data_9EPF
# 
_entry.id   9EPF 
# 
_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   9EPF         pdb_00009epf 10.2210/pdb9epf/pdb 
WWPDB D_1292137002 ?            ?                   
EMDB  EMD-19878    ?            ?                   
# 
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 2025-03-26 ? 
2 'EM metadata'     1 0 2025-03-26 ? 
3 'Additional map'  1 0 2025-03-26 1 
4 FSC               1 0 2025-03-26 ? 
5 'Half map'        1 0 2025-03-26 1 
6 'Half map'        1 0 2025-03-26 2 
7 Image             1 0 2025-03-26 ? 
8 'Primary map'     1 0 2025-03-26 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EPF 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Human Picobirnavirus CP VLP' 
_pdbx_database_related.db_id          EMD-19878 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jrcaston@cnb.csic.es 
_pdbx_contact_author.name_first         Jose 
_pdbx_contact_author.name_last          Caston 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2350-9048 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodriguez-Espinosa, M.J.' 1 0000-0003-1916-3195 
'Novoa, G.'                2 0000-0002-3018-9743 
'Martinez-Romero, J.M.'    3 ?                   
'de Pablo, P.J.'           4 0000-0003-2386-3186 
'Caston, J.R.'             5 0000-0003-2350-9048 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Human Picobirnavirus CP VLP' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodriguez-Espinosa, M.J.' 1 0000-0003-1916-3195 
primary 'Novoa, G.'                2 0000-0002-3018-9743 
primary 'Martinez-Romero, J.M.'    3 ?                   
primary 'de Pablo, P.J.'           4 0000-0003-2386-3186 
primary 'Caston, J.R.'             5 0000-0003-2350-9048 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Capsid protein precursor' 
_entity.formula_weight             56225.707 
_entity.pdbx_number_of_molecules   2 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_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       
;VAWYARYPHILEEATRLPFAYPIGQYYDTGYSVASATEWSKYVDTSLTIPGVMCVNFTPTPGESYNKNSPINIAAQNVYT
YVRHMNSGHANYEQADLMMYLLAMDSLYIFHSYVRKILAISKLYTPVNKYFPRALLVALGVDPEDVFANQAQWEYFVNMV
AYRAGAFAAPASMTYYERHAWMSNGLYVDQDVTRAQIYMFKPTMLWKYENLGTTGTKLVPLMMPKAGDNRKLVDFQVLFN
NLVSTMLGDEDFGIMSGDVFKAFGADGLVKLLAVDSTTMTLPTYDPLILAQIHSARAVGAPILETSTLTGFPGRQWQITQ
NPDVNNGAIIFHPSFGYDGQDHEELSFRAMCSNMILNLPGEAHSAEMIIEATRLATMFQVKAVPAGDTSKPVLYLPNGFG
TEVVNDYTMISVDKATPHDLTIHTFFNNILVPNAKENYVANLELLNNIIQFDWAPQLYLTYGIAQESFGPFAQLNDWTIL
TGETLARMHEVCVTSMFDVPQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VAWYARYPHILEEATRLPFAYPIGQYYDTGYSVASATEWSKYVDTSLTIPGVMCVNFTPTPGESYNKNSPINIAAQNVYT
YVRHMNSGHANYEQADLMMYLLAMDSLYIFHSYVRKILAISKLYTPVNKYFPRALLVALGVDPEDVFANQAQWEYFVNMV
AYRAGAFAAPASMTYYERHAWMSNGLYVDQDVTRAQIYMFKPTMLWKYENLGTTGTKLVPLMMPKAGDNRKLVDFQVLFN
NLVSTMLGDEDFGIMSGDVFKAFGADGLVKLLAVDSTTMTLPTYDPLILAQIHSARAVGAPILETSTLTGFPGRQWQITQ
NPDVNNGAIIFHPSFGYDGQDHEELSFRAMCSNMILNLPGEAHSAEMIIEATRLATMFQVKAVPAGDTSKPVLYLPNGFG
TEVVNDYTMISVDKATPHDLTIHTFFNNILVPNAKENYVANLELLNNIIQFDWAPQLYLTYGIAQESFGPFAQLNDWTIL
TGETLARMHEVCVTSMFDVPQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   ALA n 
1 3   TRP n 
1 4   TYR n 
1 5   ALA n 
1 6   ARG n 
1 7   TYR n 
1 8   PRO n 
1 9   HIS n 
1 10  ILE n 
1 11  LEU n 
1 12  GLU n 
1 13  GLU n 
1 14  ALA n 
1 15  THR n 
1 16  ARG n 
1 17  LEU n 
1 18  PRO n 
1 19  PHE n 
1 20  ALA n 
1 21  TYR n 
1 22  PRO n 
1 23  ILE n 
1 24  GLY n 
1 25  GLN n 
1 26  TYR n 
1 27  TYR n 
1 28  ASP n 
1 29  THR n 
1 30  GLY n 
1 31  TYR n 
1 32  SER n 
1 33  VAL n 
1 34  ALA n 
1 35  SER n 
1 36  ALA n 
1 37  THR n 
1 38  GLU n 
1 39  TRP n 
1 40  SER n 
1 41  LYS n 
1 42  TYR n 
1 43  VAL n 
1 44  ASP n 
1 45  THR n 
1 46  SER n 
1 47  LEU n 
1 48  THR n 
1 49  ILE n 
1 50  PRO n 
1 51  GLY n 
1 52  VAL n 
1 53  MET n 
1 54  CYS n 
1 55  VAL n 
1 56  ASN n 
1 57  PHE n 
1 58  THR n 
1 59  PRO n 
1 60  THR n 
1 61  PRO n 
1 62  GLY n 
1 63  GLU n 
1 64  SER n 
1 65  TYR n 
1 66  ASN n 
1 67  LYS n 
1 68  ASN n 
1 69  SER n 
1 70  PRO n 
1 71  ILE n 
1 72  ASN n 
1 73  ILE n 
1 74  ALA n 
1 75  ALA n 
1 76  GLN n 
1 77  ASN n 
1 78  VAL n 
1 79  TYR n 
1 80  THR n 
1 81  TYR n 
1 82  VAL n 
1 83  ARG n 
1 84  HIS n 
1 85  MET n 
1 86  ASN n 
1 87  SER n 
1 88  GLY n 
1 89  HIS n 
1 90  ALA n 
1 91  ASN n 
1 92  TYR n 
1 93  GLU n 
1 94  GLN n 
1 95  ALA n 
1 96  ASP n 
1 97  LEU n 
1 98  MET n 
1 99  MET n 
1 100 TYR n 
1 101 LEU n 
1 102 LEU n 
1 103 ALA n 
1 104 MET n 
1 105 ASP n 
1 106 SER n 
1 107 LEU n 
1 108 TYR n 
1 109 ILE n 
1 110 PHE n 
1 111 HIS n 
1 112 SER n 
1 113 TYR n 
1 114 VAL n 
1 115 ARG n 
1 116 LYS n 
1 117 ILE n 
1 118 LEU n 
1 119 ALA n 
1 120 ILE n 
1 121 SER n 
1 122 LYS n 
1 123 LEU n 
1 124 TYR n 
1 125 THR n 
1 126 PRO n 
1 127 VAL n 
1 128 ASN n 
1 129 LYS n 
1 130 TYR n 
1 131 PHE n 
1 132 PRO n 
1 133 ARG n 
1 134 ALA n 
1 135 LEU n 
1 136 LEU n 
1 137 VAL n 
1 138 ALA n 
1 139 LEU n 
1 140 GLY n 
1 141 VAL n 
1 142 ASP n 
1 143 PRO n 
1 144 GLU n 
1 145 ASP n 
1 146 VAL n 
1 147 PHE n 
1 148 ALA n 
1 149 ASN n 
1 150 GLN n 
1 151 ALA n 
1 152 GLN n 
1 153 TRP n 
1 154 GLU n 
1 155 TYR n 
1 156 PHE n 
1 157 VAL n 
1 158 ASN n 
1 159 MET n 
1 160 VAL n 
1 161 ALA n 
1 162 TYR n 
1 163 ARG n 
1 164 ALA n 
1 165 GLY n 
1 166 ALA n 
1 167 PHE n 
1 168 ALA n 
1 169 ALA n 
1 170 PRO n 
1 171 ALA n 
1 172 SER n 
1 173 MET n 
1 174 THR n 
1 175 TYR n 
1 176 TYR n 
1 177 GLU n 
1 178 ARG n 
1 179 HIS n 
1 180 ALA n 
1 181 TRP n 
1 182 MET n 
1 183 SER n 
1 184 ASN n 
1 185 GLY n 
1 186 LEU n 
1 187 TYR n 
1 188 VAL n 
1 189 ASP n 
1 190 GLN n 
1 191 ASP n 
1 192 VAL n 
1 193 THR n 
1 194 ARG n 
1 195 ALA n 
1 196 GLN n 
1 197 ILE n 
1 198 TYR n 
1 199 MET n 
1 200 PHE n 
1 201 LYS n 
1 202 PRO n 
1 203 THR n 
1 204 MET n 
1 205 LEU n 
1 206 TRP n 
1 207 LYS n 
1 208 TYR n 
1 209 GLU n 
1 210 ASN n 
1 211 LEU n 
1 212 GLY n 
1 213 THR n 
1 214 THR n 
1 215 GLY n 
1 216 THR n 
1 217 LYS n 
1 218 LEU n 
1 219 VAL n 
1 220 PRO n 
1 221 LEU n 
1 222 MET n 
1 223 MET n 
1 224 PRO n 
1 225 LYS n 
1 226 ALA n 
1 227 GLY n 
1 228 ASP n 
1 229 ASN n 
1 230 ARG n 
1 231 LYS n 
1 232 LEU n 
1 233 VAL n 
1 234 ASP n 
1 235 PHE n 
1 236 GLN n 
1 237 VAL n 
1 238 LEU n 
1 239 PHE n 
1 240 ASN n 
1 241 ASN n 
1 242 LEU n 
1 243 VAL n 
1 244 SER n 
1 245 THR n 
1 246 MET n 
1 247 LEU n 
1 248 GLY n 
1 249 ASP n 
1 250 GLU n 
1 251 ASP n 
1 252 PHE n 
1 253 GLY n 
1 254 ILE n 
1 255 MET n 
1 256 SER n 
1 257 GLY n 
1 258 ASP n 
1 259 VAL n 
1 260 PHE n 
1 261 LYS n 
1 262 ALA n 
1 263 PHE n 
1 264 GLY n 
1 265 ALA n 
1 266 ASP n 
1 267 GLY n 
1 268 LEU n 
1 269 VAL n 
1 270 LYS n 
1 271 LEU n 
1 272 LEU n 
1 273 ALA n 
1 274 VAL n 
1 275 ASP n 
1 276 SER n 
1 277 THR n 
1 278 THR n 
1 279 MET n 
1 280 THR n 
1 281 LEU n 
1 282 PRO n 
1 283 THR n 
1 284 TYR n 
1 285 ASP n 
1 286 PRO n 
1 287 LEU n 
1 288 ILE n 
1 289 LEU n 
1 290 ALA n 
1 291 GLN n 
1 292 ILE n 
1 293 HIS n 
1 294 SER n 
1 295 ALA n 
1 296 ARG n 
1 297 ALA n 
1 298 VAL n 
1 299 GLY n 
1 300 ALA n 
1 301 PRO n 
1 302 ILE n 
1 303 LEU n 
1 304 GLU n 
1 305 THR n 
1 306 SER n 
1 307 THR n 
1 308 LEU n 
1 309 THR n 
1 310 GLY n 
1 311 PHE n 
1 312 PRO n 
1 313 GLY n 
1 314 ARG n 
1 315 GLN n 
1 316 TRP n 
1 317 GLN n 
1 318 ILE n 
1 319 THR n 
1 320 GLN n 
1 321 ASN n 
1 322 PRO n 
1 323 ASP n 
1 324 VAL n 
1 325 ASN n 
1 326 ASN n 
1 327 GLY n 
1 328 ALA n 
1 329 ILE n 
1 330 ILE n 
1 331 PHE n 
1 332 HIS n 
1 333 PRO n 
1 334 SER n 
1 335 PHE n 
1 336 GLY n 
1 337 TYR n 
1 338 ASP n 
1 339 GLY n 
1 340 GLN n 
1 341 ASP n 
1 342 HIS n 
1 343 GLU n 
1 344 GLU n 
1 345 LEU n 
1 346 SER n 
1 347 PHE n 
1 348 ARG n 
1 349 ALA n 
1 350 MET n 
1 351 CYS n 
1 352 SER n 
1 353 ASN n 
1 354 MET n 
1 355 ILE n 
1 356 LEU n 
1 357 ASN n 
1 358 LEU n 
1 359 PRO n 
1 360 GLY n 
1 361 GLU n 
1 362 ALA n 
1 363 HIS n 
1 364 SER n 
1 365 ALA n 
1 366 GLU n 
1 367 MET n 
1 368 ILE n 
1 369 ILE n 
1 370 GLU n 
1 371 ALA n 
1 372 THR n 
1 373 ARG n 
1 374 LEU n 
1 375 ALA n 
1 376 THR n 
1 377 MET n 
1 378 PHE n 
1 379 GLN n 
1 380 VAL n 
1 381 LYS n 
1 382 ALA n 
1 383 VAL n 
1 384 PRO n 
1 385 ALA n 
1 386 GLY n 
1 387 ASP n 
1 388 THR n 
1 389 SER n 
1 390 LYS n 
1 391 PRO n 
1 392 VAL n 
1 393 LEU n 
1 394 TYR n 
1 395 LEU n 
1 396 PRO n 
1 397 ASN n 
1 398 GLY n 
1 399 PHE n 
1 400 GLY n 
1 401 THR n 
1 402 GLU n 
1 403 VAL n 
1 404 VAL n 
1 405 ASN n 
1 406 ASP n 
1 407 TYR n 
1 408 THR n 
1 409 MET n 
1 410 ILE n 
1 411 SER n 
1 412 VAL n 
1 413 ASP n 
1 414 LYS n 
1 415 ALA n 
1 416 THR n 
1 417 PRO n 
1 418 HIS n 
1 419 ASP n 
1 420 LEU n 
1 421 THR n 
1 422 ILE n 
1 423 HIS n 
1 424 THR n 
1 425 PHE n 
1 426 PHE n 
1 427 ASN n 
1 428 ASN n 
1 429 ILE n 
1 430 LEU n 
1 431 VAL n 
1 432 PRO n 
1 433 ASN n 
1 434 ALA n 
1 435 LYS n 
1 436 GLU n 
1 437 ASN n 
1 438 TYR n 
1 439 VAL n 
1 440 ALA n 
1 441 ASN n 
1 442 LEU n 
1 443 GLU n 
1 444 LEU n 
1 445 LEU n 
1 446 ASN n 
1 447 ASN n 
1 448 ILE n 
1 449 ILE n 
1 450 GLN n 
1 451 PHE n 
1 452 ASP n 
1 453 TRP n 
1 454 ALA n 
1 455 PRO n 
1 456 GLN n 
1 457 LEU n 
1 458 TYR n 
1 459 LEU n 
1 460 THR n 
1 461 TYR n 
1 462 GLY n 
1 463 ILE n 
1 464 ALA n 
1 465 GLN n 
1 466 GLU n 
1 467 SER n 
1 468 PHE n 
1 469 GLY n 
1 470 PRO n 
1 471 PHE n 
1 472 ALA n 
1 473 GLN n 
1 474 LEU n 
1 475 ASN n 
1 476 ASP n 
1 477 TRP n 
1 478 THR n 
1 479 ILE n 
1 480 LEU n 
1 481 THR n 
1 482 GLY n 
1 483 GLU n 
1 484 THR n 
1 485 LEU n 
1 486 ALA n 
1 487 ARG n 
1 488 MET n 
1 489 HIS n 
1 490 GLU n 
1 491 VAL n 
1 492 CYS n 
1 493 VAL n 
1 494 THR n 
1 495 SER n 
1 496 MET n 
1 497 PHE n 
1 498 ASP n 
1 499 VAL n 
1 500 PRO n 
1 501 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   501 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Segment-1, ORF2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              pLysS 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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  
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   VAL 1   47  47  VAL VAL A . n 
A 1 2   ALA 2   48  48  ALA ALA A . n 
A 1 3   TRP 3   49  49  TRP TRP A . n 
A 1 4   TYR 4   50  50  TYR TYR A . n 
A 1 5   ALA 5   51  51  ALA ALA A . n 
A 1 6   ARG 6   52  52  ARG ARG A . n 
A 1 7   TYR 7   53  53  TYR TYR A . n 
A 1 8   PRO 8   54  54  PRO PRO A . n 
A 1 9   HIS 9   55  55  HIS HIS A . n 
A 1 10  ILE 10  56  56  ILE ILE A . n 
A 1 11  LEU 11  57  57  LEU LEU A . n 
A 1 12  GLU 12  58  58  GLU GLU A . n 
A 1 13  GLU 13  59  59  GLU GLU A . n 
A 1 14  ALA 14  60  60  ALA ALA A . n 
A 1 15  THR 15  61  61  THR THR A . n 
A 1 16  ARG 16  62  62  ARG ARG A . n 
A 1 17  LEU 17  63  63  LEU LEU A . n 
A 1 18  PRO 18  64  64  PRO PRO A . n 
A 1 19  PHE 19  65  65  PHE PHE A . n 
A 1 20  ALA 20  66  66  ALA ALA A . n 
A 1 21  TYR 21  67  67  TYR TYR A . n 
A 1 22  PRO 22  68  68  PRO PRO A . n 
A 1 23  ILE 23  69  69  ILE ILE A . n 
A 1 24  GLY 24  70  70  GLY GLY A . n 
A 1 25  GLN 25  71  71  GLN GLN A . n 
A 1 26  TYR 26  72  72  TYR TYR A . n 
A 1 27  TYR 27  73  73  TYR TYR A . n 
A 1 28  ASP 28  74  74  ASP ASP A . n 
A 1 29  THR 29  75  75  THR THR A . n 
A 1 30  GLY 30  76  76  GLY GLY A . n 
A 1 31  TYR 31  77  77  TYR TYR A . n 
A 1 32  SER 32  78  78  SER SER A . n 
A 1 33  VAL 33  79  79  VAL VAL A . n 
A 1 34  ALA 34  80  80  ALA ALA A . n 
A 1 35  SER 35  81  81  SER SER A . n 
A 1 36  ALA 36  82  82  ALA ALA A . n 
A 1 37  THR 37  83  83  THR THR A . n 
A 1 38  GLU 38  84  84  GLU GLU A . n 
A 1 39  TRP 39  85  85  TRP TRP A . n 
A 1 40  SER 40  86  86  SER SER A . n 
A 1 41  LYS 41  87  87  LYS LYS A . n 
A 1 42  TYR 42  88  88  TYR TYR A . n 
A 1 43  VAL 43  89  89  VAL VAL A . n 
A 1 44  ASP 44  90  90  ASP ASP A . n 
A 1 45  THR 45  91  91  THR THR A . n 
A 1 46  SER 46  92  92  SER SER A . n 
A 1 47  LEU 47  93  93  LEU LEU A . n 
A 1 48  THR 48  94  94  THR THR A . n 
A 1 49  ILE 49  95  95  ILE ILE A . n 
A 1 50  PRO 50  96  96  PRO PRO A . n 
A 1 51  GLY 51  97  97  GLY GLY A . n 
A 1 52  VAL 52  98  98  VAL VAL A . n 
A 1 53  MET 53  99  99  MET MET A . n 
A 1 54  CYS 54  100 100 CYS CYS A . n 
A 1 55  VAL 55  101 101 VAL VAL A . n 
A 1 56  ASN 56  102 102 ASN ASN A . n 
A 1 57  PHE 57  103 103 PHE PHE A . n 
A 1 58  THR 58  104 104 THR THR A . n 
A 1 59  PRO 59  105 105 PRO PRO A . n 
A 1 60  THR 60  106 106 THR THR A . n 
A 1 61  PRO 61  107 107 PRO PRO A . n 
A 1 62  GLY 62  108 108 GLY GLY A . n 
A 1 63  GLU 63  109 109 GLU GLU A . n 
A 1 64  SER 64  110 110 SER SER A . n 
A 1 65  TYR 65  111 111 TYR TYR A . n 
A 1 66  ASN 66  112 112 ASN ASN A . n 
A 1 67  LYS 67  113 113 LYS LYS A . n 
A 1 68  ASN 68  114 114 ASN ASN A . n 
A 1 69  SER 69  115 115 SER SER A . n 
A 1 70  PRO 70  116 116 PRO PRO A . n 
A 1 71  ILE 71  117 117 ILE ILE A . n 
A 1 72  ASN 72  118 118 ASN ASN A . n 
A 1 73  ILE 73  119 119 ILE ILE A . n 
A 1 74  ALA 74  120 120 ALA ALA A . n 
A 1 75  ALA 75  121 121 ALA ALA A . n 
A 1 76  GLN 76  122 122 GLN GLN A . n 
A 1 77  ASN 77  123 123 ASN ASN A . n 
A 1 78  VAL 78  124 124 VAL VAL A . n 
A 1 79  TYR 79  125 125 TYR TYR A . n 
A 1 80  THR 80  126 126 THR THR A . n 
A 1 81  TYR 81  127 127 TYR TYR A . n 
A 1 82  VAL 82  128 128 VAL VAL A . n 
A 1 83  ARG 83  129 129 ARG ARG A . n 
A 1 84  HIS 84  130 130 HIS HIS A . n 
A 1 85  MET 85  131 131 MET MET A . n 
A 1 86  ASN 86  132 132 ASN ASN A . n 
A 1 87  SER 87  133 133 SER SER A . n 
A 1 88  GLY 88  134 134 GLY GLY A . n 
A 1 89  HIS 89  135 135 HIS HIS A . n 
A 1 90  ALA 90  136 136 ALA ALA A . n 
A 1 91  ASN 91  137 137 ASN ASN A . n 
A 1 92  TYR 92  138 138 TYR TYR A . n 
A 1 93  GLU 93  139 139 GLU GLU A . n 
A 1 94  GLN 94  140 140 GLN GLN A . n 
A 1 95  ALA 95  141 141 ALA ALA A . n 
A 1 96  ASP 96  142 142 ASP ASP A . n 
A 1 97  LEU 97  143 143 LEU LEU A . n 
A 1 98  MET 98  144 144 MET MET A . n 
A 1 99  MET 99  145 145 MET MET A . n 
A 1 100 TYR 100 146 146 TYR TYR A . n 
A 1 101 LEU 101 147 147 LEU LEU A . n 
A 1 102 LEU 102 148 148 LEU LEU A . n 
A 1 103 ALA 103 149 149 ALA ALA A . n 
A 1 104 MET 104 150 150 MET MET A . n 
A 1 105 ASP 105 151 151 ASP ASP A . n 
A 1 106 SER 106 152 152 SER SER A . n 
A 1 107 LEU 107 153 153 LEU LEU A . n 
A 1 108 TYR 108 154 154 TYR TYR A . n 
A 1 109 ILE 109 155 155 ILE ILE A . n 
A 1 110 PHE 110 156 156 PHE PHE A . n 
A 1 111 HIS 111 157 157 HIS HIS A . n 
A 1 112 SER 112 158 158 SER SER A . n 
A 1 113 TYR 113 159 159 TYR TYR A . n 
A 1 114 VAL 114 160 160 VAL VAL A . n 
A 1 115 ARG 115 161 161 ARG ARG A . n 
A 1 116 LYS 116 162 162 LYS LYS A . n 
A 1 117 ILE 117 163 163 ILE ILE A . n 
A 1 118 LEU 118 164 164 LEU LEU A . n 
A 1 119 ALA 119 165 165 ALA ALA A . n 
A 1 120 ILE 120 166 166 ILE ILE A . n 
A 1 121 SER 121 167 167 SER SER A . n 
A 1 122 LYS 122 168 168 LYS LYS A . n 
A 1 123 LEU 123 169 169 LEU LEU A . n 
A 1 124 TYR 124 170 170 TYR TYR A . n 
A 1 125 THR 125 171 171 THR THR A . n 
A 1 126 PRO 126 172 172 PRO PRO A . n 
A 1 127 VAL 127 173 173 VAL VAL A . n 
A 1 128 ASN 128 174 174 ASN ASN A . n 
A 1 129 LYS 129 175 175 LYS LYS A . n 
A 1 130 TYR 130 176 176 TYR TYR A . n 
A 1 131 PHE 131 177 177 PHE PHE A . n 
A 1 132 PRO 132 178 178 PRO PRO A . n 
A 1 133 ARG 133 179 179 ARG ARG A . n 
A 1 134 ALA 134 180 180 ALA ALA A . n 
A 1 135 LEU 135 181 181 LEU LEU A . n 
A 1 136 LEU 136 182 182 LEU LEU A . n 
A 1 137 VAL 137 183 183 VAL VAL A . n 
A 1 138 ALA 138 184 184 ALA ALA A . n 
A 1 139 LEU 139 185 185 LEU LEU A . n 
A 1 140 GLY 140 186 186 GLY GLY A . n 
A 1 141 VAL 141 187 187 VAL VAL A . n 
A 1 142 ASP 142 188 188 ASP ASP A . n 
A 1 143 PRO 143 189 189 PRO PRO A . n 
A 1 144 GLU 144 190 190 GLU GLU A . n 
A 1 145 ASP 145 191 191 ASP ASP A . n 
A 1 146 VAL 146 192 192 VAL VAL A . n 
A 1 147 PHE 147 193 193 PHE PHE A . n 
A 1 148 ALA 148 194 194 ALA ALA A . n 
A 1 149 ASN 149 195 195 ASN ASN A . n 
A 1 150 GLN 150 196 196 GLN GLN A . n 
A 1 151 ALA 151 197 197 ALA ALA A . n 
A 1 152 GLN 152 198 198 GLN GLN A . n 
A 1 153 TRP 153 199 199 TRP TRP A . n 
A 1 154 GLU 154 200 200 GLU GLU A . n 
A 1 155 TYR 155 201 201 TYR TYR A . n 
A 1 156 PHE 156 202 202 PHE PHE A . n 
A 1 157 VAL 157 203 203 VAL VAL A . n 
A 1 158 ASN 158 204 204 ASN ASN A . n 
A 1 159 MET 159 205 205 MET MET A . n 
A 1 160 VAL 160 206 206 VAL VAL A . n 
A 1 161 ALA 161 207 207 ALA ALA A . n 
A 1 162 TYR 162 208 208 TYR TYR A . n 
A 1 163 ARG 163 209 209 ARG ARG A . n 
A 1 164 ALA 164 210 210 ALA ALA A . n 
A 1 165 GLY 165 211 211 GLY GLY A . n 
A 1 166 ALA 166 212 212 ALA ALA A . n 
A 1 167 PHE 167 213 213 PHE PHE A . n 
A 1 168 ALA 168 214 214 ALA ALA A . n 
A 1 169 ALA 169 215 215 ALA ALA A . n 
A 1 170 PRO 170 216 216 PRO PRO A . n 
A 1 171 ALA 171 217 217 ALA ALA A . n 
A 1 172 SER 172 218 218 SER SER A . n 
A 1 173 MET 173 219 219 MET MET A . n 
A 1 174 THR 174 220 220 THR THR A . n 
A 1 175 TYR 175 221 221 TYR TYR A . n 
A 1 176 TYR 176 222 222 TYR TYR A . n 
A 1 177 GLU 177 223 223 GLU GLU A . n 
A 1 178 ARG 178 224 224 ARG ARG A . n 
A 1 179 HIS 179 225 225 HIS HIS A . n 
A 1 180 ALA 180 226 226 ALA ALA A . n 
A 1 181 TRP 181 227 227 TRP TRP A . n 
A 1 182 MET 182 228 228 MET MET A . n 
A 1 183 SER 183 229 229 SER SER A . n 
A 1 184 ASN 184 230 230 ASN ASN A . n 
A 1 185 GLY 185 231 231 GLY GLY A . n 
A 1 186 LEU 186 232 232 LEU LEU A . n 
A 1 187 TYR 187 233 233 TYR TYR A . n 
A 1 188 VAL 188 234 234 VAL VAL A . n 
A 1 189 ASP 189 235 235 ASP ASP A . n 
A 1 190 GLN 190 236 236 GLN GLN A . n 
A 1 191 ASP 191 237 237 ASP ASP A . n 
A 1 192 VAL 192 238 238 VAL VAL A . n 
A 1 193 THR 193 239 239 THR THR A . n 
A 1 194 ARG 194 240 240 ARG ARG A . n 
A 1 195 ALA 195 241 241 ALA ALA A . n 
A 1 196 GLN 196 242 242 GLN GLN A . n 
A 1 197 ILE 197 243 243 ILE ILE A . n 
A 1 198 TYR 198 244 244 TYR TYR A . n 
A 1 199 MET 199 245 245 MET MET A . n 
A 1 200 PHE 200 246 246 PHE PHE A . n 
A 1 201 LYS 201 247 247 LYS LYS A . n 
A 1 202 PRO 202 248 248 PRO PRO A . n 
A 1 203 THR 203 249 249 THR THR A . n 
A 1 204 MET 204 250 250 MET MET A . n 
A 1 205 LEU 205 251 251 LEU LEU A . n 
A 1 206 TRP 206 252 252 TRP TRP A . n 
A 1 207 LYS 207 253 253 LYS LYS A . n 
A 1 208 TYR 208 254 254 TYR TYR A . n 
A 1 209 GLU 209 255 255 GLU GLU A . n 
A 1 210 ASN 210 256 256 ASN ASN A . n 
A 1 211 LEU 211 257 257 LEU LEU A . n 
A 1 212 GLY 212 258 258 GLY GLY A . n 
A 1 213 THR 213 259 259 THR THR A . n 
A 1 214 THR 214 260 260 THR THR A . n 
A 1 215 GLY 215 261 261 GLY GLY A . n 
A 1 216 THR 216 262 262 THR THR A . n 
A 1 217 LYS 217 263 263 LYS LYS A . n 
A 1 218 LEU 218 264 264 LEU LEU A . n 
A 1 219 VAL 219 265 265 VAL VAL A . n 
A 1 220 PRO 220 266 266 PRO PRO A . n 
A 1 221 LEU 221 267 267 LEU LEU A . n 
A 1 222 MET 222 268 268 MET MET A . n 
A 1 223 MET 223 269 269 MET MET A . n 
A 1 224 PRO 224 270 270 PRO PRO A . n 
A 1 225 LYS 225 271 271 LYS LYS A . n 
A 1 226 ALA 226 272 272 ALA ALA A . n 
A 1 227 GLY 227 273 273 GLY GLY A . n 
A 1 228 ASP 228 274 274 ASP ASP A . n 
A 1 229 ASN 229 275 275 ASN ASN A . n 
A 1 230 ARG 230 276 276 ARG ARG A . n 
A 1 231 LYS 231 277 277 LYS LYS A . n 
A 1 232 LEU 232 278 278 LEU LEU A . n 
A 1 233 VAL 233 279 279 VAL VAL A . n 
A 1 234 ASP 234 280 280 ASP ASP A . n 
A 1 235 PHE 235 281 281 PHE PHE A . n 
A 1 236 GLN 236 282 282 GLN GLN A . n 
A 1 237 VAL 237 283 283 VAL VAL A . n 
A 1 238 LEU 238 284 284 LEU LEU A . n 
A 1 239 PHE 239 285 285 PHE PHE A . n 
A 1 240 ASN 240 286 286 ASN ASN A . n 
A 1 241 ASN 241 287 287 ASN ASN A . n 
A 1 242 LEU 242 288 288 LEU LEU A . n 
A 1 243 VAL 243 289 289 VAL VAL A . n 
A 1 244 SER 244 290 290 SER SER A . n 
A 1 245 THR 245 291 291 THR THR A . n 
A 1 246 MET 246 292 292 MET MET A . n 
A 1 247 LEU 247 293 293 LEU LEU A . n 
A 1 248 GLY 248 294 294 GLY GLY A . n 
A 1 249 ASP 249 295 295 ASP ASP A . n 
A 1 250 GLU 250 296 296 GLU GLU A . n 
A 1 251 ASP 251 297 297 ASP ASP A . n 
A 1 252 PHE 252 298 298 PHE PHE A . n 
A 1 253 GLY 253 299 299 GLY GLY A . n 
A 1 254 ILE 254 300 300 ILE ILE A . n 
A 1 255 MET 255 301 301 MET MET A . n 
A 1 256 SER 256 302 302 SER SER A . n 
A 1 257 GLY 257 303 303 GLY GLY A . n 
A 1 258 ASP 258 304 304 ASP ASP A . n 
A 1 259 VAL 259 305 305 VAL VAL A . n 
A 1 260 PHE 260 306 306 PHE PHE A . n 
A 1 261 LYS 261 307 307 LYS LYS A . n 
A 1 262 ALA 262 308 308 ALA ALA A . n 
A 1 263 PHE 263 309 309 PHE PHE A . n 
A 1 264 GLY 264 310 310 GLY GLY A . n 
A 1 265 ALA 265 311 311 ALA ALA A . n 
A 1 266 ASP 266 312 312 ASP ASP A . n 
A 1 267 GLY 267 313 313 GLY GLY A . n 
A 1 268 LEU 268 314 314 LEU LEU A . n 
A 1 269 VAL 269 315 315 VAL VAL A . n 
A 1 270 LYS 270 316 316 LYS LYS A . n 
A 1 271 LEU 271 317 317 LEU LEU A . n 
A 1 272 LEU 272 318 318 LEU LEU A . n 
A 1 273 ALA 273 319 319 ALA ALA A . n 
A 1 274 VAL 274 320 320 VAL VAL A . n 
A 1 275 ASP 275 321 321 ASP ASP A . n 
A 1 276 SER 276 322 322 SER SER A . n 
A 1 277 THR 277 323 323 THR THR A . n 
A 1 278 THR 278 324 324 THR THR A . n 
A 1 279 MET 279 325 325 MET MET A . n 
A 1 280 THR 280 326 326 THR THR A . n 
A 1 281 LEU 281 327 327 LEU LEU A . n 
A 1 282 PRO 282 328 328 PRO PRO A . n 
A 1 283 THR 283 329 329 THR THR A . n 
A 1 284 TYR 284 330 330 TYR TYR A . n 
A 1 285 ASP 285 331 331 ASP ASP A . n 
A 1 286 PRO 286 332 332 PRO PRO A . n 
A 1 287 LEU 287 333 333 LEU LEU A . n 
A 1 288 ILE 288 334 334 ILE ILE A . n 
A 1 289 LEU 289 335 335 LEU LEU A . n 
A 1 290 ALA 290 336 336 ALA ALA A . n 
A 1 291 GLN 291 337 337 GLN GLN A . n 
A 1 292 ILE 292 338 338 ILE ILE A . n 
A 1 293 HIS 293 339 339 HIS HIS A . n 
A 1 294 SER 294 340 340 SER SER A . n 
A 1 295 ALA 295 341 341 ALA ALA A . n 
A 1 296 ARG 296 342 342 ARG ARG A . n 
A 1 297 ALA 297 343 343 ALA ALA A . n 
A 1 298 VAL 298 344 344 VAL VAL A . n 
A 1 299 GLY 299 345 345 GLY GLY A . n 
A 1 300 ALA 300 346 346 ALA ALA A . n 
A 1 301 PRO 301 347 347 PRO PRO A . n 
A 1 302 ILE 302 348 348 ILE ILE A . n 
A 1 303 LEU 303 349 349 LEU LEU A . n 
A 1 304 GLU 304 350 350 GLU GLU A . n 
A 1 305 THR 305 351 351 THR THR A . n 
A 1 306 SER 306 352 352 SER SER A . n 
A 1 307 THR 307 353 353 THR THR A . n 
A 1 308 LEU 308 354 354 LEU LEU A . n 
A 1 309 THR 309 355 355 THR THR A . n 
A 1 310 GLY 310 356 356 GLY GLY A . n 
A 1 311 PHE 311 357 357 PHE PHE A . n 
A 1 312 PRO 312 358 358 PRO PRO A . n 
A 1 313 GLY 313 359 359 GLY GLY A . n 
A 1 314 ARG 314 360 360 ARG ARG A . n 
A 1 315 GLN 315 361 361 GLN GLN A . n 
A 1 316 TRP 316 362 362 TRP TRP A . n 
A 1 317 GLN 317 363 363 GLN GLN A . n 
A 1 318 ILE 318 364 364 ILE ILE A . n 
A 1 319 THR 319 365 365 THR THR A . n 
A 1 320 GLN 320 366 366 GLN GLN A . n 
A 1 321 ASN 321 367 367 ASN ASN A . n 
A 1 322 PRO 322 368 368 PRO PRO A . n 
A 1 323 ASP 323 369 369 ASP ASP A . n 
A 1 324 VAL 324 370 370 VAL VAL A . n 
A 1 325 ASN 325 371 371 ASN ASN A . n 
A 1 326 ASN 326 372 372 ASN ASN A . n 
A 1 327 GLY 327 373 373 GLY GLY A . n 
A 1 328 ALA 328 374 374 ALA ALA A . n 
A 1 329 ILE 329 375 375 ILE ILE A . n 
A 1 330 ILE 330 376 376 ILE ILE A . n 
A 1 331 PHE 331 377 377 PHE PHE A . n 
A 1 332 HIS 332 378 378 HIS HIS A . n 
A 1 333 PRO 333 379 379 PRO PRO A . n 
A 1 334 SER 334 380 380 SER SER A . n 
A 1 335 PHE 335 381 381 PHE PHE A . n 
A 1 336 GLY 336 382 382 GLY GLY A . n 
A 1 337 TYR 337 383 383 TYR TYR A . n 
A 1 338 ASP 338 384 384 ASP ASP A . n 
A 1 339 GLY 339 385 385 GLY GLY A . n 
A 1 340 GLN 340 386 386 GLN GLN A . n 
A 1 341 ASP 341 387 387 ASP ASP A . n 
A 1 342 HIS 342 388 388 HIS HIS A . n 
A 1 343 GLU 343 389 389 GLU GLU A . n 
A 1 344 GLU 344 390 390 GLU GLU A . n 
A 1 345 LEU 345 391 391 LEU LEU A . n 
A 1 346 SER 346 392 392 SER SER A . n 
A 1 347 PHE 347 393 393 PHE PHE A . n 
A 1 348 ARG 348 394 394 ARG ARG A . n 
A 1 349 ALA 349 395 395 ALA ALA A . n 
A 1 350 MET 350 396 396 MET MET A . n 
A 1 351 CYS 351 397 397 CYS CYS A . n 
A 1 352 SER 352 398 398 SER SER A . n 
A 1 353 ASN 353 399 399 ASN ASN A . n 
A 1 354 MET 354 400 400 MET MET A . n 
A 1 355 ILE 355 401 401 ILE ILE A . n 
A 1 356 LEU 356 402 402 LEU LEU A . n 
A 1 357 ASN 357 403 403 ASN ASN A . n 
A 1 358 LEU 358 404 404 LEU LEU A . n 
A 1 359 PRO 359 405 405 PRO PRO A . n 
A 1 360 GLY 360 406 406 GLY GLY A . n 
A 1 361 GLU 361 407 407 GLU GLU A . n 
A 1 362 ALA 362 408 408 ALA ALA A . n 
A 1 363 HIS 363 409 409 HIS HIS A . n 
A 1 364 SER 364 410 410 SER SER A . n 
A 1 365 ALA 365 411 411 ALA ALA A . n 
A 1 366 GLU 366 412 412 GLU GLU A . n 
A 1 367 MET 367 413 413 MET MET A . n 
A 1 368 ILE 368 414 414 ILE ILE A . n 
A 1 369 ILE 369 415 415 ILE ILE A . n 
A 1 370 GLU 370 416 416 GLU GLU A . n 
A 1 371 ALA 371 417 417 ALA ALA A . n 
A 1 372 THR 372 418 418 THR THR A . n 
A 1 373 ARG 373 419 419 ARG ARG A . n 
A 1 374 LEU 374 420 420 LEU LEU A . n 
A 1 375 ALA 375 421 421 ALA ALA A . n 
A 1 376 THR 376 422 422 THR THR A . n 
A 1 377 MET 377 423 423 MET MET A . n 
A 1 378 PHE 378 424 424 PHE PHE A . n 
A 1 379 GLN 379 425 425 GLN GLN A . n 
A 1 380 VAL 380 426 426 VAL VAL A . n 
A 1 381 LYS 381 427 427 LYS LYS A . n 
A 1 382 ALA 382 428 428 ALA ALA A . n 
A 1 383 VAL 383 429 429 VAL VAL A . n 
A 1 384 PRO 384 430 430 PRO PRO A . n 
A 1 385 ALA 385 431 431 ALA ALA A . n 
A 1 386 GLY 386 432 432 GLY GLY A . n 
A 1 387 ASP 387 433 433 ASP ASP A . n 
A 1 388 THR 388 434 434 THR THR A . n 
A 1 389 SER 389 435 435 SER SER A . n 
A 1 390 LYS 390 436 436 LYS LYS A . n 
A 1 391 PRO 391 437 437 PRO PRO A . n 
A 1 392 VAL 392 438 438 VAL VAL A . n 
A 1 393 LEU 393 439 439 LEU LEU A . n 
A 1 394 TYR 394 440 440 TYR TYR A . n 
A 1 395 LEU 395 441 441 LEU LEU A . n 
A 1 396 PRO 396 442 442 PRO PRO A . n 
A 1 397 ASN 397 443 443 ASN ASN A . n 
A 1 398 GLY 398 444 444 GLY GLY A . n 
A 1 399 PHE 399 445 445 PHE PHE A . n 
A 1 400 GLY 400 446 446 GLY GLY A . n 
A 1 401 THR 401 447 447 THR THR A . n 
A 1 402 GLU 402 448 448 GLU GLU A . n 
A 1 403 VAL 403 449 449 VAL VAL A . n 
A 1 404 VAL 404 450 450 VAL VAL A . n 
A 1 405 ASN 405 451 451 ASN ASN A . n 
A 1 406 ASP 406 452 452 ASP ASP A . n 
A 1 407 TYR 407 453 453 TYR TYR A . n 
A 1 408 THR 408 454 454 THR THR A . n 
A 1 409 MET 409 455 455 MET MET A . n 
A 1 410 ILE 410 456 456 ILE ILE A . n 
A 1 411 SER 411 457 457 SER SER A . n 
A 1 412 VAL 412 458 458 VAL VAL A . n 
A 1 413 ASP 413 459 459 ASP ASP A . n 
A 1 414 LYS 414 460 460 LYS LYS A . n 
A 1 415 ALA 415 461 461 ALA ALA A . n 
A 1 416 THR 416 462 462 THR THR A . n 
A 1 417 PRO 417 463 463 PRO PRO A . n 
A 1 418 HIS 418 464 464 HIS HIS A . n 
A 1 419 ASP 419 465 465 ASP ASP A . n 
A 1 420 LEU 420 466 466 LEU LEU A . n 
A 1 421 THR 421 467 467 THR THR A . n 
A 1 422 ILE 422 468 468 ILE ILE A . n 
A 1 423 HIS 423 469 469 HIS HIS A . n 
A 1 424 THR 424 470 470 THR THR A . n 
A 1 425 PHE 425 471 471 PHE PHE A . n 
A 1 426 PHE 426 472 472 PHE PHE A . n 
A 1 427 ASN 427 473 473 ASN ASN A . n 
A 1 428 ASN 428 474 474 ASN ASN A . n 
A 1 429 ILE 429 475 475 ILE ILE A . n 
A 1 430 LEU 430 476 476 LEU LEU A . n 
A 1 431 VAL 431 477 477 VAL VAL A . n 
A 1 432 PRO 432 478 478 PRO PRO A . n 
A 1 433 ASN 433 479 479 ASN ASN A . n 
A 1 434 ALA 434 480 480 ALA ALA A . n 
A 1 435 LYS 435 481 481 LYS LYS A . n 
A 1 436 GLU 436 482 482 GLU GLU A . n 
A 1 437 ASN 437 483 483 ASN ASN A . n 
A 1 438 TYR 438 484 484 TYR TYR A . n 
A 1 439 VAL 439 485 485 VAL VAL A . n 
A 1 440 ALA 440 486 486 ALA ALA A . n 
A 1 441 ASN 441 487 487 ASN ASN A . n 
A 1 442 LEU 442 488 488 LEU LEU A . n 
A 1 443 GLU 443 489 489 GLU GLU A . n 
A 1 444 LEU 444 490 490 LEU LEU A . n 
A 1 445 LEU 445 491 491 LEU LEU A . n 
A 1 446 ASN 446 492 492 ASN ASN A . n 
A 1 447 ASN 447 493 493 ASN ASN A . n 
A 1 448 ILE 448 494 494 ILE ILE A . n 
A 1 449 ILE 449 495 495 ILE ILE A . n 
A 1 450 GLN 450 496 496 GLN GLN A . n 
A 1 451 PHE 451 497 497 PHE PHE A . n 
A 1 452 ASP 452 498 498 ASP ASP A . n 
A 1 453 TRP 453 499 499 TRP TRP A . n 
A 1 454 ALA 454 500 500 ALA ALA A . n 
A 1 455 PRO 455 501 501 PRO PRO A . n 
A 1 456 GLN 456 502 502 GLN GLN A . n 
A 1 457 LEU 457 503 503 LEU LEU A . n 
A 1 458 TYR 458 504 504 TYR TYR A . n 
A 1 459 LEU 459 505 505 LEU LEU A . n 
A 1 460 THR 460 506 506 THR THR A . n 
A 1 461 TYR 461 507 507 TYR TYR A . n 
A 1 462 GLY 462 508 508 GLY GLY A . n 
A 1 463 ILE 463 509 509 ILE ILE A . n 
A 1 464 ALA 464 510 510 ALA ALA A . n 
A 1 465 GLN 465 511 511 GLN GLN A . n 
A 1 466 GLU 466 512 512 GLU GLU A . n 
A 1 467 SER 467 513 513 SER SER A . n 
A 1 468 PHE 468 514 514 PHE PHE A . n 
A 1 469 GLY 469 515 515 GLY GLY A . n 
A 1 470 PRO 470 516 516 PRO PRO A . n 
A 1 471 PHE 471 517 517 PHE PHE A . n 
A 1 472 ALA 472 518 518 ALA ALA A . n 
A 1 473 GLN 473 519 519 GLN GLN A . n 
A 1 474 LEU 474 520 520 LEU LEU A . n 
A 1 475 ASN 475 521 521 ASN ASN A . n 
A 1 476 ASP 476 522 522 ASP ASP A . n 
A 1 477 TRP 477 523 523 TRP TRP A . n 
A 1 478 THR 478 524 524 THR THR A . n 
A 1 479 ILE 479 525 525 ILE ILE A . n 
A 1 480 LEU 480 526 526 LEU LEU A . n 
A 1 481 THR 481 527 527 THR THR A . n 
A 1 482 GLY 482 528 528 GLY GLY A . n 
A 1 483 GLU 483 529 529 GLU GLU A . n 
A 1 484 THR 484 530 530 THR THR A . n 
A 1 485 LEU 485 531 531 LEU LEU A . n 
A 1 486 ALA 486 532 532 ALA ALA A . n 
A 1 487 ARG 487 533 533 ARG ARG A . n 
A 1 488 MET 488 534 534 MET MET A . n 
A 1 489 HIS 489 535 535 HIS HIS A . n 
A 1 490 GLU 490 536 536 GLU GLU A . n 
A 1 491 VAL 491 537 537 VAL VAL A . n 
A 1 492 CYS 492 538 538 CYS CYS A . n 
A 1 493 VAL 493 539 539 VAL VAL A . n 
A 1 494 THR 494 540 540 THR THR A . n 
A 1 495 SER 495 541 541 SER SER A . n 
A 1 496 MET 496 542 542 MET MET A . n 
A 1 497 PHE 497 543 543 PHE PHE A . n 
A 1 498 ASP 498 544 544 ASP ASP A . n 
A 1 499 VAL 499 545 545 VAL VAL A . n 
A 1 500 PRO 500 546 ?   ?   ?   A . n 
A 1 501 GLN 501 547 ?   ?   ?   A . n 
B 1 1   VAL 1   47  47  VAL VAL B . n 
B 1 2   ALA 2   48  48  ALA ALA B . n 
B 1 3   TRP 3   49  49  TRP TRP B . n 
B 1 4   TYR 4   50  50  TYR TYR B . n 
B 1 5   ALA 5   51  51  ALA ALA B . n 
B 1 6   ARG 6   52  52  ARG ARG B . n 
B 1 7   TYR 7   53  53  TYR TYR B . n 
B 1 8   PRO 8   54  54  PRO PRO B . n 
B 1 9   HIS 9   55  55  HIS HIS B . n 
B 1 10  ILE 10  56  56  ILE ILE B . n 
B 1 11  LEU 11  57  57  LEU LEU B . n 
B 1 12  GLU 12  58  58  GLU GLU B . n 
B 1 13  GLU 13  59  59  GLU GLU B . n 
B 1 14  ALA 14  60  60  ALA ALA B . n 
B 1 15  THR 15  61  61  THR THR B . n 
B 1 16  ARG 16  62  62  ARG ARG B . n 
B 1 17  LEU 17  63  63  LEU LEU B . n 
B 1 18  PRO 18  64  64  PRO PRO B . n 
B 1 19  PHE 19  65  65  PHE PHE B . n 
B 1 20  ALA 20  66  66  ALA ALA B . n 
B 1 21  TYR 21  67  67  TYR TYR B . n 
B 1 22  PRO 22  68  68  PRO PRO B . n 
B 1 23  ILE 23  69  69  ILE ILE B . n 
B 1 24  GLY 24  70  70  GLY GLY B . n 
B 1 25  GLN 25  71  71  GLN GLN B . n 
B 1 26  TYR 26  72  72  TYR TYR B . n 
B 1 27  TYR 27  73  73  TYR TYR B . n 
B 1 28  ASP 28  74  74  ASP ASP B . n 
B 1 29  THR 29  75  75  THR THR B . n 
B 1 30  GLY 30  76  76  GLY GLY B . n 
B 1 31  TYR 31  77  77  TYR TYR B . n 
B 1 32  SER 32  78  78  SER SER B . n 
B 1 33  VAL 33  79  79  VAL VAL B . n 
B 1 34  ALA 34  80  80  ALA ALA B . n 
B 1 35  SER 35  81  81  SER SER B . n 
B 1 36  ALA 36  82  82  ALA ALA B . n 
B 1 37  THR 37  83  83  THR THR B . n 
B 1 38  GLU 38  84  84  GLU GLU B . n 
B 1 39  TRP 39  85  85  TRP TRP B . n 
B 1 40  SER 40  86  86  SER SER B . n 
B 1 41  LYS 41  87  87  LYS LYS B . n 
B 1 42  TYR 42  88  88  TYR TYR B . n 
B 1 43  VAL 43  89  89  VAL VAL B . n 
B 1 44  ASP 44  90  90  ASP ASP B . n 
B 1 45  THR 45  91  91  THR THR B . n 
B 1 46  SER 46  92  92  SER SER B . n 
B 1 47  LEU 47  93  93  LEU LEU B . n 
B 1 48  THR 48  94  94  THR THR B . n 
B 1 49  ILE 49  95  95  ILE ILE B . n 
B 1 50  PRO 50  96  96  PRO PRO B . n 
B 1 51  GLY 51  97  97  GLY GLY B . n 
B 1 52  VAL 52  98  98  VAL VAL B . n 
B 1 53  MET 53  99  99  MET MET B . n 
B 1 54  CYS 54  100 100 CYS CYS B . n 
B 1 55  VAL 55  101 101 VAL VAL B . n 
B 1 56  ASN 56  102 102 ASN ASN B . n 
B 1 57  PHE 57  103 103 PHE PHE B . n 
B 1 58  THR 58  104 104 THR THR B . n 
B 1 59  PRO 59  105 105 PRO PRO B . n 
B 1 60  THR 60  106 106 THR THR B . n 
B 1 61  PRO 61  107 107 PRO PRO B . n 
B 1 62  GLY 62  108 108 GLY GLY B . n 
B 1 63  GLU 63  109 109 GLU GLU B . n 
B 1 64  SER 64  110 110 SER SER B . n 
B 1 65  TYR 65  111 111 TYR TYR B . n 
B 1 66  ASN 66  112 112 ASN ASN B . n 
B 1 67  LYS 67  113 113 LYS LYS B . n 
B 1 68  ASN 68  114 114 ASN ASN B . n 
B 1 69  SER 69  115 115 SER SER B . n 
B 1 70  PRO 70  116 116 PRO PRO B . n 
B 1 71  ILE 71  117 117 ILE ILE B . n 
B 1 72  ASN 72  118 118 ASN ASN B . n 
B 1 73  ILE 73  119 119 ILE ILE B . n 
B 1 74  ALA 74  120 120 ALA ALA B . n 
B 1 75  ALA 75  121 121 ALA ALA B . n 
B 1 76  GLN 76  122 122 GLN GLN B . n 
B 1 77  ASN 77  123 123 ASN ASN B . n 
B 1 78  VAL 78  124 124 VAL VAL B . n 
B 1 79  TYR 79  125 125 TYR TYR B . n 
B 1 80  THR 80  126 126 THR THR B . n 
B 1 81  TYR 81  127 127 TYR TYR B . n 
B 1 82  VAL 82  128 128 VAL VAL B . n 
B 1 83  ARG 83  129 129 ARG ARG B . n 
B 1 84  HIS 84  130 130 HIS HIS B . n 
B 1 85  MET 85  131 131 MET MET B . n 
B 1 86  ASN 86  132 132 ASN ASN B . n 
B 1 87  SER 87  133 133 SER SER B . n 
B 1 88  GLY 88  134 134 GLY GLY B . n 
B 1 89  HIS 89  135 135 HIS HIS B . n 
B 1 90  ALA 90  136 136 ALA ALA B . n 
B 1 91  ASN 91  137 137 ASN ASN B . n 
B 1 92  TYR 92  138 138 TYR TYR B . n 
B 1 93  GLU 93  139 139 GLU GLU B . n 
B 1 94  GLN 94  140 140 GLN GLN B . n 
B 1 95  ALA 95  141 141 ALA ALA B . n 
B 1 96  ASP 96  142 142 ASP ASP B . n 
B 1 97  LEU 97  143 143 LEU LEU B . n 
B 1 98  MET 98  144 144 MET MET B . n 
B 1 99  MET 99  145 145 MET MET B . n 
B 1 100 TYR 100 146 146 TYR TYR B . n 
B 1 101 LEU 101 147 147 LEU LEU B . n 
B 1 102 LEU 102 148 148 LEU LEU B . n 
B 1 103 ALA 103 149 149 ALA ALA B . n 
B 1 104 MET 104 150 150 MET MET B . n 
B 1 105 ASP 105 151 151 ASP ASP B . n 
B 1 106 SER 106 152 152 SER SER B . n 
B 1 107 LEU 107 153 153 LEU LEU B . n 
B 1 108 TYR 108 154 154 TYR TYR B . n 
B 1 109 ILE 109 155 155 ILE ILE B . n 
B 1 110 PHE 110 156 156 PHE PHE B . n 
B 1 111 HIS 111 157 157 HIS HIS B . n 
B 1 112 SER 112 158 158 SER SER B . n 
B 1 113 TYR 113 159 159 TYR TYR B . n 
B 1 114 VAL 114 160 160 VAL VAL B . n 
B 1 115 ARG 115 161 161 ARG ARG B . n 
B 1 116 LYS 116 162 162 LYS LYS B . n 
B 1 117 ILE 117 163 163 ILE ILE B . n 
B 1 118 LEU 118 164 164 LEU LEU B . n 
B 1 119 ALA 119 165 165 ALA ALA B . n 
B 1 120 ILE 120 166 166 ILE ILE B . n 
B 1 121 SER 121 167 167 SER SER B . n 
B 1 122 LYS 122 168 168 LYS LYS B . n 
B 1 123 LEU 123 169 169 LEU LEU B . n 
B 1 124 TYR 124 170 170 TYR TYR B . n 
B 1 125 THR 125 171 171 THR THR B . n 
B 1 126 PRO 126 172 172 PRO PRO B . n 
B 1 127 VAL 127 173 173 VAL VAL B . n 
B 1 128 ASN 128 174 174 ASN ASN B . n 
B 1 129 LYS 129 175 175 LYS LYS B . n 
B 1 130 TYR 130 176 176 TYR TYR B . n 
B 1 131 PHE 131 177 177 PHE PHE B . n 
B 1 132 PRO 132 178 178 PRO PRO B . n 
B 1 133 ARG 133 179 179 ARG ARG B . n 
B 1 134 ALA 134 180 180 ALA ALA B . n 
B 1 135 LEU 135 181 181 LEU LEU B . n 
B 1 136 LEU 136 182 182 LEU LEU B . n 
B 1 137 VAL 137 183 183 VAL VAL B . n 
B 1 138 ALA 138 184 184 ALA ALA B . n 
B 1 139 LEU 139 185 185 LEU LEU B . n 
B 1 140 GLY 140 186 186 GLY GLY B . n 
B 1 141 VAL 141 187 187 VAL VAL B . n 
B 1 142 ASP 142 188 188 ASP ASP B . n 
B 1 143 PRO 143 189 189 PRO PRO B . n 
B 1 144 GLU 144 190 190 GLU GLU B . n 
B 1 145 ASP 145 191 191 ASP ASP B . n 
B 1 146 VAL 146 192 192 VAL VAL B . n 
B 1 147 PHE 147 193 193 PHE PHE B . n 
B 1 148 ALA 148 194 194 ALA ALA B . n 
B 1 149 ASN 149 195 195 ASN ASN B . n 
B 1 150 GLN 150 196 196 GLN GLN B . n 
B 1 151 ALA 151 197 197 ALA ALA B . n 
B 1 152 GLN 152 198 198 GLN GLN B . n 
B 1 153 TRP 153 199 199 TRP TRP B . n 
B 1 154 GLU 154 200 200 GLU GLU B . n 
B 1 155 TYR 155 201 201 TYR TYR B . n 
B 1 156 PHE 156 202 202 PHE PHE B . n 
B 1 157 VAL 157 203 203 VAL VAL B . n 
B 1 158 ASN 158 204 204 ASN ASN B . n 
B 1 159 MET 159 205 205 MET MET B . n 
B 1 160 VAL 160 206 206 VAL VAL B . n 
B 1 161 ALA 161 207 207 ALA ALA B . n 
B 1 162 TYR 162 208 208 TYR TYR B . n 
B 1 163 ARG 163 209 209 ARG ARG B . n 
B 1 164 ALA 164 210 210 ALA ALA B . n 
B 1 165 GLY 165 211 211 GLY GLY B . n 
B 1 166 ALA 166 212 212 ALA ALA B . n 
B 1 167 PHE 167 213 213 PHE PHE B . n 
B 1 168 ALA 168 214 214 ALA ALA B . n 
B 1 169 ALA 169 215 215 ALA ALA B . n 
B 1 170 PRO 170 216 216 PRO PRO B . n 
B 1 171 ALA 171 217 217 ALA ALA B . n 
B 1 172 SER 172 218 218 SER SER B . n 
B 1 173 MET 173 219 219 MET MET B . n 
B 1 174 THR 174 220 220 THR THR B . n 
B 1 175 TYR 175 221 221 TYR TYR B . n 
B 1 176 TYR 176 222 222 TYR TYR B . n 
B 1 177 GLU 177 223 223 GLU GLU B . n 
B 1 178 ARG 178 224 224 ARG ARG B . n 
B 1 179 HIS 179 225 225 HIS HIS B . n 
B 1 180 ALA 180 226 226 ALA ALA B . n 
B 1 181 TRP 181 227 227 TRP TRP B . n 
B 1 182 MET 182 228 228 MET MET B . n 
B 1 183 SER 183 229 229 SER SER B . n 
B 1 184 ASN 184 230 230 ASN ASN B . n 
B 1 185 GLY 185 231 231 GLY GLY B . n 
B 1 186 LEU 186 232 232 LEU LEU B . n 
B 1 187 TYR 187 233 233 TYR TYR B . n 
B 1 188 VAL 188 234 234 VAL VAL B . n 
B 1 189 ASP 189 235 235 ASP ASP B . n 
B 1 190 GLN 190 236 236 GLN GLN B . n 
B 1 191 ASP 191 237 237 ASP ASP B . n 
B 1 192 VAL 192 238 238 VAL VAL B . n 
B 1 193 THR 193 239 239 THR THR B . n 
B 1 194 ARG 194 240 240 ARG ARG B . n 
B 1 195 ALA 195 241 241 ALA ALA B . n 
B 1 196 GLN 196 242 242 GLN GLN B . n 
B 1 197 ILE 197 243 243 ILE ILE B . n 
B 1 198 TYR 198 244 244 TYR TYR B . n 
B 1 199 MET 199 245 245 MET MET B . n 
B 1 200 PHE 200 246 246 PHE PHE B . n 
B 1 201 LYS 201 247 247 LYS LYS B . n 
B 1 202 PRO 202 248 248 PRO PRO B . n 
B 1 203 THR 203 249 249 THR THR B . n 
B 1 204 MET 204 250 250 MET MET B . n 
B 1 205 LEU 205 251 251 LEU LEU B . n 
B 1 206 TRP 206 252 252 TRP TRP B . n 
B 1 207 LYS 207 253 253 LYS LYS B . n 
B 1 208 TYR 208 254 254 TYR TYR B . n 
B 1 209 GLU 209 255 255 GLU GLU B . n 
B 1 210 ASN 210 256 256 ASN ASN B . n 
B 1 211 LEU 211 257 257 LEU LEU B . n 
B 1 212 GLY 212 258 258 GLY GLY B . n 
B 1 213 THR 213 259 259 THR THR B . n 
B 1 214 THR 214 260 260 THR THR B . n 
B 1 215 GLY 215 261 261 GLY GLY B . n 
B 1 216 THR 216 262 262 THR THR B . n 
B 1 217 LYS 217 263 263 LYS LYS B . n 
B 1 218 LEU 218 264 264 LEU LEU B . n 
B 1 219 VAL 219 265 265 VAL VAL B . n 
B 1 220 PRO 220 266 266 PRO PRO B . n 
B 1 221 LEU 221 267 267 LEU LEU B . n 
B 1 222 MET 222 268 268 MET MET B . n 
B 1 223 MET 223 269 269 MET MET B . n 
B 1 224 PRO 224 270 270 PRO PRO B . n 
B 1 225 LYS 225 271 271 LYS LYS B . n 
B 1 226 ALA 226 272 272 ALA ALA B . n 
B 1 227 GLY 227 273 273 GLY GLY B . n 
B 1 228 ASP 228 274 274 ASP ASP B . n 
B 1 229 ASN 229 275 275 ASN ASN B . n 
B 1 230 ARG 230 276 276 ARG ARG B . n 
B 1 231 LYS 231 277 277 LYS LYS B . n 
B 1 232 LEU 232 278 278 LEU LEU B . n 
B 1 233 VAL 233 279 279 VAL VAL B . n 
B 1 234 ASP 234 280 280 ASP ASP B . n 
B 1 235 PHE 235 281 281 PHE PHE B . n 
B 1 236 GLN 236 282 282 GLN GLN B . n 
B 1 237 VAL 237 283 283 VAL VAL B . n 
B 1 238 LEU 238 284 284 LEU LEU B . n 
B 1 239 PHE 239 285 285 PHE PHE B . n 
B 1 240 ASN 240 286 286 ASN ASN B . n 
B 1 241 ASN 241 287 287 ASN ASN B . n 
B 1 242 LEU 242 288 288 LEU LEU B . n 
B 1 243 VAL 243 289 289 VAL VAL B . n 
B 1 244 SER 244 290 290 SER SER B . n 
B 1 245 THR 245 291 291 THR THR B . n 
B 1 246 MET 246 292 292 MET MET B . n 
B 1 247 LEU 247 293 293 LEU LEU B . n 
B 1 248 GLY 248 294 294 GLY GLY B . n 
B 1 249 ASP 249 295 295 ASP ASP B . n 
B 1 250 GLU 250 296 296 GLU GLU B . n 
B 1 251 ASP 251 297 297 ASP ASP B . n 
B 1 252 PHE 252 298 298 PHE PHE B . n 
B 1 253 GLY 253 299 299 GLY GLY B . n 
B 1 254 ILE 254 300 300 ILE ILE B . n 
B 1 255 MET 255 301 301 MET MET B . n 
B 1 256 SER 256 302 302 SER SER B . n 
B 1 257 GLY 257 303 303 GLY GLY B . n 
B 1 258 ASP 258 304 304 ASP ASP B . n 
B 1 259 VAL 259 305 305 VAL VAL B . n 
B 1 260 PHE 260 306 306 PHE PHE B . n 
B 1 261 LYS 261 307 307 LYS LYS B . n 
B 1 262 ALA 262 308 308 ALA ALA B . n 
B 1 263 PHE 263 309 309 PHE PHE B . n 
B 1 264 GLY 264 310 310 GLY GLY B . n 
B 1 265 ALA 265 311 311 ALA ALA B . n 
B 1 266 ASP 266 312 312 ASP ASP B . n 
B 1 267 GLY 267 313 313 GLY GLY B . n 
B 1 268 LEU 268 314 314 LEU LEU B . n 
B 1 269 VAL 269 315 315 VAL VAL B . n 
B 1 270 LYS 270 316 316 LYS LYS B . n 
B 1 271 LEU 271 317 317 LEU LEU B . n 
B 1 272 LEU 272 318 318 LEU LEU B . n 
B 1 273 ALA 273 319 319 ALA ALA B . n 
B 1 274 VAL 274 320 320 VAL VAL B . n 
B 1 275 ASP 275 321 321 ASP ASP B . n 
B 1 276 SER 276 322 322 SER SER B . n 
B 1 277 THR 277 323 323 THR THR B . n 
B 1 278 THR 278 324 324 THR THR B . n 
B 1 279 MET 279 325 325 MET MET B . n 
B 1 280 THR 280 326 326 THR THR B . n 
B 1 281 LEU 281 327 327 LEU LEU B . n 
B 1 282 PRO 282 328 328 PRO PRO B . n 
B 1 283 THR 283 329 329 THR THR B . n 
B 1 284 TYR 284 330 330 TYR TYR B . n 
B 1 285 ASP 285 331 331 ASP ASP B . n 
B 1 286 PRO 286 332 332 PRO PRO B . n 
B 1 287 LEU 287 333 333 LEU LEU B . n 
B 1 288 ILE 288 334 334 ILE ILE B . n 
B 1 289 LEU 289 335 335 LEU LEU B . n 
B 1 290 ALA 290 336 336 ALA ALA B . n 
B 1 291 GLN 291 337 337 GLN GLN B . n 
B 1 292 ILE 292 338 338 ILE ILE B . n 
B 1 293 HIS 293 339 339 HIS HIS B . n 
B 1 294 SER 294 340 340 SER SER B . n 
B 1 295 ALA 295 341 341 ALA ALA B . n 
B 1 296 ARG 296 342 342 ARG ARG B . n 
B 1 297 ALA 297 343 343 ALA ALA B . n 
B 1 298 VAL 298 344 344 VAL VAL B . n 
B 1 299 GLY 299 345 345 GLY GLY B . n 
B 1 300 ALA 300 346 346 ALA ALA B . n 
B 1 301 PRO 301 347 347 PRO PRO B . n 
B 1 302 ILE 302 348 348 ILE ILE B . n 
B 1 303 LEU 303 349 349 LEU LEU B . n 
B 1 304 GLU 304 350 350 GLU GLU B . n 
B 1 305 THR 305 351 351 THR THR B . n 
B 1 306 SER 306 352 352 SER SER B . n 
B 1 307 THR 307 353 353 THR THR B . n 
B 1 308 LEU 308 354 354 LEU LEU B . n 
B 1 309 THR 309 355 355 THR THR B . n 
B 1 310 GLY 310 356 356 GLY GLY B . n 
B 1 311 PHE 311 357 357 PHE PHE B . n 
B 1 312 PRO 312 358 358 PRO PRO B . n 
B 1 313 GLY 313 359 359 GLY GLY B . n 
B 1 314 ARG 314 360 360 ARG ARG B . n 
B 1 315 GLN 315 361 361 GLN GLN B . n 
B 1 316 TRP 316 362 362 TRP TRP B . n 
B 1 317 GLN 317 363 363 GLN GLN B . n 
B 1 318 ILE 318 364 364 ILE ILE B . n 
B 1 319 THR 319 365 365 THR THR B . n 
B 1 320 GLN 320 366 366 GLN GLN B . n 
B 1 321 ASN 321 367 367 ASN ASN B . n 
B 1 322 PRO 322 368 368 PRO PRO B . n 
B 1 323 ASP 323 369 369 ASP ASP B . n 
B 1 324 VAL 324 370 370 VAL VAL B . n 
B 1 325 ASN 325 371 371 ASN ASN B . n 
B 1 326 ASN 326 372 372 ASN ASN B . n 
B 1 327 GLY 327 373 373 GLY GLY B . n 
B 1 328 ALA 328 374 374 ALA ALA B . n 
B 1 329 ILE 329 375 375 ILE ILE B . n 
B 1 330 ILE 330 376 376 ILE ILE B . n 
B 1 331 PHE 331 377 377 PHE PHE B . n 
B 1 332 HIS 332 378 378 HIS HIS B . n 
B 1 333 PRO 333 379 379 PRO PRO B . n 
B 1 334 SER 334 380 380 SER SER B . n 
B 1 335 PHE 335 381 381 PHE PHE B . n 
B 1 336 GLY 336 382 382 GLY GLY B . n 
B 1 337 TYR 337 383 383 TYR TYR B . n 
B 1 338 ASP 338 384 384 ASP ASP B . n 
B 1 339 GLY 339 385 385 GLY GLY B . n 
B 1 340 GLN 340 386 386 GLN GLN B . n 
B 1 341 ASP 341 387 387 ASP ASP B . n 
B 1 342 HIS 342 388 388 HIS HIS B . n 
B 1 343 GLU 343 389 389 GLU GLU B . n 
B 1 344 GLU 344 390 390 GLU GLU B . n 
B 1 345 LEU 345 391 391 LEU LEU B . n 
B 1 346 SER 346 392 392 SER SER B . n 
B 1 347 PHE 347 393 393 PHE PHE B . n 
B 1 348 ARG 348 394 394 ARG ARG B . n 
B 1 349 ALA 349 395 395 ALA ALA B . n 
B 1 350 MET 350 396 396 MET MET B . n 
B 1 351 CYS 351 397 397 CYS CYS B . n 
B 1 352 SER 352 398 398 SER SER B . n 
B 1 353 ASN 353 399 399 ASN ASN B . n 
B 1 354 MET 354 400 400 MET MET B . n 
B 1 355 ILE 355 401 401 ILE ILE B . n 
B 1 356 LEU 356 402 402 LEU LEU B . n 
B 1 357 ASN 357 403 403 ASN ASN B . n 
B 1 358 LEU 358 404 404 LEU LEU B . n 
B 1 359 PRO 359 405 405 PRO PRO B . n 
B 1 360 GLY 360 406 406 GLY GLY B . n 
B 1 361 GLU 361 407 407 GLU GLU B . n 
B 1 362 ALA 362 408 408 ALA ALA B . n 
B 1 363 HIS 363 409 409 HIS HIS B . n 
B 1 364 SER 364 410 410 SER SER B . n 
B 1 365 ALA 365 411 411 ALA ALA B . n 
B 1 366 GLU 366 412 412 GLU GLU B . n 
B 1 367 MET 367 413 413 MET MET B . n 
B 1 368 ILE 368 414 414 ILE ILE B . n 
B 1 369 ILE 369 415 415 ILE ILE B . n 
B 1 370 GLU 370 416 416 GLU GLU B . n 
B 1 371 ALA 371 417 417 ALA ALA B . n 
B 1 372 THR 372 418 418 THR THR B . n 
B 1 373 ARG 373 419 419 ARG ARG B . n 
B 1 374 LEU 374 420 420 LEU LEU B . n 
B 1 375 ALA 375 421 421 ALA ALA B . n 
B 1 376 THR 376 422 422 THR THR B . n 
B 1 377 MET 377 423 423 MET MET B . n 
B 1 378 PHE 378 424 424 PHE PHE B . n 
B 1 379 GLN 379 425 425 GLN GLN B . n 
B 1 380 VAL 380 426 426 VAL VAL B . n 
B 1 381 LYS 381 427 427 LYS LYS B . n 
B 1 382 ALA 382 428 428 ALA ALA B . n 
B 1 383 VAL 383 429 429 VAL VAL B . n 
B 1 384 PRO 384 430 430 PRO PRO B . n 
B 1 385 ALA 385 431 431 ALA ALA B . n 
B 1 386 GLY 386 432 432 GLY GLY B . n 
B 1 387 ASP 387 433 433 ASP ASP B . n 
B 1 388 THR 388 434 434 THR THR B . n 
B 1 389 SER 389 435 435 SER SER B . n 
B 1 390 LYS 390 436 436 LYS LYS B . n 
B 1 391 PRO 391 437 437 PRO PRO B . n 
B 1 392 VAL 392 438 438 VAL VAL B . n 
B 1 393 LEU 393 439 439 LEU LEU B . n 
B 1 394 TYR 394 440 440 TYR TYR B . n 
B 1 395 LEU 395 441 441 LEU LEU B . n 
B 1 396 PRO 396 442 442 PRO PRO B . n 
B 1 397 ASN 397 443 443 ASN ASN B . n 
B 1 398 GLY 398 444 444 GLY GLY B . n 
B 1 399 PHE 399 445 445 PHE PHE B . n 
B 1 400 GLY 400 446 446 GLY GLY B . n 
B 1 401 THR 401 447 447 THR THR B . n 
B 1 402 GLU 402 448 448 GLU GLU B . n 
B 1 403 VAL 403 449 449 VAL VAL B . n 
B 1 404 VAL 404 450 450 VAL VAL B . n 
B 1 405 ASN 405 451 451 ASN ASN B . n 
B 1 406 ASP 406 452 452 ASP ASP B . n 
B 1 407 TYR 407 453 453 TYR TYR B . n 
B 1 408 THR 408 454 454 THR THR B . n 
B 1 409 MET 409 455 455 MET MET B . n 
B 1 410 ILE 410 456 456 ILE ILE B . n 
B 1 411 SER 411 457 457 SER SER B . n 
B 1 412 VAL 412 458 458 VAL VAL B . n 
B 1 413 ASP 413 459 459 ASP ASP B . n 
B 1 414 LYS 414 460 460 LYS LYS B . n 
B 1 415 ALA 415 461 461 ALA ALA B . n 
B 1 416 THR 416 462 462 THR THR B . n 
B 1 417 PRO 417 463 463 PRO PRO B . n 
B 1 418 HIS 418 464 464 HIS HIS B . n 
B 1 419 ASP 419 465 465 ASP ASP B . n 
B 1 420 LEU 420 466 466 LEU LEU B . n 
B 1 421 THR 421 467 467 THR THR B . n 
B 1 422 ILE 422 468 468 ILE ILE B . n 
B 1 423 HIS 423 469 469 HIS HIS B . n 
B 1 424 THR 424 470 470 THR THR B . n 
B 1 425 PHE 425 471 471 PHE PHE B . n 
B 1 426 PHE 426 472 472 PHE PHE B . n 
B 1 427 ASN 427 473 473 ASN ASN B . n 
B 1 428 ASN 428 474 474 ASN ASN B . n 
B 1 429 ILE 429 475 475 ILE ILE B . n 
B 1 430 LEU 430 476 476 LEU LEU B . n 
B 1 431 VAL 431 477 477 VAL VAL B . n 
B 1 432 PRO 432 478 478 PRO PRO B . n 
B 1 433 ASN 433 479 479 ASN ASN B . n 
B 1 434 ALA 434 480 480 ALA ALA B . n 
B 1 435 LYS 435 481 481 LYS LYS B . n 
B 1 436 GLU 436 482 482 GLU GLU B . n 
B 1 437 ASN 437 483 483 ASN ASN B . n 
B 1 438 TYR 438 484 484 TYR TYR B . n 
B 1 439 VAL 439 485 485 VAL VAL B . n 
B 1 440 ALA 440 486 486 ALA ALA B . n 
B 1 441 ASN 441 487 487 ASN ASN B . n 
B 1 442 LEU 442 488 488 LEU LEU B . n 
B 1 443 GLU 443 489 489 GLU GLU B . n 
B 1 444 LEU 444 490 490 LEU LEU B . n 
B 1 445 LEU 445 491 491 LEU LEU B . n 
B 1 446 ASN 446 492 492 ASN ASN B . n 
B 1 447 ASN 447 493 493 ASN ASN B . n 
B 1 448 ILE 448 494 494 ILE ILE B . n 
B 1 449 ILE 449 495 495 ILE ILE B . n 
B 1 450 GLN 450 496 496 GLN GLN B . n 
B 1 451 PHE 451 497 497 PHE PHE B . n 
B 1 452 ASP 452 498 498 ASP ASP B . n 
B 1 453 TRP 453 499 499 TRP TRP B . n 
B 1 454 ALA 454 500 500 ALA ALA B . n 
B 1 455 PRO 455 501 501 PRO PRO B . n 
B 1 456 GLN 456 502 502 GLN GLN B . n 
B 1 457 LEU 457 503 503 LEU LEU B . n 
B 1 458 TYR 458 504 504 TYR TYR B . n 
B 1 459 LEU 459 505 505 LEU LEU B . n 
B 1 460 THR 460 506 506 THR THR B . n 
B 1 461 TYR 461 507 507 TYR TYR B . n 
B 1 462 GLY 462 508 508 GLY GLY B . n 
B 1 463 ILE 463 509 509 ILE ILE B . n 
B 1 464 ALA 464 510 510 ALA ALA B . n 
B 1 465 GLN 465 511 511 GLN GLN B . n 
B 1 466 GLU 466 512 512 GLU GLU B . n 
B 1 467 SER 467 513 513 SER SER B . n 
B 1 468 PHE 468 514 514 PHE PHE B . n 
B 1 469 GLY 469 515 515 GLY GLY B . n 
B 1 470 PRO 470 516 516 PRO PRO B . n 
B 1 471 PHE 471 517 517 PHE PHE B . n 
B 1 472 ALA 472 518 518 ALA ALA B . n 
B 1 473 GLN 473 519 519 GLN GLN B . n 
B 1 474 LEU 474 520 520 LEU LEU B . n 
B 1 475 ASN 475 521 521 ASN ASN B . n 
B 1 476 ASP 476 522 522 ASP ASP B . n 
B 1 477 TRP 477 523 523 TRP TRP B . n 
B 1 478 THR 478 524 524 THR THR B . n 
B 1 479 ILE 479 525 525 ILE ILE B . n 
B 1 480 LEU 480 526 526 LEU LEU B . n 
B 1 481 THR 481 527 527 THR THR B . n 
B 1 482 GLY 482 528 528 GLY GLY B . n 
B 1 483 GLU 483 529 529 GLU GLU B . n 
B 1 484 THR 484 530 530 THR THR B . n 
B 1 485 LEU 485 531 531 LEU LEU B . n 
B 1 486 ALA 486 532 532 ALA ALA B . n 
B 1 487 ARG 487 533 533 ARG ARG B . n 
B 1 488 MET 488 534 534 MET MET B . n 
B 1 489 HIS 489 535 535 HIS HIS B . n 
B 1 490 GLU 490 536 536 GLU GLU B . n 
B 1 491 VAL 491 537 537 VAL VAL B . n 
B 1 492 CYS 492 538 538 CYS CYS B . n 
B 1 493 VAL 493 539 539 VAL VAL B . n 
B 1 494 THR 494 540 540 THR THR B . n 
B 1 495 SER 495 541 541 SER SER B . n 
B 1 496 MET 496 542 542 MET MET B . n 
B 1 497 PHE 497 543 543 PHE PHE B . n 
B 1 498 ASP 498 544 544 ASP ASP B . n 
B 1 499 VAL 499 545 545 VAL VAL B . n 
B 1 500 PRO 500 546 546 PRO PRO B . n 
B 1 501 GLN 501 547 547 GLN GLN B . n 
# 
_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                   9EPF 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9EPF 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.003 ? 8123  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.507 ? 11092 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 3.959 ? 1086  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.039 ? 1230  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 1426  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9EPF 
_struct.title                        'Human Picobirnavirus CP VLP' 
_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        9EPF 
_struct_keywords.text            'Picobirnavirus, CryoEM, Assembly, VLP, VIRUS LIKE PARTICLE' 
_struct_keywords.pdbx_keywords   'VIRUS LIKE PARTICLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAPSD_HPBVH 
_struct_ref.pdbx_db_accession          Q50LE5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VAWYARYPHILEEATRLPFAYPIGQYYDTGYSVASATEWSKYVDTSLTIPGVMCVNFTPTPGESYNKNSPINIAAQNVYT
YVRHMNSGHANYEQADLMMYLLAMDSLYIFHSYVRKILAISKLYTPVNKYFPRALLVALGVDPEDVFANQAQWEYFVNMV
AYRAGAFAAPASMTYYERHAWMSNGLYVDQDVTRAQIYMFKPTMLWKYENLGTTGTKLVPLMMPKAGDNRKLVDFQVLFN
NLVSTMLGDEDFGIMSGDVFKAFGADGLVKLLAVDSTTMTLPTYDPLILAQIHSARAVGAPILETSTLTGFPGRQWQITQ
NPDVNNGAIIFHPSFGYDGQDHEELSFRAMCSNMILNLPGEAHSAEMIIEATRLATMFQVKAVPAGDTSKPVLYLPNGFG
TEVVNDYTMISVDKATPHDLTIHTFFNNILVPNAKENYVANLELLNNIIQFDWAPQLYLTYGIAQESFGPFAQLNDWTIL
TGETLARMHEVCVTSMFDV
;
_struct_ref.pdbx_align_begin           47 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EPF A 1 ? 499 ? Q50LE5 47 ? 545 ? 47 545 
2 1 9EPF B 1 ? 499 ? Q50LE5 47 ? 545 ? 47 545 
# 
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 9EPF PRO A 500 ? UNP Q50LE5 ? ? 'expression tag' 546 1 
1 9EPF GLN A 501 ? UNP Q50LE5 ? ? 'expression tag' 547 2 
2 9EPF PRO B 500 ? UNP Q50LE5 ? ? 'expression tag' 546 3 
2 9EPF GLN B 501 ? UNP Q50LE5 ? ? 'expression tag' 547 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       'UCSF CHIMERA 1.14_b42094.' 
