   A 1 382 ? -20.358 -19.984 -29.963 1.00 73.13  ? 403 ARG   A CD  1 
ATOM   2889 N  NE  . ARG   A 1 382 ? -20.713 -21.196 -29.231 1.00 66.98  ? 403 ARG   A NE  1 
ATOM   2890 C  CZ  . ARG   A 1 382 ? -21.317 -22.248 -29.768 1.00 66.70  ? 403 ARG   A CZ  1 
ATOM   2891 N  NH1 . ARG   A 1 382 ? -21.666 -22.269 -31.043 1.00 71.32  ? 403 ARG   A NH1 1 
ATOM   2892 N  NH2 . ARG   A 1 382 ? -21.580 -23.305 -29.004 1.00 68.03  ? 403 ARG   A NH2 1 
ATOM   2893 N  N   . ASP   A 1 383 ? -15.683 -16.502 -31.907 1.00 80.75  ? 404 ASP   A N   1 
ATOM   2894 C  CA  . ASP   A 1 383 ? -15.273 -15.392 -32.758 1.00 81.75  ? 404 ASP   A CA  1 
ATOM   2895 C  C   . ASP   A 1 383 ? -14.588 -15.927 -34.011 1.00 85.90  ? 404 ASP   A C   1 
ATOM   2896 O  O   . ASP   A 1 383 ? -13.649 -16.721 -33.903 1.00 84.00  ? 404 ASP   A O   1 
ATOM   2897 C  CB  . ASP   A 1 383 ? -14.328 -14.468 -31.991 1.00 83.33  ? 404 ASP   A CB  1 
ATOM   2898 C  CG  . ASP   A 1 383 ? -13.951 -13.227 -32.776 1.00 85.54  ? 404 ASP   A CG  1 
ATOM   2899 O  OD1 . ASP   A 1 383 ? -14.648 -12.900 -33.758 1.00 84.06  ? 404 ASP   A OD1 1 
ATOM   2900 O  OD2 . ASP   A 1 383 ? -12.949 -12.578 -32.407 1.00 83.59  ? 404 ASP   A OD2 1 
ATOM   2901 N  N   . PRO   A 1 384 ? -15.031 -15.530 -35.207 1.00 88.15  ? 405 PRO   A N   1 
ATOM   2902 C  CA  . PRO   A 1 384 ? -14.346 -15.982 -36.430 1.00 87.12  ? 405 PRO   A CA  1 
ATOM   2903 C  C   . PRO   A 1 384 ? -12.899 -15.528 -36.533 1.00 87.21  ? 405 PRO   A C   1 
ATOM   2904 O  O   . PRO   A 1 384 ? -12.142 -16.109 -37.321 1.00 86.04  ? 405 PRO   A O   1 
ATOM   2905 C  CB  . PRO   A 1 384 ? -15.199 -15.375 -37.552 1.00 87.17  ? 405 PRO   A CB  1 
ATOM   2906 C  CG  . PRO   A 1 384 ? -16.552 -15.230 -36.951 1.00 87.38  ? 405 PRO   A CG  1 
ATOM   2907 C  CD  . PRO   A 1 384 ? -16.317 -14.875 -35.508 1.00 87.60  ? 405 PRO   A CD  1 
ATOM   2908 N  N   . LYS   A 1 385 ? -12.494 -14.501 -35.782 1.00 88.09  ? 406 LYS   A N   1 
ATOM   2909 C  CA  . LYS   A 1 385 ? -11.122 -14.009 -35.875 1.00 87.93  ? 406 LYS   A CA  1 
ATOM   2910 C  C   . LYS   A 1 385 ? -10.118 -15.047 -35.388 1.00 90.53  ? 406 LYS   A C   1 
ATOM   2911 O  O   . LYS   A 1 385 ? -9.036  -15.194 -35.969 1.00 92.06  ? 406 LYS   A O   1 
ATOM   2912 C  CB  . LYS   A 1 385 ? -10.976 -12.710 -35.082 1.00 82.34  ? 406 LYS   A CB  1 
ATOM   2913 N  N   . TYR   A 1 386 ? -10.453 -15.772 -34.320 1.00 87.35  ? 407 TYR   A N   1 
ATOM   2914 C  CA  . TYR   A 1 386 ? -9.524  -16.706 -33.702 1.00 85.31  ? 407 TYR   A CA  1 
ATOM   2915 C  C   . TYR   A 1 386 ? -9.850  -18.172 -33.952 1.00 85.35  ? 407 TYR   A C   1 
ATOM   2916 O  O   . TYR   A 1 386 ? -9.028  -19.032 -33.617 1.00 83.95  ? 407 TYR   A O   1 
ATOM   2917 C  CB  . TYR   A 1 386 ? -9.464  -16.472 -32.185 1.00 83.82  ? 407 TYR   A CB  1 
ATOM   2918 C  CG  . TYR   A 1 386 ? -8.919  -15.123 -31.779 1.00 87.03  ? 407 TYR   A CG  1 
ATOM   2919 C  CD1 . TYR   A 1 386 ? -7.550  -14.898 -31.707 1.00 86.69  ? 407 TYR   A CD1 1 
ATOM   2920 C  CD2 . TYR   A 1 386 ? -9.774  -14.077 -31.455 1.00 89.54  ? 407 TYR   A CD2 1 
ATOM   2921 C  CE1 . TYR   A 1 386 ? -7.048  -13.670 -31.328 1.00 89.67  ? 407 TYR   A CE1 1 
ATOM   2922 C  CE2 . TYR   A 1 386 ? -9.282  -12.843 -31.076 1.00 87.93  ? 407 TYR   A CE2 1 
ATOM   2923 C  CZ  . TYR   A 1 386 ? -7.918  -12.645 -31.014 1.00 89.14  ? 407 TYR   A CZ  1 
ATOM   2924 O  OH  . TYR   A 1 386 ? -7.420  -11.418 -30.637 1.00 86.72  ? 407 TYR   A OH  1 
ATOM   2925 N  N   . TRP   A 1 387 ? -11.011 -18.487 -34.521 1.00 85.65  ? 408 TRP   A N   1 
ATOM   2926 C  CA  . TRP   A 1 387 ? -11.433 -19.871 -34.671 1.00 84.68  ? 408 TRP   A CA  1 
ATOM   2927 C  C   . TRP   A 1 387 ? -11.926 -20.131 -36.087 1.00 87.45  ? 408 TRP   A C   1 
ATOM   2928 O  O   . TRP   A 1 387 ? -12.514 -19.257 -36.731 1.00 89.59  ? 408 TRP   A O   1 
ATOM   2929 C  CB  . TRP   A 1 387 ? -12.534 -20.226 -33.660 1.00 83.20  ? 408 TRP   A CB  1 
ATOM   2930 C  CG  . TRP   A 1 387 ? -12.198 -19.815 -32.258 1.00 81.26  ? 408 TRP   A CG  1 
ATOM   2931 C  CD1 . TRP   A 1 387 ? -12.556 -18.652 -31.637 1.00 80.54  ? 408 TRP   A CD1 1 
ATOM   2932 C  CD2 . TRP   A 1 387 ? -11.426 -20.557 -31.306 1.00 78.88  ? 408 TRP   A CD2 1 
ATOM   2933 N  NE1 . TRP   A 1 387 ? -12.058 -18.627 -30.357 1.00 77.64  ? 408 TRP   A NE1 1 
ATOM   2934 C  CE2 . TRP   A 1 387 ? -11.362 -19.784 -30.129 1.00 78.09  ? 408 TRP   A CE2 1 
ATOM   2935 C  CE3 . TRP   A 1 387 ? -10.786 -21.799 -31.334 1.00 78.48  ? 408 TRP   A CE3 1 
ATOM   2936 C  CZ2 . TRP   A 1 387 ? -10.683 -20.214 -28.990 1.00 76.91  ? 408 TRP   A CZ2 1 
ATOM   2937 C  CZ3 . TRP   A 1 387 ? -10.112 -22.224 -30.203 1.00 78.68  ? 408 TRP   A CZ3 1 
ATOM   2938 C  CH2 . TRP   A 1 387 ? -10.067 -21.434 -29.047 1.00 78.53  ? 408 TRP   A CH2 1 
ATOM   2939 N  N   . THR   A 1 388 ? -11.681 -21.351 -36.560 1.00 88.28  ? 409 THR   A N   1 
ATOM   2940 C  CA  . THR   A 1 388 ? -12.093 -21.790 -37.888 1.00 87.07  ? 409 THR   A CA  1 
ATOM   2941 C  C   . THR   A 1 388 ? -13.311 -22.694 -37.760 1.00 86.67  ? 409 THR   A C   1 
ATOM   2942 O  O   . THR   A 1 388 ? -13.281 -23.675 -37.008 1.00 87.19  ? 409 THR   A O   1 
ATOM   2943 C  CB  . THR   A 1 388 ? -10.960 -22.536 -38.594 1.00 88.86  ? 409 THR   A CB  1 
ATOM   2944 O  OG1 . THR   A 1 388 ? -9.800  -21.697 -38.661 1.00 91.89  ? 409 THR   A OG1 1 
ATOM   2945 C  CG2 . THR   A 1 388 ? -11.380 -22.933 -40.003 1.00 90.12  ? 409 THR   A CG2 1 
ATOM   2946 N  N   . GLU   A 1 389 ? -14.369 -22.373 -38.514 1.00 90.70  ? 410 GLU   A N   1 
ATOM   2947 C  CA  . GLU   A 1 389 ? -15.667 -23.024 -38.378 1.00 90.04  ? 410 GLU   A CA  1 
ATOM   2948 C  C   . GLU   A 1 389 ? -16.050 -23.087 -36.904 1.00 89.10  ? 410 GLU   A C   1 
ATOM   2949 O  O   . GLU   A 1 389 ? -16.114 -24.181 -36.328 1.00 87.20  ? 410 GLU   A O   1 
ATOM   2950 C  CB  . GLU   A 1 389 ? -15.648 -24.425 -38.994 1.00 90.15  ? 410 GLU   A CB  1 
ATOM   2951 C  CG  . GLU   A 1 389 ? -15.587 -24.449 -40.516 1.00 94.82  ? 410 GLU   A CG  1 
ATOM   2952 C  CD  . GLU   A 1 389 ? -16.879 -23.987 -41.168 1.00 99.66  ? 410 GLU   A CD  1 
ATOM   2953 O  OE1 . GLU   A 1 389 ? -17.899 -23.858 -40.458 1.00 97.73  ? 410 GLU   A OE1 1 
ATOM   2954 O  OE2 . GLU   A 1 389 ? -16.872 -23.752 -42.395 1.00 100.57 ? 410 GLU   A OE2 1 
ATOM   2955 N  N   . PRO   A 1 390 ? -16.294 -21.941 -36.261 1.00 88.87  ? 411 PRO   A N   1 
ATOM   2956 C  CA  . PRO   A 1 390 ? -16.497 -21.948 -34.803 1.00 85.37  ? 411 PRO   A CA  1 
ATOM   2957 C  C   . PRO   A 1 390 ? -17.663 -22.807 -34.351 1.00 83.29  ? 411 PRO   A C   1 
ATOM   2958 O  O   . PRO   A 1 390 ? -17.615 -23.366 -33.249 1.00 83.31  ? 411 PRO   A O   1 
ATOM   2959 C  CB  . PRO   A 1 390 ? -16.730 -20.466 -34.475 1.00 86.78  ? 411 PRO   A CB  1 
ATOM   2960 C  CG  . PRO   A 1 390 ? -16.128 -19.719 -35.623 1.00 88.27  ? 411 PRO   A CG  1 
ATOM   2961 C  CD  . PRO   A 1 390 ? -16.373 -20.581 -36.820 1.00 86.21  ? 411 PRO   A CD  1 
ATOM   2962 N  N   . GLU   A 1 391 ? -18.712 -22.929 -35.166 1.00 82.39  ? 412 GLU   A N   1 
ATOM   2963 C  CA  . GLU   A 1 391 ? -19.858 -23.747 -34.795 1.00 82.27  ? 412 GLU   A CA  1 
ATOM   2964 C  C   . GLU   A 1 391 ? -19.583 -25.240 -34.922 1.00 83.38  ? 412 GLU   A C   1 
ATOM   2965 O  O   . GLU   A 1 391 ? -20.384 -26.041 -34.429 1.00 84.21  ? 412 GLU   A O   1 
ATOM   2966 C  CB  . GLU   A 1 391 ? -21.068 -23.370 -35.652 1.00 81.57  ? 412 GLU   A CB  1 
ATOM   2967 C  CG  . GLU   A 1 391 ? -21.273 -21.868 -35.818 1.00 87.89  ? 412 GLU   A CG  1 
ATOM   2968 C  CD  . GLU   A 1 391 ? -21.717 -21.182 -34.539 1.00 88.16  ? 412 GLU   A CD  1 
ATOM   2969 O  OE1 . GLU   A 1 391 ? -22.400 -21.832 -33.718 1.00 84.03  ? 412 GLU   A OE1 1 
ATOM   2970 O  OE2 . GLU   A 1 391 ? -21.382 -19.992 -34.356 1.00 87.21  ? 412 GLU   A OE2 1 
ATOM   2971 N  N   . LYS   A 1 392 ? -18.484 -25.631 -35.562 1.00 83.76  ? 413 LYS   A N   1 
ATOM   2972 C  CA  . LYS   A 1 392 ? -18.172 -27.037 -35.788 1.00 83.85  ? 413 LYS   A CA  1 
ATOM   2973 C  C   . LYS   A 1 392 ? -17.425 -27.630 -34.600 1.00 81.73  ? 413 LYS   A C   1 
ATOM   2974 O  O   . LYS   A 1 392 ? -16.586 -26.968 -33.983 1.00 80.44  ? 413 LYS   A O   1 
ATOM   2975 C  CB  . LYS   A 1 392 ? -17.336 -27.204 -37.057 1.00 84.18  ? 413 LYS   A CB  1 
ATOM   2976 C  CG  . LYS   A 1 392 ? -18.100 -26.974 -38.349 1.00 85.61  ? 413 LYS   A CG  1 
ATOM   2977 C  CD  . LYS   A 1 392 ? -19.179 -28.021 -38.550 1.00 89.73  ? 413 LYS   A CD  1 
ATOM   2978 C  CE  . LYS   A 1 392 ? -19.664 -28.025 -39.988 1.00 93.54  ? 413 LYS   A CE  1 
ATOM   2979 N  NZ  . LYS   A 1 392 ? -18.548 -28.333 -40.927 1.00 92.56  ? 413 LYS   A NZ  1 
ATOM   2980 N  N   . PHE   A 1 393 ? -17.735 -28.888 -34.292 1.00 79.43  ? 414 PHE   A N   1 
ATOM   2981 C  CA  . PHE   A 1 393 ? -17.095 -29.619 -33.199 1.00 79.03  ? 414 PHE   A CA  1 
ATOM   2982 C  C   . PHE   A 1 393 ? -15.869 -30.334 -33.752 1.00 80.32  ? 414 PHE   A C   1 
ATOM   2983 O  O   . PHE   A 1 393 ? -15.974 -31.422 -34.322 1.00 79.72  ? 414 PHE   A O   1 
ATOM   2984 C  CB  . PHE   A 1 393 ? -18.072 -30.599 -32.562 1.00 77.39  ? 414 PHE   A CB  1 
ATOM   2985 C  CG  . PHE   A 1 393 ? -17.468 -31.439 -31.472 1.00 78.05  ? 414 PHE   A CG  1 
ATOM   2986 C  CD1 . PHE   A 1 393 ? -17.105 -30.869 -30.263 1.00 76.12  ? 414 PHE   A CD1 1 
ATOM   2987 C  CD2 . PHE   A 1 393 ? -17.273 -32.799 -31.650 1.00 80.14  ? 414 PHE   A CD2 1 
ATOM   2988 C  CE1 . PHE   A 1 393 ? -16.551 -31.637 -29.255 1.00 75.45  ? 414 PHE   A CE1 1 
ATOM   2989 C  CE2 . PHE   A 1 393 ? -16.721 -33.574 -30.645 1.00 78.44  ? 414 PHE   A CE2 1 
ATOM   2990 C  CZ  . PHE   A 1 393 ? -16.358 -32.991 -29.446 1.00 75.58  ? 414 PHE   A CZ  1 
ATOM   2991 N  N   . LEU   A 1 394 ? -14.699 -29.722 -33.578 1.00 79.13  ? 415 LEU   A N   1 
ATOM   2992 C  CA  . LEU   A 1 394 ? -13.440 -30.247 -34.103 1.00 78.48  ? 415 LEU   A CA  1 
ATOM   2993 C  C   . LEU   A 1 394 ? -12.443 -30.359 -32.959 1.00 77.87  ? 415 LEU   A C   1 
ATOM   2994 O  O   . LEU   A 1 394 ? -11.678 -29.421 -32.694 1.00 75.08  ? 415 LEU   A O   1 
ATOM   2995 C  CB  . LEU   A 1 394 ? -12.898 -29.361 -35.223 1.00 80.13  ? 415 LEU   A CB  1 
ATOM   2996 C  CG  . LEU   A 1 394 ? -13.825 -29.140 -36.420 1.00 83.10  ? 415 LEU   A CG  1 
ATOM   2997 C  CD1 . LEU   A 1 394 ? -13.136 -28.303 -37.487 1.00 82.42  ? 415 LEU   A CD1 1 
ATOM   2998 C  CD2 . LEU   A 1 394 ? -14.288 -30.471 -36.993 1.00 81.44  ? 415 LEU   A CD2 1 
ATOM   2999 N  N   . PRO   A 1 395 ? -12.413 -31.499 -32.263 1.00 76.66  ? 416 PRO   A N   1 
ATOM   3000 C  CA  . PRO   A 1 395 ? -11.513 -31.635 -31.104 1.00 76.26  ? 416 PRO   A CA  1 
ATOM   3001 C  C   . PRO   A 1 395 ? -10.038 -31.487 -31.445 1.00 77.34  ? 416 PRO   A C   1 
ATOM   3002 O  O   . PRO   A 1 395 ? -9.230  -31.304 -30.525 1.00 77.29  ? 416 PRO   A O   1 
ATOM   3003 C  CB  . PRO   A 1 395 ? -11.820 -33.046 -30.580 1.00 75.39  ? 416 PRO   A CB  1 
ATOM   3004 C  CG  . PRO   A 1 395 ? -13.171 -33.377 -31.128 1.00 75.97  ? 416 PRO   A CG  1 
ATOM   3005 C  CD  . PRO   A 1 395 ? -13.249 -32.694 -32.459 1.00 76.13  ? 416 PRO   A CD  1 
ATOM   3006 N  N   . GLU   A 1 396 ? -9.664  -31.548 -32.725 1.00 81.48  ? 417 GLU   A N   1 
ATOM   3007 C  CA  . GLU   A 1 396 ? -8.267  -31.428 -33.126 1.00 82.32  ? 417 GLU   A CA  1 
ATOM   3008 C  C   . GLU   A 1 396 ? -7.677  -30.054 -32.834 1.00 81.43  ? 417 GLU   A C   1 
ATOM   3009 O  O   . GLU   A 1 396 ? -6.452  -29.907 -32.903 1.00 81.11  ? 417 GLU   A O   1 
ATOM   3010 C  CB  . GLU   A 1 396 ? -8.123  -31.743 -34.617 1.00 79.46  ? 417 GLU   A CB  1 
ATOM   3011 C  CG  . GLU   A 1 396 ? -8.596  -33.135 -35.005 1.00 82.93  ? 417 GLU   A CG  1 
ATOM   3012 C  CD  . GLU   A 1 396 ? -7.709  -34.232 -34.448 1.00 87.33  ? 417 GLU   A CD  1 
ATOM   3013 O  OE1 . GLU   A 1 396 ? -6.513  -33.963 -34.203 1.00 85.97  ? 417 GLU   A OE1 1 
ATOM   3014 O  OE2 . GLU   A 1 396 ? -8.209  -35.360 -34.253 1.00 85.49  ? 417 GLU   A OE2 1 
ATOM   3015 N  N   . ARG   A 1 397 ? -8.509  -29.053 -32.524 1.00 80.74  ? 418 ARG   A N   1 
ATOM   3016 C  CA  . ARG   A 1 397 ? -7.989  -27.730 -32.187 1.00 80.24  ? 418 ARG   A CA  1 
ATOM   3017 C  C   . ARG   A 1 397 ? -7.016  -27.788 -31.018 1.00 81.19  ? 418 ARG   A C   1 
ATOM   3018 O  O   . ARG   A 1 397 ? -6.060  -27.006 -30.965 1.00 84.39  ? 418 ARG   A O   1 
ATOM   3019 C  CB  . ARG   A 1 397 ? -9.133  -26.774 -31.843 1.00 78.03  ? 418 ARG   A CB  1 
ATOM   3020 C  CG  . ARG   A 1 397 ? -10.200 -26.617 -32.908 1.00 79.83  ? 418 ARG   A CG  1 
ATOM   3021 C  CD  . ARG   A 1 397 ? -11.298 -25.689 -32.411 1.00 77.53  ? 418 ARG   A CD  1 
ATOM   3022 N  NE  . ARG   A 1 397 ? -12.537 -25.836 -33.165 1.00 79.26  ? 418 ARG   A NE  1 
ATOM   3023 C  CZ  . ARG   A 1 397 ? -12.899 -25.054 -34.172 1.00 82.03  ? 418 ARG   A CZ  1 
ATOM   3024 N  NH1 . ARG   A 1 397 ? -12.136 -24.052 -34.579 1.00 81.43  ? 418 ARG   A NH1 1 
ATOM   3025 N  NH2 . ARG   A 1 397 ? -14.057 -25.281 -34.786 1.00 82.43  ? 418 ARG   A NH2 1 
ATOM   3026 N  N   . PHE   A 1 398 ? -7.242  -28.701 -30.074 1.00 79.36  ? 419 PHE   A N   1 
ATOM   3027 C  CA  . PHE   A 1 398 ? -6.434  -28.801 -28.869 1.00 80.23  ? 419 PHE   A CA  1 
ATOM   3028 C  C   . PHE   A 1 398 ? -5.427  -29.943 -28.936 1.00 85.36  ? 419 PHE   A C   1 
ATOM   3029 O  O   . PHE   A 1 398 ? -4.926  -30.382 -27.896 1.00 85.68  ? 419 PHE   A O   1 
ATOM   3030 C  CB  . PHE   A 1 398 ? -7.339  -28.946 -27.645 1.00 76.26  ? 419 PHE   A CB  1 
ATOM   3031 C  CG  . PHE   A 1 398 ? -8.255  -27.775 -27.437 1.00 77.53  ? 419 PHE   A CG  1 
ATOM   3032 C  CD1 . PHE   A 1 398 ? -7.823  -26.659 -26.741 1.00 76.26  ? 419 PHE   A CD1 1 
ATOM   3033 C  CD2 . PHE   A 1 398 ? -9.540  -27.781 -27.951 1.00 76.66  ? 419 PHE   A CD2 1 
ATOM   3034 C  CE1 . PHE   A 1 398 ? -8.659  -25.575 -26.552 1.00 71.20  ? 419 PHE   A CE1 1 
ATOM   3035 C  CE2 . PHE   A 1 398 ? -10.380 -26.699 -27.766 1.00 72.16  ? 419 PHE   A CE2 1 
ATOM   3036 C  CZ  . PHE   A 1 398 ? -9.939  -25.595 -27.066 1.00 71.76  ? 419 PHE   A CZ  1 
ATOM   3037 N  N   . SER   A 1 399 ? -5.126  -30.432 -30.136 1.00 86.28  ? 420 SER   A N   1 
ATOM   3038 C  CA  . SER   A 1 399 ? -4.033  -31.375 -30.299 1.00 86.72  ? 420 SER   A CA  1 
ATOM   3039 C  C   . SER   A 1 399 ? -2.714  -30.707 -29.925 1.00 88.31  ? 420 SER   A C   1 
ATOM   3040 O  O   . SER   A 1 399 ? -2.583  -29.480 -29.943 1.00 89.34  ? 420 SER   A O   1 
ATOM   3041 C  CB  . SER   A 1 399 ? -3.975  -31.891 -31.736 1.00 86.42  ? 420 SER   A CB  1 
ATOM   3042 O  OG  . SER   A 1 399 ? -3.723  -30.833 -32.645 1.00 85.92  ? 420 SER   A OG  1 
ATOM   3043 N  N   . LYS   A 1 400 ? -1.725  -31.537 -29.580 1.00 89.01  ? 421 LYS   A N   1 
ATOM   3044 C  CA  . LYS   A 1 400 ? -0.453  -31.017 -29.087 1.00 90.47  ? 421 LYS   A CA  1 
ATOM   3045 C  C   . LYS   A 1 400 ? 0.174   -30.028 -30.063 1.00 89.90  ? 421 LYS   A C   1 
ATOM   3046 O  O   . LYS   A 1 400 ? 0.815   -29.059 -29.639 1.00 88.93  ? 421 LYS   A O   1 
ATOM   3047 C  CB  . LYS   A 1 400 ? 0.510   -32.172 -28.812 1.00 89.63  ? 421 LYS   A CB  1 
ATOM   3048 C  CG  . LYS   A 1 400 ? 1.391   -31.968 -27.592 1.00 91.57  ? 421 LYS   A CG  1 
ATOM   3049 C  CD  . LYS   A 1 400 ? 0.592   -32.102 -26.307 1.00 92.31  ? 421 LYS   A CD  1 
ATOM   3050 C  CE  . LYS   A 1 400 ? 1.471   -31.897 -25.084 1.00 93.14  ? 421 LYS   A CE  1 
ATOM   3051 N  NZ  . LYS   A 1 400 ? 0.748   -32.189 -23.815 1.00 92.10  ? 421 LYS   A NZ  1 
ATOM   3052 N  N   . LYS   A 1 401 ? -0.005  -30.248 -31.367 1.00 89.66  ? 422 LYS   A N   1 
ATOM   3053 C  CA  . LYS   A 1 401 ? 0.573   -29.341 -32.354 1.00 88.96  ? 422 LYS   A CA  1 
ATOM   3054 C  C   . LYS   A 1 401 ? -0.157  -28.002 -32.383 1.00 92.12  ? 422 LYS   A C   1 
ATOM   3055 O  O   . LYS   A 1 401 ? 0.475   -26.950 -32.535 1.00 95.31  ? 422 LYS   A O   1 
ATOM   3056 C  CB  . LYS   A 1 401 ? 0.553   -29.992 -33.738 1.00 89.77  ? 422 LYS   A CB  1 
ATOM   3057 N  N   . ASN   A 1 402 ? -1.481  -28.017 -32.237 1.00 89.62  ? 423 ASN   A N   1 
ATOM   3058 C  CA  . ASN   A 1 402 ? -2.297  -26.826 -32.429 1.00 89.11  ? 423 ASN   A CA  1 
ATOM   3059 C  C   . ASN   A 1 402 ? -2.779  -26.195 -31.128 1.00 89.00  ? 423 ASN   A C   1 
ATOM   3060 O  O   . ASN   A 1 402 ? -3.460  -25.165 -31.176 1.00 88.49  ? 423 ASN   A O   1 
ATOM   3061 C  CB  . ASN   A 1 402 ? -3.509  -27.154 -33.309 1.00 87.77  ? 423 ASN   A CB  1 
ATOM   3062 C  CG  . ASN   A 1 402 ? -3.127  -27.902 -34.571 1.00 89.87  ? 423 ASN   A CG  1 
ATOM   3063 O  OD1 . ASN   A 1 402 ? -1.974  -27.873 -34.999 1.00 93.57  ? 423 ASN   A OD1 1 
ATOM   3064 N  ND2 . ASN   A 1 402 ? -4.099  -28.575 -35.176 1.00 85.22  ? 423 ASN   A ND2 1 
ATOM   3065 N  N   . LYS   A 1 403 ? -2.447  -26.768 -29.974 1.00 88.81  ? 424 LYS   A N   1 
ATOM   3066 C  CA  . LYS   A 1 403 ? -2.943  -26.255 -28.703 1.00 90.02  ? 424 LYS   A CA  1 
ATOM   3067 C  C   . LYS   A 1 403 ? -2.073  -25.140 -28.132 1.00 90.24  ? 424 LYS   A C   1 
ATOM   3068 O  O   . LYS   A 1 403 ? -2.302  -24.713 -26.996 1.00 90.95  ? 424 LYS   A O   1 
ATOM   3069 C  CB  . LYS   A 1 403 ? -3.077  -27.389 -27.684 1.00 87.59  ? 424 LYS   A CB  1 
ATOM   3070 C  CG  . LYS   A 1 403 ? -1.767  -27.902 -27.113 1.00 87.27  ? 424 LYS   A CG  1 
ATOM   3071 C  CD  . LYS   A 1 403 ? -2.030  -28.931 -26.026 1.00 87.23  ? 424 LYS   A CD  1 
ATOM   3072 C  CE  . LYS   A 1 403 ? -0.864  -29.038 -25.061 1.00 85.28  ? 424 LYS   A CE  1 
ATOM   3073 N  NZ  . LYS   A 1 403 ? -1.183  -29.951 -23.930 1.00 79.59  ? 424 LYS   A NZ  1 
ATOM   3074 N  N   . ASP   A 1 404 ? -1.084  -24.660 -28.891 1.00 89.18  ? 425 ASP   A N   1 
ATOM   3075 C  CA  . ASP   A 1 404 ? -0.259  -23.537 -28.471 1.00 88.86  ? 425 ASP   A CA  1 
ATOM   3076 C  C   . ASP   A 1 404 ? -0.587  -22.236 -29.187 1.00 92.07  ? 425 ASP   A C   1 
ATOM   3077 O  O   . ASP   A 1 404 ? -0.164  -21.173 -28.723 1.00 94.68  ? 425 ASP   A O   1 
ATOM   3078 C  CB  . ASP   A 1 404 ? 1.227   -23.861 -28.680 1.00 93.07  ? 425 ASP   A CB  1 
ATOM   3079 C  CG  . ASP   A 1 404 ? 1.511   -24.432 -30.057 1.00 95.54  ? 425 ASP   A CG  1 
ATOM   3080 O  OD1 . ASP   A 1 404 ? 0.576   -24.487 -30.886 1.00 96.02  ? 425 ASP   A OD1 1 
ATOM   3081 O  OD2 . ASP   A 1 404 ? 2.667   -24.832 -30.309 1.00 96.65  ? 425 ASP   A OD2 1 
ATOM   3082 N  N   . ASN   A 1 405 ? -1.323  -22.293 -30.298 1.00 89.50  ? 426 ASN   A N   1 
ATOM   3083 C  CA  . ASN   A 1 405 ? -1.765  -21.089 -30.989 1.00 89.99  ? 426 ASN   A CA  1 
ATOM   3084 C  C   . ASN   A 1 405 ? -2.945  -20.418 -30.302 1.00 91.05  ? 426 ASN   A C   1 
ATOM   3085 O  O   . ASN   A 1 405 ? -3.334  -19.317 -30.707 1.00 92.03  ? 426 ASN   A O   1 
ATOM   3086 C  CB  . ASN   A 1 405 ? -2.141  -21.417 -32.438 1.00 89.20  ? 426 ASN   A CB  1 
ATOM   3087 C  CG  . ASN   A 1 405 ? -0.994  -22.032 -33.218 1.00 92.71  ? 426 ASN   A CG  1 