_pdbx_struct_assembly.oligomeric_details   120-meric 
_pdbx_struct_assembly.oligomeric_count     120 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   
;1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60
;
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1  'identity operation'       1_555 x,y,z 1.0       0.0       0.0       0.0      -0.0      1.0       -0.0      0.0      -0.0      
-0.0      1.0       0.0      
2  'point symmetry operation' ?     ?     0.499178  -0.809381 0.309392  -0.59480 0.809982  0.309017  -0.498436 -0.98426 0.307817  
0.499409  0.809839  0.36747  
3  'point symmetry operation' ?     ?     -0.311170 -0.499625 0.808423  0.01862  0.501196  -0.809016 -0.307076 -1.95335 0.807450  
0.309626  0.502151  -0.00957 
4  'point symmetry operation' ?     ?     -0.311170 0.501196  0.807450  0.99253  -0.499625 -0.809016 0.309626  -1.56802 0.808423  
-0.307076 0.502151  -0.61007 
5  'point symmetry operation' ?     ?     0.499178  0.809982  0.307817  0.98103  -0.809382 0.309017  0.499409  -0.36079 0.309392  
-0.498436 0.809839  -0.60415 
6  'point symmetry operation' ?     ?     -0.811189 0.307577  0.497361  -0.25957 0.307577  -0.498949 0.810213  0.45086  0.497361  
0.810213  0.310139  -0.18028 
7  'point symmetry operation' ?     ?     -0.002699 0.999995  -0.001500 0.10296  -0.001207 0.001497  0.999998  1.05674  0.999996  
0.002701  0.001203  -1.15960 
8  'point symmetry operation' ?     ?     0.808169  0.310452  -0.500483 -0.88024 0.308427  0.500848  0.808718  1.42345  0.501734  
-0.807943 0.309018  -1.75662 
9  'point symmetry operation' ?     ?     0.500823  -0.808128 -0.310010 -1.85042 0.808574  0.309017  0.500715  1.04422  -0.308844 
-0.501436 0.808194  -1.14627 
10 'point symmetry operation' ?     ?     -0.499995 -0.809904 0.306692  -1.46682 0.808049  -0.308891 0.501640  0.44312  -0.311546 
0.498640  0.808887  -0.17204 
11 'point symmetry operation' ?     ?     -0.498606 -0.809418 0.310217  -1.45798 -0.809418 0.306672  -0.500794 -2.39494 0.310217  
-0.500794 -0.808066 -3.89238 
12 'point symmetry operation' ?     ?     -0.809017 0.308363  0.500404  -0.25074 -0.309798 0.499794  -0.808846 -2.39937 -0.499517 
-0.809394 -0.308811 -3.88093 
13 'point symmetry operation' ?     ?     -0.000041 0.999999  0.001244  0.11084  0.001203  0.001244  -0.999999 -3.00425 -0.999999 
-0.000040 -0.001203 -2.90065 
14 'point symmetry operation' ?     ?     0.810343  0.309672  -0.497440 -0.87294 -0.306208 -0.499998 -0.810086 -3.37367 -0.499580 
0.808768  -0.310346 -2.30625 
15 'point symmetry operation' ?     ?     0.502213  -0.808609 -0.306485 -1.84252 -0.807200 -0.311233 -0.501560 -2.99709 0.310178  
0.499285  -0.809014 -2.91918 
16 'point symmetry operation' ?     ?     0.309795  0.501841  -0.807578 -1.74942 0.501841  -0.807723 -0.309419 -1.95629 -0.807578 
-0.309419 -0.502073 -4.05302 
17 'point symmetry operation' ?     ?     0.312538  -0.498977 -0.808296 -2.72439 -0.498977 -0.810308 0.307283  -1.57348 -0.808296 
0.307283  -0.502230 -3.45262 
18 'point symmetry operation' ?     ?     -0.496957 -0.810826 -0.309184 -2.71619 -0.810826 0.306924  0.498357  -0.36622 -0.309184 
0.498357  -0.809966 -3.45884 
19 'point symmetry operation' ?     ?     -0.999996 -0.002741 0.0       -1.73616 -0.002741 0.999996  -0.000256 -0.00290 0.0       
-0.000256 -1.0      -4.06309 
20 'point symmetry operation' ?     ?     -0.501396 0.808532  -0.308024 -1.13866 0.808532  0.311107  -0.499489 -0.98562 -0.308024 
-0.499489 -0.809711 -4.43031 
21 'point symmetry operation' ?     ?     -0.499999 -0.808652 -0.309972 -2.71831 0.809459  -0.309143 -0.499205 -1.58904 0.307858  
-0.500512 0.809143  -0.60892 
22 'point symmetry operation' ?     ?     -0.999996 -0.0      -0.002662 -1.73889 -0.0      -1.0      0.000252  -1.94967 -0.002662 
0.000252  0.999996  -0.00207 
23 'point symmetry operation' ?     ?     -0.499995 0.808049  -0.311546 -1.14507 -0.809904 -0.308891 0.498640  -0.96532 0.306692  
0.501640  0.808887  0.36674  
24 'point symmetry operation' ?     ?     0.309019  0.498800  -0.809757 -1.75748 -0.500993 0.809094  0.307203  0.00367  0.808402  
0.310751  0.499921  -0.01218 
25 'point symmetry operation' ?     ?     0.309017  -0.500377 -0.808784 -2.72980 0.499829  0.808938  -0.309500 -0.38180 0.809123  
-0.308613 0.500079  -0.61517 
26 'point symmetry operation' ?     ?     0.002703  -0.001455 -0.999995 -2.89723 -0.999996 -0.001245 -0.002701 -1.84853 -0.001241 
0.999998  -0.001458 -1.06037 
27 'point symmetry operation' ?     ?     -0.307645 -0.502044 -0.808273 -3.26488 -0.501015 0.807644  -0.310957 -1.25350 0.808912  
0.309293  -0.499999 -2.04442 
28 'point symmetry operation' ?     ?     -0.809017 -0.309798 -0.499517 -2.88477 0.308363  0.499794  -0.809394 -1.86469 0.500404  
-0.808846 -0.308811 -3.01372 
29 'point symmetry operation' ?     ?     -0.808534 0.309607  -0.500417 -2.28220 0.309607  -0.499358 -0.809188 -2.83746 -0.500417 
-0.809188 0.307891  -2.62873 
30 'point symmetry operation' ?     ?     -0.306863 0.500173  -0.809730 -2.28990 -0.499004 -0.809016 -0.310625 -2.82748 -0.810451 
0.308739  0.497846  -1.42149 
31 'point symmetry operation' ?     ?     0.807682  0.311949  0.500338  1.15388  -0.308237 -0.499997 0.809316  -0.08574 0.502633  
-0.807892 -0.307684 -3.00857 
32 'point symmetry operation' ?     ?     0.809862  -0.307452 0.499596  0.55030  -0.309732 0.499154  0.809266  0.88713  -0.498185 
-0.810135 0.309018  -2.62543 
33 'point symmetry operation' ?     ?     0.309019  -0.500993 0.808402  0.55479  0.498800  0.809094  0.310751  0.87745  -0.809757 
0.307202  0.499921  -1.41817 
34 'point symmetry operation' ?     ?     -0.002699 -0.001207 0.999996  1.16115  0.999995  0.001497  0.002701  -0.10141 -0.001500 
0.999998  0.001203  -1.05519 
35 'point symmetry operation' ?     ?     0.305491  0.501219  0.809601  1.53141  0.501219  -0.807566 0.310832  -0.69669 0.809601  
0.310832  -0.497925 -2.03811 
36 'point symmetry operation' ?     ?     -0.310386 0.498158  0.809629  0.99468  0.498773  0.810385  -0.307410 -0.37706 -0.809250 
0.308406  -0.500000 -3.44782 
37 'point symmetry operation' ?     ?     0.497779  0.809496  0.311339  0.98650  0.810748  -0.306798 -0.498561 -1.58432 -0.308065 
0.500590  -0.809015 -3.45376 
38 'point symmetry operation' ?     ?     0.999993  0.002741  0.002661  0.00807  0.002741  -0.999996 0.000004  -1.94780 0.002661  
0.000004  -0.999996 -4.06052 
39 'point symmetry operation' ?     ?     0.502213  -0.807200 0.310178  -0.58845 -0.808609 -0.311233 0.499285  -0.96517 -0.306485 
-0.501560 -0.809014 -4.42958 
40 'point symmetry operation' ?     ?     -0.307645 -0.501015 0.808912  0.02131  -0.502044 0.807644  0.309293  0.00560  -0.808273 
-0.310957 -0.499999 -4.05091 
41 'point symmetry operation' ?     ?     -0.499999 0.809459  0.307858  0.11457  -0.808652 -0.309143 -0.500512 -2.99418 -0.309972 
-0.499205 0.809143  -1.14315 
42 'point symmetry operation' ?     ?     0.500823  0.808574  -0.308844 -0.27162 -0.808128 0.309017  -0.501436 -2.39284 -0.310010 
0.500716  0.808194  -0.17009 
43 'point symmetry operation' ?     ?     0.809862  -0.309732 -0.498185 -1.47884 -0.307452 0.499154  -0.810135 -2.40058 0.499596  
0.809266  0.309018  -0.18154 
44 'point symmetry operation' ?     ?     0.000038  -0.999999 0.001497  -1.83876 0.001459  -0.001496 -0.999998 -3.00670 0.999999  
0.000040  0.001459  -1.16168 
45 'point symmetry operation' ?     ?     -0.809501 -0.308300 0.499659  -0.85398 -0.308300 -0.501051 -0.808640 -3.37357 0.499659  
-0.808640 0.310553  -1.75598 
46 'point symmetry operation' ?     ?     0.807682  -0.308237 0.502633  0.55381  0.311949  -0.499997 -0.807892 -2.83343 0.500338  
0.809316  -0.307684 -1.43363 
47 'point symmetry operation' ?     ?     0.308230  -0.497954 0.810578  0.56149  -0.497954 -0.810463 -0.308532 -2.82373 0.810578  
-0.308532 -0.497766 -2.64088 
48 'point symmetry operation' ?     ?     0.000038  0.001459  0.999999  1.16613  -0.999999 -0.001496 0.000040  -1.84321 0.001497  
-0.999998 0.001459  -3.00225 
49 'point symmetry operation' ?     ?     0.309017  0.499829  0.809123  1.53214  -0.500377 0.808938  -0.308613 -1.24692 -0.808784 
-0.309500 0.500079  -2.01835 
50 'point symmetry operation' ?     ?     0.808169  0.308427  0.501734  1.15371  0.310452  0.500848  -0.807943 -1.85891 -0.500483 
0.808718  0.309018  -1.04889 
51 'point symmetry operation' ?     ?     -0.310386 0.498773  -0.809250 -2.29335 0.498158  0.810385  0.308406  0.87339  0.809629  
-0.307410 -0.500000 -2.64514 
52 'point symmetry operation' ?     ?     -0.000041 0.001203  -0.999999 -2.89703 0.999999  0.001244  -0.000040 -0.10722 0.001244  
-0.999999 -0.001203 -3.00788 
53 'point symmetry operation' ?     ?     -0.306863 -0.499004 -0.810451 -3.26566 0.500173  -0.809016 0.308739  -0.70326 -0.809730 
-0.310625 0.497846  -2.02480 
54 'point symmetry operation' ?     ?     -0.806834 -0.310578 -0.502554 -2.88980 -0.310578 -0.500644 0.808020  -0.09103 -0.502554 
0.808020  0.307478  -1.05450 
55 'point symmetry operation' ?     ?     -0.809011 0.306082  -0.501812 -2.28888 -0.311823 0.500202  0.807815  0.88339  0.498265  
0.810008  -0.309225 -1.43789 
56 'point symmetry operation' ?     ?     0.002703  -0.999996 -0.001241 -1.84201 -0.001455 -0.001245 0.999998  1.05385  -0.999995 
-0.002701 -0.001458 -2.90376 
57 'point symmetry operation' ?     ?     -0.809011 -0.311823 0.498265  -0.85982 0.306082  0.500202  0.810008  1.42341  -0.501812 
0.807815  -0.309225 -2.30684 
58 'point symmetry operation' ?     ?     -0.503037 0.807278  0.308637  0.11139  0.807278  0.311359  0.501357  1.04668  0.308637  
0.501357  -0.808322 -2.91709 
59 'point symmetry operation' ?     ?     0.497779  0.810748  -0.308065 -0.27055 0.809496  -0.306798 0.500590  0.44429  0.311339  
-0.498561 -0.809015 -3.89116 
60 'point symmetry operation' ?     ?     0.810343  -0.306208 -0.499580 -1.47782 0.309672  -0.499998 0.808768  0.44872  -0.497440 
-0.810086 -0.310346 -3.88293 
# 
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 VAL A 1   ? TYR A 7   ? VAL A 47  TYR A 53  1 ? 7  
HELX_P HELX_P2  AA2 TYR A 7   ? THR A 15  ? TYR A 53  THR A 61  1 ? 9  
HELX_P HELX_P3  AA3 SER A 35  ? TRP A 39  ? SER A 81  TRP A 85  5 ? 5  
HELX_P HELX_P4  AA4 SER A 69  ? MET A 85  ? SER A 115 MET A 131 1 ? 17 
HELX_P HELX_P5  AA5 GLU A 93  ? SER A 121 ? GLU A 139 SER A 167 1 ? 29 
HELX_P HELX_P6  AA6 PRO A 132 ? GLY A 140 ? PRO A 178 GLY A 186 1 ? 9  
HELX_P HELX_P7  AA7 ASP A 142 ? ASN A 149 ? ASP A 188 ASN A 195 1 ? 8  
HELX_P HELX_P8  AA8 ASN A 149 ? GLY A 165 ? ASN A 195 GLY A 211 1 ? 17 
HELX_P HELX_P9  AA9 THR A 174 ? ASN A 184 ? THR A 220 ASN A 230 1 ? 11 
HELX_P HELX_P10 AB1 LYS A 231 ? VAL A 243 ? LYS A 277 VAL A 289 1 ? 13 
HELX_P HELX_P11 AB2 ASP A 249 ? PHE A 263 ? ASP A 295 PHE A 309 1 ? 15 
HELX_P HELX_P12 AB3 GLY A 264 ? LEU A 268 ? GLY A 310 LEU A 314 5 ? 5  
HELX_P HELX_P13 AB4 ASP A 285 ? SER A 294 ? ASP A 331 SER A 340 1 ? 10 
HELX_P HELX_P14 AB5 VAL A 324 ? GLY A 327 ? VAL A 370 GLY A 373 5 ? 4  
HELX_P HELX_P15 AB6 GLU A 344 ? SER A 352 ? GLU A 390 SER A 398 5 ? 9  
HELX_P HELX_P16 AB7 SER A 364 ? ALA A 371 ? SER A 410 ALA A 417 1 ? 8  
HELX_P HELX_P17 AB8 GLU A 436 ? PHE A 451 ? GLU A 482 PHE A 497 1 ? 16 
HELX_P HELX_P18 AB9 THR A 481 ? PHE A 497 ? THR A 527 PHE A 543 1 ? 17 
HELX_P HELX_P19 AC1 ALA B 2   ? TYR B 7   ? ALA B 48  TYR B 53  1 ? 6  
HELX_P HELX_P20 AC2 TYR B 7   ? THR B 15  ? TYR B 53  THR B 61  1 ? 9  
HELX_P HELX_P21 AC3 VAL B 33  ? GLU B 38  ? VAL B 79  GLU B 84  5 ? 6  
HELX_P HELX_P22 AC4 SER B 69  ? ASN B 86  ? SER B 115 ASN B 132 1 ? 18 
HELX_P HELX_P23 AC5 GLU B 93  ? SER B 121 ? GLU B 139 SER B 167 1 ? 29 
HELX_P HELX_P24 AC6 PRO B 132 ? GLY B 140 ? PRO B 178 GLY B 186 1 ? 9  
HELX_P HELX_P25 AC7 ASP B 142 ? ASN B 149 ? ASP B 188 ASN B 195 1 ? 8  
HELX_P HELX_P26 AC8 ASN B 149 ? GLY B 165 ? ASN B 195 GLY B 211 1 ? 17 
HELX_P HELX_P27 AC9 MET B 173 ? ASN B 184 ? MET B 219 ASN B 230 1 ? 12 
HELX_P HELX_P28 AD1 LYS B 231 ? VAL B 243 ? LYS B 277 VAL B 289 1 ? 13 
HELX_P HELX_P29 AD2 ASP B 249 ? PHE B 263 ? ASP B 295 PHE B 309 1 ? 15 
HELX_P HELX_P30 AD3 GLY B 264 ? LEU B 268 ? GLY B 310 LEU B 314 5 ? 5  
HELX_P HELX_P31 AD4 ASP B 285 ? SER B 294 ? ASP B 331 SER B 340 1 ? 10 
HELX_P HELX_P32 AD5 VAL B 324 ? ALA B 328 ? VAL B 370 ALA B 374 5 ? 5  
HELX_P HELX_P33 AD6 GLU B 344 ? SER B 352 ? GLU B 390 SER B 398 5 ? 9  
HELX_P HELX_P34 AD7 SER B 364 ? ALA B 371 ? SER B 410 ALA B 417 1 ? 8  
HELX_P HELX_P35 AD8 GLU B 436 ? PHE B 451 ? GLU B 482 PHE B 497 1 ? 16 
HELX_P HELX_P36 AD9 THR B 481 ? PHE B 497 ? THR B 527 PHE B 543 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 131 A . ? PHE 177 A PRO 132 A ? PRO 178 A 1 -6.00 
2 THR 416 A . ? THR 462 A PRO 417 A ? PRO 463 A 1 1.04  
3 PHE 131 B . ? PHE 177 B PRO 132 B ? PRO 178 B 1 -5.37 
4 THR 416 B . ? THR 462 B PRO 417 B ? PRO 463 B 1 1.46  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
AA9 ? 6 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 2 ? 
AB5 ? 3 ? 
# 
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 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? parallel      
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? 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 TYR A 27  ? ASP A 28  ? TYR A 73  ASP A 74  
AA1 2 SER A 46  ? LEU A 47  ? SER A 92  LEU A 93  
AA2 1 THR A 283 ? TYR A 284 ? THR A 329 TYR A 330 
AA2 2 TYR A 187 ? VAL A 188 ? TYR A 233 VAL A 234 
AA2 3 ILE A 197 ? PRO A 202 ? ILE A 243 PRO A 248 
AA2 4 VAL A 52  ? PHE A 57  ? VAL A 98  PHE A 103 
AA2 5 ASP A 406 ? VAL A 412 ? ASP A 452 VAL A 458 
AA2 6 LEU A 420 ? PHE A 425 ? LEU A 466 PHE A 471 
AA3 1 MET A 204 ? LEU A 205 ? MET A 250 LEU A 251 
AA3 2 LEU A 221 ? MET A 222 ? LEU A 267 MET A 268 
AA4 1 LYS A 217 ? LEU A 218 ? LYS A 263 LEU A 264 
AA4 2 ILE A 318 ? GLN A 320 ? ILE A 364 GLN A 366 
AA4 3 ILE A 329 ? ILE A 330 ? ILE A 375 ILE A 376 
AA5 1 ILE A 355 ? ASN A 357 ? ILE A 401 ASN A 403 
AA5 2 TRP A 477 ? ILE A 479 ? TRP A 523 ILE A 525 
AA6 1 PHE A 378 ? LYS A 381 ? PHE A 424 LYS A 427 
AA6 2 TYR A 394 ? PRO A 396 ? TYR A 440 PRO A 442 
AA7 1 ASN A 428 ? VAL A 431 ? ASN A 474 VAL A 477 
AA7 2 TYR A 458 ? TYR A 461 ? TYR A 504 TYR A 507 
AA7 3 GLU A 466 ? SER A 467 ? GLU A 512 SER A 513 
AA8 1 TYR B 27  ? ASP B 28  ? TYR B 73  ASP B 74  
AA8 2 SER B 46  ? LEU B 47  ? SER B 92  LEU B 93  
AA9 1 PRO B 282 ? THR B 283 ? PRO B 328 THR B 329 
AA9 2 LEU B 186 ? VAL B 188 ? LEU B 232 VAL B 234 
AA9 3 ILE B 197 ? PRO B 202 ? ILE B 243 PRO B 248 
AA9 4 VAL B 52  ? PRO B 59  ? VAL B 98  PRO B 105 
AA9 5 GLU B 402 ? VAL B 412 ? GLU B 448 VAL B 458 
AA9 6 LEU B 420 ? PHE B 425 ? LEU B 466 PHE B 471 
AB1 1 MET B 204 ? LEU B 205 ? MET B 250 LEU B 251 
AB1 2 LEU B 221 ? MET B 222 ? LEU B 267 MET B 268 
AB2 1 THR B 216 ? LEU B 218 ? THR B 262 LEU B 264 
AB2 2 ILE B 318 ? GLN B 320 ? ILE B 364 GLN B 366 
AB3 1 ILE B 355 ? LEU B 358 ? ILE B 401 LEU B 404 
AB3 2 ASP B 476 ? ILE B 479 ? ASP B 522 ILE B 525 
AB4 1 PHE B 378 ? LYS B 381 ? PHE B 424 LYS B 427 
AB4 2 TYR B 394 ? PRO B 396 ? TYR B 440 PRO B 442 
AB5 1 ASN B 428 ? VAL B 431 ? ASN B 474 VAL B 477 
AB5 2 TYR B 458 ? TYR B 461 ? TYR B 504 TYR B 507 
AB5 3 GLU B 466 ? SER B 467 ? GLU B 512 SER B 513 
# 
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 TYR A 27  ? N TYR A 73  O LEU A 47  ? O LEU A 93  
AA2 1 2 O THR A 283 ? O THR A 329 N VAL A 188 ? N VAL A 234 
AA2 2 3 N TYR A 187 ? N TYR A 233 O TYR A 198 ? O TYR A 244 
AA2 3 4 O MET A 199 ? O MET A 245 N VAL A 55  ? N VAL A 101 
AA2 4 5 N CYS A 54  ? N CYS A 100 O THR A 408 ? O THR A 454 
AA2 5 6 N MET A 409 ? N MET A 455 O HIS A 423 ? O HIS A 469 
AA3 1 2 N LEU A 205 ? N LEU A 251 O LEU A 221 ? O LEU A 267 
AA4 1 2 N LEU A 218 ? N LEU A 264 O ILE A 318 ? O ILE A 364 
AA4 2 3 N THR A 319 ? N THR A 365 O ILE A 330 ? O ILE A 376 
AA5 1 2 N LEU A 356 ? N LEU A 402 O THR A 478 ? O THR A 524 
AA6 1 2 N VAL A 380 ? N VAL A 426 O LEU A 395 ? O LEU A 441 
AA7 1 2 N ILE A 429 ? N ILE A 475 O THR A 460 ? O THR A 506 
AA7 2 3 N TYR A 461 ? N TYR A 507 O GLU A 466 ? O GLU A 512 
AA8 1 2 N TYR B 27  ? N TYR B 73  O LEU B 47  ? O LEU B 93  
AA9 1 2 O THR B 283 ? O THR B 329 N LEU B 186 ? N LEU B 232 
AA9 2 3 N TYR B 187 ? N TYR B 233 O TYR B 198 ? O TYR B 244 
AA9 3 4 O MET B 199 ? O MET B 245 N VAL B 55  ? N VAL B 101 
AA9 4 5 N CYS B 54  ? N CYS B 100 O THR B 408 ? O THR B 454 
AA9 5 6 N TYR B 407 ? N TYR B 453 O PHE B 425 ? O PHE B 471 
AB1 1 2 N LEU B 205 ? N LEU B 251 O LEU B 221 ? O LEU B 267 
AB2 1 2 N THR B 216 ? N THR B 262 O GLN B 320 ? O GLN B 366 
AB3 1 2 N LEU B 356 ? N LEU B 402 O THR B 478 ? O THR B 524 
AB4 1 2 N VAL B 380 ? N VAL B 426 O LEU B 395 ? O LEU B 441 
AB5 1 2 N ILE B 429 ? N ILE B 475 O THR B 460 ? O THR B 506 
AB5 2 3 N TYR B 461 ? N TYR B 507 O GLU B 466 ? O GLU B 512 
# 
_pdbx_entry_details.entry_id                   9EPF 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   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 GLU A 109 ? ? 61.13   69.04  
2  1 ARG A 240 ? ? -93.12  54.19  
3  1 LYS A 253 ? ? -39.00  122.74 
4  1 LYS A 263 ? ? -160.48 117.20 
5  1 SER A 340 ? ? -95.60  33.31  
6  1 TRP A 499 ? ? -98.04  57.84  
7  1 PHE A 543 ? ? -92.76  53.30  
8  1 GLU B 109 ? ? 60.50   68.65  
9  1 ARG B 240 ? ? -92.24  52.90  
10 1 LYS B 253 ? ? -39.79  134.07 
11 1 SER B 340 ? ? -93.80  31.88  
12 1 TRP B 499 ? ? -94.41  57.71  
13 1 PHE B 543 ? ? -101.11 57.96  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9EPF 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      'RIGID BODY FIT' 
# 
_em_3d_reconstruction.entry_id                    9EPF 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.54 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               80582 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 VIRUS 
_em_entity_assembly.name                 'Human Picobirnavirus VLP' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9EPF 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS TALOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             500 
_em_imaging.nominal_defocus_max             3500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER/RHODIUM 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R2/2' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_virus_entity.id                    1 
_em_virus_entity.virus_host_category   ? 
_em_virus_entity.virus_type            'VIRUS-LIKE PARTICLE' 
_em_virus_entity.virus_isolate         STRAIN 
_em_virus_entity.entity_assembly_id    1 
_em_virus_entity.enveloped             NO 
_em_virus_entity.empty                 YES 
_em_virus_entity.details               ? 
# 
_em_vitrification.entry_id              9EPF 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              95 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   295 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9EPF 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       '3D ARRAY' 
_em_experiment.entity_assembly_id      1 
# 
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 PRO 546 ? A PRO 500 
2 1 Y 1 A GLN 547 ? A GLN 501 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-03-18 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9EPF 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-26 
_em_admin.title              'Human Picobirnavirus VLP' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 25 mM ? 1 Tris-HCl 
1 50 mM ? 2 NaCl     
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                7.44 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Human Picobirnavirus VLP' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               'BL21 (DE3) pLysS' 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         29.5 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       OTHER 
_em_image_recording.film_or_detector_model              'FEI FALCON III (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   83512 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ?         ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ?         ? 
MASKING                         ? 3  ? ? ? ?         ? 
'CTF CORRECTION'                ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ? 
'MODEL FITTING'                 ? 7  ? 1 ? ?         ? 
OTHER                           ? 8  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT'      ? 9  1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'        ? 10 1 ? ? ?         ? 
CLASSIFICATION                  ? 11 1 ? ? ?         ? 
RECONSTRUCTION                  ? 12 1 ? ? cryoSPARC ? 
'MODEL REFINEMENT'              ? 13 ? 1 ? ?         ? 
'VOLUME SELECTION'              ? 14 1 1 1 ?         ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ?         ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?         ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?         ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?         ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?         ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_em_virus_shell.diameter             380 
_em_virus_shell.entity_assembly_id   1 
_em_virus_shell.id                   1 
_em_virus_shell.name                 ? 
_em_virus_shell.triangulation        1 
# 
_pdbx_audit_support.funding_organization   'Spanish Ministry of Science, Innovation, and Universities' 
_pdbx_audit_support.country                Spain 
_pdbx_audit_support.grant_number           PID2020-113287RB-I00 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9EPF 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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 
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   . VAL A 1 1   ? -44.910 13.211  136.258 1.00 51.73  ? 47  VAL A N   1 
ATOM 2    C CA  . VAL A 1 1   ? -46.321 13.528  136.436 1.00 58.38  ? 47  VAL A CA  1 
ATOM 3    C C   . VAL A 1 1   ? -46.805 14.430  135.309 1.00 60.88  ? 47  VAL A C   1 
ATOM 4    O O   . VAL A 1 1   ? -46.289 15.531  135.120 1.00 61.35  ? 47  VAL A O   1 
ATOM 5    C CB  . VAL A 1 1   ? -46.574 14.186  137.803 1.00 57.06  ? 47  VAL A CB  1 
ATOM 6    C CG1 . VAL A 1 1   ? -48.043 14.074  138.179 1.00 57.85  ? 47  VAL A CG1 1 
ATOM 7    C CG2 . VAL A 1 1   ? -45.694 13.556  138.868 1.00 51.92  ? 47  VAL A CG2 1 
ATOM 8    N N   . ALA A 1 2   ? -47.801 13.958  134.558 1.00 54.00  ? 48  ALA A N   1 
ATOM 9    C CA  . ALA A 1 2   ? -48.359 14.733  133.459 1.00 52.26  ? 48  ALA A CA  1 
ATOM 10   C C   . ALA A 1 2   ? -49.098 15.979  133.924 1.00 57.12  ? 48  ALA A C   1 
ATOM 11   O O   . ALA A 1 2   ? -49.278 16.906  133.127 1.00 64.42  ? 48  ALA A O   1 
ATOM 12   C CB  . ALA A 1 2   ? -49.301 13.863  132.625 1.00 52.82  ? 48  ALA A CB  1 
ATOM 13   N N   . TRP A 1 3   ? -49.531 16.025  135.185 1.00 47.97  ? 49  TRP A N   1 
ATOM 14   C CA  . TRP A 1 3   ? -50.188 17.220  135.702 1.00 50.45  ? 49  TRP A CA  1 
ATOM 15   C C   . TRP A 1 3   ? -49.235 18.408  135.740 1.00 52.68  ? 49  TRP A C   1 
ATOM 16   O O   . TRP A 1 3   ? -49.642 19.539  135.448 1.00 58.41  ? 49  TRP A O   1 
ATOM 17   C CB  . TRP A 1 3   ? -50.755 16.935  137.091 1.00 43.11  ? 49  TRP A CB  1 
ATOM 18   C CG  . TRP A 1 3   ? -51.843 17.863  137.522 1.00 42.91  ? 49  TRP A CG  1 
ATOM 19   C CD1 . TRP A 1 3   ? -53.182 17.694  137.333 1.00 45.61  ? 49  TRP A CD1 1 
ATOM 20   C CD2 . TRP A 1 3   ? -51.694 19.087  138.252 1.00 48.15  ? 49  TRP A CD2 1 
ATOM 21   N NE1 . TRP A 1 3   ? -53.875 18.744  137.881 1.00 47.54  ? 49  TRP A NE1 1 
ATOM 22   C CE2 . TRP A 1 3   ? -52.984 19.613  138.453 1.00 49.60  ? 49  TRP A CE2 1 
ATOM 23   C CE3 . TRP A 1 3   ? -50.595 19.794  138.746 1.00 48.34  ? 49  TRP A CE3 1 
ATOM 24   C CZ2 . TRP A 1 3   ? -53.206 20.810  139.127 1.00 50.71  ? 49  TRP A CZ2 1 
ATOM 25   C CZ3 . TRP A 1 3   ? -50.818 20.983  139.415 1.00 47.18  ? 49  TRP A CZ3 1 
ATOM 26   C CH2 . TRP A 1 3   ? -52.112 21.478  139.599 1.00 50.43  ? 49  TRP A CH2 1 
ATOM 27   N N   . TYR A 1 4   ? -47.971 18.175  136.098 1.00 47.17  ? 50  TYR A N   1 
ATOM 28   C CA  . TYR A 1 4   ? -46.983 19.248  136.071 1.00 46.91  ? 50  TYR A CA  1 
ATOM 29   C C   . TYR A 1 4   ? -46.751 19.743  134.652 1.00 52.18  ? 50  TYR A C   1 
ATOM 30   O O   . TYR A 1 4   ? -46.588 20.947  134.425 1.00 56.42  ? 50  TYR A O   1 
ATOM 31   C CB  . TYR A 1 4   ? -45.666 18.780  136.691 1.00 50.20  ? 50  TYR A CB  1 
ATOM 32   C CG  . TYR A 1 4   ? -45.747 18.257  138.111 1.00 52.05  ? 50  TYR A CG  1 
ATOM 33   C CD1 . TYR A 1 4   ? -46.901 18.393  138.869 1.00 52.66  ? 50  TYR A CD1 1 
ATOM 34   C CD2 . TYR A 1 4   ? -44.660 17.620  138.690 1.00 50.70  ? 50  TYR A CD2 1 
ATOM 35   C CE1 . TYR A 1 4   ? -46.967 17.916  140.161 1.00 52.61  ? 50  TYR A CE1 1 
ATOM 36   C CE2 . TYR A 1 4   ? -44.721 17.136  139.980 1.00 51.32  ? 50  TYR A CE2 1 
ATOM 37   C CZ  . TYR A 1 4   ? -45.876 17.288  140.713 1.00 54.34  ? 50  TYR A CZ  1 
ATOM 38   O OH  . TYR A 1 4   ? -45.945 16.810  142.001 1.00 57.21  ? 50  TYR A OH  1 
ATOM 39   N N   . ALA A 1 5   ? -46.721 18.829  133.685 1.00 50.58  ? 51  ALA A N   1 
ATOM 40   C CA  . ALA A 1 5   ? -46.576 19.210  132.289 1.00 52.57  ? 51  ALA A CA  1 
ATOM 41   C C   . ALA A 1 5   ? -47.810 19.907  131.738 1.00 51.62  ? 51  ALA A C   1 
ATOM 42   O O   . ALA A 1 5   ? -47.693 20.667  130.771 1.00 53.21  ? 51  ALA A O   1 
ATOM 43   C CB  . ALA A 1 5   ? -46.262 17.979  131.435 1.00 50.55  ? 51  ALA A CB  1 
ATOM 44   N N   . ARG A 1 6   ? -48.981 19.671  132.328 1.00 49.30  ? 52  ARG A N   1 
ATOM 45   C CA  . ARG A 1 6   ? -50.221 20.262  131.849 1.00 47.22  ? 52  ARG A CA  1 
ATOM 46   C C   . ARG A 1 6   ? -50.555 21.596  132.501 1.00 50.22  ? 52  ARG A C   1 
ATOM 47   O O   . ARG A 1 6   ? -51.254 22.406  131.883 1.00 55.11  ? 52  ARG A O   1 
ATOM 48   C CB  . ARG A 1 6   ? -51.384 19.290  132.072 1.00 46.32  ? 52  ARG A CB  1 
ATOM 49   C CG  . ARG A 1 6   ? -51.710 18.433  130.867 1.00 53.11  ? 52  ARG A CG  1 
ATOM 50   C CD  . ARG A 1 6   ? -53.067 17.780  131.024 1.00 54.59  ? 52  ARG A CD  1 
ATOM 51   N NE  . ARG A 1 6   ? -52.977 16.551  131.802 1.00 56.75  ? 52  ARG A NE  1 
ATOM 52   C CZ  . ARG A 1 6   ? -53.759 16.257  132.831 1.00 57.09  ? 52  ARG A CZ  1 
ATOM 53   N NH1 . ARG A 1 6   ? -54.709 17.084  133.235 1.00 54.92  ? 52  ARG A NH1 1 
ATOM 54   N NH2 . ARG A 1 6   ? -53.582 15.105  133.472 1.00 52.10  ? 52  ARG A NH2 1 
ATOM 55   N N   . TYR A 1 7   ? -50.080 21.851  133.719 1.00 45.67  ? 53  TYR A N   1 
ATOM 56   C CA  . TYR A 1 7   ? -50.341 23.114  134.414 1.00 45.65  ? 53  TYR A CA  1 
ATOM 57   C C   . TYR A 1 7   ? -49.039 23.724  134.924 1.00 46.90  ? 53  TYR A C   1 
ATOM 58   O O   . TYR A 1 7   ? -48.867 23.963  136.130 1.00 51.06  ? 53  TYR A O   1 
ATOM 59   C CB  . TYR A 1 7   ? -51.344 22.912  135.550 1.00 44.49  ? 53  TYR A CB  1 
ATOM 60   C CG  . TYR A 1 7   ? -52.564 22.102  135.168 1.00 45.26  ? 53  TYR A CG  1 
ATOM 61   C CD1 . TYR A 1 7   ? -52.524 20.717  135.118 1.00 47.15  ? 53  TYR A CD1 1 
ATOM 62   C CD2 . TYR A 1 7   ? -53.760 22.731  134.850 1.00 49.44  ? 53  TYR A CD2 1 
ATOM 63   C CE1 . TYR A 1 7   ? -53.637 19.983  134.765 1.00 49.17  ? 53  TYR A CE1 1 
ATOM 64   C CE2 . TYR A 1 7   ? -54.878 22.005  134.497 1.00 48.16  ? 53  TYR A CE2 1 
ATOM 65   C CZ  . TYR A 1 7   ? -54.810 20.632  134.456 1.00 49.23  ? 53  TYR A CZ  1 
ATOM 66   O OH  . TYR A 1 7   ? -55.922 19.904  134.105 1.00 49.15  ? 53  TYR A OH  1 
ATOM 67   N N   . PRO A 1 8   ? -48.111 24.043  134.014 1.00 43.67  ? 54  PRO A N   1 
ATOM 68   C CA  . PRO A 1 8   ? -46.863 24.678  134.446 1.00 47.07  ? 54  PRO A CA  1 
ATOM 69   C C   . PRO A 1 8   ? -47.057 26.088  134.960 1.00 49.66  ? 54  PRO A C   1 
ATOM 70   O O   . PRO A 1 8   ? -46.255 26.535  135.785 1.00 55.24  ? 54  PRO A O   1 
ATOM 71   C CB  . PRO A 1 8   ? -46.002 24.660  133.178 1.00 48.43  ? 54  PRO A CB  1 
ATOM 72   C CG  . PRO A 1 8   ? -46.977 24.695  132.065 1.00 47.42  ? 54  PRO A CG  1 
ATOM 73   C CD  . PRO A 1 8   ? -48.266 24.082  132.548 1.00 44.70  ? 54  PRO A CD  1 
ATOM 74   N N   . HIS A 1 9   ? -48.096 26.797  134.517 1.00 46.11  ? 55  HIS A N   1 
ATOM 75   C CA  . HIS A 1 9   ? -48.353 28.136  135.038 1.00 49.60  ? 55  HIS A CA  1 
ATOM 76   C C   . HIS A 1 9   ? -48.712 28.088  136.518 1.00 49.52  ? 55  HIS A C   1 
ATOM 77   O O   . HIS A 1 9   ? -48.181 28.863  137.322 1.00 52.32  ? 55  HIS A O   1 
ATOM 78   C CB  . HIS A 1 9   ? -49.465 28.807  134.234 1.00 48.33  ? 55  HIS A CB  1 
ATOM 79   C CG  . HIS A 1 9   ? -50.595 27.889  133.887 1.00 52.22  ? 55  HIS A CG  1 
ATOM 80   N ND1 . HIS A 1 9   ? -50.658 27.206  132.692 1.00 52.81  ? 55  HIS A ND1 1 
ATOM 81   C CD2 . HIS A 1 9   ? -51.705 27.541  134.578 1.00 50.82  ? 55  HIS A CD2 1 
ATOM 82   C CE1 . HIS A 1 9   ? -51.759 26.476  132.662 1.00 53.12  ? 55  HIS A CE1 1 
ATOM 83   N NE2 . HIS A 1 9   ? -52.412 26.661  133.795 1.00 50.78  ? 55  HIS A NE2 1 
ATOM 84   N N   . ILE A 1 10  ? -49.611 27.178  136.899 1.00 41.31  ? 56  ILE A N   1 
ATOM 85   C CA  . ILE A 1 10  ? -49.964 27.065  138.309 1.00 40.70  ? 56  ILE A CA  1 
ATOM 86   C C   . ILE A 1 10  ? -48.792 26.505  139.102 1.00 41.23  ? 56  ILE A C   1 
ATOM 87   O O   . ILE A 1 10  ? -48.572 26.900  140.253 1.00 45.43  ? 56  ILE A O   1 
ATOM 88   C CB  . ILE A 1 10  ? -51.246 26.228  138.499 1.00 40.32  ? 56  ILE A CB  1 
ATOM 89   C CG1 . ILE A 1 10  ? -51.880 26.534  139.853 1.00 44.49  ? 56  ILE A CG1 1 
ATOM 90   C CG2 . ILE A 1 10  ? -50.958 24.750  138.439 1.00 41.26  ? 56  ILE A CG2 1 
ATOM 91   C CD1 . ILE A 1 10  ? -53.238 25.900  140.039 1.00 40.93  ? 56  ILE A CD1 1 
ATOM 92   N N   . LEU A 1 11  ? -48.003 25.606  138.506 1.00 44.60  ? 57  LEU A N   1 
ATOM 93   C CA  . LEU A 1 11  ? -46.815 25.125  139.205 1.00 42.67  ? 57  LEU A CA  1 
ATOM 94   C C   . LEU A 1 11  ? -45.841 26.266  139.487 1.00 44.49  ? 57  LEU A C   1 
ATOM 95   O O   . LEU A 1 11  ? -45.308 26.380  140.598 1.00 50.74  ? 57  LEU A O   1 
ATOM 96   C CB  . LEU A 1 11  ? -46.141 24.030  138.386 1.00 39.51  ? 57  LEU A CB  1 
ATOM 97   C CG  . LEU A 1 11  ? -45.231 23.091  139.166 1.00 39.72  ? 57  LEU A CG  1 
ATOM 98   C CD1 . LEU A 1 11  ? -46.023 22.352  140.225 1.00 43.26  ? 57  LEU A CD1 1 
ATOM 99   C CD2 . LEU A 1 11  ? -44.596 22.124  138.209 1.00 42.74  ? 57  LEU A CD2 1 
ATOM 100  N N   . GLU A 1 12  ? -45.608 27.125  138.493 1.00 40.23  ? 58  GLU A N   1 
ATOM 101  C CA  . GLU A 1 12  ? -44.711 28.260  138.665 1.00 35.63  ? 58  GLU A CA  1 
ATOM 102  C C   . GLU A 1 12  ? -45.248 29.243  139.695 1.00 42.24  ? 58  GLU A C   1 
ATOM 103  O O   . GLU A 1 12  ? -44.488 29.753  140.525 1.00 47.27  ? 58  GLU A O   1 
ATOM 104  C CB  . GLU A 1 12  ? -44.483 28.940  137.313 1.00 40.75  ? 58  GLU A CB  1 
ATOM 105  C CG  . GLU A 1 12  ? -43.751 30.275  137.367 1.00 51.48  ? 58  GLU A CG  1 
ATOM 106  C CD  . GLU A 1 12  ? -44.694 31.458  137.495 1.00 54.65  ? 58  GLU A CD  1 
ATOM 107  O OE1 . GLU A 1 12  ? -44.382 32.390  138.264 1.00 49.75  ? 58  GLU A OE1 1 
ATOM 108  O OE2 . GLU A 1 12  ? -45.744 31.458  136.819 1.00 54.10  ? 58  GLU A OE2 1 
ATOM 109  N N   . GLU A 1 13  ? -46.552 29.526  139.665 1.00 42.17  ? 59  GLU A N   1 
ATOM 110  C CA  . GLU A 1 13  ? -47.110 30.442  140.652 1.00 38.18  ? 59  GLU A CA  1 
ATOM 111  C C   . GLU A 1 13  ? -47.148 29.833  142.048 1.00 40.18  ? 59  GLU A C   1 
ATOM 112  O O   . GLU A 1 13  ? -47.254 30.576  143.029 1.00 41.92  ? 59  GLU A O   1 
ATOM 113  C CB  . GLU A 1 13  ? -48.514 30.900  140.242 1.00 38.98  ? 59  GLU A CB  1 
ATOM 114  C CG  . GLU A 1 13  ? -49.650 29.992  140.695 1.00 49.92  ? 59  GLU A CG  1 
ATOM 115  C CD  . GLU A 1 13  ? -50.996 30.707  140.733 1.00 49.29  ? 59  GLU A CD  1 
ATOM 116  O OE1 . GLU A 1 13  ? -51.422 31.237  139.686 1.00 48.24  ? 59  GLU A OE1 1 
ATOM 117  O OE2 . GLU A 1 13  ? -51.631 30.731  141.809 1.00 35.50  ? 59  GLU A OE2 1 
ATOM 118  N N   . ALA A 1 14  ? -47.066 28.507  142.161 1.00 40.80  ? 60  ALA A N   1 
ATOM 119  C CA  . ALA A 1 14  ? -47.014 27.865  143.467 1.00 39.30  ? 60  ALA A CA  1 
ATOM 120  C C   . ALA A 1 14  ? -45.597 27.644  143.978 1.00 45.22  ? 60  ALA A C   1 
ATOM 121  O O   . ALA A 1 14  ? -45.422 27.406  145.178 1.00 46.04  ? 60  ALA A O   1 
ATOM 122  C CB  . ALA A 1 14  ? -47.746 26.520  143.425 1.00 36.30  ? 60  ALA A CB  1 
ATOM 123  N N   . THR A 1 15  ? -44.587 27.715  143.113 1.00 47.09  ? 61  THR A N   1 
ATOM 124  C CA  . THR A 1 15  ? -43.201 27.467  143.504 1.00 39.86  ? 61  THR A CA  1 
ATOM 125  C C   . THR A 1 15  ? -42.332 28.716  143.371 1.00 43.57  ? 61  THR A C   1 
ATOM 126  O O   . THR A 1 15  ? -41.200 28.653  142.888 1.00 40.53  ? 61  THR A O   1 
ATOM 127  C CB  . THR A 1 15  ? -42.602 26.327  142.687 1.00 38.93  ? 61  THR A CB  1 
ATOM 128  O OG1 . THR A 1 15  ? -42.626 26.671  141.297 1.00 41.36  ? 61  THR A OG1 1 
ATOM 129  C CG2 . THR A 1 15  ? -43.393 25.052  142.900 1.00 37.67  ? 61  THR A CG2 1 
ATOM 130  N N   . ARG A 1 16  ? -42.848 29.865  143.797 1.00 47.95  ? 62  ARG A N   1 
ATOM 131  C CA  . ARG A 1 16  ? -42.087 31.110  143.820 1.00 45.70  ? 62  ARG A CA  1 
ATOM 132  C C   . ARG A 1 16  ? -41.403 31.229  145.176 1.00 47.15  ? 62  ARG A C   1 
ATOM 133  O O   . ARG A 1 16  ? -42.050 31.547  146.178 1.00 48.73  ? 62  ARG A O   1 
ATOM 134  C CB  . ARG A 1 16  ? -42.990 32.313  143.558 1.00 44.33  ? 62  ARG A CB  1 
ATOM 135  C CG  . ARG A 1 16  ? -43.400 32.498  142.108 1.00 44.55  ? 62  ARG A CG  1 
ATOM 136  C CD  . ARG A 1 16  ? -42.250 32.180  141.166 1.00 43.97  ? 62  ARG A CD  1 
ATOM 137  N NE  . ARG A 1 16  ? -42.424 32.786  139.852 1.00 44.49  ? 62  ARG A NE  1 
ATOM 138  C CZ  . ARG A 1 16  ? -42.330 34.086  139.605 1.00 50.67  ? 62  ARG A CZ  1 
ATOM 139  N NH1 . ARG A 1 16  ? -42.043 34.953  140.561 1.00 50.94  ? 62  ARG A NH1 1 
ATOM 140  N NH2 . ARG A 1 16  ? -42.520 34.525  138.364 1.00 51.68  ? 62  ARG A NH2 1 
ATOM 141  N N   . LEU A 1 17  ? -40.096 30.976  145.208 1.00 40.00  ? 63  LEU A N   1 
ATOM 142  C CA  . LEU A 1 17  ? -39.356 31.014  146.457 1.00 40.18  ? 63  LEU A CA  1 
ATOM 143  C C   . LEU A 1 17  ? -38.062 31.799  146.290 1.00 39.40  ? 63  LEU A C   1 
ATOM 144  O O   . LEU A 1 17  ? -37.385 31.676  145.262 1.00 36.20  ? 63  LEU A O   1 
ATOM 145  C CB  . LEU A 1 17  ? -39.039 29.596  146.948 1.00 34.96  ? 63  LEU A CB  1 
ATOM 146  C CG  . LEU A 1 17  ? -40.222 28.822  147.525 1.00 31.67  ? 63  LEU A CG  1 
ATOM 147  C CD1 . LEU A 1 17  ? -39.847 27.369  147.746 1.00 38.02  ? 63  LEU A CD1 1 
ATOM 148  C CD2 . LEU A 1 17  ? -40.700 29.461  148.816 1.00 32.38  ? 63  LEU A CD2 1 
ATOM 149  N N   . PRO A 1 18  ? -37.695 32.611  147.281 1.00 32.75  ? 64  PRO A N   1 
ATOM 150  C CA  . PRO A 1 18  ? -36.449 33.385  147.205 1.00 31.29  ? 64  PRO A CA  1 
ATOM 151  C C   . PRO A 1 18  ? -35.258 32.563  147.664 1.00 35.50  ? 64  PRO A C   1 
ATOM 152  O O   . PRO A 1 18  ? -35.163 32.172  148.833 1.00 39.26  ? 64  PRO A O   1 
ATOM 153  C CB  . PRO A 1 18  ? -36.725 34.571  148.140 1.00 34.94  ? 64  PRO A CB  1 
ATOM 154  C CG  . PRO A 1 18  ? -37.712 34.050  149.134 1.00 29.93  ? 64  PRO A CG  1 
ATOM 155  C CD  . PRO A 1 18  ? -38.448 32.887  148.516 1.00 32.31  ? 64  PRO A CD  1 
ATOM 156  N N   . PHE A 1 19  ? -34.341 32.294  146.743 1.00 34.33  ? 65  PHE A N   1 
ATOM 157  C CA  . PHE A 1 19  ? -33.105 31.596  147.050 1.00 29.38  ? 65  PHE A CA  1 
ATOM 158  C C   . PHE A 1 19  ? -31.950 32.591  147.111 1.00 34.67  ? 65  PHE A C   1 
ATOM 159  O O   . PHE A 1 19  ? -32.137 33.808  147.042 1.00 40.94  ? 65  PHE A O   1 
ATOM 160  C CB  . PHE A 1 19  ? -32.835 30.502  146.016 1.00 30.93  ? 65  PHE A CB  1 
ATOM 161  C CG  . PHE A 1 19  ? -33.662 29.267  146.211 1.00 33.89  ? 65  PHE A CG  1 
ATOM 162  C CD1 . PHE A 1 19  ? -33.429 28.426  147.283 1.00 32.03  ? 65  PHE A CD1 1 
ATOM 163  C CD2 . PHE A 1 19  ? -34.670 28.945  145.322 1.00 35.99  ? 65  PHE A CD2 1 
ATOM 164  C CE1 . PHE A 1 19  ? -34.184 27.288  147.463 1.00 28.32  ? 65  PHE A CE1 1 
ATOM 165  C CE2 . PHE A 1 19  ? -35.430 27.808  145.500 1.00 32.69  ? 65  PHE A CE2 1 
ATOM 166  C CZ  . PHE A 1 19  ? -35.186 26.980  146.573 1.00 30.91  ? 65  PHE A CZ  1 
ATOM 167  N N   . ALA A 1 20  ? -30.737 32.055  147.247 1.00 36.98  ? 66  ALA A N   1 
ATOM 168  C CA  . ALA A 1 20  ? -29.506 32.843  147.255 1.00 42.50  ? 66  ALA A CA  1 
ATOM 169  C C   . ALA A 1 20  ? -29.531 33.900  148.361 1.00 44.87  ? 66  ALA A C   1 
ATOM 170  O O   . ALA A 1 20  ? -29.481 35.106  148.114 1.00 43.47  ? 66  ALA A O   1 
ATOM 171  C CB  . ALA A 1 20  ? -29.255 33.479  145.884 1.00 41.10  ? 66  ALA A CB  1 
ATOM 172  N N   . TYR A 1 21  ? -29.616 33.421  149.593 1.00 37.55  ? 67  TYR A N   1 
ATOM 173  C CA  . TYR A 1 21  ? -29.519 34.309  150.742 1.00 30.77  ? 67  TYR A CA  1 
ATOM 174  C C   . TYR A 1 21  ? -28.081 34.795  150.890 1.00 36.26  ? 67  TYR A C   1 
ATOM 175  O O   . TYR A 1 21  ? -27.158 33.974  150.928 1.00 40.24  ? 67  TYR A O   1 
ATOM 176  C CB  . TYR A 1 21  ? -29.958 33.591  152.012 1.00 32.86  ? 67  TYR A CB  1 
ATOM 177  C CG  . TYR A 1 21  ? -31.448 33.596  152.251 1.00 31.70  ? 67  TYR A CG  1 
ATOM 178  C CD1 . TYR A 1 21  ? -32.297 32.827  151.471 1.00 33.29  ? 67  TYR A CD1 1 
ATOM 179  C CD2 . TYR A 1 21  ? -32.004 34.357  153.268 1.00 33.34  ? 67  TYR A CD2 1 
ATOM 180  C CE1 . TYR A 1 21  ? -33.658 32.824  151.690 1.00 35.25  ? 67  TYR A CE1 1 
ATOM 181  C CE2 . TYR A 1 21  ? -33.364 34.359  153.494 1.00 36.17  ? 67  TYR A CE2 1 
ATOM 182  C CZ  . TYR A 1 21  ? -34.186 33.590  152.703 1.00 34.82  ? 67  TYR A CZ  1 
ATOM 183  O OH  . TYR A 1 21  ? -35.542 33.589  152.924 1.00 33.65  ? 67  TYR A OH  1 
ATOM 184  N N   . PRO A 1 22  ? -27.846 36.105  150.965 1.00 33.85  ? 68  PRO A N   1 
ATOM 185  C CA  . PRO A 1 22  ? -26.482 36.594  151.210 1.00 34.43  ? 68  PRO A CA  1 
ATOM 186  C C   . PRO A 1 22  ? -25.991 36.160  152.583 1.00 35.69  ? 68  PRO A C   1 
ATOM 187  O O   . PRO A 1 22  ? -26.653 36.394  153.595 1.00 36.59  ? 68  PRO A O   1 
ATOM 188  C CB  . PRO A 1 22  ? -26.625 38.118  151.117 1.00 28.10  ? 68  PRO A CB  1 
ATOM 189  C CG  . PRO A 1 22  ? -27.908 38.345  150.386 1.00 28.91  ? 68  PRO A CG  1 
ATOM 190  C CD  . PRO A 1 22  ? -28.798 37.204  150.747 1.00 31.38  ? 68  PRO A CD  1 
ATOM 191  N N   . ILE A 1 23  ? -24.819 35.526  152.611 1.00 28.53  ? 69  ILE A N   1 
ATOM 192  C CA  . ILE A 1 23  ? -24.256 35.015  153.857 1.00 30.08  ? 69  ILE A CA  1 
ATOM 193  C C   . ILE A 1 23  ? -23.554 36.141  154.600 1.00 27.78  ? 69  ILE A C   1 
ATOM 194  O O   . ILE A 1 23  ? -23.322 37.220  154.045 1.00 31.39  ? 69  ILE A O   1 
ATOM 195  C CB  . ILE A 1 23  ? -23.294 33.840  153.607 1.00 29.69  ? 69  ILE A CB  1 
ATOM 196  C CG1 . ILE A 1 23  ? -22.396 34.120  152.406 1.00 33.62  ? 69  ILE A CG1 1 
ATOM 197  C CG2 . ILE A 1 23  ? -24.071 32.553  153.399 1.00 28.22  ? 69  ILE A CG2 1 
ATOM 198  C CD1 . ILE A 1 23  ? -21.455 32.985  152.090 1.00 30.71  ? 69  ILE A CD1 1 
ATOM 199  N N   . GLY A 1 24  ? -23.209 35.896  155.859 1.00 26.78  ? 70  GLY A N   1 
ATOM 200  C CA  . GLY A 1 24  ? -22.619 36.914  156.698 1.00 30.15  ? 70  GLY A CA  1 
ATOM 201  C C   . GLY A 1 24  ? -23.612 37.774  157.438 1.00 32.27  ? 70  GLY A C   1 
ATOM 202  O O   . GLY A 1 24  ? -23.201 38.717  158.124 1.00 31.71  ? 70  GLY A O   1 
ATOM 203  N N   . GLN A 1 25  ? -24.901 37.481  157.323 1.00 34.04  ? 71  GLN A N   1 
ATOM 204  C CA  . GLN A 1 25  ? -25.952 38.229  157.991 1.00 30.59  ? 71  GLN A CA  1 
ATOM 205  C C   . GLN A 1 25  ? -26.864 37.246  158.708 1.00 38.38  ? 71  GLN A C   1 
ATOM 206  O O   . GLN A 1 25  ? -27.196 36.189  158.166 1.00 42.57  ? 71  GLN A O   1 
ATOM 207  C CB  . GLN A 1 25  ? -26.739 39.075  156.984 1.00 26.84  ? 71  GLN A CB  1 
ATOM 208  C CG  . GLN A 1 25  ? -28.079 39.574  157.473 1.00 35.91  ? 71  GLN A CG  1 
ATOM 209  C CD  . GLN A 1 25  ? -28.934 40.105  156.344 1.00 43.27  ? 71  GLN A CD  1 
ATOM 210  O OE1 . GLN A 1 25  ? -28.705 39.785  155.178 1.00 41.25  ? 71  GLN A OE1 1 
ATOM 211  N NE2 . GLN A 1 25  ? -29.924 40.922  156.682 1.00 46.09  ? 71  GLN A NE2 1 
ATOM 212  N N   . TYR A 1 26  ? -27.254 37.591  159.930 1.00 39.19  ? 72  TYR A N   1 
ATOM 213  C CA  . TYR A 1 26  ? -28.077 36.695  160.730 1.00 34.42  ? 72  TYR A CA  1 
ATOM 214  C C   . TYR A 1 26  ? -29.488 36.618  160.162 1.00 39.90  ? 72  TYR A C   1 
ATOM 215  O O   . TYR A 1 26  ? -30.078 37.640  159.799 1.00 45.34  ? 72  TYR A O   1 
ATOM 216  C CB  . TYR A 1 26  ? -28.113 37.170  162.179 1.00 36.10  ? 72  TYR A CB  1 
ATOM 217  C CG  . TYR A 1 26  ? -29.213 36.545  162.998 1.00 36.33  ? 72  TYR A CG  1 
ATOM 218  C CD1 . TYR A 1 26  ? -29.150 35.213  163.376 1.00 37.01  ? 72  TYR A CD1 1 
ATOM 219  C CD2 . TYR A 1 26  ? -30.314 37.288  163.396 1.00 43.50  ? 72  TYR A CD2 1 
ATOM 220  C CE1 . TYR A 1 26  ? -30.153 34.638  164.127 1.00 41.62  ? 72  TYR A CE1 1 
ATOM 221  C CE2 . TYR A 1 26  ? -31.322 36.721  164.147 1.00 44.43  ? 72  TYR A CE2 1 
ATOM 222  C CZ  . TYR A 1 26  ? -31.237 35.396  164.509 1.00 44.07  ? 72  TYR A CZ  1 
ATOM 223  O OH  . TYR A 1 26  ? -32.240 34.827  165.258 1.00 40.32  ? 72  TYR A OH  1 
ATOM 224  N N   . TYR A 1 27  ? -30.027 35.404  160.085 1.00 34.73  ? 73  TYR A N   1 
ATOM 225  C CA  . TYR A 1 27  ? -31.362 35.161  159.554 1.00 40.00  ? 73  TYR A CA  1 
ATOM 226  C C   . TYR A 1 27  ? -32.207 34.467  160.610 1.00 39.46  ? 73  TYR A C   1 
ATOM 227  O O   . TYR A 1 27  ? -31.715 33.588  161.324 1.00 42.45  ? 73  TYR A O   1 
ATOM 228  C CB  . TYR A 1 27  ? -31.308 34.307  158.286 1.00 33.93  ? 73  TYR A CB  1 
ATOM 229  C CG  . TYR A 1 27  ? -30.647 34.992  157.117 1.00 33.82  ? 73  TYR A CG  1 
ATOM 230  C CD1 . TYR A 1 27  ? -31.247 36.073  156.493 1.00 34.53  ? 73  TYR A CD1 1 
ATOM 231  C CD2 . TYR A 1 27  ? -29.425 34.553  156.634 1.00 37.06  ? 73  TYR A CD2 1 
ATOM 232  C CE1 . TYR A 1 27  ? -30.645 36.702  155.423 1.00 35.52  ? 73  TYR A CE1 1 
ATOM 233  C CE2 . TYR A 1 27  ? -28.816 35.174  155.566 1.00 39.29  ? 73  TYR A CE2 1 
ATOM 234  C CZ  . TYR A 1 27  ? -29.430 36.247  154.964 1.00 41.07  ? 73  TYR A CZ  1 
ATOM 235  O OH  . TYR A 1 27  ? -28.824 36.870  153.900 1.00 38.50  ? 73  TYR A OH  1 
ATOM 236  N N   . ASP A 1 28  ? -33.471 34.866  160.708 1.00 41.19  ? 74  ASP A N   1 
ATOM 237  C CA  . ASP A 1 28  ? -34.423 34.247  161.620 1.00 43.08  ? 74  ASP A CA  1 
ATOM 238  C C   . ASP A 1 28  ? -35.453 33.478  160.804 1.00 46.92  ? 74  ASP A C   1 
ATOM 239  O O   . ASP A 1 28  ? -36.094 34.045  159.913 1.00 49.90  ? 74  ASP A O   1 
ATOM 240  C CB  . ASP A 1 28  ? -35.105 35.297  162.494 1.00 47.05  ? 74  ASP A CB  1 
ATOM 241  C CG  . ASP A 1 28  ? -35.862 34.684  163.651 1.00 49.23  ? 74  ASP A CG  1 
ATOM 242  O OD1 . ASP A 1 28  ? -35.225 34.357  164.674 1.00 50.74  ? 74  ASP A OD1 1 
ATOM 243  O OD2 . ASP A 1 28  ? -37.095 34.527  163.538 1.00 46.10  ? 74  ASP A OD2 1 
ATOM 244  N N   . THR A 1 29  ? -35.611 32.191  161.110 1.00 45.20  ? 75  THR A N   1 
ATOM 245  C CA  . THR A 1 29  ? -36.535 31.347  160.364 1.00 40.90  ? 75  THR A CA  1 
ATOM 246  C C   . THR A 1 29  ? -37.989 31.577  160.747 1.00 43.22  ? 75  THR A C   1 
ATOM 247  O O   . THR A 1 29  ? -38.882 31.206  159.980 1.00 46.25  ? 75  THR A O   1 
ATOM 248  C CB  . THR A 1 29  ? -36.184 29.874  160.569 1.00 44.48  ? 75  THR A CB  1 
ATOM 249  O OG1 . THR A 1 29  ? -36.216 29.567  161.967 1.00 42.50  ? 75  THR A OG1 1 
ATOM 250  C CG2 . THR A 1 29  ? -34.797 29.578  160.026 1.00 43.11  ? 75  THR A CG2 1 
ATOM 251  N N   . GLY A 1 30  ? -38.248 32.177  161.904 1.00 45.94  ? 76  GLY A N   1 
ATOM 252  C CA  . GLY A 1 30  ? -39.608 32.392  162.349 1.00 47.42  ? 76  GLY A CA  1 
ATOM 253  C C   . GLY A 1 30  ? -40.202 31.152  162.986 1.00 51.40  ? 76  GLY A C   1 
ATOM 254  O O   . GLY A 1 30  ? -39.557 30.116  163.146 1.00 54.14  ? 76  GLY A O   1 
ATOM 255  N N   . TYR A 1 31  ? -41.474 31.269  163.354 1.00 49.81  ? 77  TYR A N   1 
ATOM 256  C CA  . TYR A 1 31  ? -42.204 30.200  164.021 1.00 47.41  ? 77  TYR A CA  1 
ATOM 257  C C   . TYR A 1 31  ? -43.267 29.645  163.085 1.00 50.46  ? 77  TYR A C   1 
ATOM 258  O O   . TYR A 1 31  ? -44.097 30.398  162.567 1.00 55.64  ? 77  TYR A O   1 
ATOM 259  C CB  . TYR A 1 31  ? -42.863 30.704  165.306 1.00 47.32  ? 77  TYR A CB  1 
ATOM 260  C CG  . TYR A 1 31  ? -41.913 30.923  166.458 1.00 50.84  ? 77  TYR A CG  1 
ATOM 261  C CD1 . TYR A 1 31  ? -41.099 32.045  166.509 1.00 55.47  ? 77  TYR A CD1 1 
ATOM 262  C CD2 . TYR A 1 31  ? -41.840 30.014  167.502 1.00 50.44  ? 77  TYR A CD2 1 
ATOM 263  C CE1 . TYR A 1 31  ? -40.233 32.251  167.563 1.00 55.31  ? 77  TYR A CE1 1 
ATOM 264  C CE2 . TYR A 1 31  ? -40.977 30.212  168.561 1.00 53.75  ? 77  TYR A CE2 1 
ATOM 265  C CZ  . TYR A 1 31  ? -40.176 31.331  168.586 1.00 55.08  ? 77  TYR A CZ  1 
ATOM 266  O OH  . TYR A 1 31  ? -39.315 31.529  169.641 1.00 56.01  ? 77  TYR A OH  1 
ATOM 267  N N   . SER A 1 32  ? -43.239 28.328  162.871 1.00 51.79  ? 78  SER A N   1 
ATOM 268  C CA  . SER A 1 32  ? -44.341 27.684  162.167 1.00 51.97  ? 78  SER A CA  1 
ATOM 269  C C   . SER A 1 32  ? -45.587 27.625  163.038 1.00 52.76  ? 78  SER A C   1 
ATOM 270  O O   . SER A 1 32  ? -46.707 27.744  162.529 1.00 56.94  ? 78  SER A O   1 
ATOM 271  C CB  . SER A 1 32  ? -43.938 26.280  161.720 1.00 49.72  ? 78  SER A CB  1 
ATOM 272  O OG  . SER A 1 32  ? -44.065 25.358  162.786 1.00 50.58  ? 78  SER A OG  1 
ATOM 273  N N   . VAL A 1 33  ? -45.412 27.444  164.343 1.00 49.80  ? 79  VAL A N   1 
ATOM 274  C CA  . VAL A 1 33  ? -46.497 27.500  165.313 1.00 49.98  ? 79  VAL A CA  1 
ATOM 275  C C   . VAL A 1 33  ? -46.370 28.821  166.056 1.00 56.57  ? 79  VAL A C   1 
ATOM 276  O O   . VAL A 1 33  ? -45.424 29.017  166.830 1.00 61.05  ? 79  VAL A O   1 
ATOM 277  C CB  . VAL A 1 33  ? -46.450 26.313  166.286 1.00 46.71  ? 79  VAL A CB  1 
ATOM 278  C CG1 . VAL A 1 33  ? -47.522 26.456  167.349 1.00 53.75  ? 79  VAL A CG1 1 
ATOM 279  C CG2 . VAL A 1 33  ? -46.598 25.005  165.532 1.00 50.59  ? 79  VAL A CG2 1 
ATOM 280  N N   . ALA A 1 34  ? -47.321 29.728  165.827 1.00 61.00  ? 80  ALA A N   1 
ATOM 281  C CA  . ALA A 1 34  ? -47.230 31.059  166.413 1.00 62.73  ? 80  ALA A CA  1 
ATOM 282  C C   . ALA A 1 34  ? -47.370 31.041  167.928 1.00 61.68  ? 80  ALA A C   1 
ATOM 283  O O   . ALA A 1 34  ? -46.982 32.013  168.585 1.00 61.18  ? 80  ALA A O   1 
ATOM 284  C CB  . ALA A 1 34  ? -48.291 31.975  165.805 1.00 61.50  ? 80  ALA A CB  1 
ATOM 285  N N   . SER A 1 35  ? -47.904 29.964  168.496 1.00 55.01  ? 81  SER A N   1 
ATOM 286  C CA  . SER A 1 35  ? -48.090 29.846  169.934 1.00 55.19  ? 81  SER A CA  1 
ATOM 287  C C   . SER A 1 35  ? -46.946 29.110  170.618 1.00 56.12  ? 81  SER A C   1 
ATOM 288  O O   . SER A 1 35  ? -47.082 28.726  171.783 1.00 54.98  ? 81  SER A O   1 
ATOM 289  C CB  . SER A 1 35  ? -49.415 29.142  170.235 1.00 57.77  ? 81  SER A CB  1 
ATOM 290  O OG  . SER A 1 35  ? -49.413 27.817  169.735 1.00 57.62  ? 81  SER A OG  1 
ATOM 291  N N   . ALA A 1 36  ? -45.830 28.905  169.924 1.00 58.29  ? 82  ALA A N   1 
ATOM 292  C CA  . ALA A 1 36  ? -44.674 28.220  170.483 1.00 56.99  ? 82  ALA A CA  1 
ATOM 293  C C   . ALA A 1 36  ? -43.786 29.140  171.306 1.00 60.05  ? 82  ALA A C   1 
ATOM 294  O O   . ALA A 1 36  ? -42.783 28.679  171.860 1.00 63.31  ? 82  ALA A O   1 
ATOM 295  C CB  . ALA A 1 36  ? -43.853 27.571  169.367 1.00 56.43  ? 82  ALA A CB  1 
ATOM 296  N N   . THR A 1 37  ? -44.126 30.426  171.397 1.00 63.50  ? 83  THR A N   1 
ATOM 297  C CA  . THR A 1 37  ? -43.336 31.362  172.184 1.00 62.08  ? 83  THR A CA  1 
ATOM 298  C C   . THR A 1 37  ? -43.335 31.028  173.669 1.00 63.49  ? 83  THR A C   1 
ATOM 299  O O   . THR A 1 37  ? -42.454 31.507  174.391 1.00 62.08  ? 83  THR A O   1 
ATOM 300  C CB  . THR A 1 37  ? -43.849 32.788  171.978 1.00 62.81  ? 83  THR A CB  1 
ATOM 301  O OG1 . THR A 1 37  ? -45.183 32.896  172.487 1.00 62.77  ? 83  THR A OG1 1 
ATOM 302  C CG2 . THR A 1 37  ? -43.846 33.144  170.498 1.00 61.20  ? 83  THR A CG2 1 
ATOM 303  N N   . GLU A 1 38  ? -44.292 30.227  174.142 1.00 67.63  ? 84  GLU A N   1 
ATOM 304  C CA  . GLU A 1 38  ? -44.270 29.795  175.535 1.00 67.91  ? 84  GLU A CA  1 
ATOM 305  C C   . GLU A 1 38  ? -43.049 28.929  175.820 1.00 69.59  ? 84  GLU A C   1 
ATOM 306  O O   . GLU A 1 38  ? -42.532 28.924  176.943 1.00 70.56  ? 84  GLU A O   1 
ATOM 307  C CB  . GLU A 1 38  ? -45.564 29.055  175.874 1.00 67.62  ? 84  GLU A CB  1 
ATOM 308  C CG  . GLU A 1 38  ? -45.722 27.712  175.186 1.00 69.92  ? 84  GLU A CG  1 
ATOM 309  C CD  . GLU A 1 38  ? -47.173 27.337  174.976 1.00 73.05  ? 84  GLU A CD  1 
ATOM 310  O OE1 . GLU A 1 38  ? -47.484 26.128  174.984 1.00 71.47  ? 84  GLU A OE1 1 
ATOM 311  O OE2 . GLU A 1 38  ? -48.003 28.253  174.799 1.00 74.47  ? 84  GLU A OE2 1 
ATOM 312  N N   . TRP A 1 39  ? -42.579 28.186  174.820 1.00 65.67  ? 85  TRP A N   1 
ATOM 313  C CA  . TRP A 1 39  ? -41.283 27.516  174.885 1.00 62.77  ? 85  TRP A CA  1 
ATOM 314  C C   . TRP A 1 39  ? -40.274 28.445  174.226 1.00 67.79  ? 85  TRP A C   1 
ATOM 315  O O   . TRP A 1 39  ? -40.011 28.347  173.025 1.00 69.29  ? 85  TRP A O   1 