ATOM   3088 O  OD1 . ASN   A 1 405 ? 0.172   -21.710 -32.992 1.00 94.90  ? 426 ASN   A OD1 1 
ATOM   3089 N  ND2 . ASN   A 1 405 ? -1.323  -22.923 -34.148 1.00 96.83  ? 426 ASN   A ND2 1 
ATOM   3090 N  N   . ILE   A 1 406 ? -3.514  -21.047 -29.279 1.00 88.31  ? 427 ILE   A N   1 
ATOM   3091 C  CA  . ILE   A 1 406 ? -4.719  -20.554 -28.625 1.00 85.49  ? 427 ILE   A CA  1 
ATOM   3092 C  C   . ILE   A 1 406 ? -4.317  -19.645 -27.471 1.00 83.24  ? 427 ILE   A C   1 
ATOM   3093 O  O   . ILE   A 1 406 ? -3.590  -20.062 -26.562 1.00 80.45  ? 427 ILE   A O   1 
ATOM   3094 C  CB  . ILE   A 1 406 ? -5.596  -21.717 -28.138 1.00 83.96  ? 427 ILE   A CB  1 
ATOM   3095 C  CG1 . ILE   A 1 406 ? -5.868  -22.681 -29.297 1.00 83.56  ? 427 ILE   A CG1 1 
ATOM   3096 C  CG2 . ILE   A 1 406 ? -6.896  -21.196 -27.548 1.00 84.78  ? 427 ILE   A CG2 1 
ATOM   3097 C  CD1 . ILE   A 1 406 ? -6.690  -23.889 -28.920 1.00 81.73  ? 427 ILE   A CD1 1 
ATOM   3098 N  N   . ASP   A 1 407 ? -4.786  -18.403 -27.513 1.00 82.76  ? 428 ASP   A N   1 
ATOM   3099 C  CA  . ASP   A 1 407 ? -4.483  -17.441 -26.460 1.00 81.34  ? 428 ASP   A CA  1 
ATOM   3100 C  C   . ASP   A 1 407 ? -5.184  -17.856 -25.170 1.00 80.81  ? 428 ASP   A C   1 
ATOM   3101 O  O   . ASP   A 1 407 ? -6.388  -18.135 -25.189 1.00 76.73  ? 428 ASP   A O   1 
ATOM   3102 C  CB  . ASP   A 1 407 ? -4.934  -16.043 -26.892 1.00 78.62  ? 428 ASP   A CB  1 
ATOM   3103 C  CG  . ASP   A 1 407 ? -4.190  -14.929 -26.175 1.00 80.79  ? 428 ASP   A CG  1 
ATOM   3104 O  OD1 . ASP   A 1 407 ? -3.928  -15.052 -24.961 1.00 80.35  ? 428 ASP   A OD1 1 
ATOM   3105 O  OD2 . ASP   A 1 407 ? -3.872  -13.916 -26.835 1.00 82.61  ? 428 ASP   A OD2 1 
ATOM   3106 N  N   . PRO   A 1 408 ? -4.476  -17.912 -24.037 1.00 81.39  ? 429 PRO   A N   1 
ATOM   3107 C  CA  . PRO   A 1 408 ? -5.129  -18.293 -22.774 1.00 78.69  ? 429 PRO   A CA  1 
ATOM   3108 C  C   . PRO   A 1 408 ? -6.162  -17.295 -22.279 1.00 79.39  ? 429 PRO   A C   1 
ATOM   3109 O  O   . PRO   A 1 408 ? -6.807  -17.557 -21.257 1.00 79.25  ? 429 PRO   A O   1 
ATOM   3110 C  CB  . PRO   A 1 408 ? -3.955  -18.389 -21.785 1.00 79.34  ? 429 PRO   A CB  1 
ATOM   3111 C  CG  . PRO   A 1 408 ? -2.736  -18.539 -22.634 1.00 84.77  ? 429 PRO   A CG  1 
ATOM   3112 C  CD  . PRO   A 1 408 ? -3.018  -17.770 -23.884 1.00 82.20  ? 429 PRO   A CD  1 
ATOM   3113 N  N   . TYR   A 1 409 ? -6.340  -16.161 -22.956 1.00 78.88  ? 430 TYR   A N   1 
ATOM   3114 C  CA  . TYR   A 1 409 ? -7.285  -15.142 -22.524 1.00 75.10  ? 430 TYR   A CA  1 
ATOM   3115 C  C   . TYR   A 1 409 ? -8.424  -14.933 -23.511 1.00 73.69  ? 430 TYR   A C   1 
ATOM   3116 O  O   . TYR   A 1 409 ? -9.303  -14.102 -23.255 1.00 74.15  ? 430 TYR   A O   1 
ATOM   3117 C  CB  . TYR   A 1 409 ? -6.546  -13.826 -22.266 1.00 74.06  ? 430 TYR   A CB  1 
ATOM   3118 C  CG  . TYR   A 1 409 ? -5.430  -13.997 -21.263 1.00 77.61  ? 430 TYR   A CG  1 
ATOM   3119 C  CD1 . TYR   A 1 409 ? -5.673  -13.893 -19.900 1.00 79.58  ? 430 TYR   A CD1 1 
ATOM   3120 C  CD2 . TYR   A 1 409 ? -4.138  -14.296 -21.677 1.00 79.59  ? 430 TYR   A CD2 1 
ATOM   3121 C  CE1 . TYR   A 1 409 ? -4.659  -14.062 -18.979 1.00 83.43  ? 430 TYR   A CE1 1 
ATOM   3122 C  CE2 . TYR   A 1 409 ? -3.117  -14.468 -20.764 1.00 81.36  ? 430 TYR   A CE2 1 
ATOM   3123 C  CZ  . TYR   A 1 409 ? -3.383  -14.350 -19.415 1.00 84.22  ? 430 TYR   A CZ  1 
ATOM   3124 O  OH  . TYR   A 1 409 ? -2.370  -14.518 -18.499 1.00 85.84  ? 430 TYR   A OH  1 
ATOM   3125 N  N   . ILE   A 1 410 ? -8.431  -15.659 -24.628 1.00 73.58  ? 431 ILE   A N   1 
ATOM   3126 C  CA  . ILE   A 1 410 ? -9.612  -15.751 -25.476 1.00 73.86  ? 431 ILE   A CA  1 
ATOM   3127 C  C   . ILE   A 1 410 ? -10.383 -17.040 -25.214 1.00 74.49  ? 431 ILE   A C   1 
ATOM   3128 O  O   . ILE   A 1 410 ? -11.595 -17.086 -25.474 1.00 71.95  ? 431 ILE   A O   1 
ATOM   3129 C  CB  . ILE   A 1 410 ? -9.240  -15.644 -26.969 1.00 74.04  ? 431 ILE   A CB  1 
ATOM   3130 C  CG1 . ILE   A 1 410 ? -8.434  -16.869 -27.407 1.00 80.62  ? 431 ILE   A CG1 1 
ATOM   3131 C  CG2 . ILE   A 1 410 ? -8.455  -14.368 -27.231 1.00 76.24  ? 431 ILE   A CG2 1 
ATOM   3132 C  CD1 . ILE   A 1 410 ? -7.975  -16.825 -28.843 1.00 83.14  ? 431 ILE   A CD1 1 
ATOM   3133 N  N   . TYR   A 1 411 ? -9.721  -18.081 -24.710 1.00 73.52  ? 432 TYR   A N   1 
ATOM   3134 C  CA  . TYR   A 1 411 ? -10.354 -19.328 -24.291 1.00 67.40  ? 432 TYR   A CA  1 
ATOM   3135 C  C   . TYR   A 1 411 ? -10.239 -19.390 -22.771 1.00 67.32  ? 432 TYR   A C   1 
ATOM   3136 O  O   . TYR   A 1 411 ? -9.199  -19.781 -22.233 1.00 67.96  ? 432 TYR   A O   1 
ATOM   3137 C  CB  . TYR   A 1 411 ? -9.691  -20.528 -24.966 1.00 67.73  ? 432 TYR   A CB  1 
ATOM   3138 C  CG  . TYR   A 1 411 ? -10.182 -21.881 -24.492 1.00 68.50  ? 432 TYR   A CG  1 
ATOM   3139 C  CD1 . TYR   A 1 411 ? -11.299 -22.476 -25.063 1.00 66.65  ? 432 TYR   A CD1 1 
ATOM   3140 C  CD2 . TYR   A 1 411 ? -9.516  -22.573 -23.486 1.00 66.80  ? 432 TYR   A CD2 1 
ATOM   3141 C  CE1 . TYR   A 1 411 ? -11.745 -23.711 -24.637 1.00 65.87  ? 432 TYR   A CE1 1 
ATOM   3142 C  CE2 . TYR   A 1 411 ? -9.956  -23.809 -23.055 1.00 65.48  ? 432 TYR   A CE2 1 
ATOM   3143 C  CZ  . TYR   A 1 411 ? -11.071 -24.373 -23.635 1.00 66.36  ? 432 TYR   A CZ  1 
ATOM   3144 O  OH  . TYR   A 1 411 ? -11.519 -25.602 -23.214 1.00 67.52  ? 432 TYR   A OH  1 
ATOM   3145 N  N   . THR   A 1 412 ? -11.306 -18.993 -22.080 1.00 68.86  ? 433 THR   A N   1 
ATOM   3146 C  CA  . THR   A 1 412 ? -11.318 -18.884 -20.620 1.00 68.78  ? 433 THR   A CA  1 
ATOM   3147 C  C   . THR   A 1 412 ? -12.552 -19.579 -20.058 1.00 64.74  ? 433 THR   A C   1 
ATOM   3148 O  O   . THR   A 1 412 ? -13.466 -18.926 -19.537 1.00 66.53  ? 433 THR   A O   1 
ATOM   3149 C  CB  . THR   A 1 412 ? -11.277 -17.419 -20.182 1.00 71.99  ? 433 THR   A CB  1 
ATOM   3150 O  OG1 . THR   A 1 412 ? -12.258 -16.673 -20.914 1.00 67.26  ? 433 THR   A OG1 1 
ATOM   3151 C  CG2 . THR   A 1 412 ? -9.900  -16.823 -20.428 1.00 69.94  ? 433 THR   A CG2 1 
ATOM   3152 N  N   . PRO   A 1 413 ? -12.607 -20.912 -20.136 1.00 64.20  ? 434 PRO   A N   1 
ATOM   3153 C  CA  . PRO   A 1 413 ? -13.769 -21.612 -19.566 1.00 63.70  ? 434 PRO   A CA  1 
ATOM   3154 C  C   . PRO   A 1 413 ? -13.788 -21.588 -18.049 1.00 60.07  ? 434 PRO   A C   1 
ATOM   3155 O  O   . PRO   A 1 413 ? -14.867 -21.505 -17.450 1.00 59.51  ? 434 PRO   A O   1 
ATOM   3156 C  CB  . PRO   A 1 413 ? -13.618 -23.036 -20.116 1.00 63.41  ? 434 PRO   A CB  1 
ATOM   3157 C  CG  . PRO   A 1 413 ? -12.147 -23.199 -20.293 1.00 64.11  ? 434 PRO   A CG  1 
ATOM   3158 C  CD  . PRO   A 1 413 ? -11.619 -21.848 -20.701 1.00 63.92  ? 434 PRO   A CD  1 
ATOM   3159 N  N   . PHE   A 1 414 ? -12.621 -21.657 -17.408 1.00 59.84  ? 435 PHE   A N   1 
ATOM   3160 C  CA  . PHE   A 1 414 ? -12.512 -21.602 -15.957 1.00 57.51  ? 435 PHE   A CA  1 
ATOM   3161 C  C   . PHE   A 1 414 ? -12.040 -20.240 -15.460 1.00 57.51  ? 435 PHE   A C   1 
ATOM   3162 O  O   . PHE   A 1 414 ? -11.623 -20.119 -14.302 1.00 52.83  ? 435 PHE   A O   1 
ATOM   3163 C  CB  . PHE   A 1 414 ? -11.572 -22.698 -15.454 1.00 55.69  ? 435 PHE   A CB  1 
ATOM   3164 C  CG  . PHE   A 1 414 ? -12.095 -24.088 -15.666 1.00 59.14  ? 435 PHE   A CG  1 
ATOM   3165 C  CD1 . PHE   A 1 414 ? -12.922 -24.680 -14.726 1.00 57.81  ? 435 PHE   A CD1 1 
ATOM   3166 C  CD2 . PHE   A 1 414 ? -11.757 -24.805 -16.802 1.00 61.32  ? 435 PHE   A CD2 1 
ATOM   3167 C  CE1 . PHE   A 1 414 ? -13.405 -25.961 -14.915 1.00 56.99  ? 435 PHE   A CE1 1 
ATOM   3168 C  CE2 . PHE   A 1 414 ? -12.236 -26.086 -16.996 1.00 61.77  ? 435 PHE   A CE2 1 
ATOM   3169 C  CZ  . PHE   A 1 414 ? -13.061 -26.665 -16.051 1.00 59.21  ? 435 PHE   A CZ  1 
ATOM   3170 N  N   . GLY   A 1 415 ? -12.096 -19.219 -16.308 1.00 59.20  ? 436 GLY   A N   1 
ATOM   3171 C  CA  . GLY   A 1 415 ? -11.594 -17.914 -15.944 1.00 59.95  ? 436 GLY   A CA  1 
ATOM   3172 C  C   . GLY   A 1 415 ? -10.080 -17.848 -16.019 1.00 61.97  ? 436 GLY   A C   1 
ATOM   3173 O  O   . GLY   A 1 415 ? -9.407  -18.729 -16.563 1.00 60.93  ? 436 GLY   A O   1 
ATOM   3174 N  N   . SER   A 1 416 ? -9.540  -16.770 -15.457 1.00 64.42  ? 437 SER   A N   1 
ATOM   3175 C  CA  . SER   A 1 416 ? -8.096  -16.582 -15.423 1.00 65.68  ? 437 SER   A CA  1 
ATOM   3176 C  C   . SER   A 1 416 ? -7.744  -15.648 -14.275 1.00 66.59  ? 437 SER   A C   1 
ATOM   3177 O  O   . SER   A 1 416 ? -8.582  -14.882 -13.791 1.00 68.76  ? 437 SER   A O   1 
ATOM   3178 C  CB  . SER   A 1 416 ? -7.567  -16.030 -16.752 1.00 67.82  ? 437 SER   A CB  1 
ATOM   3179 O  OG  . SER   A 1 416 ? -6.157  -15.892 -16.715 1.00 70.92  ? 437 SER   A OG  1 
ATOM   3180 N  N   . GLY   A 1 417 ? -6.487  -15.723 -13.848 1.00 65.41  ? 438 GLY   A N   1 
ATOM   3181 C  CA  . GLY   A 1 417 ? -5.993  -14.876 -12.790 1.00 70.42  ? 438 GLY   A CA  1 
ATOM   3182 C  C   . GLY   A 1 417 ? -6.238  -15.450 -11.410 1.00 69.39  ? 438 GLY   A C   1 
ATOM   3183 O  O   . GLY   A 1 417 ? -6.716  -16.578 -11.253 1.00 66.61  ? 438 GLY   A O   1 
ATOM   3184 N  N   . PRO   A 1 418 ? -5.918  -14.667 -10.376 1.00 69.19  ? 439 PRO   A N   1 
ATOM   3185 C  CA  . PRO   A 1 418 ? -6.055  -15.170 -8.999  1.00 68.64  ? 439 PRO   A CA  1 
ATOM   3186 C  C   . PRO   A 1 418 ? -7.477  -15.539 -8.620  1.00 68.37  ? 439 PRO   A C   1 
ATOM   3187 O  O   . PRO   A 1 418 ? -7.668  -16.291 -7.657  1.00 69.05  ? 439 PRO   A O   1 
ATOM   3188 C  CB  . PRO   A 1 418 ? -5.537  -14.003 -8.145  1.00 69.98  ? 439 PRO   A CB  1 
ATOM   3189 C  CG  . PRO   A 1 418 ? -4.709  -13.174 -9.077  1.00 71.74  ? 439 PRO   A CG  1 
ATOM   3190 C  CD  . PRO   A 1 418 ? -5.358  -13.307 -10.418 1.00 69.69  ? 439 PRO   A CD  1 
ATOM   3191 N  N   . ARG   A 1 419 ? -8.481  -15.036 -9.337  1.00 68.42  ? 440 ARG   A N   1 
ATOM   3192 C  CA  . ARG   A 1 419 ? -9.876  -15.336 -9.049  1.00 67.27  ? 440 ARG   A CA  1 
ATOM   3193 C  C   . ARG   A 1 419 ? -10.472 -16.302 -10.071 1.00 64.13  ? 440 ARG   A C   1 
ATOM   3194 O  O   . ARG   A 1 419 ? -11.673 -16.264 -10.350 1.00 62.31  ? 440 ARG   A O   1 
ATOM   3195 C  CB  . ARG   A 1 419 ? -10.690 -14.045 -8.973  1.00 67.37  ? 440 ARG   A CB  1 
ATOM   3196 C  CG  . ARG   A 1 419 ? -11.945 -14.164 -8.127  1.00 69.25  ? 440 ARG   A CG  1 
ATOM   3197 C  CD  . ARG   A 1 419 ? -12.101 -13.003 -7.163  1.00 69.76  ? 440 ARG   A CD  1 
ATOM   3198 N  NE  . ARG   A 1 419 ? -13.195 -13.250 -6.233  1.00 71.15  ? 440 ARG   A NE  1 
ATOM   3199 C  CZ  . ARG   A 1 419 ? -13.603 -12.400 -5.301  1.00 71.11  ? 440 ARG   A CZ  1 
ATOM   3200 N  NH1 . ARG   A 1 419 ? -13.024 -11.222 -5.138  1.00 70.23  ? 440 ARG   A NH1 1 
ATOM   3201 N  NH2 . ARG   A 1 419 ? -14.620 -12.740 -4.515  1.00 69.80  ? 440 ARG   A NH2 1 
ATOM   3202 N  N   . ASN   A 1 420 ? -9.641  -17.173 -10.639 1.00 63.55  ? 441 ASN   A N   1 
ATOM   3203 C  CA  . ASN   A 1 420 ? -10.123 -18.223 -11.521 1.00 62.61  ? 441 ASN   A CA  1 
ATOM   3204 C  C   . ASN   A 1 420 ? -10.756 -19.339 -10.690 1.00 59.42  ? 441 ASN   A C   1 
ATOM   3205 O  O   . ASN   A 1 420 ? -10.748 -19.312 -9.456  1.00 59.70  ? 441 ASN   A O   1 
ATOM   3206 C  CB  . ASN   A 1 420 ? -8.986  -18.748 -12.395 1.00 63.25  ? 441 ASN   A CB  1 
ATOM   3207 C  CG  . ASN   A 1 420 ? -7.921  -19.480 -11.595 1.00 66.53  ? 441 ASN   A CG  1 
ATOM   3208 O  OD1 . ASN   A 1 420 ? -7.761  -19.256 -10.395 1.00 68.57  ? 441 ASN   A OD1 1 
ATOM   3209 N  ND2 . ASN   A 1 420 ? -7.182  -20.360 -12.263 1.00 68.18  ? 441 ASN   A ND2 1 
ATOM   3210 N  N   . CYS   A 1 421 ? -11.312 -20.339 -11.372 1.00 56.71  ? 442 CYS   A N   1 
ATOM   3211 C  CA  . CYS   A 1 421 ? -12.012 -21.419 -10.681 1.00 56.12  ? 442 CYS   A CA  1 
ATOM   3212 C  C   . CYS   A 1 421 ? -11.049 -22.206 -9.801  1.00 58.07  ? 442 CYS   A C   1 
ATOM   3213 O  O   . CYS   A 1 421 ? -10.119 -22.849 -10.300 1.00 60.45  ? 442 CYS   A O   1 
ATOM   3214 C  CB  . CYS   A 1 421 ? -12.684 -22.345 -11.693 1.00 54.58  ? 442 CYS   A CB  1 
ATOM   3215 S  SG  . CYS   A 1 421 ? -13.588 -23.734 -10.960 1.00 59.96  ? 442 CYS   A SG  1 
ATOM   3216 N  N   . ILE   A 1 422 ? -11.280 -22.158 -8.485  1.00 59.67  ? 443 ILE   A N   1 
ATOM   3217 C  CA  . ILE   A 1 422 ? -10.434 -22.890 -7.551  1.00 60.20  ? 443 ILE   A CA  1 
ATOM   3218 C  C   . ILE   A 1 422 ? -10.638 -24.394 -7.670  1.00 60.84  ? 443 ILE   A C   1 
ATOM   3219 O  O   . ILE   A 1 422 ? -9.804  -25.170 -7.189  1.00 64.98  ? 443 ILE   A O   1 
ATOM   3220 C  CB  . ILE   A 1 422 ? -10.692 -22.419 -6.106  1.00 61.14  ? 443 ILE   A CB  1 
ATOM   3221 C  CG1 . ILE   A 1 422 ? -9.449  -22.639 -5.238  1.00 64.31  ? 443 ILE   A CG1 1 
ATOM   3222 C  CG2 . ILE   A 1 422 ? -11.885 -23.149 -5.508  1.00 60.98  ? 443 ILE   A CG2 1 
ATOM   3223 C  CD1 . ILE   A 1 422 ? -9.617  -22.182 -3.804  1.00 68.03  ? 443 ILE   A CD1 1 
ATOM   3224 N  N   . GLY   A 1 423 ? -11.726 -24.831 -8.301  1.00 57.71  ? 444 GLY   A N   1 
ATOM   3225 C  CA  . GLY   A 1 423 ? -11.994 -26.247 -8.453  1.00 57.10  ? 444 GLY   A CA  1 
ATOM   3226 C  C   . GLY   A 1 423 ? -11.900 -26.719 -9.888  1.00 59.79  ? 444 GLY   A C   1 
ATOM   3227 O  O   . GLY   A 1 423 ? -12.630 -27.627 -10.297 1.00 60.65  ? 444 GLY   A O   1 
ATOM   3228 N  N   . MET   A 1 424 ? -11.009 -26.103 -10.669 1.00 60.89  ? 445 MET   A N   1 
ATOM   3229 C  CA  . MET   A 1 424 ? -10.851 -26.496 -12.066 1.00 59.59  ? 445 MET   A CA  1 
ATOM   3230 C  C   . MET   A 1 424 ? -10.282 -27.905 -12.185 1.00 60.08  ? 445 MET   A C   1 
ATOM   3231 O  O   . MET   A 1 424 ? -10.770 -28.717 -12.981 1.00 57.53  ? 445 MET   A O   1 
ATOM   3232 C  CB  . MET   A 1 424 ? -9.960  -25.491 -12.795 1.00 57.81  ? 445 MET   A CB  1 
ATOM   3233 C  CG  . MET   A 1 424 ? -9.560  -25.928 -14.194 1.00 61.00  ? 445 MET   A CG  1 
ATOM   3234 S  SD  . MET   A 1 424 ? -8.535  -24.713 -15.043 1.00 69.17  ? 445 MET   A SD  1 
ATOM   3235 C  CE  . MET   A 1 424 ? -7.118  -24.641 -13.951 1.00 65.81  ? 445 MET   A CE  1 
ATOM   3236 N  N   . ARG   A 1 425 ? -9.242  -28.214 -11.404 1.00 61.85  ? 446 ARG   A N   1 
ATOM   3237 C  CA  . ARG   A 1 425 ? -8.659  -29.551 -11.451 1.00 61.13  ? 446 ARG   A CA  1 
ATOM   3238 C  C   . ARG   A 1 425 ? -9.652  -30.604 -10.978 1.00 63.97  ? 446 ARG   A C   1 
ATOM   3239 O  O   . ARG   A 1 425 ? -9.764  -31.677 -11.582 1.00 66.49  ? 446 ARG   A O   1 
ATOM   3240 C  CB  . ARG   A 1 425 ? -7.382  -29.602 -10.612 1.00 64.18  ? 446 ARG   A CB  1 
ATOM   3241 C  CG  . ARG   A 1 425 ? -6.185  -28.922 -11.253 1.00 69.17  ? 446 ARG   A CG  1 
ATOM   3242 C  CD  . ARG   A 1 425 ? -4.901  -29.277 -10.521 1.00 75.81  ? 446 ARG   A CD  1 
ATOM   3243 N  NE  . ARG   A 1 425 ? -4.922  -28.833 -9.133  1.00 77.25  ? 446 ARG   A NE  1 
ATOM   3244 C  CZ  . ARG   A 1 425 ? -4.391  -27.697 -8.702  1.00 79.98  ? 446 ARG   A CZ  1 
ATOM   3245 N  NH1 . ARG   A 1 425 ? -3.776  -26.865 -9.526  1.00 81.57  ? 446 ARG   A NH1 1 
ATOM   3246 N  NH2 . ARG   A 1 425 ? -4.477  -27.390 -7.411  1.00 81.13  ? 446 ARG   A NH2 1 
ATOM   3247 N  N   . PHE   A 1 426 ? -10.381 -30.315 -9.898  1.00 62.60  ? 447 PHE   A N   1 
ATOM   3248 C  CA  . PHE   A 1 426 ? -11.382 -31.255 -9.404  1.00 62.42  ? 447 PHE   A CA  1 
ATOM   3249 C  C   . PHE   A 1 426 ? -12.444 -31.521 -10.462 1.00 62.18  ? 447 PHE   A C   1 
ATOM   3250 O  O   . PHE   A 1 426 ? -12.825 -32.673 -10.699 1.00 63.08  ? 447 PHE   A O   1 
ATOM   3251 C  CB  . PHE   A 1 426 ? -12.021 -30.715 -8.122  1.00 63.57  ? 447 PHE   A CB  1 
ATOM   3252 C  CG  . PHE   A 1 426 ? -12.988 -31.671 -7.469  1.00 64.96  ? 447 PHE   A CG  1 
ATOM   3253 C  CD1 . PHE   A 1 426 ? -14.318 -31.718 -7.862  1.00 63.45  ? 447 PHE   A CD1 1 
ATOM   3254 C  CD2 . PHE   A 1 426 ? -12.569 -32.509 -6.449  1.00 65.21  ? 447 PHE   A CD2 1 
ATOM   3255 C  CE1 . PHE   A 1 426 ? -15.204 -32.592 -7.261  1.00 63.47  ? 447 PHE   A CE1 1 
ATOM   3256 C  CE2 . PHE   A 1 426 ? -13.452 -33.382 -5.842  1.00 65.04  ? 447 PHE   A CE2 1 
ATOM   3257 C  CZ  . PHE   A 1 426 ? -14.771 -33.424 -6.248  1.00 61.61  ? 447 PHE   A CZ  1 
ATOM   3258 N  N   . ALA   A 1 427 ? -12.930 -30.462 -11.111 1.00 60.59  ? 448 ALA   A N   1 
ATOM   3259 C  CA  . ALA   A 1 427 ? -13.977 -30.618 -12.115 1.00 60.84  ? 448 ALA   A CA  1 
ATOM   3260 C  C   . ALA   A 1 427 ? -13.493 -31.455 -13.292 1.00 61.33  ? 448 ALA   A C   1 
ATOM   3261 O  O   . ALA   A 1 427 ? -14.191 -32.367 -13.748 1.00 61.00  ? 448 ALA   A O   1 
ATOM   3262 C  CB  . ALA   A 1 427 ? -14.453 -29.244 -12.589 1.00 56.51  ? 448 ALA   A CB  1 
ATOM   3263 N  N   . LEU   A 1 428 ? -12.289 -31.165 -13.792 1.00 61.95  ? 449 LEU   A N   1 
ATOM   3264 C  CA  . LEU   A 1 428 ? -11.767 -31.902 -14.939 1.00 60.58  ? 449 LEU   A CA  1 
ATOM   3265 C  C   . LEU   A 1 428 ? -11.520 -33.363 -14.590 1.00 64.72  ? 449 LEU   A C   1 
ATOM   3266 O  O   . LEU   A 1 428 ? -11.913 -34.265 -15.338 1.00 62.55  ? 449 LEU   A O   1 
ATOM   3267 C  CB  . LEU   A 1 428 ? -10.484 -31.242 -15.443 1.00 59.73  ? 449 LEU   A CB  1 
ATOM   3268 C  CG  . LEU   A 1 428 ? -10.671 -29.883 -16.111 1.00 61.43  ? 449 LEU   A CG  1 
ATOM   3269 C  CD1 . LEU   A 1 428 ? -9.324  -29.269 -16.439 1.00 61.09  ? 449 LEU   A CD1 1 
ATOM   3270 C  CD2 . LEU   A 1 428 ? -11.519 -30.025 -17.363 1.00 62.27  ? 449 LEU   A CD2 1 
ATOM   3271 N  N   . MET   A 1 429 ? -10.877 -33.615 -13.448 1.00 65.41  ? 450 MET   A N   1 
ATOM   3272 C  CA  . MET   A 1 429 ? -10.638 -34.990 -13.025 1.00 64.70  ? 450 MET   A CA  1 
ATOM   3273 C  C   . MET   A 1 429 ? -11.950 -35.738 -12.826 1.00 64.56  ? 450 MET   A C   1 
ATOM   3274 O  O   . MET   A 1 429 ? -12.090 -36.888 -13.259 1.00 69.40  ? 450 MET   A O   1 
ATOM   3275 C  CB  . MET   A 1 429 ? -9.810  -35.004 -11.740 1.00 68.21  ? 450 MET   A CB  1 
ATOM   3276 C  CG  . MET   A 1 429 ? -9.507  -36.394 -11.212 1.00 74.13  ? 450 MET   A CG  1 
ATOM   3277 S  SD  . MET   A 1 429 ? -8.487  -37.346 -12.349 1.00 81.87  ? 450 MET   A SD  1 
ATOM   3278 C  CE  . MET   A 1 429 ? -7.064  -36.271 -12.487 1.00 77.02  ? 450 MET   A CE  1 
ATOM   3279 N  N   . ASN   A 1 430 ? -12.928 -35.093 -12.185 1.00 64.01  ? 451 ASN   A N   1 
ATOM   3280 C  CA  . ASN   A 1 430 ? -14.217 -35.733 -11.937 1.00 64.06  ? 451 ASN   A CA  1 
ATOM   3281 C  C   . ASN   A 1 430 ? -14.935 -36.057 -13.242 1.00 65.12  ? 451 ASN   A C   1 
ATOM   3282 O  O   . ASN   A 1 430 ? -15.451 -37.166 -13.423 1.00 65.39  ? 451 ASN   A O   1 
ATOM   3283 C  CB  . ASN   A 1 430 ? -15.079 -34.825 -11.057 1.00 63.06  ? 451 ASN   A CB  1 
ATOM   3284 C  CG  . ASN   A 1 430 ? -16.366 -35.488 -10.610 1.00 64.50  ? 451 ASN   A CG  1 
ATOM   3285 O  OD1 . ASN   A 1 430 ? -16.456 -36.713 -10.541 1.00 70.10  ? 451 ASN   A OD1 1 
ATOM   3286 N  ND2 . ASN   A 1 430 ? -17.371 -34.676 -10.298 1.00 65.61  ? 451 ASN   A ND2 1 
ATOM   3287 N  N   . MET   A 1 431 ? -14.977 -35.095 -14.168 1.00 64.28  ? 452 MET   A N   1 