ATOM 316  C CB  . TRP A 1 39  ? -41.333 26.156  174.199 1.00 60.27  ? 85  TRP A CB  1 
ATOM 317  C CG  . TRP A 1 39  ? -42.578 25.388  174.486 1.00 66.48  ? 85  TRP A CG  1 
ATOM 318  C CD1 . TRP A 1 39  ? -43.160 25.199  175.703 1.00 66.65  ? 85  TRP A CD1 1 
ATOM 319  C CD2 . TRP A 1 39  ? -43.392 24.692  173.538 1.00 68.50  ? 85  TRP A CD2 1 
ATOM 320  N NE1 . TRP A 1 39  ? -44.291 24.432  175.572 1.00 65.33  ? 85  TRP A NE1 1 
ATOM 321  C CE2 . TRP A 1 39  ? -44.455 24.107  174.251 1.00 65.43  ? 85  TRP A CE2 1 
ATOM 322  C CE3 . TRP A 1 39  ? -43.327 24.509  172.155 1.00 66.93  ? 85  TRP A CE3 1 
ATOM 323  C CZ2 . TRP A 1 39  ? -45.443 23.353  173.628 1.00 62.45  ? 85  TRP A CZ2 1 
ATOM 324  C CZ3 . TRP A 1 39  ? -44.309 23.760  171.539 1.00 63.62  ? 85  TRP A CZ3 1 
ATOM 325  C CH2 . TRP A 1 39  ? -45.353 23.192  172.275 1.00 61.50  ? 85  TRP A CH2 1 
ATOM 326  N N   . SER A 1 40  ? -39.703 29.350  175.020 1.00 63.47  ? 86  SER A N   1 
ATOM 327  C CA  . SER A 1 40  ? -38.916 30.443  174.462 1.00 62.55  ? 86  SER A CA  1 
ATOM 328  C C   . SER A 1 40  ? -37.623 29.935  173.838 1.00 60.14  ? 86  SER A C   1 
ATOM 329  O O   . SER A 1 40  ? -37.396 30.092  172.633 1.00 59.63  ? 86  SER A O   1 
ATOM 330  C CB  . SER A 1 40  ? -38.615 31.474  175.552 1.00 63.96  ? 86  SER A CB  1 
ATOM 331  O OG  . SER A 1 40  ? -38.046 30.850  176.690 1.00 62.55  ? 86  SER A OG  1 
ATOM 332  N N   . LYS A 1 41  ? -36.770 29.312  174.644 1.00 57.91  ? 87  LYS A N   1 
ATOM 333  C CA  . LYS A 1 41  ? -35.486 28.821  174.168 1.00 60.74  ? 87  LYS A CA  1 
ATOM 334  C C   . LYS A 1 41  ? -35.497 27.326  173.873 1.00 56.95  ? 87  LYS A C   1 
ATOM 335  O O   . LYS A 1 41  ? -34.436 26.749  173.615 1.00 53.10  ? 87  LYS A O   1 
ATOM 336  C CB  . LYS A 1 41  ? -34.405 29.217  175.184 1.00 57.37  ? 87  LYS A CB  1 
ATOM 337  C CG  . LYS A 1 41  ? -34.042 28.211  176.254 1.00 55.19  ? 87  LYS A CG  1 
ATOM 338  C CD  . LYS A 1 41  ? -32.608 28.433  176.701 1.00 59.30  ? 87  LYS A CD  1 
ATOM 339  C CE  . LYS A 1 41  ? -32.210 27.432  177.753 1.00 60.95  ? 87  LYS A CE  1 
ATOM 340  N NZ  . LYS A 1 41  ? -30.765 27.495  178.107 1.00 57.61  ? 87  LYS A NZ  1 
ATOM 341  N N   . TYR A 1 42  ? -36.674 26.702  173.855 1.00 53.90  ? 88  TYR A N   1 
ATOM 342  C CA  . TYR A 1 42  ? -36.809 25.319  173.418 1.00 52.75  ? 88  TYR A CA  1 
ATOM 343  C C   . TYR A 1 42  ? -36.926 25.188  171.905 1.00 52.44  ? 88  TYR A C   1 
ATOM 344  O O   . TYR A 1 42  ? -36.986 24.062  171.403 1.00 49.54  ? 88  TYR A O   1 
ATOM 345  C CB  . TYR A 1 42  ? -38.031 24.678  174.082 1.00 54.54  ? 88  TYR A CB  1 
ATOM 346  C CG  . TYR A 1 42  ? -37.700 23.840  175.293 1.00 53.46  ? 88  TYR A CG  1 
ATOM 347  C CD1 . TYR A 1 42  ? -36.933 22.691  175.180 1.00 51.12  ? 88  TYR A CD1 1 
ATOM 348  C CD2 . TYR A 1 42  ? -38.142 24.211  176.556 1.00 55.24  ? 88  TYR A CD2 1 
ATOM 349  C CE1 . TYR A 1 42  ? -36.625 21.925  176.289 1.00 53.23  ? 88  TYR A CE1 1 
ATOM 350  C CE2 . TYR A 1 42  ? -37.837 23.454  177.670 1.00 54.36  ? 88  TYR A CE2 1 
ATOM 351  C CZ  . TYR A 1 42  ? -37.079 22.313  177.531 1.00 57.25  ? 88  TYR A CZ  1 
ATOM 352  O OH  . TYR A 1 42  ? -36.774 21.557  178.640 1.00 58.09  ? 88  TYR A OH  1 
ATOM 353  N N   . VAL A 1 43  ? -36.967 26.300  171.175 1.00 51.13  ? 89  VAL A N   1 
ATOM 354  C CA  . VAL A 1 43  ? -37.080 26.306  169.720 1.00 49.12  ? 89  VAL A CA  1 
ATOM 355  C C   . VAL A 1 43  ? -35.920 27.121  169.165 1.00 49.21  ? 89  VAL A C   1 
ATOM 356  O O   . VAL A 1 43  ? -35.621 28.210  169.671 1.00 53.30  ? 89  VAL A O   1 
ATOM 357  C CB  . VAL A 1 43  ? -38.426 26.882  169.253 1.00 48.42  ? 89  VAL A CB  1 
ATOM 358  C CG1 . VAL A 1 43  ? -38.602 26.675  167.760 1.00 47.10  ? 89  VAL A CG1 1 
ATOM 359  C CG2 . VAL A 1 43  ? -39.574 26.244  170.016 1.00 46.55  ? 89  VAL A CG2 1 
ATOM 360  N N   . ASP A 1 44  ? -35.267 26.599  168.130 1.00 48.89  ? 90  ASP A N   1 
ATOM 361  C CA  . ASP A 1 44  ? -34.114 27.256  167.517 1.00 51.99  ? 90  ASP A CA  1 
ATOM 362  C C   . ASP A 1 44  ? -34.557 27.899  166.208 1.00 50.18  ? 90  ASP A C   1 
ATOM 363  O O   . ASP A 1 44  ? -34.565 27.254  165.158 1.00 52.69  ? 90  ASP A O   1 
ATOM 364  C CB  . ASP A 1 44  ? -32.979 26.264  167.291 1.00 53.82  ? 90  ASP A CB  1 
ATOM 365  C CG  . ASP A 1 44  ? -31.668 26.947  166.951 1.00 55.64  ? 90  ASP A CG  1 
ATOM 366  O OD1 . ASP A 1 44  ? -30.905 27.269  167.886 1.00 58.03  ? 90  ASP A OD1 1 
ATOM 367  O OD2 . ASP A 1 44  ? -31.402 27.170  165.751 1.00 53.05  ? 90  ASP A OD2 1 
ATOM 368  N N   . THR A 1 45  ? -34.925 29.175  166.276 1.00 47.88  ? 91  THR A N   1 
ATOM 369  C CA  . THR A 1 45  ? -35.282 29.943  165.093 1.00 48.58  ? 91  THR A CA  1 
ATOM 370  C C   . THR A 1 45  ? -34.088 30.654  164.471 1.00 47.66  ? 91  THR A C   1 
ATOM 371  O O   . THR A 1 45  ? -34.221 31.223  163.383 1.00 50.14  ? 91  THR A O   1 
ATOM 372  C CB  . THR A 1 45  ? -36.364 30.969  165.437 1.00 48.81  ? 91  THR A CB  1 
ATOM 373  O OG1 . THR A 1 45  ? -35.841 31.918  166.375 1.00 51.97  ? 91  THR A OG1 1 
ATOM 374  C CG2 . THR A 1 45  ? -37.570 30.277  166.047 1.00 45.72  ? 91  THR A CG2 1 
ATOM 375  N N   . SER A 1 46  ? -32.934 30.636  165.130 1.00 45.30  ? 92  SER A N   1 
ATOM 376  C CA  . SER A 1 46  ? -31.746 31.289  164.605 1.00 46.18  ? 92  SER A CA  1 
ATOM 377  C C   . SER A 1 46  ? -31.128 30.459  163.489 1.00 38.70  ? 92  SER A C   1 
ATOM 378  O O   . SER A 1 46  ? -31.315 29.242  163.412 1.00 38.06  ? 92  SER A O   1 
ATOM 379  C CB  . SER A 1 46  ? -30.721 31.513  165.716 1.00 48.63  ? 92  SER A CB  1 
ATOM 380  O OG  . SER A 1 46  ? -31.328 32.076  166.865 1.00 53.38  ? 92  SER A OG  1 
ATOM 381  N N   . LEU A 1 47  ? -30.385 31.134  162.614 1.00 35.47  ? 93  LEU A N   1 
ATOM 382  C CA  . LEU A 1 47  ? -29.721 30.463  161.499 1.00 35.64  ? 93  LEU A CA  1 
ATOM 383  C C   . LEU A 1 47  ? -28.520 31.311  161.092 1.00 41.26  ? 93  LEU A C   1 
ATOM 384  O O   . LEU A 1 47  ? -28.674 32.307  160.380 1.00 46.63  ? 93  LEU A O   1 
ATOM 385  C CB  . LEU A 1 47  ? -30.682 30.257  160.339 1.00 31.43  ? 93  LEU A CB  1 
ATOM 386  C CG  . LEU A 1 47  ? -30.135 29.480  159.145 1.00 33.18  ? 93  LEU A CG  1 
ATOM 387  C CD1 . LEU A 1 47  ? -30.037 28.006  159.476 1.00 31.88  ? 93  LEU A CD1 1 
ATOM 388  C CD2 . LEU A 1 47  ? -31.020 29.698  157.940 1.00 38.49  ? 93  LEU A CD2 1 
ATOM 389  N N   . THR A 1 48  ? -27.333 30.905  161.536 1.00 38.61  ? 94  THR A N   1 
ATOM 390  C CA  . THR A 1 48  ? -26.092 31.600  161.226 1.00 39.81  ? 94  THR A CA  1 
ATOM 391  C C   . THR A 1 48  ? -25.191 30.677  160.420 1.00 42.00  ? 94  THR A C   1 
ATOM 392  O O   . THR A 1 48  ? -24.996 29.515  160.789 1.00 44.73  ? 94  THR A O   1 
ATOM 393  C CB  . THR A 1 48  ? -25.378 32.054  162.500 1.00 43.57  ? 94  THR A CB  1 
ATOM 394  O OG1 . THR A 1 48  ? -24.882 30.910  163.204 1.00 46.86  ? 94  THR A OG1 1 
ATOM 395  C CG2 . THR A 1 48  ? -26.333 32.820  163.398 1.00 39.62  ? 94  THR A CG2 1 
ATOM 396  N N   . ILE A 1 49  ? -24.647 31.194  159.327 1.00 31.97  ? 95  ILE A N   1 
ATOM 397  C CA  . ILE A 1 49  ? -23.786 30.438  158.424 1.00 33.39  ? 95  ILE A CA  1 
ATOM 398  C C   . ILE A 1 49  ? -22.373 31.001  158.534 1.00 31.29  ? 95  ILE A C   1 
ATOM 399  O O   . ILE A 1 49  ? -22.163 32.186  158.245 1.00 35.64  ? 95  ILE A O   1 
ATOM 400  C CB  . ILE A 1 49  ? -24.290 30.505  156.974 1.00 28.26  ? 95  ILE A CB  1 
ATOM 401  C CG1 . ILE A 1 49  ? -25.770 30.133  156.905 1.00 25.26  ? 95  ILE A CG1 1 
ATOM 402  C CG2 . ILE A 1 49  ? -23.467 29.592  156.085 1.00 31.38  ? 95  ILE A CG2 1 
ATOM 403  C CD1 . ILE A 1 49  ? -26.078 28.756  157.436 1.00 32.55  ? 95  ILE A CD1 1 
ATOM 404  N N   . PRO A 1 50  ? -21.388 30.209  158.948 1.00 29.01  ? 96  PRO A N   1 
ATOM 405  C CA  . PRO A 1 50  ? -20.003 30.685  158.925 1.00 35.53  ? 96  PRO A CA  1 
ATOM 406  C C   . PRO A 1 50  ? -19.511 30.838  157.496 1.00 39.44  ? 96  PRO A C   1 
ATOM 407  O O   . PRO A 1 50  ? -20.021 30.214  156.564 1.00 42.79  ? 96  PRO A O   1 
ATOM 408  C CB  . PRO A 1 50  ? -19.239 29.585  159.663 1.00 38.13  ? 96  PRO A CB  1 
ATOM 409  C CG  . PRO A 1 50  ? -20.043 28.361  159.411 1.00 35.93  ? 96  PRO A CG  1 
ATOM 410  C CD  . PRO A 1 50  ? -21.481 28.804  159.375 1.00 32.64  ? 96  PRO A CD  1 
ATOM 411  N N   . GLY A 1 51  ? -18.505 31.691  157.328 1.00 30.19  ? 97  GLY A N   1 
ATOM 412  C CA  . GLY A 1 51  ? -18.041 32.002  155.991 1.00 34.72  ? 97  GLY A CA  1 
ATOM 413  C C   . GLY A 1 51  ? -16.545 31.945  155.777 1.00 34.26  ? 97  GLY A C   1 
ATOM 414  O O   . GLY A 1 51  ? -16.084 32.001  154.634 1.00 36.32  ? 97  GLY A O   1 
ATOM 415  N N   . VAL A 1 52  ? -15.770 31.838  156.853 1.00 28.45  ? 98  VAL A N   1 
ATOM 416  C CA  . VAL A 1 52  ? -14.319 31.790  156.735 1.00 33.69  ? 98  VAL A CA  1 
ATOM 417  C C   . VAL A 1 52  ? -13.750 30.997  157.902 1.00 34.64  ? 98  VAL A C   1 
ATOM 418  O O   . VAL A 1 52  ? -14.277 31.027  159.018 1.00 36.00  ? 98  VAL A O   1 
ATOM 419  C CB  . VAL A 1 52  ? -13.707 33.211  156.654 1.00 33.60  ? 98  VAL A CB  1 
ATOM 420  C CG1 . VAL A 1 52  ? -13.656 33.861  158.014 1.00 33.16  ? 98  VAL A CG1 1 
ATOM 421  C CG2 . VAL A 1 52  ? -12.315 33.156  156.051 1.00 32.01  ? 98  VAL A CG2 1 
ATOM 422  N N   . MET A 1 53  ? -12.679 30.258  157.624 1.00 31.42  ? 99  MET A N   1 
ATOM 423  C CA  . MET A 1 53  ? -11.932 29.542  158.647 1.00 29.15  ? 99  MET A CA  1 
ATOM 424  C C   . MET A 1 53  ? -10.452 29.679  158.333 1.00 35.08  ? 99  MET A C   1 
ATOM 425  O O   . MET A 1 53  ? -10.039 29.481  157.187 1.00 42.75  ? 99  MET A O   1 
ATOM 426  C CB  . MET A 1 53  ? -12.335 28.066  158.712 1.00 27.64  ? 99  MET A CB  1 
ATOM 427  C CG  . MET A 1 53  ? -11.198 27.123  159.061 1.00 30.64  ? 99  MET A CG  1 
ATOM 428  S SD  . MET A 1 53  ? -11.703 25.397  159.024 1.00 41.90  ? 99  MET A SD  1 
ATOM 429  C CE  . MET A 1 53  ? -12.486 25.249  160.624 1.00 31.25  ? 99  MET A CE  1 
ATOM 430  N N   . CYS A 1 54  ? -9.662  30.018  159.346 1.00 28.89  ? 100 CYS A N   1 
ATOM 431  C CA  . CYS A 1 54  ? -8.242  30.287  159.180 1.00 21.26  ? 100 CYS A CA  1 
ATOM 432  C C   . CYS A 1 54  ? -7.433  29.135  159.757 1.00 31.75  ? 100 CYS A C   1 
ATOM 433  O O   . CYS A 1 54  ? -7.681  28.701  160.887 1.00 36.84  ? 100 CYS A O   1 
ATOM 434  C CB  . CYS A 1 54  ? -7.856  31.600  159.862 1.00 21.50  ? 100 CYS A CB  1 
ATOM 435  S SG  . CYS A 1 54  ? -6.418  32.409  159.143 1.00 41.94  ? 100 CYS A SG  1 
ATOM 436  N N   . VAL A 1 55  ? -6.473  28.646  158.982 1.00 33.44  ? 101 VAL A N   1 
ATOM 437  C CA  . VAL A 1 55  ? -5.586  27.567  159.399 1.00 22.12  ? 101 VAL A CA  1 
ATOM 438  C C   . VAL A 1 55  ? -4.285  28.200  159.875 1.00 29.79  ? 101 VAL A C   1 
ATOM 439  O O   . VAL A 1 55  ? -3.502  28.713  159.069 1.00 35.73  ? 101 VAL A O   1 
ATOM 440  C CB  . VAL A 1 55  ? -5.339  26.568  158.263 1.00 16.79  ? 101 VAL A CB  1 
ATOM 441  C CG1 . VAL A 1 55  ? -4.512  25.402  158.759 1.00 27.70  ? 101 VAL A CG1 1 
ATOM 442  C CG2 . VAL A 1 55  ? -6.659  26.082  157.693 1.00 22.28  ? 101 VAL A CG2 1 
ATOM 443  N N   . ASN A 1 56  ? -4.049  28.164  161.183 1.00 24.70  ? 102 ASN A N   1 
ATOM 444  C CA  . ASN A 1 56  ? -2.860  28.773  161.774 1.00 23.38  ? 102 ASN A CA  1 
ATOM 445  C C   . ASN A 1 56  ? -1.700  27.796  161.655 1.00 29.33  ? 102 ASN A C   1 
ATOM 446  O O   . ASN A 1 56  ? -1.519  26.920  162.502 1.00 38.96  ? 102 ASN A O   1 
ATOM 447  C CB  . ASN A 1 56  ? -3.120  29.147  163.227 1.00 28.27  ? 102 ASN A CB  1 
ATOM 448  C CG  . ASN A 1 56  ? -4.240  30.148  163.376 1.00 29.88  ? 102 ASN A CG  1 
ATOM 449  O OD1 . ASN A 1 56  ? -4.909  30.496  162.405 1.00 28.43  ? 102 ASN A OD1 1 
ATOM 450  N ND2 . ASN A 1 56  ? -4.449  30.624  164.596 1.00 26.92  ? 102 ASN A ND2 1 
ATOM 451  N N   . PHE A 1 57  ? -0.899  27.951  160.606 1.00 25.94  ? 103 PHE A N   1 
ATOM 452  C CA  . PHE A 1 57  ? 0.205   27.049  160.328 1.00 25.16  ? 103 PHE A CA  1 
ATOM 453  C C   . PHE A 1 57  ? 1.499   27.590  160.929 1.00 21.40  ? 103 PHE A C   1 
ATOM 454  O O   . PHE A 1 57  ? 1.526   28.628  161.594 1.00 23.85  ? 103 PHE A O   1 
ATOM 455  C CB  . PHE A 1 57  ? 0.338   26.821  158.820 1.00 25.90  ? 103 PHE A CB  1 
ATOM 456  C CG  . PHE A 1 57  ? 1.060   27.922  158.095 1.00 26.76  ? 103 PHE A CG  1 
ATOM 457  C CD1 . PHE A 1 57  ? 0.423   29.113  157.807 1.00 29.56  ? 103 PHE A CD1 1 
ATOM 458  C CD2 . PHE A 1 57  ? 2.370   27.756  157.684 1.00 25.82  ? 103 PHE A CD2 1 
ATOM 459  C CE1 . PHE A 1 57  ? 1.082   30.121  157.135 1.00 26.17  ? 103 PHE A CE1 1 
ATOM 460  C CE2 . PHE A 1 57  ? 3.033   28.763  157.013 1.00 26.39  ? 103 PHE A CE2 1 
ATOM 461  C CZ  . PHE A 1 57  ? 2.388   29.944  156.738 1.00 27.30  ? 103 PHE A CZ  1 
ATOM 462  N N   . THR A 1 58  ? 2.586   26.862  160.696 1.00 30.56  ? 104 THR A N   1 
ATOM 463  C CA  . THR A 1 58  ? 3.903   27.213  161.212 1.00 29.24  ? 104 THR A CA  1 
ATOM 464  C C   . THR A 1 58  ? 4.984   26.601  160.330 1.00 29.03  ? 104 THR A C   1 
ATOM 465  O O   . THR A 1 58  ? 4.996   25.381  160.123 1.00 36.39  ? 104 THR A O   1 
ATOM 466  C CB  . THR A 1 58  ? 4.061   26.729  162.653 1.00 25.48  ? 104 THR A CB  1 
ATOM 467  O OG1 . THR A 1 58  ? 3.375   27.620  163.540 1.00 22.41  ? 104 THR A OG1 1 
ATOM 468  C CG2 . THR A 1 58  ? 5.527   26.666  163.035 1.00 20.02  ? 104 THR A CG2 1 
ATOM 469  N N   . PRO A 1 59  ? 5.900   27.401  159.790 1.00 23.49  ? 105 PRO A N   1 
ATOM 470  C CA  . PRO A 1 59  ? 6.975   26.839  158.966 1.00 32.14  ? 105 PRO A CA  1 
ATOM 471  C C   . PRO A 1 59  ? 8.029   26.153  159.821 1.00 30.23  ? 105 PRO A C   1 
ATOM 472  O O   . PRO A 1 59  ? 8.482   26.689  160.835 1.00 36.94  ? 105 PRO A O   1 
ATOM 473  C CB  . PRO A 1 59  ? 7.549   28.066  158.250 1.00 26.22  ? 105 PRO A CB  1 
ATOM 474  C CG  . PRO A 1 59  ? 7.241   29.206  159.153 1.00 27.72  ? 105 PRO A CG  1 
ATOM 475  C CD  . PRO A 1 59  ? 5.980   28.868  159.897 1.00 20.51  ? 105 PRO A CD  1 
ATOM 476  N N   . THR A 1 60  ? 8.423   24.954  159.399 1.00 25.34  ? 106 THR A N   1 
ATOM 477  C CA  . THR A 1 60  ? 9.353   24.132  160.158 1.00 27.65  ? 106 THR A CA  1 
ATOM 478  C C   . THR A 1 60  ? 10.355  23.473  159.222 1.00 30.96  ? 106 THR A C   1 
ATOM 479  O O   . THR A 1 60  ? 10.043  23.217  158.053 1.00 33.46  ? 106 THR A O   1 
ATOM 480  C CB  . THR A 1 60  ? 8.618   23.045  160.957 1.00 26.64  ? 106 THR A CB  1 
ATOM 481  O OG1 . THR A 1 60  ? 7.608   22.451  160.135 1.00 29.71  ? 106 THR A OG1 1 
ATOM 482  C CG2 . THR A 1 60  ? 7.969   23.640  162.193 1.00 27.42  ? 106 THR A CG2 1 
ATOM 483  N N   . PRO A 1 61  ? 11.569  23.196  159.706 1.00 30.90  ? 107 PRO A N   1 
ATOM 484  C CA  . PRO A 1 61  ? 12.533  22.444  158.886 1.00 27.94  ? 107 PRO A CA  1 
ATOM 485  C C   . PRO A 1 61  ? 12.205  20.967  158.744 1.00 36.10  ? 107 PRO A C   1 
ATOM 486  O O   . PRO A 1 61  ? 12.728  20.328  157.823 1.00 41.72  ? 107 PRO A O   1 
ATOM 487  C CB  . PRO A 1 61  ? 13.861  22.643  159.629 1.00 26.22  ? 107 PRO A CB  1 
ATOM 488  C CG  . PRO A 1 61  ? 13.647  23.829  160.492 1.00 30.18  ? 107 PRO A CG  1 
ATOM 489  C CD  . PRO A 1 61  ? 12.209  23.793  160.887 1.00 33.17  ? 107 PRO A CD  1 
ATOM 490  N N   . GLY A 1 62  ? 11.361  20.403  159.605 1.00 31.62  ? 108 GLY A N   1 
ATOM 491  C CA  . GLY A 1 62  ? 11.000  19.006  159.460 1.00 30.07  ? 108 GLY A CA  1 
ATOM 492  C C   . GLY A 1 62  ? 11.736  17.984  160.308 1.00 38.14  ? 108 GLY A C   1 
ATOM 493  O O   . GLY A 1 62  ? 12.296  17.026  159.768 1.00 44.43  ? 108 GLY A O   1 
ATOM 494  N N   . GLU A 1 63  ? 11.749  18.175  161.630 1.00 40.13  ? 109 GLU A N   1 
ATOM 495  C CA  . GLU A 1 63  ? 12.129  17.130  162.587 1.00 38.98  ? 109 GLU A CA  1 
ATOM 496  C C   . GLU A 1 63  ? 13.573  16.661  162.372 1.00 41.98  ? 109 GLU A C   1 
ATOM 497  O O   . GLU A 1 63  ? 13.848  15.553  161.909 1.00 43.97  ? 109 GLU A O   1 
ATOM 498  C CB  . GLU A 1 63  ? 11.142  15.956  162.521 1.00 40.03  ? 109 GLU A CB  1 
ATOM 499  C CG  . GLU A 1 63  ? 11.396  14.814  163.512 1.00 42.45  ? 109 GLU A CG  1 
ATOM 500  C CD  . GLU A 1 63  ? 11.357  15.250  164.965 1.00 47.80  ? 109 GLU A CD  1 
ATOM 501  O OE1 . GLU A 1 63  ? 12.310  15.914  165.422 1.00 48.48  ? 109 GLU A OE1 1 
ATOM 502  O OE2 . GLU A 1 63  ? 10.370  14.923  165.656 1.00 47.92  ? 109 GLU A OE2 1 
ATOM 503  N N   . SER A 1 64  ? 14.494  17.565  162.687 1.00 40.05  ? 110 SER A N   1 
ATOM 504  C CA  . SER A 1 64  ? 15.919  17.266  162.681 1.00 32.13  ? 110 SER A CA  1 
ATOM 505  C C   . SER A 1 64  ? 16.377  16.917  164.091 1.00 36.27  ? 110 SER A C   1 
ATOM 506  O O   . SER A 1 64  ? 16.166  17.698  165.025 1.00 42.82  ? 110 SER A O   1 
ATOM 507  C CB  . SER A 1 64  ? 16.718  18.454  162.154 1.00 29.17  ? 110 SER A CB  1 
ATOM 508  O OG  . SER A 1 64  ? 18.024  18.058  161.776 1.00 42.15  ? 110 SER A OG  1 
ATOM 509  N N   . TYR A 1 65  ? 17.003  15.747  164.246 1.00 40.60  ? 111 TYR A N   1 
ATOM 510  C CA  . TYR A 1 65  ? 17.649  15.415  165.509 1.00 40.14  ? 111 TYR A CA  1 
ATOM 511  C C   . TYR A 1 65  ? 19.018  14.770  165.316 1.00 41.30  ? 111 TYR A C   1 
ATOM 512  O O   . TYR A 1 65  ? 19.693  14.486  166.312 1.00 44.15  ? 111 TYR A O   1 
ATOM 513  C CB  . TYR A 1 65  ? 16.761  14.501  166.366 1.00 41.20  ? 111 TYR A CB  1 
ATOM 514  C CG  . TYR A 1 65  ? 16.182  13.311  165.641 1.00 41.12  ? 111 TYR A CG  1 
ATOM 515  C CD1 . TYR A 1 65  ? 16.861  12.103  165.598 1.00 41.00  ? 111 TYR A CD1 1 
ATOM 516  C CD2 . TYR A 1 65  ? 14.953  13.393  165.004 1.00 45.21  ? 111 TYR A CD2 1 
ATOM 517  C CE1 . TYR A 1 65  ? 16.334  11.011  164.941 1.00 44.55  ? 111 TYR A CE1 1 
ATOM 518  C CE2 . TYR A 1 65  ? 14.419  12.308  164.342 1.00 47.39  ? 111 TYR A CE2 1 
ATOM 519  C CZ  . TYR A 1 65  ? 15.114  11.119  164.314 1.00 49.23  ? 111 TYR A CZ  1 
ATOM 520  O OH  . TYR A 1 65  ? 14.586  10.033  163.655 1.00 49.81  ? 111 TYR A OH  1 
ATOM 521  N N   . ASN A 1 66  ? 19.450  14.533  164.081 1.00 42.33  ? 112 ASN A N   1 
ATOM 522  C CA  . ASN A 1 66  ? 20.806  14.070  163.813 1.00 41.36  ? 112 ASN A CA  1 
ATOM 523  C C   . ASN A 1 66  ? 21.256  14.662  162.481 1.00 41.84  ? 112 ASN A C   1 
ATOM 524  O O   . ASN A 1 66  ? 20.608  15.555  161.929 1.00 41.76  ? 112 ASN A O   1 
ATOM 525  C CB  . ASN A 1 66  ? 20.888  12.537  163.828 1.00 39.71  ? 112 ASN A CB  1 
ATOM 526  C CG  . ASN A 1 66  ? 19.929  11.883  162.854 1.00 43.45  ? 112 ASN A CG  1 
ATOM 527  O OD1 . ASN A 1 66  ? 19.943  12.169  161.658 1.00 43.27  ? 112 ASN A OD1 1 
ATOM 528  N ND2 . ASN A 1 66  ? 19.101  10.980  163.361 1.00 45.75  ? 112 ASN A ND2 1 
ATOM 529  N N   . LYS A 1 67  ? 22.372  14.159  161.961 1.00 37.35  ? 113 LYS A N   1 
ATOM 530  C CA  . LYS A 1 67  ? 22.952  14.673  160.729 1.00 36.99  ? 113 LYS A CA  1 
ATOM 531  C C   . LYS A 1 67  ? 22.438  13.966  159.482 1.00 34.40  ? 113 LYS A C   1 
ATOM 532  O O   . LYS A 1 67  ? 22.879  14.295  158.377 1.00 36.41  ? 113 LYS A O   1 
ATOM 533  C CB  . LYS A 1 67  ? 24.479  14.576  160.784 1.00 28.45  ? 113 LYS A CB  1 
ATOM 534  C CG  . LYS A 1 67  ? 25.189  15.745  160.125 1.00 34.90  ? 113 LYS A CG  1 
ATOM 535  C CD  . LYS A 1 67  ? 26.239  16.344  161.039 1.00 42.31  ? 113 LYS A CD  1 
ATOM 536  C CE  . LYS A 1 67  ? 26.780  17.645  160.471 1.00 40.24  ? 113 LYS A CE  1 
ATOM 537  N NZ  . LYS A 1 67  ? 28.038  18.067  161.146 1.00 39.48  ? 113 LYS A NZ  1 
ATOM 538  N N   . ASN A 1 68  ? 21.531  13.006  159.626 1.00 33.06  ? 114 ASN A N   1 
ATOM 539  C CA  . ASN A 1 68  ? 20.912  12.348  158.484 1.00 36.80  ? 114 ASN A CA  1 
ATOM 540  C C   . ASN A 1 68  ? 19.572  12.963  158.105 1.00 43.57  ? 114 ASN A C   1 
ATOM 541  O O   . ASN A 1 68  ? 18.896  12.438  157.215 1.00 44.02  ? 114 ASN A O   1 
ATOM 542  C CB  . ASN A 1 68  ? 20.732  10.854  158.768 1.00 37.86  ? 114 ASN A CB  1 
ATOM 543  C CG  . ASN A 1 68  ? 22.015  10.072  158.595 1.00 44.31  ? 114 ASN A CG  1 
ATOM 544  O OD1 . ASN A 1 68  ? 22.559  9.987   157.495 1.00 45.19  ? 114 ASN A OD1 1 
ATOM 545  N ND2 . ASN A 1 68  ? 22.510  9.496   159.683 1.00 43.45  ? 114 ASN A ND2 1 
ATOM 546  N N   . SER A 1 69  ? 19.177  14.052  158.756 1.00 39.18  ? 115 SER A N   1 
ATOM 547  C CA  . SER A 1 69  ? 17.903  14.681  158.464 1.00 33.15  ? 115 SER A CA  1 
ATOM 548  C C   . SER A 1 69  ? 17.928  15.326  157.079 1.00 36.41  ? 115 SER A C   1 
ATOM 549  O O   . SER A 1 69  ? 18.993  15.702  156.580 1.00 44.00  ? 115 SER A O   1 
ATOM 550  C CB  . SER A 1 69  ? 17.581  15.731  159.520 1.00 35.11  ? 115 SER A CB  1 
ATOM 551  O OG  . SER A 1 69  ? 17.628  15.167  160.818 1.00 38.13  ? 115 SER A OG  1 
ATOM 552  N N   . PRO A 1 70  ? 16.767  15.448  156.429 1.00 34.16  ? 116 PRO A N   1 
ATOM 553  C CA  . PRO A 1 70  ? 16.732  16.124  155.123 1.00 31.27  ? 116 PRO A CA  1 
ATOM 554  C C   . PRO A 1 70  ? 17.228  17.554  155.180 1.00 26.93  ? 116 PRO A C   1 
ATOM 555  O O   . PRO A 1 70  ? 17.852  18.024  154.221 1.00 28.94  ? 116 PRO A O   1 
ATOM 556  C CB  . PRO A 1 70  ? 15.250  16.055  154.734 1.00 29.09  ? 116 PRO A CB  1 
ATOM 557  C CG  . PRO A 1 70  ? 14.704  14.913  155.517 1.00 31.81  ? 116 PRO A CG  1 
ATOM 558  C CD  . PRO A 1 70  ? 15.445  14.929  156.815 1.00 32.18  ? 116 PRO A CD  1 
ATOM 559  N N   . ILE A 1 71  ? 16.975  18.260  156.282 1.00 32.75  ? 117 ILE A N   1 
ATOM 560  C CA  . ILE A 1 71  ? 17.472  19.624  156.432 1.00 33.92  ? 117 ILE A CA  1 
ATOM 561  C C   . ILE A 1 71  ? 18.995  19.647  156.423 1.00 33.51  ? 117 ILE A C   1 
ATOM 562  O O   . ILE A 1 71  ? 19.609  20.479  155.748 1.00 42.00  ? 117 ILE A O   1 
ATOM 563  C CB  . ILE A 1 71  ? 16.895  20.255  157.713 1.00 32.04  ? 117 ILE A CB  1 
ATOM 564  C CG1 . ILE A 1 71  ? 17.619  21.555  158.060 1.00 30.13  ? 117 ILE A CG1 1 
ATOM 565  C CG2 . ILE A 1 71  ? 16.950  19.276  158.852 1.00 37.64  ? 117 ILE A CG2 1 
ATOM 566  C CD1 . ILE A 1 71  ? 17.373  22.659  157.088 1.00 31.85  ? 117 ILE A CD1 1 
ATOM 567  N N   . ASN A 1 72  ? 19.631  18.730  157.156 1.00 27.77  ? 118 ASN A N   1 
ATOM 568  C CA  . ASN A 1 72  ? 21.091  18.688  157.171 1.00 24.82  ? 118 ASN A CA  1 
ATOM 569  C C   . ASN A 1 72  ? 21.657  18.238  155.831 1.00 28.76  ? 118 ASN A C   1 
ATOM 570  O O   . ASN A 1 72  ? 22.705  18.736  155.402 1.00 41.97  ? 118 ASN A O   1 
ATOM 571  C CB  . ASN A 1 72  ? 21.581  17.772  158.289 1.00 27.58  ? 118 ASN A CB  1 
ATOM 572  C CG  . ASN A 1 72  ? 21.274  18.320  159.665 1.00 28.60  ? 118 ASN A CG  1 
ATOM 573  O OD1 . ASN A 1 72  ? 21.985  19.184  160.173 1.00 31.64  ? 118 ASN A OD1 1 
ATOM 574  N ND2 . ASN A 1 72  ? 20.211  17.818  160.278 1.00 33.13  ? 118 ASN A ND2 1 
ATOM 575  N N   . ILE A 1 73  ? 20.986  17.303  155.158 1.00 28.73  ? 119 ILE A N   1 
ATOM 576  C CA  . ILE A 1 73  ? 21.442  16.879  153.838 1.00 30.22  ? 119 ILE A CA  1 
ATOM 577  C C   . ILE A 1 73  ? 21.387  18.043  152.855 1.00 35.00  ? 119 ILE A C   1 
ATOM 578  O O   . ILE A 1 73  ? 22.330  18.274  152.087 1.00 40.15  ? 119 ILE A O   1 
ATOM 579  C CB  . ILE A 1 73  ? 20.610  15.680  153.351 1.00 31.89  ? 119 ILE A CB  1 
ATOM 580  C CG1 . ILE A 1 73  ? 20.906  14.450  154.206 1.00 30.66  ? 119 ILE A CG1 1 
ATOM 581  C CG2 . ILE A 1 73  ? 20.894  15.391  151.889 1.00 35.23  ? 119 ILE A CG2 1 
ATOM 582  C CD1 . ILE A 1 73  ? 19.952  13.307  153.975 1.00 32.83  ? 119 ILE A CD1 1 
ATOM 583  N N   . ALA A 1 74  ? 20.287  18.801  152.870 1.00 33.15  ? 120 ALA A N   1 
ATOM 584  C CA  . ALA A 1 74  ? 20.181  19.975  152.013 1.00 27.61  ? 120 ALA A CA  1 
ATOM 585  C C   . ALA A 1 74  ? 21.190  21.043  152.399 1.00 34.72  ? 120 ALA A C   1 
ATOM 586  O O   . ALA A 1 74  ? 21.704  21.748  151.526 1.00 41.46  ? 120 ALA A O   1 
ATOM 587  C CB  . ALA A 1 74  ? 18.766  20.543  152.070 1.00 29.05  ? 120 ALA A CB  1 
ATOM 588  N N   . ALA A 1 75  ? 21.474  21.187  153.695 1.00 35.95  ? 121 ALA A N   1 
ATOM 589  C CA  . ALA A 1 75  ? 22.509  22.115  154.132 1.00 27.22  ? 121 ALA A CA  1 
ATOM 590  C C   . ALA A 1 75  ? 23.850  21.755  153.518 1.00 27.49  ? 121 ALA A C   1 
ATOM 591  O O   . ALA A 1 75  ? 24.545  22.613  152.962 1.00 33.10  ? 121 ALA A O   1 
ATOM 592  C CB  . ALA A 1 75  ? 22.603  22.111  155.657 1.00 26.69  ? 121 ALA A CB  1 
ATOM 593  N N   . GLN A 1 76  ? 24.225  20.479  153.604 1.00 35.33  ? 122 GLN A N   1 
ATOM 594  C CA  . GLN A 1 76  ? 25.489  20.039  153.028 1.00 36.91  ? 122 GLN A CA  1 
ATOM 595  C C   . GLN A 1 76  ? 25.511  20.253  151.520 1.00 39.86  ? 122 GLN A C   1 
ATOM 596  O O   . GLN A 1 76  ? 26.512  20.727  150.970 1.00 50.84  ? 122 GLN A O   1 
ATOM 597  C CB  . GLN A 1 76  ? 25.736  18.571  153.369 1.00 31.20  ? 122 GLN A CB  1 
ATOM 598  C CG  . GLN A 1 76  ? 26.595  17.833  152.362 1.00 37.02  ? 122 GLN A CG  1 
ATOM 599  C CD  . GLN A 1 76  ? 26.372  16.336  152.401 1.00 50.86  ? 122 GLN A CD  1 
ATOM 600  O OE1 . GLN A 1 76  ? 26.343  15.728  153.471 1.00 54.88  ? 122 GLN A OE1 1 
ATOM 601  N NE2 . GLN A 1 76  ? 26.212  15.732  151.230 1.00 50.43  ? 122 GLN A NE2 1 
ATOM 602  N N   . ASN A 1 77  ? 24.412  19.925  150.838 1.00 33.21  ? 123 ASN A N   1 
ATOM 603  C CA  . ASN A 1 77  ? 24.367  20.080  149.386 1.00 29.46  ? 123 ASN A CA  1 
ATOM 604  C C   . ASN A 1 77  ? 24.507  21.541  148.976 1.00 31.08  ? 123 ASN A C   1 
ATOM 605  O O   . ASN A 1 77  ? 25.286  21.872  148.074 1.00 42.58  ? 123 ASN A O   1 
ATOM 606  C CB  . ASN A 1 77  ? 23.068  19.492  148.838 1.00 33.80  ? 123 ASN A CB  1 
ATOM 607  C CG  . ASN A 1 77  ? 23.102  17.982  148.757 1.00 44.43  ? 123 ASN A CG  1 
ATOM 608  O OD1 . ASN A 1 77  ? 23.846  17.327  149.485 1.00 44.64  ? 123 ASN A OD1 1 
ATOM 609  N ND2 . ASN A 1 77  ? 22.292  17.419  147.870 1.00 43.53  ? 123 ASN A ND2 1 
ATOM 610  N N   . VAL A 1 78  ? 23.758  22.434  149.628 1.00 29.81  ? 124 VAL A N   1 
ATOM 611  C CA  . VAL A 1 78  ? 23.802  23.842  149.254 1.00 32.69  ? 124 VAL A CA  1 
ATOM 612  C C   . VAL A 1 78  ? 25.148  24.458  149.614 1.00 35.97  ? 124 VAL A C   1 
ATOM 613  O O   . VAL A 1 78  ? 25.667  25.296  148.868 1.00 39.48  ? 124 VAL A O   1 
ATOM 614  C CB  . VAL A 1 78  ? 22.618  24.607  149.882 1.00 30.03  ? 124 VAL A CB  1 
ATOM 615  C CG1 . VAL A 1 78  ? 22.838  24.869  151.363 1.00 34.28  ? 124 VAL A CG1 1 
ATOM 616  C CG2 . VAL A 1 78  ? 22.373  25.909  149.137 1.00 27.66  ? 124 VAL A CG2 1 
ATOM 617  N N   . TYR A 1 79  ? 25.748  24.054  150.738 1.00 33.93  ? 125 TYR A N   1 
ATOM 618  C CA  . TYR A 1 79  ? 27.074  24.555  151.078 1.00 27.60  ? 125 TYR A CA  1 
ATOM 619  C C   . TYR A 1 79  ? 28.113  24.085  150.074 1.00 31.09  ? 125 TYR A C   1 
ATOM 620  O O   . TYR A 1 79  ? 29.000  24.853  149.691 1.00 33.93  ? 125 TYR A O   1 
ATOM 621  C CB  . TYR A 1 79  ? 27.461  24.114  152.483 1.00 30.51  ? 125 TYR A CB  1 
ATOM 622  C CG  . TYR A 1 79  ? 28.788  24.659  152.958 1.00 37.77  ? 125 TYR A CG  1 
ATOM 623  C CD1 . TYR A 1 79  ? 28.912  25.976  153.372 1.00 40.18  ? 125 TYR A CD1 1 
ATOM 624  C CD2 . TYR A 1 79  ? 29.915  23.851  153.001 1.00 37.73  ? 125 TYR A CD2 1 
ATOM 625  C CE1 . TYR A 1 79  ? 30.122  26.475  153.810 1.00 36.55  ? 125 TYR A CE1 1 
ATOM 626  C CE2 . TYR A 1 79  ? 31.128  24.341  153.437 1.00 37.01  ? 125 TYR A CE2 1 
ATOM 627  C CZ  . TYR A 1 79  ? 31.227  25.653  153.840 1.00 37.94  ? 125 TYR A CZ  1 
ATOM 628  O OH  . TYR A 1 79  ? 32.435  26.145  154.275 1.00 42.79  ? 125 TYR A OH  1 
ATOM 629  N N   . THR A 1 80  ? 28.030  22.825  149.643 1.00 38.25  ? 126 THR A N   1 
ATOM 630  C CA  . THR A 1 80  ? 28.955  22.339  148.627 1.00 34.00  ? 126 THR A CA  1 
ATOM 631  C C   . THR A 1 80  ? 28.786  23.108  147.325 1.00 34.93  ? 126 THR A C   1 
ATOM 632  O O   . THR A 1 80  ? 29.774  23.496  146.692 1.00 39.71  ? 126 THR A O   1 
ATOM 633  C CB  . THR A 1 80  ? 28.747  20.844  148.395 1.00 29.59  ? 126 THR A CB  1 
ATOM 634  O OG1 . THR A 1 80  ? 28.824  20.152  149.647 1.00 34.62  ? 126 THR A OG1 1 
ATOM 635  C CG2 . THR A 1 80  ? 29.807  20.301  147.455 1.00 31.02  ? 126 THR A CG2 1 
ATOM 636  N N   . TYR A 1 81  ? 27.539  23.353  146.919 1.00 34.02  ? 127 TYR A N   1 
ATOM 637  C CA  . TYR A 1 81  ? 27.303  24.088  145.682 1.00 32.98  ? 127 TYR A CA  1 
ATOM 638  C C   . TYR A 1 81  ? 27.831  25.514  145.775 1.00 36.03  ? 127 TYR A C   1 
ATOM 639  O O   . TYR A 1 81  ? 28.427  26.030  144.824 1.00 40.14  ? 127 TYR A O   1 
ATOM 640  C CB  . TYR A 1 81  ? 25.815  24.091  145.344 1.00 32.67  ? 127 TYR A CB  1 
ATOM 641  C CG  . TYR A 1 81  ? 25.507  24.792  144.045 1.00 34.20  ? 127 TYR A CG  1 
ATOM 642  C CD1 . TYR A 1 81  ? 25.856  24.223  142.831 1.00 34.67  ? 127 TYR A CD1 1 
ATOM 643  C CD2 . TYR A 1 81  ? 24.872  26.023  144.032 1.00 38.15  ? 127 TYR A CD2 1 
ATOM 644  C CE1 . TYR A 1 81  ? 25.579  24.859  141.642 1.00 35.30  ? 127 TYR A CE1 1 
ATOM 645  C CE2 . TYR A 1 81  ? 24.591  26.666  142.848 1.00 37.06  ? 127 TYR A CE2 1 
ATOM 646  C CZ  . TYR A 1 81  ? 24.945  26.079  141.656 1.00 36.00  ? 127 TYR A CZ  1 
ATOM 647  O OH  . TYR A 1 81  ? 24.665  26.719  140.473 1.00 34.84  ? 127 TYR A OH  1 
ATOM 648  N N   . VAL A 1 82  ? 27.613  26.171  146.914 1.00 38.94  ? 128 VAL A N   1 
ATOM 649  C CA  . VAL A 1 82  ? 28.063  27.550  147.072 1.00 33.08  ? 128 VAL A CA  1 
ATOM 650  C C   . VAL A 1 82  ? 29.586  27.617  147.117 1.00 37.69  ? 128 VAL A C   1 
ATOM 651  O O   . VAL A 1 82  ? 30.206  28.429  146.422 1.00 43.55  ? 128 VAL A O   1 
ATOM 652  C CB  . VAL A 1 82  ? 27.429  28.179  148.325 1.00 30.60  ? 128 VAL A CB  1 
ATOM 653  C CG1 . VAL A 1 82  ? 28.275  29.329  148.835 1.00 32.21  ? 128 VAL A CG1 1 
ATOM 654  C CG2 . VAL A 1 82  ? 26.023  28.658  148.016 1.00 32.85  ? 128 VAL A CG2 1 
ATOM 655  N N   . ARG A 1 83  ? 30.212  26.756  147.921 1.00 42.05  ? 129 ARG A N   1 
ATOM 656  C CA  . ARG A 1 83  ? 31.650  26.825  148.146 1.00 39.65  ? 129 ARG A CA  1 
ATOM 657  C C   . ARG A 1 83  ? 32.470  26.267  146.991 1.00 41.36  ? 129 ARG A C   1 
ATOM 658  O O   . ARG A 1 83  ? 33.652  26.608  146.877 1.00 46.42  ? 129 ARG A O   1 
ATOM 659  C CB  . ARG A 1 83  ? 32.011  26.080  149.430 1.00 40.18  ? 129 ARG A CB  1 
ATOM 660  C CG  . ARG A 1 83  ? 31.900  26.926  150.682 1.00 37.65  ? 129 ARG A CG  1 
ATOM 661  C CD  . ARG A 1 83  ? 33.131  27.784  150.881 1.00 41.84  ? 129 ARG A CD  1 
ATOM 662  N NE  . ARG A 1 83  ? 34.119  27.124  151.725 1.00 43.74  ? 129 ARG A NE  1 
ATOM 663  C CZ  . ARG A 1 83  ? 35.427  27.155  151.512 1.00 43.93  ? 129 ARG A CZ  1 
ATOM 664  N NH1 . ARG A 1 83  ? 35.944  27.810  150.485 1.00 45.07  ? 129 ARG A NH1 1 
ATOM 665  N NH2 . ARG A 1 83  ? 36.237  26.516  152.350 1.00 42.48  ? 129 ARG A NH2 1 
ATOM 666  N N   . HIS A 1 84  ? 31.894  25.417  146.144 1.00 38.69  ? 130 HIS A N   1 
ATOM 667  C CA  . HIS A 1 84  ? 32.631  24.926  144.990 1.00 36.36  ? 130 HIS A CA  1 
ATOM 668  C C   . HIS A 1 84  ? 32.589  25.889  143.810 1.00 41.74  ? 130 HIS A C   1 
ATOM 669  O O   . HIS A 1 84  ? 33.338  25.697  142.847 1.00 49.36  ? 130 HIS A O   1 
ATOM 670  C CB  . HIS A 1 84  ? 32.111  23.545  144.575 1.00 42.01  ? 130 HIS A CB  1 
ATOM 671  C CG  . HIS A 1 84  ? 31.188  23.564  143.398 1.00 46.17  ? 130 HIS A CG  1 
ATOM 672  N ND1 . HIS A 1 84  ? 29.838  23.811  143.515 1.00 50.68  ? 130 HIS A ND1 1 
ATOM 673  C CD2 . HIS A 1 84  ? 31.418  23.349  142.081 1.00 48.71  ? 130 HIS A CD2 1 
ATOM 674  C CE1 . HIS A 1 84  ? 29.276  23.752  142.321 1.00 51.02  ? 130 HIS A CE1 1 
ATOM 675  N NE2 . HIS A 1 84  ? 30.214  23.476  141.433 1.00 51.70  ? 130 HIS A NE2 1 
ATOM 676  N N   . MET A 1 85  ? 31.737  26.912  143.861 1.00 45.08  ? 131 MET A N   1 
ATOM 677  C CA  . MET A 1 85  ? 31.814  28.051  142.957 1.00 48.70  ? 131 MET A CA  1 
ATOM 678  C C   . MET A 1 85  ? 32.269  29.321  143.661 1.00 50.40  ? 131 MET A C   1 
ATOM 679  O O   . MET A 1 85  ? 32.143  30.411  143.094 1.00 50.56  ? 131 MET A O   1 
ATOM 680  C CB  . MET A 1 85  ? 30.469  28.299  142.274 1.00 42.74  ? 131 MET A CB  1 
ATOM 681  C CG  . MET A 1 85  ? 29.630  27.063  142.071 1.00 47.32  ? 131 MET A CG  1 
ATOM 682  S SD  . MET A 1 85  ? 28.147  27.399  141.103 1.00 61.14  ? 131 MET A SD  1 
ATOM 683  C CE  . MET A 1 85  ? 28.774  28.582  139.914 1.00 51.42  ? 131 MET A CE  1 
ATOM 684  N N   . ASN A 1 86  ? 32.786  29.210  144.880 1.00 46.81  ? 132 ASN A N   1 
ATOM 685  C CA  . ASN A 1 86  ? 33.216  30.361  145.660 1.00 44.18  ? 132 ASN A CA  1 
ATOM 686  C C   . ASN A 1 86  ? 34.732  30.363  145.760 1.00 45.70  ? 132 ASN A C   1 
ATOM 687  O O   . ASN A 1 86  ? 35.333  29.374  146.195 1.00 44.38  ? 132 ASN A O   1 
ATOM 688  C CB  . ASN A 1 86  ? 32.593  30.343  147.058 1.00 47.15  ? 132 ASN A CB  1 
ATOM 689  C CG  . ASN A 1 86  ? 33.218  31.363  147.990 1.00 47.81  ? 132 ASN A CG  1 
ATOM 690  O OD1 . ASN A 1 86  ? 33.561  32.469  147.577 1.00 55.82  ? 132 ASN A OD1 1 
ATOM 691  N ND2 . ASN A 1 86  ? 33.363  30.997  149.258 1.00 42.16  ? 132 ASN A ND2 1 
ATOM 692  N N   . SER A 1 87  ? 35.344  31.471  145.352 1.00 65.30  ? 133 SER A N   1 
ATOM 693  C CA  . SER A 1 87  ? 36.773  31.710  145.521 1.00 69.57  ? 133 SER A CA  1 
ATOM 694  C C   . SER A 1 87  ? 36.920  32.950  146.390 1.00 60.60  ? 133 SER A C   1 
ATOM 695  O O   . SER A 1 87  ? 36.787  34.076  145.901 1.00 53.94  ? 133 SER A O   1 
ATOM 696  C CB  . SER A 1 87  ? 37.470  31.886  144.173 1.00 66.27  ? 133 SER A CB  1 
ATOM 697  O OG  . SER A 1 87  ? 37.065  30.884  143.255 1.00 67.54  ? 133 SER A OG  1 
ATOM 698  N N   . GLY A 1 88  ? 37.185  32.749  147.676 1.00 61.73  ? 134 GLY A N   1 
ATOM 699  C CA  . GLY A 1 88  ? 37.139  33.858  148.603 1.00 61.20  ? 134 GLY A CA  1 
ATOM 700  C C   . GLY A 1 88  ? 36.660  33.480  149.989 1.00 68.03  ? 134 GLY A C   1 
ATOM 701  O O   . GLY A 1 88  ? 37.284  32.668  150.678 1.00 68.21  ? 134 GLY A O   1 
ATOM 702  N N   . HIS A 1 89  ? 35.554  34.094  150.401 1.00 64.73  ? 135 HIS A N   1 
ATOM 703  C CA  . HIS A 1 89  ? 35.064  34.012  151.772 1.00 61.03  ? 135 HIS A CA  1 
ATOM 704  C C   . HIS A 1 89  ? 34.839  32.565  152.193 1.00 55.05  ? 135 HIS A C   1 
ATOM 705  O O   . HIS A 1 89  ? 34.006  31.862  151.612 1.00 44.82  ? 135 HIS A O   1 
ATOM 706  C CB  . HIS A 1 89  ? 33.766  34.800  151.883 1.00 50.69  ? 135 HIS A CB  1 
ATOM 707  C CG  . HIS A 1 89  ? 33.703  35.969  150.954 1.00 53.05  ? 135 HIS A CG  1 
ATOM 708  N ND1 . HIS A 1 89  ? 32.916  35.974  149.823 1.00 52.18  ? 135 HIS A ND1 1 
ATOM 709  C CD2 . HIS A 1 89  ? 34.340  37.163  150.975 1.00 56.21  ? 135 HIS A CD2 1 
ATOM 710  C CE1 . HIS A 1 89  ? 33.064  37.125  149.192 1.00 53.91  ? 135 HIS A CE1 1 
ATOM 711  N NE2 . HIS A 1 89  ? 33.922  37.864  149.870 1.00 59.05  ? 135 HIS A NE2 1 
ATOM 712  N N   . ALA A 1 90  ? 35.584  32.123  153.209 1.00 49.81  ? 136 ALA A N   1 
ATOM 713  C CA  . ALA A 1 90  ? 35.368  30.832  153.865 1.00 49.97  ? 136 ALA A CA  1 
ATOM 714  C C   . ALA A 1 90  ? 35.352  31.094  155.368 1.00 51.57  ? 136 ALA A C   1 
ATOM 715  O O   . ALA A 1 90  ? 36.373  30.964  156.047 1.00 52.53  ? 136 ALA A O   1 
ATOM 716  C CB  . ALA A 1 90  ? 36.442  29.824  153.470 1.00 49.35  ? 136 ALA A CB  1 
ATOM 717  N N   . ASN A 1 91  ? 34.183  31.461  155.888 1.00 51.87  ? 137 ASN A N   1 
ATOM 718  C CA  . ASN A 1 91  ? 34.043  31.741  157.309 1.00 50.50  ? 137 ASN A CA  1 
ATOM 719  C C   . ASN A 1 91  ? 32.730  31.251  157.899 1.00 53.41  ? 137 ASN A C   1 
ATOM 720  O O   . ASN A 1 91  ? 32.479  31.500  159.082 1.00 55.96  ? 137 ASN A O   1 
ATOM 721  C CB  . ASN A 1 91  ? 34.184  33.248  157.572 1.00 47.13  ? 137 ASN A CB  1 
ATOM 722  C CG  . ASN A 1 91  ? 33.631  34.087  156.442 1.00 49.19  ? 137 ASN A CG  1 
ATOM 723  O OD1 . ASN A 1 91  ? 32.444  34.013  156.124 1.00 53.02  ? 137 ASN A OD1 1 
ATOM 724  N ND2 . ASN A 1 91  ? 34.488  34.893  155.828 1.00 45.81  ? 137 ASN A ND2 1 
ATOM 725  N N   . TYR A 1 92  ? 31.892  30.572  157.127 1.00 43.69  ? 138 TYR A N   1 
ATOM 726  C CA  . TYR A 1 92  ? 30.625  30.046  157.605 1.00 39.93  ? 138 TYR A CA  1 
ATOM 727  C C   . TYR A 1 92  ? 30.509  28.576  157.224 1.00 42.46  ? 138 TYR A C   1 
ATOM 728  O O   . TYR A 1 92  ? 31.343  28.030  156.499 1.00 45.19  ? 138 TYR A O   1 
ATOM 729  C CB  . TYR A 1 92  ? 29.445  30.842  157.035 1.00 39.69  ? 138 TYR A CB  1 
ATOM 730  C CG  . TYR A 1 92  ? 29.433  30.929  155.529 1.00 40.76  ? 138 TYR A CG  1 
ATOM 731  C CD1 . TYR A 1 92  ? 28.782  29.971  154.768 1.00 45.17  ? 138 TYR A CD1 1 
ATOM 732  C CD2 . TYR A 1 92  ? 30.072  31.967  154.867 1.00 37.44  ? 138 TYR A CD2 1 
ATOM 733  C CE1 . TYR A 1 92  ? 28.768  30.041  153.394 1.00 41.31  ? 138 TYR A CE1 1 
ATOM 734  C CE2 . TYR A 1 92  ? 30.061  32.045  153.491 1.00 40.17  ? 138 TYR A CE2 1 
ATOM 735  C CZ  . TYR A 1 92  ? 29.406  31.079  152.761 1.00 38.34  ? 138 TYR A CZ  1 
ATOM 736  O OH  . TYR A 1 92  ? 29.387  31.143  151.391 1.00 38.82  ? 138 TYR A OH  1 
ATOM 737  N N   . GLU A 1 93  ? 29.459  27.936  157.725 1.00 47.63  ? 139 GLU A N   1 
ATOM 738  C CA  . GLU A 1 93  ? 29.236  26.517  157.506 1.00 44.45  ? 139 GLU A CA  1 
ATOM 739  C C   . GLU A 1 93  ? 27.902  26.287  156.807 1.00 46.38  ? 139 GLU A C   1 
ATOM 740  O O   . GLU A 1 93  ? 27.123  27.215  156.559 1.00 47.89  ? 139 GLU A O   1 
ATOM 741  C CB  . GLU A 1 93  ? 29.277  25.744  158.829 1.00 46.44  ? 139 GLU A CB  1 
ATOM 742  C CG  . GLU A 1 93  ? 30.135  26.392  159.901 1.00 47.96  ? 139 GLU A CG  1 
ATOM 743  C CD  . GLU A 1 93  ? 31.603  26.045  159.757 1.00 55.80  ? 139 GLU A CD  1 
ATOM 744  O OE1 . GLU A 1 93  ? 31.937  25.221  158.881 1.00 57.53  ? 139 GLU A OE1 1 
ATOM 745  O OE2 . GLU A 1 93  ? 32.423  26.596  160.521 1.00 57.25  ? 139 GLU A OE2 1 
ATOM 746  N N   . GLN A 1 94  ? 27.652  25.013  156.494 1.00 40.58  ? 140 GLN A N   1 
ATOM 747  C CA  . GLN A 1 94  ? 26.382  24.626  155.893 1.00 42.02  ? 140 GLN A CA  1 
ATOM 748  C C   . GLN A 1 94  ? 25.219  24.977  156.805 1.00 45.91  ? 140 GLN A C   1 
ATOM 749  O O   . GLN A 1 94  ? 24.175  25.456  156.344 1.00 52.54  ? 140 GLN A O   1 
ATOM 750  C CB  . GLN A 1 94  ? 26.389  23.128  155.593 1.00 42.07  ? 140 GLN A CB  1 
ATOM 751  C CG  . GLN A 1 94  ? 27.190  22.305  156.583 1.00 40.91  ? 140 GLN A CG  1 
ATOM 752  C CD  . GLN A 1 94  ? 27.321  20.858  156.161 1.00 46.38  ? 140 GLN A CD  1 
ATOM 753  O OE1 . GLN A 1 94  ? 27.934  20.551  155.139 1.00 50.30  ? 140 GLN A OE1 1 
ATOM 754  N NE2 . GLN A 1 94  ? 26.736  19.959  156.942 1.00 41.82  ? 140 GLN A NE2 1 
ATOM 755  N N   . ALA A 1 95  ? 25.384  24.748  158.106 1.00 38.72  ? 141 ALA A N   1 
ATOM 756  C CA  . ALA A 1 95  ? 24.332  25.079  159.055 1.00 40.54  ? 141 ALA A CA  1 
ATOM 757  C C   . ALA A 1 95  ? 24.045  26.574  159.052 1.00 49.25  ? 141 ALA A C   1 
ATOM 758  O O   . ALA A 1 95  ? 22.883  26.992  159.066 1.00 57.48  ? 141 ALA A O   1 
ATOM 759  C CB  . ALA A 1 95  ? 24.728  24.603  160.449 1.00 40.36  ? 141 ALA A CB  1 
ATOM 760  N N   . ASP A 1 96  ? 25.097  27.397  159.028 1.00 42.78  ? 142 ASP A N   1 
ATOM 761  C CA  . ASP A 1 96  ? 24.906  28.845  158.996 1.00 39.33  ? 142 ASP A CA  1 
ATOM 762  C C   . ASP A 1 96  ? 24.184  29.276  157.727 1.00 40.51  ? 142 ASP A C   1 
ATOM 763  O O   . ASP A 1 96  ? 23.263  30.105  157.774 1.00 48.31  ? 142 ASP A O   1 
ATOM 764  C CB  . ASP A 1 96  ? 26.256  29.550  159.103 1.00 41.04  ? 142 ASP A CB  1 
ATOM 765  C CG  . ASP A 1 96  ? 26.955  29.274  160.415 1.00 51.23  ? 142 ASP A CG  1 
ATOM 766  O OD1 . ASP A 1 96  ? 26.273  29.253  161.460 1.00 55.11  ? 142 ASP A OD1 1 
ATOM 767  O OD2 . ASP A 1 96  ? 28.186  29.072  160.404 1.00 50.24  ? 142 ASP A OD2 1 
ATOM 768  N N   . LEU A 1 97  ? 24.585  28.715  156.584 1.00 32.14  ? 143 LEU A N   1 
ATOM 769  C CA  . LEU A 1 97  ? 23.905  29.030  155.333 1.00 30.64  ? 143 LEU A CA  1 
ATOM 770  C C   . LEU A 1 97  ? 22.433  28.648  155.404 1.00 36.38  ? 143 LEU A C   1 
ATOM 771  O O   . LEU A 1 97  ? 21.565  29.374  154.900 1.00 42.60  ? 143 LEU A O   1 
ATOM 772  C CB  . LEU A 1 97  ? 24.595  28.315  154.172 1.00 29.41  ? 143 LEU A CB  1 
ATOM 773  C CG  . LEU A 1 97  ? 24.307  28.825  152.760 1.00 31.09  ? 143 LEU A CG  1 
ATOM 774  C CD1 . LEU A 1 97  ? 24.641  30.298  152.642 1.00 28.80  ? 143 LEU A CD1 1 
ATOM 775  C CD2 . LEU A 1 97  ? 25.079  28.021  151.737 1.00 30.75  ? 143 LEU A CD2 1 
ATOM 776  N N   . MET A 1 98  ? 22.124  27.522  156.047 1.00 29.01  ? 144 MET A N   1 
ATOM 777  C CA  . MET A 1 98  ? 20.730  27.108  156.118 1.00 28.28  ? 144 MET A CA  1 
ATOM 778  C C   . MET A 1 98  ? 19.911  27.965  157.075 1.00 33.69  ? 144 MET A C   1 
ATOM 779  O O   . MET A 1 98  ? 18.735  28.214  156.803 1.00 44.84  ? 144 MET A O   1 
ATOM 780  C CB  . MET A 1 98  ? 20.617  25.638  156.503 1.00 26.63  ? 144 MET A CB  1 
ATOM 781  C CG  . MET A 1 98  ? 20.345  24.759  155.303 1.00 29.19  ? 144 MET A CG  1 
ATOM 782  S SD  . MET A 1 98  ? 18.639  24.848  154.744 1.00 36.87  ? 144 MET A SD  1 
ATOM 783  C CE  . MET A 1 98  ? 18.858  24.649  152.981 1.00 30.22  ? 144 MET A CE  1 
ATOM 784  N N   . MET A 1 99  ? 20.486  28.420  158.192 1.00 23.37  ? 145 MET A N   1 
ATOM 785  C CA  . MET A 1 99  ? 19.744  29.385  159.005 1.00 29.51  ? 145 MET A CA  1 
ATOM 786  C C   . MET A 1 99  ? 19.507  30.682  158.245 1.00 36.66  ? 145 MET A C   1 
ATOM 787  O O   . MET A 1 99  ? 18.442  31.297  158.386 1.00 50.73  ? 145 MET A O   1 
ATOM 788  C CB  . MET A 1 99  ? 20.443  29.682  160.335 1.00 32.24  ? 145 MET A CB  1 
ATOM 789  C CG  . MET A 1 99  ? 21.281  28.571  160.903 1.00 39.08  ? 145 MET A CG  1 
ATOM 790  S SD  . MET A 1 99  ? 20.285  27.252  161.615 1.00 44.81  ? 145 MET A SD  1 
ATOM 791  C CE  . MET A 1 99  ? 19.682  28.051  163.097 1.00 36.78  ? 145 MET A CE  1 
ATOM 792  N N   . TYR A 1 100 ? 20.464  31.022  157.413 1.00 30.81  ? 146 TYR A N   1 
ATOM 793  C CA  . TYR A 1 100 ? 20.125  32.211  156.623 1.00 30.86  ? 146 TYR A CA  1 
ATOM 794  C C   . TYR A 1 100 ? 18.894  31.802  155.890 1.00 33.81  ? 146 TYR A C   1 
ATOM 795  O O   . TYR A 1 100 ? 17.779  32.223  156.169 1.00 43.86  ? 146 TYR A O   1 
ATOM 796  C CB  . TYR A 1 100 ? 21.297  32.671  155.766 1.00 28.29  ? 146 TYR A CB  1 
ATOM 797  C CG  . TYR A 1 100 ? 21.103  33.546  154.547 1.00 26.65  ? 146 TYR A CG  1 
ATOM 798  C CD1 . TYR A 1 100 ? 21.034  34.920  154.665 1.00 26.82  ? 146 TYR A CD1 1 
ATOM 799  C CD2 . TYR A 1 100 ? 21.106  32.999  153.280 1.00 31.41  ? 146 TYR A CD2 1 
ATOM 800  C CE1 . TYR A 1 100 ? 20.895  35.728  153.556 1.00 29.81  ? 146 TYR A CE1 1 
ATOM 801  C CE2 . TYR A 1 100 ? 20.960  33.793  152.161 1.00 33.25  ? 146 TYR A CE2 1 
ATOM 802  C CZ  . TYR A 1 100 ? 20.854  35.159  152.303 1.00 34.08  ? 146 TYR A CZ  1 
ATOM 803  O OH  . TYR A 1 100 ? 20.715  35.945  151.205 1.00 41.67  ? 146 TYR A OH  1 
ATOM 804  N N   . LEU A 1 101 ? 19.027  30.876  155.007 1.00 18.41  ? 147 LEU A N   1 
ATOM 805  C CA  . LEU A 1 101 ? 17.927  30.565  154.097 1.00 19.85  ? 147 LEU A CA  1 
ATOM 806  C C   . LEU A 1 101 ? 16.588  30.493  154.824 1.00 26.46  ? 147 LEU A C   1 
ATOM 807  O O   . LEU A 1 101 ? 15.564  30.935  154.287 1.00 34.00  ? 147 LEU A O   1 
ATOM 808  C CB  . LEU A 1 101 ? 18.212  29.252  153.370 1.00 25.80  ? 147 LEU A CB  1 
ATOM 809  C CG  . LEU A 1 101 ? 19.404  29.276  152.413 1.00 25.28  ? 147 LEU A CG  1 
ATOM 810  C CD1 . LEU A 1 101 ? 19.455  28.012  151.582 1.00 29.40  ? 147 LEU A CD1 1 
ATOM 811  C CD2 . LEU A 1 101 ? 19.338  30.495  151.518 1.00 27.37  ? 147 LEU A CD2 1 
ATOM 812  N N   . LEU A 1 102 ? 16.571  29.942  156.038 1.00 23.29  ? 148 LEU A N   1 
ATOM 813  C CA  . LEU A 1 102 ? 15.332  29.879  156.808 1.00 28.72  ? 148 LEU A CA  1 
ATOM 814  C C   . LEU A 1 102 ? 14.836  31.265  157.200 1.00 27.76  ? 148 LEU A C   1 
ATOM 815  O O   . LEU A 1 102 ? 13.626  31.519  157.176 1.00 33.93  ? 148 LEU A O   1 
ATOM 816  C CB  . LEU A 1 102 ? 15.530  29.011  158.049 1.00 31.10  ? 148 LEU A CB  1 
ATOM 817  C CG  . LEU A 1 102 ? 15.812  27.528  157.795 1.00 29.87  ? 148 LEU A CG  1 
ATOM 818  C CD1 . LEU A 1 102 ? 15.909  26.771  159.109 1.00 30.14  ? 148 LEU A CD1 1 
ATOM 819  C CD2 . LEU A 1 102 ? 14.757  26.916  156.887 1.00 26.87  ? 148 LEU A CD2 1 
ATOM 820  N N   . ALA A 1 103 ? 15.743  32.169  157.575 1.00 18.62  ? 149 ALA A N   1 
ATOM 821  C CA  . ALA A 1 103 ? 15.330  33.542  157.854 1.00 18.91  ? 149 ALA A CA  1 
ATOM 822  C C   . ALA A 1 103 ? 14.768  34.214  156.605 1.00 27.94  ? 149 ALA A C   1 
ATOM 823  O O   . ALA A 1 103 ? 13.774  34.956  156.679 1.00 38.32  ? 149 ALA A O   1 
ATOM 824  C CB  . ALA A 1 103 ? 16.506  34.335  158.421 1.00 25.95  ? 149 ALA A CB  1 
ATOM 825  N N   . MET A 1 104 ? 15.397  33.971  155.450 1.00 27.89  ? 150 MET A N   1 
ATOM 826  C CA  . MET A 1 104 ? 14.829  34.446  154.190 1.00 27.33  ? 150 MET A CA  1 
ATOM 827  C C   . MET A 1 104 ? 13.407  33.936  154.000 1.00 34.36  ? 150 MET A C   1 
ATOM 828  O O   . MET A 1 104 ? 12.512  34.695  153.606 1.00 44.36  ? 150 MET A O   1 
ATOM 829  C CB  . MET A 1 104 ? 15.707  34.015  153.012 1.00 29.85  ? 150 MET A CB  1 
ATOM 830  C CG  . MET A 1 104 ? 17.161  34.494  153.025 1.00 35.82  ? 150 MET A CG  1 
ATOM 831  S SD  . MET A 1 104 ? 17.578  36.002  153.925 1.00 53.27  ? 150 MET A SD  1 
ATOM 832  C CE  . MET A 1 104 ? 16.414  37.173  153.228 1.00 34.25  ? 150 MET A CE  1 
ATOM 833  N N   . ASP A 1 105 ? 13.183  32.648  154.269 1.00 25.70  ? 151 ASP A N   1 
ATOM 834  C CA  . ASP A 1 105 ? 11.839  32.091  154.144 1.00 23.23  ? 151 ASP A CA  1 
ATOM 835  C C   . ASP A 1 105 ? 10.862  32.783  155.083 1.00 24.67  ? 151 ASP A C   1 
ATOM 836  O O   . ASP A 1 105 ? 9.724   33.076  154.701 1.00 30.87  ? 151 ASP A O   1 
ATOM 837  C CB  . ASP A 1 105 ? 11.851  30.590  154.427 1.00 36.07  ? 151 ASP A CB  1 
ATOM 838  C CG  . ASP A 1 105 ? 10.557  29.911  154.012 1.00 37.04  ? 151 ASP A CG  1 
ATOM 839  O OD1 . ASP A 1 105 ? 9.715   30.571  153.369 1.00 32.75  ? 151 ASP A OD1 1 
ATOM 840  O OD2 . ASP A 1 105 ? 10.373  28.723  154.340 1.00 33.45  ? 151 ASP A OD2 1 
ATOM 841  N N   . SER A 1 106 ? 11.281  33.030  156.325 1.00 32.57  ? 152 SER A N   1 
ATOM 842  C CA  . SER A 1 106 ? 10.378  33.653  157.288 1.00 26.48  ? 152 SER A CA  1 
ATOM 843  C C   . SER A 1 106 ? 9.960   35.044  156.829 1.00 21.56  ? 152 SER A C   1 
ATOM 844  O O   . SER A 1 106 ? 8.776   35.401  156.892 1.00 40.76  ? 152 SER A O   1 
ATOM 845  C CB  . SER A 1 106 ? 11.036  33.720  158.664 1.00 29.65  ? 152 SER A CB  1 
ATOM 846  O OG  . SER A 1 106 ? 11.913  34.827  158.750 1.00 31.86  ? 152 SER A OG  1 
ATOM 847  N N   . LEU A 1 107 ? 10.909  35.841  156.339 1.00 12.48  ? 153 LEU A N   1 
ATOM 848  C CA  . LEU A 1 107 ? 10.513  37.175  155.896 1.00 20.22  ? 153 LEU A CA  1 
ATOM 849  C C   . LEU A 1 107 ? 9.736   37.148  154.581 1.00 19.45  ? 153 LEU A C   1 
ATOM 850  O O   . LEU A 1 107 ? 8.886   38.019  154.357 1.00 29.45  ? 153 LEU A O   1 
ATOM 851  C CB  . LEU A 1 107 ? 11.729  38.099  155.814 1.00 21.34  ? 153 LEU A CB  1 
ATOM 852  C CG  . LEU A 1 107 ? 12.926  37.786  154.931 1.00 30.44  ? 153 LEU A CG  1 
ATOM 853  C CD1 . LEU A 1 107 ? 12.820  38.502  153.608 1.00 20.21  ? 153 LEU A CD1 1 
ATOM 854  C CD2 . LEU A 1 107 ? 14.162  38.233  155.685 1.00 32.97  ? 153 LEU A CD2 1 
ATOM 855  N N   . TYR A 1 108 ? 9.974   36.157  153.718 1.00 16.57  ? 154 TYR A N   1 
ATOM 856  C CA  . TYR A 1 108 ? 9.114   35.996  152.547 1.00 13.31  ? 154 TYR A CA  1 
ATOM 857  C C   . TYR A 1 108 ? 7.682   35.681  152.961 1.00 18.24  ? 154 TYR A C   1 
ATOM 858  O O   . TYR A 1 108 ? 6.723   36.198  152.372 1.00 27.89  ? 154 TYR A O   1 
ATOM 859  C CB  . TYR A 1 108 ? 9.656   34.894  151.640 1.00 19.53  ? 154 TYR A CB  1 
ATOM 860  C CG  . TYR A 1 108 ? 10.968  35.228  150.972 1.00 22.87  ? 154 TYR A CG  1 
ATOM 861  C CD1 . TYR A 1 108 ? 11.446  36.528  150.944 1.00 27.28  ? 154 TYR A CD1 1 
ATOM 862  C CD2 . TYR A 1 108 ? 11.732  34.238  150.376 1.00 25.10  ? 154 TYR A CD2 1 
ATOM 863  C CE1 . TYR A 1 108 ? 12.645  36.833  150.337 1.00 29.32  ? 154 TYR A CE1 1 
ATOM 864  C CE2 . TYR A 1 108 ? 12.931  34.533  149.768 1.00 24.14  ? 154 TYR A CE2 1 
ATOM 865  C CZ  . TYR A 1 108 ? 13.383  35.832  149.751 1.00 22.69  ? 154 TYR A CZ  1 
ATOM 866  O OH  . TYR A 1 108 ? 14.579  36.134  149.144 1.00 28.63  ? 154 TYR A OH  1 
ATOM 867  N N   . ILE A 1 109 ? 7.523   34.826  153.973 1.00 25.28  ? 155 ILE A N   1 
ATOM 868  C CA  . ILE A 1 109 ? 6.197   34.516  154.498 1.00 19.37  ? 155 ILE A CA  1 
ATOM 869  C C   . ILE A 1 109 ? 5.541   35.774  155.047 1.00 20.09  ? 155 ILE A C   1 
ATOM 870  O O   . ILE A 1 109 ? 4.346   36.012  154.839 1.00 27.56  ? 155 ILE A O   1 
ATOM 871  C CB  . ILE A 1 109 ? 6.295   33.414  155.569 1.00 16.26  ? 155 ILE A CB  1 
ATOM 872  C CG1 . ILE A 1 109 ? 6.530   32.055  154.912 1.00 20.39  ? 155 ILE A CG1 1 
ATOM 873  C CG2 . ILE A 1 109 ? 5.042   33.377  156.423 1.00 18.99  ? 155 ILE A CG2 1 
ATOM 874  C CD1 . ILE A 1 109 ? 6.850   30.961  155.896 1.00 26.01  ? 155 ILE A CD1 1 
ATOM 875  N N   . PHE A 1 110 ? 6.312   36.596  155.762 1.00 12.00  ? 156 PHE A N   1 
ATOM 876  C CA  . PHE A 1 110 ? 5.768   37.849  156.282 1.00 15.18  ? 156 PHE A CA  1 
ATOM 877  C C   . PHE A 1 110 ? 5.305   38.767  155.156 1.00 20.27  ? 156 PHE A C   1 
ATOM 878  O O   . PHE A 1 110 ? 4.248   39.405  155.261 1.00 25.49  ? 156 PHE A O   1 
ATOM 879  C CB  . PHE A 1 110 ? 6.808   38.560  157.144 1.00 21.53  ? 156 PHE A CB  1 