ATOM   3288 C  CA  . MET   A 1 431 ? -15.706 -35.298 -15.417 1.00 64.63  ? 452 MET   A CA  1 
ATOM   3289 C  C   . MET   A 1 431 ? -15.026 -36.337 -16.301 1.00 66.00  ? 452 MET   A C   1 
ATOM   3290 O  O   . MET   A 1 431 ? -15.699 -37.179 -16.907 1.00 66.54  ? 452 MET   A O   1 
ATOM   3291 C  CB  . MET   A 1 431 ? -15.850 -33.973 -16.163 1.00 64.90  ? 452 MET   A CB  1 
ATOM   3292 C  CG  . MET   A 1 431 ? -16.740 -32.960 -15.465 1.00 64.98  ? 452 MET   A CG  1 
ATOM   3293 S  SD  . MET   A 1 431 ? -16.932 -31.446 -16.422 1.00 63.86  ? 452 MET   A SD  1 
ATOM   3294 C  CE  . MET   A 1 431 ? -15.222 -31.023 -16.742 1.00 64.97  ? 452 MET   A CE  1 
ATOM   3295 N  N   . LYS   A 1 432 ? -13.696 -36.286 -16.398 1.00 68.64  ? 453 LYS   A N   1 
ATOM   3296 C  CA  . LYS   A 1 432 ? -12.977 -37.256 -17.217 1.00 68.20  ? 453 LYS   A CA  1 
ATOM   3297 C  C   . LYS   A 1 432 ? -13.120 -38.666 -16.659 1.00 69.42  ? 453 LYS   A C   1 
ATOM   3298 O  O   . LYS   A 1 432 ? -13.288 -39.627 -17.419 1.00 71.93  ? 453 LYS   A O   1 
ATOM   3299 C  CB  . LYS   A 1 432 ? -11.504 -36.867 -17.318 1.00 67.88  ? 453 LYS   A CB  1 
ATOM   3300 C  CG  . LYS   A 1 432 ? -11.243 -35.632 -18.162 1.00 64.75  ? 453 LYS   A CG  1 
ATOM   3301 C  CD  . LYS   A 1 432 ? -9.778  -35.246 -18.114 1.00 62.44  ? 453 LYS   A CD  1 
ATOM   3302 C  CE  . LYS   A 1 432 ? -9.478  -34.099 -19.061 1.00 67.24  ? 453 LYS   A CE  1 
ATOM   3303 N  NZ  . LYS   A 1 432 ? -8.056  -33.668 -18.958 1.00 69.56  ? 453 LYS   A NZ  1 
ATOM   3304 N  N   . LEU   A 1 433 ? -13.055 -38.807 -15.333 1.00 67.44  ? 454 LEU   A N   1 
ATOM   3305 C  CA  . LEU   A 1 433 ? -13.197 -40.122 -14.716 1.00 70.28  ? 454 LEU   A CA  1 
ATOM   3306 C  C   . LEU   A 1 433 ? -14.551 -40.740 -15.037 1.00 69.93  ? 454 LEU   A C   1 
ATOM   3307 O  O   . LEU   A 1 433 ? -14.654 -41.955 -15.246 1.00 71.80  ? 454 LEU   A O   1 
ATOM   3308 C  CB  . LEU   A 1 433 ? -12.990 -40.015 -13.205 1.00 69.69  ? 454 LEU   A CB  1 
ATOM   3309 C  CG  . LEU   A 1 433 ? -11.525 -40.004 -12.764 1.00 73.12  ? 454 LEU   A CG  1 
ATOM   3310 C  CD1 . LEU   A 1 433 ? -11.377 -39.521 -11.340 1.00 73.52  ? 454 LEU   A CD1 1 
ATOM   3311 C  CD2 . LEU   A 1 433 ? -10.941 -41.392 -12.906 1.00 74.87  ? 454 LEU   A CD2 1 
ATOM   3312 N  N   . ALA   A 1 434 ? -15.605 -39.923 -15.077 1.00 68.84  ? 455 ALA   A N   1 
ATOM   3313 C  CA  . ALA   A 1 434 ? -16.904 -40.420 -15.518 1.00 69.36  ? 455 ALA   A CA  1 
ATOM   3314 C  C   . ALA   A 1 434 ? -16.869 -40.805 -16.992 1.00 72.28  ? 455 ALA   A C   1 
ATOM   3315 O  O   . ALA   A 1 434 ? -17.366 -41.870 -17.376 1.00 74.20  ? 455 ALA   A O   1 
ATOM   3316 C  CB  . ALA   A 1 434 ? -17.984 -39.369 -15.261 1.00 67.16  ? 455 ALA   A CB  1 
ATOM   3317 N  N   . LEU   A 1 435 ? -16.269 -39.953 -17.829 1.00 71.84  ? 456 LEU   A N   1 
ATOM   3318 C  CA  . LEU   A 1 435 ? -16.218 -40.222 -19.264 1.00 71.28  ? 456 LEU   A CA  1 
ATOM   3319 C  C   . LEU   A 1 435 ? -15.465 -41.509 -19.573 1.00 75.22  ? 456 LEU   A C   1 
ATOM   3320 O  O   . LEU   A 1 435 ? -15.815 -42.219 -20.521 1.00 78.96  ? 456 LEU   A O   1 
ATOM   3321 C  CB  . LEU   A 1 435 ? -15.573 -39.044 -19.996 1.00 71.78  ? 456 LEU   A CB  1 
ATOM   3322 C  CG  . LEU   A 1 435 ? -16.383 -37.751 -20.110 1.00 70.93  ? 456 LEU   A CG  1 
ATOM   3323 C  CD1 . LEU   A 1 435 ? -15.498 -36.615 -20.597 1.00 68.13  ? 456 LEU   A CD1 1 
ATOM   3324 C  CD2 . LEU   A 1 435 ? -17.566 -37.946 -21.044 1.00 70.63  ? 456 LEU   A CD2 1 
ATOM   3325 N  N   . ILE   A 1 436 ? -14.428 -41.822 -18.794 1.00 74.15  ? 457 ILE   A N   1 
ATOM   3326 C  CA  . ILE   A 1 436 ? -13.663 -43.045 -19.023 1.00 74.55  ? 457 ILE   A CA  1 
ATOM   3327 C  C   . ILE   A 1 436 ? -14.523 -44.272 -18.747 1.00 74.95  ? 457 ILE   A C   1 
ATOM   3328 O  O   . ILE   A 1 436 ? -14.749 -45.105 -19.633 1.00 77.98  ? 457 ILE   A O   1 
ATOM   3329 C  CB  . ILE   A 1 436 ? -12.388 -43.052 -18.162 1.00 76.81  ? 457 ILE   A CB  1 
ATOM   3330 C  CG1 . ILE   A 1 436 ? -11.450 -41.925 -18.588 1.00 74.68  ? 457 ILE   A CG1 1 
ATOM   3331 C  CG2 . ILE   A 1 436 ? -11.685 -44.392 -18.269 1.00 76.73  ? 457 ILE   A CG2 1 
ATOM   3332 C  CD1 . ILE   A 1 436 ? -10.338 -41.677 -17.606 1.00 72.08  ? 457 ILE   A CD1 1 
ATOM   3333 N  N   . ARG   A 1 437 ? -15.023 -44.393 -17.513 1.00 75.68  ? 458 ARG   A N   1 
ATOM   3334 C  CA  . ARG   A 1 437 ? -15.808 -45.565 -17.136 1.00 76.41  ? 458 ARG   A CA  1 
ATOM   3335 C  C   . ARG   A 1 437 ? -17.045 -45.710 -18.010 1.00 75.43  ? 458 ARG   A C   1 
ATOM   3336 O  O   . ARG   A 1 437 ? -17.382 -46.818 -18.445 1.00 76.61  ? 458 ARG   A O   1 
ATOM   3337 C  CB  . ARG   A 1 437 ? -16.208 -45.477 -15.663 1.00 76.96  ? 458 ARG   A CB  1 
ATOM   3338 C  CG  . ARG   A 1 437 ? -15.196 -46.067 -14.700 1.00 81.86  ? 458 ARG   A CG  1 
ATOM   3339 C  CD  . ARG   A 1 437 ? -15.011 -47.551 -14.955 1.00 82.50  ? 458 ARG   A CD  1 
ATOM   3340 N  NE  . ARG   A 1 437 ? -14.124 -48.166 -13.976 1.00 85.52  ? 458 ARG   A NE  1 
ATOM   3341 C  CZ  . ARG   A 1 437 ? -13.645 -49.398 -14.070 1.00 87.71  ? 458 ARG   A CZ  1 
ATOM   3342 N  NH1 . ARG   A 1 437 ? -13.937 -50.175 -15.101 1.00 86.90  ? 458 ARG   A NH1 1 
ATOM   3343 N  NH2 . ARG   A 1 437 ? -12.853 -49.862 -13.108 1.00 87.56  ? 458 ARG   A NH2 1 
ATOM   3344 N  N   . VAL   A 1 438 ? -17.732 -44.598 -18.277 1.00 76.75  ? 459 VAL   A N   1 
ATOM   3345 C  CA  . VAL   A 1 438 ? -18.957 -44.643 -19.069 1.00 77.47  ? 459 VAL   A CA  1 
ATOM   3346 C  C   . VAL   A 1 438 ? -18.673 -45.141 -20.482 1.00 78.55  ? 459 VAL   A C   1 
ATOM   3347 O  O   . VAL   A 1 438 ? -19.394 -45.995 -21.011 1.00 78.36  ? 459 VAL   A O   1 
ATOM   3348 C  CB  . VAL   A 1 438 ? -19.628 -43.258 -19.068 1.00 76.34  ? 459 VAL   A CB  1 
ATOM   3349 C  CG1 . VAL   A 1 438 ? -20.508 -43.081 -20.275 1.00 77.98  ? 459 VAL   A CG1 1 
ATOM   3350 C  CG2 . VAL   A 1 438 ? -20.435 -43.069 -17.797 1.00 74.75  ? 459 VAL   A CG2 1 
ATOM   3351 N  N   . LEU   A 1 439 ? -17.612 -44.629 -21.109 1.00 77.99  ? 460 LEU   A N   1 
ATOM   3352 C  CA  . LEU   A 1 439 ? -17.280 -45.052 -22.466 1.00 78.51  ? 460 LEU   A CA  1 
ATOM   3353 C  C   . LEU   A 1 439 ? -16.679 -46.451 -22.509 1.00 78.97  ? 460 LEU   A C   1 
ATOM   3354 O  O   . LEU   A 1 439 ? -16.798 -47.136 -23.532 1.00 77.76  ? 460 LEU   A O   1 
ATOM   3355 C  CB  . LEU   A 1 439 ? -16.323 -44.052 -23.114 1.00 77.28  ? 460 LEU   A CB  1 
ATOM   3356 C  CG  . LEU   A 1 439 ? -16.970 -42.751 -23.585 1.00 74.24  ? 460 LEU   A CG  1 
ATOM   3357 C  CD1 . LEU   A 1 439 ? -15.930 -41.812 -24.166 1.00 73.52  ? 460 LEU   A CD1 1 
ATOM   3358 C  CD2 . LEU   A 1 439 ? -18.058 -43.046 -24.605 1.00 76.64  ? 460 LEU   A CD2 1 
ATOM   3359 N  N   . GLN   A 1 440 ? -16.035 -46.892 -21.425 1.00 78.28  ? 461 GLN   A N   1 
ATOM   3360 C  CA  . GLN   A 1 440 ? -15.459 -48.233 -21.402 1.00 79.03  ? 461 GLN   A CA  1 
ATOM   3361 C  C   . GLN   A 1 440 ? -16.524 -49.310 -21.543 1.00 78.40  ? 461 GLN   A C   1 
ATOM   3362 O  O   . GLN   A 1 440 ? -16.233 -50.409 -22.029 1.00 80.68  ? 461 GLN   A O   1 
ATOM   3363 C  CB  . GLN   A 1 440 ? -14.672 -48.454 -20.108 1.00 76.57  ? 461 GLN   A CB  1 
ATOM   3364 C  CG  . GLN   A 1 440 ? -13.250 -47.933 -20.135 1.00 77.42  ? 461 GLN   A CG  1 
ATOM   3365 C  CD  . GLN   A 1 440 ? -12.493 -48.248 -18.859 1.00 79.83  ? 461 GLN   A CD  1 
ATOM   3366 O  OE1 . GLN   A 1 440 ? -13.063 -48.763 -17.897 1.00 81.37  ? 461 GLN   A OE1 1 
ATOM   3367 N  NE2 . GLN   A 1 440 ? -11.201 -47.942 -18.847 1.00 80.98  ? 461 GLN   A NE2 1 
ATOM   3368 N  N   . ASN   A 1 441 ? -17.757 -49.023 -21.125 1.00 79.18  ? 462 ASN   A N   1 
ATOM   3369 C  CA  . ASN   A 1 441 ? -18.808 -50.027 -21.085 1.00 78.57  ? 462 ASN   A CA  1 
ATOM   3370 C  C   . ASN   A 1 441 ? -19.990 -49.741 -21.999 1.00 78.77  ? 462 ASN   A C   1 
ATOM   3371 O  O   . ASN   A 1 441 ? -20.803 -50.646 -22.219 1.00 80.62  ? 462 ASN   A O   1 
ATOM   3372 C  CB  . ASN   A 1 441 ? -19.327 -50.195 -19.648 1.00 77.85  ? 462 ASN   A CB  1 
ATOM   3373 C  CG  . ASN   A 1 441 ? -18.304 -50.830 -18.727 1.00 79.55  ? 462 ASN   A CG  1 
ATOM   3374 O  OD1 . ASN   A 1 441 ? -18.332 -52.036 -18.489 1.00 82.84  ? 462 ASN   A OD1 1 
ATOM   3375 N  ND2 . ASN   A 1 441 ? -17.392 -50.018 -18.204 1.00 76.34  ? 462 ASN   A ND2 1 
ATOM   3376 N  N   . PHE   A 1 442 ? -20.117 -48.531 -22.540 1.00 78.63  ? 463 PHE   A N   1 
ATOM   3377 C  CA  . PHE   A 1 442 ? -21.302 -48.170 -23.302 1.00 81.33  ? 463 PHE   A CA  1 
ATOM   3378 C  C   . PHE   A 1 442 ? -20.918 -47.381 -24.545 1.00 78.76  ? 463 PHE   A C   1 
ATOM   3379 O  O   . PHE   A 1 442 ? -19.866 -46.740 -24.606 1.00 78.49  ? 463 PHE   A O   1 
ATOM   3380 C  CB  . PHE   A 1 442 ? -22.290 -47.357 -22.456 1.00 82.14  ? 463 PHE   A CB  1 
ATOM   3381 C  CG  . PHE   A 1 442 ? -22.784 -48.084 -21.240 1.00 81.59  ? 463 PHE   A CG  1 
ATOM   3382 C  CD1 . PHE   A 1 442 ? -23.852 -48.962 -21.328 1.00 81.43  ? 463 PHE   A CD1 1 
ATOM   3383 C  CD2 . PHE   A 1 442 ? -22.179 -47.893 -20.009 1.00 81.18  ? 463 PHE   A CD2 1 
ATOM   3384 C  CE1 . PHE   A 1 442 ? -24.310 -49.633 -20.212 1.00 82.62  ? 463 PHE   A CE1 1 
ATOM   3385 C  CE2 . PHE   A 1 442 ? -22.631 -48.563 -18.889 1.00 82.62  ? 463 PHE   A CE2 1 
ATOM   3386 C  CZ  . PHE   A 1 442 ? -23.698 -49.434 -18.991 1.00 83.63  ? 463 PHE   A CZ  1 
ATOM   3387 N  N   . SER   A 1 443 ? -21.798 -47.443 -25.542 1.00 76.92  ? 464 SER   A N   1 
ATOM   3388 C  CA  . SER   A 1 443 ? -21.708 -46.635 -26.750 1.00 80.03  ? 464 SER   A CA  1 
ATOM   3389 C  C   . SER   A 1 443 ? -22.987 -45.821 -26.875 1.00 83.15  ? 464 SER   A C   1 
ATOM   3390 O  O   . SER   A 1 443 ? -24.087 -46.364 -26.729 1.00 83.60  ? 464 SER   A O   1 
ATOM   3391 C  CB  . SER   A 1 443 ? -21.505 -47.509 -27.991 1.00 83.93  ? 464 SER   A CB  1 
ATOM   3392 O  OG  . SER   A 1 443 ? -20.344 -48.312 -27.868 1.00 87.30  ? 464 SER   A OG  1 
ATOM   3393 N  N   . PHE   A 1 444 ? -22.843 -44.528 -27.146 1.00 83.57  ? 465 PHE   A N   1 
ATOM   3394 C  CA  . PHE   A 1 444 ? -23.960 -43.589 -27.130 1.00 81.43  ? 465 PHE   A CA  1 
ATOM   3395 C  C   . PHE   A 1 444 ? -24.255 -43.123 -28.549 1.00 81.97  ? 465 PHE   A C   1 
ATOM   3396 O  O   . PHE   A 1 444 ? -23.368 -42.605 -29.235 1.00 82.47  ? 465 PHE   A O   1 
ATOM   3397 C  CB  . PHE   A 1 444 ? -23.654 -42.399 -26.221 1.00 78.46  ? 465 PHE   A CB  1 
ATOM   3398 C  CG  . PHE   A 1 444 ? -23.589 -42.755 -24.765 1.00 75.55  ? 465 PHE   A CG  1 
ATOM   3399 C  CD1 . PHE   A 1 444 ? -22.499 -43.437 -24.254 1.00 77.37  ? 465 PHE   A CD1 1 
ATOM   3400 C  CD2 . PHE   A 1 444 ? -24.621 -42.411 -23.909 1.00 74.70  ? 465 PHE   A CD2 1 
ATOM   3401 C  CE1 . PHE   A 1 444 ? -22.439 -43.768 -22.920 1.00 78.05  ? 465 PHE   A CE1 1 
ATOM   3402 C  CE2 . PHE   A 1 444 ? -24.564 -42.738 -22.568 1.00 73.07  ? 465 PHE   A CE2 1 
ATOM   3403 C  CZ  . PHE   A 1 444 ? -23.472 -43.417 -22.074 1.00 76.59  ? 465 PHE   A CZ  1 
ATOM   3404 N  N   . LYS   A 1 445 ? -25.502 -43.295 -28.974 1.00 84.60  ? 466 LYS   A N   1 
ATOM   3405 C  CA  . LYS   A 1 445 ? -25.944 -42.955 -30.315 1.00 88.93  ? 466 LYS   A CA  1 
ATOM   3406 C  C   . LYS   A 1 445 ? -27.217 -42.125 -30.251 1.00 88.86  ? 466 LYS   A C   1 
ATOM   3407 O  O   . LYS   A 1 445 ? -27.977 -42.219 -29.281 1.00 88.23  ? 466 LYS   A O   1 
ATOM   3408 C  CB  . LYS   A 1 445 ? -26.194 -44.219 -31.150 1.00 87.52  ? 466 LYS   A CB  1 
ATOM   3409 N  N   . PRO   A 1 446 ? -27.472 -41.302 -31.268 1.00 86.68  ? 467 PRO   A N   1 
ATOM   3410 C  CA  . PRO   A 1 446 ? -28.669 -40.456 -31.254 1.00 88.71  ? 467 PRO   A CA  1 
ATOM   3411 C  C   . PRO   A 1 446 ? -29.953 -41.272 -31.251 1.00 90.57  ? 467 PRO   A C   1 
ATOM   3412 O  O   . PRO   A 1 446 ? -29.981 -42.451 -31.609 1.00 92.24  ? 467 PRO   A O   1 
ATOM   3413 C  CB  . PRO   A 1 446 ? -28.542 -39.638 -32.545 1.00 87.91  ? 467 PRO   A CB  1 
ATOM   3414 C  CG  . PRO   A 1 446 ? -27.091 -39.644 -32.856 1.00 87.06  ? 467 PRO   A CG  1 
ATOM   3415 C  CD  . PRO   A 1 446 ? -26.584 -40.980 -32.399 1.00 86.45  ? 467 PRO   A CD  1 
ATOM   3416 N  N   . CYS   A 1 447 ? -31.029 -40.618 -30.830 1.00 89.84  ? 468 CYS   A N   1 
ATOM   3417 C  CA  . CYS   A 1 447 ? -32.361 -41.199 -30.796 1.00 87.70  ? 468 CYS   A CA  1 
ATOM   3418 C  C   . CYS   A 1 447 ? -33.273 -40.473 -31.773 1.00 89.48  ? 468 CYS   A C   1 
ATOM   3419 O  O   . CYS   A 1 447 ? -32.897 -39.474 -32.393 1.00 89.84  ? 468 CYS   A O   1 
ATOM   3420 C  CB  . CYS   A 1 447 ? -32.947 -41.136 -29.380 1.00 87.95  ? 468 CYS   A CB  1 
ATOM   3421 S  SG  . CYS   A 1 447 ? -32.696 -42.633 -28.408 1.00 94.80  ? 468 CYS   A SG  1 
ATOM   3422 N  N   . LYS   A 1 448 ? -34.488 -41.005 -31.916 1.00 89.71  ? 469 LYS   A N   1 
ATOM   3423 C  CA  . LYS   A 1 448 ? -35.526 -40.266 -32.620 1.00 90.45  ? 469 LYS   A CA  1 
ATOM   3424 C  C   . LYS   A 1 448 ? -35.907 -39.005 -31.860 1.00 90.80  ? 469 LYS   A C   1 
ATOM   3425 O  O   . LYS   A 1 448 ? -36.253 -37.989 -32.474 1.00 90.65  ? 469 LYS   A O   1 
ATOM   3426 C  CB  . LYS   A 1 448 ? -36.754 -41.150 -32.835 1.00 88.17  ? 469 LYS   A CB  1 
ATOM   3427 N  N   . GLU   A 1 449 ? -35.844 -39.050 -30.530 1.00 88.31  ? 470 GLU   A N   1 
ATOM   3428 C  CA  . GLU   A 1 449 ? -36.141 -37.893 -29.699 1.00 88.77  ? 470 GLU   A CA  1 
ATOM   3429 C  C   . GLU   A 1 449 ? -34.957 -36.947 -29.556 1.00 89.78  ? 470 GLU   A C   1 
ATOM   3430 O  O   . GLU   A 1 449 ? -35.101 -35.894 -28.926 1.00 88.86  ? 470 GLU   A O   1 
ATOM   3431 C  CB  . GLU   A 1 449 ? -36.604 -38.351 -28.313 1.00 85.00  ? 470 GLU   A CB  1 
ATOM   3432 N  N   . THR   A 1 450 ? -33.800 -37.291 -30.115 1.00 88.81  ? 471 THR   A N   1 
ATOM   3433 C  CA  . THR   A 1 450 ? -32.617 -36.451 -30.000 1.00 88.30  ? 471 THR   A CA  1 
ATOM   3434 C  C   . THR   A 1 450 ? -32.692 -35.291 -30.987 1.00 87.17  ? 471 THR   A C   1 
ATOM   3435 O  O   . THR   A 1 450 ? -33.041 -35.478 -32.158 1.00 89.34  ? 471 THR   A O   1 
ATOM   3436 C  CB  . THR   A 1 450 ? -31.352 -37.277 -30.242 1.00 89.05  ? 471 THR   A CB  1 
ATOM   3437 O  OG1 . THR   A 1 450 ? -31.292 -38.347 -29.290 1.00 89.04  ? 471 THR   A OG1 1 
ATOM   3438 C  CG2 . THR   A 1 450 ? -30.107 -36.414 -30.097 1.00 86.86  ? 471 THR   A CG2 1 
ATOM   3439 N  N   . GLN   A 1 451 ? -32.362 -34.093 -30.510 1.00 88.98  ? 472 GLN   A N   1 
ATOM   3440 C  CA  . GLN   A 1 451 ? -32.377 -32.882 -31.330 1.00 92.90  ? 472 GLN   A CA  1 
ATOM   3441 C  C   . GLN   A 1 451 ? -31.013 -32.744 -31.996 1.00 91.90  ? 472 GLN   A C   1 
ATOM   3442 O  O   . GLN   A 1 451 ? -30.047 -32.299 -31.372 1.00 87.62  ? 472 GLN   A O   1 
ATOM   3443 C  CB  . GLN   A 1 451 ? -32.712 -31.667 -30.472 1.00 90.86  ? 472 GLN   A CB  1 
ATOM   3444 C  CG  . GLN   A 1 451 ? -32.818 -30.356 -31.232 1.00 93.23  ? 472 GLN   A CG  1 
ATOM   3445 C  CD  . GLN   A 1 451 ? -33.199 -29.196 -30.327 1.00 92.48  ? 472 GLN   A CD  1 
ATOM   3446 O  OE1 . GLN   A 1 451 ? -32.392 -28.731 -29.522 1.00 88.95  ? 472 GLN   A OE1 1 
ATOM   3447 N  NE2 . GLN   A 1 451 ? -34.438 -28.735 -30.446 1.00 93.77  ? 472 GLN   A NE2 1 
ATOM   3448 N  N   . ILE   A 1 452 ? -30.936 -33.126 -33.275 1.00 93.02  ? 473 ILE   A N   1 
ATOM   3449 C  CA  . ILE   A 1 452 ? -29.653 -33.096 -33.980 1.00 93.71  ? 473 ILE   A CA  1 
ATOM   3450 C  C   . ILE   A 1 452 ? -29.078 -31.686 -34.062 1.00 93.21  ? 473 ILE   A C   1 
ATOM   3451 O  O   . ILE   A 1 452 ? -27.892 -31.509 -33.735 1.00 93.09  ? 473 ILE   A O   1 
ATOM   3452 C  CB  . ILE   A 1 452 ? -29.790 -33.776 -35.355 1.00 93.30  ? 473 ILE   A CB  1 
ATOM   3453 C  CG1 . ILE   A 1 452 ? -29.919 -35.292 -35.189 1.00 91.38  ? 473 ILE   A CG1 1 
ATOM   3454 C  CG2 . ILE   A 1 452 ? -28.611 -33.423 -36.250 1.00 91.94  ? 473 ILE   A CG2 1 
ATOM   3455 C  CD1 . ILE   A 1 452 ? -28.733 -35.929 -34.503 1.00 86.96  ? 473 ILE   A CD1 1 
ATOM   3456 N  N   . PRO   A 1 453 ? -29.829 -30.652 -34.485 1.00 92.00  ? 474 PRO   A N   1 
ATOM   3457 C  CA  . PRO   A 1 453 ? -29.308 -29.278 -34.312 1.00 91.03  ? 474 PRO   A CA  1 
ATOM   3458 C  C   . PRO   A 1 453 ? -29.678 -28.723 -32.937 1.00 93.01  ? 474 PRO   A C   1 
ATOM   3459 O  O   . PRO   A 1 453 ? -30.662 -28.003 -32.756 1.00 94.89  ? 474 PRO   A O   1 
ATOM   3460 C  CB  . PRO   A 1 453 ? -29.987 -28.512 -35.449 1.00 91.07  ? 474 PRO   A CB  1 
ATOM   3461 C  CG  . PRO   A 1 453 ? -31.299 -29.196 -35.608 1.00 93.08  ? 474 PRO   A CG  1 
ATOM   3462 C  CD  . PRO   A 1 453 ? -31.080 -30.655 -35.272 1.00 92.33  ? 474 PRO   A CD  1 
ATOM   3463 N  N   . LEU   A 1 454 ? -28.878 -29.092 -31.937 1.00 90.03  ? 475 LEU   A N   1 
ATOM   3464 C  CA  . LEU   A 1 454 ? -29.188 -28.740 -30.557 1.00 85.78  ? 475 LEU   A CA  1 
ATOM   3465 C  C   . LEU   A 1 454 ? -29.287 -27.231 -30.396 1.00 86.53  ? 475 LEU   A C   1 
ATOM   3466 O  O   . LEU   A 1 454 ? -28.400 -26.485 -30.822 1.00 84.99  ? 475 LEU   A O   1 
ATOM   3467 C  CB  . LEU   A 1 454 ? -28.127 -29.303 -29.613 1.00 84.32  ? 475 LEU   A CB  1 
ATOM   3468 C  CG  . LEU   A 1 454 ? -28.417 -29.124 -28.122 1.00 81.11  ? 475 LEU   A CG  1 
ATOM   3469 C  CD1 . LEU   A 1 454 ? -29.790 -29.682 -27.773 1.00 81.21  ? 475 LEU   A CD1 1 
ATOM   3470 C  CD2 . LEU   A 1 454 ? -27.338 -29.780 -27.273 1.00 75.99  ? 475 LEU   A CD2 1 
ATOM   3471 N  N   . LYS   A 1 455 ? -30.375 -26.787 -29.776 1.00 86.61  ? 476 LYS   A N   1 
ATOM   3472 C  CA  . LYS   A 1 455 ? -30.679 -25.373 -29.610 1.00 82.99  ? 476 LYS   A CA  1 
ATOM   3473 C  C   . LYS   A 1 455 ? -30.554 -25.002 -28.139 1.00 79.38  ? 476 LYS   A C   1 
ATOM   3474 O  O   . LYS   A 1 455 ? -31.077 -25.707 -27.270 1.00 77.25  ? 476 LYS   A O   1 
ATOM   3475 C  CB  . LYS   A 1 455 ? -32.081 -25.057 -30.134 1.00 86.53  ? 476 LYS   A CB  1 
ATOM   3476 C  CG  . LYS   A 1 455 ? -32.227 -25.248 -31.638 1.00 88.27  ? 476 LYS   A CG  1 
ATOM   3477 C  CD  . LYS   A 1 455 ? -33.565 -25.872 -32.003 1.00 92.07  ? 476 LYS   A CD  1 
ATOM   3478 C  CE  . LYS   A 1 455 ? -34.728 -24.958 -31.661 1.00 93.67  ? 476 LYS   A CE  1 
ATOM   3479 N  NZ  . LYS   A 1 455 ? -36.031 -25.581 -32.025 1.00 93.80  ? 476 LYS   A NZ  1 
ATOM   3480 N  N   . LEU   A 1 456 ? -29.850 -23.908 -27.869 1.00 77.73  ? 477 LEU   A N   1 
ATOM   3481 C  CA  . LEU   A 1 456 ? -29.629 -23.459 -26.506 1.00 73.67  ? 477 LEU   A CA  1 
ATOM   3482 C  C   . LEU   A 1 456 ? -30.854 -22.725 -25.969 1.00 71.78  ? 477 LEU   A C   1 
ATOM   3483 O  O   . LEU   A 1 456 ? -31.691 -22.217 -26.719 1.00 68.93  ? 477 LEU   A O   1 
ATOM   3484 C  CB  . LEU   A 1 456 ? -28.403 -22.551 -26.436 1.00 68.67  ? 477 LEU   A CB  1 
ATOM   3485 C  CG  . LEU   A 1 456 ? -27.068 -23.234 -26.729 1.00 65.90  ? 477 LEU   A CG  1 
ATOM   3486 C  CD1 . LEU   A 1 456 ? -25.990 -22.204 -27.008 1.00 67.94  ? 477 LEU   A CD1 1 
ATOM   3487 C  CD2 . LEU   A 1 456 ? -26.668 -24.128 -25.566 1.00 68.43  ? 477 LEU   A CD2 1 