ATOM 880  C CG  . PHE A 1 110 ? 6.344   39.883  157.681 1.00 20.37  ? 156 PHE A CG  1 
ATOM 881  C CD1 . PHE A 1 110 ? 5.522   39.942  158.792 1.00 26.25  ? 156 PHE A CD1 1 
ATOM 882  C CD2 . PHE A 1 110 ? 6.719   41.065  157.069 1.00 15.09  ? 156 PHE A CD2 1 
ATOM 883  C CE1 . PHE A 1 110 ? 5.094   41.155  159.287 1.00 23.62  ? 156 PHE A CE1 1 
ATOM 884  C CE2 . PHE A 1 110 ? 6.289   42.280  157.559 1.00 18.58  ? 156 PHE A CE2 1 
ATOM 885  C CZ  . PHE A 1 110 ? 5.477   42.325  158.670 1.00 22.79  ? 156 PHE A CZ  1 
ATOM 886  N N   . HIS A 1 111 ? 6.093   38.869  154.083 1.00 22.51  ? 157 HIS A N   1 
ATOM 887  C CA  . HIS A 1 111 ? 5.684   39.707  152.960 1.00 17.10  ? 157 HIS A CA  1 
ATOM 888  C C   . HIS A 1 111 ? 4.404   39.190  152.320 1.00 20.31  ? 157 HIS A C   1 
ATOM 889  O O   . HIS A 1 111 ? 3.514   39.977  151.981 1.00 20.50  ? 157 HIS A O   1 
ATOM 890  C CB  . HIS A 1 111 ? 6.789   39.792  151.911 1.00 15.98  ? 157 HIS A CB  1 
ATOM 891  C CG  . HIS A 1 111 ? 6.343   40.424  150.629 1.00 22.53  ? 157 HIS A CG  1 
ATOM 892  N ND1 . HIS A 1 111 ? 5.990   39.686  149.519 1.00 25.40  ? 157 HIS A ND1 1 
ATOM 893  C CD2 . HIS A 1 111 ? 6.173   41.722  150.286 1.00 23.19  ? 157 HIS A CD2 1 
ATOM 894  C CE1 . HIS A 1 111 ? 5.632   40.504  148.545 1.00 23.44  ? 157 HIS A CE1 1 
ATOM 895  N NE2 . HIS A 1 111 ? 5.735   41.745  148.984 1.00 17.13  ? 157 HIS A NE2 1 
ATOM 896  N N   . SER A 1 112 ? 4.295   37.873  152.138 1.00 25.57  ? 158 SER A N   1 
ATOM 897  C CA  . SER A 1 112 ? 3.061   37.320  151.588 1.00 20.31  ? 158 SER A CA  1 
ATOM 898  C C   . SER A 1 112 ? 1.875   37.594  152.503 1.00 18.83  ? 158 SER A C   1 
ATOM 899  O O   . SER A 1 112 ? 0.778   37.907  152.024 1.00 24.32  ? 158 SER A O   1 
ATOM 900  C CB  . SER A 1 112 ? 3.212   35.820  151.348 1.00 27.10  ? 158 SER A CB  1 
ATOM 901  O OG  . SER A 1 112 ? 3.845   35.568  150.107 1.00 32.03  ? 158 SER A OG  1 
ATOM 902  N N   . TYR A 1 113 ? 2.085   37.496  153.815 1.00 20.11  ? 159 TYR A N   1 
ATOM 903  C CA  . TYR A 1 113 ? 1.026   37.771  154.780 1.00 20.37  ? 159 TYR A CA  1 
ATOM 904  C C   . TYR A 1 113 ? 0.527   39.207  154.659 1.00 19.68  ? 159 TYR A C   1 
ATOM 905  O O   . TYR A 1 113 ? -0.682  39.451  154.549 1.00 24.81  ? 159 TYR A O   1 
ATOM 906  C CB  . TYR A 1 113 ? 1.552   37.490  156.187 1.00 16.75  ? 159 TYR A CB  1 
ATOM 907  C CG  . TYR A 1 113 ? 0.593   37.776  157.315 1.00 16.29  ? 159 TYR A CG  1 
ATOM 908  C CD1 . TYR A 1 113 ? -0.733  37.381  157.249 1.00 21.88  ? 159 TYR A CD1 1 
ATOM 909  C CD2 . TYR A 1 113 ? 1.025   38.428  158.458 1.00 13.62  ? 159 TYR A CD2 1 
ATOM 910  C CE1 . TYR A 1 113 ? -1.602  37.637  158.289 1.00 19.08  ? 159 TYR A CE1 1 
ATOM 911  C CE2 . TYR A 1 113 ? 0.165   38.688  159.499 1.00 19.86  ? 159 TYR A CE2 1 
ATOM 912  C CZ  . TYR A 1 113 ? -1.146  38.292  159.410 1.00 18.44  ? 159 TYR A CZ  1 
ATOM 913  O OH  . TYR A 1 113 ? -2.003  38.554  160.451 1.00 27.90  ? 159 TYR A OH  1 
ATOM 914  N N   . VAL A 1 114 ? 1.448   40.174  154.665 1.00 21.93  ? 160 VAL A N   1 
ATOM 915  C CA  . VAL A 1 114 ? 1.021   41.570  154.595 1.00 20.17  ? 160 VAL A CA  1 
ATOM 916  C C   . VAL A 1 114 ? 0.410   41.886  153.234 1.00 20.12  ? 160 VAL A C   1 
ATOM 917  O O   . VAL A 1 114 ? -0.523  42.693  153.139 1.00 21.84  ? 160 VAL A O   1 
ATOM 918  C CB  . VAL A 1 114 ? 2.177   42.531  154.934 1.00 19.52  ? 160 VAL A CB  1 
ATOM 919  C CG1 . VAL A 1 114 ? 2.586   42.376  156.388 1.00 24.86  ? 160 VAL A CG1 1 
ATOM 920  C CG2 . VAL A 1 114 ? 3.358   42.318  154.016 1.00 23.58  ? 160 VAL A CG2 1 
ATOM 921  N N   . ARG A 1 115 ? 0.911   41.267  152.162 1.00 24.89  ? 161 ARG A N   1 
ATOM 922  C CA  . ARG A 1 115 ? 0.327   41.502  150.845 1.00 19.17  ? 161 ARG A CA  1 
ATOM 923  C C   . ARG A 1 115 ? -1.100  40.975  150.772 1.00 23.31  ? 161 ARG A C   1 
ATOM 924  O O   . ARG A 1 115 ? -1.977  41.624  150.190 1.00 34.39  ? 161 ARG A O   1 
ATOM 925  C CB  . ARG A 1 115 ? 1.196   40.863  149.766 1.00 25.89  ? 161 ARG A CB  1 
ATOM 926  C CG  . ARG A 1 115 ? 0.720   41.139  148.359 1.00 27.43  ? 161 ARG A CG  1 
ATOM 927  C CD  . ARG A 1 115 ? 1.736   40.672  147.339 1.00 29.80  ? 161 ARG A CD  1 
ATOM 928  N NE  . ARG A 1 115 ? 1.367   39.390  146.755 1.00 28.37  ? 161 ARG A NE  1 
ATOM 929  C CZ  . ARG A 1 115 ? 1.161   39.193  145.461 1.00 35.29  ? 161 ARG A CZ  1 
ATOM 930  N NH1 . ARG A 1 115 ? 1.295   40.173  144.583 1.00 35.58  ? 161 ARG A NH1 1 
ATOM 931  N NH2 . ARG A 1 115 ? 0.811   37.982  145.037 1.00 33.71  ? 161 ARG A NH2 1 
ATOM 932  N N   . LYS A 1 116 ? -1.353  39.798  151.352 1.00 28.03  ? 162 LYS A N   1 
ATOM 933  C CA  . LYS A 1 116 ? -2.721  39.294  151.425 1.00 23.91  ? 162 LYS A CA  1 
ATOM 934  C C   . LYS A 1 116 ? -3.602  40.212  152.260 1.00 21.28  ? 162 LYS A C   1 
ATOM 935  O O   . LYS A 1 116 ? -4.760  40.461  151.906 1.00 20.38  ? 162 LYS A O   1 
ATOM 936  C CB  . LYS A 1 116 ? -2.736  37.878  151.997 1.00 25.87  ? 162 LYS A CB  1 
ATOM 937  C CG  . LYS A 1 116 ? -4.093  37.198  151.921 1.00 22.70  ? 162 LYS A CG  1 
ATOM 938  C CD  . LYS A 1 116 ? -4.070  35.833  152.586 1.00 24.40  ? 162 LYS A CD  1 
ATOM 939  C CE  . LYS A 1 116 ? -3.703  35.942  154.054 1.00 26.13  ? 162 LYS A CE  1 
ATOM 940  N NZ  . LYS A 1 116 ? -3.482  34.606  154.670 1.00 31.92  ? 162 LYS A NZ  1 
ATOM 941  N N   . ILE A 1 117 ? -3.072  40.720  153.377 1.00 25.74  ? 163 ILE A N   1 
ATOM 942  C CA  . ILE A 1 117 ? -3.839  41.644  154.208 1.00 20.24  ? 163 ILE A CA  1 
ATOM 943  C C   . ILE A 1 117 ? -4.241  42.871  153.402 1.00 21.70  ? 163 ILE A C   1 
ATOM 944  O O   . ILE A 1 117 ? -5.383  43.339  153.479 1.00 28.50  ? 163 ILE A O   1 
ATOM 945  C CB  . ILE A 1 117 ? -3.032  42.036  155.459 1.00 23.68  ? 163 ILE A CB  1 
ATOM 946  C CG1 . ILE A 1 117 ? -2.935  40.861  156.424 1.00 26.27  ? 163 ILE A CG1 1 
ATOM 947  C CG2 . ILE A 1 117 ? -3.671  43.220  156.157 1.00 22.51  ? 163 ILE A CG2 1 
ATOM 948  C CD1 . ILE A 1 117 ? -1.971  41.099  157.547 1.00 27.06  ? 163 ILE A CD1 1 
ATOM 949  N N   . LEU A 1 118 ? -3.306  43.415  152.621 1.00 28.33  ? 164 LEU A N   1 
ATOM 950  C CA  . LEU A 1 118 ? -3.618  44.566  151.779 1.00 24.08  ? 164 LEU A CA  1 
ATOM 951  C C   . LEU A 1 118 ? -4.659  44.229  150.719 1.00 25.92  ? 164 LEU A C   1 
ATOM 952  O O   . LEU A 1 118 ? -5.631  44.971  150.540 1.00 30.50  ? 164 LEU A O   1 
ATOM 953  C CB  . LEU A 1 118 ? -2.348  45.088  151.111 1.00 24.25  ? 164 LEU A CB  1 
ATOM 954  C CG  . LEU A 1 118 ? -2.581  46.187  150.076 1.00 25.22  ? 164 LEU A CG  1 
ATOM 955  C CD1 . LEU A 1 118 ? -2.544  47.557  150.713 1.00 35.60  ? 164 LEU A CD1 1 
ATOM 956  C CD2 . LEU A 1 118 ? -1.557  46.084  148.961 1.00 26.92  ? 164 LEU A CD2 1 
ATOM 957  N N   . ALA A 1 119 ? -4.476  43.117  150.007 1.00 26.79  ? 165 ALA A N   1 
ATOM 958  C CA  . ALA A 1 119 ? -5.344  42.815  148.876 1.00 25.46  ? 165 ALA A CA  1 
ATOM 959  C C   . ALA A 1 119 ? -6.741  42.384  149.300 1.00 27.75  ? 165 ALA A C   1 
ATOM 960  O O   . ALA A 1 119 ? -7.678  42.499  148.503 1.00 24.40  ? 165 ALA A O   1 
ATOM 961  C CB  . ALA A 1 119 ? -4.707  41.739  148.004 1.00 21.05  ? 165 ALA A CB  1 
ATOM 962  N N   . ILE A 1 120 ? -6.904  41.878  150.524 1.00 30.89  ? 166 ILE A N   1 
ATOM 963  C CA  . ILE A 1 120 ? -8.219  41.430  150.971 1.00 21.10  ? 166 ILE A CA  1 
ATOM 964  C C   . ILE A 1 120 ? -9.159  42.614  151.162 1.00 23.72  ? 166 ILE A C   1 
ATOM 965  O O   . ILE A 1 120 ? -10.340 42.550  150.803 1.00 29.40  ? 166 ILE A O   1 
ATOM 966  C CB  . ILE A 1 120 ? -8.077  40.599  152.258 1.00 20.81  ? 166 ILE A CB  1 
ATOM 967  C CG1 . ILE A 1 120 ? -7.781  39.140  151.916 1.00 20.25  ? 166 ILE A CG1 1 
ATOM 968  C CG2 . ILE A 1 120 ? -9.326  40.701  153.114 1.00 24.23  ? 166 ILE A CG2 1 
ATOM 969  C CD1 . ILE A 1 120 ? -7.565  38.269  153.126 1.00 26.80  ? 166 ILE A CD1 1 
ATOM 970  N N   . SER A 1 121 ? -8.649  43.721  151.705 1.00 22.63  ? 167 SER A N   1 
ATOM 971  C CA  . SER A 1 121 ? -9.492  44.834  152.123 1.00 27.15  ? 167 SER A CA  1 
ATOM 972  C C   . SER A 1 121 ? -10.212 45.521  150.970 1.00 28.25  ? 167 SER A C   1 
ATOM 973  O O   . SER A 1 121 ? -11.126 46.313  151.223 1.00 23.82  ? 167 SER A O   1 
ATOM 974  C CB  . SER A 1 121 ? -8.655  45.859  152.882 1.00 22.46  ? 167 SER A CB  1 
ATOM 975  O OG  . SER A 1 121 ? -7.615  46.363  152.065 1.00 27.84  ? 167 SER A OG  1 
ATOM 976  N N   . LYS A 1 122 ? -9.828  45.252  149.725 1.00 31.95  ? 168 LYS A N   1 
ATOM 977  C CA  . LYS A 1 122 ? -10.487 45.836  148.566 1.00 25.23  ? 168 LYS A CA  1 
ATOM 978  C C   . LYS A 1 122 ? -11.618 44.959  148.042 1.00 29.63  ? 168 LYS A C   1 
ATOM 979  O O   . LYS A 1 122 ? -12.194 45.260  146.992 1.00 33.95  ? 168 LYS A O   1 
ATOM 980  C CB  . LYS A 1 122 ? -9.467  46.101  147.461 1.00 29.32  ? 168 LYS A CB  1 
ATOM 981  C CG  . LYS A 1 122 ? -8.235  46.856  147.922 1.00 35.07  ? 168 LYS A CG  1 
ATOM 982  C CD  . LYS A 1 122 ? -7.002  46.397  147.170 1.00 32.18  ? 168 LYS A CD  1 
ATOM 983  C CE  . LYS A 1 122 ? -6.574  47.420  146.140 1.00 33.70  ? 168 LYS A CE  1 
ATOM 984  N NZ  . LYS A 1 122 ? -5.294  47.037  145.487 1.00 36.80  ? 168 LYS A NZ  1 
ATOM 985  N N   . LEU A 1 123 ? -11.947 43.885  148.752 1.00 34.24  ? 169 LEU A N   1 
ATOM 986  C CA  . LEU A 1 123 ? -12.947 42.923  148.308 1.00 33.28  ? 169 LEU A CA  1 
ATOM 987  C C   . LEU A 1 123 ? -14.278 43.235  148.979 1.00 34.36  ? 169 LEU A C   1 
ATOM 988  O O   . LEU A 1 123 ? -14.398 43.140  150.204 1.00 34.80  ? 169 LEU A O   1 
ATOM 989  C CB  . LEU A 1 123 ? -12.506 41.497  148.632 1.00 25.92  ? 169 LEU A CB  1 
ATOM 990  C CG  . LEU A 1 123 ? -11.511 40.877  147.653 1.00 33.06  ? 169 LEU A CG  1 
ATOM 991  C CD1 . LEU A 1 123 ? -11.280 39.418  147.991 1.00 38.56  ? 169 LEU A CD1 1 
ATOM 992  C CD2 . LEU A 1 123 ? -11.998 41.031  146.222 1.00 31.60  ? 169 LEU A CD2 1 
ATOM 993  N N   . TYR A 1 124 ? -15.273 43.597  148.172 1.00 30.25  ? 170 TYR A N   1 
ATOM 994  C CA  . TYR A 1 124 ? -16.612 43.902  148.657 1.00 24.48  ? 170 TYR A CA  1 
ATOM 995  C C   . TYR A 1 124 ? -17.613 43.311  147.680 1.00 28.41  ? 170 TYR A C   1 
ATOM 996  O O   . TYR A 1 124 ? -17.559 43.609  146.484 1.00 34.24  ? 170 TYR A O   1 
ATOM 997  C CB  . TYR A 1 124 ? -16.827 45.412  148.790 1.00 22.20  ? 170 TYR A CB  1 
ATOM 998  C CG  . TYR A 1 124 ? -16.286 46.017  150.063 1.00 18.62  ? 170 TYR A CG  1 
ATOM 999  C CD1 . TYR A 1 124 ? -17.065 46.080  151.207 1.00 21.16  ? 170 TYR A CD1 1 
ATOM 1000 C CD2 . TYR A 1 124 ? -15.004 46.541  150.115 1.00 20.61  ? 170 TYR A CD2 1 
ATOM 1001 C CE1 . TYR A 1 124 ? -16.579 46.636  152.369 1.00 22.27  ? 170 TYR A CE1 1 
ATOM 1002 C CE2 . TYR A 1 124 ? -14.509 47.099  151.273 1.00 24.07  ? 170 TYR A CE2 1 
ATOM 1003 C CZ  . TYR A 1 124 ? -15.301 47.145  152.397 1.00 26.21  ? 170 TYR A CZ  1 
ATOM 1004 O OH  . TYR A 1 124 ? -14.816 47.701  153.556 1.00 33.90  ? 170 TYR A OH  1 
ATOM 1005 N N   . THR A 1 125 ? -18.516 42.475  148.179 1.00 24.10  ? 171 THR A N   1 
ATOM 1006 C CA  . THR A 1 125 ? -19.534 41.865  147.342 1.00 24.78  ? 171 THR A CA  1 
ATOM 1007 C C   . THR A 1 125 ? -20.878 41.888  148.053 1.00 27.68  ? 171 THR A C   1 
ATOM 1008 O O   . THR A 1 125 ? -20.935 41.841  149.286 1.00 29.97  ? 171 THR A O   1 
ATOM 1009 C CB  . THR A 1 125 ? -19.158 40.420  146.979 1.00 30.27  ? 171 THR A CB  1 
ATOM 1010 O OG1 . THR A 1 125 ? -20.110 39.888  146.049 1.00 32.81  ? 171 THR A OG1 1 
ATOM 1011 C CG2 . THR A 1 125 ? -19.111 39.546  148.217 1.00 30.81  ? 171 THR A CG2 1 
ATOM 1012 N N   . PRO A 1 126 ? -21.979 41.985  147.300 1.00 27.69  ? 172 PRO A N   1 
ATOM 1013 C CA  . PRO A 1 126 ? -23.303 41.983  147.939 1.00 24.54  ? 172 PRO A CA  1 
ATOM 1014 C C   . PRO A 1 126 ? -23.754 40.619  148.426 1.00 28.74  ? 172 PRO A C   1 
ATOM 1015 O O   . PRO A 1 126 ? -24.620 40.556  149.309 1.00 33.65  ? 172 PRO A O   1 
ATOM 1016 C CB  . PRO A 1 126 ? -24.235 42.497  146.829 1.00 18.18  ? 172 PRO A CB  1 
ATOM 1017 C CG  . PRO A 1 126 ? -23.333 43.086  145.790 1.00 26.37  ? 172 PRO A CG  1 
ATOM 1018 C CD  . PRO A 1 126 ? -22.064 42.313  145.869 1.00 26.53  ? 172 PRO A CD  1 
ATOM 1019 N N   . VAL A 1 127 ? -23.202 39.529  147.885 1.00 25.72  ? 173 VAL A N   1 
ATOM 1020 C CA  . VAL A 1 127 ? -23.655 38.190  148.256 1.00 24.05  ? 173 VAL A CA  1 
ATOM 1021 C C   . VAL A 1 127 ? -22.970 37.648  149.497 1.00 29.47  ? 173 VAL A C   1 
ATOM 1022 O O   . VAL A 1 127 ? -23.373 36.593  150.001 1.00 36.17  ? 173 VAL A O   1 
ATOM 1023 C CB  . VAL A 1 127 ? -23.439 37.193  147.103 1.00 23.93  ? 173 VAL A CB  1 
ATOM 1024 C CG1 . VAL A 1 127 ? -24.148 37.675  145.853 1.00 24.04  ? 173 VAL A CG1 1 
ATOM 1025 C CG2 . VAL A 1 127 ? -21.958 36.996  146.843 1.00 21.62  ? 173 VAL A CG2 1 
ATOM 1026 N N   . ASN A 1 128 ? -21.945 38.329  150.005 1.00 26.72  ? 174 ASN A N   1 
ATOM 1027 C CA  . ASN A 1 128 ? -21.218 37.870  151.182 1.00 24.17  ? 174 ASN A CA  1 
ATOM 1028 C C   . ASN A 1 128 ? -20.920 39.066  152.069 1.00 23.71  ? 174 ASN A C   1 
ATOM 1029 O O   . ASN A 1 128 ? -20.164 39.958  151.676 1.00 27.51  ? 174 ASN A O   1 
ATOM 1030 C CB  . ASN A 1 128 ? -19.923 37.157  150.786 1.00 21.87  ? 174 ASN A CB  1 
ATOM 1031 C CG  . ASN A 1 128 ? -19.449 36.185  151.841 1.00 28.70  ? 174 ASN A CG  1 
ATOM 1032 O OD1 . ASN A 1 128 ? -19.621 36.416  153.036 1.00 33.64  ? 174 ASN A OD1 1 
ATOM 1033 N ND2 . ASN A 1 128 ? -18.844 35.088  151.405 1.00 30.74  ? 174 ASN A ND2 1 
ATOM 1034 N N   . LYS A 1 129 ? -21.515 39.084  153.260 1.00 26.72  ? 175 LYS A N   1 
ATOM 1035 C CA  . LYS A 1 129 ? -21.286 40.167  154.205 1.00 28.59  ? 175 LYS A CA  1 
ATOM 1036 C C   . LYS A 1 129 ? -19.974 40.024  154.962 1.00 29.60  ? 175 LYS A C   1 
ATOM 1037 O O   . LYS A 1 129 ? -19.552 40.979  155.621 1.00 31.21  ? 175 LYS A O   1 
ATOM 1038 C CB  . LYS A 1 129 ? -22.443 40.247  155.202 1.00 28.05  ? 175 LYS A CB  1 
ATOM 1039 C CG  . LYS A 1 129 ? -23.732 40.787  154.614 1.00 26.69  ? 175 LYS A CG  1 
ATOM 1040 C CD  . LYS A 1 129 ? -23.766 42.299  154.672 1.00 26.52  ? 175 LYS A CD  1 
ATOM 1041 C CE  . LYS A 1 129 ? -24.674 42.859  153.597 1.00 28.86  ? 175 LYS A CE  1 
ATOM 1042 N NZ  . LYS A 1 129 ? -24.662 42.008  152.376 1.00 33.46  ? 175 LYS A NZ  1 
ATOM 1043 N N   . TYR A 1 130 ? -19.328 38.860  154.893 1.00 24.30  ? 176 TYR A N   1 
ATOM 1044 C CA  . TYR A 1 130 ? -18.043 38.677  155.555 1.00 23.74  ? 176 TYR A CA  1 
ATOM 1045 C C   . TYR A 1 130 ? -16.925 39.438  154.859 1.00 27.70  ? 176 TYR A C   1 
ATOM 1046 O O   . TYR A 1 130 ? -15.914 39.751  155.495 1.00 33.15  ? 176 TYR A O   1 
ATOM 1047 C CB  . TYR A 1 130 ? -17.688 37.193  155.612 1.00 24.55  ? 176 TYR A CB  1 
ATOM 1048 C CG  . TYR A 1 130 ? -18.535 36.384  156.564 1.00 22.68  ? 176 TYR A CG  1 
ATOM 1049 C CD1 . TYR A 1 130 ? -18.559 36.669  157.920 1.00 25.70  ? 176 TYR A CD1 1 
ATOM 1050 C CD2 . TYR A 1 130 ? -19.305 35.329  156.105 1.00 25.13  ? 176 TYR A CD2 1 
ATOM 1051 C CE1 . TYR A 1 130 ? -19.327 35.927  158.791 1.00 26.48  ? 176 TYR A CE1 1 
ATOM 1052 C CE2 . TYR A 1 130 ? -20.077 34.584  156.968 1.00 28.95  ? 176 TYR A CE2 1 
ATOM 1053 C CZ  . TYR A 1 130 ? -20.084 34.886  158.308 1.00 29.06  ? 176 TYR A CZ  1 
ATOM 1054 O OH  . TYR A 1 130 ? -20.853 34.139  159.166 1.00 34.11  ? 176 TYR A OH  1 
ATOM 1055 N N   . PHE A 1 131 ? -17.085 39.737  153.579 1.00 28.80  ? 177 PHE A N   1 
ATOM 1056 C CA  . PHE A 1 131 ? -16.034 40.386  152.810 1.00 23.96  ? 177 PHE A CA  1 
ATOM 1057 C C   . PHE A 1 131 ? -15.998 41.875  153.126 1.00 24.42  ? 177 PHE A C   1 
ATOM 1058 O O   . PHE A 1 131 ? -17.019 42.554  152.970 1.00 29.14  ? 177 PHE A O   1 
ATOM 1059 C CB  . PHE A 1 131 ? -16.267 40.173  151.321 1.00 28.90  ? 177 PHE A CB  1 
ATOM 1060 C CG  . PHE A 1 131 ? -15.770 38.852  150.809 1.00 30.63  ? 177 PHE A CG  1 
ATOM 1061 C CD1 . PHE A 1 131 ? -15.548 37.796  151.674 1.00 27.82  ? 177 PHE A CD1 1 
ATOM 1062 C CD2 . PHE A 1 131 ? -15.538 38.662  149.460 1.00 37.76  ? 177 PHE A CD2 1 
ATOM 1063 C CE1 . PHE A 1 131 ? -15.093 36.582  151.204 1.00 29.69  ? 177 PHE A CE1 1 
ATOM 1064 C CE2 . PHE A 1 131 ? -15.085 37.449  148.985 1.00 35.01  ? 177 PHE A CE2 1 
ATOM 1065 C CZ  . PHE A 1 131 ? -14.863 36.408  149.858 1.00 31.72  ? 177 PHE A CZ  1 
ATOM 1066 N N   . PRO A 1 132 ? -14.863 42.422  153.573 1.00 24.84  ? 178 PRO A N   1 
ATOM 1067 C CA  . PRO A 1 132 ? -13.621 41.741  153.928 1.00 32.25  ? 178 PRO A CA  1 
ATOM 1068 C C   . PRO A 1 132 ? -13.331 41.831  155.420 1.00 29.79  ? 178 PRO A C   1 
ATOM 1069 O O   . PRO A 1 132 ? -12.255 41.455  155.877 1.00 31.19  ? 178 PRO A O   1 
ATOM 1070 C CB  . PRO A 1 132 ? -12.592 42.512  153.106 1.00 23.48  ? 178 PRO A CB  1 
ATOM 1071 C CG  . PRO A 1 132 ? -13.118 43.946  153.145 1.00 22.96  ? 178 PRO A CG  1 
ATOM 1072 C CD  . PRO A 1 132 ? -14.619 43.862  153.401 1.00 23.70  ? 178 PRO A CD  1 
ATOM 1073 N N   . ARG A 1 133 ? -14.289 42.344  156.194 1.00 29.84  ? 179 ARG A N   1 
ATOM 1074 C CA  . ARG A 1 133 ? -14.034 42.634  157.599 1.00 26.56  ? 179 ARG A CA  1 
ATOM 1075 C C   . ARG A 1 133 ? -13.787 41.360  158.396 1.00 32.19  ? 179 ARG A C   1 
ATOM 1076 O O   . ARG A 1 133 ? -12.927 41.337  159.283 1.00 39.58  ? 179 ARG A O   1 
ATOM 1077 C CB  . ARG A 1 133 ? -15.202 43.427  158.183 1.00 27.82  ? 179 ARG A CB  1 
ATOM 1078 C CG  . ARG A 1 133 ? -15.115 43.667  159.675 1.00 33.64  ? 179 ARG A CG  1 
ATOM 1079 C CD  . ARG A 1 133 ? -16.499 43.741  160.303 1.00 37.27  ? 179 ARG A CD  1 
ATOM 1080 N NE  . ARG A 1 133 ? -16.456 43.987  161.741 1.00 41.88  ? 179 ARG A NE  1 
ATOM 1081 C CZ  . ARG A 1 133 ? -15.927 45.060  162.314 1.00 41.61  ? 179 ARG A CZ  1 
ATOM 1082 N NH1 . ARG A 1 133 ? -15.428 46.056  161.600 1.00 34.48  ? 179 ARG A NH1 1 
ATOM 1083 N NH2 . ARG A 1 133 ? -15.912 45.144  163.641 1.00 39.39  ? 179 ARG A NH2 1 
ATOM 1084 N N   . ALA A 1 134 ? -14.526 40.290  158.098 1.00 34.48  ? 180 ALA A N   1 
ATOM 1085 C CA  . ALA A 1 134 ? -14.306 39.028  158.798 1.00 33.84  ? 180 ALA A CA  1 
ATOM 1086 C C   . ALA A 1 134 ? -12.921 38.466  158.505 1.00 35.72  ? 180 ALA A C   1 
ATOM 1087 O O   . ALA A 1 134 ? -12.234 37.989  159.415 1.00 39.73  ? 180 ALA A O   1 
ATOM 1088 C CB  . ALA A 1 134 ? -15.382 38.017  158.413 1.00 26.84  ? 180 ALA A CB  1 
ATOM 1089 N N   . LEU A 1 135 ? -12.494 38.514  157.243 1.00 27.17  ? 181 LEU A N   1 
ATOM 1090 C CA  . LEU A 1 135 ? -11.160 38.039  156.895 1.00 24.45  ? 181 LEU A CA  1 
ATOM 1091 C C   . LEU A 1 135 ? -10.082 38.876  157.571 1.00 24.03  ? 181 LEU A C   1 
ATOM 1092 O O   . LEU A 1 135 ? -9.090  38.334  158.071 1.00 32.55  ? 181 LEU A O   1 
ATOM 1093 C CB  . LEU A 1 135 ? -10.980 38.051  155.379 1.00 26.45  ? 181 LEU A CB  1 
ATOM 1094 C CG  . LEU A 1 135 ? -11.690 36.938  154.608 1.00 20.48  ? 181 LEU A CG  1 
ATOM 1095 C CD1 . LEU A 1 135 ? -13.082 37.369  154.205 1.00 29.52  ? 181 LEU A CD1 1 
ATOM 1096 C CD2 . LEU A 1 135 ? -10.889 36.545  153.384 1.00 23.11  ? 181 LEU A CD2 1 
ATOM 1097 N N   . LEU A 1 136 ? -10.260 40.199  157.598 1.00 32.05  ? 182 LEU A N   1 
ATOM 1098 C CA  . LEU A 1 136 ? -9.286  41.059  158.261 1.00 27.72  ? 182 LEU A CA  1 
ATOM 1099 C C   . LEU A 1 136 ? -9.238  40.802  159.760 1.00 26.65  ? 182 LEU A C   1 
ATOM 1100 O O   . LEU A 1 136 ? -8.160  40.856  160.362 1.00 32.65  ? 182 LEU A O   1 
ATOM 1101 C CB  . LEU A 1 136 ? -9.603  42.526  157.979 1.00 24.73  ? 182 LEU A CB  1 
ATOM 1102 C CG  . LEU A 1 136 ? -9.409  42.976  156.531 1.00 18.89  ? 182 LEU A CG  1 
ATOM 1103 C CD1 . LEU A 1 136 ? -9.615  44.471  156.403 1.00 27.32  ? 182 LEU A CD1 1 
ATOM 1104 C CD2 . LEU A 1 136 ? -8.035  42.580  156.034 1.00 24.53  ? 182 LEU A CD2 1 
ATOM 1105 N N   . VAL A 1 137 ? -10.388 40.535  160.379 1.00 23.57  ? 183 VAL A N   1 
ATOM 1106 C CA  . VAL A 1 137 ? -10.412 40.184  161.794 1.00 26.47  ? 183 VAL A CA  1 
ATOM 1107 C C   . VAL A 1 137 ? -9.684  38.867  162.028 1.00 26.16  ? 183 VAL A C   1 
ATOM 1108 O O   . VAL A 1 137 ? -8.910  38.730  162.983 1.00 30.06  ? 183 VAL A O   1 
ATOM 1109 C CB  . VAL A 1 137 ? -11.865 40.131  162.301 1.00 25.49  ? 183 VAL A CB  1 
ATOM 1110 C CG1 . VAL A 1 137 ? -11.993 39.178  163.476 1.00 22.01  ? 183 VAL A CG1 1 
ATOM 1111 C CG2 . VAL A 1 137 ? -12.339 41.520  162.688 1.00 31.23  ? 183 VAL A CG2 1 
ATOM 1112 N N   . ALA A 1 138 ? -9.916  37.881  161.159 1.00 27.08  ? 184 ALA A N   1 
ATOM 1113 C CA  . ALA A 1 138 ? -9.255  36.589  161.308 1.00 28.38  ? 184 ALA A CA  1 
ATOM 1114 C C   . ALA A 1 138 ? -7.744  36.718  161.170 1.00 30.08  ? 184 ALA A C   1 
ATOM 1115 O O   . ALA A 1 138 ? -6.992  36.090  161.923 1.00 37.57  ? 184 ALA A O   1 
ATOM 1116 C CB  . ALA A 1 138 ? -9.803  35.598  160.283 1.00 28.15  ? 184 ALA A CB  1 
ATOM 1117 N N   . LEU A 1 139 ? -7.280  37.525  160.213 1.00 32.09  ? 185 LEU A N   1 
ATOM 1118 C CA  . LEU A 1 139 ? -5.842  37.716  160.052 1.00 18.63  ? 185 LEU A CA  1 
ATOM 1119 C C   . LEU A 1 139 ? -5.243  38.498  161.212 1.00 22.35  ? 185 LEU A C   1 
ATOM 1120 O O   . LEU A 1 139 ? -4.031  38.428  161.443 1.00 34.04  ? 185 LEU A O   1 
ATOM 1121 C CB  . LEU A 1 139 ? -5.547  38.418  158.730 1.00 19.83  ? 185 LEU A CB  1 
ATOM 1122 C CG  . LEU A 1 139 ? -5.781  37.561  157.488 1.00 27.45  ? 185 LEU A CG  1 
ATOM 1123 C CD1 . LEU A 1 139 ? -5.555  38.367  156.224 1.00 32.43  ? 185 LEU A CD1 1 
ATOM 1124 C CD2 . LEU A 1 139 ? -4.883  36.338  157.514 1.00 25.66  ? 185 LEU A CD2 1 
ATOM 1125 N N   . GLY A 1 140 ? -6.060  39.243  161.944 1.00 29.61  ? 186 GLY A N   1 
ATOM 1126 C CA  . GLY A 1 140 ? -5.606  39.964  163.107 1.00 26.74  ? 186 GLY A CA  1 
ATOM 1127 C C   . GLY A 1 140 ? -5.268  41.422  162.896 1.00 30.55  ? 186 GLY A C   1 
ATOM 1128 O O   . GLY A 1 140 ? -4.376  41.932  163.580 1.00 41.05  ? 186 GLY A O   1 
ATOM 1129 N N   . VAL A 1 141 ? -5.945  42.108  161.978 1.00 28.80  ? 187 VAL A N   1 
ATOM 1130 C CA  . VAL A 1 141 ? -5.675  43.519  161.723 1.00 26.34  ? 187 VAL A CA  1 
ATOM 1131 C C   . VAL A 1 141 ? -6.922  44.336  162.023 1.00 34.58  ? 187 VAL A C   1 
ATOM 1132 O O   . VAL A 1 141 ? -7.967  43.787  162.386 1.00 39.92  ? 187 VAL A O   1 
ATOM 1133 C CB  . VAL A 1 141 ? -5.206  43.749  160.276 1.00 27.52  ? 187 VAL A CB  1 
ATOM 1134 C CG1 . VAL A 1 141 ? -4.065  42.816  159.938 1.00 32.53  ? 187 VAL A CG1 1 
ATOM 1135 C CG2 . VAL A 1 141 ? -6.357  43.556  159.311 1.00 32.31  ? 187 VAL A CG2 1 
ATOM 1136 N N   . ASP A 1 142 ? -6.818  45.656  161.877 1.00 42.20  ? 188 ASP A N   1 
ATOM 1137 C CA  . ASP A 1 142 ? -7.951  46.539  162.097 1.00 43.06  ? 188 ASP A CA  1 
ATOM 1138 C C   . ASP A 1 142 ? -8.508  46.974  160.752 1.00 44.15  ? 188 ASP A C   1 
ATOM 1139 O O   . ASP A 1 142 ? -7.828  47.713  160.019 1.00 50.76  ? 188 ASP A O   1 
ATOM 1140 C CB  . ASP A 1 142 ? -7.539  47.754  162.923 1.00 44.07  ? 188 ASP A CB  1 
ATOM 1141 C CG  . ASP A 1 142 ? -8.723  48.459  163.548 1.00 47.02  ? 188 ASP A CG  1 
ATOM 1142 O OD1 . ASP A 1 142 ? -9.807  47.846  163.625 1.00 43.97  ? 188 ASP A OD1 1 
ATOM 1143 O OD2 . ASP A 1 142 ? -8.571  49.626  163.964 1.00 46.90  ? 188 ASP A OD2 1 
ATOM 1144 N N   . PRO A 1 143 ? -9.711  46.536  160.374 1.00 34.26  ? 189 PRO A N   1 
ATOM 1145 C CA  . PRO A 1 143 ? -10.262 46.940  159.072 1.00 38.45  ? 189 PRO A CA  1 
ATOM 1146 C C   . PRO A 1 143 ? -10.414 48.441  158.920 1.00 39.86  ? 189 PRO A C   1 
ATOM 1147 O O   . PRO A 1 143 ? -10.216 48.963  157.818 1.00 43.51  ? 189 PRO A O   1 
ATOM 1148 C CB  . PRO A 1 143 ? -11.620 46.227  159.031 1.00 43.18  ? 189 PRO A CB  1 
ATOM 1149 C CG  . PRO A 1 143 ? -11.508 45.121  160.029 1.00 36.97  ? 189 PRO A CG  1 
ATOM 1150 C CD  . PRO A 1 143 ? -10.610 45.629  161.103 1.00 31.59  ? 189 PRO A CD  1 
ATOM 1151 N N   . GLU A 1 144 ? -10.757 49.153  159.995 1.00 38.58  ? 190 GLU A N   1 
ATOM 1152 C CA  . GLU A 1 144 ? -10.815 50.609  159.924 1.00 39.53  ? 190 GLU A CA  1 
ATOM 1153 C C   . GLU A 1 144 ? -9.440  51.193  159.633 1.00 43.03  ? 190 GLU A C   1 
ATOM 1154 O O   . GLU A 1 144 ? -9.311  52.128  158.832 1.00 44.92  ? 190 GLU A O   1 
ATOM 1155 C CB  . GLU A 1 144 ? -11.379 51.183  161.224 1.00 40.00  ? 190 GLU A CB  1 
ATOM 1156 C CG  . GLU A 1 144 ? -12.856 50.886  161.475 1.00 44.35  ? 190 GLU A CG  1 
ATOM 1157 C CD  . GLU A 1 144 ? -13.143 49.412  161.690 1.00 48.63  ? 190 GLU A CD  1 
ATOM 1158 O OE1 . GLU A 1 144 ? -14.008 48.862  160.978 1.00 47.51  ? 190 GLU A OE1 1 
ATOM 1159 O OE2 . GLU A 1 144 ? -12.504 48.803  162.575 1.00 49.71  ? 190 GLU A OE2 1 
ATOM 1160 N N   . ASP A 1 145 ? -8.400  50.649  160.267 1.00 41.57  ? 191 ASP A N   1 
ATOM 1161 C CA  . ASP A 1 145 ? -7.044  51.111  159.998 1.00 36.97  ? 191 ASP A CA  1 
ATOM 1162 C C   . ASP A 1 145 ? -6.656  50.867  158.547 1.00 37.57  ? 191 ASP A C   1 
ATOM 1163 O O   . ASP A 1 145 ? -6.059  51.739  157.906 1.00 46.21  ? 191 ASP A O   1 
ATOM 1164 C CB  . ASP A 1 145 ? -6.057  50.419  160.935 1.00 41.62  ? 191 ASP A CB  1 
ATOM 1165 C CG  . ASP A 1 145 ? -4.615  50.687  160.559 1.00 50.83  ? 191 ASP A CG  1 
ATOM 1166 O OD1 . ASP A 1 145 ? -4.083  51.743  160.958 1.00 51.27  ? 191 ASP A OD1 1 
ATOM 1167 O OD2 . ASP A 1 145 ? -4.013  49.843  159.862 1.00 48.68  ? 191 ASP A OD2 1 
ATOM 1168 N N   . VAL A 1 146 ? -6.985  49.690  158.011 1.00 25.04  ? 192 VAL A N   1 
ATOM 1169 C CA  . VAL A 1 146 ? -6.641  49.400  156.622 1.00 26.90  ? 192 VAL A CA  1 
ATOM 1170 C C   . VAL A 1 146 ? -7.405  50.320  155.676 1.00 36.34  ? 192 VAL A C   1 
ATOM 1171 O O   . VAL A 1 146 ? -6.846  50.834  154.701 1.00 42.14  ? 192 VAL A O   1 
ATOM 1172 C CB  . VAL A 1 146 ? -6.894  47.918  156.299 1.00 28.87  ? 192 VAL A CB  1 
ATOM 1173 C CG1 . VAL A 1 146 ? -6.370  47.595  154.917 1.00 32.43  ? 192 VAL A CG1 1 
ATOM 1174 C CG2 . VAL A 1 146 ? -6.235  47.030  157.334 1.00 36.68  ? 192 VAL A CG2 1 
ATOM 1175 N N   . PHE A 1 147 ? -8.692  50.547  155.946 1.00 34.69  ? 193 PHE A N   1 
ATOM 1176 C CA  . PHE A 1 147 ? -9.471  51.451  155.108 1.00 33.09  ? 193 PHE A CA  1 
ATOM 1177 C C   . PHE A 1 147 ? -8.918  52.869  155.146 1.00 37.25  ? 193 PHE A C   1 
ATOM 1178 O O   . PHE A 1 147 ? -8.903  53.554  154.118 1.00 41.67  ? 193 PHE A O   1 
ATOM 1179 C CB  . PHE A 1 147 ? -10.934 51.442  155.544 1.00 39.13  ? 193 PHE A CB  1 
ATOM 1180 C CG  . PHE A 1 147 ? -11.844 52.201  154.623 1.00 45.61  ? 193 PHE A CG  1 
ATOM 1181 C CD1 . PHE A 1 147 ? -11.902 51.891  153.276 1.00 43.72  ? 193 PHE A CD1 1 
ATOM 1182 C CD2 . PHE A 1 147 ? -12.634 53.231  155.102 1.00 41.51  ? 193 PHE A CD2 1 
ATOM 1183 C CE1 . PHE A 1 147 ? -12.735 52.590  152.426 1.00 42.70  ? 193 PHE A CE1 1 
ATOM 1184 C CE2 . PHE A 1 147 ? -13.468 53.933  154.256 1.00 35.63  ? 193 PHE A CE2 1 
ATOM 1185 C CZ  . PHE A 1 147 ? -13.518 53.611  152.917 1.00 35.97  ? 193 PHE A CZ  1 
ATOM 1186 N N   . ALA A 1 148 ? -8.461  53.325  156.313 1.00 37.44  ? 194 ALA A N   1 
ATOM 1187 C CA  . ALA A 1 148 ? -7.946  54.686  156.416 1.00 37.19  ? 194 ALA A CA  1 
ATOM 1188 C C   . ALA A 1 148 ? -6.561  54.815  155.792 1.00 38.89  ? 194 ALA A C   1 
ATOM 1189 O O   . ALA A 1 148 ? -6.221  55.871  155.246 1.00 42.53  ? 194 ALA A O   1 
ATOM 1190 C CB  . ALA A 1 148 ? -7.917  55.126  157.878 1.00 36.97  ? 194 ALA A CB  1 
ATOM 1191 N N   . ASN A 1 149 ? -5.745  53.765  155.859 1.00 33.53  ? 195 ASN A N   1 
ATOM 1192 C CA  . ASN A 1 149 ? -4.353  53.837  155.433 1.00 28.43  ? 195 ASN A CA  1 
ATOM 1193 C C   . ASN A 1 149 ? -4.031  52.802  154.362 1.00 33.65  ? 195 ASN A C   1 
ATOM 1194 O O   . ASN A 1 149 ? -2.995  52.142  154.413 1.00 41.43  ? 195 ASN A O   1 
ATOM 1195 C CB  . ASN A 1 149 ? -3.420  53.664  156.628 1.00 32.58  ? 195 ASN A CB  1 
ATOM 1196 C CG  . ASN A 1 149 ? -3.931  54.362  157.869 1.00 37.41  ? 195 ASN A CG  1 
ATOM 1197 O OD1 . ASN A 1 149 ? -4.061  53.751  158.928 1.00 39.49  ? 195 ASN A OD1 1 
ATOM 1198 N ND2 . ASN A 1 149 ? -4.219  55.650  157.748 1.00 36.62  ? 195 ASN A ND2 1 
ATOM 1199 N N   . GLN A 1 150 ? -4.944  52.609  153.409 1.00 29.46  ? 196 GLN A N   1 
ATOM 1200 C CA  . GLN A 1 150 ? -4.649  51.757  152.260 1.00 31.44  ? 196 GLN A CA  1 
ATOM 1201 C C   . GLN A 1 150 ? -3.362  52.170  151.552 1.00 39.03  ? 196 GLN A C   1 
ATOM 1202 O O   . GLN A 1 150 ? -2.543  51.314  151.195 1.00 47.84  ? 196 GLN A O   1 
ATOM 1203 C CB  . GLN A 1 150 ? -5.821  51.780  151.283 1.00 26.76  ? 196 GLN A CB  1 
ATOM 1204 C CG  . GLN A 1 150 ? -5.559  51.032  149.993 1.00 29.36  ? 196 GLN A CG  1 
ATOM 1205 C CD  . GLN A 1 150 ? -5.952  49.575  150.084 1.00 37.19  ? 196 GLN A CD  1 
ATOM 1206 O OE1 . GLN A 1 150 ? -6.697  49.177  150.978 1.00 40.95  ? 196 GLN A OE1 1 
ATOM 1207 N NE2 . GLN A 1 150 ? -5.454  48.769  149.155 1.00 35.68  ? 196 GLN A NE2 1 
ATOM 1208 N N   . ALA A 1 151 ? -3.174  53.470  151.317 1.00 29.85  ? 197 ALA A N   1 
ATOM 1209 C CA  . ALA A 1 151 ? -1.968  53.924  150.629 1.00 28.17  ? 197 ALA A CA  1 
ATOM 1210 C C   . ALA A 1 151 ? -0.719  53.612  151.441 1.00 29.96  ? 197 ALA A C   1 
ATOM 1211 O O   . ALA A 1 151 ? 0.296   53.160  150.890 1.00 36.88  ? 197 ALA A O   1 
ATOM 1212 C CB  . ALA A 1 151 ? -2.060  55.421  150.342 1.00 27.82  ? 197 ALA A CB  1 
ATOM 1213 N N   . GLN A 1 152 ? -0.776  53.849  152.752 1.00 31.17  ? 198 GLN A N   1 
ATOM 1214 C CA  . GLN A 1 152 ? 0.357   53.538  153.613 1.00 31.59  ? 198 GLN A CA  1 
ATOM 1215 C C   . GLN A 1 152 ? 0.655   52.047  153.608 1.00 29.02  ? 198 GLN A C   1 
ATOM 1216 O O   . GLN A 1 152 ? 1.820   51.644  153.576 1.00 35.49  ? 198 GLN A O   1 
ATOM 1217 C CB  . GLN A 1 152 ? 0.081   54.029  155.032 1.00 26.22  ? 198 GLN A CB  1 
ATOM 1218 C CG  . GLN A 1 152 ? 0.242   55.525  155.215 1.00 25.00  ? 198 GLN A CG  1 
ATOM 1219 C CD  . GLN A 1 152 ? -1.041  56.280  154.954 1.00 37.96  ? 198 GLN A CD  1 
ATOM 1220 O OE1 . GLN A 1 152 ? -1.622  56.184  153.874 1.00 43.62  ? 198 GLN A OE1 1 
ATOM 1221 N NE2 . GLN A 1 152 ? -1.494  57.036  155.945 1.00 39.54  ? 198 GLN A NE2 1 
ATOM 1222 N N   . TRP A 1 153 ? -0.386  51.213  153.634 1.00 22.07  ? 199 TRP A N   1 
ATOM 1223 C CA  . TRP A 1 153 ? -0.194  49.767  153.592 1.00 26.33  ? 199 TRP A CA  1 
ATOM 1224 C C   . TRP A 1 153 ? 0.456   49.330  152.285 1.00 29.61  ? 199 TRP A C   1 
ATOM 1225 O O   . TRP A 1 153 ? 1.371   48.497  152.286 1.00 38.14  ? 199 TRP A O   1 
ATOM 1226 C CB  . TRP A 1 153 ? -1.537  49.064  153.782 1.00 22.16  ? 199 TRP A CB  1 
ATOM 1227 C CG  . TRP A 1 153 ? -1.909  48.816  155.208 1.00 24.56  ? 199 TRP A CG  1 
ATOM 1228 C CD1 . TRP A 1 153 ? -2.581  49.660  156.041 1.00 29.01  ? 199 TRP A CD1 1 
ATOM 1229 C CD2 . TRP A 1 153 ? -1.644  47.633  155.967 1.00 27.53  ? 199 TRP A CD2 1 
ATOM 1230 N NE1 . TRP A 1 153 ? -2.741  49.081  157.274 1.00 31.40  ? 199 TRP A NE1 1 
ATOM 1231 C CE2 . TRP A 1 153 ? -2.176  47.834  157.254 1.00 29.60  ? 199 TRP A CE2 1 
ATOM 1232 C CE3 . TRP A 1 153 ? -1.004  46.425  155.683 1.00 25.80  ? 199 TRP A CE3 1 
ATOM 1233 C CZ2 . TRP A 1 153 ? -2.088  46.872  158.254 1.00 26.14  ? 199 TRP A CZ2 1 
ATOM 1234 C CZ3 . TRP A 1 153 ? -0.917  45.474  156.675 1.00 30.18  ? 199 TRP A CZ3 1 
ATOM 1235 C CH2 . TRP A 1 153 ? -1.455  45.701  157.945 1.00 32.81  ? 199 TRP A CH2 1 
ATOM 1236 N N   . GLU A 1 154 ? -0.007  49.880  151.161 1.00 20.37  ? 200 GLU A N   1 
ATOM 1237 C CA  . GLU A 1 154 ? 0.580   49.540  149.868 1.00 23.06  ? 200 GLU A CA  1 
ATOM 1238 C C   . GLU A 1 154 ? 2.051   49.927  149.807 1.00 30.60  ? 200 GLU A C   1 
ATOM 1239 O O   . GLU A 1 154 ? 2.899   49.130  149.383 1.00 38.70  ? 200 GLU A O   1 
ATOM 1240 C CB  . GLU A 1 154 ? -0.192  50.232  148.748 1.00 23.61  ? 200 GLU A CB  1 
ATOM 1241 C CG  . GLU A 1 154 ? 0.011   49.616  147.381 1.00 33.70  ? 200 GLU A CG  1 
ATOM 1242 C CD  . GLU A 1 154 ? -0.365  50.568  146.264 1.00 43.70  ? 200 GLU A CD  1 
ATOM 1243 O OE1 . GLU A 1 154 ? 0.413   50.688  145.295 1.00 42.54  ? 200 GLU A OE1 1 
ATOM 1244 O OE2 . GLU A 1 154 ? -1.440  51.195  146.354 1.00 43.23  ? 200 GLU A OE2 1 
ATOM 1245 N N   . TYR A 1 155 ? 2.376   51.148  150.226 1.00 31.80  ? 201 TYR A N   1 
ATOM 1246 C CA  . TYR A 1 155 ? 3.771   51.565  150.164 1.00 23.85  ? 201 TYR A CA  1 
ATOM 1247 C C   . TYR A 1 155 ? 4.628   50.804  151.165 1.00 29.95  ? 201 TYR A C   1 
ATOM 1248 O O   . TYR A 1 155 ? 5.800   50.531  150.888 1.00 39.41  ? 201 TYR A O   1 
ATOM 1249 C CB  . TYR A 1 155 ? 3.874   53.075  150.365 1.00 23.82  ? 201 TYR A CB  1 
ATOM 1250 C CG  . TYR A 1 155 ? 3.477   53.847  149.127 1.00 29.00  ? 201 TYR A CG  1 
ATOM 1251 C CD1 . TYR A 1 155 ? 3.070   53.181  147.979 1.00 23.43  ? 201 TYR A CD1 1 
ATOM 1252 C CD2 . TYR A 1 155 ? 3.507   55.232  149.102 1.00 30.27  ? 201 TYR A CD2 1 
ATOM 1253 C CE1 . TYR A 1 155 ? 2.710   53.866  146.845 1.00 20.01  ? 201 TYR A CE1 1 
ATOM 1254 C CE2 . TYR A 1 155 ? 3.144   55.929  147.967 1.00 33.54  ? 201 TYR A CE2 1 
ATOM 1255 C CZ  . TYR A 1 155 ? 2.746   55.238  146.841 1.00 33.46  ? 201 TYR A CZ  1 
ATOM 1256 O OH  . TYR A 1 155 ? 2.383   55.920  145.705 1.00 44.28  ? 201 TYR A OH  1 
ATOM 1257 N N   . PHE A 1 156 ? 4.058   50.415  152.306 1.00 29.16  ? 202 PHE A N   1 
ATOM 1258 C CA  . PHE A 1 156 ? 4.805   49.623  153.275 1.00 27.79  ? 202 PHE A CA  1 
ATOM 1259 C C   . PHE A 1 156 ? 5.124   48.240  152.730 1.00 23.10  ? 202 PHE A C   1 
ATOM 1260 O O   . PHE A 1 156 ? 6.242   47.746  152.894 1.00 33.21  ? 202 PHE A O   1 
ATOM 1261 C CB  . PHE A 1 156 ? 4.022   49.511  154.581 1.00 24.36  ? 202 PHE A CB  1 
ATOM 1262 C CG  . PHE A 1 156 ? 4.458   48.366  155.445 1.00 24.64  ? 202 PHE A CG  1 
ATOM 1263 C CD1 . PHE A 1 156 ? 5.682   48.396  156.087 1.00 25.48  ? 202 PHE A CD1 1 
ATOM 1264 C CD2 . PHE A 1 156 ? 3.649   47.259  155.610 1.00 30.01  ? 202 PHE A CD2 1 
ATOM 1265 C CE1 . PHE A 1 156 ? 6.087   47.346  156.883 1.00 26.69  ? 202 PHE A CE1 1 
ATOM 1266 C CE2 . PHE A 1 156 ? 4.049   46.207  156.403 1.00 32.88  ? 202 PHE A CE2 1 
ATOM 1267 C CZ  . PHE A 1 156 ? 5.269   46.250  157.041 1.00 24.68  ? 202 PHE A CZ  1 
ATOM 1268 N N   . VAL A 1 157 ? 4.152   47.587  152.088 1.00 12.24  ? 203 VAL A N   1 
ATOM 1269 C CA  . VAL A 1 157 ? 4.435   46.259  151.550 1.00 22.82  ? 203 VAL A CA  1 
ATOM 1270 C C   . VAL A 1 157 ? 5.411   46.351  150.379 1.00 26.65  ? 203 VAL A C   1 
ATOM 1271 O O   . VAL A 1 157 ? 6.274   45.477  150.211 1.00 38.05  ? 203 VAL A O   1 
ATOM 1272 C CB  . VAL A 1 157 ? 3.135   45.517  151.176 1.00 20.24  ? 203 VAL A CB  1 
ATOM 1273 C CG1 . VAL A 1 157 ? 2.375   46.236  150.095 1.00 26.30  ? 203 VAL A CG1 1 
ATOM 1274 C CG2 . VAL A 1 157 ? 3.441   44.097  150.739 1.00 25.17  ? 203 VAL A CG2 1 
ATOM 1275 N N   . ASN A 1 158 ? 5.318   47.407  149.566 1.00 11.88  ? 204 ASN A N   1 
ATOM 1276 C CA  . ASN A 1 158 ? 6.304   47.583  148.503 1.00 14.30  ? 204 ASN A CA  1 
ATOM 1277 C C   . ASN A 1 158 ? 7.705   47.793  149.072 1.00 25.97  ? 204 ASN A C   1 
ATOM 1278 O O   . ASN A 1 158 ? 8.677   47.214  148.571 1.00 26.92  ? 204 ASN A O   1 
ATOM 1279 C CB  . ASN A 1 158 ? 5.901   48.748  147.604 1.00 23.06  ? 204 ASN A CB  1 
ATOM 1280 C CG  . ASN A 1 158 ? 5.043   48.308  146.440 1.00 29.12  ? 204 ASN A CG  1 
ATOM 1281 O OD1 . ASN A 1 158 ? 5.218   47.214  145.906 1.00 26.78  ? 204 ASN A OD1 1 
ATOM 1282 N ND2 . ASN A 1 158 ? 4.106   49.158  146.041 1.00 34.71  ? 204 ASN A ND2 1 
ATOM 1283 N N   . MET A 1 159 ? 7.829   48.609  150.121 1.00 26.91  ? 205 MET A N   1 
ATOM 1284 C CA  . MET A 1 159 ? 9.127   48.797  150.759 1.00 20.50  ? 205 MET A CA  1 
ATOM 1285 C C   . MET A 1 159 ? 9.623   47.507  151.398 1.00 24.05  ? 205 MET A C   1 
ATOM 1286 O O   . MET A 1 159 ? 10.831  47.252  151.417 1.00 32.23  ? 205 MET A O   1 
ATOM 1287 C CB  . MET A 1 159 ? 9.042   49.919  151.797 1.00 23.14  ? 205 MET A CB  1 
ATOM 1288 C CG  . MET A 1 159 ? 10.376  50.332  152.417 1.00 34.65  ? 205 MET A CG  1 
ATOM 1289 S SD  . MET A 1 159 ? 10.887  49.336  153.835 1.00 49.97  ? 205 MET A SD  1 
ATOM 1290 C CE  . MET A 1 159 ? 10.583  50.475  155.181 1.00 21.70  ? 205 MET A CE  1 
ATOM 1291 N N   . VAL A 1 160 ? 8.711   46.688  151.923 1.00 18.94  ? 206 VAL A N   1 
ATOM 1292 C CA  . VAL A 1 160 ? 9.096   45.396  152.481 1.00 23.11  ? 206 VAL A CA  1 
ATOM 1293 C C   . VAL A 1 160 ? 9.690   44.511  151.397 1.00 22.84  ? 206 VAL A C   1 
ATOM 1294 O O   . VAL A 1 160 ? 10.723  43.864  151.600 1.00 26.20  ? 206 VAL A O   1 
ATOM 1295 C CB  . VAL A 1 160 ? 7.886   44.729  153.162 1.00 20.39  ? 206 VAL A CB  1 
ATOM 1296 C CG1 . VAL A 1 160 ? 8.037   43.218  153.167 1.00 15.70  ? 206 VAL A CG1 1 
ATOM 1297 C CG2 . VAL A 1 160 ? 7.722   45.252  154.574 1.00 25.80  ? 206 VAL A CG2 1 
ATOM 1298 N N   . ALA A 1 161 ? 9.054   44.477  150.225 1.00 19.98  ? 207 ALA A N   1 
ATOM 1299 C CA  . ALA A 1 161 ? 9.610   43.715  149.110 1.00 19.83  ? 207 ALA A CA  1 
ATOM 1300 C C   . ALA A 1 161 ? 10.978  44.249  148.701 1.00 20.30  ? 207 ALA A C   1 
ATOM 1301 O O   . ALA A 1 161 ? 11.916  43.473  148.472 1.00 28.81  ? 207 ALA A O   1 
ATOM 1302 C CB  . ALA A 1 161 ? 8.650   43.746  147.923 1.00 26.02  ? 207 ALA A CB  1 
ATOM 1303 N N   . TYR A 1 162 ? 11.114  45.575  148.617 1.00 24.43  ? 208 TYR A N   1 
ATOM 1304 C CA  . TYR A 1 162 ? 12.383  46.163  148.201 1.00 18.54  ? 208 TYR A CA  1 
ATOM 1305 C C   . TYR A 1 162 ? 13.500  45.829  149.183 1.00 20.22  ? 208 TYR A C   1 
ATOM 1306 O O   . TYR A 1 162 ? 14.606  45.461  148.770 1.00 23.29  ? 208 TYR A O   1 
ATOM 1307 C CB  . TYR A 1 162 ? 12.235  47.676  148.052 1.00 16.58  ? 208 TYR A CB  1 
ATOM 1308 C CG  . TYR A 1 162 ? 11.425  48.087  146.846 1.00 20.74  ? 208 TYR A CG  1 
ATOM 1309 C CD1 . TYR A 1 162 ? 11.572  47.432  145.633 1.00 21.57  ? 208 TYR A CD1 1 
ATOM 1310 C CD2 . TYR A 1 162 ? 10.509  49.124  146.923 1.00 23.80  ? 208 TYR A CD2 1 
ATOM 1311 C CE1 . TYR A 1 162 ? 10.832  47.802  144.531 1.00 21.55  ? 208 TYR A CE1 1 
ATOM 1312 C CE2 . TYR A 1 162 ? 9.763   49.499  145.827 1.00 26.13  ? 208 TYR A CE2 1 
ATOM 1313 C CZ  . TYR A 1 162 ? 9.929   48.836  144.634 1.00 24.29  ? 208 TYR A CZ  1 
ATOM 1314 O OH  . TYR A 1 162 ? 9.188   49.209  143.538 1.00 30.33  ? 208 TYR A OH  1 
ATOM 1315 N N   . ARG A 1 163 ? 13.233  45.945  150.486 1.00 17.56  ? 209 ARG A N   1 
ATOM 1316 C CA  . ARG A 1 163 ? 14.236  45.615  151.490 1.00 11.40  ? 209 ARG A CA  1 
ATOM 1317 C C   . ARG A 1 163 ? 14.513  44.123  151.575 1.00 11.74  ? 209 ARG A C   1 
ATOM 1318 O O   . ARG A 1 163 ? 15.629  43.735  151.933 1.00 19.47  ? 209 ARG A O   1 
ATOM 1319 C CB  . ARG A 1 163 ? 13.813  46.147  152.860 1.00 8.11   ? 209 ARG A CB  1 
ATOM 1320 C CG  . ARG A 1 163 ? 14.016  47.653  153.064 1.00 18.84  ? 209 ARG A CG  1 
ATOM 1321 C CD  . ARG A 1 163 ? 15.426  48.146  152.692 1.00 29.65  ? 209 ARG A CD  1 
ATOM 1322 N NE  . ARG A 1 163 ? 15.610  48.365  151.261 1.00 28.82  ? 209 ARG A NE  1 
ATOM 1323 C CZ  . ARG A 1 163 ? 16.763  48.224  150.622 1.00 16.97  ? 209 ARG A CZ  1 
ATOM 1324 N NH1 . ARG A 1 163 ? 17.874  47.908  151.265 1.00 12.43  ? 209 ARG A NH1 1 
ATOM 1325 N NH2 . ARG A 1 163 ? 16.802  48.400  149.305 1.00 10.68  ? 209 ARG A NH2 1 
ATOM 1326 N N   . ALA A 1 164 ? 13.530  43.281  151.259 1.00 23.56  ? 210 ALA A N   1 
ATOM 1327 C CA  . ALA A 1 164 ? 13.778  41.852  151.152 1.00 22.91  ? 210 ALA A CA  1 
ATOM 1328 C C   . ALA A 1 164 ? 14.577  41.504  149.909 1.00 20.05  ? 210 ALA A C   1 
ATOM 1329 O O   . ALA A 1 164 ? 15.134  40.405  149.833 1.00 23.32  ? 210 ALA A O   1 
ATOM 1330 C CB  . ALA A 1 164 ? 12.455  41.086  151.147 1.00 21.07  ? 210 ALA A CB  1 
ATOM 1331 N N   . GLY A 1 165 ? 14.640  42.408  148.938 1.00 26.10  ? 211 GLY A N   1 
ATOM 1332 C CA  . GLY A 1 165 ? 15.494  42.204  147.790 1.00 24.66  ? 211 GLY A CA  1 
ATOM 1333 C C   . GLY A 1 165 ? 16.971  42.411  148.037 1.00 23.58  ? 211 GLY A C   1 
ATOM 1334 O O   . GLY A 1 165 ? 17.779  42.148  147.143 1.00 24.76  ? 211 GLY A O   1 
ATOM 1335 N N   . ALA A 1 166 ? 17.351  42.883  149.226 1.00 26.50  ? 212 ALA A N   1 
ATOM 1336 C CA  . ALA A 1 166 ? 18.764  43.083  149.530 1.00 23.44  ? 212 ALA A CA  1 
ATOM 1337 C C   . ALA A 1 166 ? 19.500  41.753  149.633 1.00 26.78  ? 212 ALA A C   1 
ATOM 1338 O O   . ALA A 1 166 ? 20.579  41.584  149.054 1.00 36.16  ? 212 ALA A O   1 
ATOM 1339 C CB  . ALA A 1 166 ? 18.916  43.883  150.822 1.00 21.86  ? 212 ALA A CB  1 
ATOM 1340 N N   . PHE A 1 167 ? 18.941  40.804  150.376 1.00 30.25  ? 213 PHE A N   1 
ATOM 1341 C CA  . PHE A 1 167 ? 19.521  39.476  150.492 1.00 27.85  ? 213 PHE A CA  1 
ATOM 1342 C C   . PHE A 1 167 ? 19.082  38.599  149.323 1.00 30.64  ? 213 PHE A C   1 
ATOM 1343 O O   . PHE A 1 167 ? 18.156  38.923  148.578 1.00 37.89  ? 213 PHE A O   1 
ATOM 1344 C CB  . PHE A 1 167 ? 19.132  38.828  151.816 1.00 23.56  ? 213 PHE A CB  1 
ATOM 1345 C CG  . PHE A 1 167 ? 19.015  39.797  152.951 1.00 33.28  ? 213 PHE A CG  1 
ATOM 1346 C CD1 . PHE A 1 167 ? 20.130  40.157  153.685 1.00 35.84  ? 213 PHE A CD1 1 
ATOM 1347 C CD2 . PHE A 1 167 ? 17.792  40.349  153.285 1.00 29.25  ? 213 PHE A CD2 1 
ATOM 1348 C CE1 . PHE A 1 167 ? 20.027  41.049  154.729 1.00 35.33  ? 213 PHE A CE1 1 
ATOM 1349 C CE2 . PHE A 1 167 ? 17.683  41.239  154.327 1.00 28.26  ? 213 PHE A CE2 1 
ATOM 1350 C CZ  . PHE A 1 167 ? 18.802  41.591  155.048 1.00 32.55  ? 213 PHE A CZ  1 
ATOM 1351 N N   . ALA A 1 168 ? 19.764  37.469  149.170 1.00 23.07  ? 214 ALA A N   1 
ATOM 1352 C CA  . ALA A 1 168 ? 19.538  36.576  148.047 1.00 23.04  ? 214 ALA A CA  1 
ATOM 1353 C C   . ALA A 1 168 ? 19.277  35.164  148.548 1.00 30.29  ? 214 ALA A C   1 
ATOM 1354 O O   . ALA A 1 168 ? 19.922  34.691  149.485 1.00 37.59  ? 214 ALA A O   1 
ATOM 1355 C CB  . ALA A 1 168 ? 20.732  36.581  147.090 1.00 24.39  ? 214 ALA A CB  1 
ATOM 1356 N N   . ALA A 1 169 ? 18.315  34.499  147.918 1.00 26.08  ? 215 ALA A N   1 
ATOM 1357 C CA  . ALA A 1 169 ? 17.981  33.117  148.215 1.00 21.37  ? 215 ALA A CA  1 
ATOM 1358 C C   . ALA A 1 169 ? 17.727  32.384  146.908 1.00 24.67  ? 215 ALA A C   1 
ATOM 1359 O O   . ALA A 1 169 ? 17.315  33.003  145.919 1.00 28.42  ? 215 ALA A O   1 
ATOM 1360 C CB  . ALA A 1 169 ? 16.747  33.016  149.125 1.00 22.37  ? 215 ALA A CB  1 
ATOM 1361 N N   . PRO A 1 170 ? 17.978  31.076  146.865 1.00 24.14  ? 216 PRO A N   1 
ATOM 1362 C CA  . PRO A 1 170 ? 17.747  30.326  145.625 1.00 23.07  ? 216 PRO A CA  1 
ATOM 1363 C C   . PRO A 1 170 ? 16.272  30.278  145.262 1.00 32.65  ? 216 PRO A C   1 
ATOM 1364 O O   . PRO A 1 170 ? 15.400  30.208  146.130 1.00 42.17  ? 216 PRO A O   1 
ATOM 1365 C CB  . PRO A 1 170 ? 18.284  28.926  145.947 1.00 31.10  ? 216 PRO A CB  1 
ATOM 1366 C CG  . PRO A 1 170 ? 19.135  29.098  147.157 1.00 33.66  ? 216 PRO A CG  1 
ATOM 1367 C CD  . PRO A 1 170 ? 18.545  30.227  147.923 1.00 30.47  ? 216 PRO A CD  1 
ATOM 1368 N N   . ALA A 1 171 ? 16.001  30.306  143.960 1.00 32.81  ? 217 ALA A N   1 
ATOM 1369 C CA  . ALA A 1 171 ? 14.644  30.176  143.452 1.00 31.65  ? 217 ALA A CA  1 
ATOM 1370 C C   . ALA A 1 171 ? 14.313  28.759  143.012 1.00 32.69  ? 217 ALA A C   1 
ATOM 1371 O O   . ALA A 1 171 ? 13.133  28.439  142.841 1.00 30.31  ? 217 ALA A O   1 
ATOM 1372 C CB  . ALA A 1 171 ? 14.420  31.136  142.281 1.00 32.20  ? 217 ALA A CB  1 
ATOM 1373 N N   . SER A 1 172 ? 15.324  27.910  142.819 1.00 39.72  ? 218 SER A N   1 
ATOM 1374 C CA  . SER A 1 172 ? 15.062  26.515  142.489 1.00 39.64  ? 218 SER A CA  1 
ATOM 1375 C C   . SER A 1 172 ? 14.422  25.789  143.663 1.00 41.20  ? 218 SER A C   1 
ATOM 1376 O O   . SER A 1 172 ? 13.559  24.925  143.470 1.00 49.37  ? 218 SER A O   1 
ATOM 1377 C CB  . SER A 1 172 ? 16.359  25.825  142.071 1.00 44.61  ? 218 SER A CB  1 
ATOM 1378 O OG  . SER A 1 172 ? 17.041  26.579  141.084 1.00 47.78  ? 218 SER A OG  1 
ATOM 1379 N N   . MET A 1 173 ? 14.832  26.124  144.883 1.00 36.32  ? 219 MET A N   1 
ATOM 1380 C CA  . MET A 1 173 ? 14.232  25.529  146.068 1.00 37.84  ? 219 MET A CA  1 
ATOM 1381 C C   . MET A 1 173 ? 12.779  25.966  146.185 1.00 40.62  ? 219 MET A C   1 
ATOM 1382 O O   . MET A 1 173 ? 12.476  27.159  146.117 1.00 42.90  ? 219 MET A O   1 
ATOM 1383 C CB  . MET A 1 173 ? 15.023  25.931  147.312 1.00 34.54  ? 219 MET A CB  1 
ATOM 1384 C CG  . MET A 1 173 ? 14.201  26.028  148.579 1.00 38.50  ? 219 MET A CG  1 
ATOM 1385 S SD  . MET A 1 173 ? 15.228  26.034  150.057 1.00 60.63  ? 219 MET A SD  1 
ATOM 1386 C CE  . MET A 1 173 ? 16.716  26.802  149.428 1.00 36.45  ? 219 MET A CE  1 
ATOM 1387 N N   . THR A 1 174 ? 11.882  24.997  146.358 1.00 34.23  ? 220 THR A N   1 
ATOM 1388 C CA  . THR A 1 174 ? 10.446  25.243  146.338 1.00 31.12  ? 220 THR A CA  1 
ATOM 1389 C C   . THR A 1 174 ? 9.879   25.571  147.711 1.00 32.67  ? 220 THR A C   1 
ATOM 1390 O O   . THR A 1 174 ? 8.667   25.772  147.834 1.00 40.24  ? 220 THR A O   1 
ATOM 1391 C CB  . THR A 1 174 ? 9.710   24.035  145.753 1.00 31.66  ? 220 THR A CB  1 
ATOM 1392 O OG1 . THR A 1 174 ? 9.419   23.101  146.798 1.00 35.33  ? 220 THR A OG1 1 
ATOM 1393 C CG2 . THR A 1 174 ? 10.565  23.354  144.699 1.00 29.65  ? 220 THR A CG2 1 
ATOM 1394 N N   . TYR A 1 175 ? 10.725  25.622  148.740 1.00 25.70  ? 221 TYR A N   1 
ATOM 1395 C CA  . TYR A 1 175 ? 10.273  25.995  150.076 1.00 23.80  ? 221 TYR A CA  1 
ATOM 1396 C C   . TYR A 1 175 ? 9.580   27.352  150.058 1.00 38.86  ? 221 TYR A C   1 
ATOM 1397 O O   . TYR A 1 175 ? 8.439   27.495  150.522 1.00 47.91  ? 221 TYR A O   1 
ATOM 1398 C CB  . TYR A 1 175 ? 11.478  26.009  151.017 1.00 23.24  ? 221 TYR A CB  1 
ATOM 1399 C CG  . TYR A 1 175 ? 11.175  25.864  152.486 1.00 27.32  ? 221 TYR A CG  1 
ATOM 1400 C CD1 . TYR A 1 175 ? 10.001  25.275  152.924 1.00 35.94  ? 221 TYR A CD1 1 
ATOM 1401 C CD2 . TYR A 1 175 ? 12.085  26.295  153.439 1.00 30.31  ? 221 TYR A CD2 1 
ATOM 1402 C CE1 . TYR A 1 175 ? 9.737   25.137  154.271 1.00 41.43  ? 221 TYR A CE1 1 
ATOM 1403 C CE2 . TYR A 1 175 ? 11.830  26.160  154.785 1.00 32.06  ? 221 TYR A CE2 1 
ATOM 1404 C CZ  . TYR A 1 175 ? 10.655  25.584  155.197 1.00 36.71  ? 221 TYR A CZ  1 
ATOM 1405 O OH  . TYR A 1 175 ? 10.399  25.449  156.541 1.00 36.62  ? 221 TYR A OH  1 
ATOM 1406 N N   . TYR A 1 176 ? 10.254  28.359  149.497 1.00 31.08  ? 222 TYR A N   1 
ATOM 1407 C CA  . TYR A 1 176 ? 9.710   29.711  149.481 1.00 22.55  ? 222 TYR A CA  1 
ATOM 1408 C C   . TYR A 1 176 ? 8.438   29.790  148.648 1.00 31.42  ? 222 TYR A C   1 
ATOM 1409 O O   . TYR A 1 176 ? 7.466   30.435  149.054 1.00 41.93  ? 222 TYR A O   1 
ATOM 1410 C CB  . TYR A 1 176 ? 10.756  30.684  148.944 1.00 29.08  ? 222 TYR A CB  1 
ATOM 1411 C CG  . TYR A 1 176 ? 12.135  30.485  149.523 1.00 28.55  ? 222 TYR A CG  1 
ATOM 1412 C CD1 . TYR A 1 176 ? 12.346  30.527  150.891 1.00 28.87  ? 222 TYR A CD1 1 
ATOM 1413 C CD2 . TYR A 1 176 ? 13.230  30.274  148.699 1.00 27.12  ? 222 TYR A CD2 1 
ATOM 1414 C CE1 . TYR A 1 176 ? 13.603  30.353  151.424 1.00 24.98  ? 222 TYR A CE1 1 
ATOM 1415 C CE2 . TYR A 1 176 ? 14.491  30.103  149.225 1.00 29.15  ? 222 TYR A CE2 1 
ATOM 1416 C CZ  . TYR A 1 176 ? 14.671  30.140  150.588 1.00 25.49  ? 222 TYR A CZ  1 
ATOM 1417 O OH  . TYR A 1 176 ? 15.923  29.969  151.122 1.00 31.92  ? 222 TYR A OH  1 
ATOM 1418 N N   . GLU A 1 177 ? 8.433   29.152  147.476 1.00 34.87  ? 223 GLU A N   1 
ATOM 1419 C CA  . GLU A 1 177 ? 7.262   29.204  146.608 1.00 32.15  ? 223 GLU A CA  1 
ATOM 1420 C C   . GLU A 1 177 ? 6.059   28.551  147.268 1.00 34.43  ? 223 GLU A C   1 
ATOM 1421 O O   . GLU A 1 177 ? 4.955   29.107  147.243 1.00 45.93  ? 223 GLU A O   1 
ATOM 1422 C CB  . GLU A 1 177 ? 7.556   28.538  145.260 1.00 28.46  ? 223 GLU A CB  1 
ATOM 1423 C CG  . GLU A 1 177 ? 8.669   29.163  144.400 1.00 42.42  ? 223 GLU A CG  1 
ATOM 1424 C CD  . GLU A 1 177 ? 10.016  29.281  145.093 1.00 47.05  ? 223 GLU A CD  1 
ATOM 1425 O OE1 . GLU A 1 177 ? 10.242  28.568  146.091 1.00 45.60  ? 223 GLU A OE1 1 
ATOM 1426 O OE2 . GLU A 1 177 ? 10.849  30.093  144.638 1.00 45.97  ? 223 GLU A OE2 1 
ATOM 1427 N N   . ARG A 1 178 ? 6.254   27.378  147.873 1.00 28.44  ? 224 ARG A N   1 
ATOM 1428 C CA  . ARG A 1 178 ? 5.150   26.706  148.545 1.00 33.54  ? 224 ARG A CA  1 
ATOM 1429 C C   . ARG A 1 178 ? 4.617   27.545  149.695 1.00 37.53  ? 224 ARG A C   1 
ATOM 1430 O O   . ARG A 1 178 ? 3.400   27.696  149.847 1.00 45.97  ? 224 ARG A O   1 
ATOM 1431 C CB  . ARG A 1 178 ? 5.593   25.337  149.055 1.00 33.55  ? 224 ARG A CB  1 
ATOM 1432 C CG  . ARG A 1 178 ? 4.668   24.774  150.112 1.00 32.13  ? 224 ARG A CG  1 
ATOM 1433 C CD  . ARG A 1 178 ? 3.594   23.898  149.493 1.00 42.69  ? 224 ARG A CD  1 
ATOM 1434 N NE  . ARG A 1 178 ? 2.489   23.662  150.413 1.00 46.13  ? 224 ARG A NE  1 
ATOM 1435 C CZ  . ARG A 1 178 ? 2.543   22.846  151.457 1.00 41.75  ? 224 ARG A CZ  1 
ATOM 1436 N NH1 . ARG A 1 178 ? 3.644   22.176  151.755 1.00 35.01  ? 224 ARG A NH1 1 
ATOM 1437 N NH2 . ARG A 1 178 ? 1.468   22.705  152.225 1.00 34.25  ? 224 ARG A NH2 1 
ATOM 1438 N N   . HIS A 1 179 ? 5.511   28.106  150.513 1.00 33.04  ? 225 HIS A N   1 
ATOM 1439 C CA  . HIS A 1 179 ? 5.046   28.893  151.651 1.00 28.30  ? 225 HIS A CA  1 
ATOM 1440 C C   . HIS A 1 179 ? 4.304   30.146  151.201 1.00 31.51  ? 225 HIS A C   1 
ATOM 1441 O O   . HIS A 1 179 ? 3.252   30.482  151.758 1.00 42.23  ? 225 HIS A O   1 
ATOM 1442 C CB  . HIS A 1 179 ? 6.221   29.253  152.552 1.00 23.19  ? 225 HIS A CB  1 