ATOM   3488 N  N   . SER   A 1 457 ? -30.950 -22.680 -24.643 1.00 72.61  ? 478 SER   A N   1 
ATOM   3489 C  CA  . SER   A 1 457 ? -32.046 -21.980 -23.996 1.00 69.06  ? 478 SER   A CA  1 
ATOM   3490 C  C   . SER   A 1 457 ? -31.894 -20.471 -24.165 1.00 67.53  ? 478 SER   A C   1 
ATOM   3491 O  O   . SER   A 1 457 ? -30.798 -19.946 -24.384 1.00 70.05  ? 478 SER   A O   1 
ATOM   3492 C  CB  . SER   A 1 457 ? -32.108 -22.338 -22.510 1.00 69.63  ? 478 SER   A CB  1 
ATOM   3493 O  OG  . SER   A 1 457 ? -33.117 -21.595 -21.848 1.00 65.73  ? 478 SER   A OG  1 
ATOM   3494 N  N   . LEU   A 1 458 ? -33.021 -19.770 -24.059 1.00 67.10  ? 479 LEU   A N   1 
ATOM   3495 C  CA  . LEU   A 1 458 ? -33.047 -18.316 -24.138 1.00 69.09  ? 479 LEU   A CA  1 
ATOM   3496 C  C   . LEU   A 1 458 ? -32.976 -17.652 -22.769 1.00 69.18  ? 479 LEU   A C   1 
ATOM   3497 O  O   . LEU   A 1 458 ? -33.058 -16.423 -22.685 1.00 66.36  ? 479 LEU   A O   1 
ATOM   3498 C  CB  . LEU   A 1 458 ? -34.303 -17.849 -24.882 1.00 69.32  ? 479 LEU   A CB  1 
ATOM   3499 C  CG  . LEU   A 1 458 ? -34.447 -18.362 -26.316 1.00 69.86  ? 479 LEU   A CG  1 
ATOM   3500 C  CD1 . LEU   A 1 458 ? -35.695 -17.791 -26.975 1.00 68.89  ? 479 LEU   A CD1 1 
ATOM   3501 C  CD2 . LEU   A 1 458 ? -33.204 -18.035 -27.131 1.00 70.20  ? 479 LEU   A CD2 1 
ATOM   3502 N  N   . GLY   A 1 459 ? -32.825 -18.430 -21.701 1.00 67.29  ? 480 GLY   A N   1 
ATOM   3503 C  CA  . GLY   A 1 459 ? -32.705 -17.900 -20.361 1.00 59.96  ? 480 GLY   A CA  1 
ATOM   3504 C  C   . GLY   A 1 459 ? -31.276 -17.543 -20.012 1.00 59.03  ? 480 GLY   A C   1 
ATOM   3505 O  O   . GLY   A 1 459 ? -30.416 -17.373 -20.880 1.00 61.49  ? 480 GLY   A O   1 
ATOM   3506 N  N   . GLY   A 1 460 ? -31.021 -17.443 -18.710 1.00 59.86  ? 481 GLY   A N   1 
ATOM   3507 C  CA  . GLY   A 1 460 ? -29.722 -17.023 -18.224 1.00 60.40  ? 481 GLY   A CA  1 
ATOM   3508 C  C   . GLY   A 1 460 ? -28.782 -18.159 -17.875 1.00 61.37  ? 481 GLY   A C   1 
ATOM   3509 O  O   . GLY   A 1 460 ? -27.830 -17.968 -17.113 1.00 62.95  ? 481 GLY   A O   1 
ATOM   3510 N  N   . LEU   A 1 461 ? -29.044 -19.347 -18.412 1.00 60.78  ? 482 LEU   A N   1 
ATOM   3511 C  CA  . LEU   A 1 461 ? -28.187 -20.505 -18.206 1.00 61.62  ? 482 LEU   A CA  1 
ATOM   3512 C  C   . LEU   A 1 461 ? -27.847 -21.129 -19.550 1.00 62.23  ? 482 LEU   A C   1 
ATOM   3513 O  O   . LEU   A 1 461 ? -28.706 -21.237 -20.430 1.00 62.75  ? 482 LEU   A O   1 
ATOM   3514 C  CB  . LEU   A 1 461 ? -28.856 -21.542 -17.299 1.00 63.83  ? 482 LEU   A CB  1 
ATOM   3515 C  CG  . LEU   A 1 461 ? -29.046 -21.104 -15.846 1.00 64.76  ? 482 LEU   A CG  1 
ATOM   3516 C  CD1 . LEU   A 1 461 ? -29.777 -22.171 -15.047 1.00 66.18  ? 482 LEU   A CD1 1 
ATOM   3517 C  CD2 . LEU   A 1 461 ? -27.701 -20.780 -15.213 1.00 68.83  ? 482 LEU   A CD2 1 
ATOM   3518 N  N   . LEU   A 1 462 ? -26.589 -21.537 -19.704 1.00 62.69  ? 483 LEU   A N   1 
ATOM   3519 C  CA  . LEU   A 1 462 ? -26.137 -22.172 -20.939 1.00 62.31  ? 483 LEU   A CA  1 
ATOM   3520 C  C   . LEU   A 1 462 ? -26.512 -23.645 -20.876 1.00 63.01  ? 483 LEU   A C   1 
ATOM   3521 O  O   . LEU   A 1 462 ? -25.724 -24.498 -20.465 1.00 62.84  ? 483 LEU   A O   1 
ATOM   3522 C  CB  . LEU   A 1 462 ? -24.640 -21.982 -21.134 1.00 64.85  ? 483 LEU   A CB  1 
ATOM   3523 C  CG  . LEU   A 1 462 ? -24.144 -22.396 -22.517 1.00 64.80  ? 483 LEU   A CG  1 
ATOM   3524 C  CD1 . LEU   A 1 462 ? -24.901 -21.634 -23.589 1.00 64.13  ? 483 LEU   A CD1 1 
ATOM   3525 C  CD2 . LEU   A 1 462 ? -22.660 -22.144 -22.635 1.00 63.57  ? 483 LEU   A CD2 1 
ATOM   3526 N  N   . GLN   A 1 463 ? -27.734 -23.945 -21.290 1.00 66.39  ? 484 GLN   A N   1 
ATOM   3527 C  CA  . GLN   A 1 463 ? -28.286 -25.288 -21.238 1.00 66.51  ? 484 GLN   A CA  1 
ATOM   3528 C  C   . GLN   A 1 463 ? -29.097 -25.540 -22.500 1.00 67.05  ? 484 GLN   A C   1 
ATOM   3529 O  O   . GLN   A 1 463 ? -29.549 -24.593 -23.152 1.00 64.80  ? 484 GLN   A O   1 
ATOM   3530 C  CB  . GLN   A 1 463 ? -29.164 -25.480 -19.993 1.00 65.56  ? 484 GLN   A CB  1 
ATOM   3531 C  CG  . GLN   A 1 463 ? -30.368 -24.558 -19.933 1.00 64.73  ? 484 GLN   A CG  1 
ATOM   3532 C  CD  . GLN   A 1 463 ? -31.208 -24.778 -18.691 1.00 63.89  ? 484 GLN   A CD  1 
ATOM   3533 O  OE1 . GLN   A 1 463 ? -30.705 -25.216 -17.655 1.00 64.20  ? 484 GLN   A OE1 1 
ATOM   3534 N  NE2 . GLN   A 1 463 ? -32.497 -24.478 -18.789 1.00 67.59  ? 484 GLN   A NE2 1 
ATOM   3535 N  N   . PRO   A 1 464 ? -29.281 -26.804 -22.876 1.00 72.42  ? 485 PRO   A N   1 
ATOM   3536 C  CA  . PRO   A 1 464 ? -30.103 -27.105 -24.053 1.00 75.27  ? 485 PRO   A CA  1 
ATOM   3537 C  C   . PRO   A 1 464 ? -31.552 -26.699 -23.841 1.00 78.14  ? 485 PRO   A C   1 
ATOM   3538 O  O   . PRO   A 1 464 ? -32.063 -26.694 -22.718 1.00 77.75  ? 485 PRO   A O   1 
ATOM   3539 C  CB  . PRO   A 1 464 ? -29.970 -28.626 -24.203 1.00 72.91  ? 485 PRO   A CB  1 
ATOM   3540 C  CG  . PRO   A 1 464 ? -28.744 -28.989 -23.425 1.00 71.82  ? 485 PRO   A CG  1 
ATOM   3541 C  CD  . PRO   A 1 464 ? -28.688 -28.019 -22.293 1.00 70.17  ? 485 PRO   A CD  1 
ATOM   3542 N  N   . GLU   A 1 465 ? -32.211 -26.341 -24.944 1.00 78.23  ? 486 GLU   A N   1 
ATOM   3543 C  CA  . GLU   A 1 465 ? -33.629 -26.003 -24.910 1.00 81.17  ? 486 GLU   A CA  1 
ATOM   3544 C  C   . GLU   A 1 465 ? -34.441 -27.185 -24.398 1.00 83.74  ? 486 GLU   A C   1 
ATOM   3545 O  O   . GLU   A 1 465 ? -35.053 -27.115 -23.328 1.00 84.38  ? 486 GLU   A O   1 
ATOM   3546 C  CB  . GLU   A 1 465 ? -34.109 -25.587 -26.300 1.00 83.36  ? 486 GLU   A CB  1 
ATOM   3547 C  CG  . GLU   A 1 465 ? -35.574 -25.191 -26.368 1.00 87.56  ? 486 GLU   A CG  1 
ATOM   3548 C  CD  . GLU   A 1 465 ? -36.123 -25.249 -27.779 1.00 95.90  ? 486 GLU   A CD  1 
ATOM   3549 O  OE1 . GLU   A 1 465 ? -35.798 -26.217 -28.498 1.00 94.37  ? 486 GLU   A OE1 1 
ATOM   3550 O  OE2 . GLU   A 1 465 ? -36.869 -24.325 -28.171 1.00 102.36 ? 486 GLU   A OE2 1 
ATOM   3551 N  N   . LYS   A 1 466 ? -34.439 -28.279 -25.152 1.00 82.09  ? 487 LYS   A N   1 
ATOM   3552 C  CA  . LYS   A 1 466 ? -35.042 -29.520 -24.698 1.00 79.91  ? 487 LYS   A CA  1 
ATOM   3553 C  C   . LYS   A 1 466 ? -33.968 -30.444 -24.136 1.00 80.67  ? 487 LYS   A C   1 
ATOM   3554 O  O   . LYS   A 1 466 ? -32.829 -30.439 -24.613 1.00 81.59  ? 487 LYS   A O   1 
ATOM   3555 C  CB  . LYS   A 1 466 ? -35.775 -30.220 -25.847 1.00 80.95  ? 487 LYS   A CB  1 
ATOM   3556 N  N   . PRO   A 1 467 ? -34.294 -31.241 -23.118 1.00 80.73  ? 488 PRO   A N   1 
ATOM   3557 C  CA  . PRO   A 1 467 ? -33.273 -32.101 -22.507 1.00 81.14  ? 488 PRO   A CA  1 
ATOM   3558 C  C   . PRO   A 1 467 ? -32.694 -33.080 -23.517 1.00 84.89  ? 488 PRO   A C   1 
ATOM   3559 O  O   . PRO   A 1 467 ? -33.397 -33.590 -24.391 1.00 85.51  ? 488 PRO   A O   1 
ATOM   3560 C  CB  . PRO   A 1 467 ? -34.038 -32.822 -21.390 1.00 79.43  ? 488 PRO   A CB  1 
ATOM   3561 C  CG  . PRO   A 1 467 ? -35.470 -32.763 -21.813 1.00 82.96  ? 488 PRO   A CG  1 
ATOM   3562 C  CD  . PRO   A 1 467 ? -35.621 -31.445 -22.513 1.00 82.11  ? 488 PRO   A CD  1 
ATOM   3563 N  N   . VAL   A 1 468 ? -31.395 -33.332 -23.393 1.00 83.79  ? 489 VAL   A N   1 
ATOM   3564 C  CA  . VAL   A 1 468 ? -30.693 -34.206 -24.327 1.00 80.89  ? 489 VAL   A CA  1 
ATOM   3565 C  C   . VAL   A 1 468 ? -30.973 -35.656 -23.954 1.00 82.50  ? 489 VAL   A C   1 
ATOM   3566 O  O   . VAL   A 1 468 ? -30.747 -36.072 -22.812 1.00 79.35  ? 489 VAL   A O   1 
ATOM   3567 C  CB  . VAL   A 1 468 ? -29.186 -33.917 -24.332 1.00 79.75  ? 489 VAL   A CB  1 
ATOM   3568 C  CG1 . VAL   A 1 468 ? -28.476 -34.840 -25.309 1.00 80.47  ? 489 VAL   A CG1 1 
ATOM   3569 C  CG2 . VAL   A 1 468 ? -28.926 -32.461 -24.690 1.00 80.56  ? 489 VAL   A CG2 1 
ATOM   3570 N  N   . VAL   A 1 469 ? -31.463 -36.428 -24.920 1.00 85.09  ? 490 VAL   A N   1 
ATOM   3571 C  CA  . VAL   A 1 469 ? -31.750 -37.845 -24.743 1.00 84.51  ? 490 VAL   A CA  1 
ATOM   3572 C  C   . VAL   A 1 469 ? -31.010 -38.624 -25.821 1.00 85.92  ? 490 VAL   A C   1 
ATOM   3573 O  O   . VAL   A 1 469 ? -30.972 -38.209 -26.985 1.00 85.75  ? 490 VAL   A O   1 
ATOM   3574 C  CB  . VAL   A 1 469 ? -33.265 -38.136 -24.792 1.00 83.77  ? 490 VAL   A CB  1 
ATOM   3575 C  CG1 . VAL   A 1 469 ? -33.930 -37.687 -23.499 1.00 81.04  ? 490 VAL   A CG1 1 
ATOM   3576 C  CG2 . VAL   A 1 469 ? -33.901 -37.442 -25.985 1.00 85.44  ? 490 VAL   A CG2 1 
ATOM   3577 N  N   . LEU   A 1 470 ? -30.413 -39.748 -25.429 1.00 85.35  ? 491 LEU   A N   1 
ATOM   3578 C  CA  . LEU   A 1 470 ? -29.607 -40.553 -26.334 1.00 85.89  ? 491 LEU   A CA  1 
ATOM   3579 C  C   . LEU   A 1 470 ? -29.868 -42.029 -26.076 1.00 88.54  ? 491 LEU   A C   1 
ATOM   3580 O  O   . LEU   A 1 470 ? -30.420 -42.415 -25.043 1.00 88.34  ? 491 LEU   A O   1 
ATOM   3581 C  CB  . LEU   A 1 470 ? -28.110 -40.252 -26.179 1.00 82.35  ? 491 LEU   A CB  1 
ATOM   3582 C  CG  . LEU   A 1 470 ? -27.615 -38.854 -26.550 1.00 79.06  ? 491 LEU   A CG  1 
ATOM   3583 C  CD1 . LEU   A 1 470 ? -26.139 -38.713 -26.214 1.00 75.24  ? 491 LEU   A CD1 1 
ATOM   3584 C  CD2 . LEU   A 1 470 ? -27.859 -38.568 -28.023 1.00 81.17  ? 491 LEU   A CD2 1 
ATOM   3585 N  N   . LYS   A 1 471 ? -29.460 -42.855 -27.038 1.00 88.10  ? 492 LYS   A N   1 
ATOM   3586 C  CA  . LYS   A 1 471 ? -29.591 -44.302 -26.932 1.00 85.80  ? 492 LYS   A CA  1 
ATOM   3587 C  C   . LYS   A 1 471 ? -28.295 -44.894 -26.393 1.00 87.30  ? 492 LYS   A C   1 
ATOM   3588 O  O   . LYS   A 1 471 ? -27.206 -44.549 -26.861 1.00 87.05  ? 492 LYS   A O   1 
ATOM   3589 C  CB  . LYS   A 1 471 ? -29.931 -44.914 -28.291 1.00 87.47  ? 492 LYS   A CB  1 
ATOM   3590 N  N   . VAL   A 1 472 ? -28.419 -45.784 -25.411 1.00 86.35  ? 493 VAL   A N   1 
ATOM   3591 C  CA  . VAL   A 1 472 ? -27.276 -46.370 -24.722 1.00 86.22  ? 493 VAL   A CA  1 
ATOM   3592 C  C   . VAL   A 1 472 ? -27.269 -47.869 -24.981 1.00 91.48  ? 493 VAL   A C   1 
ATOM   3593 O  O   . VAL   A 1 472 ? -28.271 -48.551 -24.740 1.00 92.25  ? 493 VAL   A O   1 
ATOM   3594 C  CB  . VAL   A 1 472 ? -27.315 -46.077 -23.211 1.00 85.29  ? 493 VAL   A CB  1 
ATOM   3595 C  CG1 . VAL   A 1 472 ? -26.043 -46.562 -22.546 1.00 85.05  ? 493 VAL   A CG1 1 
ATOM   3596 C  CG2 . VAL   A 1 472 ? -27.518 -44.590 -22.967 1.00 84.93  ? 493 VAL   A CG2 1 
ATOM   3597 N  N   . GLU   A 1 473 ? -26.138 -48.377 -25.468 1.00 91.29  ? 494 GLU   A N   1 
ATOM   3598 C  CA  . GLU   A 1 473 ? -25.963 -49.794 -25.754 1.00 89.11  ? 494 GLU   A CA  1 
ATOM   3599 C  C   . GLU   A 1 473 ? -24.678 -50.285 -25.104 1.00 86.59  ? 494 GLU   A C   1 
ATOM   3600 O  O   . GLU   A 1 473 ? -23.677 -49.564 -25.066 1.00 86.74  ? 494 GLU   A O   1 
ATOM   3601 C  CB  . GLU   A 1 473 ? -25.922 -50.056 -27.265 1.00 89.43  ? 494 GLU   A CB  1 
ATOM   3602 C  CG  . GLU   A 1 473 ? -27.199 -49.674 -27.999 1.00 94.46  ? 494 GLU   A CG  1 
ATOM   3603 C  CD  . GLU   A 1 473 ? -27.072 -49.808 -29.505 1.00 101.90 ? 494 GLU   A CD  1 
ATOM   3604 O  OE1 . GLU   A 1 473 ? -25.929 -49.879 -30.004 1.00 102.74 ? 494 GLU   A OE1 1 
ATOM   3605 O  OE2 . GLU   A 1 473 ? -28.117 -49.844 -30.189 1.00 103.19 ? 494 GLU   A OE2 1 
ATOM   3606 N  N   . SER   A 1 474 ? -24.712 -51.515 -24.596 1.00 85.78  ? 495 SER   A N   1 
ATOM   3607 C  CA  . SER   A 1 474 ? -23.552 -52.095 -23.932 1.00 85.09  ? 495 SER   A CA  1 
ATOM   3608 C  C   . SER   A 1 474 ? -22.592 -52.675 -24.963 1.00 84.71  ? 495 SER   A C   1 
ATOM   3609 O  O   . SER   A 1 474 ? -23.009 -53.375 -25.891 1.00 87.59  ? 495 SER   A O   1 
ATOM   3610 C  CB  . SER   A 1 474 ? -23.990 -53.174 -22.943 1.00 87.38  ? 495 SER   A CB  1 
ATOM   3611 O  OG  . SER   A 1 474 ? -24.765 -54.172 -23.585 1.00 96.48  ? 495 SER   A OG  1 
ATOM   3612 N  N   . ARG   A 1 475 ? -21.305 -52.382 -24.797 1.00 82.77  ? 496 ARG   A N   1 
ATOM   3613 C  CA  . ARG   A 1 475 ? -20.283 -52.823 -25.740 1.00 85.37  ? 496 ARG   A CA  1 
ATOM   3614 C  C   . ARG   A 1 475 ? -20.016 -54.320 -25.619 1.00 84.37  ? 496 ARG   A C   1 
ATOM   3615 O  O   . ARG   A 1 475 ? -19.498 -54.790 -24.606 1.00 83.23  ? 496 ARG   A O   1 
ATOM   3616 C  CB  . ARG   A 1 475 ? -18.986 -52.040 -25.523 1.00 82.45  ? 496 ARG   A CB  1 
ATOM   3617 C  CG  . ARG   A 1 475 ? -19.111 -50.550 -25.801 1.00 77.92  ? 496 ARG   A CG  1 
ATOM   3618 C  CD  . ARG   A 1 475 ? -17.819 -49.811 -25.483 1.00 76.14  ? 496 ARG   A CD  1 
ATOM   3619 N  NE  . ARG   A 1 475 ? -16.699 -50.265 -26.299 1.00 78.12  ? 496 ARG   A NE  1 
ATOM   3620 C  CZ  . ARG   A 1 475 ? -15.457 -49.816 -26.176 1.00 76.63  ? 496 ARG   A CZ  1 
ATOM   3621 N  NH1 . ARG   A 1 475 ? -15.140 -48.899 -25.277 1.00 77.22  ? 496 ARG   A NH1 1 
ATOM   3622 N  NH2 . ARG   A 1 475 ? -14.509 -50.301 -26.973 1.00 75.52  ? 496 ARG   A NH2 1 
HETATM 3623 C  CHA . HEM   B 2 .   ? -15.159 -19.638 -10.163 1.00 54.63  ? 601 HEM   A CHA 1 
HETATM 3624 C  CHB . HEM   B 2 .   ? -16.019 -22.311 -14.187 1.00 53.97  ? 601 HEM   A CHB 1 
HETATM 3625 C  CHC . HEM   B 2 .   ? -16.582 -26.175 -11.308 1.00 52.30  ? 601 HEM   A CHC 1 
HETATM 3626 C  CHD . HEM   B 2 .   ? -15.371 -23.632 -7.390  1.00 54.24  ? 601 HEM   A CHD 1 
HETATM 3627 C  C1A . HEM   B 2 .   ? -15.360 -20.024 -11.480 1.00 54.07  ? 601 HEM   A C1A 1 
HETATM 3628 C  C2A . HEM   B 2 .   ? -15.334 -19.141 -12.629 1.00 52.56  ? 601 HEM   A C2A 1 
HETATM 3629 C  C3A . HEM   B 2 .   ? -15.566 -19.882 -13.722 1.00 50.76  ? 601 HEM   A C3A 1 
HETATM 3630 C  C4A . HEM   B 2 .   ? -15.754 -21.256 -13.318 1.00 51.52  ? 601 HEM   A C4A 1 
HETATM 3631 C  CMA . HEM   B 2 .   ? -15.636 -19.395 -15.176 1.00 51.05  ? 601 HEM   A CMA 1 
HETATM 3632 C  CAA . HEM   B 2 .   ? -15.069 -17.614 -12.618 1.00 54.30  ? 601 HEM   A CAA 1 
HETATM 3633 C  CBA . HEM   B 2 .   ? -13.584 -17.334 -12.801 1.00 58.31  ? 601 HEM   A CBA 1 
HETATM 3634 C  CGA . HEM   B 2 .   ? -13.362 -15.909 -13.200 1.00 61.09  ? 601 HEM   A CGA 1 
HETATM 3635 O  O1A . HEM   B 2 .   ? -14.236 -15.056 -12.839 1.00 58.98  ? 601 HEM   A O1A 1 
HETATM 3636 O  O2A . HEM   B 2 .   ? -12.210 -15.538 -13.562 1.00 63.02  ? 601 HEM   A O2A 1 
HETATM 3637 C  C1B . HEM   B 2 .   ? -16.272 -23.598 -13.759 1.00 55.94  ? 601 HEM   A C1B 1 
HETATM 3638 C  C2B . HEM   B 2 .   ? -16.644 -24.733 -14.595 1.00 57.60  ? 601 HEM   A C2B 1 
HETATM 3639 C  C3B . HEM   B 2 .   ? -16.803 -25.804 -13.809 1.00 55.60  ? 601 HEM   A C3B 1 
HETATM 3640 C  C4B . HEM   B 2 .   ? -16.532 -25.377 -12.432 1.00 53.85  ? 601 HEM   A C4B 1 
HETATM 3641 C  CMB . HEM   B 2 .   ? -16.814 -24.669 -16.138 1.00 54.81  ? 601 HEM   A CMB 1 
HETATM 3642 C  CAB . HEM   B 2 .   ? -17.190 -27.231 -14.255 1.00 57.20  ? 601 HEM   A CAB 1 
HETATM 3643 C  CBB . HEM   B 2 .   ? -17.694 -28.230 -13.522 1.00 64.27  ? 601 HEM   A CBB 1 
HETATM 3644 C  C1C . HEM   B 2 .   ? -16.297 -25.836 -10.013 1.00 53.95  ? 601 HEM   A C1C 1 
HETATM 3645 C  C2C . HEM   B 2 .   ? -16.321 -26.740 -8.887  1.00 52.47  ? 601 HEM   A C2C 1 
HETATM 3646 C  C3C . HEM   B 2 .   ? -15.983 -26.046 -7.787  1.00 52.94  ? 601 HEM   A C3C 1 
HETATM 3647 C  C4C . HEM   B 2 .   ? -15.738 -24.690 -8.195  1.00 56.50  ? 601 HEM   A C4C 1 
HETATM 3648 C  CMC . HEM   B 2 .   ? -16.675 -28.228 -8.996  1.00 57.84  ? 601 HEM   A CMC 1 
HETATM 3649 C  CAC . HEM   B 2 .   ? -15.860 -26.518 -6.326  1.00 54.29  ? 601 HEM   A CAC 1 
HETATM 3650 C  CBC . HEM   B 2 .   ? -15.002 -27.456 -5.926  1.00 58.20  ? 601 HEM   A CBC 1 
HETATM 3651 C  C1D . HEM   B 2 .   ? -15.236 -22.334 -7.821  1.00 54.49  ? 601 HEM   A C1D 1 
HETATM 3652 C  C2D . HEM   B 2 .   ? -14.943 -21.205 -6.978  1.00 56.86  ? 601 HEM   A C2D 1 
HETATM 3653 C  C3D . HEM   B 2 .   ? -14.877 -20.100 -7.715  1.00 57.18  ? 601 HEM   A C3D 1 
HETATM 3654 C  C4D . HEM   B 2 .   ? -15.135 -20.485 -9.093  1.00 55.73  ? 601 HEM   A C4D 1 
HETATM 3655 C  CMD . HEM   B 2 .   ? -14.748 -21.330 -5.454  1.00 55.58  ? 601 HEM   A CMD 1 
HETATM 3656 C  CAD . HEM   B 2 .   ? -14.592 -18.676 -7.215  1.00 60.25  ? 601 HEM   A CAD 1 
HETATM 3657 C  CBD . HEM   B 2 .   ? -13.089 -18.443 -7.149  1.00 63.45  ? 601 HEM   A CBD 1 
HETATM 3658 C  CGD . HEM   B 2 .   ? -12.761 -17.196 -6.356  1.00 65.03  ? 601 HEM   A CGD 1 
HETATM 3659 O  O1D . HEM   B 2 .   ? -13.711 -16.399 -6.123  1.00 65.16  ? 601 HEM   A O1D 1 
HETATM 3660 O  O2D . HEM   B 2 .   ? -11.559 -16.938 -6.043  1.00 65.96  ? 601 HEM   A O2D 1 
HETATM 3661 N  NA  . HEM   B 2 .   ? -15.642 -21.301 -11.935 1.00 50.26  ? 601 HEM   A NA  1 
HETATM 3662 N  NB  . HEM   B 2 .   ? -16.217 -24.033 -12.453 1.00 54.87  ? 601 HEM   A NB  1 
HETATM 3663 N  NC  . HEM   B 2 .   ? -15.941 -24.594 -9.546  1.00 55.05  ? 601 HEM   A NC  1 
HETATM 3664 N  ND  . HEM   B 2 .   ? -15.348 -21.860 -9.112  1.00 54.58  ? 601 HEM   A ND  1 
HETATM 3665 FE FE  . HEM   B 2 .   ? -15.760 -22.973 -10.774 1.00 50.02  ? 601 HEM   A FE  1 
HETATM 3666 C  C10 . A1ASS C 3 .   ? -22.310 -21.845 -14.082 1.00 66.88  ? 602 A1ASS A C10 1 
HETATM 3667 C  C15 . A1ASS C 3 .   ? -20.375 -20.401 -7.709  1.00 61.51  ? 602 A1ASS A C15 1 
HETATM 3668 C  C21 . A1ASS C 3 .   ? -18.382 -21.566 -9.686  1.00 57.67  ? 602 A1ASS A C21 1 
HETATM 3669 C  C02 . A1ASS C 3 .   ? -22.714 -17.575 -6.838  1.00 63.01  ? 602 A1ASS A C02 1 
HETATM 3670 C  C04 . A1ASS C 3 .   ? -21.937 -18.612 -7.616  1.00 64.13  ? 602 A1ASS A C04 1 
HETATM 3671 C  C05 . A1ASS C 3 .   ? -22.113 -18.687 -8.983  1.00 64.44  ? 602 A1ASS A C05 1 
HETATM 3672 C  C06 . A1ASS C 3 .   ? -21.429 -19.618 -9.781  1.00 62.41  ? 602 A1ASS A C06 1 
HETATM 3673 C  C08 . A1ASS C 3 .   ? -22.570 -20.495 -11.853 1.00 64.59  ? 602 A1ASS A C08 1 
HETATM 3674 C  C09 . A1ASS C 3 .   ? -22.755 -20.517 -13.377 1.00 67.17  ? 602 A1ASS A C09 1 
HETATM 3675 C  C11 . A1ASS C 3 .   ? -23.658 -21.915 -14.819 1.00 69.11  ? 602 A1ASS A C11 1 
HETATM 3676 C  C12 . A1ASS C 3 .   ? -24.202 -20.841 -13.862 1.00 69.97  ? 602 A1ASS A C12 1 
HETATM 3677 C  C14 . A1ASS C 3 .   ? -21.069 -19.465 -6.957  1.00 63.23  ? 602 A1ASS A C14 1 
HETATM 3678 C  C16 . A1ASS C 3 .   ? -20.547 -20.496 -9.100  1.00 61.85  ? 602 A1ASS A C16 1 
HETATM 3679 C  C18 . A1ASS C 3 .   ? -20.187 -22.524 -10.615 1.00 61.98  ? 602 A1ASS A C18 1 
HETATM 3680 C  C19 . A1ASS C 3 .   ? -19.035 -23.189 -11.002 1.00 58.77  ? 602 A1ASS A C19 1 
HETATM 3681 F  F01 . A1ASS C 3 .   ? -22.858 -16.422 -7.542  1.00 64.72  ? 602 A1ASS A F01 1 
HETATM 3682 F  F03 . A1ASS C 3 .   ? -22.152 -17.148 -5.668  1.00 62.21  ? 602 A1ASS A F03 1 
HETATM 3683 F  F22 . A1ASS C 3 .   ? -23.969 -17.903 -6.479  1.00 63.65  ? 602 A1ASS A F22 1 
HETATM 3684 N  N07 . A1ASS C 3 .   ? -21.634 -19.671 -11.179 1.00 63.99  ? 602 A1ASS A N07 1 
HETATM 3685 N  N17 . A1ASS C 3 .   ? -19.777 -21.480 -9.766  1.00 60.42  ? 602 A1ASS A N17 1 
HETATM 3686 N  N20 . A1ASS C 3 .   ? -17.921 -22.591 -10.417 1.00 57.70  ? 602 A1ASS A N20 1 
HETATM 3687 O  O13 . A1ASS C 3 .   ? -23.276 -21.240 -11.178 1.00 67.44  ? 602 A1ASS A O13 1 
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