ATOM 1443 C CG  . HIS A 1 179 ? 6.458   28.259  153.641 1.00 36.58  ? 225 HIS A CG  1 
ATOM 1444 N ND1 . HIS A 1 179 ? 5.436   27.730  154.397 1.00 45.31  ? 225 HIS A ND1 1 
ATOM 1445 C CD2 . HIS A 1 179 ? 7.598   27.691  154.098 1.00 34.54  ? 225 HIS A CD2 1 
ATOM 1446 C CE1 . HIS A 1 179 ? 5.936   26.880  155.276 1.00 36.98  ? 225 HIS A CE1 1 
ATOM 1447 N NE2 . HIS A 1 179 ? 7.246   26.839  155.115 1.00 29.31  ? 225 HIS A NE2 1 
ATOM 1448 N N   . ALA A 1 180 ? 4.831   30.848  150.194 1.00 30.42  ? 226 ALA A N   1 
ATOM 1449 C CA  . ALA A 1 180 ? 4.166   32.052  149.708 1.00 29.34  ? 226 ALA A CA  1 
ATOM 1450 C C   . ALA A 1 180 ? 2.807   31.728  149.102 1.00 32.59  ? 226 ALA A C   1 
ATOM 1451 O O   . ALA A 1 180 ? 1.824   32.434  149.359 1.00 38.07  ? 226 ALA A O   1 
ATOM 1452 C CB  . ALA A 1 180 ? 5.053   32.766  148.691 1.00 27.87  ? 226 ALA A CB  1 
ATOM 1453 N N   . TRP A 1 181 ? 2.727   30.663  148.300 1.00 28.25  ? 227 TRP A N   1 
ATOM 1454 C CA  . TRP A 1 181 ? 1.447   30.274  147.722 1.00 36.34  ? 227 TRP A CA  1 
ATOM 1455 C C   . TRP A 1 181 ? 0.446   29.874  148.796 1.00 36.32  ? 227 TRP A C   1 
ATOM 1456 O O   . TRP A 1 181 ? -0.739  30.206  148.690 1.00 39.46  ? 227 TRP A O   1 
ATOM 1457 C CB  . TRP A 1 181 ? 1.650   29.132  146.728 1.00 31.89  ? 227 TRP A CB  1 
ATOM 1458 C CG  . TRP A 1 181 ? 0.411   28.348  146.442 1.00 36.57  ? 227 TRP A CG  1 
ATOM 1459 C CD1 . TRP A 1 181 ? -0.626  28.715  145.636 1.00 37.37  ? 227 TRP A CD1 1 
ATOM 1460 C CD2 . TRP A 1 181 ? 0.082   27.053  146.954 1.00 40.59  ? 227 TRP A CD2 1 
ATOM 1461 N NE1 . TRP A 1 181 ? -1.583  27.730  145.618 1.00 38.00  ? 227 TRP A NE1 1 
ATOM 1462 C CE2 . TRP A 1 181 ? -1.172  26.699  146.420 1.00 40.11  ? 227 TRP A CE2 1 
ATOM 1463 C CE3 . TRP A 1 181 ? 0.725   26.160  147.814 1.00 41.44  ? 227 TRP A CE3 1 
ATOM 1464 C CZ2 . TRP A 1 181 ? -1.793  25.490  146.718 1.00 40.91  ? 227 TRP A CZ2 1 
ATOM 1465 C CZ3 . TRP A 1 181 ? 0.108   24.962  148.108 1.00 39.01  ? 227 TRP A CZ3 1 
ATOM 1466 C CH2 . TRP A 1 181 ? -1.139  24.637  147.562 1.00 39.44  ? 227 TRP A CH2 1 
ATOM 1467 N N   . MET A 1 182 ? 0.899   29.167  149.831 1.00 32.18  ? 228 MET A N   1 
ATOM 1468 C CA  . MET A 1 182 ? -0.004  28.762  150.899 1.00 26.99  ? 228 MET A CA  1 
ATOM 1469 C C   . MET A 1 182 ? -0.510  29.962  151.687 1.00 36.29  ? 228 MET A C   1 
ATOM 1470 O O   . MET A 1 182 ? -1.698  30.035  152.022 1.00 43.39  ? 228 MET A O   1 
ATOM 1471 C CB  . MET A 1 182 ? 0.701   27.773  151.824 1.00 32.82  ? 228 MET A CB  1 
ATOM 1472 C CG  . MET A 1 182 ? -0.120  26.552  152.173 1.00 40.91  ? 228 MET A CG  1 
ATOM 1473 S SD  . MET A 1 182 ? 0.815   25.410  153.200 1.00 54.49  ? 228 MET A SD  1 
ATOM 1474 C CE  . MET A 1 182 ? 1.314   26.513  154.515 1.00 37.45  ? 228 MET A CE  1 
ATOM 1475 N N   . SER A 1 183 ? 0.369   30.912  151.993 1.00 33.81  ? 229 SER A N   1 
ATOM 1476 C CA  . SER A 1 183 ? 0.023   32.021  152.870 1.00 31.90  ? 229 SER A CA  1 
ATOM 1477 C C   . SER A 1 183 ? -0.543  33.225  152.131 1.00 33.21  ? 229 SER A C   1 
ATOM 1478 O O   . SER A 1 183 ? -0.931  34.201  152.782 1.00 32.65  ? 229 SER A O   1 
ATOM 1479 C CB  . SER A 1 183 ? 1.253   32.451  153.676 1.00 31.29  ? 229 SER A CB  1 
ATOM 1480 O OG  . SER A 1 183 ? 0.911   33.414  154.656 1.00 38.17  ? 229 SER A OG  1 
ATOM 1481 N N   . ASN A 1 184 ? -0.603  33.190  150.804 1.00 37.08  ? 230 ASN A N   1 
ATOM 1482 C CA  . ASN A 1 184 ? -1.002  34.345  150.008 1.00 35.84  ? 230 ASN A CA  1 
ATOM 1483 C C   . ASN A 1 184 ? -2.130  33.932  149.062 1.00 33.70  ? 230 ASN A C   1 
ATOM 1484 O O   . ASN A 1 184 ? -2.055  34.082  147.841 1.00 37.49  ? 230 ASN A O   1 
ATOM 1485 C CB  . ASN A 1 184 ? 0.235   34.906  149.291 1.00 40.10  ? 230 ASN A CB  1 
ATOM 1486 C CG  . ASN A 1 184 ? -0.069  36.058  148.322 1.00 44.23  ? 230 ASN A CG  1 
ATOM 1487 O OD1 . ASN A 1 184 ? -1.216  36.449  148.107 1.00 40.40  ? 230 ASN A OD1 1 
ATOM 1488 N ND2 . ASN A 1 184 ? 0.987   36.597  147.725 1.00 41.65  ? 230 ASN A ND2 1 
ATOM 1489 N N   . GLY A 1 185 ? -3.166  33.308  149.614 1.00 34.39  ? 231 GLY A N   1 
ATOM 1490 C CA  . GLY A 1 185 ? -4.291  32.906  148.793 1.00 37.55  ? 231 GLY A CA  1 
ATOM 1491 C C   . GLY A 1 185 ? -5.546  32.698  149.605 1.00 37.45  ? 231 GLY A C   1 
ATOM 1492 O O   . GLY A 1 185 ? -5.499  32.425  150.808 1.00 43.02  ? 231 GLY A O   1 
ATOM 1493 N N   . LEU A 1 186 ? -6.680  32.833  148.923 1.00 27.83  ? 232 LEU A N   1 
ATOM 1494 C CA  . LEU A 1 186 ? -7.995  32.564  149.489 1.00 24.62  ? 232 LEU A CA  1 
ATOM 1495 C C   . LEU A 1 186 ? -8.593  31.365  148.769 1.00 30.79  ? 232 LEU A C   1 
ATOM 1496 O O   . LEU A 1 186 ? -8.589  31.316  147.535 1.00 38.86  ? 232 LEU A O   1 
ATOM 1497 C CB  . LEU A 1 186 ? -8.917  33.776  149.349 1.00 26.80  ? 232 LEU A CB  1 
ATOM 1498 C CG  . LEU A 1 186 ? -8.470  35.079  150.006 1.00 31.16  ? 232 LEU A CG  1 
ATOM 1499 C CD1 . LEU A 1 186 ? -9.556  36.126  149.870 1.00 29.82  ? 232 LEU A CD1 1 
ATOM 1500 C CD2 . LEU A 1 186 ? -8.127  34.850  151.461 1.00 30.25  ? 232 LEU A CD2 1 
ATOM 1501 N N   . TYR A 1 187 ? -9.102  30.403  149.535 1.00 28.19  ? 233 TYR A N   1 
ATOM 1502 C CA  . TYR A 1 187 ? -9.549  29.132  148.981 1.00 24.27  ? 233 TYR A CA  1 
ATOM 1503 C C   . TYR A 1 187 ? -10.977 28.842  149.412 1.00 25.62  ? 233 TYR A C   1 
ATOM 1504 O O   . TYR A 1 187 ? -11.287 28.867  150.607 1.00 27.36  ? 233 TYR A O   1 
ATOM 1505 C CB  . TYR A 1 187 ? -8.616  28.000  149.414 1.00 23.70  ? 233 TYR A CB  1 
ATOM 1506 C CG  . TYR A 1 187 ? -7.181  28.247  149.021 1.00 25.15  ? 233 TYR A CG  1 
ATOM 1507 C CD1 . TYR A 1 187 ? -6.798  28.231  147.689 1.00 28.18  ? 233 TYR A CD1 1 
ATOM 1508 C CD2 . TYR A 1 187 ? -6.214  28.521  149.977 1.00 26.70  ? 233 TYR A CD2 1 
ATOM 1509 C CE1 . TYR A 1 187 ? -5.492  28.465  147.321 1.00 29.34  ? 233 TYR A CE1 1 
ATOM 1510 C CE2 . TYR A 1 187 ? -4.904  28.757  149.618 1.00 29.50  ? 233 TYR A CE2 1 
ATOM 1511 C CZ  . TYR A 1 187 ? -4.551  28.728  148.288 1.00 29.61  ? 233 TYR A CZ  1 
ATOM 1512 O OH  . TYR A 1 187 ? -3.247  28.960  147.921 1.00 38.03  ? 233 TYR A OH  1 
ATOM 1513 N N   . VAL A 1 188 ? -11.836 28.558  148.438 1.00 30.49  ? 234 VAL A N   1 
ATOM 1514 C CA  . VAL A 1 188 ? -13.237 28.239  148.679 1.00 27.86  ? 234 VAL A CA  1 
ATOM 1515 C C   . VAL A 1 188 ? -13.390 26.730  148.778 1.00 29.90  ? 234 VAL A C   1 
ATOM 1516 O O   . VAL A 1 188 ? -12.731 25.967  148.063 1.00 37.54  ? 234 VAL A O   1 
ATOM 1517 C CB  . VAL A 1 188 ? -14.143 28.814  147.571 1.00 24.59  ? 234 VAL A CB  1 
ATOM 1518 C CG1 . VAL A 1 188 ? -14.308 30.308  147.744 1.00 28.87  ? 234 VAL A CG1 1 
ATOM 1519 C CG2 . VAL A 1 188 ? -13.568 28.504  146.204 1.00 28.80  ? 234 VAL A CG2 1 
ATOM 1520 N N   . ASP A 1 189 ? -14.271 26.291  149.679 1.00 27.38  ? 235 ASP A N   1 
ATOM 1521 C CA  . ASP A 1 189 ? -14.520 24.862  149.832 1.00 35.40  ? 235 ASP A CA  1 
ATOM 1522 C C   . ASP A 1 189 ? -15.332 24.294  148.676 1.00 35.67  ? 235 ASP A C   1 
ATOM 1523 O O   . ASP A 1 189 ? -15.254 23.092  148.401 1.00 38.61  ? 235 ASP A O   1 
ATOM 1524 C CB  . ASP A 1 189 ? -15.228 24.591  151.159 1.00 35.74  ? 235 ASP A CB  1 
ATOM 1525 C CG  . ASP A 1 189 ? -16.493 25.397  151.316 1.00 40.17  ? 235 ASP A CG  1 
ATOM 1526 O OD1 . ASP A 1 189 ? -16.506 26.566  150.882 1.00 40.44  ? 235 ASP A OD1 1 
ATOM 1527 O OD2 . ASP A 1 189 ? -17.475 24.866  151.874 1.00 44.95  ? 235 ASP A OD2 1 
ATOM 1528 N N   . GLN A 1 190 ? -16.115 25.129  147.998 1.00 35.35  ? 236 GLN A N   1 
ATOM 1529 C CA  . GLN A 1 190 ? -16.862 24.728  146.816 1.00 34.68  ? 236 GLN A CA  1 
ATOM 1530 C C   . GLN A 1 190 ? -16.764 25.823  145.766 1.00 43.13  ? 236 GLN A C   1 
ATOM 1531 O O   . GLN A 1 190 ? -16.446 26.973  146.076 1.00 48.46  ? 236 GLN A O   1 
ATOM 1532 C CB  . GLN A 1 190 ? -18.336 24.456  147.134 1.00 41.95  ? 236 GLN A CB  1 
ATOM 1533 C CG  . GLN A 1 190 ? -18.575 23.281  148.057 1.00 43.29  ? 236 GLN A CG  1 
ATOM 1534 C CD  . GLN A 1 190 ? -20.010 23.203  148.535 1.00 46.65  ? 236 GLN A CD  1 
ATOM 1535 O OE1 . GLN A 1 190 ? -20.910 22.855  147.774 1.00 42.96  ? 236 GLN A OE1 1 
ATOM 1536 N NE2 . GLN A 1 190 ? -20.230 23.530  149.803 1.00 47.46  ? 236 GLN A NE2 1 
ATOM 1537 N N   . ASP A 1 191 ? -17.039 25.455  144.518 1.00 47.85  ? 237 ASP A N   1 
ATOM 1538 C CA  . ASP A 1 191 ? -17.052 26.420  143.419 1.00 49.30  ? 237 ASP A CA  1 
ATOM 1539 C C   . ASP A 1 191 ? -18.442 27.043  143.273 1.00 46.01  ? 237 ASP A C   1 
ATOM 1540 O O   . ASP A 1 191 ? -19.113 26.922  142.250 1.00 47.19  ? 237 ASP A O   1 
ATOM 1541 C CB  . ASP A 1 191 ? -16.601 25.754  142.125 1.00 52.88  ? 237 ASP A CB  1 
ATOM 1542 C CG  . ASP A 1 191 ? -15.513 26.536  141.420 1.00 54.24  ? 237 ASP A CG  1 
ATOM 1543 O OD1 . ASP A 1 191 ? -15.111 27.596  141.942 1.00 54.34  ? 237 ASP A OD1 1 
ATOM 1544 O OD2 . ASP A 1 191 ? -15.061 26.092  140.343 1.00 55.31  ? 237 ASP A OD2 1 
ATOM 1545 N N   . VAL A 1 192 ? -18.867 27.722  144.338 1.00 44.39  ? 238 VAL A N   1 
ATOM 1546 C CA  . VAL A 1 192 ? -20.148 28.411  144.377 1.00 45.59  ? 238 VAL A CA  1 
ATOM 1547 C C   . VAL A 1 192 ? -19.914 29.842  144.845 1.00 45.04  ? 238 VAL A C   1 
ATOM 1548 O O   . VAL A 1 192 ? -18.897 30.161  145.460 1.00 46.95  ? 238 VAL A O   1 
ATOM 1549 C CB  . VAL A 1 192 ? -21.173 27.701  145.284 1.00 42.97  ? 238 VAL A CB  1 
ATOM 1550 C CG1 . VAL A 1 192 ? -21.545 26.351  144.702 1.00 42.94  ? 238 VAL A CG1 1 
ATOM 1551 C CG2 . VAL A 1 192 ? -20.618 27.542  146.685 1.00 42.30  ? 238 VAL A CG2 1 
ATOM 1552 N N   . THR A 1 193 ? -20.878 30.709  144.532 1.00 43.96  ? 239 THR A N   1 
ATOM 1553 C CA  . THR A 1 193 ? -20.730 32.129  144.838 1.00 46.38  ? 239 THR A CA  1 
ATOM 1554 C C   . THR A 1 193 ? -20.693 32.375  146.342 1.00 47.32  ? 239 THR A C   1 
ATOM 1555 O O   . THR A 1 193 ? -19.824 33.099  146.841 1.00 47.83  ? 239 THR A O   1 
ATOM 1556 C CB  . THR A 1 193 ? -21.866 32.923  144.196 1.00 48.06  ? 239 THR A CB  1 
ATOM 1557 O OG1 . THR A 1 193 ? -22.976 32.980  145.099 1.00 52.45  ? 239 THR A OG1 1 
ATOM 1558 C CG2 . THR A 1 193 ? -22.309 32.260  142.903 1.00 46.83  ? 239 THR A CG2 1 
ATOM 1559 N N   . ARG A 1 194 ? -21.630 31.790  147.079 1.00 40.60  ? 240 ARG A N   1 
ATOM 1560 C CA  . ARG A 1 194 ? -21.683 31.960  148.530 1.00 37.00  ? 240 ARG A CA  1 
ATOM 1561 C C   . ARG A 1 194 ? -20.930 30.847  149.253 1.00 42.58  ? 240 ARG A C   1 
ATOM 1562 O O   . ARG A 1 194 ? -21.464 30.172  150.131 1.00 45.83  ? 240 ARG A O   1 
ATOM 1563 C CB  . ARG A 1 194 ? -23.134 32.035  148.986 1.00 38.90  ? 240 ARG A CB  1 
ATOM 1564 C CG  . ARG A 1 194 ? -23.839 33.316  148.570 1.00 40.14  ? 240 ARG A CG  1 
ATOM 1565 C CD  . ARG A 1 194 ? -25.221 33.031  148.010 1.00 39.48  ? 240 ARG A CD  1 
ATOM 1566 N NE  . ARG A 1 194 ? -26.072 32.368  148.989 1.00 49.91  ? 240 ARG A NE  1 
ATOM 1567 C CZ  . ARG A 1 194 ? -26.506 31.120  148.879 1.00 53.34  ? 240 ARG A CZ  1 
ATOM 1568 N NH1 . ARG A 1 194 ? -26.191 30.368  147.838 1.00 50.27  ? 240 ARG A NH1 1 
ATOM 1569 N NH2 . ARG A 1 194 ? -27.274 30.613  149.840 1.00 47.96  ? 240 ARG A NH2 1 
ATOM 1570 N N   . ALA A 1 195 ? -19.668 30.658  148.885 1.00 40.11  ? 241 ALA A N   1 
ATOM 1571 C CA  . ALA A 1 195 ? -18.838 29.618  149.470 1.00 31.41  ? 241 ALA A CA  1 
ATOM 1572 C C   . ALA A 1 195 ? -18.120 30.135  150.712 1.00 34.51  ? 241 ALA A C   1 
ATOM 1573 O O   . ALA A 1 195 ? -18.166 31.320  151.046 1.00 42.41  ? 241 ALA A O   1 
ATOM 1574 C CB  . ALA A 1 195 ? -17.825 29.104  148.449 1.00 30.14  ? 241 ALA A CB  1 
ATOM 1575 N N   . GLN A 1 196 ? -17.449 29.220  151.401 1.00 29.89  ? 242 GLN A N   1 
ATOM 1576 C CA  . GLN A 1 196 ? -16.675 29.542  152.590 1.00 28.90  ? 242 GLN A CA  1 
ATOM 1577 C C   . GLN A 1 196 ? -15.195 29.617  152.244 1.00 33.36  ? 242 GLN A C   1 
ATOM 1578 O O   . GLN A 1 196 ? -14.690 28.818  151.451 1.00 40.76  ? 242 GLN A O   1 
ATOM 1579 C CB  . GLN A 1 196 ? -16.911 28.508  153.687 1.00 26.13  ? 242 GLN A CB  1 
ATOM 1580 C CG  . GLN A 1 196 ? -18.224 28.693  154.418 1.00 25.79  ? 242 GLN A CG  1 
ATOM 1581 C CD  . GLN A 1 196 ? -19.290 27.727  153.959 1.00 34.79  ? 242 GLN A CD  1 
ATOM 1582 O OE1 . GLN A 1 196 ? -19.152 27.077  152.924 1.00 40.20  ? 242 GLN A OE1 1 
ATOM 1583 N NE2 . GLN A 1 196 ? -20.367 27.630  154.726 1.00 32.78  ? 242 GLN A NE2 1 
ATOM 1584 N N   . ILE A 1 197 ? -14.502 30.575  152.851 1.00 24.64  ? 243 ILE A N   1 
ATOM 1585 C CA  . ILE A 1 197 ? -13.126 30.905  152.499 1.00 25.52  ? 243 ILE A CA  1 
ATOM 1586 C C   . ILE A 1 197 ? -12.180 30.197  153.459 1.00 27.94  ? 243 ILE A C   1 
ATOM 1587 O O   . ILE A 1 197 ? -12.392 30.210  154.677 1.00 25.96  ? 243 ILE A O   1 
ATOM 1588 C CB  . ILE A 1 197 ? -12.897 32.425  152.527 1.00 28.37  ? 243 ILE A CB  1 
ATOM 1589 C CG1 . ILE A 1 197 ? -13.901 33.130  151.619 1.00 30.71  ? 243 ILE A CG1 1 
ATOM 1590 C CG2 . ILE A 1 197 ? -11.485 32.759  152.090 1.00 33.28  ? 243 ILE A CG2 1 
ATOM 1591 C CD1 . ILE A 1 197 ? -13.679 32.871  150.158 1.00 26.64  ? 243 ILE A CD1 1 
ATOM 1592 N N   . TYR A 1 198 ? -11.143 29.573  152.909 1.00 28.37  ? 244 TYR A N   1 
ATOM 1593 C CA  . TYR A 1 198 ? -10.077 28.960  153.689 1.00 26.68  ? 244 TYR A CA  1 
ATOM 1594 C C   . TYR A 1 198 ? -8.841  29.847  153.628 1.00 30.08  ? 244 TYR A C   1 
ATOM 1595 O O   . TYR A 1 198 ? -8.451  30.299  152.547 1.00 37.43  ? 244 TYR A O   1 
ATOM 1596 C CB  . TYR A 1 198 ? -9.747  27.565  153.160 1.00 29.21  ? 244 TYR A CB  1 
ATOM 1597 C CG  . TYR A 1 198 ? -10.594 26.461  153.743 1.00 31.17  ? 244 TYR A CG  1 
ATOM 1598 C CD1 . TYR A 1 198 ? -10.542 26.161  155.095 1.00 30.26  ? 244 TYR A CD1 1 
ATOM 1599 C CD2 . TYR A 1 198 ? -11.436 25.709  152.938 1.00 29.58  ? 244 TYR A CD2 1 
ATOM 1600 C CE1 . TYR A 1 198 ? -11.309 25.148  155.628 1.00 30.09  ? 244 TYR A CE1 1 
ATOM 1601 C CE2 . TYR A 1 198 ? -12.208 24.695  153.464 1.00 28.56  ? 244 TYR A CE2 1 
ATOM 1602 C CZ  . TYR A 1 198 ? -12.140 24.421  154.810 1.00 28.73  ? 244 TYR A CZ  1 
ATOM 1603 O OH  . TYR A 1 198 ? -12.901 23.411  155.340 1.00 32.65  ? 244 TYR A OH  1 
ATOM 1604 N N   . MET A 1 199 ? -8.226  30.089  154.782 1.00 23.73  ? 245 MET A N   1 
ATOM 1605 C CA  . MET A 1 199 ? -7.071  30.968  154.873 1.00 28.78  ? 245 MET A CA  1 
ATOM 1606 C C   . MET A 1 199 ? -5.965  30.306  155.679 1.00 33.44  ? 245 MET A C   1 
ATOM 1607 O O   . MET A 1 199 ? -6.219  29.462  156.541 1.00 36.22  ? 245 MET A O   1 
ATOM 1608 C CB  . MET A 1 199 ? -7.432  32.309  155.517 1.00 27.91  ? 245 MET A CB  1 
ATOM 1609 C CG  . MET A 1 199 ? -8.224  33.232  154.619 1.00 31.63  ? 245 MET A CG  1 
ATOM 1610 S SD  . MET A 1 199 ? -8.223  34.932  155.208 1.00 48.38  ? 245 MET A SD  1 
ATOM 1611 C CE  . MET A 1 199 ? -8.217  34.672  156.977 1.00 33.94  ? 245 MET A CE  1 
ATOM 1612 N N   . PHE A 1 200 ? -4.730  30.706  155.385 1.00 25.79  ? 246 PHE A N   1 
ATOM 1613 C CA  . PHE A 1 200 ? -3.553  30.255  156.110 1.00 19.01  ? 246 PHE A CA  1 
ATOM 1614 C C   . PHE A 1 200 ? -2.878  31.465  156.734 1.00 24.24  ? 246 PHE A C   1 
ATOM 1615 O O   . PHE A 1 200 ? -2.549  32.424  156.031 1.00 35.13  ? 246 PHE A O   1 
ATOM 1616 C CB  . PHE A 1 200 ? -2.579  29.526  155.182 1.00 28.24  ? 246 PHE A CB  1 
ATOM 1617 C CG  . PHE A 1 200 ? -3.028  28.150  154.797 1.00 28.24  ? 246 PHE A CG  1 
ATOM 1618 C CD1 . PHE A 1 200 ? -2.681  27.054  155.563 1.00 27.66  ? 246 PHE A CD1 1 
ATOM 1619 C CD2 . PHE A 1 200 ? -3.801  27.953  153.667 1.00 27.75  ? 246 PHE A CD2 1 
ATOM 1620 C CE1 . PHE A 1 200 ? -3.093  25.788  155.209 1.00 26.90  ? 246 PHE A CE1 1 
ATOM 1621 C CE2 . PHE A 1 200 ? -4.216  26.689  153.310 1.00 24.63  ? 246 PHE A CE2 1 
ATOM 1622 C CZ  . PHE A 1 200 ? -3.863  25.606  154.080 1.00 23.47  ? 246 PHE A CZ  1 
ATOM 1623 N N   . LYS A 1 201 ? -2.675  31.421  158.048 1.00 21.75  ? 247 LYS A N   1 
ATOM 1624 C CA  . LYS A 1 201 ? -2.061  32.522  158.769 1.00 25.32  ? 247 LYS A CA  1 
ATOM 1625 C C   . LYS A 1 201 ? -0.845  32.000  159.521 1.00 32.69  ? 247 LYS A C   1 
ATOM 1626 O O   . LYS A 1 201 ? -0.969  31.052  160.315 1.00 38.43  ? 247 LYS A O   1 
ATOM 1627 C CB  . LYS A 1 201 ? -3.054  33.166  159.741 1.00 19.97  ? 247 LYS A CB  1 
ATOM 1628 C CG  . LYS A 1 201 ? -2.734  34.603  160.098 1.00 14.87  ? 247 LYS A CG  1 
ATOM 1629 C CD  . LYS A 1 201 ? -2.149  34.707  161.492 1.00 18.36  ? 247 LYS A CD  1 
ATOM 1630 C CE  . LYS A 1 201 ? -3.169  34.327  162.542 1.00 24.14  ? 247 LYS A CE  1 
ATOM 1631 N NZ  . LYS A 1 201 ? -2.597  34.411  163.910 1.00 35.08  ? 247 LYS A NZ  1 
ATOM 1632 N N   . PRO A 1 202 ? 0.339   32.573  159.304 1.00 22.97  ? 248 PRO A N   1 
ATOM 1633 C CA  . PRO A 1 202 ? 1.527   32.119  160.041 1.00 18.90  ? 248 PRO A CA  1 
ATOM 1634 C C   . PRO A 1 202 ? 1.403   32.464  161.517 1.00 24.09  ? 248 PRO A C   1 
ATOM 1635 O O   . PRO A 1 202 ? 1.349   33.636  161.892 1.00 31.97  ? 248 PRO A O   1 
ATOM 1636 C CB  . PRO A 1 202 ? 2.675   32.884  159.372 1.00 21.70  ? 248 PRO A CB  1 
ATOM 1637 C CG  . PRO A 1 202 ? 2.030   34.062  158.736 1.00 17.48  ? 248 PRO A CG  1 
ATOM 1638 C CD  . PRO A 1 202 ? 0.660   33.623  158.325 1.00 18.81  ? 248 PRO A CD  1 
ATOM 1639 N N   . THR A 1 203 ? 1.350   31.429  162.356 1.00 27.57  ? 249 THR A N   1 
ATOM 1640 C CA  . THR A 1 203 ? 1.265   31.635  163.796 1.00 28.95  ? 249 THR A CA  1 
ATOM 1641 C C   . THR A 1 203 ? 2.548   32.228  164.358 1.00 32.52  ? 249 THR A C   1 
ATOM 1642 O O   . THR A 1 203 ? 2.521   32.883  165.405 1.00 36.56  ? 249 THR A O   1 
ATOM 1643 C CB  . THR A 1 203 ? 0.962   30.309  164.496 1.00 27.38  ? 249 THR A CB  1 
ATOM 1644 O OG1 . THR A 1 203 ? -0.116  29.652  163.825 1.00 28.62  ? 249 THR A OG1 1 
ATOM 1645 C CG2 . THR A 1 203 ? 0.565   30.541  165.945 1.00 25.22  ? 249 THR A CG2 1 
ATOM 1646 N N   . MET A 1 204 ? 3.668   32.033  163.668 1.00 30.95  ? 250 MET A N   1 
ATOM 1647 C CA  . MET A 1 204 ? 4.974   32.321  164.232 1.00 26.91  ? 250 MET A CA  1 
ATOM 1648 C C   . MET A 1 204 ? 5.962   32.586  163.108 1.00 32.88  ? 250 MET A C   1 
ATOM 1649 O O   . MET A 1 204 ? 5.725   32.233  161.950 1.00 32.76  ? 250 MET A O   1 
ATOM 1650 C CB  . MET A 1 204 ? 5.446   31.155  165.104 1.00 25.15  ? 250 MET A CB  1 
ATOM 1651 C CG  . MET A 1 204 ? 6.260   30.126  164.343 1.00 32.68  ? 250 MET A CG  1 
ATOM 1652 S SD  . MET A 1 204 ? 6.909   28.840  165.411 1.00 62.93  ? 250 MET A SD  1 
ATOM 1653 C CE  . MET A 1 204 ? 7.698   29.844  166.643 1.00 39.22  ? 250 MET A CE  1 
ATOM 1654 N N   . LEU A 1 205 ? 7.078   33.215  163.466 1.00 39.83  ? 251 LEU A N   1 
ATOM 1655 C CA  . LEU A 1 205 ? 8.181   33.451  162.547 1.00 30.75  ? 251 LEU A CA  1 
ATOM 1656 C C   . LEU A 1 205 ? 9.486   33.057  163.231 1.00 31.95  ? 251 LEU A C   1 
ATOM 1657 O O   . LEU A 1 205 ? 9.492   32.512  164.338 1.00 41.87  ? 251 LEU A O   1 
ATOM 1658 C CB  . LEU A 1 205 ? 8.208   34.907  162.071 1.00 36.11  ? 251 LEU A CB  1 
ATOM 1659 C CG  . LEU A 1 205 ? 7.080   35.289  161.108 1.00 36.45  ? 251 LEU A CG  1 
ATOM 1660 C CD1 . LEU A 1 205 ? 7.231   36.728  160.648 1.00 34.27  ? 251 LEU A CD1 1 
ATOM 1661 C CD2 . LEU A 1 205 ? 7.031   34.344  159.919 1.00 32.77  ? 251 LEU A CD2 1 
ATOM 1662 N N   . TRP A 1 206 ? 10.604  33.349  162.568 1.00 32.28  ? 252 TRP A N   1 
ATOM 1663 C CA  . TRP A 1 206 ? 11.900  32.768  162.912 1.00 31.92  ? 252 TRP A CA  1 
ATOM 1664 C C   . TRP A 1 206 ? 12.963  33.859  163.063 1.00 35.63  ? 252 TRP A C   1 
ATOM 1665 O O   . TRP A 1 206 ? 13.992  33.840  162.388 1.00 47.08  ? 252 TRP A O   1 
ATOM 1666 C CB  . TRP A 1 206 ? 12.324  31.723  161.883 1.00 27.47  ? 252 TRP A CB  1 
ATOM 1667 C CG  . TRP A 1 206 ? 11.583  30.422  162.012 1.00 31.32  ? 252 TRP A CG  1 
ATOM 1668 C CD1 . TRP A 1 206 ? 10.871  29.787  161.041 1.00 34.48  ? 252 TRP A CD1 1 
ATOM 1669 C CD2 . TRP A 1 206 ? 11.480  29.601  163.185 1.00 33.68  ? 252 TRP A CD2 1 
ATOM 1670 N NE1 . TRP A 1 206 ? 10.334  28.622  161.531 1.00 32.79  ? 252 TRP A NE1 1 
ATOM 1671 C CE2 . TRP A 1 206 ? 10.694  28.485  162.845 1.00 29.80  ? 252 TRP A CE2 1 
ATOM 1672 C CE3 . TRP A 1 206 ? 11.980  29.700  164.487 1.00 33.04  ? 252 TRP A CE3 1 
ATOM 1673 C CZ2 . TRP A 1 206 ? 10.393  27.479  163.757 1.00 22.19  ? 252 TRP A CZ2 1 
ATOM 1674 C CZ3 . TRP A 1 206 ? 11.678  28.701  165.390 1.00 29.63  ? 252 TRP A CZ3 1 
ATOM 1675 C CH2 . TRP A 1 206 ? 10.894  27.605  165.022 1.00 22.99  ? 252 TRP A CH2 1 
ATOM 1676 N N   . LYS A 1 207 ? 12.674  34.852  163.906 1.00 31.97  ? 253 LYS A N   1 
ATOM 1677 C CA  . LYS A 1 207 ? 13.675  35.837  164.312 1.00 31.34  ? 253 LYS A CA  1 
ATOM 1678 C C   . LYS A 1 207 ? 15.033  35.178  164.523 1.00 36.64  ? 253 LYS A C   1 
ATOM 1679 O O   . LYS A 1 207 ? 15.170  34.249  165.322 1.00 39.59  ? 253 LYS A O   1 
ATOM 1680 C CB  . LYS A 1 207 ? 13.218  36.532  165.596 1.00 30.98  ? 253 LYS A CB  1 
ATOM 1681 C CG  . LYS A 1 207 ? 13.835  37.895  165.842 1.00 32.40  ? 253 LYS A CG  1 
ATOM 1682 C CD  . LYS A 1 207 ? 13.660  38.299  167.296 1.00 32.53  ? 253 LYS A CD  1 
ATOM 1683 C CE  . LYS A 1 207 ? 14.611  39.413  167.690 1.00 43.56  ? 253 LYS A CE  1 
ATOM 1684 N NZ  . LYS A 1 207 ? 15.845  39.406  166.864 1.00 42.94  ? 253 LYS A NZ  1 
ATOM 1685 N N   . TYR A 1 208 ? 16.038  35.667  163.793 1.00 42.93  ? 254 TYR A N   1 
ATOM 1686 C CA  . TYR A 1 208 ? 17.287  34.937  163.599 1.00 46.45  ? 254 TYR A CA  1 
ATOM 1687 C C   . TYR A 1 208 ? 18.189  34.948  164.833 1.00 51.13  ? 254 TYR A C   1 
ATOM 1688 O O   . TYR A 1 208 ? 18.774  33.917  165.174 1.00 54.14  ? 254 TYR A O   1 
ATOM 1689 C CB  . TYR A 1 208 ? 18.011  35.491  162.369 1.00 47.06  ? 254 TYR A CB  1 
ATOM 1690 C CG  . TYR A 1 208 ? 19.506  35.318  162.378 1.00 47.31  ? 254 TYR A CG  1 
ATOM 1691 C CD1 . TYR A 1 208 ? 20.080  34.079  162.126 1.00 46.01  ? 254 TYR A CD1 1 
ATOM 1692 C CD2 . TYR A 1 208 ? 20.344  36.387  162.639 1.00 48.11  ? 254 TYR A CD2 1 
ATOM 1693 C CE1 . TYR A 1 208 ? 21.447  33.914  162.133 1.00 50.27  ? 254 TYR A CE1 1 
ATOM 1694 C CE2 . TYR A 1 208 ? 21.708  36.235  162.637 1.00 49.44  ? 254 TYR A CE2 1 
ATOM 1695 C CZ  . TYR A 1 208 ? 22.257  34.995  162.394 1.00 52.01  ? 254 TYR A CZ  1 
ATOM 1696 O OH  . TYR A 1 208 ? 23.624  34.840  162.398 1.00 53.73  ? 254 TYR A OH  1 
ATOM 1697 N N   . GLU A 1 209 ? 18.334  36.098  165.496 1.00 52.75  ? 255 GLU A N   1 
ATOM 1698 C CA  . GLU A 1 209 ? 18.845  36.179  166.869 1.00 54.07  ? 255 GLU A CA  1 
ATOM 1699 C C   . GLU A 1 209 ? 20.236  35.542  166.997 1.00 50.50  ? 255 GLU A C   1 
ATOM 1700 O O   . GLU A 1 209 ? 20.416  34.471  167.576 1.00 45.76  ? 255 GLU A O   1 
ATOM 1701 C CB  . GLU A 1 209 ? 17.847  35.545  167.849 1.00 49.17  ? 255 GLU A CB  1 
ATOM 1702 C CG  . GLU A 1 209 ? 18.207  35.686  169.329 1.00 52.19  ? 255 GLU A CG  1 
ATOM 1703 C CD  . GLU A 1 209 ? 18.752  34.406  169.936 1.00 54.40  ? 255 GLU A CD  1 
ATOM 1704 O OE1 . GLU A 1 209 ? 19.296  34.460  171.057 1.00 60.14  ? 255 GLU A OE1 1 
ATOM 1705 O OE2 . GLU A 1 209 ? 18.653  33.346  169.287 1.00 57.07  ? 255 GLU A OE2 1 
ATOM 1706 N N   . ASN A 1 210 ? 21.221  36.199  166.390 1.00 60.54  ? 256 ASN A N   1 
ATOM 1707 C CA  . ASN A 1 210 ? 22.607  35.781  166.593 1.00 63.92  ? 256 ASN A CA  1 
ATOM 1708 C C   . ASN A 1 210 ? 23.173  36.460  167.833 1.00 68.76  ? 256 ASN A C   1 
ATOM 1709 O O   . ASN A 1 210 ? 23.131  37.689  167.953 1.00 67.25  ? 256 ASN A O   1 
ATOM 1710 C CB  . ASN A 1 210 ? 23.466  36.109  165.378 1.00 67.32  ? 256 ASN A CB  1 
ATOM 1711 C CG  . ASN A 1 210 ? 24.914  35.705  165.567 1.00 64.39  ? 256 ASN A CG  1 
ATOM 1712 O OD1 . ASN A 1 210 ? 25.286  34.558  165.323 1.00 65.67  ? 256 ASN A OD1 1 
ATOM 1713 N ND2 . ASN A 1 210 ? 25.740  36.648  166.003 1.00 60.42  ? 256 ASN A ND2 1 
ATOM 1714 N N   . LEU A 1 211 ? 23.707  35.659  168.753 1.00 73.62  ? 257 LEU A N   1 
ATOM 1715 C CA  . LEU A 1 211 ? 24.429  36.164  169.910 1.00 72.03  ? 257 LEU A CA  1 
ATOM 1716 C C   . LEU A 1 211 ? 25.223  35.020  170.520 1.00 73.14  ? 257 LEU A C   1 
ATOM 1717 O O   . LEU A 1 211 ? 24.762  33.876  170.559 1.00 73.17  ? 257 LEU A O   1 
ATOM 1718 C CB  . LEU A 1 211 ? 23.483  36.799  170.940 1.00 72.26  ? 257 LEU A CB  1 
ATOM 1719 C CG  . LEU A 1 211 ? 22.274  36.009  171.444 1.00 69.07  ? 257 LEU A CG  1 
ATOM 1720 C CD1 . LEU A 1 211 ? 22.615  35.149  172.653 1.00 70.77  ? 257 LEU A CD1 1 
ATOM 1721 C CD2 . LEU A 1 211 ? 21.136  36.963  171.765 1.00 67.44  ? 257 LEU A CD2 1 
ATOM 1722 N N   . GLY A 1 212 ? 26.427  35.338  170.989 1.00 80.55  ? 258 GLY A N   1 
ATOM 1723 C CA  . GLY A 1 212 ? 27.316  34.323  171.517 1.00 79.98  ? 258 GLY A CA  1 
ATOM 1724 C C   . GLY A 1 212 ? 28.020  33.544  170.426 1.00 79.54  ? 258 GLY A C   1 
ATOM 1725 O O   . GLY A 1 212 ? 27.544  33.486  169.289 1.00 79.82  ? 258 GLY A O   1 
ATOM 1726 N N   . THR A 1 213 ? 29.162  32.937  170.759 1.00 83.38  ? 259 THR A N   1 
ATOM 1727 C CA  . THR A 1 213 ? 29.923  32.195  169.761 1.00 85.61  ? 259 THR A CA  1 
ATOM 1728 C C   . THR A 1 213 ? 29.396  30.782  169.556 1.00 84.15  ? 259 THR A C   1 
ATOM 1729 O O   . THR A 1 213 ? 29.881  30.078  168.664 1.00 79.93  ? 259 THR A O   1 
ATOM 1730 C CB  . THR A 1 213 ? 31.399  32.137  170.154 1.00 84.95  ? 259 THR A CB  1 
ATOM 1731 O OG1 . THR A 1 213 ? 32.125  31.387  169.174 1.00 86.72  ? 259 THR A OG1 1 
ATOM 1732 C CG2 . THR A 1 213 ? 31.559  31.473  171.512 1.00 83.96  ? 259 THR A CG2 1 
ATOM 1733 N N   . THR A 1 214 ? 28.423  30.350  170.353 1.00 80.69  ? 260 THR A N   1 
ATOM 1734 C CA  . THR A 1 214 ? 27.885  28.994  170.254 1.00 81.67  ? 260 THR A CA  1 
ATOM 1735 C C   . THR A 1 214 ? 26.817  28.888  169.168 1.00 79.92  ? 260 THR A C   1 
ATOM 1736 O O   . THR A 1 214 ? 25.701  28.431  169.405 1.00 76.86  ? 260 THR A O   1 
ATOM 1737 C CB  . THR A 1 214 ? 27.335  28.555  171.606 1.00 82.27  ? 260 THR A CB  1 
ATOM 1738 O OG1 . THR A 1 214 ? 26.119  29.261  171.882 1.00 80.74  ? 260 THR A OG1 1 
ATOM 1739 C CG2 . THR A 1 214 ? 28.344  28.847  172.705 1.00 79.05  ? 260 THR A CG2 1 
ATOM 1740 N N   . GLY A 1 215 ? 27.163  29.317  167.959 1.00 67.65  ? 261 GLY A N   1 
ATOM 1741 C CA  . GLY A 1 215 ? 26.264  29.197  166.833 1.00 64.53  ? 261 GLY A CA  1 
ATOM 1742 C C   . GLY A 1 215 ? 25.107  30.183  166.882 1.00 63.05  ? 261 GLY A C   1 
ATOM 1743 O O   . GLY A 1 215 ? 25.046  31.098  167.704 1.00 62.81  ? 261 GLY A O   1 
ATOM 1744 N N   . THR A 1 216 ? 24.173  29.971  165.962 1.00 48.38  ? 262 THR A N   1 
ATOM 1745 C CA  . THR A 1 216 ? 22.964  30.769  165.837 1.00 48.17  ? 262 THR A CA  1 
ATOM 1746 C C   . THR A 1 216 ? 21.770  29.977  166.361 1.00 48.34  ? 262 THR A C   1 
ATOM 1747 O O   . THR A 1 216 ? 21.871  28.789  166.678 1.00 49.93  ? 262 THR A O   1 
ATOM 1748 C CB  . THR A 1 216 ? 22.750  31.198  164.385 1.00 50.69  ? 262 THR A CB  1 
ATOM 1749 O OG1 . THR A 1 216 ? 22.053  30.165  163.680 1.00 52.71  ? 262 THR A OG1 1 
ATOM 1750 C CG2 . THR A 1 216 ? 24.083  31.458  163.703 1.00 45.49  ? 262 THR A CG2 1 
ATOM 1751 N N   . LYS A 1 217 ? 20.624  30.651  166.451 1.00 40.55  ? 263 LYS A N   1 
ATOM 1752 C CA  . LYS A 1 217 ? 19.431  30.042  167.035 1.00 33.82  ? 263 LYS A CA  1 
ATOM 1753 C C   . LYS A 1 217 ? 18.211  30.825  166.572 1.00 34.22  ? 263 LYS A C   1 
ATOM 1754 O O   . LYS A 1 217 ? 18.079  32.006  166.901 1.00 47.85  ? 263 LYS A O   1 
ATOM 1755 C CB  . LYS A 1 217 ? 19.532  30.029  168.554 1.00 34.32  ? 263 LYS A CB  1 
ATOM 1756 C CG  . LYS A 1 217 ? 18.230  29.734  169.266 1.00 38.26  ? 263 LYS A CG  1 
ATOM 1757 C CD  . LYS A 1 217 ? 18.481  29.248  170.680 1.00 40.09  ? 263 LYS A CD  1 
ATOM 1758 C CE  . LYS A 1 217 ? 19.412  30.183  171.430 1.00 37.97  ? 263 LYS A CE  1 
ATOM 1759 N NZ  . LYS A 1 217 ? 18.894  31.577  171.458 1.00 42.05  ? 263 LYS A NZ  1 
ATOM 1760 N N   . LEU A 1 218 ? 17.319  30.169  165.833 1.00 29.09  ? 264 LEU A N   1 
ATOM 1761 C CA  . LEU A 1 218 ? 16.110  30.817  165.322 1.00 28.55  ? 264 LEU A CA  1 
ATOM 1762 C C   . LEU A 1 218 ? 15.075  30.868  166.439 1.00 31.78  ? 264 LEU A C   1 
ATOM 1763 O O   . LEU A 1 218 ? 14.299  29.935  166.642 1.00 37.22  ? 264 LEU A O   1 
ATOM 1764 C CB  . LEU A 1 218 ? 15.577  30.077  164.103 1.00 28.87  ? 264 LEU A CB  1 
ATOM 1765 C CG  . LEU A 1 218 ? 16.419  30.140  162.829 1.00 27.85  ? 264 LEU A CG  1 
ATOM 1766 C CD1 . LEU A 1 218 ? 15.561  29.862  161.613 1.00 30.28  ? 264 LEU A CD1 1 
ATOM 1767 C CD2 . LEU A 1 218 ? 17.095  31.482  162.697 1.00 27.51  ? 264 LEU A CD2 1 
ATOM 1768 N N   . VAL A 1 219 ? 15.062  31.975  167.169 1.00 37.51  ? 265 VAL A N   1 
ATOM 1769 C CA  . VAL A 1 219 ? 14.119  32.135  168.282 1.00 36.67  ? 265 VAL A CA  1 
ATOM 1770 C C   . VAL A 1 219 ? 12.727  32.420  167.732 1.00 39.62  ? 265 VAL A C   1 
ATOM 1771 O O   . VAL A 1 219 ? 12.600  33.092  166.692 1.00 37.05  ? 265 VAL A O   1 
ATOM 1772 C CB  . VAL A 1 219 ? 14.591  33.250  169.219 1.00 44.28  ? 265 VAL A CB  1 
ATOM 1773 C CG1 . VAL A 1 219 ? 13.472  33.722  170.133 1.00 41.67  ? 265 VAL A CG1 1 
ATOM 1774 C CG2 . VAL A 1 219 ? 15.737  32.749  170.065 1.00 42.68  ? 265 VAL A CG2 1 
ATOM 1775 N N   . PRO A 1 220 ? 11.671  31.916  168.368 1.00 46.34  ? 266 PRO A N   1 
ATOM 1776 C CA  . PRO A 1 220 ? 10.307  32.221  167.924 1.00 36.32  ? 266 PRO A CA  1 
ATOM 1777 C C   . PRO A 1 220 ? 10.022  33.716  167.898 1.00 37.21  ? 266 PRO A C   1 
ATOM 1778 O O   . PRO A 1 220 ? 10.491  34.474  168.749 1.00 41.54  ? 266 PRO A O   1 
ATOM 1779 C CB  . PRO A 1 220 ? 9.432   31.522  168.971 1.00 36.82  ? 266 PRO A CB  1 
ATOM 1780 C CG  . PRO A 1 220 ? 10.341  30.670  169.803 1.00 42.25  ? 266 PRO A CG  1 
ATOM 1781 C CD  . PRO A 1 220 ? 11.720  30.743  169.253 1.00 47.24  ? 266 PRO A CD  1 
ATOM 1782 N N   . LEU A 1 221 ? 9.237   34.135  166.908 1.00 32.04  ? 267 LEU A N   1 
ATOM 1783 C CA  . LEU A 1 221 ? 8.647   35.468  166.870 1.00 28.73  ? 267 LEU A CA  1 
ATOM 1784 C C   . LEU A 1 221 ? 7.143   35.313  166.701 1.00 37.26  ? 267 LEU A C   1 
ATOM 1785 O O   . LEU A 1 221 ? 6.683   34.777  165.688 1.00 43.71  ? 267 LEU A O   1 
ATOM 1786 C CB  . LEU A 1 221 ? 9.228   36.312  165.735 1.00 32.84  ? 267 LEU A CB  1 
ATOM 1787 C CG  . LEU A 1 221 ? 8.581   37.690  165.583 1.00 34.04  ? 267 LEU A CG  1 
ATOM 1788 C CD1 . LEU A 1 221 ? 8.983   38.599  166.732 1.00 34.64  ? 267 LEU A CD1 1 
ATOM 1789 C CD2 . LEU A 1 221 ? 8.938   38.322  164.251 1.00 34.06  ? 267 LEU A CD2 1 
ATOM 1790 N N   . MET A 1 222 ? 6.385   35.785  167.684 1.00 41.39  ? 268 MET A N   1 
ATOM 1791 C CA  . MET A 1 222 ? 4.945   35.596  167.675 1.00 34.36  ? 268 MET A CA  1 
ATOM 1792 C C   . MET A 1 222 ? 4.292   36.491  166.626 1.00 33.73  ? 268 MET A C   1 
ATOM 1793 O O   . MET A 1 222 ? 4.883   37.454  166.133 1.00 39.02  ? 268 MET A O   1 
ATOM 1794 C CB  . MET A 1 222 ? 4.357   35.885  169.056 1.00 38.30  ? 268 MET A CB  1 
ATOM 1795 C CG  . MET A 1 222 ? 4.338   34.687  170.001 1.00 41.77  ? 268 MET A CG  1 
ATOM 1796 S SD  . MET A 1 222 ? 4.031   33.087  169.222 1.00 49.20  ? 268 MET A SD  1 
ATOM 1797 C CE  . MET A 1 222 ? 2.373   33.312  168.585 1.00 39.74  ? 268 MET A CE  1 
ATOM 1798 N N   . MET A 1 223 ? 3.052   36.156  166.286 1.00 31.56  ? 269 MET A N   1 
ATOM 1799 C CA  . MET A 1 223 ? 2.291   36.856  165.267 1.00 33.40  ? 269 MET A CA  1 
ATOM 1800 C C   . MET A 1 223 ? 0.924   37.235  165.813 1.00 42.98  ? 269 MET A C   1 
ATOM 1801 O O   . MET A 1 223 ? 0.424   36.590  166.740 1.00 48.16  ? 269 MET A O   1 
ATOM 1802 C CB  . MET A 1 223 ? 2.123   35.984  164.015 1.00 33.58  ? 269 MET A CB  1 
ATOM 1803 C CG  . MET A 1 223 ? 3.431   35.626  163.349 1.00 41.88  ? 269 MET A CG  1 
ATOM 1804 S SD  . MET A 1 223 ? 4.132   37.018  162.454 1.00 42.91  ? 269 MET A SD  1 
ATOM 1805 C CE  . MET A 1 223 ? 2.974   37.134  161.098 1.00 32.20  ? 269 MET A CE  1 
ATOM 1806 N N   . PRO A 1 224 ? 0.304   38.285  165.271 1.00 39.85  ? 270 PRO A N   1 
ATOM 1807 C CA  . PRO A 1 224 ? -1.018  38.695  165.766 1.00 37.55  ? 270 PRO A CA  1 
ATOM 1808 C C   . PRO A 1 224 ? -2.048  37.593  165.571 1.00 34.34  ? 270 PRO A C   1 
ATOM 1809 O O   . PRO A 1 224 ? -2.067  36.914  164.543 1.00 35.47  ? 270 PRO A O   1 
ATOM 1810 C CB  . PRO A 1 224 ? -1.348  39.930  164.919 1.00 31.73  ? 270 PRO A CB  1 
ATOM 1811 C CG  . PRO A 1 224 ? -0.033  40.403  164.400 1.00 29.94  ? 270 PRO A CG  1 
ATOM 1812 C CD  . PRO A 1 224 ? 0.783   39.171  164.199 1.00 36.04  ? 270 PRO A CD  1 
ATOM 1813 N N   . LYS A 1 225 ? -2.908  37.423  166.569 1.00 27.96  ? 271 LYS A N   1 
ATOM 1814 C CA  . LYS A 1 225 ? -3.987  36.454  166.488 1.00 30.05  ? 271 LYS A CA  1 
ATOM 1815 C C   . LYS A 1 225 ? -5.273  37.144  166.041 1.00 38.34  ? 271 LYS A C   1 
ATOM 1816 O O   . LYS A 1 225 ? -5.337  38.367  165.898 1.00 48.21  ? 271 LYS A O   1 
ATOM 1817 C CB  . LYS A 1 225 ? -4.171  35.751  167.830 1.00 35.05  ? 271 LYS A CB  1 
ATOM 1818 C CG  . LYS A 1 225 ? -2.871  35.333  168.488 1.00 35.18  ? 271 LYS A CG  1 
ATOM 1819 C CD  . LYS A 1 225 ? -3.107  34.278  169.552 1.00 38.45  ? 271 LYS A CD  1 
ATOM 1820 C CE  . LYS A 1 225 ? -1.994  33.248  169.551 1.00 41.26  ? 271 LYS A CE  1 
ATOM 1821 N NZ  . LYS A 1 225 ? -1.499  32.985  168.173 1.00 40.52  ? 271 LYS A NZ  1 
ATOM 1822 N N   . ALA A 1 226 ? -6.313  36.349  165.815 1.00 37.72  ? 272 ALA A N   1 
ATOM 1823 C CA  . ALA A 1 226 ? -7.595  36.900  165.416 1.00 37.01  ? 272 ALA A CA  1 
ATOM 1824 C C   . ALA A 1 226 ? -8.220  37.685  166.564 1.00 36.71  ? 272 ALA A C   1 
ATOM 1825 O O   . ALA A 1 226 ? -8.021  37.382  167.743 1.00 36.52  ? 272 ALA A O   1 
ATOM 1826 C CB  . ALA A 1 226 ? -8.541  35.793  164.960 1.00 35.03  ? 272 ALA A CB  1 
ATOM 1827 N N   . GLY A 1 227 ? -8.990  38.707  166.202 1.00 45.08  ? 273 GLY A N   1 
ATOM 1828 C CA  . GLY A 1 227 ? -9.573  39.574  167.202 1.00 47.04  ? 273 GLY A CA  1 
ATOM 1829 C C   . GLY A 1 227 ? -8.605  40.553  167.817 1.00 50.68  ? 273 GLY A C   1 
ATOM 1830 O O   . GLY A 1 227 ? -8.891  41.111  168.879 1.00 53.41  ? 273 GLY A O   1 
ATOM 1831 N N   . ASP A 1 228 ? -7.459  40.778  167.180 1.00 48.05  ? 274 ASP A N   1 
ATOM 1832 C CA  . ASP A 1 228 ? -6.478  41.757  167.628 1.00 46.03  ? 274 ASP A CA  1 
ATOM 1833 C C   . ASP A 1 228 ? -6.509  42.935  166.669 1.00 47.68  ? 274 ASP A C   1 
ATOM 1834 O O   . ASP A 1 228 ? -6.364  42.755  165.456 1.00 50.79  ? 274 ASP A O   1 
ATOM 1835 C CB  . ASP A 1 228 ? -5.076  41.150  167.691 1.00 42.18  ? 274 ASP A CB  1 
ATOM 1836 C CG  . ASP A 1 228 ? -4.909  40.192  168.848 1.00 49.59  ? 274 ASP A CG  1 
ATOM 1837 O OD1 . ASP A 1 228 ? -5.649  40.328  169.844 1.00 52.11  ? 274 ASP A OD1 1 
ATOM 1838 O OD2 . ASP A 1 228 ? -4.036  39.303  168.764 1.00 50.80  ? 274 ASP A OD2 1 
ATOM 1839 N N   . ASN A 1 229 ? -6.700  44.136  167.211 1.00 47.70  ? 275 ASN A N   1 
ATOM 1840 C CA  . ASN A 1 229 ? -6.769  45.345  166.394 1.00 48.51  ? 275 ASN A CA  1 
ATOM 1841 C C   . ASN A 1 229 ? -5.353  45.867  166.151 1.00 52.77  ? 275 ASN A C   1 
ATOM 1842 O O   . ASN A 1 229 ? -4.965  46.959  166.572 1.00 63.47  ? 275 ASN A O   1 
ATOM 1843 C CB  . ASN A 1 229 ? -7.652  46.387  167.063 1.00 52.72  ? 275 ASN A CB  1 
ATOM 1844 C CG  . ASN A 1 229 ? -9.089  45.928  167.196 1.00 55.51  ? 275 ASN A CG  1 
ATOM 1845 O OD1 . ASN A 1 229 ? -9.615  45.239  166.323 1.00 52.52  ? 275 ASN A OD1 1 
ATOM 1846 N ND2 . ASN A 1 229 ? -9.731  46.306  168.295 1.00 57.63  ? 275 ASN A ND2 1 
ATOM 1847 N N   . ARG A 1 230 ? -4.571  45.053  165.452 1.00 40.98  ? 276 ARG A N   1 
ATOM 1848 C CA  . ARG A 1 230 ? -3.219  45.426  165.073 1.00 41.43  ? 276 ARG A CA  1 
ATOM 1849 C C   . ARG A 1 230 ? -3.261  46.364  163.876 1.00 45.27  ? 276 ARG A C   1 
ATOM 1850 O O   . ARG A 1 230 ? -4.064  46.193  162.956 1.00 49.58  ? 276 ARG A O   1 
ATOM 1851 C CB  . ARG A 1 230 ? -2.385  44.190  164.744 1.00 41.21  ? 276 ARG A CB  1 
ATOM 1852 C CG  . ARG A 1 230 ? -1.928  43.415  165.966 1.00 44.94  ? 276 ARG A CG  1 
ATOM 1853 C CD  . ARG A 1 230 ? -1.164  44.307  166.924 1.00 44.56  ? 276 ARG A CD  1 
ATOM 1854 N NE  . ARG A 1 230 ? -1.905  44.550  168.154 1.00 48.06  ? 276 ARG A NE  1 
ATOM 1855 C CZ  . ARG A 1 230 ? -1.867  43.762  169.219 1.00 50.14  ? 276 ARG A CZ  1 
ATOM 1856 N NH1 . ARG A 1 230 ? -1.129  42.665  169.240 1.00 48.06  ? 276 ARG A NH1 1 
ATOM 1857 N NH2 . ARG A 1 230 ? -2.588  44.083  170.289 1.00 46.80  ? 276 ARG A NH2 1 
ATOM 1858 N N   . LYS A 1 231 ? -2.391  47.365  163.899 1.00 43.49  ? 277 LYS A N   1 
ATOM 1859 C CA  . LYS A 1 231 ? -2.378  48.400  162.878 1.00 39.57  ? 277 LYS A CA  1 
ATOM 1860 C C   . LYS A 1 231 ? -1.053  48.373  162.117 1.00 43.65  ? 277 LYS A C   1 
ATOM 1861 O O   . LYS A 1 231 ? -0.168  47.546  162.375 1.00 47.95  ? 277 LYS A O   1 
ATOM 1862 C CB  . LYS A 1 231 ? -2.638  49.769  163.507 1.00 40.26  ? 277 LYS A CB  1 
ATOM 1863 C CG  . LYS A 1 231 ? -3.979  49.882  164.209 1.00 42.56  ? 277 LYS A CG  1 
ATOM 1864 C CD  . LYS A 1 231 ? -4.148  51.247  164.852 1.00 45.17  ? 277 LYS A CD  1 
ATOM 1865 C CE  . LYS A 1 231 ? -5.444  51.329  165.636 1.00 44.01  ? 277 LYS A CE  1 
ATOM 1866 N NZ  . LYS A 1 231 ? -5.514  50.283  166.691 1.00 42.50  ? 277 LYS A NZ  1 
ATOM 1867 N N   . LEU A 1 232 ? -0.927  49.299  161.163 1.00 36.33  ? 278 LEU A N   1 
ATOM 1868 C CA  . LEU A 1 232 ? 0.279   49.361  160.350 1.00 36.55  ? 278 LEU A CA  1 
ATOM 1869 C C   . LEU A 1 232 ? 1.504   49.690  161.188 1.00 39.06  ? 278 LEU A C   1 
ATOM 1870 O O   . LEU A 1 232 ? 2.603   49.230  160.874 1.00 42.63  ? 278 LEU A O   1 
ATOM 1871 C CB  . LEU A 1 232 ? 0.113   50.386  159.232 1.00 34.91  ? 278 LEU A CB  1 
ATOM 1872 C CG  . LEU A 1 232 ? 1.227   50.350  158.187 1.00 29.44  ? 278 LEU A CG  1 
ATOM 1873 C CD1 . LEU A 1 232 ? 1.467   48.925  157.741 1.00 31.53  ? 278 LEU A CD1 1 
ATOM 1874 C CD2 . LEU A 1 232 ? 0.878   51.219  157.007 1.00 30.22  ? 278 LEU A CD2 1 
ATOM 1875 N N   . VAL A 1 233 ? 1.342   50.482  162.250 1.00 42.47  ? 279 VAL A N   1 
ATOM 1876 C CA  . VAL A 1 233 ? 2.468   50.743  163.139 1.00 41.96  ? 279 VAL A CA  1 
ATOM 1877 C C   . VAL A 1 233 ? 2.943   49.453  163.797 1.00 41.82  ? 279 VAL A C   1 
ATOM 1878 O O   . VAL A 1 233 ? 4.151   49.195  163.874 1.00 45.71  ? 279 VAL A O   1 
ATOM 1879 C CB  . VAL A 1 233 ? 2.092   51.818  164.177 1.00 40.81  ? 279 VAL A CB  1 
ATOM 1880 C CG1 . VAL A 1 233 ? 0.773   51.479  164.854 1.00 43.52  ? 279 VAL A CG1 1 
ATOM 1881 C CG2 . VAL A 1 233 ? 3.196   51.970  165.209 1.00 39.37  ? 279 VAL A CG2 1 
ATOM 1882 N N   . ASP A 1 234 ? 2.014   48.614  164.258 1.00 33.35  ? 280 ASP A N   1 
ATOM 1883 C CA  . ASP A 1 234 ? 2.393   47.341  164.862 1.00 32.77  ? 280 ASP A CA  1 
ATOM 1884 C C   . ASP A 1 234 ? 3.059   46.422  163.847 1.00 35.83  ? 280 ASP A C   1 
ATOM 1885 O O   . ASP A 1 234 ? 4.038   45.738  164.170 1.00 46.88  ? 280 ASP A O   1 
ATOM 1886 C CB  . ASP A 1 234 ? 1.165   46.669  165.471 1.00 39.86  ? 280 ASP A CB  1 
ATOM 1887 C CG  . ASP A 1 234 ? 0.311   47.634  166.267 1.00 49.57  ? 280 ASP A CG  1 
ATOM 1888 O OD1 . ASP A 1 234 ? 0.793   48.141  167.301 1.00 52.58  ? 280 ASP A OD1 1 
ATOM 1889 O OD2 . ASP A 1 234 ? -0.840  47.892  165.858 1.00 49.88  ? 280 ASP A OD2 1 
ATOM 1890 N N   . PHE A 1 235 ? 2.548   46.389  162.615 1.00 30.44  ? 281 PHE A N   1 
ATOM 1891 C CA  . PHE A 1 235 ? 3.167   45.537  161.604 1.00 28.76  ? 281 PHE A CA  1 
ATOM 1892 C C   . PHE A 1 235 ? 4.554   46.036  161.213 1.00 34.49  ? 281 PHE A C   1 
ATOM 1893 O O   . PHE A 1 235 ? 5.460   45.227  160.979 1.00 39.78  ? 281 PHE A O   1 
ATOM 1894 C CB  . PHE A 1 235 ? 2.265   45.438  160.379 1.00 29.70  ? 281 PHE A CB  1 
ATOM 1895 C CG  . PHE A 1 235 ? 1.247   44.348  160.478 1.00 37.09  ? 281 PHE A CG  1 
ATOM 1896 C CD1 . PHE A 1 235 ? 0.184   44.458  161.357 1.00 39.36  ? 281 PHE A CD1 1 
ATOM 1897 C CD2 . PHE A 1 235 ? 1.357   43.207  159.708 1.00 34.76  ? 281 PHE A CD2 1 
ATOM 1898 C CE1 . PHE A 1 235 ? -0.754  43.456  161.459 1.00 31.61  ? 281 PHE A CE1 1 
ATOM 1899 C CE2 . PHE A 1 235 ? 0.423   42.202  159.807 1.00 37.23  ? 281 PHE A CE2 1 
ATOM 1900 C CZ  . PHE A 1 235 ? -0.634  42.327  160.683 1.00 32.81  ? 281 PHE A CZ  1 
ATOM 1901 N N   . GLN A 1 236 ? 4.739   47.354  161.137 1.00 31.76  ? 282 GLN A N   1 
ATOM 1902 C CA  . GLN A 1 236 ? 6.064   47.906  160.884 1.00 27.98  ? 282 GLN A CA  1 
ATOM 1903 C C   . GLN A 1 236 ? 7.018   47.575  162.023 1.00 31.56  ? 282 GLN A C   1 
ATOM 1904 O O   . GLN A 1 236 ? 8.193   47.276  161.788 1.00 40.50  ? 282 GLN A O   1 
ATOM 1905 C CB  . GLN A 1 236 ? 5.970   49.417  160.681 1.00 29.99  ? 282 GLN A CB  1 
ATOM 1906 C CG  . GLN A 1 236 ? 5.472   49.827  159.310 1.00 31.28  ? 282 GLN A CG  1 
ATOM 1907 C CD  . GLN A 1 236 ? 5.202   51.312  159.209 1.00 34.06  ? 282 GLN A CD  1 
ATOM 1908 O OE1 . GLN A 1 236 ? 5.011   51.989  160.218 1.00 35.52  ? 282 GLN A OE1 1 
ATOM 1909 N NE2 . GLN A 1 236 ? 5.182   51.827  157.986 1.00 37.46  ? 282 GLN A NE2 1 
ATOM 1910 N N   . VAL A 1 237 ? 6.528   47.628  163.263 1.00 30.55  ? 283 VAL A N   1 
ATOM 1911 C CA  . VAL A 1 237 ? 7.349   47.237  164.405 1.00 32.60  ? 283 VAL A CA  1 
ATOM 1912 C C   . VAL A 1 237 ? 7.754   45.774  164.287 1.00 33.10  ? 283 VAL A C   1 
ATOM 1913 O O   . VAL A 1 237 ? 8.909   45.413  164.541 1.00 37.54  ? 283 VAL A O   1 
ATOM 1914 C CB  . VAL A 1 237 ? 6.600   47.518  165.721 1.00 32.80  ? 283 VAL A CB  1 
ATOM 1915 C CG1 . VAL A 1 237 ? 7.058   46.572  166.817 1.00 30.56  ? 283 VAL A CG1 1 
ATOM 1916 C CG2 . VAL A 1 237 ? 6.802   48.962  166.144 1.00 32.04  ? 283 VAL A CG2 1 
ATOM 1917 N N   . LEU A 1 238 ? 6.814   44.911  163.895 1.00 25.24  ? 284 LEU A N   1 
ATOM 1918 C CA  . LEU A 1 238 ? 7.132   43.496  163.726 1.00 22.91  ? 284 LEU A CA  1 
ATOM 1919 C C   . LEU A 1 238 ? 8.185   43.286  162.644 1.00 28.10  ? 284 LEU A C   1 
ATOM 1920 O O   . LEU A 1 238 ? 9.123   42.503  162.828 1.00 36.47  ? 284 LEU A O   1 
ATOM 1921 C CB  . LEU A 1 238 ? 5.868   42.705  163.392 1.00 22.50  ? 284 LEU A CB  1 
ATOM 1922 C CG  . LEU A 1 238 ? 4.978   42.281  164.560 1.00 28.37  ? 284 LEU A CG  1 
ATOM 1923 C CD1 . LEU A 1 238 ? 3.647   41.767  164.044 1.00 31.51  ? 284 LEU A CD1 1 
ATOM 1924 C CD2 . LEU A 1 238 ? 5.666   41.229  165.412 1.00 32.21  ? 284 LEU A CD2 1 
ATOM 1925 N N   . PHE A 1 239 ? 8.047   43.974  161.509 1.00 23.56  ? 285 PHE A N   1 
ATOM 1926 C CA  . PHE A 1 239 ? 9.027   43.822  160.437 1.00 23.12  ? 285 PHE A CA  1 
ATOM 1927 C C   . PHE A 1 239 ? 10.402  44.318  160.865 1.00 30.47  ? 285 PHE A C   1 
ATOM 1928 O O   . PHE A 1 239 ? 11.417  43.663  160.599 1.00 34.25  ? 285 PHE A O   1 
ATOM 1929 C CB  . PHE A 1 239 ? 8.563   44.563  159.186 1.00 24.65  ? 285 PHE A CB  1 
ATOM 1930 C CG  . PHE A 1 239 ? 9.448   44.346  157.995 1.00 25.59  ? 285 PHE A CG  1 
ATOM 1931 C CD1 . PHE A 1 239 ? 9.616   43.080  157.465 1.00 24.97  ? 285 PHE A CD1 1 
ATOM 1932 C CD2 . PHE A 1 239 ? 10.115  45.405  157.406 1.00 24.91  ? 285 PHE A CD2 1 
ATOM 1933 C CE1 . PHE A 1 239 ? 10.427  42.874  156.369 1.00 22.88  ? 285 PHE A CE1 1 
ATOM 1934 C CE2 . PHE A 1 239 ? 10.929  45.204  156.310 1.00 29.21  ? 285 PHE A CE2 1 
ATOM 1935 C CZ  . PHE A 1 239 ? 11.084  43.937  155.792 1.00 27.23  ? 285 PHE A CZ  1 
ATOM 1936 N N   . ASN A 1 240 ? 10.457  45.476  161.527 1.00 34.38  ? 286 ASN A N   1 
ATOM 1937 C CA  . ASN A 1 240 ? 11.736  46.003  161.987 1.00 25.50  ? 286 ASN A CA  1 
ATOM 1938 C C   . ASN A 1 240 ? 12.371  45.090  163.023 1.00 31.68  ? 286 ASN A C   1 
ATOM 1939 O O   . ASN A 1 240 ? 13.595  44.929  163.036 1.00 39.01  ? 286 ASN A O   1 
ATOM 1940 C CB  . ASN A 1 240 ? 11.552  47.408  162.555 1.00 29.57  ? 286 ASN A CB  1 
ATOM 1941 C CG  . ASN A 1 240 ? 11.068  48.395  161.514 1.00 39.06  ? 286 ASN A CG  1 
ATOM 1942 O OD1 . ASN A 1 240 ? 11.309  48.222  160.320 1.00 36.90  ? 286 ASN A OD1 1 
ATOM 1943 N ND2 . ASN A 1 240 ? 10.380  49.438  161.962 1.00 41.82  ? 286 ASN A ND2 1 
ATOM 1944 N N   . ASN A 1 241 ? 11.560  44.490  163.897 1.00 36.41  ? 287 ASN A N   1 
ATOM 1945 C CA  . ASN A 1 241 ? 12.074  43.510  164.844 1.00 35.52  ? 287 ASN A CA  1 
ATOM 1946 C C   . ASN A 1 241 ? 12.627  42.293  164.118 1.00 31.09  ? 287 ASN A C   1 
ATOM 1947 O O   . ASN A 1 241 ? 13.685  41.775  164.492 1.00 29.22  ? 287 ASN A O   1 
ATOM 1948 C CB  . ASN A 1 241 ? 10.956  43.117  165.815 1.00 33.12  ? 287 ASN A CB  1 
ATOM 1949 C CG  . ASN A 1 241 ? 11.433  42.240  166.959 1.00 41.39  ? 287 ASN A CG  1 
ATOM 1950 O OD1 . ASN A 1 241 ? 12.325  41.409  166.804 1.00 43.83  ? 287 ASN A OD1 1 
ATOM 1951 N ND2 . ASN A 1 241 ? 10.831  42.427  168.126 1.00 44.32  ? 287 ASN A ND2 1 
ATOM 1952 N N   . LEU A 1 242 ? 11.937  41.835  163.072 1.00 29.03  ? 288 LEU A N   1 
ATOM 1953 C CA  . LEU A 1 242 ? 12.420  40.696  162.299 1.00 30.55  ? 288 LEU A CA  1 
ATOM 1954 C C   . LEU A 1 242 ? 13.760  40.994  161.640 1.00 34.60  ? 288 LEU A C   1 
ATOM 1955 O O   . LEU A 1 242 ? 14.665  40.153  161.657 1.00 38.40  ? 288 LEU A O   1 
ATOM 1956 C CB  . LEU A 1 242 ? 11.386  40.307  161.244 1.00 31.59  ? 288 LEU A CB  1 
ATOM 1957 C CG  . LEU A 1 242 ? 11.535  38.930  160.600 1.00 32.59  ? 288 LEU A CG  1 
ATOM 1958 C CD1 . LEU A 1 242 ? 11.461  37.837  161.648 1.00 33.40  ? 288 LEU A CD1 1 
ATOM 1959 C CD2 . LEU A 1 242 ? 10.477  38.727  159.533 1.00 29.38  ? 288 LEU A CD2 1 
ATOM 1960 N N   . VAL A 1 243 ? 13.909  42.181  161.061 1.00 43.39  ? 289 VAL A N   1 
ATOM 1961 C CA  . VAL A 1 243 ? 15.115  42.534  160.322 1.00 37.39  ? 289 VAL A CA  1 
ATOM 1962 C C   . VAL A 1 243 ? 16.081  43.354  161.185 1.00 39.99  ? 289 VAL A C   1 
ATOM 1963 O O   . VAL A 1 243 ? 17.051  43.911  160.673 1.00 39.60  ? 289 VAL A O   1 
ATOM 1964 C CB  . VAL A 1 243 ? 14.769  43.258  159.010 1.00 32.51  ? 289 VAL A CB  1 
ATOM 1965 C CG1 . VAL A 1 243 ? 15.927  43.203  158.023 1.00 39.62  ? 289 VAL A CG1 1 
ATOM 1966 C CG2 . VAL A 1 243 ? 13.533  42.646  158.390 1.00 34.43  ? 289 VAL A CG2 1 
ATOM 1967 N N   . SER A 1 244 ? 15.837  43.430  162.495 1.00 50.14  ? 290 SER A N   1 
ATOM 1968 C CA  . SER A 1 244 ? 16.745  44.164  163.370 1.00 46.32  ? 290 SER A CA  1 
ATOM 1969 C C   . SER A 1 244 ? 18.109  43.489  163.439 1.00 51.98  ? 290 SER A C   1 
ATOM 1970 O O   . SER A 1 244 ? 19.145  44.137  163.248 1.00 53.07  ? 290 SER A O   1 
ATOM 1971 C CB  . SER A 1 244 ? 16.141  44.293  164.768 1.00 48.73  ? 290 SER A CB  1 
ATOM 1972 O OG  . SER A 1 244 ? 16.667  43.310  165.642 1.00 55.03  ? 290 SER A OG  1 
ATOM 1973 N N   . THR A 1 245 ? 18.131  42.185  163.708 1.00 53.63  ? 291 THR A N   1 
ATOM 1974 C CA  . THR A 1 245 ? 19.366  41.419  163.783 1.00 50.77  ? 291 THR A CA  1 
ATOM 1975 C C   . THR A 1 245 ? 19.740  40.783  162.453 1.00 50.06  ? 291 THR A C   1 
ATOM 1976 O O   . THR A 1 245 ? 20.547  39.847  162.426 1.00 52.04  ? 291 THR A O   1 
ATOM 1977 C CB  . THR A 1 245 ? 19.254  40.338  164.857 1.00 55.73  ? 291 THR A CB  1 
ATOM 1978 O OG1 . THR A 1 245 ? 20.478  39.597  164.916 1.00 56.16  ? 291 THR A OG1 1 
ATOM 1979 C CG2 . THR A 1 245 ? 18.110  39.391  164.532 1.00 54.27  ? 291 THR A CG2 1 
ATOM 1980 N N   . MET A 1 246 ? 19.174  41.269  161.355 1.00 51.02  ? 292 MET A N   1 
ATOM 1981 C CA  . MET A 1 246 ? 19.398  40.710  160.030 1.00 50.91  ? 292 MET A CA  1 
ATOM 1982 C C   . MET A 1 246 ? 20.291  41.590  159.172 1.00 52.32  ? 292 MET A C   1 
ATOM 1983 O O   . MET A 1 246 ? 21.188  41.081  158.498 1.00 53.88  ? 292 MET A O   1 
ATOM 1984 C CB  . MET A 1 246 ? 18.052  40.497  159.329 1.00 55.26  ? 292 MET A CB  1 
ATOM 1985 C CG  . MET A 1 246 ? 18.126  39.883  157.951 1.00 56.81  ? 292 MET A CG  1 
ATOM 1986 S SD  . MET A 1 246 ? 17.890  38.101  158.033 1.00 57.47  ? 292 MET A SD  1 
ATOM 1987 C CE  . MET A 1 246 ? 16.287  38.011  158.822 1.00 49.80  ? 292 MET A CE  1 
ATOM 1988 N N   . LEU A 1 247 ? 20.071  42.901  159.193 1.00 52.25  ? 293 LEU A N   1 
ATOM 1989 C CA  . LEU A 1 247 ? 20.981  43.856  158.583 1.00 53.06  ? 293 LEU A CA  1 
ATOM 1990 C C   . LEU A 1 247 ? 22.080  44.228  159.569 1.00 55.49  ? 293 LEU A C   1 
ATOM 1991 O O   . LEU A 1 247 ? 21.941  44.049  160.781 1.00 55.67  ? 293 LEU A O   1 
ATOM 1992 C CB  . LEU A 1 247 ? 20.241  45.119  158.138 1.00 56.19  ? 293 LEU A CB  1 
ATOM 1993 C CG  . LEU A 1 247 ? 19.109  44.969  157.123 1.00 57.55  ? 293 LEU A CG  1 
ATOM 1994 C CD1 . LEU A 1 247 ? 18.099  46.089  157.296 1.00 54.64  ? 293 LEU A CD1 1 
ATOM 1995 C CD2 . LEU A 1 247 ? 19.660  44.963  155.708 1.00 55.42  ? 293 LEU A CD2 1 
ATOM 1996 N N   . GLY A 1 248 ? 23.182  44.744  159.034 1.00 60.14  ? 294 GLY A N   1 
ATOM 1997 C CA  . GLY A 1 248 ? 24.318  45.088  159.859 1.00 62.03  ? 294 GLY A CA  1 
ATOM 1998 C C   . GLY A 1 248 ? 25.180  43.916  160.259 1.00 62.87  ? 294 GLY A C   1 
ATOM 1999 O O   . GLY A 1 248 ? 26.164  44.108  160.983 1.00 64.82  ? 294 GLY A O   1 
ATOM 2000 N N   . ASP A 1 249 ? 24.841  42.710  159.814 1.00 63.60  ? 295 ASP A N   1 
ATOM 2001 C CA  . ASP A 1 249 ? 25.617  41.510  160.095 1.00 64.59  ? 295 ASP A CA  1 
ATOM 2002 C C   . ASP A 1 249 ? 26.552  41.254  158.920 1.00 64.41  ? 295 ASP A C   1 
ATOM 2003 O O   . ASP A 1 249 ? 26.095  40.930  157.818 1.00 64.93  ? 295 ASP A O   1 
ATOM 2004 C CB  . ASP A 1 249 ? 24.697  40.312  160.324 1.00 61.77  ? 295 ASP A CB  1 
ATOM 2005 C CG  . ASP A 1 249 ? 25.216  39.372  161.393 1.00 64.93  ? 295 ASP A CG  1 
ATOM 2006 O OD1 . ASP A 1 249 ? 25.300  39.791  162.566 1.00 65.52  ? 295 ASP A OD1 1 
ATOM 2007 O OD2 . ASP A 1 249 ? 25.542  38.215  161.059 1.00 67.65  ? 295 ASP A OD2 1 
ATOM 2008 N N   . GLU A 1 250 ? 27.858  41.409  159.153 1.00 59.33  ? 296 GLU A N   1 
ATOM 2009 C CA  . GLU A 1 250 ? 28.815  41.216  158.070 1.00 61.37  ? 296 GLU A CA  1 
ATOM 2010 C C   . GLU A 1 250 ? 28.848  39.770  157.599 1.00 61.27  ? 296 GLU A C   1 
ATOM 2011 O O   . GLU A 1 250 ? 29.061  39.513  156.410 1.00 64.92  ? 296 GLU A O   1 
ATOM 2012 C CB  . GLU A 1 250 ? 30.209  41.669  158.502 1.00 63.34  ? 296 GLU A CB  1 
ATOM 2013 C CG  . GLU A 1 250 ? 31.091  42.134  157.346 1.00 64.36  ? 296 GLU A CG  1 
ATOM 2014 C CD  . GLU A 1 250 ? 30.308  42.833  156.246 1.00 65.63  ? 296 GLU A CD  1 
ATOM 2015 O OE1 . GLU A 1 250 ? 29.857  43.975  156.468 1.00 66.21  ? 296 GLU A OE1 1 
ATOM 2016 O OE2 . GLU A 1 250 ? 30.145  42.242  155.158 1.00 63.09  ? 296 GLU A OE2 1 
ATOM 2017 N N   . ASP A 1 251 ? 28.631  38.814  158.504 1.00 55.08  ? 297 ASP A N   1 
ATOM 2018 C CA  . ASP A 1 251 ? 28.554  37.420  158.085 1.00 54.36  ? 297 ASP A CA  1 
ATOM 2019 C C   . ASP A 1 251 ? 27.344  37.188  157.187 1.00 50.86  ? 297 ASP A C   1 
ATOM 2020 O O   . ASP A 1 251 ? 27.420  36.434  156.209 1.00 47.30  ? 297 ASP A O   1 
ATOM 2021 C CB  . ASP A 1 251 ? 28.506  36.507  159.308 1.00 51.71  ? 297 ASP A CB  1 
ATOM 2022 C CG  . ASP A 1 251 ? 29.198  35.185  159.070 1.00 58.88  ? 297 ASP A CG  1 
ATOM 2023 O OD1 . ASP A 1 251 ? 29.018  34.612  157.978 1.00 65.55  ? 297 ASP A OD1 1 
ATOM 2024 O OD2 . ASP A 1 251 ? 29.925  34.718  159.972 1.00 59.02  ? 297 ASP A OD2 1 
ATOM 2025 N N   . PHE A 1 252 ? 26.220  37.834  157.501 1.00 47.22  ? 298 PHE A N   1 
ATOM 2026 C CA  . PHE A 1 252 ? 25.044  37.748  156.641 1.00 45.39  ? 298 PHE A CA  1 
ATOM 2027 C C   . PHE A 1 252 ? 25.299  38.389  155.284 1.00 48.58  ? 298 PHE A C   1 
ATOM 2028 O O   . PHE A 1 252 ? 24.855  37.870  154.254 1.00 48.34  ? 298 PHE A O   1 
ATOM 2029 C CB  . PHE A 1 252 ? 23.852  38.408  157.326 1.00 48.06  ? 298 PHE A CB  1 
ATOM 2030 C CG  . PHE A 1 252 ? 22.798  37.442  157.759 1.00 52.35  ? 298 PHE A CG  1 
ATOM 2031 C CD1 . PHE A 1 252 ? 22.958  36.704  158.914 1.00 50.43  ? 298 PHE A CD1 1 
ATOM 2032 C CD2 . PHE A 1 252 ? 21.641  37.281  157.022 1.00 52.29  ? 298 PHE A CD2 1 
ATOM 2033 C CE1 . PHE A 1 252 ? 21.992  35.815  159.315 1.00 51.79  ? 298 PHE A CE1 1 
ATOM 2034 C CE2 . PHE A 1 252 ? 20.671  36.395  157.428 1.00 51.12  ? 298 PHE A CE2 1 
ATOM 2035 C CZ  . PHE A 1 252 ? 20.846  35.662  158.575 1.00 49.81  ? 298 PHE A CZ  1 
ATOM 2036 N N   . GLY A 1 253 ? 25.999  39.524  155.264 1.00 48.82  ? 299 GLY A N   1 
ATOM 2037 C CA  . GLY A 1 253 ? 26.366  40.123  153.991 1.00 43.62  ? 299 GLY A CA  1 
ATOM 2038 C C   . GLY A 1 253 ? 27.268  39.220  153.174 1.00 47.18  ? 299 GLY A C   1 
ATOM 2039 O O   . GLY A 1 253 ? 27.135  39.132  151.951 1.00 50.78  ? 299 GLY A O   1 
ATOM 2040 N N   . ILE A 1 254 ? 28.192  38.530  153.843 1.00 47.00  ? 300 ILE A N   1 
ATOM 2041 C CA  . ILE A 1 254 ? 29.068  37.582  153.162 1.00 39.83  ? 300 ILE A CA  1 
ATOM 2042 C C   . ILE A 1 254 ? 28.261  36.430  152.575 1.00 41.15  ? 300 ILE A C   1 
ATOM 2043 O O   . ILE A 1 254 ? 28.482  36.020  151.428 1.00 39.78  ? 300 ILE A O   1 
ATOM 2044 C CB  . ILE A 1 254 ? 30.156  37.085  154.132 1.00 38.23  ? 300 ILE A CB  1 
ATOM 2045 C CG1 . ILE A 1 254 ? 31.233  38.156  154.307 1.00 40.82  ? 300 ILE A CG1 1 
ATOM 2046 C CG2 . ILE A 1 254 ? 30.767  35.790  153.640 1.00 43.97  ? 300 ILE A CG2 1 
ATOM 2047 C CD1 . ILE A 1 254 ? 31.802  38.658  153.001 1.00 40.23  ? 300 ILE A CD1 1 
ATOM 2048 N N   . MET A 1 255 ? 27.314  35.891  153.347 1.00 40.87  ? 301 MET A N   1 
ATOM 2049 C CA  . MET A 1 255 ? 26.464  34.820  152.831 1.00 35.39  ? 301 MET A CA  1 
ATOM 2050 C C   . MET A 1 255 ? 25.647  35.289  151.634 1.00 32.39  ? 301 MET A C   1 
ATOM 2051 O O   . MET A 1 255 ? 25.504  34.560  150.646 1.00 34.46  ? 301 MET A O   1 
ATOM 2052 C CB  . MET A 1 255 ? 25.527  34.297  153.919 1.00 37.42  ? 301 MET A CB  1 
ATOM 2053 C CG  . MET A 1 255 ? 26.006  33.062  154.655 1.00 33.79  ? 301 MET A CG  1 
ATOM 2054 S SD  . MET A 1 255 ? 25.150  32.878  156.229 1.00 47.83  ? 301 MET A SD  1 
ATOM 2055 C CE  . MET A 1 255 ? 26.511  32.887  157.379 1.00 43.80  ? 301 MET A CE  1 
ATOM 2056 N N   . SER A 1 256 ? 25.082  36.496  151.716 1.00 32.27  ? 302 SER A N   1 
ATOM 2057 C CA  . SER A 1 256 ? 24.288  37.021  150.611 1.00 32.88  ? 302 SER A CA  1 
ATOM 2058 C C   . SER A 1 256 ? 25.139  37.217  149.365 1.00 36.27  ? 302 SER A C   1 
ATOM 2059 O O   . SER A 1 256 ? 24.707  36.890  148.255 1.00 43.40  ? 302 SER A O   1 
ATOM 2060 C CB  . SER A 1 256 ? 23.621  38.333  151.017 1.00 38.07  ? 302 SER A CB  1 
ATOM 2061 O OG  . SER A 1 256 ? 22.896  38.181  152.222 1.00 46.12  ? 302 SER A OG  1 
ATOM 2062 N N   . GLY A 1 257 ? 26.351  37.746  149.526 1.00 37.16  ? 303 GLY A N   1 
ATOM 2063 C CA  . GLY A 1 257 ? 27.239  37.880  148.385 1.00 34.12  ? 303 GLY A CA  1 
ATOM 2064 C C   . GLY A 1 257 ? 27.606  36.541  147.777 1.00 42.38  ? 303 GLY A C   1 
ATOM 2065 O O   . GLY A 1 257 ? 27.649  36.398  146.552 1.00 44.80  ? 303 GLY A O   1 
ATOM 2066 N N   . ASP A 1 258 ? 27.868  35.539  148.619 1.00 44.93  ? 304 ASP A N   1 
ATOM 2067 C CA  . ASP A 1 258 ? 28.242  34.227  148.103 1.00 37.70  ? 304 ASP A CA  1 
ATOM 2068 C C   . ASP A 1 258 ? 27.089  33.567  147.358 1.00 34.35  ? 304 ASP A C   1 
ATOM 2069 O O   . ASP A 1 258 ? 27.296  32.968  146.297 1.00 39.05  ? 304 ASP A O   1 
ATOM 2070 C CB  . ASP A 1 258 ? 28.732  33.334  149.239 1.00 40.88  ? 304 ASP A CB  1 
ATOM 2071 C CG  . ASP A 1 258 ? 30.160  33.636  149.637 1.00 50.36  ? 304 ASP A CG  1 
ATOM 2072 O OD1 . ASP A 1 258 ? 30.597  34.790  149.448 1.00 51.58  ? 304 ASP A OD1 1 
ATOM 2073 O OD2 . ASP A 1 258 ? 30.850  32.718  150.129 1.00 50.07  ? 304 ASP A OD2 1 
ATOM 2074 N N   . VAL A 1 259 ? 25.868  33.658  147.889 1.00 30.39  ? 305 VAL A N   1 
ATOM 2075 C CA  . VAL A 1 259 ? 24.734  33.082  147.170 1.00 33.05  ? 305 VAL A CA  1 
ATOM 2076 C C   . VAL A 1 259 ? 24.395  33.880  145.916 1.00 33.95  ? 305 VAL A C   1 
ATOM 2077 O O   . VAL A 1 259 ? 23.908  33.298  144.939 1.00 41.81  ? 305 VAL A O   1 
ATOM 2078 C CB  . VAL A 1 259 ? 23.494  32.937  148.070 1.00 25.76  ? 305 VAL A CB  1 
ATOM 2079 C CG1 . VAL A 1 259 ? 23.788  32.004  149.231 1.00 31.02  ? 305 VAL A CG1 1 
ATOM 2080 C CG2 . VAL A 1 259 ? 23.037  34.277  148.580 1.00 33.84  ? 305 VAL A CG2 1 
ATOM 2081 N N   . PHE A 1 260 ? 24.639  35.194  145.909 1.00 34.43  ? 306 PHE A N   1 
ATOM 2082 C CA  . PHE A 1 260 ? 24.489  35.971  144.683 1.00 31.31  ? 306 PHE A CA  1 
ATOM 2083 C C   . PHE A 1 260 ? 25.502  35.540  143.631 1.00 35.51  ? 306 PHE A C   1 
ATOM 2084 O O   . PHE A 1 260 ? 25.187  35.497  142.437 1.00 34.54  ? 306 PHE A O   1 
ATOM 2085 C CB  . PHE A 1 260 ? 24.636  37.461  144.990 1.00 30.49  ? 306 PHE A CB  1 
ATOM 2086 C CG  . PHE A 1 260 ? 24.152  38.360  143.891 1.00 32.68  ? 306 PHE A CG  1 
ATOM 2087 C CD1 . PHE A 1 260 ? 24.984  38.700  142.839 1.00 33.41  ? 306 PHE A CD1 1 
ATOM 2088 C CD2 . PHE A 1 260 ? 22.868  38.867  143.910 1.00 35.74  ? 306 PHE A CD2 1 
ATOM 2089 C CE1 . PHE A 1 260 ? 24.543  39.526  141.829 1.00 31.11  ? 306 PHE A CE1 1 
ATOM 2090 C CE2 . PHE A 1 260 ? 22.421  39.693  142.900 1.00 35.75  ? 306 PHE A CE2 1 
ATOM 2091 C CZ  . PHE A 1 260 ? 23.261  40.022  141.859 1.00 35.93  ? 306 PHE A CZ  1 
ATOM 2092 N N   . LYS A 1 261 ? 26.733  35.249  144.053 1.00 35.63  ? 307 LYS A N   1 
ATOM 2093 C CA  . LYS A 1 261 ? 27.734  34.749  143.119 1.00 31.94  ? 307 LYS A CA  1 
ATOM 2094 C C   . LYS A 1 261 ? 27.361  33.365  142.600 1.00 37.38  ? 307 LYS A C   1 
ATOM 2095 O O   . LYS A 1 261 ? 27.528  33.077  141.410 1.00 44.18  ? 307 LYS A O   1 
ATOM 2096 C CB  . LYS A 1 261 ? 29.106  34.722  143.790 1.00 35.90  ? 307 LYS A CB  1 
ATOM 2097 C CG  . LYS A 1 261 ? 30.208  34.109  142.942 1.00 36.78  ? 307 LYS A CG  1 
ATOM 2098 C CD  . LYS A 1 261 ? 31.585  34.595  143.373 1.00 39.29  ? 307 LYS A CD  1 
ATOM 2099 C CE  . LYS A 1 261 ? 31.672  34.786  144.878 1.00 39.50  ? 307 LYS A CE  1 
ATOM 2100 N NZ  . LYS A 1 261 ? 31.664  33.485  145.596 1.00 41.76  ? 307 LYS A NZ  1 
ATOM 2101 N N   . ALA A 1 262 ? 26.850  32.500  143.477 1.00 26.90  ? 308 ALA A N   1 
ATOM 2102 C CA  . ALA A 1 262 ? 26.517  31.135  143.079 1.00 24.01  ? 308 ALA A CA  1 
ATOM 2103 C C   . ALA A 1 262 ? 25.312  31.111  142.147 1.00 27.75  ? 308 ALA A C   1 
ATOM 2104 O O   . ALA A 1 262 ? 25.416  30.699  140.987 1.00 31.72  ? 308 ALA A O   1 
ATOM 2105 C CB  . ALA A 1 262 ? 26.258  30.278  144.319 1.00 25.42  ? 308 ALA A CB  1 
ATOM 2106 N N   . PHE A 1 263 ? 24.156  31.549  142.637 1.00 37.58  ? 309 PHE A N   1 
ATOM 2107 C CA  . PHE A 1 263 ? 22.949  31.663  141.825 1.00 30.42  ? 309 PHE A CA  1 
ATOM 2108 C C   . PHE A 1 263 ? 22.925  33.076  141.258 1.00 35.65  ? 309 PHE A C   1 
ATOM 2109 O O   . PHE A 1 263 ? 22.946  34.054  142.007 1.00 45.33  ? 309 PHE A O   1 
ATOM 2110 C CB  . PHE A 1 263 ? 21.694  31.380  142.645 1.00 24.87  ? 309 PHE A CB  1 
ATOM 2111 C CG  . PHE A 1 263 ? 21.792  30.163  143.516 1.00 31.06  ? 309 PHE A CG  1 
ATOM 2112 C CD1 . PHE A 1 263 ? 21.430  28.920  143.032 1.00 32.96  ? 309 PHE A CD1 1 
ATOM 2113 C CD2 . PHE A 1 263 ? 22.226  30.265  144.825 1.00 30.17  ? 309 PHE A CD2 1 
ATOM 2114 C CE1 . PHE A 1 263 ? 21.511  27.802  143.833 1.00 30.38  ? 309 PHE A CE1 1 
ATOM 2115 C CE2 . PHE A 1 263 ? 22.311  29.148  145.628 1.00 30.49  ? 309 PHE A CE2 1 
ATOM 2116 C CZ  . PHE A 1 263 ? 21.952  27.917  145.133 1.00 31.82  ? 309 PHE A CZ  1 
ATOM 2117 N N   . GLY A 1 264 ? 22.872  33.183  139.937 1.00 38.13  ? 310 GLY A N   1 
ATOM 2118 C CA  . GLY A 1 264 ? 22.848  34.484  139.301 1.00 41.78  ? 310 GLY A CA  1 
ATOM 2119 C C   . GLY A 1 264 ? 21.621  35.283  139.692 1.00 39.40  ? 310 GLY A C   1 
ATOM 2120 O O   . GLY A 1 264 ? 20.648  34.775  140.248 1.00 44.49  ? 310 GLY A O   1 
ATOM 2121 N N   . ALA A 1 265 ? 21.681  36.582  139.395 1.00 35.29  ? 311 ALA A N   1 
ATOM 2122 C CA  . ALA A 1 265 ? 20.573  37.469  139.729 1.00 43.12  ? 311 ALA A CA  1 
ATOM 2123 C C   . ALA A 1 265 ? 19.277  37.053  139.050 1.00 46.74  ? 311 ALA A C   1 
ATOM 2124 O O   . ALA A 1 265 ? 18.195  37.364  139.560 1.00 41.88  ? 311 ALA A O   1 
ATOM 2125 C CB  . ALA A 1 265 ? 20.921  38.909  139.353 1.00 40.31  ? 311 ALA A CB  1 
ATOM 2126 N N   . ASP A 1 266 ? 19.358  36.360  137.913 1.00 52.24  ? 312 ASP A N   1 
ATOM 2127 C CA  . ASP A 1 266 ? 18.152  35.845  137.275 1.00 49.57  ? 312 ASP A CA  1 
ATOM 2128 C C   . ASP A 1 266 ? 17.618  34.624  138.012 1.00 45.37  ? 312 ASP A C   1 
ATOM 2129 O O   . ASP A 1 266 ? 16.407  34.375  138.019 1.00 46.34  ? 312 ASP A O   1 
ATOM 2130 C CB  . ASP A 1 266 ? 18.437  35.504  135.813 1.00 51.34  ? 312 ASP A CB  1 
ATOM 2131 C CG  . ASP A 1 266 ? 19.055  36.661  135.054 1.00 54.05  ? 312 ASP A CG  1 
ATOM 2132 O OD1 . ASP A 1 266 ? 19.557  37.600  135.706 1.00 54.71  ? 312 ASP A OD1 1 
ATOM 2133 O OD2 . ASP A 1 266 ? 19.039  36.630  133.806 1.00 56.70  ? 312 ASP A OD2 1 
ATOM 2134 N N   . GLY A 1 267 ? 18.503  33.852  138.634 1.00 38.46  ? 313 GLY A N   1 
ATOM 2135 C CA  . GLY A 1 267 ? 18.142  32.634  139.325 1.00 41.54  ? 313 GLY A CA  1 
ATOM 2136 C C   . GLY A 1 267 ? 17.759  32.798  140.777 1.00 40.92  ? 313 GLY A C   1 
ATOM 2137 O O   . GLY A 1 267 ? 17.578  31.792  141.471 1.00 39.97  ? 313 GLY A O   1 
ATOM 2138 N N   . LEU A 1 268 ? 17.638  34.026  141.265 1.00 36.50  ? 314 LEU A N   1 
ATOM 2139 C CA  . LEU A 1 268 ? 17.229  34.271  142.638 1.00 36.10  ? 314 LEU A CA  1 
ATOM 2140 C C   . LEU A 1 268 ? 15.713  34.392  142.731 1.00 38.01  ? 314 LEU A C   1 
ATOM 2141 O O   . LEU A 1 268 ? 15.005  34.456  141.725 1.00 41.74  ? 314 LEU A O   1 
ATOM 2142 C CB  . LEU A 1 268 ? 17.886  35.540  143.178 1.00 33.51  ? 314 LEU A CB  1 
ATOM 2143 C CG  . LEU A 1 268 ? 19.412  35.541  143.221 1.00 33.06  ? 314 LEU A CG  1 
ATOM 2144 C CD1 . LEU A 1 268 ? 19.924  36.920  143.583 1.00 34.49  ? 314 LEU A CD1 1 
ATOM 2145 C CD2 . LEU A 1 268 ? 19.921  34.499  144.197 1.00 36.56  ? 314 LEU A CD2 1 
ATOM 2146 N N   . VAL A 1 269 ? 15.221  34.419  143.960 1.00 35.75  ? 315 VAL A N   1 
ATOM 2147 C CA  . VAL A 1 269 ? 13.801  34.612  144.225 1.00 37.37  ? 315 VAL A CA  1 
ATOM 2148 C C   . VAL A 1 269 ? 13.533  36.097  144.422 1.00 38.08  ? 315 VAL A C   1 
ATOM 2149 O O   . VAL A 1 269 ? 14.213  36.771  145.204 1.00 38.07  ? 315 VAL A O   1 
ATOM 2150 C CB  . VAL A 1 269 ? 13.351  33.788  145.446 1.00 32.42  ? 315 VAL A CB  1 
ATOM 2151 C CG1 . VAL A 1 269 ? 14.280  34.017  146.617 1.00 33.92  ? 315 VAL A CG1 1 
ATOM 2152 C CG2 . VAL A 1 269 ? 11.925  34.140  145.826 1.00 31.61  ? 315 VAL A CG2 1 
ATOM 2153 N N   . LYS A 1 270 ? 12.546  36.616  143.695 1.00 37.50  ? 316 LYS A N   1 
ATOM 2154 C CA  . LYS A 1 270 ? 12.217  38.034  143.723 1.00 37.21  ? 316 LYS A CA  1 
ATOM 2155 C C   . LYS A 1 270 ? 10.767  38.207  144.144 1.00 40.56  ? 316 LYS A C   1 
ATOM 2156 O O   . LYS A 1 270 ? 9.882   37.517  143.629 1.00 43.66  ? 316 LYS A O   1 
ATOM 2157 C CB  . LYS A 1 270 ? 12.450  38.683  142.356 1.00 38.63  ? 316 LYS A CB  1 
ATOM 2158 C CG  . LYS A 1 270 ? 13.853  38.487  141.807 1.00 42.51  ? 316 LYS A CG  1 
ATOM 2159 C CD  . LYS A 1 270 ? 13.867  38.571  140.291 1.00 44.56  ? 316 LYS A CD  1 
ATOM 2160 C CE  . LYS A 1 270 ? 13.144  37.392  139.663 1.00 45.17  ? 316 LYS A CE  1 
ATOM 2161 N NZ  . LYS A 1 270 ? 13.872  36.113  139.871 1.00 48.25  ? 316 LYS A NZ  1 
ATOM 2162 N N   . LEU A 1 271 ? 10.530  39.124  145.077 1.00 39.47  ? 317 LEU A N   1 
ATOM 2163 C CA  . LEU A 1 271 ? 9.178   39.425  145.525 1.00 30.60  ? 317 LEU A CA  1 
ATOM 2164 C C   . LEU A 1 271 ? 8.547   40.425  144.567 1.00 34.90  ? 317 LEU A C   1 
ATOM 2165 O O   . LEU A 1 271 ? 9.065   41.531  144.386 1.00 38.39  ? 317 LEU A O   1 
ATOM 2166 C CB  . LEU A 1 271 ? 9.196   39.974  146.948 1.00 30.46  ? 317 LEU A CB  1 
ATOM 2167 C CG  . LEU A 1 271 ? 9.710   39.014  148.019 1.00 33.39  ? 317 LEU A CG  1 
ATOM 2168 C CD1 . LEU A 1 271 ? 9.609   39.648  149.392 1.00 31.63  ? 317 LEU A CD1 1 
ATOM 2169 C CD2 . LEU A 1 271 ? 8.948   37.703  147.974 1.00 34.29  ? 317 LEU A CD2 1 
ATOM 2170 N N   . LEU A 1 272 ? 7.432   40.038  143.957 1.00 44.49  ? 318 LEU A N   1 
ATOM 2171 C CA  . LEU A 1 272 ? 6.806   40.877  142.947 1.00 45.15  ? 318 LEU A CA  1 
ATOM 2172 C C   . LEU A 1 272 ? 6.155   42.097  143.584 1.00 40.45  ? 318 LEU A C   1 
ATOM 2173 O O   . LEU A 1 272 ? 5.553   42.015  144.658 1.00 39.12  ? 318 LEU A O   1 
ATOM 2174 C CB  . LEU A 1 272 ? 5.770   40.075  142.164 1.00 44.79  ? 318 LEU A CB  1 
ATOM 2175 C CG  . LEU A 1 272 ? 6.354   39.150  141.096 1.00 46.42  ? 318 LEU A CG  1 
ATOM 2176 C CD1 . LEU A 1 272 ? 5.329   38.116  140.665 1.00 43.02  ? 318 LEU A CD1 1 
ATOM 2177 C CD2 . LEU A 1 272 ? 6.847   39.953  139.906 1.00 44.94  ? 318 LEU A CD2 1 
ATOM 2178 N N   . ALA A 1 273 ? 6.279   43.235  142.909 1.00 40.99  ? 319 ALA A N   1 
ATOM 2179 C CA  . ALA A 1 273 ? 5.705   44.473  143.410 1.00 41.87  ? 319 ALA A CA  1 
ATOM 2180 C C   . ALA A 1 273 ? 4.187   44.453  143.284 1.00 41.70  ? 319 ALA A C   1 
ATOM 2181 O O   . ALA A 1 273 ? 3.617   43.735  142.459 1.00 44.91  ? 319 ALA A O   1 
ATOM 2182 C CB  . ALA A 1 273 ? 6.278   45.671  142.655 1.00 40.62  ? 319 ALA A CB  1 
ATOM 2183 N N   . VAL A 1 274 ? 3.531   45.261  144.116 1.00 37.51  ? 320 VAL A N   1 
ATOM 2184 C CA  . VAL A 1 274 ? 2.080   45.336  144.152 1.00 35.10  ? 320 VAL A CA  1 
ATOM 2185 C C   . VAL A 1 274 ? 1.677   46.788  143.932 1.00 37.87  ? 320 VAL A C   1 
ATOM 2186 O O   . VAL A 1 274 ? 2.449   47.717  144.178 1.00 37.38  ? 320 VAL A O   1 
ATOM 2187 C CB  . VAL A 1 274 ? 1.505   44.799  145.482 1.00 31.00  ? 320 VAL A CB  1 
ATOM 2188 C CG1 . VAL A 1 274 ? 1.554   45.863  146.565 1.00 33.49  ? 320 VAL A CG1 1 
ATOM 2189 C CG2 . VAL A 1 274 ? 0.101   44.271  145.292 1.00 36.05  ? 320 VAL A CG2 1 
ATOM 2190 N N   . ASP A 1 275 ? 0.455   46.976  143.443 1.00 39.08  ? 321 ASP A N   1 
ATOM 2191 C CA  . ASP A 1 275 ? -0.060  48.307  143.146 1.00 40.50  ? 321 ASP A CA  1 
ATOM 2192 C C   . ASP A 1 275 ? -1.540  48.356  143.515 1.00 41.78  ? 321 ASP A C   1 
ATOM 2193 O O   . ASP A 1 275 ? -2.079  47.433  144.132 1.00 46.77  ? 321 ASP A O   1 
ATOM 2194 C CB  . ASP A 1 275 ? 0.220   48.678  141.682 1.00 40.90  ? 321 ASP A CB  1 
ATOM 2195 C CG  . ASP A 1 275 ? -0.420  47.721  140.691 1.00 47.89  ? 321 ASP A CG  1 
ATOM 2196 O OD1 . ASP A 1 275 ? -1.463  47.113  141.003 1.00 49.55  ? 321 ASP A OD1 1 
ATOM 2197 O OD2 . ASP A 1 275 ? 0.129   47.579  139.579 1.00 49.68  ? 321 ASP A OD2 1 
ATOM 2198 N N   . SER A 1 276 ? -2.200  49.451  143.135 1.00 34.65  ? 322 SER A N   1 
ATOM 2199 C CA  . SER A 1 276 ? -3.587  49.673  143.519 1.00 37.57  ? 322 SER A CA  1 
ATOM 2200 C C   . SER A 1 276 ? -4.573  48.819  142.733 1.00 43.51  ? 322 SER A C   1 
ATOM 2201 O O   . SER A 1 276 ? -5.686  48.587  143.215 1.00 47.55  ? 322 SER A O   1 
ATOM 2202 C CB  . SER A 1 276 ? -3.949  51.149  143.349 1.00 39.99  ? 322 SER A CB  1 
ATOM 2203 O OG  . SER A 1 276 ? -4.116  51.478  141.982 1.00 43.28  ? 322 SER A OG  1 
ATOM 2204 N N   . THR A 1 277 ? -4.202  48.351  141.541 1.00 42.51  ? 323 THR A N   1 
ATOM 2205 C CA  . THR A 1 277 ? -5.106  47.589  140.688 1.00 42.36  ? 323 THR A CA  1 
ATOM 2206 C C   . THR A 1 277 ? -4.873  46.086  140.787 1.00 46.45  ? 323 THR A C   1 
ATOM 2207 O O   . THR A 1 277 ? -5.241  45.340  139.874 1.00 48.67  ? 323 THR A O   1 
ATOM 2208 C CB  . THR A 1 277 ? -4.984  48.048  139.235 1.00 42.18  ? 323 THR A CB  1 
ATOM 2209 O OG1 . THR A 1 277 ? -5.671  47.124  138.383 1.00 50.35  ? 323 THR A OG1 1 
ATOM 2210 C CG2 . THR A 1 277 ? -3.527  48.123  138.817 1.00 40.50  ? 323 THR A CG2 1 
ATOM 2211 N N   . THR A 1 278 ? -4.268  45.624  141.877 1.00 46.84  ? 324 THR A N   1 
ATOM 2212 C CA  . THR A 1 278 ? -4.031  44.204  142.101 1.00 44.64  ? 324 THR A CA  1 
ATOM 2213 C C   . THR A 1 278 ? -5.178  43.638  142.926 1.00 46.01  ? 324 THR A C   1 
ATOM 2214 O O   . THR A 1 278 ? -5.428  44.097  144.045 1.00 42.46  ? 324 THR A O   1 
ATOM 2215 C CB  . THR A 1 278 ? -2.703  43.970  142.814 1.00 40.71  ? 324 THR A CB  1 
ATOM 2216 O OG1 . THR A 1 278 ? -2.479  45.032  143.748 1.00 45.53  ? 324 THR A OG1 1 
ATOM 2217 C CG2 . THR A 1 278 ? -1.566  43.918  141.812 1.00 41.90  ? 324 THR A CG2 1 
ATOM 2218 N N   . MET A 1 279 ? -5.862  42.642  142.376 1.00 51.30  ? 325 MET A N   1 
ATOM 2219 C CA  . MET A 1 279 ? -7.061  42.085  142.979 1.00 46.92  ? 325 MET A CA  1 
ATOM 2220 C C   . MET A 1 279 ? -6.806  40.640  143.379 1.00 48.31  ? 325 MET A C   1 
ATOM 2221 O O   . MET A 1 279 ? -6.417  39.822  142.540 1.00 54.73  ? 325 MET A O   1 
ATOM 2222 C CB  . MET A 1 279 ? -8.235  42.160  142.001 1.00 49.54  ? 325 MET A CB  1 
ATOM 2223 C CG  . MET A 1 279 ? -9.134  43.364  142.194 1.00 55.49  ? 325 MET A CG  1 
ATOM 2224 S SD  . MET A 1 279 ? -9.653  43.600  143.898 1.00 66.06  ? 325 MET A SD  1 
ATOM 2225 C CE  . MET A 1 279 ? -9.673  45.386  143.964 1.00 44.81  ? 325 MET A CE  1 
ATOM 2226 N N   . THR A 1 280 ? -7.010  40.330  144.654 1.00 43.63  ? 326 THR A N   1 
ATOM 2227 C CA  . THR A 1 280 ? -7.005  38.945  145.098 1.00 45.98  ? 326 THR A CA  1 
ATOM 2228 C C   . THR A 1 280 ? -8.413  38.370  144.986 1.00 44.72  ? 326 THR A C   1 
ATOM 2229 O O   . THR A 1 280 ? -9.407  39.035  145.283 1.00 43.71  ? 326 THR A O   1 
ATOM 2230 C CB  . THR A 1 280 ? -6.481  38.835  146.534 1.00 43.53  ? 326 THR A CB  1 
ATOM 2231 O OG1 . THR A 1 280 ? -5.065  39.059  146.542 1.00 42.10  ? 326 THR A OG1 1 
ATOM 2232 C CG2 . THR A 1 280 ? -6.775  37.465  147.136 1.00 39.48  ? 326 THR A CG2 1 
ATOM 2233 N N   . LEU A 1 281 ? -8.484  37.105  144.569 1.00 39.43  ? 327 LEU A N   1 
ATOM 2234 C CA  . LEU A 1 281 ? -9.737  36.468  144.217 1.00 37.44  ? 327 LEU A CA  1 
ATOM 2235 C C   . LEU A 1 281 ? -9.747  35.066  144.799 1.00 40.45  ? 327 LEU A C   1 
ATOM 2236 O O   . LEU A 1 281 ? -8.782  34.316  144.596 1.00 45.22  ? 327 LEU A O   1 
ATOM 2237 C CB  . LEU A 1 281 ? -9.926  36.398  142.698 1.00 38.71  ? 327 LEU A CB  1 
ATOM 2238 C CG  . LEU A 1 281 ? -10.905 37.376  142.050 1.00 46.46  ? 327 LEU A CG  1 
ATOM 2239 C CD1 . LEU A 1 281 ? -11.374 36.840  140.705 1.00 46.67  ? 327 LEU A CD1 1 
ATOM 2240 C CD2 . LEU A 1 281 ? -12.086 37.627  142.972 1.00 42.07  ? 327 LEU A CD2 1 
ATOM 2241 N N   . PRO A 1 282 ? -10.794 34.691  145.529 1.00 30.56  ? 328 PRO A N   1 
ATOM 2242 C CA  . PRO A 1 282 ? -10.888 33.315  146.021 1.00 29.51  ? 328 PRO A CA  1 
ATOM 2243 C C   . PRO A 1 282 ? -10.916 32.322  144.874 1.00 31.79  ? 328 PRO A C   1 
ATOM 2244 O O   . PRO A 1 282 ? -11.513 32.565  143.822 1.00 36.48  ? 328 PRO A O   1 
ATOM 2245 C CB  . PRO A 1 282 ? -12.205 33.305  146.804 1.00 26.35  ? 328 PRO A CB  1 
ATOM 2246 C CG  . PRO A 1 282 ? -12.453 34.732  147.142 1.00 27.75  ? 328 PRO A CG  1 
ATOM 2247 C CD  . PRO A 1 282 ? -11.913 35.523  145.998 1.00 29.29  ? 328 PRO A CD  1 
ATOM 2248 N N   . THR A 1 283 ? -10.249 31.191  145.086 1.00 30.52  ? 329 THR A N   1 
ATOM 2249 C CA  . THR A 1 283 ? -10.116 30.170  144.058 1.00 31.82  ? 329 THR A CA  1 
ATOM 2250 C C   . THR A 1 283 ? -10.410 28.805  144.660 1.00 35.86  ? 329 THR A C   1 
ATOM 2251 O O   . THR A 1 283 ? -10.263 28.587  145.864 1.00 41.68  ? 329 THR A O   1 
ATOM 2252 C CB  . THR A 1 283 ? -8.716  30.168  143.429 1.00 34.49  ? 329 THR A CB  1 
ATOM 2253 O OG1 . THR A 1 283 ? -7.726  30.068  144.459 1.00 32.45  ? 329 THR A OG1 1 
ATOM 2254 C CG2 . THR A 1 283 ? -8.482  31.441  142.630 1.00 35.60  ? 329 THR A CG2 1 
ATOM 2255 N N   . TYR A 1 284 ? -10.831 27.883  143.799 1.00 33.92  ? 330 TYR A N   1 
ATOM 2256 C CA  . TYR A 1 284 ? -11.113 26.509  144.189 1.00 33.61  ? 330 TYR A CA  1 
ATOM 2257 C C   . TYR A 1 284 ? -9.871  25.661  143.946 1.00 40.33  ? 330 TYR A C   1 
ATOM 2258 O O   . TYR A 1 284 ? -9.400  25.556  142.809 1.00 37.93  ? 330 TYR A O   1 
ATOM 2259 C CB  . TYR A 1 284 ? -12.306 25.958  143.408 1.00 33.82  ? 330 TYR A CB  1 
ATOM 2260 C CG  . TYR A 1 284 ? -12.690 24.547  143.785 1.00 36.82  ? 330 TYR A CG  1 
ATOM 2261 C CD1 . TYR A 1 284 ? -13.430 24.292  144.930 1.00 39.22  ? 330 TYR A CD1 1 
ATOM 2262 C CD2 . TYR A 1 284 ? -12.319 23.472  142.993 1.00 40.63  ? 330 TYR A CD2 1 
ATOM 2263 C CE1 . TYR A 1 284 ? -13.785 23.007  145.276 1.00 44.86  ? 330 TYR A CE1 1 
ATOM 2264 C CE2 . TYR A 1 284 ? -12.669 22.182  143.333 1.00 38.50  ? 330 TYR A CE2 1 
ATOM 2265 C CZ  . TYR A 1 284 ? -13.403 21.956  144.476 1.00 43.34  ? 330 TYR A CZ  1 
ATOM 2266 O OH  . TYR A 1 284 ? -13.756 20.674  144.823 1.00 42.46  ? 330 TYR A OH  1 
ATOM 2267 N N   . ASP A 1 285 ? -9.344  25.063  145.013 1.00 40.82  ? 331 ASP A N   1 
ATOM 2268 C CA  . ASP A 1 285 ? -8.154  24.230  144.908 1.00 36.50  ? 331 ASP A CA  1 
ATOM 2269 C C   . ASP A 1 285 ? -8.361  22.906  145.636 1.00 38.82  ? 331 ASP A C   1 
ATOM 2270 O O   . ASP A 1 285 ? -8.262  22.845  146.870 1.00 44.10  ? 331 ASP A O   1 
ATOM 2271 C CB  . ASP A 1 285 ? -6.935  24.964  145.463 1.00 34.09  ? 331 ASP A CB  1 
ATOM 2272 C CG  . ASP A 1 285 ? -5.639  24.479  144.853 1.00 40.85  ? 331 ASP A CG  1 
ATOM 2273 O OD1 . ASP A 1 285 ? -5.686  23.564  144.006 1.00 43.96  ? 331 ASP A OD1 1 
ATOM 2274 O OD2 . ASP A 1 285 ? -4.572  25.012  145.220 1.00 43.07  ? 331 ASP A OD2 1 
ATOM 2275 N N   . PRO A 1 286 ? -8.655  21.829  144.904 1.00 33.09  ? 332 PRO A N   1 
ATOM 2276 C CA  . PRO A 1 286 ? -8.884  20.534  145.560 1.00 32.35  ? 332 PRO A CA  1 
ATOM 2277 C C   . PRO A 1 286 ? -7.685  20.017  146.332 1.00 34.92  ? 332 PRO A C   1 
ATOM 2278 O O   . PRO A 1 286 ? -7.877  19.344  147.349 1.00 38.09  ? 332 PRO A O   1 
ATOM 2279 C CB  . PRO A 1 286 ? -9.243  19.599  144.395 1.00 35.68  ? 332 PRO A CB  1 
ATOM 2280 C CG  . PRO A 1 286 ? -9.516  20.495  143.225 1.00 35.93  ? 332 PRO A CG  1 
ATOM 2281 C CD  . PRO A 1 286 ? -8.713  21.729  143.438 1.00 33.93  ? 332 PRO A CD  1 
ATOM 2282 N N   . LEU A 1 287 ? -6.460  20.304  145.890 1.00 34.84  ? 333 LEU A N   1 
ATOM 2283 C CA  . LEU A 1 287 ? -5.287  19.827  146.616 1.00 34.86  ? 333 LEU A CA  1 
ATOM 2284 C C   . LEU A 1 287 ? -5.201  20.464  147.997 1.00 34.62  ? 333 LEU A C   1 
ATOM 2285 O O   . LEU A 1 287 ? -5.002  19.770  149.005 1.00 40.82  ? 333 LEU A O   1 
ATOM 2286 C CB  . LEU A 1 287 ? -4.021  20.114  145.810 1.00 33.72  ? 333 LEU A CB  1 
ATOM 2287 C CG  . LEU A 1 287 ? -3.735  19.172  144.639 1.00 35.13  ? 333 LEU A CG  1 
ATOM 2288 C CD1 . LEU A 1 287 ? -2.311  19.356  144.142 1.00 35.30  ? 333 LEU A CD1 1 
ATOM 2289 C CD2 . LEU A 1 287 ? -3.987  17.728  145.033 1.00 31.59  ? 333 LEU A CD2 1 
ATOM 2290 N N   . ILE A 1 288 ? -5.348  21.790  148.064 1.00 26.73  ? 334 ILE A N   1 
ATOM 2291 C CA  . ILE A 1 288 ? -5.301  22.453  149.359 1.00 24.46  ? 334 ILE A CA  1 
ATOM 2292 C C   . ILE A 1 288 ? -6.503  22.045  150.195 1.00 29.45  ? 334 ILE A C   1 
ATOM 2293 O O   . ILE A 1 288 ? -6.398  21.928  151.420 1.00 37.19  ? 334 ILE A O   1 
ATOM 2294 C CB  . ILE A 1 288 ? -5.197  23.983  149.199 1.00 24.21  ? 334 ILE A CB  1 
ATOM 2295 C CG1 . ILE A 1 288 ? -4.648  24.615  150.475 1.00 32.70  ? 334 ILE A CG1 1 
ATOM 2296 C CG2 . ILE A 1 288 ? -6.544  24.602  148.916 1.00 34.04  ? 334 ILE A CG2 1 
ATOM 2297 C CD1 . ILE A 1 288 ? -3.143  24.570  150.577 1.00 32.43  ? 334 ILE A CD1 1 
ATOM 2298 N N   . LEU A 1 289 ? -7.649  21.785  149.558 1.00 31.01  ? 335 LEU A N   1 
ATOM 2299 C CA  . LEU A 1 289 ? -8.807  21.308  150.308 1.00 30.45  ? 335 LEU A CA  1 
ATOM 2300 C C   . LEU A 1 289 ? -8.524  19.961  150.960 1.00 28.74  ? 335 LEU A C   1 
ATOM 2301 O O   . LEU A 1 289 ? -8.829  19.755  152.140 1.00 32.44  ? 335 LEU A O   1 
ATOM 2302 C CB  . LEU A 1 289 ? -10.022 21.208  149.390 1.00 26.79  ? 335 LEU A CB  1 
ATOM 2303 C CG  . LEU A 1 289 ? -10.772 22.512  149.130 1.00 33.49  ? 335 LEU A CG  1 
ATOM 2304 C CD1 . LEU A 1 289 ? -11.946 22.268  148.203 1.00 31.05  ? 335 LEU A CD1 1 
ATOM 2305 C CD2 . LEU A 1 289 ? -11.230 23.128  150.437 1.00 33.14  ? 335 LEU A CD2 1 
ATOM 2306 N N   . ALA A 1 290 ? -7.928  19.035  150.207 1.00 29.54  ? 336 ALA A N   1 
ATOM 2307 C CA  . ALA A 1 290 ? -7.624  17.717  150.750 1.00 28.37  ? 336 ALA A CA  1 
ATOM 2308 C C   . ALA A 1 290 ? -6.603  17.802  151.875 1.00 24.24  ? 336 ALA A C   1 
ATOM 2309 O O   . ALA A 1 290 ? -6.774  17.169  152.926 1.00 31.41  ? 336 ALA A O   1 
ATOM 2310 C CB  . ALA A 1 290 ? -7.121  16.796  149.640 1.00 27.77  ? 336 ALA A CB  1 
ATOM 2311 N N   . GLN A 1 291 ? -5.538  18.583  151.683 1.00 27.38  ? 337 GLN A N   1 
ATOM 2312 C CA  . GLN A 1 291 ? -4.526  18.677  152.727 1.00 28.34  ? 337 GLN A CA  1 
ATOM 2313 C C   . GLN A 1 291 ? -5.016  19.443  153.948 1.00 28.07  ? 337 GLN A C   1 
ATOM 2314 O O   . GLN A 1 291 ? -4.490  19.228  155.044 1.00 30.17  ? 337 GLN A O   1 
ATOM 2315 C CB  . GLN A 1 291 ? -3.247  19.309  152.180 1.00 20.18  ? 337 GLN A CB  1 
ATOM 2316 C CG  . GLN A 1 291 ? -3.297  20.798  151.974 1.00 22.60  ? 337 GLN A CG  1 
ATOM 2317 C CD  . GLN A 1 291 ? -2.010  21.325  151.386 1.00 31.49  ? 337 GLN A CD  1 
ATOM 2318 O OE1 . GLN A 1 291 ? -1.214  21.962  152.074 1.00 36.69  ? 337 GLN A OE1 1 
ATOM 2319 N NE2 . GLN A 1 291 ? -1.789  21.050  150.107 1.00 33.98  ? 337 GLN A NE2 1 
ATOM 2320 N N   . ILE A 1 292 ? -6.004  20.326  153.789 1.00 23.86  ? 338 ILE A N   1 
ATOM 2321 C CA  . ILE A 1 292 ? -6.662  20.921  154.946 1.00 19.22  ? 338 ILE A CA  1 
ATOM 2322 C C   . ILE A 1 292 ? -7.513  19.879  155.657 1.00 23.18  ? 338 ILE A C   1 
ATOM 2323 O O   . ILE A 1 292 ? -7.550  19.821  156.892 1.00 30.23  ? 338 ILE A O   1 
ATOM 2324 C CB  . ILE A 1 292 ? -7.500  22.137  154.512 1.00 24.78  ? 338 ILE A CB  1 
ATOM 2325 C CG1 . ILE A 1 292 ? -6.601  23.346  154.267 1.00 31.31  ? 338 ILE A CG1 1 
ATOM 2326 C CG2 . ILE A 1 292 ? -8.540  22.474  155.562 1.00 21.02  ? 338 ILE A CG2 1 
ATOM 2327 C CD1 . ILE A 1 292 ? -7.309  24.500  153.601 1.00 23.34  ? 338 ILE A CD1 1 
ATOM 2328 N N   . HIS A 1 293 ? -8.205  19.038  154.888 1.00 29.31  ? 339 HIS A N   1 
ATOM 2329 C CA  . HIS A 1 293 ? -9.063  18.017  155.478 1.00 25.71  ? 339 HIS A CA  1 
ATOM 2330 C C   . HIS A 1 293 ? -8.254  17.013  156.287 1.00 28.17  ? 339 HIS A C   1 
ATOM 2331 O O   . HIS A 1 293 ? -8.706  16.547  157.338 1.00 31.26  ? 339 HIS A O   1 
ATOM 2332 C CB  . HIS A 1 293 ? -9.855  17.310  154.382 1.00 28.39  ? 339 HIS A CB  1 
ATOM 2333 C CG  . HIS A 1 293 ? -10.723 16.199  154.881 1.00 34.25  ? 339 HIS A CG  1 
ATOM 2334 N ND1 . HIS A 1 293 ? -11.401 16.265  156.079 1.00 40.42  ? 339 HIS A ND1 1 
ATOM 2335 C CD2 . HIS A 1 293 ? -11.032 14.999  154.339 1.00 33.87  ? 339 HIS A CD2 1 
ATOM 2336 C CE1 . HIS A 1 293 ? -12.087 15.150  156.256 1.00 29.56  ? 339 HIS A CE1 1 
ATOM 2337 N NE2 . HIS A 1 293 ? -11.880 14.366  155.214 1.00 29.36  ? 339 HIS A NE2 1 
ATOM 2338 N N   . SER A 1 294 ? -7.054  16.674  155.819 1.00 35.03  ? 340 SER A N   1 
ATOM 2339 C CA  . SER A 1 294 ? -6.201  15.706  156.498 1.00 23.93  ? 340 SER A CA  1 
ATOM 2340 C C   . SER A 1 294 ? -5.182  16.373  157.416 1.00 20.03  ? 340 SER A C   1 
ATOM 2341 O O   . SER A 1 294 ? -4.067  15.869  157.573 1.00 29.49  ? 340 SER A O   1 
ATOM 2342 C CB  . SER A 1 294 ? -5.491  14.819  155.477 1.00 24.80  ? 340 SER A CB  1 
ATOM 2343 O OG  . SER A 1 294 ? -6.417  14.244  154.573 1.00 33.34  ? 340 SER A OG  1 
ATOM 2344 N N   . ALA A 1 295 ? -5.544  17.497  158.024 1.00 22.65  ? 341 ALA A N   1 
ATOM 2345 C CA  . ALA A 1 295 ? -4.647  18.247  158.890 1.00 18.57  ? 341 ALA A CA  1 
ATOM 2346 C C   . ALA A 1 295 ? -4.926  17.933  160.353 1.00 22.98  ? 341 ALA A C   1 
ATOM 2347 O O   . ALA A 1 295 ? -6.075  17.748  160.761 1.00 29.25  ? 341 ALA A O   1 
ATOM 2348 C CB  . ALA A 1 295 ? -4.788  19.750  158.649 1.00 22.01  ? 341 ALA A CB  1 
ATOM 2349 N N   . ARG A 1 296 ? -3.857  17.878  161.143 1.00 24.75  ? 342 ARG A N   1 
ATOM 2350 C CA  . ARG A 1 296 ? -3.949  17.613  162.572 1.00 28.28  ? 342 ARG A CA  1 
ATOM 2351 C C   . ARG A 1 296 ? -3.254  18.729  163.333 1.00 26.15  ? 342 ARG A C   1 
ATOM 2352 O O   . ARG A 1 296 ? -2.108  19.072  163.028 1.00 25.91  ? 342 ARG A O   1 
ATOM 2353 C CB  . ARG A 1 296 ? -3.327  16.258  162.921 1.00 26.30  ? 342 ARG A CB  1 
ATOM 2354 C CG  . ARG A 1 296 ? -4.067  15.077  162.319 1.00 30.35  ? 342 ARG A CG  1 
ATOM 2355 C CD  . ARG A 1 296 ? -3.275  13.792  162.466 1.00 30.63  ? 342 ARG A CD  1 
ATOM 2356 N NE  . ARG A 1 296 ? -3.245  13.324  163.845 1.00 32.83  ? 342 ARG A NE  1 
ATOM 2357 C CZ  . ARG A 1 296 ? -4.186  12.574  164.400 1.00 31.40  ? 342 ARG A CZ  1 
ATOM 2358 N NH1 . ARG A 1 296 ? -5.257  12.198  163.724 1.00 30.00  ? 342 ARG A NH1 1 
ATOM 2359 N NH2 . ARG A 1 296 ? -4.050  12.195  165.667 1.00 29.93  ? 342 ARG A NH2 1 
ATOM 2360 N N   . ALA A 1 297 ? -3.947  19.292  164.318 1.00 28.85  ? 343 ALA A N   1 
ATOM 2361 C CA  . ALA A 1 297 ? -3.395  20.380  165.111 1.00 23.47  ? 343 ALA A CA  1 
ATOM 2362 C C   . ALA A 1 297 ? -2.358  19.856  166.094 1.00 31.84  ? 343 ALA A C   1 
ATOM 2363 O O   . ALA A 1 297 ? -2.504  18.764  166.650 1.00 37.72  ? 343 ALA A O   1 
ATOM 2364 C CB  . ALA A 1 297 ? -4.506  21.112  165.861 1.00 21.52  ? 343 ALA A CB  1 
ATOM 2365 N N   . VAL A 1 298 ? -1.306  20.645  166.309 1.00 26.52  ? 344 VAL A N   1 
ATOM 2366 C CA  . VAL A 1 298 ? -0.217  20.260  167.201 1.00 23.58  ? 344 VAL A CA  1 
ATOM 2367 C C   . VAL A 1 298 ? -0.168  21.087  168.474 1.00 30.66  ? 344 VAL A C   1 
ATOM 2368 O O   . VAL A 1 298 ? 0.563   20.714  169.405 1.00 38.38  ? 344 VAL A O   1 
ATOM 2369 C CB  . VAL A 1 298 ? 1.148   20.327  166.486 1.00 29.26  ? 344 VAL A CB  1 
ATOM 2370 C CG1 . VAL A 1 298 ? 1.073   19.633  165.139 1.00 29.78  ? 344 VAL A CG1 1 
ATOM 2371 C CG2 . VAL A 1 298 ? 1.591   21.769  166.325 1.00 32.78  ? 344 VAL A CG2 1 
ATOM 2372 N N   . GLY A 1 299 ? -0.910  22.185  168.555 1.00 32.38  ? 345 GLY A N   1 
ATOM 2373 C CA  . GLY A 1 299 ? -0.914  23.026  169.733 1.00 34.23  ? 345 GLY A CA  1 
ATOM 2374 C C   . GLY A 1 299 ? -0.071  24.278  169.556 1.00 31.70  ? 345 GLY A C   1 
ATOM 2375 O O   . GLY A 1 299 ? 0.610   24.481  168.549 1.00 31.82  ? 345 GLY A O   1 
ATOM 2376 N N   . ALA A 1 300 ? -0.130  25.131  170.573 1.00 43.76  ? 346 ALA A N   1 
ATOM 2377 C CA  . ALA A 1 300 ? 0.548   26.414  170.513 1.00 45.62  ? 346 ALA A CA  1 
ATOM 2378 C C   . ALA A 1 300 ? 2.059   26.239  170.655 1.00 43.70  ? 346 ALA A C   1 
ATOM 2379 O O   . ALA A 1 300 ? 2.525   25.320  171.333 1.00 41.13  ? 346 ALA A O   1 
ATOM 2380 C CB  . ALA A 1 300 ? 0.030   27.342  171.608 1.00 43.43  ? 346 ALA A CB  1 
ATOM 2381 N N   . PRO A 1 301 ? 2.845   27.107  170.021 1.00 44.86  ? 347 PRO A N   1 
ATOM 2382 C CA  . PRO A 1 301 ? 4.299   27.049  170.197 1.00 44.37  ? 347 PRO A CA  1 
ATOM 2383 C C   . PRO A 1 301 ? 4.699   27.363  171.629 1.00 44.15  ? 347 PRO A C   1 
ATOM 2384 O O   . PRO A 1 301 ? 4.024   28.112  172.338 1.00 49.62  ? 347 PRO A O   1 
ATOM 2385 C CB  . PRO A 1 301 ? 4.819   28.119  169.231 1.00 37.26  ? 347 PRO A CB  1 
ATOM 2386 C CG  . PRO A 1 301 ? 3.717   28.327  168.255 1.00 40.30  ? 347 PRO A CG  1 
ATOM 2387 C CD  . PRO A 1 301 ? 2.452   28.113  169.021 1.00 39.41  ? 347 PRO A CD  1 
ATOM 2388 N N   . ILE A 1 302 ? 5.814   26.774  172.050 1.00 38.91  ? 348 ILE A N   1 
ATOM 2389 C CA  . ILE A 1 302 ? 6.352   26.974  173.390 1.00 39.84  ? 348 ILE A CA  1 
ATOM 2390 C C   . ILE A 1 302 ? 7.458   28.014  173.316 1.00 44.67  ? 348 ILE A C   1 
ATOM 2391 O O   . ILE A 1 302 ? 8.425   27.853  172.561 1.00 49.16  ? 348 ILE A O   1 
ATOM 2392 C CB  . ILE A 1 302 ? 6.878   25.659  173.987 1.00 38.27  ? 348 ILE A CB  1 
ATOM 2393 C CG1 . ILE A 1 302 ? 5.915   24.512  173.693 1.00 40.30  ? 348 ILE A CG1 1 
ATOM 2394 C CG2 . ILE A 1 302 ? 7.082   25.801  175.484 1.00 40.16  ? 348 ILE A CG2 1 
ATOM 2395 C CD1 . ILE A 1 302 ? 6.477   23.158  174.038 1.00 41.49  ? 348 ILE A CD1 1 
ATOM 2396 N N   . LEU A 1 303 ? 7.320   29.076  174.098 1.00 53.67  ? 349 LEU A N   1 
ATOM 2397 C CA  . LEU A 1 303 ? 8.282   30.165  174.135 1.00 52.22  ? 349 LEU A CA  1 
ATOM 2398 C C   . LEU A 1 303 ? 9.044   30.143  175.453 1.00 49.48  ? 349 LEU A C   1 
ATOM 2399 O O   . LEU A 1 303 ? 8.728   29.384  176.373 1.00 50.98  ? 349 LEU A O   1 
ATOM 2400 C CB  . LEU A 1 303 ? 7.579   31.513  173.945 1.00 52.42  ? 349 LEU A CB  1 
ATOM 2401 C CG  . LEU A 1 303 ? 6.393   31.529  172.979 1.00 50.39  ? 349 LEU A CG  1 
ATOM 2402 C CD1 . LEU A 1 303 ? 5.529   32.752  173.221 1.00 50.40  ? 349 LEU A CD1 1 
ATOM 2403 C CD2 . LEU A 1 303 ? 6.870   31.493  171.541 1.00 49.91  ? 349 LEU A CD2 1 
ATOM 2404 N N   . GLU A 1 304 ? 10.070  30.993  175.532 1.00 58.31  ? 350 GLU A N   1 
ATOM 2405 C CA  . GLU A 1 304 ? 10.843  31.103  176.765 1.00 62.06  ? 350 GLU A CA  1 
ATOM 2406 C C   . GLU A 1 304 ? 9.987   31.633  177.907 1.00 60.55  ? 350 GLU A C   1 
ATOM 2407 O O   . GLU A 1 304 ? 10.116  31.180  179.050 1.00 61.63  ? 350 GLU A O   1 
ATOM 2408 C CB  . GLU A 1 304 ? 12.063  32.001  176.553 1.00 61.73  ? 350 GLU A CB  1 
ATOM 2409 C CG  . GLU A 1 304 ? 13.157  31.426  175.656 1.00 63.58  ? 350 GLU A CG  1 
ATOM 2410 C CD  . GLU A 1 304 ? 12.729  31.260  174.210 1.00 70.68  ? 350 GLU A CD  1 
ATOM 2411 O OE1 . GLU A 1 304 ? 11.770  31.939  173.788 1.00 69.27  ? 350 GLU A OE1 1 
ATOM 2412 O OE2 . GLU A 1 304 ? 13.357  30.453  173.494 1.00 68.22  ? 350 GLU A OE2 1 
ATOM 2413 N N   . THR A 1 305 ? 9.110   32.594  177.619 1.00 59.25  ? 351 THR A N   1 
ATOM 2414 C CA  . THR A 1 305 ? 8.257   33.182  178.643 1.00 61.24  ? 351 THR A CA  1 
ATOM 2415 C C   . THR A 1 305 ? 7.131   32.259  179.086 1.00 62.64  ? 351 THR A C   1 
ATOM 2416 O O   . THR A 1 305 ? 6.515   32.518  180.125 1.00 65.49  ? 351 THR A O   1 
ATOM 2417 C CB  . THR A 1 305 ? 7.662   34.498  178.140 1.00 63.59  ? 351 THR A CB  1 
ATOM 2418 O OG1 . THR A 1 305 ? 6.864   34.250  176.976 1.00 61.00  ? 351 THR A OG1 1 
ATOM 2419 C CG2 . THR A 1 305 ? 8.768   35.480  177.791 1.00 63.47  ? 351 THR A CG2 1 
ATOM 2420 N N   . SER A 1 306 ? 6.847   31.199  178.334 1.00 64.62  ? 352 SER A N   1 
ATOM 2421 C CA  . SER A 1 306 ? 5.769   30.283  178.681 1.00 63.53  ? 352 SER A CA  1 
ATOM 2422 C C   . SER A 1 306 ? 6.221   29.370  179.812 1.00 61.67  ? 352 SER A C   1 
ATOM 2423 O O   . SER A 1 306 ? 7.206   28.638  179.671 1.00 59.44  ? 352 SER A O   1 
ATOM 2424 C CB  . SER A 1 306 ? 5.355   29.467  177.460 1.00 60.02  ? 352 SER A CB  1 
ATOM 2425 O OG  . SER A 1 306 ? 6.459   28.758  176.929 1.00 63.26  ? 352 SER A OG  1 
ATOM 2426 N N   . THR A 1 307 ? 5.504   29.412  180.931 1.00 65.13  ? 353 THR A N   1 
ATOM 2427 C CA  . THR A 1 307 ? 5.837   28.575  182.074 1.00 66.99  ? 353 THR A CA  1 
ATOM 2428 C C   . THR A 1 307 ? 5.233   27.187  181.910 1.00 65.57  ? 353 THR A C   1 
ATOM 2429 O O   . THR A 1 307 ? 4.067   27.038  181.534 1.00 65.09  ? 353 THR A O   1 
ATOM 2430 C CB  . THR A 1 307 ? 5.341   29.213  183.373 1.00 67.13  ? 353 THR A CB  1 
ATOM 2431 O OG1 . THR A 1 307 ? 5.365   28.240  184.425 1.00 69.30  ? 353 THR A OG1 1 
ATOM 2432 C CG2 . THR A 1 307 ? 3.926   29.745  183.207 1.00 66.42  ? 353 THR A CG2 1 
ATOM 2433 N N   . LEU A 1 308 ? 6.041   26.167  182.190 1.00 60.34  ? 354 LEU A N   1 
ATOM 2434 C CA  . LEU A 1 308 ? 5.610   24.779  182.046 1.00 58.57  ? 354 LEU A CA  1 
ATOM 2435 C C   . LEU A 1 308 ? 6.177   23.996  183.220 1.00 60.77  ? 354 LEU A C   1 
ATOM 2436 O O   . LEU A 1 308 ? 7.397   23.847  183.333 1.00 63.52  ? 354 LEU A O   1 
ATOM 2437 C CB  . LEU A 1 308 ? 6.077   24.195  180.716 1.00 58.41  ? 354 LEU A CB  1 
ATOM 2438 C CG  . LEU A 1 308 ? 5.171   24.455  179.513 1.00 58.20  ? 354 LEU A CG  1 
ATOM 2439 C CD1 . LEU A 1 308 ? 5.629   23.648  178.311 1.00 55.29  ? 354 LEU A CD1 1 
ATOM 2440 C CD2 . LEU A 1 308 ? 3.727   24.140  179.854 1.00 61.17  ? 354 LEU A CD2 1 
ATOM 2441 N N   . THR A 1 309 ? 5.299   23.499  184.086 1.00 63.44  ? 355 THR A N   1 
ATOM 2442 C CA  . THR A 1 309 ? 5.721   22.799  185.294 1.00 63.83  ? 355 THR A CA  1 
ATOM 2443 C C   . THR A 1 309 ? 6.267   21.428  184.913 1.00 63.22  ? 355 THR A C   1 
ATOM 2444 O O   . THR A 1 309 ? 5.538   20.587  184.380 1.00 66.60  ? 355 THR A O   1 
ATOM 2445 C CB  . THR A 1 309 ? 4.558   22.672  186.272 1.00 66.34  ? 355 THR A CB  1 
ATOM 2446 O OG1 . THR A 1 309 ? 3.879   23.929  186.373 1.00 64.85  ? 355 THR A OG1 1 
ATOM 2447 C CG2 . THR A 1 309 ? 5.063   22.264  187.646 1.00 63.75  ? 355 THR A CG2 1 
ATOM 2448 N N   . GLY A 1 310 ? 7.548   21.201  185.189 1.00 56.23  ? 356 GLY A N   1 
ATOM 2449 C CA  . GLY A 1 310 ? 8.184   19.932  184.909 1.00 55.78  ? 356 GLY A CA  1 
ATOM 2450 C C   . GLY A 1 310 ? 8.793   19.799  183.532 1.00 55.79  ? 356 GLY A C   1 
ATOM 2451 O O   . GLY A 1 310 ? 9.426   18.774  183.254 1.00 59.44  ? 356 GLY A O   1 
ATOM 2452 N N   . PHE A 1 311 ? 8.632   20.796  182.665 1.00 53.91  ? 357 PHE A N   1 
ATOM 2453 C CA  . PHE A 1 311 ? 9.176   20.768  181.308 1.00 53.60  ? 357 PHE A CA  1 
ATOM 2454 C C   . PHE A 1 311 ? 9.990   22.034  181.083 1.00 55.43  ? 357 PHE A C   1 
ATOM 2455 O O   . PHE A 1 311 ? 9.547   22.957  180.386 1.00 54.89  ? 357 PHE A O   1 
ATOM 2456 C CB  . PHE A 1 311 ? 8.064   20.647  180.266 1.00 51.92  ? 357 PHE A CB  1 
ATOM 2457 C CG  . PHE A 1 311 ? 7.388   19.309  180.249 1.00 50.29  ? 357 PHE A CG  1 
ATOM 2458 C CD1 . PHE A 1 311 ? 7.872   18.285  179.455 1.00 52.11  ? 357 PHE A CD1 1 
ATOM 2459 C CD2 . PHE A 1 311 ? 6.263   19.078  181.018 1.00 52.51  ? 357 PHE A CD2 1 
ATOM 2460 C CE1 . PHE A 1 311 ? 7.249   17.056  179.434 1.00 52.00  ? 357 PHE A CE1 1 
ATOM 2461 C CE2 . PHE A 1 311 ? 5.636   17.849  181.000 1.00 51.17  ? 357 PHE A CE2 1 
ATOM 2462 C CZ  . PHE A 1 311 ? 6.130   16.838  180.207 1.00 51.17  ? 357 PHE A CZ  1 
ATOM 2463 N N   . PRO A 1 312 ? 11.191  22.114  181.655 1.00 57.83  ? 358 PRO A N   1 
ATOM 2464 C CA  . PRO A 1 312 ? 12.021  23.306  181.467 1.00 58.24  ? 358 PRO A CA  1 
ATOM 2465 C C   . PRO A 1 312 ? 12.896  23.206  180.228 1.00 57.47  ? 358 PRO A C   1 
ATOM 2466 O O   . PRO A 1 312 ? 13.399  22.139  179.869 1.00 54.28  ? 358 PRO A O   1 
ATOM 2467 C CB  . PRO A 1 312 ? 12.872  23.330  182.743 1.00 55.73  ? 358 PRO A CB  1 
ATOM 2468 C CG  . PRO A 1 312 ? 12.982  21.888  183.152 1.00 53.64  ? 358 PRO A CG  1 
ATOM 2469 C CD  . PRO A 1 312 ? 11.852  21.114  182.510 1.00 54.24  ? 358 PRO A CD  1 
ATOM 2470 N N   . GLY A 1 313 ? 13.076  24.344  179.568 1.00 52.99  ? 359 GLY A N   1 
ATOM 2471 C CA  . GLY A 1 313 ? 13.900  24.395  178.374 1.00 51.63  ? 359 GLY A CA  1 
ATOM 2472 C C   . GLY A 1 313 ? 13.361  23.596  177.208 1.00 50.16  ? 359 GLY A C   1 
ATOM 2473 O O   . GLY A 1 313 ? 14.125  22.888  176.540 1.00 49.74  ? 359 GLY A O   1 
ATOM 2474 N N   . ARG A 1 314 ? 12.061  23.690  176.945 1.00 47.41  ? 360 ARG A N   1 
ATOM 2475 C CA  . ARG A 1 314 ? 11.413  22.966  175.858 1.00 44.99  ? 360 ARG A CA  1 
ATOM 2476 C C   . ARG A 1 314 ? 10.871  23.924  174.801 1.00 50.11  ? 360 ARG A C   1 
ATOM 2477 O O   . ARG A 1 314 ? 9.856   23.657  174.156 1.00 55.12  ? 360 ARG A O   1 
ATOM 2478 C CB  . ARG A 1 314 ? 10.301  22.074  176.401 1.00 44.02  ? 360 ARG A CB  1 
ATOM 2479 C CG  . ARG A 1 314 ? 10.055  20.820  175.586 1.00 48.36  ? 360 ARG A CG  1 
ATOM 2480 C CD  . ARG A 1 314 ? 11.242  19.881  175.671 1.00 49.32  ? 360 ARG A CD  1 
ATOM 2481 N NE  . ARG A 1 314 ? 11.371  19.283  176.994 1.00 48.32  ? 360 ARG A NE  1 
ATOM 2482 C CZ  . ARG A 1 314 ? 11.232  17.990  177.247 1.00 50.95  ? 360 ARG A CZ  1 
ATOM 2483 N NH1 . ARG A 1 314 ? 10.960  17.123  176.286 1.00 49.40  ? 360 ARG A NH1 1 
ATOM 2484 N NH2 . ARG A 1 314 ? 11.374  17.555  178.496 1.00 51.04  ? 360 ARG A NH2 1 
ATOM 2485 N N   . GLN A 1 315 ? 11.548  25.053  174.612 1.00 43.44  ? 361 GLN A N   1 
ATOM 2486 C CA  . GLN A 1 315 ? 11.090  26.060  173.670 1.00 39.83  ? 361 GLN A CA  1 
ATOM 2487 C C   . GLN A 1 315 ? 11.301  25.596  172.231 1.00 40.08  ? 361 GLN A C   1 
ATOM 2488 O O   . GLN A 1 315 ? 12.138  24.738  171.938 1.00 43.29  ? 361 GLN A O   1 
ATOM 2489 C CB  . GLN A 1 315 ? 11.818  27.381  173.907 1.00 42.14  ? 361 GLN A CB  1 
ATOM 2490 C CG  . GLN A 1 315 ? 13.295  27.222  174.203 1.00 45.81  ? 361 GLN A CG  1 
ATOM 2491 C CD  . GLN A 1 315 ? 13.609  27.358  175.677 1.00 46.47  ? 361 GLN A CD  1 
ATOM 2492 O OE1 . GLN A 1 315 ? 12.708  27.400  176.513 1.00 45.66  ? 361 GLN A OE1 1 
ATOM 2493 N NE2 . GLN A 1 315 ? 14.892  27.423  176.005 1.00 45.60  ? 361 GLN A NE2 1 
ATOM 2494 N N   . TRP A 1 316 ? 10.518  26.183  171.325 1.00 35.76  ? 362 TRP A N   1 
ATOM 2495 C CA  . TRP A 1 316 ? 10.550  25.833  169.905 1.00 35.74  ? 362 TRP A CA  1 
ATOM 2496 C C   . TRP A 1 316 ? 11.623  26.659  169.195 1.00 41.46  ? 362 TRP A C   1 
ATOM 2497 O O   . TRP A 1 316 ? 11.354  27.655  168.522 1.00 44.01  ? 362 TRP A O   1 
ATOM 2498 C CB  . TRP A 1 316 ? 9.185   26.059  169.273 1.00 36.41  ? 362 TRP A CB  1 
ATOM 2499 C CG  . TRP A 1 316 ? 8.172   25.013  169.584 1.00 38.05  ? 362 TRP A CG  1 
ATOM 2500 C CD1 . TRP A 1 316 ? 8.149   24.185  170.666 1.00 38.41  ? 362 TRP A CD1 1 
ATOM 2501 C CD2 . TRP A 1 316 ? 7.009   24.700  168.814 1.00 36.99  ? 362 TRP A CD2 1 
ATOM 2502 N NE1 . TRP A 1 316 ? 7.049   23.365  170.609 1.00 34.84  ? 362 TRP A NE1 1 
ATOM 2503 C CE2 . TRP A 1 316 ? 6.333   23.664  169.480 1.00 35.68  ? 362 TRP A CE2 1 
ATOM 2504 C CE3 . TRP A 1 316 ? 6.478   25.195  167.620 1.00 32.43  ? 362 TRP A CE3 1 
ATOM 2505 C CZ2 . TRP A 1 316 ? 5.152   23.114  168.995 1.00 36.93  ? 362 TRP A CZ2 1 
ATOM 2506 C CZ3 . TRP A 1 316 ? 5.308   24.647  167.140 1.00 37.32  ? 362 TRP A CZ3 1 
ATOM 2507 C CH2 . TRP A 1 316 ? 4.658   23.617  167.824 1.00 36.27  ? 362 TRP A CH2 1 
ATOM 2508 N N   . GLN A 1 317 ? 12.865  26.218  169.346 1.00 36.70  ? 363 GLN A N   1 
ATOM 2509 C CA  . GLN A 1 317 ? 14.001  26.888  168.735 1.00 29.37  ? 363 GLN A CA  1 
ATOM 2510 C C   . GLN A 1 317 ? 14.753  25.931  167.822 1.00 32.19  ? 363 GLN A C   1 
ATOM 2511 O O   . GLN A 1 317 ? 14.728  24.711  168.004 1.00 43.81  ? 363 GLN A O   1 
ATOM 2512 C CB  . GLN A 1 317 ? 14.947  27.445  169.803 1.00 33.39  ? 363 GLN A CB  1 
ATOM 2513 C CG  . GLN A 1 317 ? 15.675  26.381  170.598 1.00 37.09  ? 363 GLN A CG  1 
ATOM 2514 C CD  . GLN A 1 317 ? 16.181  26.896  171.926 1.00 41.81  ? 363 GLN A CD  1 
ATOM 2515 O OE1 . GLN A 1 317 ? 15.895  28.029  172.314 1.00 43.86  ? 363 GLN A OE1 1 
ATOM 2516 N NE2 . GLN A 1 317 ? 16.936  26.066  172.635 1.00 40.52  ? 363 GLN A NE2 1 
ATOM 2517 N N   . ILE A 1 318 ? 15.422  26.501  166.828 1.00 23.50  ? 364 ILE A N   1 
ATOM 2518 C CA  . ILE A 1 318 ? 16.262  25.750  165.905 1.00 34.03  ? 364 ILE A CA  1 
ATOM 2519 C C   . ILE A 1 318 ? 17.700  25.951  166.362 1.00 38.10  ? 364 ILE A C   1 
ATOM 2520 O O   . ILE A 1 318 ? 18.369  26.909  165.959 1.00 36.20  ? 364 ILE A O   1 
ATOM 2521 C CB  . ILE A 1 318 ? 16.061  26.193  164.453 1.00 23.55  ? 364 ILE A CB  1 
ATOM 2522 C CG1 . ILE A 1 318 ? 14.579  26.144  164.092 1.00 19.44  ? 364 ILE A CG1 1 
ATOM 2523 C CG2 . ILE A 1 318 ? 16.857  25.308  163.514 1.00 30.08  ? 364 ILE A CG2 1 
ATOM 2524 C CD1 . ILE A 1 318 ? 14.294  26.536  162.671 1.00 27.86  ? 364 ILE A CD1 1 
ATOM 2525 N N   . THR A 1 319 ? 18.181  25.040  167.202 1.00 44.59  ? 365 THR A N   1 
ATOM 2526 C CA  . THR A 1 319 ? 19.502  25.168  167.796 1.00 45.54  ? 365 THR A CA  1 
ATOM 2527 C C   . THR A 1 319 ? 20.572  24.692  166.822 1.00 47.61  ? 365 THR A C   1 
ATOM 2528 O O   . THR A 1 319 ? 20.414  23.669  166.150 1.00 49.65  ? 365 THR A O   1 
ATOM 2529 C CB  . THR A 1 319 ? 19.570  24.368  169.099 1.00 52.26  ? 365 THR A CB  1 
ATOM 2530 O OG1 . THR A 1 319 ? 18.898  25.090  170.137 1.00 51.84  ? 365 THR A OG1 1 
ATOM 2531 C CG2 . THR A 1 319 ? 21.010  24.118  169.521 1.00 50.67  ? 365 THR A CG2 1 
ATOM 2532 N N   . GLN A 1 320 ? 21.664  25.453  166.739 1.00 50.14  ? 366 GLN A N   1 
ATOM 2533 C CA  . GLN A 1 320 ? 22.807  25.129  165.885 1.00 48.21  ? 366 GLN A CA  1 
ATOM 2534 C C   . GLN A 1 320 ? 24.083  25.348  166.692 1.00 51.04  ? 366 GLN A C   1 
ATOM 2535 O O   . GLN A 1 320 ? 24.568  26.476  166.805 1.00 58.20  ? 366 GLN A O   1 
ATOM 2536 C CB  . GLN A 1 320 ? 22.795  25.970  164.624 1.00 49.13  ? 366 GLN A CB  1 
ATOM 2537 C CG  . GLN A 1 320 ? 23.830  25.546  163.616 1.00 51.30  ? 366 GLN A CG  1 
ATOM 2538 C CD  . GLN A 1 320 ? 24.989  26.517  163.524 1.00 53.86  ? 366 GLN A CD  1 
ATOM 2539 O OE1 . GLN A 1 320 ? 24.796  27.732  163.520 1.00 54.61  ? 366 GLN A OE1 1 
ATOM 2540 N NE2 . GLN A 1 320 ? 26.202  25.984  163.447 1.00 52.66  ? 366 GLN A NE2 1 
ATOM 2541 N N   . ASN A 1 321 ? 24.626  24.270  167.249 1.00 55.67  ? 367 ASN A N   1 
ATOM 2542 C CA  . ASN A 1 321 ? 25.840  24.335  168.052 1.00 60.59  ? 367 ASN A CA  1 
ATOM 2543 C C   . ASN A 1 321 ? 26.913  23.462  167.417 1.00 63.55  ? 367 ASN A C   1 
ATOM 2544 O O   . ASN A 1 321 ? 26.683  22.257  167.219 1.00 65.19  ? 367 ASN A O   1 
ATOM 2545 C CB  . ASN A 1 321 ? 25.564  23.885  169.487 1.00 64.12  ? 367 ASN A CB  1 
ATOM 2546 C CG  . ASN A 1 321 ? 26.343  24.688  170.507 1.00 64.70  ? 367 ASN A CG  1 
ATOM 2547 O OD1 . ASN A 1 321 ? 27.421  25.201  170.217 1.00 61.00  ? 367 ASN A OD1 1 
ATOM 2548 N ND2 . ASN A 1 321 ? 25.798  24.798  171.713 1.00 67.31  ? 367 ASN A ND2 1 
ATOM 2549 N N   . PRO A 1 322 ? 28.083  24.010  167.073 1.00 63.27  ? 368 PRO A N   1 
ATOM 2550 C CA  . PRO A 1 322 ? 29.125  23.183  166.442 1.00 62.37  ? 368 PRO A CA  1 
ATOM 2551 C C   . PRO A 1 322 ? 29.615  22.036  167.308 1.00 64.29  ? 368 PRO A C   1 
ATOM 2552 O O   . PRO A 1 322 ? 30.025  21.005  166.760 1.00 64.51  ? 368 PRO A O   1 
ATOM 2553 C CB  . PRO A 1 322 ? 30.252  24.188  166.160 1.00 58.43  ? 368 PRO A CB  1 
ATOM 2554 C CG  . PRO A 1 322 ? 29.595  25.532  166.201 1.00 60.04  ? 368 PRO A CG  1 
ATOM 2555 C CD  . PRO A 1 322 ? 28.495  25.416  167.204 1.00 61.10  ? 368 PRO A CD  1 
ATOM 2556 N N   . ASP A 1 323 ? 29.596  22.175  168.631 1.00 65.96  ? 369 ASP A N   1 
ATOM 2557 C CA  . ASP A 1 323 ? 30.084  21.134  169.524 1.00 64.25  ? 369 ASP A CA  1 
ATOM 2558 C C   . ASP A 1 323 ? 28.977  20.232  170.054 1.00 65.84  ? 369 ASP A C   1 
ATOM 2559 O O   . ASP A 1 323 ? 29.251  19.370  170.895 1.00 63.89  ? 369 ASP A O   1 
ATOM 2560 C CB  . ASP A 1 323 ? 30.842  21.759  170.699 1.00 62.78  ? 369 ASP A CB  1 
ATOM 2561 C CG  . ASP A 1 323 ? 30.178  23.018  171.215 1.00 65.24  ? 369 ASP A CG  1 
ATOM 2562 O OD1 . ASP A 1 323 ? 28.931  23.071  171.222 1.00 64.78  ? 369 ASP A OD1 1 
ATOM 2563 O OD2 . ASP A 1 323 ? 30.902  23.953  171.619 1.00 65.78  ? 369 ASP A OD2 1 
ATOM 2564 N N   . VAL A 1 324 ? 27.742  20.408  169.594 1.00 62.52  ? 370 VAL A N   1 
ATOM 2565 C CA  . VAL A 1 324 ? 26.611  19.595  170.027 1.00 59.43  ? 370 VAL A CA  1 
ATOM 2566 C C   . VAL A 1 324 ? 26.068  18.860  168.811 1.00 60.19  ? 370 VAL A C   1 
ATOM 2567 O O   . VAL A 1 324 ? 25.760  19.485  167.788 1.00 59.50  ? 370 VAL A O   1 
ATOM 2568 C CB  . VAL A 1 324 ? 25.516  20.444  170.689 1.00 57.42  ? 370 VAL A CB  1 
ATOM 2569 C CG1 . VAL A 1 324 ? 24.302  19.589  171.006 1.00 55.73  ? 370 VAL A CG1 1 
ATOM 2570 C CG2 . VAL A 1 324 ? 26.051  21.107  171.948 1.00 57.88  ? 370 VAL A CG2 1 
ATOM 2571 N N   . ASN A 1 325 ? 25.954  17.535  168.924 1.00 64.22  ? 371 ASN A N   1 
ATOM 2572 C CA  . ASN A 1 325 ? 25.450  16.683  167.845 1.00 62.95  ? 371 ASN A CA  1 
ATOM 2573 C C   . ASN A 1 325 ? 26.265  16.862  166.567 1.00 61.20  ? 371 ASN A C   1 
ATOM 2574 O O   . ASN A 1 325 ? 25.724  16.851  165.459 1.00 57.80  ? 371 ASN A O   1 
ATOM 2575 C CB  . ASN A 1 325 ? 23.965  16.937  167.584 1.00 60.70  ? 371 ASN A CB  1 
ATOM 2576 C CG  . ASN A 1 325 ? 23.079  16.391  168.685 1.00 61.97  ? 371 ASN A CG  1 
ATOM 2577 O OD1 . ASN A 1 325 ? 23.342  16.597  169.869 1.00 64.43  ? 371 ASN A OD1 1 
ATOM 2578 N ND2 . ASN A 1 325 ? 22.022  15.687  168.299 1.00 61.32  ? 371 ASN A ND2 1 
ATOM 2579 N N   . ASN A 1 326 ? 27.581  17.023  166.727 1.00 62.05  ? 372 ASN A N   1 
ATOM 2580 C CA  . ASN A 1 326 ? 28.516  17.176  165.610 1.00 61.27  ? 372 ASN A CA  1 
ATOM 2581 C C   . ASN A 1 326 ? 28.147  18.351  164.709 1.00 60.22  ? 372 ASN A C   1 
ATOM 2582 O O   . ASN A 1 326 ? 28.332  18.296  163.492 1.00 59.24  ? 372 ASN A O   1 
ATOM 2583 C CB  . ASN A 1 326 ? 28.622  15.888  164.785 1.00 62.70  ? 372 ASN A CB  1 
ATOM 2584 C CG  . ASN A 1 326 ? 28.356  14.642  165.609 1.00 64.37  ? 372 ASN A CG  1 
ATOM 2585 O OD1 . ASN A 1 326 ? 29.071  14.353  166.568 1.00 63.08  ? 372 ASN A OD1 1 
ATOM 2586 N ND2 . ASN A 1 326 ? 27.323  13.897  165.235 1.00 60.25  ? 372 ASN A ND2 1 
ATOM 2587 N N   . GLY A 1 327 ? 27.622  19.424  165.298 1.00 56.03  ? 373 GLY A N   1 
ATOM 2588 C CA  . GLY A 1 327 ? 27.298  20.615  164.541 1.00 55.46  ? 373 GLY A CA  1 
ATOM 2589 C C   . GLY A 1 327 ? 26.056  20.522  163.688 1.00 53.84  ? 373 GLY A C   1 
ATOM 2590 O O   . GLY A 1 327 ? 25.806  21.431  162.888 1.00 48.90  ? 373 GLY A O   1 
ATOM 2591 N N   . ALA A 1 328 ? 25.271  19.459  163.827 1.00 49.23  ? 374 ALA A N   1 
ATOM 2592 C CA  . ALA A 1 328 ? 24.080  19.296  163.013 1.00 47.29  ? 374 ALA A CA  1 
ATOM 2593 C C   . ALA A 1 328 ? 22.982  20.254  163.462 1.00 48.54  ? 374 ALA A C   1 
ATOM 2594 O O   . ALA A 1 328 ? 22.920  20.678  164.619 1.00 49.27  ? 374 ALA A O   1 
ATOM 2595 C CB  . ALA A 1 328 ? 23.575  17.856  163.081 1.00 46.23  ? 374 ALA A CB  1 
ATOM 2596 N N   . ILE A 1 329 ? 22.105  20.595  162.520 1.00 41.11  ? 375 ILE A N   1 
ATOM 2597 C CA  . ILE A 1 329 ? 20.940  21.413  162.833 1.00 34.83  ? 375 ILE A CA  1 
ATOM 2598 C C   . ILE A 1 329 ? 19.950  20.561  163.614 1.00 37.31  ? 375 ILE A C   1 
ATOM 2599 O O   . ILE A 1 329 ? 19.559  19.476  163.171 1.00 44.25  ? 375 ILE A O   1 
ATOM 2600 C CB  . ILE A 1 329 ? 20.304  21.973  161.555 1.00 32.53  ? 375 ILE A CB  1 
ATOM 2601 C CG1 . ILE A 1 329 ? 21.181  23.072  160.957 1.00 32.28  ? 375 ILE A CG1 1 
ATOM 2602 C CG2 . ILE A 1 329 ? 18.914  22.508  161.842 1.00 37.14  ? 375 ILE A CG2 1 
ATOM 2603 C CD1 . ILE A 1 329 ? 20.854  23.385  159.517 1.00 34.54  ? 375 ILE A CD1 1 
ATOM 2604 N N   . ILE A 1 330 ? 19.542  21.046  164.782 1.00 35.76  ? 376 ILE A N   1 
ATOM 2605 C CA  . ILE A 1 330 ? 18.662  20.306  165.677 1.00 33.37  ? 376 ILE A CA  1 
ATOM 2606 C C   . ILE A 1 330 ? 17.364  21.085  165.819 1.00 39.69  ? 376 ILE A C   1 
ATOM 2607 O O   . ILE A 1 330 ? 17.377  22.268  166.180 1.00 41.52  ? 376 ILE A O   1 
ATOM 2608 C CB  . ILE A 1 330 ? 19.314  20.072  167.048 1.00 32.00  ? 376 ILE A CB  1 
ATOM 2609 C CG1 . ILE A 1 330 ? 20.575  19.219  166.903 1.00 41.16  ? 376 ILE A CG1 1 
ATOM 2610 C CG2 . ILE A 1 330 ? 18.333  19.406  167.995 1.00 32.09  ? 376 ILE A CG2 1 
ATOM 2611 C CD1 . ILE A 1 330 ? 20.359  17.930  166.153 1.00 43.25  ? 376 ILE A CD1 1 
ATOM 2612 N N   . PHE A 1 331 ? 16.244  20.423  165.532 1.00 38.82  ? 377 PHE A N   1 
ATOM 2613 C CA  . PHE A 1 331 ? 14.925  21.011  165.754 1.00 27.59  ? 377 PHE A CA  1 
ATOM 2614 C C   . PHE A 1 331 ? 13.987  19.869  166.133 1.00 32.84  ? 377 PHE A C   1 
ATOM 2615 O O   . PHE A 1 331 ? 13.436  19.197  165.257 1.00 33.06  ? 377 PHE A O   1 
ATOM 2616 C CB  . PHE A 1 331 ? 14.433  21.758  164.524 1.00 27.25  ? 377 PHE A CB  1 
ATOM 2617 C CG  . PHE A 1 331 ? 13.014  22.233  164.635 1.00 32.24  ? 377 PHE A CG  1 
ATOM 2618 C CD1 . PHE A 1 331 ? 12.645  23.125  165.627 1.00 35.23  ? 377 PHE A CD1 1 
ATOM 2619 C CD2 . PHE A 1 331 ? 12.052  21.795  163.746 1.00 33.65  ? 377 PHE A CD2 1 
ATOM 2620 C CE1 . PHE A 1 331 ? 11.344  23.564  165.734 1.00 29.40  ? 377 PHE A CE1 1 
ATOM 2621 C CE2 . PHE A 1 331 ? 10.750  22.234  163.847 1.00 30.43  ? 377 PHE A CE2 1 
ATOM 2622 C CZ  . PHE A 1 331 ? 10.396  23.120  164.841 1.00 26.08  ? 377 PHE A CZ  1 
ATOM 2623 N N   . HIS A 1 332 ? 13.815  19.660  167.435 1.00 40.56  ? 378 HIS A N   1 
ATOM 2624 C CA  . HIS A 1 332 ? 13.010  18.562  167.956 1.00 44.12  ? 378 HIS A CA  1 
ATOM 2625 C C   . HIS A 1 332 ? 11.987  19.152  168.915 1.00 45.83  ? 378 HIS A C   1 
ATOM 2626 O O   . HIS A 1 332 ? 12.239  19.192  170.137 1.00 48.67  ? 378 HIS A O   1 
ATOM 2627 C CB  . HIS A 1 332 ? 13.890  17.522  168.653 1.00 36.02  ? 378 HIS A CB  1 
ATOM 2628 C CG  . HIS A 1 332 ? 13.287  16.154  168.703 1.00 43.54  ? 378 HIS A CG  1 
ATOM 2629 N ND1 . HIS A 1 332 ? 14.010  15.036  169.058 1.00 44.64  ? 378 HIS A ND1 1 
ATOM 2630 C CD2 . HIS A 1 332 ? 12.031  15.723  168.442 1.00 47.53  ? 378 HIS A CD2 1 
ATOM 2631 C CE1 . HIS A 1 332 ? 13.225  13.975  169.013 1.00 46.97  ? 378 HIS A CE1 1 
ATOM 2632 N NE2 . HIS A 1 332 ? 12.019  14.364  168.642 1.00 47.80  ? 378 HIS A NE2 1 
ATOM 2633 N N   . PRO A 1 333 ? 10.839  19.616  168.431 1.00 31.40  ? 379 PRO A N   1 
ATOM 2634 C CA  . PRO A 1 333 ? 9.891   20.297  169.316 1.00 32.28  ? 379 PRO A CA  1 
ATOM 2635 C C   . PRO A 1 333 ? 8.973   19.333  170.044 1.00 38.04  ? 379 PRO A C   1 
ATOM 2636 O O   . PRO A 1 333 ? 8.828   18.174  169.645 1.00 43.57  ? 379 PRO A O   1 
ATOM 2637 C CB  . PRO A 1 333 ? 9.110   21.198  168.354 1.00 34.65  ? 379 PRO A CB  1 
ATOM 2638 C CG  . PRO A 1 333 ? 9.191   20.500  167.024 1.00 33.26  ? 379 PRO A CG  1 
ATOM 2639 C CD  . PRO A 1 333 ? 10.322  19.499  167.058 1.00 30.20  ? 379 PRO A CD  1 
ATOM 2640 N N   . SER A 1 334 ? 8.349   19.806  171.117 1.00 39.47  ? 380 SER A N   1 
ATOM 2641 C CA  . SER A 1 334 ? 7.388   19.029  171.885 1.00 33.78  ? 380 SER A CA  1 
ATOM 2642 C C   . SER A 1 334 ? 6.008   19.628  171.669 1.00 34.10  ? 380 SER A C   1 
ATOM 2643 O O   . SER A 1 334 ? 5.809   20.828  171.883 1.00 45.92  ? 380 SER A O   1 
ATOM 2644 C CB  . SER A 1 334 ? 7.748   19.019  173.369 1.00 37.92  ? 380 SER A CB  1 
ATOM 2645 O OG  . SER A 1 334 ? 9.053   18.507  173.567 1.00 45.22  ? 380 SER A OG  1 
ATOM 2646 N N   . PHE A 1 335 ? 5.064   18.798  171.246 1.00 31.73  ? 381 PHE A N   1 
ATOM 2647 C CA  . PHE A 1 335 ? 3.723   19.257  170.930 1.00 34.33  ? 381 PHE A CA  1 
ATOM 2648 C C   . PHE A 1 335 ? 2.803   19.078  172.135 1.00 37.00  ? 381 PHE A C   1 
ATOM 2649 O O   . PHE A 1 335 ? 3.225   18.669  173.217 1.00 43.80  ? 381 PHE A O   1 
ATOM 2650 C CB  . PHE A 1 335 ? 3.181   18.506  169.716 1.00 33.95  ? 381 PHE A CB  1 
ATOM 2651 C CG  . PHE A 1 335 ? 3.957   18.752  168.453 1.00 30.75  ? 381 PHE A CG  1 
ATOM 2652 C CD1 . PHE A 1 335 ? 4.815   19.831  168.349 1.00 32.76  ? 381 PHE A CD1 1 
ATOM 2653 C CD2 . PHE A 1 335 ? 3.829   17.903  167.370 1.00 36.85  ? 381 PHE A CD2 1 
ATOM 2654 C CE1 . PHE A 1 335 ? 5.528   20.059  167.190 1.00 34.96  ? 381 PHE A CE1 1 
ATOM 2655 C CE2 . PHE A 1 335 ? 4.539   18.127  166.209 1.00 37.25  ? 381 PHE A CE2 1 
ATOM 2656 C CZ  . PHE A 1 335 ? 5.391   19.205  166.120 1.00 33.29  ? 381 PHE A CZ  1 
ATOM 2657 N N   . GLY A 1 336 ? 1.527   19.397  171.938 1.00 31.72  ? 382 GLY A N   1 
ATOM 2658 C CA  . GLY A 1 336 ? 0.534   19.251  172.980 1.00 38.56  ? 382 GLY A CA  1 
ATOM 2659 C C   . GLY A 1 336 ? 0.385   20.436  173.909 1.00 41.76  ? 382 GLY A C   1 
ATOM 2660 O O   . GLY A 1 336 ? -0.354  20.336  174.895 1.00 43.37  ? 382 GLY A O   1 
ATOM 2661 N N   . TYR A 1 337 ? 1.066   21.544  173.638 1.00 42.12  ? 383 TYR A N   1 
ATOM 2662 C CA  . TYR A 1 337 ? 0.926   22.741  174.455 1.00 41.16  ? 383 TYR A CA  1 
ATOM 2663 C C   . TYR A 1 337 ? -0.154  23.645  173.879 1.00 45.93  ? 383 TYR A C   1 
ATOM 2664 O O   . TYR A 1 337 ? -0.154  23.954  172.685 1.00 47.65  ? 383 TYR A O   1 
ATOM 2665 C CB  . TYR A 1 337 ? 2.256   23.489  174.530 1.00 42.76  ? 383 TYR A CB  1 
ATOM 2666 C CG  . TYR A 1 337 ? 2.224   24.726  175.395 1.00 41.62  ? 383 TYR A CG  1 
ATOM 2667 C CD1 . TYR A 1 337 ? 1.684   24.691  176.671 1.00 44.09  ? 383 TYR A CD1 1 
ATOM 2668 C CD2 . TYR A 1 337 ? 2.740   25.929  174.935 1.00 43.84  ? 383 TYR A CD2 1 
ATOM 2669 C CE1 . TYR A 1 337 ? 1.656   25.819  177.463 1.00 47.35  ? 383 TYR A CE1 1 
ATOM 2670 C CE2 . TYR A 1 337 ? 2.718   27.061  175.721 1.00 45.89  ? 383 TYR A CE2 1 
ATOM 2671 C CZ  . TYR A 1 337 ? 2.174   27.001  176.983 1.00 49.05  ? 383 TYR A CZ  1 
ATOM 2672 O OH  . TYR A 1 337 ? 2.148   28.127  177.770 1.00 52.33  ? 383 TYR A OH  1 
ATOM 2673 N N   . ASP A 1 338 ? -1.080  24.073  174.737 1.00 51.96  ? 384 ASP A N   1 
ATOM 2674 C CA  . ASP A 1 338 ? -2.200  24.901  174.309 1.00 50.84  ? 384 ASP A CA  1 
ATOM 2675 C C   . ASP A 1 338 ? -2.068  26.365  174.694 1.00 49.61  ? 384 ASP A C   1 
ATOM 2676 O O   . ASP A 1 338 ? -2.636  27.219  174.012 1.00 53.50  ? 384 ASP A O   1 
ATOM 2677 C CB  . ASP A 1 338 ? -3.513  24.361  174.886 1.00 49.83  ? 384 ASP A CB  1 
ATOM 2678 C CG  . ASP A 1 338 ? -3.417  24.058  176.361 1.00 56.48  ? 384 ASP A CG  1 
ATOM 2679 O OD1 . ASP A 1 338 ? -2.326  24.242  176.939 1.00 58.25  ? 384 ASP A OD1 1 
ATOM 2680 O OD2 . ASP A 1 338 ? -4.435  23.638  176.944 1.00 55.40  ? 384 ASP A OD2 1 
ATOM 2681 N N   . GLY A 1 339 ? -1.341  26.676  175.762 1.00 46.28  ? 385 GLY A N   1 
ATOM 2682 C CA  . GLY A 1 339 ? -1.172  28.053  176.176 1.00 48.52  ? 385 GLY A CA  1 
ATOM 2683 C C   . GLY A 1 339 ? -1.226  28.230  177.677 1.00 52.07  ? 385 GLY A C   1 
ATOM 2684 O O   . GLY A 1 339 ? -0.653  29.180  178.220 1.00 56.56  ? 385 GLY A O   1 
ATOM 2685 N N   . GLN A 1 340 ? -1.911  27.321  178.361 1.00 54.54  ? 386 GLN A N   1 
ATOM 2686 C CA  . GLN A 1 340 ? -2.014  27.340  179.810 1.00 56.42  ? 386 GLN A CA  1 
ATOM 2687 C C   . GLN A 1 340 ? -1.299  26.132  180.398 1.00 60.47  ? 386 GLN A C   1 
ATOM 2688 O O   . GLN A 1 340 ? -1.087  25.118  179.729 1.00 62.26  ? 386 GLN A O   1 
ATOM 2689 C CB  . GLN A 1 340 ? -3.478  27.356  180.259 1.00 57.67  ? 386 GLN A CB  1 
ATOM 2690 C CG  . GLN A 1 340 ? -4.426  28.014  179.273 1.00 60.45  ? 386 GLN A CG  1 
ATOM 2691 C CD  . GLN A 1 340 ? -4.187  29.504  179.142 1.00 63.86  ? 386 GLN A CD  1 
ATOM 2692 O OE1 . GLN A 1 340 ? -4.110  30.221  180.139 1.00 66.82  ? 386 GLN A OE1 1 
ATOM 2693 N NE2 . GLN A 1 340 ? -4.072  29.979  177.908 1.00 61.06  ? 386 GLN A NE2 1 
ATOM 2694 N N   . ASP A 1 341 ? -0.927  26.255  181.669 1.00 65.09  ? 387 ASP A N   1 
ATOM 2695 C CA  . ASP A 1 341 ? -0.179  25.209  182.362 1.00 62.86  ? 387 ASP A CA  1 
ATOM 2696 C C   . ASP A 1 341 ? -1.146  24.234  183.033 1.00 65.23  ? 387 ASP A C   1 
ATOM 2697 O O   . ASP A 1 341 ? -1.246  24.145  184.255 1.00 66.58  ? 387 ASP A O   1 
ATOM 2698 C CB  . ASP A 1 341 ? 0.781   25.827  183.373 1.00 62.64  ? 387 ASP A CB  1 
ATOM 2699 C CG  . ASP A 1 341 ? 1.824   24.844  183.857 1.00 67.35  ? 387 ASP A CG  1 
ATOM 2700 O OD1 . ASP A 1 341 ? 2.012   23.806  183.192 1.00 70.47  ? 387 ASP A OD1 1 
ATOM 2701 O OD2 . ASP A 1 341 ? 2.453   25.107  184.903 1.00 67.57  ? 387 ASP A OD2 1 
ATOM 2702 N N   . HIS A 1 342 ? -1.870  23.494  182.197 1.00 60.90  ? 388 HIS A N   1 
ATOM 2703 C CA  . HIS A 1 342 ? -2.760  22.447  182.680 1.00 57.72  ? 388 HIS A CA  1 
ATOM 2704 C C   . HIS A 1 342 ? -2.694  21.276  181.706 1.00 58.87  ? 388 HIS A C   1 
ATOM 2705 O O   . HIS A 1 342 ? -1.964  21.308  180.710 1.00 60.63  ? 388 HIS A O   1 
ATOM 2706 C CB  . HIS A 1 342 ? -4.186  22.982  182.875 1.00 56.53  ? 388 HIS A CB  1 
ATOM 2707 C CG  . HIS A 1 342 ? -4.891  23.318  181.600 1.00 59.08  ? 388 HIS A CG  1 
ATOM 2708 N ND1 . HIS A 1 342 ? -4.444  24.294  180.737 1.00 60.25  ? 388 HIS A ND1 1 
ATOM 2709 C CD2 . HIS A 1 342 ? -6.018  22.813  181.046 1.00 61.06  ? 388 HIS A CD2 1 
ATOM 2710 C CE1 . HIS A 1 342 ? -5.264  24.375  179.704 1.00 61.99  ? 388 HIS A CE1 1 
ATOM 2711 N NE2 . HIS A 1 342 ? -6.227  23.486  179.866 1.00 61.73  ? 388 HIS A NE2 1 
ATOM 2712 N N   . GLU A 1 343 ? -3.470  20.231  182.001 1.00 54.41  ? 389 GLU A N   1 
ATOM 2713 C CA  . GLU A 1 343 ? -3.355  18.970  181.277 1.00 51.13  ? 389 GLU A CA  1 
ATOM 2714 C C   . GLU A 1 343 ? -3.801  19.085  179.825 1.00 55.26  ? 389 GLU A C   1 
ATOM 2715 O O   . GLU A 1 343 ? -3.113  18.587  178.927 1.00 53.81  ? 389 GLU A O   1 
ATOM 2716 C CB  . GLU A 1 343 ? -4.167  17.889  181.990 1.00 51.70  ? 389 GLU A CB  1 
ATOM 2717 C CG  . GLU A 1 343 ? -3.493  16.529  182.063 1.00 56.77  ? 389 GLU A CG  1 
ATOM 2718 C CD  . GLU A 1 343 ? -3.541  15.778  180.745 1.00 58.00  ? 389 GLU A CD  1 
ATOM 2719 O OE1 . GLU A 1 343 ? -4.359  16.142  179.877 1.00 60.26  ? 389 GLU A OE1 1 
ATOM 2720 O OE2 . GLU A 1 343 ? -2.773  14.810  180.580 1.00 52.44  ? 389 GLU A OE2 1 
ATOM 2721 N N   . GLU A 1 344 ? -4.941  19.732  179.573 1.00 57.61  ? 390 GLU A N   1 
ATOM 2722 C CA  . GLU A 1 344 ? -5.584  19.735  178.257 1.00 53.48  ? 390 GLU A CA  1 
ATOM 2723 C C   . GLU A 1 344 ? -5.884  18.298  177.815 1.00 52.27  ? 390 GLU A C   1 
ATOM 2724 O O   . GLU A 1 344 ? -5.261  17.731  176.915 1.00 53.37  ? 390 GLU A O   1 
ATOM 2725 C CB  . GLU A 1 344 ? -4.740  20.497  177.223 1.00 51.90  ? 390 GLU A CB  1 
ATOM 2726 C CG  . GLU A 1 344 ? -5.282  20.500  175.784 1.00 53.01  ? 390 GLU A CG  1 
ATOM 2727 C CD  . GLU A 1 344 ? -6.627  21.203  175.615 1.00 57.91  ? 390 GLU A CD  1 
ATOM 2728 O OE1 . GLU A 1 344 ? -7.231  21.644  176.616 1.00 59.69  ? 390 GLU A OE1 1 
ATOM 2729 O OE2 . GLU A 1 344 ? -7.087  21.312  174.459 1.00 53.74  ? 390 GLU A OE2 1 
ATOM 2730 N N   . LEU A 1 345 ? -6.842  17.705  178.531 1.00 44.46  ? 391 LEU A N   1 
ATOM 2731 C CA  . LEU A 1 345 ? -7.222  16.312  178.338 1.00 39.98  ? 391 LEU A CA  1 
ATOM 2732 C C   . LEU A 1 345 ? -7.652  15.999  176.912 1.00 41.81  ? 391 LEU A C   1 
ATOM 2733 O O   . LEU A 1 345 ? -7.551  14.841  176.496 1.00 41.35  ? 391 LEU A O   1 
ATOM 2734 C CB  . LEU A 1 345 ? -8.359  15.947  179.292 1.00 41.24  ? 391 LEU A CB  1 
ATOM 2735 C CG  . LEU A 1 345 ? -8.015  15.104  180.517 1.00 43.23  ? 391 LEU A CG  1 
ATOM 2736 C CD1 . LEU A 1 345 ? -7.170  15.908  181.487 1.00 41.51  ? 391 LEU A CD1 1 
ATOM 2737 C CD2 . LEU A 1 345 ? -9.279  14.607  181.191 1.00 47.63  ? 391 LEU A CD2 1 
ATOM 2738 N N   . SER A 1 346 ? -8.133  16.992  176.161 1.00 47.50  ? 392 SER A N   1 
ATOM 2739 C CA  . SER A 1 346 ? -8.607  16.746  174.805 1.00 45.30  ? 392 SER A CA  1 
ATOM 2740 C C   . SER A 1 346 ? -7.510  16.239  173.881 1.00 41.75  ? 392 SER A C   1 
ATOM 2741 O O   . SER A 1 346 ? -7.813  15.533  172.915 1.00 42.73  ? 392 SER A O   1 
ATOM 2742 C CB  . SER A 1 346 ? -9.216  18.021  174.225 1.00 44.86  ? 392 SER A CB  1 
ATOM 2743 O OG  . SER A 1 346 ? -8.220  18.827  173.620 1.00 50.70  ? 392 SER A OG  1 
ATOM 2744 N N   . PHE A 1 347 ? -6.250  16.576  174.153 1.00 39.81  ? 393 PHE A N   1 
ATOM 2745 C CA  . PHE A 1 347 ? -5.146  16.126  173.315 1.00 38.28  ? 393 PHE A CA  1 
ATOM 2746 C C   . PHE A 1 347 ? -4.919  14.624  173.395 1.00 39.82  ? 393 PHE A C   1 
ATOM 2747 O O   . PHE A 1 347 ? -4.203  14.078  172.551 1.00 43.37  ? 393 PHE A O   1 
ATOM 2748 C CB  . PHE A 1 347 ? -3.861  16.858  173.703 1.00 41.42  ? 393 PHE A CB  1 
ATOM 2749 C CG  . PHE A 1 347 ? -3.463  17.935  172.738 1.00 40.27  ? 393 PHE A CG  1 
ATOM 2750 C CD1 . PHE A 1 347 ? -3.269  17.647  171.399 1.00 35.66  ? 393 PHE A CD1 1 
ATOM 2751 C CD2 . PHE A 1 347 ? -3.286  19.236  173.171 1.00 35.18  ? 393 PHE A CD2 1 
ATOM 2752 C CE1 . PHE A 1 347 ? -2.905  18.637  170.512 1.00 35.65  ? 393 PHE A CE1 1 
ATOM 2753 C CE2 . PHE A 1 347 ? -2.922  20.228  172.288 1.00 37.42  ? 393 PHE A CE2 1 
ATOM 2754 C CZ  . PHE A 1 347 ? -2.733  19.929  170.957 1.00 37.45  ? 393 PHE A CZ  1 
ATOM 2755 N N   . ARG A 1 348 ? -5.506  13.952  174.387 1.00 45.10  ? 394 ARG A N   1 
ATOM 2756 C CA  . ARG A 1 348 ? -5.355  12.509  174.521 1.00 40.77  ? 394 ARG A CA  1 
ATOM 2757 C C   . ARG A 1 348 ? -5.984  11.750  173.362 1.00 37.89  ? 394 ARG A C   1 
ATOM 2758 O O   . ARG A 1 348 ? -5.560  10.628  173.072 1.00 41.00  ? 394 ARG A O   1 
ATOM 2759 C CB  . ARG A 1 348 ? -5.967  12.049  175.843 1.00 36.67  ? 394 ARG A CB  1 
ATOM 2760 C CG  . ARG A 1 348 ? -5.133  12.402  177.058 1.00 36.74  ? 394 ARG A CG  1 
ATOM 2761 C CD  . ARG A 1 348 ? -5.616  11.676  178.297 1.00 35.97  ? 394 ARG A CD  1 
ATOM 2762 N NE  . ARG A 1 348 ? -5.594  12.544  179.467 1.00 41.68  ? 394 ARG A NE  1 
ATOM 2763 C CZ  . ARG A 1 348 ? -5.638  12.116  180.720 1.00 42.19  ? 394 ARG A CZ  1 
ATOM 2764 N NH1 . ARG A 1 348 ? -5.726  10.829  181.008 1.00 40.57  ? 394 ARG A NH1 1 
ATOM 2765 N NH2 . ARG A 1 348 ? -5.596  13.002  181.710 1.00 43.90  ? 394 ARG A NH2 1 
ATOM 2766 N N   . ALA A 1 349 ? -6.980  12.334  172.695 1.00 34.34  ? 395 ALA A N   1 
ATOM 2767 C CA  . ALA A 1 349 ? -7.632  11.672  171.573 1.00 33.41  ? 395 ALA A CA  1 
ATOM 2768 C C   . ALA A 1 349 ? -6.765  11.633  170.324 1.00 38.60  ? 395 ALA A C   1 
ATOM 2769 O O   . ALA A 1 349 ? -7.107  10.916  169.379 1.00 42.01  ? 395 ALA A O   1 
ATOM 2770 C CB  . ALA A 1 349 ? -8.959  12.360  171.257 1.00 34.75  ? 395 ALA A CB  1 
ATOM 2771 N N   . MET A 1 350 ? -5.665  12.379  170.293 1.00 40.65  ? 396 MET A N   1 
ATOM 2772 C CA  . MET A 1 350 ? -4.751  12.378  169.160 1.00 40.81  ? 396 MET A CA  1 
ATOM 2773 C C   . MET A 1 350 ? -3.817  11.176  169.159 1.00 43.18  ? 396 MET A C   1 
ATOM 2774 O O   . MET A 1 350 ? -3.069  10.991  168.194 1.00 45.47  ? 396 MET A O   1 
ATOM 2775 C CB  . MET A 1 350 ? -3.919  13.663  169.151 1.00 39.84  ? 396 MET A CB  1 
ATOM 2776 C CG  . MET A 1 350 ? -4.702  14.930  168.852 1.00 41.65  ? 396 MET A CG  1 
ATOM 2777 S SD  . MET A 1 350 ? -5.400  14.972  167.193 1.00 49.20  ? 396 MET A SD  1 
ATOM 2778 C CE  . MET A 1 350 ? -7.142  15.045  167.579 1.00 39.27  ? 396 MET A CE  1 
ATOM 2779 N N   . CYS A 1 351 ? -3.840  10.361  170.213 1.00 36.00  ? 397 CYS A N   1 
ATOM 2780 C CA  . CYS A 1 351 ? -2.915  9.244   170.346 1.00 31.53  ? 397 CYS A CA  1 
ATOM 2781 C C   . CYS A 1 351 ? -3.298  8.042   169.494 1.00 36.81  ? 397 CYS A C   1 
ATOM 2782 O O   . CYS A 1 351 ? -2.518  7.088   169.420 1.00 37.41  ? 397 CYS A O   1 
ATOM 2783 C CB  . CYS A 1 351 ? -2.816  8.824   171.813 1.00 33.64  ? 397 CYS A CB  1 
ATOM 2784 S SG  . CYS A 1 351 ? -1.995  10.037  172.865 1.00 52.36  ? 397 CYS A SG  1 
ATOM 2785 N N   . SER A 1 352 ? -4.469  8.053   168.866 1.00 35.62  ? 398 SER A N   1 
ATOM 2786 C CA  . SER A 1 352 ? -4.840  6.979   167.961 1.00 35.64  ? 398 SER A CA  1 
ATOM 2787 C C   . SER A 1 352 ? -4.299  7.252   166.561 1.00 38.66  ? 398 SER A C   1 
ATOM 2788 O O   . SER A 1 352 ? -3.932  8.378   166.216 1.00 42.25  ? 398 SER A O   1 
ATOM 2789 C CB  . SER A 1 352 ? -6.357  6.813   167.912 1.00 31.54  ? 398 SER A CB  1 
ATOM 2790 O OG  . SER A 1 352 ? -6.922  7.619   166.895 1.00 39.32  ? 398 SER A OG  1 
ATOM 2791 N N   . ASN A 1 353 ? -4.250  6.199   165.751 1.00 35.03  ? 399 ASN A N   1 
ATOM 2792 C CA  . ASN A 1 353 ? -3.765  6.330   164.384 1.00 31.09  ? 399 ASN A CA  1 
ATOM 2793 C C   . ASN A 1 353 ? -4.712  7.195   163.565 1.00 35.31  ? 399 ASN A C   1 
ATOM 2794 O O   . ASN A 1 353 ? -5.935  7.106   163.700 1.00 38.11  ? 399 ASN A O   1 
ATOM 2795 C CB  . ASN A 1 353 ? -3.621  4.955   163.736 1.00 30.79  ? 399 ASN A CB  1 
ATOM 2796 C CG  . ASN A 1 353 ? -2.453  4.171   164.291 1.00 40.88  ? 399 ASN A CG  1 
ATOM 2797 O OD1 . ASN A 1 353 ? -1.341  4.683   164.400 1.00 43.97  ? 399 ASN A OD1 1 
ATOM 2798 N ND2 . ASN A 1 353 ? -2.701  2.918   164.651 1.00 40.47  ? 399 ASN A ND2 1 
ATOM 2799 N N   . MET A 1 354 ? -4.142  8.036   162.709 1.00 34.84  ? 400 MET A N   1 
ATOM 2800 C CA  . MET A 1 354 ? -4.952  8.931   161.903 1.00 35.48  ? 400 MET A CA  1 
ATOM 2801 C C   . MET A 1 354 ? -5.573  8.183   160.729 1.00 34.15  ? 400 MET A C   1 
ATOM 2802 O O   . MET A 1 354 ? -5.108  7.118   160.317 1.00 37.32  ? 400 MET A O   1 
ATOM 2803 C CB  . MET A 1 354 ? -4.119  10.104  161.390 1.00 35.08  ? 400 MET A CB  1 
ATOM 2804 C CG  . MET A 1 354 ? -3.146  9.739   160.290 1.00 35.59  ? 400 MET A CG  1 
ATOM 2805 S SD  . MET A 1 354 ? -2.706  11.155  159.268 1.00 54.35  ? 400 MET A SD  1 
ATOM 2806 C CE  . MET A 1 354 ? -4.102  11.211  158.151 1.00 38.10  ? 400 MET A CE  1 
ATOM 2807 N N   . ILE A 1 355 ? -6.644  8.758   160.192 1.00 36.04  ? 401 ILE A N   1 
ATOM 2808 C CA  . ILE A 1 355 ? -7.355  8.202   159.048 1.00 31.79  ? 401 ILE A CA  1 
ATOM 2809 C C   . ILE A 1 355 ? -7.236  9.192   157.902 1.00 34.26  ? 401 ILE A C   1 
ATOM 2810 O O   . ILE A 1 355 ? -7.729  10.322  158.001 1.00 38.30  ? 401 ILE A O   1 
ATOM 2811 C CB  . ILE A 1 355 ? -8.832  7.923   159.370 1.00 28.18  ? 401 ILE A CB  1 
ATOM 2812 C CG1 . ILE A 1 355 ? -8.945  6.814   160.413 1.00 34.13  ? 401 ILE A CG1 1 
ATOM 2813 C CG2 . ILE A 1 355 ? -9.590  7.547   158.112 1.00 30.55  ? 401 ILE A CG2 1 
ATOM 2814 C CD1 . ILE A 1 355 ? -10.307 6.717   161.044 1.00 35.93  ? 401 ILE A CD1 1 
ATOM 2815 N N   . LEU A 1 356 ? -6.591  8.773   156.819 1.00 30.80  ? 402 LEU A N   1 
ATOM 2816 C CA  . LEU A 1 356 ? -6.396  9.633   155.661 1.00 32.11  ? 402 LEU A CA  1 
ATOM 2817 C C   . LEU A 1 356 ? -7.604  9.506   154.743 1.00 36.74  ? 402 LEU A C   1 
ATOM 2818 O O   . LEU A 1 356 ? -7.843  8.441   154.165 1.00 38.81  ? 402 LEU A O   1 
ATOM 2819 C CB  . LEU A 1 356 ? -5.105  9.271   154.930 1.00 31.68  ? 402 LEU A CB  1 
ATOM 2820 C CG  . LEU A 1 356 ? -4.874  9.893   153.553 1.00 29.67  ? 402 LEU A CG  1 
ATOM 2821 C CD1 . LEU A 1 356 ? -3.474  10.457  153.454 1.00 30.09  ? 402 LEU A CD1 1 
ATOM 2822 C CD2 . LEU A 1 356 ? -5.087  8.853   152.478 1.00 32.75  ? 402 LEU A CD2 1 
ATOM 2823 N N   . ASN A 1 357 ? -8.358  10.592  154.611 1.00 36.41  ? 403 ASN A N   1 
ATOM 2824 C CA  . ASN A 1 357 ? -9.578  10.622  153.820 1.00 29.39  ? 403 ASN A CA  1 
ATOM 2825 C C   . ASN A 1 357 ? -9.300  11.304  152.489 1.00 31.97  ? 403 ASN A C   1 
ATOM 2826 O O   . ASN A 1 357 ? -8.659  12.359  152.451 1.00 42.98  ? 403 ASN A O   1 
ATOM 2827 C CB  . ASN A 1 357 ? -10.685 11.359  154.570 1.00 34.12  ? 403 ASN A CB  1 
ATOM 2828 C CG  . ASN A 1 357 ? -12.057 11.060  154.023 1.00 36.13  ? 403 ASN A CG  1 
ATOM 2829 O OD1 . ASN A 1 357 ? -12.244 10.926  152.816 1.00 44.86  ? 403 ASN A OD1 1 
ATOM 2830 N ND2 . ASN A 1 357 ? -13.034 10.975  154.909 1.00 35.52  ? 403 ASN A ND2 1 
ATOM 2831 N N   . LEU A 1 358 ? -9.781  10.704  151.405 1.00 29.15  ? 404 LEU A N   1 
ATOM 2832 C CA  . LEU A 1 358 ? -9.502  11.232  150.084 1.00 34.21  ? 404 LEU A CA  1 
ATOM 2833 C C   . LEU A 1 358 ? -10.772 11.284  149.248 1.00 41.49  ? 404 LEU A C   1 
ATOM 2834 O O   . LEU A 1 358 ? -11.647 10.422  149.387 1.00 46.65  ? 404 LEU A O   1 
ATOM 2835 C CB  . LEU A 1 358 ? -8.453  10.368  149.375 1.00 39.47  ? 404 LEU A CB  1 
ATOM 2836 C CG  . LEU A 1 358 ? -7.027  10.559  149.887 1.00 36.37  ? 404 LEU A CG  1 
ATOM 2837 C CD1 . LEU A 1 358 ? -6.044  9.738   149.075 1.00 36.19  ? 404 LEU A CD1 1 
ATOM 2838 C CD2 . LEU A 1 358 ? -6.657  12.029  149.870 1.00 36.46  ? 404 LEU A CD2 1 
ATOM 2839 N N   . PRO A 1 359 ? -10.904 12.279  148.378 1.00 45.65  ? 405 PRO A N   1 
ATOM 2840 C CA  . PRO A 1 359 ? -12.020 12.293  147.432 1.00 44.67  ? 405 PRO A CA  1 
ATOM 2841 C C   . PRO A 1 359 ? -11.740 11.393  146.238 1.00 48.79  ? 405 PRO A C   1 
ATOM 2842 O O   . PRO A 1 359 ? -10.598 11.044  145.937 1.00 53.81  ? 405 PRO A O   1 
ATOM 2843 C CB  . PRO A 1 359 ? -12.098 13.761  147.005 1.00 45.17  ? 405 PRO A CB  1 
ATOM 2844 C CG  . PRO A 1 359 ? -10.692 14.233  147.111 1.00 48.20  ? 405 PRO A CG  1 
ATOM 2845 C CD  . PRO A 1 359 ? -10.084 13.498  148.280 1.00 44.36  ? 405 PRO A CD  1 
ATOM 2846 N N   . GLY A 1 360 ? -12.815 11.024  145.555 1.00 47.87  ? 406 GLY A N   1 
ATOM 2847 C CA  . GLY A 1 360 ? -12.681 10.183  144.388 1.00 48.77  ? 406 GLY A CA  1 
ATOM 2848 C C   . GLY A 1 360 ? -12.338 8.748   144.754 1.00 50.92  ? 406 GLY A C   1 
ATOM 2849 O O   . GLY A 1 360 ? -12.363 8.337   145.914 1.00 51.04  ? 406 GLY A O   1 
ATOM 2850 N N   . GLU A 1 361 ? -11.999 7.982   143.720 1.00 57.79  ? 407 GLU A N   1 
ATOM 2851 C CA  . GLU A 1 361 ? -11.692 6.565   143.857 1.00 56.93  ? 407 GLU A CA  1 
ATOM 2852 C C   . GLU A 1 361 ? -10.223 6.251   143.620 1.00 59.68  ? 407 GLU A C   1 
ATOM 2853 O O   . GLU A 1 361 ? -9.606  5.541   144.420 1.00 62.42  ? 407 GLU A O   1 
ATOM 2854 C CB  . GLU A 1 361 ? -12.560 5.747   142.889 1.00 59.80  ? 407 GLU A CB  1 
ATOM 2855 C CG  . GLU A 1 361 ? -14.071 5.903   143.076 1.00 62.96  ? 407 GLU A CG  1 
ATOM 2856 C CD  . GLU A 1 361 ? -14.544 5.614   144.492 1.00 64.40  ? 407 GLU A CD  1 
ATOM 2857 O OE1 . GLU A 1 361 ? -14.411 6.494   145.370 1.00 61.50  ? 407 GLU A OE1 1 
ATOM 2858 O OE2 . GLU A 1 361 ? -15.055 4.501   144.728 1.00 65.15  ? 407 GLU A OE2 1 
ATOM 2859 N N   . ALA A 1 362 ? -9.641  6.760   142.538 1.00 60.89  ? 408 ALA A N   1 
ATOM 2860 C CA  . ALA A 1 362 ? -8.246  6.509   142.204 1.00 57.94  ? 408 ALA A CA  1 
ATOM 2861 C C   . ALA A 1 362 ? -7.397  7.701   142.625 1.00 59.75  ? 408 ALA A C   1 
ATOM 2862 O O   . ALA A 1 362 ? -7.675  8.838   142.228 1.00 62.68  ? 408 ALA A O   1 
ATOM 2863 C CB  . ALA A 1 362 ? -8.082  6.245   140.707 1.00 58.46  ? 408 ALA A CB  1 
ATOM 2864 N N   . HIS A 1 363 ? -6.366  7.438   143.422 1.00 50.68  ? 409 HIS A N   1 
ATOM 2865 C CA  . HIS A 1 363 ? -5.511  8.478   143.979 1.00 49.78  ? 409 HIS A CA  1 
ATOM 2866 C C   . HIS A 1 363 ? -4.092  8.314   143.460 1.00 50.61  ? 409 HIS A C   1 
ATOM 2867 O O   . HIS A 1 363 ? -3.498  7.239   143.590 1.00 51.56  ? 409 HIS A O   1 
ATOM 2868 C CB  . HIS A 1 363 ? -5.524  8.430   145.507 1.00 47.50  ? 409 HIS A CB  1 
ATOM 2869 C CG  . HIS A 1 363 ? -6.864  8.106   146.087 1.00 48.27  ? 409 HIS A CG  1 
ATOM 2870 N ND1 . HIS A 1 363 ? -7.960  8.927   145.933 1.00 48.87  ? 409 HIS A ND1 1 
ATOM 2871 C CD2 . HIS A 1 363 ? -7.287  7.047   146.817 1.00 48.06  ? 409 HIS A CD2 1 
ATOM 2872 C CE1 . HIS A 1 363 ? -8.999  8.390   146.547 1.00 47.72  ? 409 HIS A CE1 1 
ATOM 2873 N NE2 . HIS A 1 363 ? -8.617  7.249   147.091 1.00 50.20  ? 409 HIS A NE2 1 
ATOM 2874 N N   . SER A 1 364 ? -3.551  9.382   142.881 1.00 50.48  ? 410 SER A N   1 
ATOM 2875 C CA  . SER A 1 364 ? -2.187  9.353   142.382 1.00 48.52  ? 410 SER A CA  1 
ATOM 2876 C C   . SER A 1 364 ? -1.194  9.535   143.525 1.00 47.23  ? 410 SER A C   1 
ATOM 2877 O O   . SER A 1 364 ? -1.539  9.986   144.620 1.00 52.55  ? 410 SER A O   1 
ATOM 2878 C CB  . SER A 1 364 ? -1.980  10.439  141.327 1.00 51.47  ? 410 SER A CB  1 
ATOM 2879 O OG  . SER A 1 364 ? -2.684  11.619  141.669 1.00 52.92  ? 410 SER A OG  1 
ATOM 2880 N N   . ALA A 1 365 ? 0.060   9.167   143.256 1.00 43.95  ? 411 ALA A N   1 
ATOM 2881 C CA  . ALA A 1 365 ? 1.100   9.279   144.272 1.00 41.73  ? 411 ALA A CA  1 
ATOM 2882 C C   . ALA A 1 365 ? 1.328   10.728  144.678 1.00 44.17  ? 411 ALA A C   1 
ATOM 2883 O O   . ALA A 1 365 ? 1.443   11.034  145.871 1.00 44.44  ? 411 ALA A O   1 
ATOM 2884 C CB  . ALA A 1 365 ? 2.397   8.656   143.762 1.00 41.03  ? 411 ALA A CB  1 
ATOM 2885 N N   . GLU A 1 366 ? 1.390   11.636  143.701 1.00 52.40  ? 412 GLU A N   1 
ATOM 2886 C CA  . GLU A 1 366 ? 1.607   13.044  144.014 1.00 50.60  ? 412 GLU A CA  1 
ATOM 2887 C C   . GLU A 1 366 ? 0.440   13.618  144.804 1.00 45.66  ? 412 GLU A C   1 
ATOM 2888 O O   . GLU A 1 366 ? 0.640   14.391  145.747 1.00 50.31  ? 412 GLU A O   1 
ATOM 2889 C CB  . GLU A 1 366 ? 1.824   13.844  142.730 1.00 53.46  ? 412 GLU A CB  1 
ATOM 2890 C CG  . GLU A 1 366 ? 2.992   13.369  141.883 1.00 54.53  ? 412 GLU A CG  1 
ATOM 2891 C CD  . GLU A 1 366 ? 2.604   12.258  140.929 1.00 58.80  ? 412 GLU A CD  1 
ATOM 2892 O OE1 . GLU A 1 366 ? 1.428   12.219  140.509 1.00 58.37  ? 412 GLU A OE1 1 
ATOM 2893 O OE2 . GLU A 1 366 ? 3.473   11.425  140.597 1.00 56.24  ? 412 GLU A OE2 1 
ATOM 2894 N N   . MET A 1 367 ? -0.787  13.255  144.428 1.00 42.01  ? 413 MET A N   1 
ATOM 2895 C CA  . MET A 1 367 ? -1.957  13.750  145.142 1.00 44.81  ? 413 MET A CA  1 
ATOM 2896 C C   . MET A 1 367 ? -1.979  13.218  146.571 1.00 40.84  ? 413 MET A C   1 
ATOM 2897 O O   . MET A 1 367 ? -2.274  13.964  147.509 1.00 44.18  ? 413 MET A O   1 
ATOM 2898 C CB  . MET A 1 367 ? -3.219  13.371  144.359 1.00 47.18  ? 413 MET A CB  1 
ATOM 2899 C CG  . MET A 1 367 ? -4.548  14.019  144.774 1.00 50.38  ? 413 MET A CG  1 
ATOM 2900 S SD  . MET A 1 367 ? -5.093  13.871  146.479 1.00 63.04  ? 413 MET A SD  1 
ATOM 2901 C CE  . MET A 1 367 ? -5.262  12.096  146.570 1.00 50.72  ? 413 MET A CE  1 
ATOM 2902 N N   . ILE A 1 368 ? -1.635  11.943  146.760 1.00 39.85  ? 414 ILE A N   1 
ATOM 2903 C CA  . ILE A 1 368 ? -1.579  11.379  148.107 1.00 39.31  ? 414 ILE A CA  1 
ATOM 2904 C C   . ILE A 1 368 ? -0.514  12.084  148.938 1.00 41.99  ? 414 ILE A C   1 
ATOM 2905 O O   . ILE A 1 368 ? -0.727  12.393  150.116 1.00 46.22  ? 414 ILE A O   1 
ATOM 2906 C CB  . ILE A 1 368 ? -1.337  9.860   148.049 1.00 37.34  ? 414 ILE A CB  1 
ATOM 2907 C CG1 . ILE A 1 368 ? -2.601  9.136   147.592 1.00 43.25  ? 414 ILE A CG1 1 
ATOM 2908 C CG2 . ILE A 1 368 ? -0.911  9.332   149.405 1.00 29.87  ? 414 ILE A CG2 1 
ATOM 2909 C CD1 . ILE A 1 368 ? -2.381  7.677   147.278 1.00 38.14  ? 414 ILE A CD1 1 
ATOM 2910 N N   . ILE A 1 369 ? 0.652   12.348  148.340 1.00 42.21  ? 415 ILE A N   1 
ATOM 2911 C CA  . ILE A 1 369 ? 1.702   13.072  149.048 1.00 36.20  ? 415 ILE A CA  1 
ATOM 2912 C C   . ILE A 1 369 ? 1.253   14.470  149.443 1.00 41.84  ? 415 ILE A C   1 
ATOM 2913 O O   . ILE A 1 369 ? 1.457   14.881  150.591 1.00 45.78  ? 415 ILE A O   1 
ATOM 2914 C CB  . ILE A 1 369 ? 2.980   13.149  148.192 1.00 39.09  ? 415 ILE A CB  1 
ATOM 2915 C CG1 . ILE A 1 369 ? 3.707   11.809  148.195 1.00 36.10  ? 415 ILE A CG1 1 
ATOM 2916 C CG2 . ILE A 1 369 ? 3.904   14.235  148.708 1.00 40.61  ? 415 ILE A CG2 1 
ATOM 2917 C CD1 . ILE A 1 369 ? 4.279   11.440  149.540 1.00 36.64  ? 415 ILE A CD1 1 
ATOM 2918 N N   . GLU A 1 370 ? 0.635   15.210  148.526 1.00 39.93  ? 416 GLU A N   1 
ATOM 2919 C CA  . GLU A 1 370 ? 0.144   16.547  148.828 1.00 35.33  ? 416 GLU A CA  1 
ATOM 2920 C C   . GLU A 1 370 ? -1.031  16.545  149.792 1.00 32.03  ? 416 GLU A C   1 
ATOM 2921 O O   . GLU A 1 370 ? -1.310  17.578  150.407 1.00 37.70  ? 416 GLU A O   1 
ATOM 2922 C CB  . GLU A 1 370 ? -0.266  17.269  147.540 1.00 36.91  ? 416 GLU A CB  1 
ATOM 2923 C CG  . GLU A 1 370 ? 0.868   17.491  146.550 1.00 42.59  ? 416 GLU A CG  1 
ATOM 2924 C CD  . GLU A 1 370 ? 1.730   18.686  146.903 1.00 47.74  ? 416 GLU A CD  1 
ATOM 2925 O OE1 . GLU A 1 370 ? 1.170   19.772  147.161 1.00 51.65  ? 416 GLU A OE1 1 
ATOM 2926 O OE2 . GLU A 1 370 ? 2.971   18.542  146.916 1.00 43.41  ? 416 GLU A OE2 1 
ATOM 2927 N N   . ALA A 1 371 ? -1.724  15.419  149.937 1.00 29.69  ? 417 ALA A N   1 
ATOM 2928 C CA  . ALA A 1 371 ? -2.892  15.346  150.801 1.00 32.95  ? 417 ALA A CA  1 
ATOM 2929 C C   . ALA A 1 371 ? -2.551  15.121  152.265 1.00 28.37  ? 417 ALA A C   1 
ATOM 2930 O O   . ALA A 1 371 ? -3.464  15.093  153.095 1.00 30.00  ? 417 ALA A O   1 
ATOM 2931 C CB  . ALA A 1 371 ? -3.824  14.229  150.329 1.00 34.24  ? 417 ALA A CB  1 
ATOM 2932 N N   . THR A 1 372 ? -1.276  14.960  152.608 1.00 28.81  ? 418 THR A N   1 
ATOM 2933 C CA  . THR A 1 372 ? -0.886  14.672  153.982 1.00 32.52  ? 418 THR A CA  1 
ATOM 2934 C C   . THR A 1 372 ? 0.264   15.563  154.432 1.00 34.35  ? 418 THR A C   1 
ATOM 2935 O O   . THR A 1 372 ? 1.061   15.170  155.287 1.00 37.50  ? 418 THR A O   1 
ATOM 2936 C CB  . THR A 1 372 ? -0.510  13.200  154.147 1.00 32.72  ? 418 THR A CB  1 
ATOM 2937 O OG1 . THR A 1 372 ? 0.068   12.999  155.440 1.00 38.79  ? 418 THR A OG1 1 
ATOM 2938 C CG2 . THR A 1 372 ? 0.493   12.789  153.087 1.00 25.36  ? 418 THR A CG2 1 
ATOM 2939 N N   . ARG A 1 373 ? 0.366   16.767  153.867 1.00 35.11  ? 419 ARG A N   1 
ATOM 2940 C CA  . ARG A 1 373 ? 1.468   17.651  154.227 1.00 33.79  ? 419 ARG A CA  1 
ATOM 2941 C C   . ARG A 1 373 ? 1.298   18.228  155.625 1.00 36.30  ? 419 ARG A C   1 
ATOM 2942 O O   . ARG A 1 373 ? 2.289   18.426  156.336 1.00 34.66  ? 419 ARG A O   1 
ATOM 2943 C CB  . ARG A 1 373 ? 1.595   18.773  153.200 1.00 29.75  ? 419 ARG A CB  1 
ATOM 2944 C CG  . ARG A 1 373 ? 1.518   18.294  151.767 1.00 29.60  ? 419 ARG A CG  1 
ATOM 2945 C CD  . ARG A 1 373 ? 2.259   19.234  150.841 1.00 37.61  ? 419 ARG A CD  1 
ATOM 2946 N NE  . ARG A 1 373 ? 3.698   19.170  151.056 1.00 44.04  ? 419 ARG A NE  1 
ATOM 2947 C CZ  . ARG A 1 373 ? 4.602   19.208  150.088 1.00 45.94  ? 419 ARG A CZ  1 
ATOM 2948 N NH1 . ARG A 1 373 ? 4.250   19.331  148.819 1.00 44.33  ? 419 ARG A NH1 1 
ATOM 2949 N NH2 . ARG A 1 373 ? 5.891   19.123  150.400 1.00 39.59  ? 419 ARG A NH2 1 
ATOM 2950 N N   . LEU A 1 374 ? 0.063   18.507  156.035 1.00 31.44  ? 420 LEU A N   1 
ATOM 2951 C CA  . LEU A 1 374 ? -0.213  19.060  157.352 1.00 26.87  ? 420 LEU A CA  1 
ATOM 2952 C C   . LEU A 1 374 ? -0.513  17.992  158.394 1.00 31.04  ? 420 LEU A C   1 
ATOM 2953 O O   . LEU A 1 374 ? -0.706  18.328  159.566 1.00 33.61  ? 420 LEU A O   1 
ATOM 2954 C CB  . LEU A 1 374 ? -1.382  20.045  157.275 1.00 21.85  ? 420 LEU A CB  1 
ATOM 2955 C CG  . LEU A 1 374 ? -1.333  21.078  156.149 1.00 23.16  ? 420 LEU A CG  1 
ATOM 2956 C CD1 . LEU A 1 374 ? -2.563  21.964  156.180 1.00 30.30  ? 420 LEU A CD1 1 
ATOM 2957 C CD2 . LEU A 1 374 ? -0.071  21.915  156.244 1.00 29.57  ? 420 LEU A CD2 1 
ATOM 2958 N N   . ALA A 1 375 ? -0.561  16.722  158.000 1.00 25.71  ? 421 ALA A N   1 
ATOM 2959 C CA  . ALA A 1 375 ? -0.820  15.653  158.952 1.00 20.89  ? 421 ALA A CA  1 
ATOM 2960 C C   . ALA A 1 375 ? 0.385   15.441  159.860 1.00 27.21  ? 421 ALA A C   1 
ATOM 2961 O O   . ALA A 1 375 ? 1.538   15.503  159.428 1.00 38.63  ? 421 ALA A O   1 
ATOM 2962 C CB  . ALA A 1 375 ? -1.160  14.356  158.222 1.00 21.49  ? 421 ALA A CB  1 
ATOM 2963 N N   . THR A 1 376 ? 0.106   15.186  161.135 1.00 28.08  ? 422 THR A N   1 
ATOM 2964 C CA  . THR A 1 376 ? 1.165   15.021  162.127 1.00 31.79  ? 422 THR A CA  1 
ATOM 2965 C C   . THR A 1 376 ? 0.604   14.233  163.296 1.00 37.66  ? 422 THR A C   1 
ATOM 2966 O O   . THR A 1 376 ? -0.312  14.708  163.975 1.00 42.63  ? 422 THR A O   1 
ATOM 2967 C CB  . THR A 1 376 ? 1.692   16.375  162.599 1.00 29.43  ? 422 THR A CB  1 
ATOM 2968 O OG1 . THR A 1 376 ? 2.425   17.002  161.539 1.00 37.64  ? 422 THR A OG1 1 
ATOM 2969 C CG2 . THR A 1 376 ? 2.601   16.202  163.805 1.00 30.47  ? 422 THR A CG2 1 
ATOM 2970 N N   . MET A 1 377 ? 1.145   13.043  163.537 1.00 35.09  ? 423 MET A N   1 
ATOM 2971 C CA  . MET A 1 377 ? 0.715   12.208  164.646 1.00 34.48  ? 423 MET A CA  1 
ATOM 2972 C C   . MET A 1 377 ? 1.798   12.167  165.712 1.00 35.30  ? 423 MET A C   1 
ATOM 2973 O O   . MET A 1 377 ? 2.994   12.136  165.407 1.00 39.91  ? 423 MET A O   1 
ATOM 2974 C CB  . MET A 1 377 ? 0.392   10.778  164.197 1.00 35.06  ? 423 MET A CB  1 
ATOM 2975 C CG  . MET A 1 377 ? -0.507  10.678  162.984 1.00 35.01  ? 423 MET A CG  1 
ATOM 2976 S SD  . MET A 1 377 ? -0.091  9.250   161.969 1.00 49.74  ? 423 MET A SD  1 
ATOM 2977 C CE  . MET A 1 377 ? 0.005   7.976   163.219 1.00 38.80  ? 423 MET A CE  1 
ATOM 2978 N N   . PHE A 1 378 ? 1.368   12.170  166.967 1.00 29.47  ? 424 PHE A N   1 
ATOM 2979 C CA  . PHE A 1 378 ? 2.295   12.041  168.076 1.00 31.54  ? 424 PHE A CA  1 
ATOM 2980 C C   . PHE A 1 378 ? 2.792   10.603  168.181 1.00 37.28  ? 424 PHE A C   1 
ATOM 2981 O O   . PHE A 1 378 ? 2.113   9.653   167.786 1.00 37.59  ? 424 PHE A O   1 
ATOM 2982 C CB  . PHE A 1 378 ? 1.633   12.466  169.384 1.00 29.93  ? 424 PHE A CB  1 
ATOM 2983 C CG  . PHE A 1 378 ? 1.011   13.832  169.334 1.00 31.81  ? 424 PHE A CG  1 
ATOM 2984 C CD1 . PHE A 1 378 ? 1.560   14.832  168.551 1.00 31.90  ? 424 PHE A CD1 1 
ATOM 2985 C CD2 . PHE A 1 378 ? -0.116  14.118  170.082 1.00 35.33  ? 424 PHE A CD2 1 
ATOM 2986 C CE1 . PHE A 1 378 ? 0.989   16.085  168.506 1.00 31.91  ? 424 PHE A CE1 1 
ATOM 2987 C CE2 . PHE A 1 378 ? -0.688  15.372  170.042 1.00 34.55  ? 424 PHE A CE2 1 
ATOM 2988 C CZ  . PHE A 1 378 ? -0.135  16.355  169.253 1.00 35.81  ? 424 PHE A CZ  1 
ATOM 2989 N N   . GLN A 1 379 ? 3.998   10.451  168.721 1.00 39.16  ? 425 GLN A N   1 
ATOM 2990 C CA  . GLN A 1 379 ? 4.614   9.138   168.871 1.00 32.08  ? 425 GLN A CA  1 
ATOM 2991 C C   . GLN A 1 379 ? 4.785   8.728   170.324 1.00 35.09  ? 425 GLN A C   1 
ATOM 2992 O O   . GLN A 1 379 ? 4.292   7.668   170.724 1.00 42.03  ? 425 GLN A O   1 
ATOM 2993 C CB  . GLN A 1 379 ? 5.975   9.112   168.164 1.00 31.16  ? 425 GLN A CB  1 
ATOM 2994 C CG  . GLN A 1 379 ? 6.792   7.873   168.467 1.00 35.05  ? 425 GLN A CG  1 
ATOM 2995 C CD  . GLN A 1 379 ? 7.806   7.562   167.390 1.00 43.91  ? 425 GLN A CD  1 
ATOM 2996 O OE1 . GLN A 1 379 ? 8.699   8.362   167.114 1.00 44.46  ? 425 GLN A OE1 1 
ATOM 2997 N NE2 . GLN A 1 379 ? 7.683   6.390   166.783 1.00 41.97  ? 425 GLN A NE2 1 
ATOM 2998 N N   . VAL A 1 380 ? 5.483   9.528   171.124 1.00 34.67  ? 426 VAL A N   1 
ATOM 2999 C CA  . VAL A 1 380 ? 5.712   9.214   172.531 1.00 31.71  ? 426 VAL A CA  1 
ATOM 3000 C C   . VAL A 1 380 ? 5.513   10.480  173.346 1.00 36.11  ? 426 VAL A C   1 
ATOM 3001 O O   . VAL A 1 380 ? 5.565   11.592  172.814 1.00 43.29  ? 426 VAL A O   1 
ATOM 3002 C CB  . VAL A 1 380 ? 7.122   8.631   172.772 1.00 37.04  ? 426 VAL A CB  1 
ATOM 3003 C CG1 . VAL A 1 380 ? 7.312   7.333   172.005 1.00 39.41  ? 426 VAL A CG1 1 
ATOM 3004 C CG2 . VAL A 1 380 ? 8.183   9.641   172.382 1.00 32.45  ? 426 VAL A CG2 1 
ATOM 3005 N N   . LYS A 1 381 ? 5.279   10.306  174.643 1.00 36.70  ? 427 LYS A N   1 
ATOM 3006 C CA  . LYS A 1 381 ? 5.204   11.444  175.545 1.00 35.44  ? 427 LYS A CA  1 
ATOM 3007 C C   . LYS A 1 381 ? 6.603   11.918  175.911 1.00 35.48  ? 427 LYS A C   1 
ATOM 3008 O O   . LYS A 1 381 ? 7.514   11.113  176.119 1.00 40.95  ? 427 LYS A O   1 
ATOM 3009 C CB  . LYS A 1 381 ? 4.433   11.072  176.809 1.00 32.62  ? 427 LYS A CB  1 
ATOM 3010 C CG  . LYS A 1 381 ? 2.976   10.730  176.578 1.00 38.26  ? 427 LYS A CG  1 
ATOM 3011 C CD  . LYS A 1 381 ? 2.233   10.621  177.895 1.00 41.02  ? 427 LYS A CD  1 
ATOM 3012 C CE  . LYS A 1 381 ? 2.849   9.557   178.783 1.00 37.62  ? 427 LYS A CE  1 
ATOM 3013 N NZ  . LYS A 1 381 ? 2.199   9.500   180.119 1.00 38.19  ? 427 LYS A NZ  1 
ATOM 3014 N N   . ALA A 1 382 ? 6.774   13.234  175.986 1.00 41.12  ? 428 ALA A N   1 
ATOM 3015 C CA  . ALA A 1 382 ? 8.042   13.787  176.435 1.00 43.70  ? 428 ALA A CA  1 
ATOM 3016 C C   . ALA A 1 382 ? 8.234   13.513  177.920 1.00 44.70  ? 428 ALA A C   1 
ATOM 3017 O O   . ALA A 1 382 ? 7.303   13.647  178.718 1.00 44.20  ? 428 ALA A O   1 
ATOM 3018 C CB  . ALA A 1 382 ? 8.099   15.289  176.161 1.00 44.33  ? 428 ALA A CB  1 
ATOM 3019 N N   . VAL A 1 383 ? 9.447   13.125  178.288 1.00 50.49  ? 429 VAL A N   1 
ATOM 3020 C CA  . VAL A 1 383 ? 9.725   12.774  179.685 1.00 52.12  ? 429 VAL A CA  1 
ATOM 3021 C C   . VAL A 1 383 ? 9.755   14.046  180.525 1.00 53.41  ? 429 VAL A C   1 
ATOM 3022 O O   . VAL A 1 383 ? 10.542  14.962  180.230 1.00 50.16  ? 429 VAL A O   1 
ATOM 3023 C CB  . VAL A 1 383 ? 11.046  12.015  179.790 1.00 52.91  ? 429 VAL A CB  1 
ATOM 3024 C CG1 . VAL A 1 383 ? 11.146  11.317  181.136 1.00 52.50  ? 429 VAL A CG1 1 
ATOM 3025 C CG2 . VAL A 1 383 ? 11.169  11.012  178.655 1.00 51.95  ? 429 VAL A CG2 1 
ATOM 3026 N N   . PRO A 1 384 ? 8.932   14.154  181.571 1.00 55.57  ? 430 PRO A N   1 
ATOM 3027 C CA  . PRO A 1 384 ? 8.922   15.369  182.398 1.00 56.21  ? 430 PRO A CA  1 
ATOM 3028 C C   . PRO A 1 384 ? 10.070  15.354  183.396 1.00 58.56  ? 430 PRO A C   1 
ATOM 3029 O O   . PRO A 1 384 ? 10.250  14.387  184.139 1.00 55.58  ? 430 PRO A O   1 
ATOM 3030 C CB  . PRO A 1 384 ? 7.562   15.302  183.102 1.00 55.32  ? 430 PRO A CB  1 
ATOM 3031 C CG  . PRO A 1 384 ? 7.268   13.844  183.189 1.00 55.24  ? 430 PRO A CG  1 
ATOM 3032 C CD  . PRO A 1 384 ? 7.893   13.193  181.981 1.00 53.42  ? 430 PRO A CD  1 
ATOM 3033 N N   . ALA A 1 385 ? 10.849  16.431  183.412 1.00 66.85  ? 431 ALA A N   1 
ATOM 3034 C CA  . ALA A 1 385 ? 11.925  16.575  184.382 1.00 61.67  ? 431 ALA A CA  1 
ATOM 3035 C C   . ALA A 1 385 ? 11.336  16.993  185.723 1.00 66.26  ? 431 ALA A C   1 
ATOM 3036 O O   . ALA A 1 385 ? 10.745  18.072  185.839 1.00 69.36  ? 431 ALA A O   1 
ATOM 3037 C CB  . ALA A 1 385 ? 12.951  17.597  183.897 1.00 61.49  ? 431 ALA A CB  1 
ATOM 3038 N N   . GLY A 1 386 ? 11.500  16.146  186.732 1.00 75.03  ? 432 GLY A N   1 
ATOM 3039 C CA  . GLY A 1 386 ? 10.930  16.392  188.043 1.00 77.62  ? 432 GLY A CA  1 
ATOM 3040 C C   . GLY A 1 386 ? 9.710   15.530  188.304 1.00 81.08  ? 432 GLY A C   1 
ATOM 3041 O O   . GLY A 1 386 ? 9.245   14.762  187.456 1.00 78.70  ? 432 GLY A O   1 
ATOM 3042 N N   . ASP A 1 387 ? 9.186   15.672  189.519 1.00 90.16  ? 433 ASP A N   1 
ATOM 3043 C CA  . ASP A 1 387 ? 8.050   14.883  189.975 1.00 89.07  ? 433 ASP A CA  1 
ATOM 3044 C C   . ASP A 1 387 ? 6.705   15.515  189.639 1.00 90.24  ? 433 ASP A C   1 
ATOM 3045 O O   . ASP A 1 387 ? 5.670   14.870  189.833 1.00 89.07  ? 433 ASP A O   1 
ATOM 3046 C CB  . ASP A 1 387 ? 8.144   14.658  191.486 1.00 88.36  ? 433 ASP A CB  1 
ATOM 3047 C CG  . ASP A 1 387 ? 8.627   15.887  192.227 1.00 89.96  ? 433 ASP A CG  1 
ATOM 3048 O OD1 . ASP A 1 387 ? 9.635   16.484  191.797 1.00 89.65  ? 433 ASP A OD1 1 
ATOM 3049 O OD2 . ASP A 1 387 ? 7.996   16.259  193.239 1.00 90.73  ? 433 ASP A OD2 1 
ATOM 3050 N N   . THR A 1 388 ? 6.691   16.749  189.144 1.00 82.94  ? 434 THR A N   1 
ATOM 3051 C CA  . THR A 1 388 ? 5.460   17.453  188.807 1.00 81.05  ? 434 THR A CA  1 
ATOM 3052 C C   . THR A 1 388 ? 5.362   17.569  187.292 1.00 80.43  ? 434 THR A C   1 
ATOM 3053 O O   . THR A 1 388 ? 6.287   18.065  186.643 1.00 81.94  ? 434 THR A O   1 
ATOM 3054 C CB  . THR A 1 388 ? 5.419   18.835  189.457 1.00 80.23  ? 434 THR A CB  1 
ATOM 3055 O OG1 . THR A 1 388 ? 6.072   18.783  190.731 1.00 80.23  ? 434 THR A OG1 1 
ATOM 3056 C CG2 . THR A 1 388 ? 3.980   19.284  189.651 1.00 78.36  ? 434 THR A CG2 1 
ATOM 3057 N N   . SER A 1 389 ? 4.246   17.107  186.736 1.00 72.19  ? 435 SER A N   1 
ATOM 3058 C CA  . SER A 1 389 ? 4.044   17.063  185.291 1.00 72.51  ? 435 SER A CA  1 
ATOM 3059 C C   . SER A 1 389 ? 2.655   17.586  184.940 1.00 73.21  ? 435 SER A C   1 
ATOM 3060 O O   . SER A 1 389 ? 1.875   16.925  184.255 1.00 76.53  ? 435 SER A O   1 
ATOM 3061 C CB  . SER A 1 389 ? 4.250   15.650  184.752 1.00 72.80  ? 435 SER A CB  1 
ATOM 3062 O OG  . SER A 1 389 ? 4.114   15.623  183.343 1.00 73.86  ? 435 SER A OG  1 
ATOM 3063 N N   . LYS A 1 390 ? 2.327   18.778  185.440 1.00 62.14  ? 436 LYS A N   1 
ATOM 3064 C CA  . LYS A 1 390 ? 1.001   19.343  185.196 1.00 64.12  ? 436 LYS A CA  1 
ATOM 3065 C C   . LYS A 1 390 ? 0.618   19.384  183.719 1.00 64.66  ? 436 LYS A C   1 
ATOM 3066 O O   . LYS A 1 390 ? -0.528  19.022  183.403 1.00 66.30  ? 436 LYS A O   1 
ATOM 3067 C CB  . LYS A 1 390 ? 0.909   20.737  185.830 1.00 62.49  ? 436 LYS A CB  1 
ATOM 3068 C CG  . LYS A 1 390 ? 0.756   20.720  187.345 1.00 64.56  ? 436 LYS A CG  1 
ATOM 3069 C CD  . LYS A 1 390 ? 0.356   22.082  187.907 1.00 62.31  ? 436 LYS A CD  1 
ATOM 3070 C CE  . LYS A 1 390 ? -0.720  22.783  187.083 1.00 62.02  ? 436 LYS A CE  1 
ATOM 3071 N NZ  . LYS A 1 390 ? -1.841  21.892  186.659 1.00 62.17  ? 436 LYS A NZ  1 
ATOM 3072 N N   . PRO A 1 391 ? 1.474   19.795  182.787 1.00 56.49  ? 437 PRO A N   1 
ATOM 3073 C CA  . PRO A 1 391 ? 1.161   19.614  181.369 1.00 52.39  ? 437 PRO A CA  1 
ATOM 3074 C C   . PRO A 1 391 ? 1.696   18.279  180.861 1.00 57.44  ? 437 PRO A C   1 
ATOM 3075 O O   . PRO A 1 391 ? 2.505   17.613  181.508 1.00 58.21  ? 437 PRO A O   1 
ATOM 3076 C CB  . PRO A 1 391 ? 1.893   20.784  180.709 1.00 47.30  ? 437 PRO A CB  1 
ATOM 3077 C CG  . PRO A 1 391 ? 3.111   20.919  181.532 1.00 54.05  ? 437 PRO A CG  1 
ATOM 3078 C CD  . PRO A 1 391 ? 2.696   20.606  182.954 1.00 55.19  ? 437 PRO A CD  1 
ATOM 3079 N N   . VAL A 1 392 ? 1.220   17.897  179.679 1.00 51.74  ? 438 VAL A N   1 
ATOM 3080 C CA  . VAL A 1 392 ? 1.670   16.687  179.003 1.00 48.01  ? 438 VAL A CA  1 
ATOM 3081 C C   . VAL A 1 392 ? 2.060   17.050  177.579 1.00 46.50  ? 438 VAL A C   1 
ATOM 3082 O O   . VAL A 1 392 ? 1.272   17.664  176.852 1.00 47.23  ? 438 VAL A O   1 
ATOM 3083 C CB  . VAL A 1 392 ? 0.595   15.586  179.010 1.00 44.64  ? 438 VAL A CB  1 
ATOM 3084 C CG1 . VAL A 1 392 ? 1.043   14.409  178.167 1.00 44.19  ? 438 VAL A CG1 1 
ATOM 3085 C CG2 . VAL A 1 392 ? 0.330   15.135  180.430 1.00 46.42  ? 438 VAL A CG2 1 
ATOM 3086 N N   . LEU A 1 393 ? 3.270   16.666  177.184 1.00 41.12  ? 439 LEU A N   1 
ATOM 3087 C CA  . LEU A 1 393 ? 3.817   16.988  175.876 1.00 40.43  ? 439 LEU A CA  1 
ATOM 3088 C C   . LEU A 1 393 ? 4.129   15.700  175.131 1.00 40.82  ? 439 LEU A C   1 
ATOM 3089 O O   . LEU A 1 393 ? 4.613   14.732  175.725 1.00 47.81  ? 439 LEU A O   1 
ATOM 3090 C CB  . LEU A 1 393 ? 5.081   17.841  176.005 1.00 39.35  ? 439 LEU A CB  1 
ATOM 3091 C CG  . LEU A 1 393 ? 4.925   19.180  176.730 1.00 42.67  ? 439 LEU A CG  1 
ATOM 3092 C CD1 . LEU A 1 393 ? 6.217   19.976  176.672 1.00 42.96  ? 439 LEU A CD1 1 
ATOM 3093 C CD2 . LEU A 1 393 ? 3.775   19.981  176.154 1.00 39.71  ? 439 LEU A CD2 1 
ATOM 3094 N N   . TYR A 1 394 ? 3.853   15.690  173.832 1.00 33.06  ? 440 TYR A N   1 
ATOM 3095 C CA  . TYR A 1 394 ? 4.031   14.510  172.999 1.00 33.96  ? 440 TYR A CA  1 
ATOM 3096 C C   . TYR A 1 394 ? 5.089   14.785  171.941 1.00 35.24  ? 440 TYR A C   1 
ATOM 3097 O O   . TYR A 1 394 ? 5.020   15.798  171.238 1.00 37.99  ? 440 TYR A O   1 
ATOM 3098 C CB  . TYR A 1 394 ? 2.715   14.105  172.333 1.00 36.62  ? 440 TYR A CB  1 
ATOM 3099 C CG  . TYR A 1 394 ? 1.554   13.970  173.289 1.00 39.64  ? 440 TYR A CG  1 
ATOM 3100 C CD1 . TYR A 1 394 ? 1.294   12.768  173.930 1.00 34.62  ? 440 TYR A CD1 1 
ATOM 3101 C CD2 . TYR A 1 394 ? 0.714   15.043  173.545 1.00 42.60  ? 440 TYR A CD2 1 
ATOM 3102 C CE1 . TYR A 1 394 ? 0.233   12.641  174.803 1.00 34.37  ? 440 TYR A CE1 1 
ATOM 3103 C CE2 . TYR A 1 394 ? -0.347  14.926  174.415 1.00 42.35  ? 440 TYR A CE2 1 
ATOM 3104 C CZ  . TYR A 1 394 ? -0.583  13.724  175.041 1.00 41.78  ? 440 TYR A CZ  1 
ATOM 3105 O OH  . TYR A 1 394 ? -1.643  13.607  175.909 1.00 46.73  ? 440 TYR A OH  1 
ATOM 3106 N N   . LEU A 1 395 ? 6.056   13.885  171.830 1.00 35.54  ? 441 LEU A N   1 
ATOM 3107 C CA  . LEU A 1 395 ? 7.096   14.005  170.815 1.00 28.50  ? 441 LEU A CA  1 
ATOM 3108 C C   . LEU A 1 395 ? 6.603   13.419  169.500 1.00 32.22  ? 441 LEU A C   1 
ATOM 3109 O O   . LEU A 1 395 ? 6.192   12.254  169.466 1.00 39.33  ? 441 LEU A O   1 
ATOM 3110 C CB  . LEU A 1 395 ? 8.364   13.287  171.249 1.00 33.49  ? 441 LEU A CB  1 
ATOM 3111 C CG  . LEU A 1 395 ? 9.041   13.799  172.520 1.00 39.68  ? 441 LEU A CG  1 
ATOM 3112 C CD1 . LEU A 1 395 ? 10.240  12.937  172.860 1.00 42.00  ? 441 LEU A CD1 1 
ATOM 3113 C CD2 . LEU A 1 395 ? 9.453   15.249  172.358 1.00 36.30  ? 441 LEU A CD2 1 
ATOM 3114 N N   . PRO A 1 396 ? 6.620   14.179  168.413 1.00 32.08  ? 442 PRO A N   1 
ATOM 3115 C CA  . PRO A 1 396 ? 6.143   13.653  167.134 1.00 31.73  ? 442 PRO A CA  1 
ATOM 3116 C C   . PRO A 1 396 ? 7.110   12.641  166.540 1.00 41.48  ? 442 PRO A C   1 
ATOM 3117 O O   . PRO A 1 396 ? 8.308   12.630  166.828 1.00 45.96  ? 442 PRO A O   1 
ATOM 3118 C CB  . PRO A 1 396 ? 6.053   14.902  166.253 1.00 32.62  ? 442 PRO A CB  1 
ATOM 3119 C CG  . PRO A 1 396 ? 7.100   15.802  166.803 1.00 35.54  ? 442 PRO A CG  1 
ATOM 3120 C CD  . PRO A 1 396 ? 7.138   15.552  168.288 1.00 37.06  ? 442 PRO A CD  1 
ATOM 3121 N N   . ASN A 1 397 ? 6.557   11.776  165.696 1.00 41.17  ? 443 ASN A N   1 
ATOM 3122 C CA  . ASN A 1 397 ? 7.350   10.837  164.919 1.00 39.01  ? 443 ASN A CA  1 
ATOM 3123 C C   . ASN A 1 397 ? 8.069   11.524  163.766 1.00 40.20  ? 443 ASN A C   1 
ATOM 3124 O O   . ASN A 1 397 ? 9.138   11.066  163.353 1.00 42.29  ? 443 ASN A O   1 
ATOM 3125 C CB  . ASN A 1 397 ? 6.438   9.713   164.397 1.00 40.78  ? 443 ASN A CB  1 
ATOM 3126 C CG  . ASN A 1 397 ? 7.202   8.544   163.785 1.00 48.08  ? 443 ASN A CG  1 
ATOM 3127 O OD1 . ASN A 1 397 ? 8.142   8.716   163.011 1.00 46.66  ? 443 ASN A OD1 1 
ATOM 3128 N ND2 . ASN A 1 397 ? 6.785   7.334   164.135 1.00 44.31  ? 443 ASN A ND2 1 
ATOM 3129 N N   . GLY A 1 398 ? 7.536   12.642  163.286 1.00 40.04  ? 444 GLY A N   1 
ATOM 3130 C CA  . GLY A 1 398 ? 8.087   13.354  162.153 1.00 36.79  ? 444 GLY A CA  1 
ATOM 3131 C C   . GLY A 1 398 ? 7.003   14.156  161.468 1.00 43.84  ? 444 GLY A C   1 
ATOM 3132 O O   . GLY A 1 398 ? 5.888   13.662  161.282 1.00 49.16  ? 444 GLY A O   1 
ATOM 3133 N N   . PHE A 1 399 ? 7.307   15.397  161.101 1.00 36.28  ? 445 PHE A N   1 
ATOM 3134 C CA  . PHE A 1 399 ? 6.324   16.295  160.518 1.00 30.17  ? 445 PHE A CA  1 
ATOM 3135 C C   . PHE A 1 399 ? 6.872   16.886  159.229 1.00 32.59  ? 445 PHE A C   1 
ATOM 3136 O O   . PHE A 1 399 ? 8.062   16.777  158.923 1.00 35.10  ? 445 PHE A O   1 
ATOM 3137 C CB  . PHE A 1 399 ? 5.937   17.412  161.497 1.00 32.06  ? 445 PHE A CB  1 
ATOM 3138 C CG  . PHE A 1 399 ? 7.099   17.994  162.246 1.00 32.53  ? 445 PHE A CG  1 
ATOM 3139 C CD1 . PHE A 1 399 ? 7.858   19.010  161.694 1.00 29.15  ? 445 PHE A CD1 1 
ATOM 3140 C CD2 . PHE A 1 399 ? 7.434   17.524  163.502 1.00 34.55  ? 445 PHE A CD2 1 
ATOM 3141 C CE1 . PHE A 1 399 ? 8.924   19.545  162.382 1.00 30.82  ? 445 PHE A CE1 1 
ATOM 3142 C CE2 . PHE A 1 399 ? 8.500   18.055  164.193 1.00 31.83  ? 445 PHE A CE2 1 
ATOM 3143 C CZ  . PHE A 1 399 ? 9.246   19.068  163.633 1.00 31.51  ? 445 PHE A CZ  1 
ATOM 3144 N N   . GLY A 1 400 ? 5.984   17.509  158.466 1.00 26.20  ? 446 GLY A N   1 
ATOM 3145 C CA  . GLY A 1 400 ? 6.352   18.130  157.214 1.00 25.40  ? 446 GLY A CA  1 
ATOM 3146 C C   . GLY A 1 400 ? 6.863   19.540  157.413 1.00 27.77  ? 446 GLY A C   1 
ATOM 3147 O O   . GLY A 1 400 ? 7.185   19.969  158.524 1.00 35.90  ? 446 GLY A O   1 
ATOM 3148 N N   . THR A 1 401 ? 6.935   20.276  156.303 1.00 27.28  ? 447 THR A N   1 
ATOM 3149 C CA  . THR A 1 401 ? 7.438   21.643  156.345 1.00 27.25  ? 447 THR A CA  1 
ATOM 3150 C C   . THR A 1 401 ? 6.517   22.581  157.113 1.00 28.21  ? 447 THR A C   1 
ATOM 3151 O O   . THR A 1 401 ? 6.962   23.654  157.534 1.00 29.89  ? 447 THR A O   1 
ATOM 3152 C CB  . THR A 1 401 ? 7.646   22.168  154.926 1.00 25.86  ? 447 THR A CB  1 
ATOM 3153 O OG1 . THR A 1 401 ? 6.576   21.715  154.088 1.00 32.33  ? 447 THR A OG1 1 
ATOM 3154 C CG2 . THR A 1 401 ? 8.963   21.666  154.364 1.00 26.73  ? 447 THR A CG2 1 
ATOM 3155 N N   . GLU A 1 402 ? 5.254   22.210  157.303 1.00 36.67  ? 448 GLU A N   1 
ATOM 3156 C CA  . GLU A 1 402 ? 4.285   23.035  158.010 1.00 30.93  ? 448 GLU A CA  1 
ATOM 3157 C C   . GLU A 1 402 ? 3.583   22.211  159.079 1.00 30.56  ? 448 GLU A C   1 
ATOM 3158 O O   . GLU A 1 402 ? 3.286   21.031  158.870 1.00 35.41  ? 448 GLU A O   1 
ATOM 3159 C CB  . GLU A 1 402 ? 3.248   23.618  157.050 1.00 29.40  ? 448 GLU A CB  1 
ATOM 3160 C CG  . GLU A 1 402 ? 3.841   24.313  155.843 1.00 35.08  ? 448 GLU A CG  1 
ATOM 3161 C CD  . GLU A 1 402 ? 3.923   23.408  154.631 1.00 46.87  ? 448 GLU A CD  1 
ATOM 3162 O OE1 . GLU A 1 402 ? 3.397   22.278  154.693 1.00 40.67  ? 448 GLU A OE1 1 
ATOM 3163 O OE2 . GLU A 1 402 ? 4.514   23.826  153.613 1.00 47.81  ? 448 GLU A OE2 1 
ATOM 3164 N N   . VAL A 1 403 ? 3.319   22.836  160.222 1.00 23.88  ? 449 VAL A N   1 
ATOM 3165 C CA  . VAL A 1 403 ? 2.537   22.232  161.292 1.00 28.37  ? 449 VAL A CA  1 
ATOM 3166 C C   . VAL A 1 403 ? 1.405   23.182  161.654 1.00 27.14  ? 449 VAL A C   1 
ATOM 3167 O O   . VAL A 1 403 ? 1.608   24.396  161.756 1.00 30.92  ? 449 VAL A O   1 
ATOM 3168 C CB  . VAL A 1 403 ? 3.399   21.904  162.529 1.00 27.28  ? 449 VAL A CB  1 
ATOM 3169 C CG1 . VAL A 1 403 ? 4.275   20.699  162.250 1.00 28.28  ? 449 VAL A CG1 1 
ATOM 3170 C CG2 . VAL A 1 403 ? 4.246   23.093  162.924 1.00 27.22  ? 449 VAL A CG2 1 
ATOM 3171 N N   . VAL A 1 404 ? 0.211   22.627  161.833 1.00 28.13  ? 450 VAL A N   1 
ATOM 3172 C CA  . VAL A 1 404 ? -0.981  23.401  162.152 1.00 30.51  ? 450 VAL A CA  1 
ATOM 3173 C C   . VAL A 1 404 ? -1.126  23.447  163.666 1.00 29.49  ? 450 VAL A C   1 
ATOM 3174 O O   . VAL A 1 404 ? -1.072  22.408  164.333 1.00 39.19  ? 450 VAL A O   1 
ATOM 3175 C CB  . VAL A 1 404 ? -2.232  22.800  161.495 1.00 27.65  ? 450 VAL A CB  1 
ATOM 3176 C CG1 . VAL A 1 404 ? -3.480  23.507  161.984 1.00 24.87  ? 450 VAL A CG1 1 
ATOM 3177 C CG2 . VAL A 1 404 ? -2.126  22.886  159.985 1.00 24.70  ? 450 VAL A CG2 1 
ATOM 3178 N N   . ASN A 1 405 ? -1.299  24.649  164.212 1.00 22.77  ? 451 ASN A N   1 
ATOM 3179 C CA  . ASN A 1 405 ? -1.460  24.816  165.652 1.00 24.44  ? 451 ASN A CA  1 
ATOM 3180 C C   . ASN A 1 405 ? -2.932  24.874  166.050 1.00 35.30  ? 451 ASN A C   1 
ATOM 3181 O O   . ASN A 1 405 ? -3.385  24.099  166.897 1.00 42.40  ? 451 ASN A O   1 
ATOM 3182 C CB  . ASN A 1 405 ? -0.730  26.079  166.117 1.00 24.15  ? 451 ASN A CB  1 
ATOM 3183 C CG  . ASN A 1 405 ? 0.614   26.249  165.452 1.00 36.35  ? 451 ASN A CG  1 
ATOM 3184 O OD1 . ASN A 1 405 ? 0.696   26.602  164.277 1.00 41.02  ? 451 ASN A OD1 1 
ATOM 3185 N ND2 . ASN A 1 405 ? 1.680   26.010  166.203 1.00 40.79  ? 451 ASN A ND2 1 
ATOM 3186 N N   . ASP A 1 406 ? -3.684  25.793  165.453 1.00 33.87  ? 452 ASP A N   1 
ATOM 3187 C CA  . ASP A 1 406 ? -5.088  25.988  165.776 1.00 26.05  ? 452 ASP A CA  1 
ATOM 3188 C C   . ASP A 1 406 ? -5.886  26.152  164.492 1.00 34.63  ? 452 ASP A C   1 
ATOM 3189 O O   . ASP A 1 406 ? -5.346  26.118  163.384 1.00 40.37  ? 452 ASP A O   1 
ATOM 3190 C CB  . ASP A 1 406 ? -5.295  27.214  166.674 1.00 38.14  ? 452 ASP A CB  1 
ATOM 3191 C CG  . ASP A 1 406 ? -4.191  27.385  167.694 1.00 45.00  ? 452 ASP A CG  1 
ATOM 3192 O OD1 . ASP A 1 406 ? -4.124  26.575  168.640 1.00 43.36  ? 452 ASP A OD1 1 
ATOM 3193 O OD2 . ASP A 1 406 ? -3.388  28.331  167.549 1.00 42.25  ? 452 ASP A OD2 1 
ATOM 3194 N N   . TYR A 1 407 ? -7.193  26.322  164.660 1.00 32.76  ? 453 TYR A N   1 
ATOM 3195 C CA  . TYR A 1 407 ? -8.093  26.718  163.588 1.00 25.25  ? 453 TYR A CA  1 
ATOM 3196 C C   . TYR A 1 407 ? -8.957  27.858  164.099 1.00 30.76  ? 453 TYR A C   1 
ATOM 3197 O O   . TYR A 1 407 ? -9.537  27.758  165.184 1.00 41.27  ? 453 TYR A O   1 
ATOM 3198 C CB  . TYR A 1 407 ? -8.977  25.556  163.137 1.00 26.87  ? 453 TYR A CB  1 
ATOM 3199 C CG  . TYR A 1 407 ? -8.221  24.351  162.644 1.00 28.25  ? 453 TYR A CG  1 
ATOM 3200 C CD1 . TYR A 1 407 ? -7.858  24.234  161.312 1.00 27.23  ? 453 TYR A CD1 1 
ATOM 3201 C CD2 . TYR A 1 407 ? -7.882  23.322  163.509 1.00 25.68  ? 453 TYR A CD2 1 
ATOM 3202 C CE1 . TYR A 1 407 ? -7.171  23.132  160.858 1.00 28.47  ? 453 TYR A CE1 1 
ATOM 3203 C CE2 . TYR A 1 407 ? -7.196  22.217  163.063 1.00 28.71  ? 453 TYR A CE2 1 
ATOM 3204 C CZ  . TYR A 1 407 ? -6.845  22.126  161.737 1.00 29.97  ? 453 TYR A CZ  1 
ATOM 3205 O OH  . TYR A 1 407 ? -6.160  21.023  161.291 1.00 31.40  ? 453 TYR A OH  1 
ATOM 3206 N N   . THR A 1 408 ? -9.046  28.935  163.326 1.00 33.37  ? 454 THR A N   1 
ATOM 3207 C CA  . THR A 1 408 ? -9.866  30.081  163.689 1.00 29.22  ? 454 THR A CA  1 
ATOM 3208 C C   . THR A 1 408 ? -11.054 30.162  162.745 1.00 30.48  ? 454 THR A C   1 
ATOM 3209 O O   . THR A 1 408 ? -10.877 30.209  161.525 1.00 34.33  ? 454 THR A O   1 
ATOM 3210 C CB  . THR A 1 408 ? -9.067  31.383  163.642 1.00 32.78  ? 454 THR A CB  1 
ATOM 3211 O OG1 . THR A 1 408 ? -7.809  31.197  164.301 1.00 45.79  ? 454 THR A OG1 1 
ATOM 3212 C CG2 . THR A 1 408 ? -9.834  32.490  164.335 1.00 33.62  ? 454 THR A CG2 1 
ATOM 3213 N N   . MET A 1 409 ? -12.256 30.179  163.312 1.00 32.78  ? 455 MET A N   1 
ATOM 3214 C CA  . MET A 1 409 ? -13.485 30.281  162.540 1.00 33.84  ? 455 MET A CA  1 
ATOM 3215 C C   . MET A 1 409 ? -14.231 31.544  162.936 1.00 37.55  ? 455 MET A C   1 
ATOM 3216 O O   . MET A 1 409 ? -14.359 31.855  164.124 1.00 41.41  ? 455 MET A O   1 
ATOM 3217 C CB  . MET A 1 409 ? -14.386 29.067  162.755 1.00 34.49  ? 455 MET A CB  1 
ATOM 3218 C CG  . MET A 1 409 ? -15.396 28.854  161.644 1.00 37.90  ? 455 MET A CG  1 
ATOM 3219 S SD  . MET A 1 409 ? -16.338 27.343  161.878 1.00 43.08  ? 455 MET A SD  1 
ATOM 3220 C CE  . MET A 1 409 ? -16.529 27.372  163.653 1.00 37.82  ? 455 MET A CE  1 
ATOM 3221 N N   . ILE A 1 410 ? -14.730 32.264  161.936 1.00 32.77  ? 456 ILE A N   1 
ATOM 3222 C CA  . ILE A 1 410 ? -15.464 33.506  162.139 1.00 35.95  ? 456 ILE A CA  1 
ATOM 3223 C C   . ILE A 1 410 ? -16.894 33.292  161.668 1.00 37.19  ? 456 ILE A C   1 
ATOM 3224 O O   . ILE A 1 410 ? -17.120 32.857  160.534 1.00 37.06  ? 456 ILE A O   1 
ATOM 3225 C CB  . ILE A 1 410 ? -14.810 34.683  161.393 1.00 31.17  ? 456 ILE A CB  1 
ATOM 3226 C CG1 . ILE A 1 410 ? -13.286 34.571  161.453 1.00 30.19  ? 456 ILE A CG1 1 
ATOM 3227 C CG2 . ILE A 1 410 ? -15.267 36.003  161.979 1.00 32.68  ? 456 ILE A CG2 1 
ATOM 3228 C CD1 . ILE A 1 410 ? -12.707 34.804  162.817 1.00 32.56  ? 456 ILE A CD1 1 
ATOM 3229 N N   . SER A 1 411 ? -17.854 33.598  162.537 1.00 36.22  ? 457 SER A N   1 
ATOM 3230 C CA  . SER A 1 411 ? -19.260 33.395  162.226 1.00 36.29  ? 457 SER A CA  1 
ATOM 3231 C C   . SER A 1 411 ? -20.088 34.450  162.943 1.00 40.98  ? 457 SER A C   1 
ATOM 3232 O O   . SER A 1 411 ? -19.625 35.098  163.884 1.00 41.60  ? 457 SER A O   1 
ATOM 3233 C CB  . SER A 1 411 ? -19.725 31.990  162.621 1.00 39.87  ? 457 SER A CB  1 
ATOM 3234 O OG  . SER A 1 411 ? -21.135 31.884  162.549 1.00 42.60  ? 457 SER A OG  1 
ATOM 3235 N N   . VAL A 1 412 ? -21.323 34.614  162.481 1.00 43.96  ? 458 VAL A N   1 
ATOM 3236 C CA  . VAL A 1 412 ? -22.226 35.615  163.037 1.00 39.84  ? 458 VAL A CA  1 
ATOM 3237 C C   . VAL A 1 412 ? -22.744 35.145  164.388 1.00 40.47  ? 458 VAL A C   1 
ATOM 3238 O O   . VAL A 1 412 ? -23.130 33.982  164.556 1.00 43.59  ? 458 VAL A O   1 
ATOM 3239 C CB  . VAL A 1 412 ? -23.386 35.896  162.068 1.00 38.67  ? 458 VAL A CB  1 
ATOM 3240 C CG1 . VAL A 1 412 ? -24.126 37.148  162.490 1.00 45.48  ? 458 VAL A CG1 1 
ATOM 3241 C CG2 . VAL A 1 412 ? -22.869 36.045  160.655 1.00 40.06  ? 458 VAL A CG2 1 
ATOM 3242 N N   . ASP A 1 413 ? -22.753 36.054  165.358 1.00 48.86  ? 459 ASP A N   1 
ATOM 3243 C CA  . ASP A 1 413 ? -23.315 35.751  166.665 1.00 51.51  ? 459 ASP A CA  1 
ATOM 3244 C C   . ASP A 1 413 ? -24.827 35.588  166.570 1.00 54.63  ? 459 ASP A C   1 
ATOM 3245 O O   . ASP A 1 413 ? -25.493 36.263  165.781 1.00 54.12  ? 459 ASP A O   1 
ATOM 3246 C CB  . ASP A 1 413 ? -22.972 36.858  167.659 1.00 52.18  ? 459 ASP A CB  1 
ATOM 3247 C CG  . ASP A 1 413 ? -23.192 36.438  169.095 1.00 56.77  ? 459 ASP A CG  1 
ATOM 3248 O OD1 . ASP A 1 413 ? -23.322 35.221  169.346 1.00 54.77  ? 459 ASP A OD1 1 
ATOM 3249 O OD2 . ASP A 1 413 ? -23.237 37.324  169.973 1.00 59.52  ? 459 ASP A OD2 1 
ATOM 3250 N N   . LYS A 1 414 ? -25.370 34.680  167.383 1.00 52.61  ? 460 LYS A N   1 
ATOM 3251 C CA  . LYS A 1 414 ? -26.812 34.463  167.382 1.00 51.24  ? 460 LYS A CA  1 
ATOM 3252 C C   . LYS A 1 414 ? -27.554 35.582  168.101 1.00 52.97  ? 460 LYS A C   1 
ATOM 3253 O O   . LYS A 1 414 ? -28.710 35.867  167.771 1.00 55.22  ? 460 LYS A O   1 
ATOM 3254 C CB  . LYS A 1 414 ? -27.143 33.116  168.024 1.00 53.28  ? 460 LYS A CB  1 
ATOM 3255 C CG  . LYS A 1 414 ? -26.142 32.018  167.711 1.00 55.00  ? 460 LYS A CG  1 
ATOM 3256 C CD  . LYS A 1 414 ? -26.826 30.668  167.560 1.00 57.84  ? 460 LYS A CD  1 
ATOM 3257 C CE  . LYS A 1 414 ? -27.770 30.387  168.719 1.00 54.55  ? 460 LYS A CE  1 
ATOM 3258 N NZ  . LYS A 1 414 ? -27.060 30.352  170.027 1.00 52.71  ? 460 LYS A NZ  1 
ATOM 3259 N N   . ALA A 1 415 ? -26.920 36.220  169.078 1.00 48.92  ? 461 ALA A N   1 
ATOM 3260 C CA  . ALA A 1 415 ? -27.572 37.251  169.867 1.00 52.35  ? 461 ALA A CA  1 
ATOM 3261 C C   . ALA A 1 415 ? -27.365 38.629  169.241 1.00 56.05  ? 461 ALA A C   1 
ATOM 3262 O O   . ALA A 1 415 ? -26.585 38.809  168.305 1.00 57.47  ? 461 ALA A O   1 
ATOM 3263 C CB  . ALA A 1 415 ? -27.052 37.233  171.304 1.00 48.69  ? 461 ALA A CB  1 
ATOM 3264 N N   . THR A 1 416 ? -28.089 39.606  169.774 1.00 56.36  ? 462 THR A N   1 
ATOM 3265 C CA  . THR A 1 416 ? -27.954 40.981  169.315 1.00 55.73  ? 462 THR A CA  1 
ATOM 3266 C C   . THR A 1 416 ? -26.564 41.508  169.667 1.00 60.04  ? 462 THR A C   1 
ATOM 3267 O O   . THR A 1 416 ? -26.056 41.236  170.760 1.00 59.54  ? 462 THR A O   1 
ATOM 3268 C CB  . THR A 1 416 ? -29.033 41.852  169.964 1.00 55.93  ? 462 THR A CB  1 
ATOM 3269 O OG1 . THR A 1 416 ? -30.226 41.078  170.136 1.00 59.79  ? 462 THR A OG1 1 
ATOM 3270 C CG2 . THR A 1 416 ? -29.362 43.060  169.101 1.00 56.80  ? 462 THR A CG2 1 
ATOM 3271 N N   . PRO A 1 417 ? -25.915 42.265  168.768 1.00 59.98  ? 463 PRO A N   1 
ATOM 3272 C CA  . PRO A 1 417 ? -26.355 42.707  167.442 1.00 58.98  ? 463 PRO A CA  1 
ATOM 3273 C C   . PRO A 1 417 ? -25.843 41.829  166.307 1.00 57.59  ? 463 PRO A C   1 
ATOM 3274 O O   . PRO A 1 417 ? -25.690 42.305  165.185 1.00 59.47  ? 463 PRO A O   1 
ATOM 3275 C CB  . PRO A 1 417 ? -25.780 44.128  167.354 1.00 56.56  ? 463 PRO A CB  1 
ATOM 3276 C CG  . PRO A 1 417 ? -24.613 44.169  168.347 1.00 59.07  ? 463 PRO A CG  1 
ATOM 3277 C CD  . PRO A 1 417 ? -24.618 42.865  169.113 1.00 57.01  ? 463 PRO A CD  1 
ATOM 3278 N N   . HIS A 1 418 ? -25.566 40.554  166.579 1.00 53.18  ? 464 HIS A N   1 
ATOM 3279 C CA  . HIS A 1 418 ? -25.139 39.591  165.564 1.00 54.00  ? 464 HIS A CA  1 
ATOM 3280 C C   . HIS A 1 418 ? -23.849 40.043  164.876 1.00 52.37  ? 464 HIS A C   1 
ATOM 3281 O O   . HIS A 1 418 ? -23.782 40.201  163.656 1.00 53.29  ? 464 HIS A O   1 
ATOM 3282 C CB  . HIS A 1 418 ? -26.253 39.345  164.542 1.00 50.80  ? 464 HIS A CB  1 
ATOM 3283 C CG  . HIS A 1 418 ? -27.622 39.288  165.143 1.00 50.80  ? 464 HIS A CG  1 
ATOM 3284 N ND1 . HIS A 1 418 ? -27.970 38.378  166.117 1.00 51.84  ? 464 HIS A ND1 1 
ATOM 3285 C CD2 . HIS A 1 418 ? -28.730 40.031  164.909 1.00 54.28  ? 464 HIS A CD2 1 
ATOM 3286 C CE1 . HIS A 1 418 ? -29.233 38.562  166.457 1.00 50.97  ? 464 HIS A CE1 1 
ATOM 3287 N NE2 . HIS A 1 418 ? -29.717 39.559  165.739 1.00 54.24  ? 464 HIS A NE2 1 
ATOM 3288 N N   . ASP A 1 419 ? -22.818 40.254  165.688 1.00 53.47  ? 465 ASP A N   1 
ATOM 3289 C CA  . ASP A 1 419 ? -21.501 40.580  165.171 1.00 54.33  ? 465 ASP A CA  1 
ATOM 3290 C C   . ASP A 1 419 ? -20.696 39.298  164.971 1.00 54.42  ? 465 ASP A C   1 
ATOM 3291 O O   . ASP A 1 419 ? -21.158 38.191  165.255 1.00 57.96  ? 465 ASP A O   1 
ATOM 3292 C CB  . ASP A 1 419 ? -20.782 41.549  166.106 1.00 55.26  ? 465 ASP A CB  1 
ATOM 3293 C CG  . ASP A 1 419 ? -21.008 41.224  167.567 1.00 62.54  ? 465 ASP A CG  1 
ATOM 3294 O OD1 . ASP A 1 419 ? -21.618 40.173  167.855 1.00 64.04  ? 465 ASP A OD1 1 
ATOM 3295 O OD2 . ASP A 1 419 ? -20.577 42.020  168.428 1.00 61.95  ? 465 ASP A OD2 1 
ATOM 3296 N N   . LEU A 1 420 ? -19.473 39.447  164.474 1.00 44.30  ? 466 LEU A N   1 
ATOM 3297 C CA  . LEU A 1 420 ? -18.615 38.298  164.237 1.00 43.93  ? 466 LEU A CA  1 
ATOM 3298 C C   . LEU A 1 420 ? -18.180 37.669  165.557 1.00 41.69  ? 466 LEU A C   1 
ATOM 3299 O O   . LEU A 1 420 ? -18.101 38.327  166.597 1.00 39.58  ? 466 LEU A O   1 
ATOM 3300 C CB  . LEU A 1 420 ? -17.389 38.700  163.421 1.00 39.14  ? 466 LEU A CB  1 
ATOM 3301 C CG  . LEU A 1 420 ? -17.665 39.446  162.117 1.00 38.83  ? 466 LEU A CG  1 
ATOM 3302 C CD1 . LEU A 1 420 ? -16.417 40.168  161.646 1.00 38.43  ? 466 LEU A CD1 1 
ATOM 3303 C CD2 . LEU A 1 420 ? -18.166 38.488  161.053 1.00 40.54  ? 466 LEU A CD2 1 
ATOM 3304 N N   . THR A 1 421 ? -17.899 36.370  165.502 1.00 39.09  ? 467 THR A N   1 
ATOM 3305 C CA  . THR A 1 421 ? -17.462 35.611  166.662 1.00 40.55  ? 467 THR A CA  1 
ATOM 3306 C C   . THR A 1 421 ? -16.095 34.995  166.398 1.00 46.52  ? 467 THR A C   1 
ATOM 3307 O O   . THR A 1 421 ? -15.784 34.588  165.275 1.00 48.15  ? 467 THR A O   1 
ATOM 3308 C CB  . THR A 1 421 ? -18.460 34.506  167.020 1.00 44.49  ? 467 THR A CB  1 
ATOM 3309 O OG1 . THR A 1 421 ? -18.839 33.799  165.833 1.00 46.46  ? 467 THR A OG1 1 
ATOM 3310 C CG2 . THR A 1 421 ? -19.696 35.098  167.670 1.00 45.86  ? 467 THR A CG2 1 
ATOM 3311 N N   . ILE A 1 422 ? -15.285 34.924  167.449 1.00 47.42  ? 468 ILE A N   1 
ATOM 3312 C CA  . ILE A 1 422 ? -13.937 34.373  167.382 1.00 43.47  ? 468 ILE A CA  1 
ATOM 3313 C C   . ILE A 1 422 ? -13.989 32.966  167.956 1.00 41.16  ? 468 ILE A C   1 
ATOM 3314 O O   . ILE A 1 422 ? -14.413 32.771  169.101 1.00 43.84  ? 468 ILE A O   1 
ATOM 3315 C CB  . ILE A 1 422 ? -12.931 35.243  168.151 1.00 48.04  ? 468 ILE A CB  1 
ATOM 3316 C CG1 . ILE A 1 422 ? -12.692 36.567  167.425 1.00 46.41  ? 468 ILE A CG1 1 
ATOM 3317 C CG2 . ILE A 1 422 ? -11.619 34.499  168.337 1.00 45.89  ? 468 ILE A CG2 1 
ATOM 3318 C CD1 . ILE A 1 422 ? -12.374 36.416  165.966 1.00 46.45  ? 468 ILE A CD1 1 
ATOM 3319 N N   . HIS A 1 423 ? -13.561 31.983  167.165 1.00 40.88  ? 469 HIS A N   1 
ATOM 3320 C CA  . HIS A 1 423 ? -13.558 30.587  167.600 1.00 39.00  ? 469 HIS A CA  1 
ATOM 3321 C C   . HIS A 1 423 ? -12.220 29.966  167.214 1.00 41.53  ? 469 HIS A C   1 
ATOM 3322 O O   . HIS A 1 423 ? -11.968 29.705  166.035 1.00 42.95  ? 469 HIS A O   1 
ATOM 3323 C CB  . HIS A 1 423 ? -14.720 29.814  166.992 1.00 38.71  ? 469 HIS A CB  1 
ATOM 3324 C CG  . HIS A 1 423 ? -16.024 30.035  167.691 1.00 46.21  ? 469 HIS A CG  1 
ATOM 3325 N ND1 . HIS A 1 423 ? -17.215 30.191  167.015 1.00 51.11  ? 469 HIS A ND1 1 
ATOM 3326 C CD2 . HIS A 1 423 ? -16.326 30.123  169.008 1.00 43.06  ? 469 HIS A CD2 1 
ATOM 3327 C CE1 . HIS A 1 423 ? -18.193 30.366  167.885 1.00 49.25  ? 469 HIS A CE1 1 
ATOM 3328 N NE2 . HIS A 1 423 ? -17.680 30.329  169.101 1.00 47.03  ? 469 HIS A NE2 1 
ATOM 3329 N N   . THR A 1 424 ? -11.373 29.728  168.210 1.00 39.09  ? 470 THR A N   1 
ATOM 3330 C CA  . THR A 1 424 ? -10.098 29.049  168.021 1.00 32.81  ? 470 THR A CA  1 
ATOM 3331 C C   . THR A 1 424 ? -10.163 27.676  168.673 1.00 33.21  ? 470 THR A C   1 
ATOM 3332 O O   . THR A 1 424 ? -10.625 27.548  169.811 1.00 38.23  ? 470 THR A O   1 
ATOM 3333 C CB  . THR A 1 424 ? -8.949  29.863  168.615 1.00 34.76  ? 470 THR A CB  1 
ATOM 3334 O OG1 . THR A 1 424 ? -9.277  30.242  169.957 1.00 44.51  ? 470 THR A OG1 1 
ATOM 3335 C CG2 . THR A 1 424 ? -8.699  31.112  167.786 1.00 35.82  ? 470 THR A CG2 1 
ATOM 3336 N N   . PHE A 1 425 ? -9.706  26.654  167.952 1.00 30.14  ? 471 PHE A N   1 
ATOM 3337 C CA  . PHE A 1 425 ? -9.813  25.286  168.434 1.00 36.09  ? 471 PHE A CA  1 
ATOM 3338 C C   . PHE A 1 425 ? -8.807  24.405  167.709 1.00 39.18  ? 471 PHE A C   1 
ATOM 3339 O O   . PHE A 1 425 ? -8.421  24.684  166.571 1.00 39.05  ? 471 PHE A O   1 
ATOM 3340 C CB  . PHE A 1 425 ? -11.232 24.738  168.235 1.00 29.06  ? 471 PHE A CB  1 
ATOM 3341 C CG  . PHE A 1 425 ? -11.708 24.789  166.809 1.00 28.69  ? 471 PHE A CG  1 
ATOM 3342 C CD1 . PHE A 1 425 ? -12.250 25.948  166.284 1.00 30.69  ? 471 PHE A CD1 1 
ATOM 3343 C CD2 . PHE A 1 425 ? -11.619 23.675  165.995 1.00 33.83  ? 471 PHE A CD2 1 
ATOM 3344 C CE1 . PHE A 1 425 ? -12.684 25.995  164.977 1.00 32.00  ? 471 PHE A CE1 1 
ATOM 3345 C CE2 . PHE A 1 425 ? -12.054 23.718  164.687 1.00 28.38  ? 471 PHE A CE2 1 
ATOM 3346 C CZ  . PHE A 1 425 ? -12.586 24.878  164.179 1.00 25.09  ? 471 PHE A CZ  1 
ATOM 3347 N N   . PHE A 1 426 ? -8.387  23.336  168.381 1.00 31.51  ? 472 PHE A N   1 
ATOM 3348 C CA  . PHE A 1 426 ? -7.565  22.308  167.762 1.00 34.32  ? 472 PHE A CA  1 
ATOM 3349 C C   . PHE A 1 426 ? -8.472  21.295  167.069 1.00 30.98  ? 472 PHE A C   1 
ATOM 3350 O O   . PHE A 1 426 ? -9.682  21.496  166.941 1.00 34.96  ? 472 PHE A O   1 
ATOM 3351 C CB  . PHE A 1 426 ? -6.671  21.626  168.796 1.00 36.34  ? 472 PHE A CB  1 
ATOM 3352 C CG  . PHE A 1 426 ? -6.115  22.553  169.832 1.00 33.48  ? 472 PHE A CG  1 
ATOM 3353 C CD1 . PHE A 1 426 ? -5.001  23.324  169.562 1.00 28.98  ? 472 PHE A CD1 1 
ATOM 3354 C CD2 . PHE A 1 426 ? -6.697  22.642  171.082 1.00 36.75  ? 472 PHE A CD2 1 
ATOM 3355 C CE1 . PHE A 1 426 ? -4.483  24.170  170.517 1.00 33.01  ? 472 PHE A CE1 1 
ATOM 3356 C CE2 . PHE A 1 426 ? -6.184  23.489  172.040 1.00 36.49  ? 472 PHE A CE2 1 
ATOM 3357 C CZ  . PHE A 1 426 ? -5.076  24.254  171.755 1.00 32.77  ? 472 PHE A CZ  1 
ATOM 3358 N N   . ASN A 1 427 ? -7.894  20.180  166.619 1.00 32.01  ? 473 ASN A N   1 
ATOM 3359 C CA  . ASN A 1 427 ? -8.704  19.099  166.074 1.00 26.63  ? 473 ASN A CA  1 
ATOM 3360 C C   . ASN A 1 427 ? -9.535  18.413  167.147 1.00 29.38  ? 473 ASN A C   1 
ATOM 3361 O O   . ASN A 1 427 ? -10.465 17.673  166.815 1.00 38.11  ? 473 ASN A O   1 
ATOM 3362 C CB  . ASN A 1 427 ? -7.815  18.073  165.372 1.00 29.08  ? 473 ASN A CB  1 
ATOM 3363 C CG  . ASN A 1 427 ? -7.639  18.366  163.898 1.00 29.94  ? 473 ASN A CG  1 
ATOM 3364 O OD1 . ASN A 1 427 ? -6.782  19.155  163.508 1.00 33.29  ? 473 ASN A OD1 1 
ATOM 3365 N ND2 . ASN A 1 427 ? -8.446  17.722  163.068 1.00 32.97  ? 473 ASN A ND2 1 
ATOM 3366 N N   . ASN A 1 428 ? -9.219  18.634  168.418 1.00 33.63  ? 474 ASN A N   1 
ATOM 3367 C CA  . ASN A 1 428 ? -9.917  18.016  169.535 1.00 36.03  ? 474 ASN A CA  1 
ATOM 3368 C C   . ASN A 1 428 ? -10.512 19.099  170.424 1.00 39.70  ? 474 ASN A C   1 
ATOM 3369 O O   . ASN A 1 428 ? -9.829  20.070  170.766 1.00 46.77  ? 474 ASN A O   1 
ATOM 3370 C CB  . ASN A 1 428 ? -8.968  17.131  170.342 1.00 34.27  ? 474 ASN A CB  1 
ATOM 3371 C CG  . ASN A 1 428 ? -7.635  17.801  170.604 1.00 32.62  ? 474 ASN A CG  1 
ATOM 3372 O OD1 . ASN A 1 428 ? -7.505  18.616  171.514 1.00 32.82  ? 474 ASN A OD1 1 
ATOM 3373 N ND2 . ASN A 1 428 ? -6.638  17.466  169.799 1.00 37.85  ? 474 ASN A ND2 1 
ATOM 3374 N N   . ILE A 1 429 ? -11.777 18.929  170.798 1.00 34.94  ? 475 ILE A N   1 
ATOM 3375 C CA  . ILE A 1 429 ? -12.483 19.870  171.658 1.00 39.73  ? 475 ILE A CA  1 
ATOM 3376 C C   . ILE A 1 429 ? -12.957 19.127  172.897 1.00 42.16  ? 475 ILE A C   1 
ATOM 3377 O O   . ILE A 1 429 ? -13.567 18.058  172.790 1.00 43.83  ? 475 ILE A O   1 
ATOM 3378 C CB  . ILE A 1 429 ? -13.668 20.533  170.932 1.00 44.74  ? 475 ILE A CB  1 
ATOM 3379 C CG1 . ILE A 1 429 ? -13.212 21.140  169.604 1.00 43.26  ? 475 ILE A CG1 1 
ATOM 3380 C CG2 . ILE A 1 429 ? -14.307 21.593  171.812 1.00 41.57  ? 475 ILE A CG2 1 
ATOM 3381 C CD1 . ILE A 1 429 ? -13.616 20.345  168.395 1.00 39.24  ? 475 ILE A CD1 1 
ATOM 3382 N N   . LEU A 1 430 ? -12.678 19.692  174.067 1.00 43.94  ? 476 LEU A N   1 
ATOM 3383 C CA  . LEU A 1 430 ? -13.104 19.129  175.340 1.00 46.55  ? 476 LEU A CA  1 
ATOM 3384 C C   . LEU A 1 430 ? -14.238 19.972  175.905 1.00 49.85  ? 476 LEU A C   1 
ATOM 3385 O O   . LEU A 1 430 ? -14.101 21.192  176.039 1.00 57.97  ? 476 LEU A O   1 
ATOM 3386 C CB  . LEU A 1 430 ? -11.939 19.071  176.330 1.00 44.48  ? 476 LEU A CB  1 
ATOM 3387 C CG  . LEU A 1 430 ? -12.287 18.916  177.809 1.00 47.65  ? 476 LEU A CG  1 
ATOM 3388 C CD1 . LEU A 1 430 ? -12.733 17.496  178.101 1.00 49.22  ? 476 LEU A CD1 1 
ATOM 3389 C CD2 . LEU A 1 430 ? -11.096 19.291  178.673 1.00 46.29  ? 476 LEU A CD2 1 
ATOM 3390 N N   . VAL A 1 431 ? -15.349 19.324  176.233 1.00 46.86  ? 477 VAL A N   1 
ATOM 3391 C CA  . VAL A 1 431 ? -16.538 19.999  176.732 1.00 50.63  ? 477 VAL A CA  1 
ATOM 3392 C C   . VAL A 1 431 ? -16.841 19.491  178.137 1.00 54.67  ? 477 VAL A C   1 
ATOM 3393 O O   . VAL A 1 431 ? -17.286 18.351  178.303 1.00 55.97  ? 477 VAL A O   1 
ATOM 3394 C CB  . VAL A 1 431 ? -17.747 19.800  175.802 1.00 50.85  ? 477 VAL A CB  1 
ATOM 3395 C CG1 . VAL A 1 431 ? -17.647 20.746  174.625 1.00 57.11  ? 477 VAL A CG1 1 
ATOM 3396 C CG2 . VAL A 1 431 ? -17.806 18.371  175.297 1.00 49.97  ? 477 VAL A CG2 1 
ATOM 3397 N N   . PRO A 1 432 ? -16.618 20.289  179.179 1.00 60.71  ? 478 PRO A N   1 
ATOM 3398 C CA  . PRO A 1 432 ? -16.962 19.844  180.535 1.00 61.19  ? 478 PRO A CA  1 
ATOM 3399 C C   . PRO A 1 432 ? -18.443 20.012  180.832 1.00 64.48  ? 478 PRO A C   1 
ATOM 3400 O O   . PRO A 1 432 ? -19.213 20.413  179.955 1.00 70.70  ? 478 PRO A O   1 
ATOM 3401 C CB  . PRO A 1 432 ? -16.098 20.746  181.421 1.00 61.92  ? 478 PRO A CB  1 
ATOM 3402 C CG  . PRO A 1 432 ? -15.953 22.007  180.632 1.00 59.63  ? 478 PRO A CG  1 
ATOM 3403 C CD  . PRO A 1 432 ? -16.055 21.650  179.166 1.00 57.92  ? 478 PRO A CD  1 
ATOM 3404 N N   . ASN A 1 433 ? -18.854 19.709  182.060 1.00 64.97  ? 479 ASN A N   1 
ATOM 3405 C CA  . ASN A 1 433 ? -20.257 19.823  182.447 1.00 67.58  ? 479 ASN A CA  1 
ATOM 3406 C C   . ASN A 1 433 ? -20.607 21.290  182.661 1.00 68.13  ? 479 ASN A C   1 
ATOM 3407 O O   . ASN A 1 433 ? -20.057 21.945  183.551 1.00 69.34  ? 479 ASN A O   1 
ATOM 3408 C CB  . ASN A 1 433 ? -20.538 19.010  183.706 1.00 67.76  ? 479 ASN A CB  1 
ATOM 3409 C CG  . ASN A 1 433 ? -21.733 18.094  183.549 1.00 71.49  ? 479 ASN A CG  1 
ATOM 3410 O OD1 . ASN A 1 433 ? -22.294 17.968  182.461 1.00 71.48  ? 479 ASN A OD1 1 
ATOM 3411 N ND2 . ASN A 1 433 ? -22.131 17.450  184.639 1.00 69.21  ? 479 ASN A ND2 1 
ATOM 3412 N N   . ALA A 1 434 ? -21.527 21.804  181.849 1.00 67.60  ? 480 ALA A N   1 
ATOM 3413 C CA  . ALA A 1 434 ? -22.011 23.166  182.002 1.00 70.55  ? 480 ALA A CA  1 
ATOM 3414 C C   . ALA A 1 434 ? -23.357 23.291  181.306 1.00 68.71  ? 480 ALA A C   1 
ATOM 3415 O O   . ALA A 1 434 ? -23.725 22.471  180.462 1.00 67.52  ? 480 ALA A O   1 
ATOM 3416 C CB  . ALA A 1 434 ? -21.013 24.185  181.447 1.00 70.48  ? 480 ALA A CB  1 
ATOM 3417 N N   . LYS A 1 435 ? -24.095 24.338  181.678 1.00 77.15  ? 481 LYS A N   1 
ATOM 3418 C CA  . LYS A 1 435 ? -25.398 24.579  181.069 1.00 80.35  ? 481 LYS A CA  1 
ATOM 3419 C C   . LYS A 1 435 ? -25.278 24.889  179.583 1.00 82.49  ? 481 LYS A C   1 
ATOM 3420 O O   . LYS A 1 435 ? -26.088 24.406  178.784 1.00 82.38  ? 481 LYS A O   1 
ATOM 3421 C CB  . LYS A 1 435 ? -26.106 25.725  181.790 1.00 81.59  ? 481 LYS A CB  1 
ATOM 3422 C CG  . LYS A 1 435 ? -26.932 25.294  182.989 1.00 80.28  ? 481 LYS A CG  1 
ATOM 3423 C CD  . LYS A 1 435 ? -28.329 24.875  182.572 1.00 78.56  ? 481 LYS A CD  1 
ATOM 3424 C CE  . LYS A 1 435 ? -29.069 26.019  181.898 1.00 79.86  ? 481 LYS A CE  1 
ATOM 3425 N NZ  . LYS A 1 435 ? -30.544 25.837  181.954 1.00 78.88  ? 481 LYS A NZ  1 
ATOM 3426 N N   . GLU A 1 436 ? -24.279 25.680  179.193 1.00 79.20  ? 482 GLU A N   1 
ATOM 3427 C CA  . GLU A 1 436 ? -24.168 26.174  177.830 1.00 78.83  ? 482 GLU A CA  1 
ATOM 3428 C C   . GLU A 1 436 ? -23.044 25.533  177.029 1.00 75.59  ? 482 GLU A C   1 
ATOM 3429 O O   . GLU A 1 436 ? -22.962 25.772  175.818 1.00 76.89  ? 482 GLU A O   1 
ATOM 3430 C CB  . GLU A 1 436 ? -23.969 27.696  177.838 1.00 79.74  ? 482 GLU A CB  1 
ATOM 3431 C CG  . GLU A 1 436 ? -22.552 28.125  178.169 1.00 80.27  ? 482 GLU A CG  1 
ATOM 3432 C CD  . GLU A 1 436 ? -22.318 28.262  179.660 1.00 81.27  ? 482 GLU A CD  1 
ATOM 3433 O OE1 . GLU A 1 436 ? -23.131 27.730  180.445 1.00 78.98  ? 482 GLU A OE1 1 
ATOM 3434 O OE2 . GLU A 1 436 ? -21.320 28.904  180.048 1.00 82.21  ? 482 GLU A OE2 1 
ATOM 3435 N N   . ASN A 1 437 ? -22.179 24.738  177.662 1.00 62.96  ? 483 ASN A N   1 
ATOM 3436 C CA  . ASN A 1 437 ? -21.074 24.129  176.929 1.00 62.91  ? 483 ASN A CA  1 
ATOM 3437 C C   . ASN A 1 437 ? -21.565 23.184  175.840 1.00 65.13  ? 483 ASN A C   1 
ATOM 3438 O O   . ASN A 1 437 ? -21.007 23.174  174.738 1.00 65.77  ? 483 ASN A O   1 
ATOM 3439 C CB  . ASN A 1 437 ? -20.141 23.396  177.892 1.00 62.21  ? 483 ASN A CB  1 
ATOM 3440 C CG  . ASN A 1 437 ? -18.927 24.224  178.267 1.00 67.66  ? 483 ASN A CG  1 
ATOM 3441 O OD1 . ASN A 1 437 ? -18.969 25.030  179.196 1.00 70.90  ? 483 ASN A OD1 1 
ATOM 3442 N ND2 . ASN A 1 437 ? -17.834 24.028  177.541 1.00 66.50  ? 483 ASN A ND2 1 
ATOM 3443 N N   . TYR A 1 438 ? -22.605 22.396  176.118 1.00 61.97  ? 484 TYR A N   1 
ATOM 3444 C CA  . TYR A 1 438 ? -23.086 21.437  175.128 1.00 60.97  ? 484 TYR A CA  1 
ATOM 3445 C C   . TYR A 1 438 ? -23.694 22.134  173.916 1.00 61.51  ? 484 TYR A C   1 
ATOM 3446 O O   . TYR A 1 438 ? -23.421 21.749  172.773 1.00 61.81  ? 484 TYR A O   1 
ATOM 3447 C CB  . TYR A 1 438 ? -24.091 20.487  175.773 1.00 58.65  ? 484 TYR A CB  1 
ATOM 3448 C CG  . TYR A 1 438 ? -23.518 19.753  176.959 1.00 58.38  ? 484 TYR A CG  1 
ATOM 3449 C CD1 . TYR A 1 438 ? -22.580 18.745  176.786 1.00 58.01  ? 484 TYR A CD1 1 
ATOM 3450 C CD2 . TYR A 1 438 ? -23.893 20.083  178.251 1.00 58.54  ? 484 TYR A CD2 1 
ATOM 3451 C CE1 . TYR A 1 438 ? -22.045 18.077  177.866 1.00 56.18  ? 484 TYR A CE1 1 
ATOM 3452 C CE2 . TYR A 1 438 ? -23.362 19.421  179.336 1.00 60.46  ? 484 TYR A CE2 1 
ATOM 3453 C CZ  . TYR A 1 438 ? -22.440 18.420  179.139 1.00 60.25  ? 484 TYR A CZ  1 
ATOM 3454 O OH  . TYR A 1 438 ? -21.912 17.762  180.222 1.00 61.48  ? 484 TYR A OH  1 
ATOM 3455 N N   . VAL A 1 439 ? -24.510 23.166  174.138 1.00 64.53  ? 485 VAL A N   1 
ATOM 3456 C CA  . VAL A 1 439 ? -25.100 23.878  173.009 1.00 63.29  ? 485 VAL A CA  1 
ATOM 3457 C C   . VAL A 1 439 ? -24.033 24.655  172.247 1.00 64.39  ? 485 VAL A C   1 
ATOM 3458 O O   . VAL A 1 439 ? -24.091 24.765  171.016 1.00 65.55  ? 485 VAL A O   1 
ATOM 3459 C CB  . VAL A 1 439 ? -26.249 24.788  173.477 1.00 64.98  ? 485 VAL A CB  1 
ATOM 3460 C CG1 . VAL A 1 439 ? -27.530 23.982  173.620 1.00 58.80  ? 485 VAL A CG1 1 
ATOM 3461 C CG2 . VAL A 1 439 ? -25.899 25.460  174.785 1.00 63.91  ? 485 VAL A CG2 1 
ATOM 3462 N N   . ALA A 1 440 ? -23.039 25.202  172.956 1.00 58.46  ? 486 ALA A N   1 
ATOM 3463 C CA  . ALA A 1 440 ? -21.934 25.861  172.270 1.00 56.03  ? 486 ALA A CA  1 
ATOM 3464 C C   . ALA A 1 440 ? -21.173 24.880  171.389 1.00 58.14  ? 486 ALA A C   1 
ATOM 3465 O O   . ALA A 1 440 ? -20.806 25.208  170.254 1.00 59.41  ? 486 ALA A O   1 
ATOM 3466 C CB  . ALA A 1 440 ? -20.998 26.510  173.287 1.00 55.64  ? 486 ALA A CB  1 
ATOM 3467 N N   . ASN A 1 441 ? -20.934 23.668  171.892 1.00 55.16  ? 487 ASN A N   1 
ATOM 3468 C CA  . ASN A 1 441 ? -20.267 22.652  171.088 1.00 53.78  ? 487 ASN A CA  1 
ATOM 3469 C C   . ASN A 1 441 ? -21.122 22.241  169.896 1.00 55.64  ? 487 ASN A C   1 
ATOM 3470 O O   . ASN A 1 441 ? -20.593 21.950  168.820 1.00 57.15  ? 487 ASN A O   1 
ATOM 3471 C CB  . ASN A 1 441 ? -19.929 21.439  171.951 1.00 51.86  ? 487 ASN A CB  1 
ATOM 3472 C CG  . ASN A 1 441 ? -19.233 20.346  171.170 1.00 55.82  ? 487 ASN A CG  1 
ATOM 3473 O OD1 . ASN A 1 441 ? -18.304 20.610  170.408 1.00 58.94  ? 487 ASN A OD1 1 
ATOM 3474 N ND2 . ASN A 1 441 ? -19.676 19.110  171.357 1.00 57.34  ? 487 ASN A ND2 1 
ATOM 3475 N N   . LEU A 1 442 ? -22.444 22.196  170.073 1.00 54.32  ? 488 LEU A N   1 
ATOM 3476 C CA  . LEU A 1 442 ? -23.322 21.886  168.948 1.00 54.36  ? 488 LEU A CA  1 
ATOM 3477 C C   . LEU A 1 442 ? -23.245 22.958  167.867 1.00 56.21  ? 488 LEU A C   1 
ATOM 3478 O O   . LEU A 1 442 ? -23.193 22.639  166.672 1.00 56.68  ? 488 LEU A O   1 
ATOM 3479 C CB  . LEU A 1 442 ? -24.762 21.720  169.427 1.00 53.13  ? 488 LEU A CB  1 
ATOM 3480 C CG  . LEU A 1 442 ? -25.239 20.284  169.634 1.00 55.11  ? 488 LEU A CG  1 
ATOM 3481 C CD1 . LEU A 1 442 ? -26.739 20.264  169.848 1.00 55.14  ? 488 LEU A CD1 1 
ATOM 3482 C CD2 . LEU A 1 442 ? -24.852 19.415  168.450 1.00 53.64  ? 488 LEU A CD2 1 
ATOM 3483 N N   . GLU A 1 443 ? -23.250 24.233  168.264 1.00 54.76  ? 489 GLU A N   1 
ATOM 3484 C CA  . GLU A 1 443 ? -23.072 25.301  167.284 1.00 55.71  ? 489 GLU A CA  1 
ATOM 3485 C C   . GLU A 1 443 ? -21.717 25.192  166.601 1.00 58.51  ? 489 GLU A C   1 
ATOM 3486 O O   . GLU A 1 443 ? -21.607 25.397  165.386 1.00 61.34  ? 489 GLU A O   1 
ATOM 3487 C CB  . GLU A 1 443 ? -23.228 26.676  167.935 1.00 55.97  ? 489 GLU A CB  1 
ATOM 3488 C CG  . GLU A 1 443 ? -24.458 26.845  168.801 1.00 58.64  ? 489 GLU A CG  1 
ATOM 3489 C CD  . GLU A 1 443 ? -24.384 28.076  169.682 1.00 64.09  ? 489 GLU A CD  1 
ATOM 3490 O OE1 . GLU A 1 443 ? -23.298 28.687  169.761 1.00 60.52  ? 489 GLU A OE1 1 
ATOM 3491 O OE2 . GLU A 1 443 ? -25.414 28.435  170.292 1.00 64.57  ? 489 GLU A OE2 1 
ATOM 3492 N N   . LEU A 1 444 ? -20.673 24.871  167.368 1.00 47.86  ? 490 LEU A N   1 
ATOM 3493 C CA  . LEU A 1 444 ? -19.349 24.676  166.788 1.00 44.60  ? 490 LEU A CA  1 
ATOM 3494 C C   . LEU A 1 444 ? -19.373 23.580  165.730 1.00 44.78  ? 490 LEU A C   1 
ATOM 3495 O O   . LEU A 1 444 ? -18.862 23.758  164.618 1.00 47.59  ? 490 LEU A O   1 
ATOM 3496 C CB  . LEU A 1 444 ? -18.350 24.333  167.893 1.00 46.92  ? 490 LEU A CB  1 
ATOM 3497 C CG  . LEU A 1 444 ? -16.855 24.486  167.622 1.00 47.79  ? 490 LEU A CG  1 
ATOM 3498 C CD1 . LEU A 1 444 ? -16.579 25.723  166.795 1.00 45.65  ? 490 LEU A CD1 1 
ATOM 3499 C CD2 . LEU A 1 444 ? -16.089 24.534  168.933 1.00 48.14  ? 490 LEU A CD2 1 
ATOM 3500 N N   . LEU A 1 445 ? -19.982 22.442  166.060 1.00 43.20  ? 491 LEU A N   1 
ATOM 3501 C CA  . LEU A 1 445 ? -20.026 21.317  165.132 1.00 43.71  ? 491 LEU A CA  1 
ATOM 3502 C C   . LEU A 1 445 ? -20.801 21.674  163.872 1.00 43.34  ? 491 LEU A C   1 
ATOM 3503 O O   . LEU A 1 445 ? -20.359 21.379  162.755 1.00 46.43  ? 491 LEU A O   1 
ATOM 3504 C CB  . LEU A 1 445 ? -20.648 20.100  165.815 1.00 42.26  ? 491 LEU A CB  1 
ATOM 3505 C CG  . LEU A 1 445 ? -19.695 19.007  166.299 1.00 39.03  ? 491 LEU A CG  1 
ATOM 3506 C CD1 . LEU A 1 445 ? -18.579 19.597  167.138 1.00 43.70  ? 491 LEU A CD1 1 
ATOM 3507 C CD2 . LEU A 1 445 ? -20.458 17.959  167.085 1.00 45.19  ? 491 LEU A CD2 1 
ATOM 3508 N N   . ASN A 1 446 ? -21.967 22.306  164.031 1.00 40.40  ? 492 ASN A N   1 
ATOM 3509 C CA  . ASN A 1 446 ? -22.756 22.674  162.861 1.00 41.62  ? 492 ASN A CA  1 
ATOM 3510 C C   . ASN A 1 446 ? -22.019 23.678  161.988 1.00 46.82  ? 492 ASN A C   1 
ATOM 3511 O O   . ASN A 1 446 ? -22.074 23.582  160.757 1.00 49.74  ? 492 ASN A O   1 
ATOM 3512 C CB  . ASN A 1 446 ? -24.115 23.234  163.278 1.00 41.12  ? 492 ASN A CB  1 
ATOM 3513 C CG  . ASN A 1 446 ? -25.128 23.200  162.148 1.00 44.98  ? 492 ASN A CG  1 
ATOM 3514 O OD1 . ASN A 1 446 ? -24.766 23.100  160.978 1.00 50.24  ? 492 ASN A OD1 1 
ATOM 3515 N ND2 . ASN A 1 446 ? -26.404 23.285  162.493 1.00 45.30  ? 492 ASN A ND2 1 
ATOM 3516 N N   . ASN A 1 447 ? -21.323 24.639  162.599 1.00 43.06  ? 493 ASN A N   1 
ATOM 3517 C CA  . ASN A 1 447 ? -20.532 25.581  161.819 1.00 36.62  ? 493 ASN A CA  1 
ATOM 3518 C C   . ASN A 1 447 ? -19.430 24.866  161.052 1.00 40.36  ? 493 ASN A C   1 
ATOM 3519 O O   . ASN A 1 447 ? -19.172 25.182  159.885 1.00 45.84  ? 493 ASN A O   1 
ATOM 3520 C CB  . ASN A 1 447 ? -19.941 26.648  162.737 1.00 36.59  ? 493 ASN A CB  1 
ATOM 3521 C CG  . ASN A 1 447 ? -20.979 27.626  163.238 1.00 42.65  ? 493 ASN A CG  1 
ATOM 3522 O OD1 . ASN A 1 447 ? -22.045 27.776  162.642 1.00 48.82  ? 493 ASN A OD1 1 
ATOM 3523 N ND2 . ASN A 1 447 ? -20.676 28.295  164.343 1.00 44.80  ? 493 ASN A ND2 1 
ATOM 3524 N N   . ILE A 1 448 ? -18.773 23.895  161.688 1.00 35.93  ? 494 ILE A N   1 
ATOM 3525 C CA  . ILE A 1 448 ? -17.667 23.203  161.034 1.00 35.07  ? 494 ILE A CA  1 
ATOM 3526 C C   . ILE A 1 448 ? -18.170 22.344  159.877 1.00 36.51  ? 494 ILE A C   1 
ATOM 3527 O O   . ILE A 1 448 ? -17.509 22.236  158.838 1.00 41.26  ? 494 ILE A O   1 
ATOM 3528 C CB  . ILE A 1 448 ? -16.872 22.382  162.066 1.00 33.99  ? 494 ILE A CB  1 
ATOM 3529 C CG1 . ILE A 1 448 ? -16.121 23.325  163.007 1.00 34.50  ? 494 ILE A CG1 1 
ATOM 3530 C CG2 . ILE A 1 448 ? -15.890 21.454  161.382 1.00 31.85  ? 494 ILE A CG2 1 
ATOM 3531 C CD1 . ILE A 1 448 ? -15.884 22.766  164.383 1.00 38.85  ? 494 ILE A CD1 1 
ATOM 3532 N N   . ILE A 1 449 ? -19.348 21.731  160.027 1.00 38.51  ? 495 ILE A N   1 
ATOM 3533 C CA  . ILE A 1 449 ? -19.896 20.920  158.938 1.00 37.62  ? 495 ILE A CA  1 
ATOM 3534 C C   . ILE A 1 449 ? -20.141 21.744  157.679 1.00 39.55  ? 495 ILE A C   1 
ATOM 3535 O O   . ILE A 1 449 ? -20.051 21.208  156.568 1.00 38.24  ? 495 ILE A O   1 
ATOM 3536 C CB  . ILE A 1 449 ? -21.195 20.210  159.369 1.00 34.73  ? 495 ILE A CB  1 
ATOM 3537 C CG1 . ILE A 1 449 ? -20.953 19.332  160.590 1.00 36.79  ? 495 ILE A CG1 1 
ATOM 3538 C CG2 . ILE A 1 449 ? -21.747 19.344  158.252 1.00 34.19  ? 495 ILE A CG2 1 
ATOM 3539 C CD1 . ILE A 1 449 ? -22.191 19.115  161.407 1.00 36.46  ? 495 ILE A CD1 1 
ATOM 3540 N N   . GLN A 1 450 ? -20.431 23.041  157.818 1.00 32.46  ? 496 GLN A N   1 
ATOM 3541 C CA  . GLN A 1 450 ? -20.662 23.879  156.646 1.00 27.62  ? 496 GLN A CA  1 
ATOM 3542 C C   . GLN A 1 450 ? -19.464 23.874  155.707 1.00 34.59  ? 496 GLN A C   1 
ATOM 3543 O O   . GLN A 1 450 ? -19.634 23.840  154.484 1.00 30.47  ? 496 GLN A O   1 
ATOM 3544 C CB  . GLN A 1 450 ? -20.986 25.307  157.078 1.00 29.87  ? 496 GLN A CB  1 
ATOM 3545 C CG  . GLN A 1 450 ? -22.147 25.412  158.044 1.00 29.61  ? 496 GLN A CG  1 
ATOM 3546 C CD  . GLN A 1 450 ? -23.368 24.665  157.562 1.00 34.09  ? 496 GLN A CD  1 
ATOM 3547 O OE1 . GLN A 1 450 ? -23.825 24.861  156.438 1.00 40.09  ? 496 GLN A OE1 1 
ATOM 3548 N NE2 . GLN A 1 450 ? -23.909 23.804  158.414 1.00 39.31  ? 496 GLN A NE2 1 
ATOM 3549 N N   . PHE A 1 451 ? -18.255 23.917  156.256 1.00 33.36  ? 497 PHE A N   1 
ATOM 3550 C CA  . PHE A 1 451 ? -17.056 23.776  155.445 1.00 28.06  ? 497 PHE A CA  1 
ATOM 3551 C C   . PHE A 1 451 ? -16.970 22.361  154.892 1.00 32.29  ? 497 PHE A C   1 
ATOM 3552 O O   . PHE A 1 451 ? -17.196 21.383  155.610 1.00 37.05  ? 497 PHE A O   1 
ATOM 3553 C CB  . PHE A 1 451 ? -15.824 24.106  156.280 1.00 24.18  ? 497 PHE A CB  1 
ATOM 3554 C CG  . PHE A 1 451 ? -15.821 25.505  156.819 1.00 30.06  ? 497 PHE A CG  1 
ATOM 3555 C CD1 . PHE A 1 451 ? -16.439 25.800  158.019 1.00 32.68  ? 497 PHE A CD1 1 
ATOM 3556 C CD2 . PHE A 1 451 ? -15.221 26.530  156.112 1.00 33.99  ? 497 PHE A CD2 1 
ATOM 3557 C CE1 . PHE A 1 451 ? -16.446 27.086  158.509 1.00 29.54  ? 497 PHE A CE1 1 
ATOM 3558 C CE2 . PHE A 1 451 ? -15.223 27.816  156.602 1.00 33.68  ? 497 PHE A CE2 1 
ATOM 3559 C CZ  . PHE A 1 451 ? -15.838 28.094  157.801 1.00 31.20  ? 497 PHE A CZ  1 
ATOM 3560 N N   . ASP A 1 452 ? -16.637 22.249  153.606 1.00 37.61  ? 498 ASP A N   1 
ATOM 3561 C CA  . ASP A 1 452 ? -16.733 20.955  152.940 1.00 41.50  ? 498 ASP A CA  1 
ATOM 3562 C C   . ASP A 1 452 ? -15.661 19.990  153.431 1.00 45.16  ? 498 ASP A C   1 
ATOM 3563 O O   . ASP A 1 452 ? -15.969 18.954  154.029 1.00 51.28  ? 498 ASP A O   1 
ATOM 3564 C CB  . ASP A 1 452 ? -16.637 21.135  151.425 1.00 39.24  ? 498 ASP A CB  1 
ATOM 3565 C CG  . ASP A 1 452 ? -17.522 20.169  150.669 1.00 48.23  ? 498 ASP A CG  1 
ATOM 3566 O OD1 . ASP A 1 452 ? -17.782 19.065  151.191 1.00 52.84  ? 498 ASP A OD1 1 
ATOM 3567 O OD2 . ASP A 1 452 ? -17.958 20.509  149.551 1.00 48.92  ? 498 ASP A OD2 1 
ATOM 3568 N N   . TRP A 1 453 ? -14.396 20.312  153.189 1.00 29.15  ? 499 TRP A N   1 
ATOM 3569 C CA  . TRP A 1 453 ? -13.290 19.457  153.615 1.00 29.73  ? 499 TRP A CA  1 
ATOM 3570 C C   . TRP A 1 453 ? -12.694 19.964  154.925 1.00 32.12  ? 499 TRP A C   1 
ATOM 3571 O O   . TRP A 1 453 ? -11.509 20.273  155.029 1.00 40.17  ? 499 TRP A O   1 
ATOM 3572 C CB  . TRP A 1 453 ? -12.239 19.371  152.514 1.00 35.02  ? 499 TRP A CB  1 
ATOM 3573 C CG  . TRP A 1 453 ? -12.776 18.799  151.245 1.00 37.77  ? 499 TRP A CG  1 
ATOM 3574 C CD1 . TRP A 1 453 ? -13.078 19.479  150.104 1.00 39.58  ? 499 TRP A CD1 1 
ATOM 3575 C CD2 . TRP A 1 453 ? -13.080 17.424  150.986 1.00 36.68  ? 499 TRP A CD2 1 
ATOM 3576 N NE1 . TRP A 1 453 ? -13.552 18.613  149.150 1.00 42.15  ? 499 TRP A NE1 1 
ATOM 3577 C CE2 . TRP A 1 453 ? -13.563 17.345  149.667 1.00 40.03  ? 499 TRP A CE2 1 
ATOM 3578 C CE3 . TRP A 1 453 ? -12.991 16.252  151.743 1.00 36.94  ? 499 TRP A CE3 1 
ATOM 3579 C CZ2 . TRP A 1 453 ? -13.954 16.143  149.087 1.00 42.71  ? 499 TRP A CZ2 1 
ATOM 3580 C CZ3 . TRP A 1 453 ? -13.380 15.060  151.165 1.00 36.82  ? 499 TRP A CZ3 1 
ATOM 3581 C CH2 . TRP A 1 453 ? -13.855 15.013  149.852 1.00 41.37  ? 499 TRP A CH2 1 
ATOM 3582 N N   . ALA A 1 454 ? -13.545 20.048  155.933 1.00 27.08  ? 500 ALA A N   1 
ATOM 3583 C CA  . ALA A 1 454 ? -13.095 20.477  157.243 1.00 26.67  ? 500 ALA A CA  1 
ATOM 3584 C C   . ALA A 1 454 ? -12.191 19.415  157.866 1.00 32.00  ? 500 ALA A C   1 
ATOM 3585 O O   . ALA A 1 454 ? -12.331 18.224  157.577 1.00 39.71  ? 500 ALA A O   1 
ATOM 3586 C CB  . ALA A 1 454 ? -14.287 20.737  158.155 1.00 29.00  ? 500 ALA A CB  1 
ATOM 3587 N N   . PRO A 1 455 ? -11.243 19.823  158.706 1.00 28.59  ? 501 PRO A N   1 
ATOM 3588 C CA  . PRO A 1 455 ? -10.396 18.842  159.388 1.00 23.75  ? 501 PRO A CA  1 
ATOM 3589 C C   . PRO A 1 455 ? -11.211 17.939  160.299 1.00 31.66  ? 501 PRO A C   1 
ATOM 3590 O O   . PRO A 1 455 ? -12.209 18.352  160.893 1.00 38.75  ? 501 PRO A O   1 
ATOM 3591 C CB  . PRO A 1 455 ? -9.423  19.710  160.193 1.00 26.07  ? 501 PRO A CB  1 
ATOM 3592 C CG  . PRO A 1 455 ? -10.104 21.028  160.319 1.00 30.10  ? 501 PRO A CG  1 
ATOM 3593 C CD  . PRO A 1 455 ? -10.867 21.203  159.049 1.00 29.36  ? 501 PRO A CD  1 
ATOM 3594 N N   . GLN A 1 456 ? -10.773 16.687  160.398 1.00 24.92  ? 502 GLN A N   1 
ATOM 3595 C CA  . GLN A 1 456 ? -11.478 15.714  161.218 1.00 24.50  ? 502 GLN A CA  1 
ATOM 3596 C C   . GLN A 1 456 ? -11.387 16.091  162.691 1.00 27.11  ? 502 GLN A C   1 
ATOM 3597 O O   . GLN A 1 456 ? -10.316 16.433  163.197 1.00 34.45  ? 502 GLN A O   1 
ATOM 3598 C CB  . GLN A 1 456 ? -10.905 14.316  160.993 1.00 28.44  ? 502 GLN A CB  1 
ATOM 3599 C CG  . GLN A 1 456 ? -10.960 13.855  159.547 1.00 24.93  ? 502 GLN A CG  1 
ATOM 3600 C CD  . GLN A 1 456 ? -9.865  12.867  159.209 1.00 30.44  ? 502 GLN A CD  1 
ATOM 3601 O OE1 . GLN A 1 456 ? -9.156  12.384  160.089 1.00 36.90  ? 502 GLN A OE1 1 
ATOM 3602 N NE2 . GLN A 1 456 ? -9.719  12.562  157.925 1.00 30.94  ? 502 GLN A NE2 1 
ATOM 3603 N N   . LEU A 1 457 ? -12.520 16.022  163.378 1.00 27.60  ? 503 LEU A N   1 
ATOM 3604 C CA  . LEU A 1 457 ? -12.622 16.430  164.769 1.00 28.20  ? 503 LEU A CA  1 
ATOM 3605 C C   . LEU A 1 457 ? -12.586 15.217  165.688 1.00 30.76  ? 503 LEU A C   1 
ATOM 3606 O O   . LEU A 1 457 ? -12.951 14.107  165.296 1.00 42.70  ? 503 LEU A O   1 
ATOM 3607 C CB  . LEU A 1 457 ? -13.909 17.216  165.011 1.00 32.11  ? 503 LEU A CB  1 
ATOM 3608 C CG  . LEU A 1 457 ? -13.798 18.734  165.105 1.00 31.34  ? 503 LEU A CG  1 
ATOM 3609 C CD1 . LEU A 1 457 ? -13.019 19.293  163.933 1.00 34.96  ? 503 LEU A CD1 1 
ATOM 3610 C CD2 . LEU A 1 457 ? -15.186 19.337  165.161 1.00 31.49  ? 503 LEU A CD2 1 
ATOM 3611 N N   . TYR A 1 458 ? -12.144 15.443  166.924 1.00 27.04  ? 504 TYR A N   1 
ATOM 3612 C CA  . TYR A 1 458 ? -12.065 14.400  167.945 1.00 30.55  ? 504 TYR A CA  1 
ATOM 3613 C C   . TYR A 1 458 ? -12.651 14.973  169.230 1.00 35.54  ? 504 TYR A C   1 
ATOM 3614 O O   . TYR A 1 458 ? -11.923 15.505  170.071 1.00 41.66  ? 504 TYR A O   1 
ATOM 3615 C CB  . TYR A 1 458 ? -10.629 13.933  168.139 1.00 30.71  ? 504 TYR A CB  1 
ATOM 3616 C CG  . TYR A 1 458 ? -10.120 13.029  167.040 1.00 33.36  ? 504 TYR A CG  1 
ATOM 3617 C CD1 . TYR A 1 458 ? -9.713  13.550  165.821 1.00 35.68  ? 504 TYR A CD1 1 
ATOM 3618 C CD2 . TYR A 1 458 ? -10.042 11.657  167.223 1.00 32.91  ? 504 TYR A CD2 1 
ATOM 3619 C CE1 . TYR A 1 458 ? -9.246  12.733  164.817 1.00 38.04  ? 504 TYR A CE1 1 
ATOM 3620 C CE2 . TYR A 1 458 ? -9.576  10.830  166.222 1.00 32.08  ? 504 TYR A CE2 1 
ATOM 3621 C CZ  . TYR A 1 458 ? -9.180  11.374  165.021 1.00 38.25  ? 504 TYR A CZ  1 
ATOM 3622 O OH  . TYR A 1 458 ? -8.714  10.557  164.018 1.00 40.38  ? 504 TYR A OH  1 
ATOM 3623 N N   . LEU A 1 459 ? -13.965 14.859  169.383 1.00 31.82  ? 505 LEU A N   1 
ATOM 3624 C CA  . LEU A 1 459 ? -14.637 15.379  170.562 1.00 28.16  ? 505 LEU A CA  1 
ATOM 3625 C C   . LEU A 1 459 ? -14.380 14.485  171.766 1.00 33.33  ? 505 LEU A C   1 
ATOM 3626 O O   . LEU A 1 459 ? -14.217 13.269  171.642 1.00 46.80  ? 505 LEU A O   1 
ATOM 3627 C CB  . LEU A 1 459 ? -16.144 15.498  170.323 1.00 35.84  ? 505 LEU A CB  1 
ATOM 3628 C CG  . LEU A 1 459 ? -16.669 16.389  169.192 1.00 40.49  ? 505 LEU A CG  1 
ATOM 3629 C CD1 . LEU A 1 459 ? -15.971 17.737  169.197 1.00 38.76  ? 505 LEU A CD1 1 
ATOM 3630 C CD2 . LEU A 1 459 ? -16.563 15.719  167.826 1.00 40.09  ? 505 LEU A CD2 1 
ATOM 3631 N N   . THR A 1 460 ? -14.339 15.104  172.943 1.00 35.59  ? 506 THR A N   1 
ATOM 3632 C CA  . THR A 1 460 ? -14.205 14.378  174.195 1.00 40.45  ? 506 THR A CA  1 
ATOM 3633 C C   . THR A 1 460 ? -15.081 15.041  175.247 1.00 43.30  ? 506 THR A C   1 
ATOM 3634 O O   . THR A 1 460 ? -15.297 16.254  175.229 1.00 48.33  ? 506 THR A O   1 
ATOM 3635 C CB  . THR A 1 460 ? -12.747 14.323  174.669 1.00 39.60  ? 506 THR A CB  1 
ATOM 3636 O OG1 . THR A 1 460 ? -12.700 13.901  176.037 1.00 36.31  ? 506 THR A OG1 1 
ATOM 3637 C CG2 . THR A 1 460 ? -12.097 15.682  174.541 1.00 44.32  ? 506 THR A CG2 1 
ATOM 3638 N N   . TYR A 1 461 ? -15.582 14.228  176.172 1.00 45.09  ? 507 TYR A N   1 
ATOM 3639 C CA  . TYR A 1 461 ? -16.491 14.692  177.207 1.00 43.28  ? 507 TYR A CA  1 
ATOM 3640 C C   . TYR A 1 461 ? -15.865 14.474  178.575 1.00 48.90  ? 507 TYR A C   1 
ATOM 3641 O O   . TYR A 1 461 ? -15.285 13.423  178.858 1.00 52.29  ? 507 TYR A O   1 
ATOM 3642 C CB  . TYR A 1 461 ? -17.847 13.978  177.122 1.00 40.88  ? 507 TYR A CB  1 
ATOM 3643 C CG  . TYR A 1 461 ? -18.766 14.562  176.077 1.00 42.41  ? 507 TYR A CG  1 
ATOM 3644 C CD1 . TYR A 1 461 ? -18.573 14.295  174.730 1.00 38.82  ? 507 TYR A CD1 1 
ATOM 3645 C CD2 . TYR A 1 461 ? -19.822 15.385  176.435 1.00 49.15  ? 507 TYR A CD2 1 
ATOM 3646 C CE1 . TYR A 1 461 ? -19.405 14.831  173.773 1.00 40.59  ? 507 TYR A CE1 1 
ATOM 3647 C CE2 . TYR A 1 461 ? -20.661 15.925  175.482 1.00 48.22  ? 507 TYR A CE2 1 
ATOM 3648 C CZ  . TYR A 1 461 ? -20.448 15.643  174.152 1.00 48.28  ? 507 TYR A CZ  1 
ATOM 3649 O OH  . TYR A 1 461 ? -21.280 16.177  173.196 1.00 51.75  ? 507 TYR A OH  1 
ATOM 3650 N N   . GLY A 1 462 ? -15.992 15.487  179.427 1.00 52.35  ? 508 GLY A N   1 
ATOM 3651 C CA  . GLY A 1 462 ? -15.387 15.447  180.742 1.00 52.86  ? 508 GLY A CA  1 
ATOM 3652 C C   . GLY A 1 462 ? -16.141 14.592  181.738 1.00 54.06  ? 508 GLY A C   1 
ATOM 3653 O O   . GLY A 1 462 ? -15.556 14.095  182.705 1.00 50.64  ? 508 GLY A O   1 
ATOM 3654 N N   . ILE A 1 463 ? -17.443 14.411  181.516 1.00 57.43  ? 509 ILE A N   1 
ATOM 3655 C CA  . ILE A 1 463 ? -18.236 13.625  182.455 1.00 57.93  ? 509 ILE A CA  1 
ATOM 3656 C C   . ILE A 1 463 ? -18.177 12.143  182.119 1.00 59.27  ? 509 ILE A C   1 
ATOM 3657 O O   . ILE A 1 463 ? -18.112 11.303  183.022 1.00 58.55  ? 509 ILE A O   1 
ATOM 3658 C CB  . ILE A 1 463 ? -19.688 14.121  182.483 1.00 53.78  ? 509 ILE A CB  1 
ATOM 3659 C CG1 . ILE A 1 463 ? -20.184 14.393  181.064 1.00 53.61  ? 509 ILE A CG1 1 
ATOM 3660 C CG2 . ILE A 1 463 ? -19.797 15.363  183.343 1.00 56.39  ? 509 ILE A CG2 1 
ATOM 3661 C CD1 . ILE A 1 463 ? -21.647 14.719  180.995 1.00 55.44  ? 509 ILE A CD1 1 
ATOM 3662 N N   . ALA A 1 464 ? -18.215 11.794  180.836 1.00 56.47  ? 510 ALA A N   1 
ATOM 3663 C CA  . ALA A 1 464 ? -18.138 10.399  180.432 1.00 54.82  ? 510 ALA A CA  1 
ATOM 3664 C C   . ALA A 1 464 ? -16.716 9.864   180.423 1.00 57.09  ? 510 ALA A C   1 
ATOM 3665 O O   . ALA A 1 464 ? -16.532 8.645   180.334 1.00 60.34  ? 510 ALA A O   1 
ATOM 3666 C CB  . ALA A 1 464 ? -18.758 10.217  179.043 1.00 53.69  ? 510 ALA A CB  1 
ATOM 3667 N N   . GLN A 1 465 ? -15.717 10.743  180.517 1.00 51.34  ? 511 GLN A N   1 
ATOM 3668 C CA  . GLN A 1 465 ? -14.308 10.355  180.448 1.00 53.28  ? 511 GLN A CA  1 
ATOM 3669 C C   . GLN A 1 465 ? -14.027 9.550   179.184 1.00 54.39  ? 511 GLN A C   1 
ATOM 3670 O O   . GLN A 1 465 ? -13.257 8.589   179.190 1.00 57.22  ? 511 GLN A O   1 
ATOM 3671 C CB  . GLN A 1 465 ? -13.882 9.574   181.694 1.00 54.20  ? 511 GLN A CB  1 
ATOM 3672 C CG  . GLN A 1 465 ? -13.707 10.423  182.939 1.00 53.13  ? 511 GLN A CG  1 
ATOM 3673 C CD  . GLN A 1 465 ? -14.645 10.018  184.054 1.00 56.72  ? 511 GLN A CD  1 
ATOM 3674 O OE1 . GLN A 1 465 ? -15.861 10.009  183.886 1.00 59.77  ? 511 GLN A OE1 1 
ATOM 3675 N NE2 . GLN A 1 465 ? -14.080 9.679   185.207 1.00 56.61  ? 511 GLN A NE2 1 
ATOM 3676 N N   . GLU A 1 466 ? -14.666 9.945   178.086 1.00 46.07  ? 512 GLU A N   1 
ATOM 3677 C CA  . GLU A 1 466 ? -14.569 9.204   176.837 1.00 48.42  ? 512 GLU A CA  1 
ATOM 3678 C C   . GLU A 1 466 ? -14.494 10.175  175.671 1.00 47.28  ? 512 GLU A C   1 
ATOM 3679 O O   . GLU A 1 466 ? -15.297 11.107  175.584 1.00 47.75  ? 512 GLU A O   1 
ATOM 3680 C CB  . GLU A 1 466 ? -15.765 8.262   176.669 1.00 49.64  ? 512 GLU A CB  1 
ATOM 3681 C CG  . GLU A 1 466 ? -16.013 7.820   175.243 1.00 51.04  ? 512 GLU A CG  1 
ATOM 3682 C CD  . GLU A 1 466 ? -16.756 6.505   175.165 1.00 55.25  ? 512 GLU A CD  1 
ATOM 3683 O OE1 . GLU A 1 466 ? -16.439 5.694   174.270 1.00 55.25  ? 512 GLU A OE1 1 
ATOM 3684 O OE2 . GLU A 1 466 ? -17.657 6.283   175.998 1.00 57.09  ? 512 GLU A OE2 1 
ATOM 3685 N N   . SER A 1 467 ? -13.532 9.953   174.782 1.00 46.07  ? 513 SER A N   1 
ATOM 3686 C CA  . SER A 1 467 ? -13.380 10.765  173.587 1.00 40.26  ? 513 SER A CA  1 
ATOM 3687 C C   . SER A 1 467 ? -14.123 10.104  172.429 1.00 39.69  ? 513 SER A C   1 
ATOM 3688 O O   . SER A 1 467 ? -14.740 9.047   172.580 1.00 45.57  ? 513 SER A O   1 
ATOM 3689 C CB  . SER A 1 467 ? -11.901 10.971  173.269 1.00 42.26  ? 513 SER A CB  1 
ATOM 3690 O OG  . SER A 1 467 ? -11.187 11.392  174.418 1.00 49.27  ? 513 SER A OG  1 
ATOM 3691 N N   . PHE A 1 468 ? -14.068 10.719  171.251 1.00 36.67  ? 514 PHE A N   1 
ATOM 3692 C CA  . PHE A 1 468 ? -14.723 10.175  170.073 1.00 36.35  ? 514 PHE A CA  1 
ATOM 3693 C C   . PHE A 1 468 ? -13.781 10.258  168.882 1.00 40.86  ? 514 PHE A C   1 
ATOM 3694 O O   . PHE A 1 468 ? -12.887 11.106  168.834 1.00 41.28  ? 514 PHE A O   1 
ATOM 3695 C CB  . PHE A 1 468 ? -16.030 10.908  169.758 1.00 26.67  ? 514 PHE A CB  1 
ATOM 3696 C CG  . PHE A 1 468 ? -16.846 10.243  168.693 1.00 34.67  ? 514 PHE A CG  1 
ATOM 3697 C CD1 . PHE A 1 468 ? -17.472 9.036   168.937 1.00 42.19  ? 514 PHE A CD1 1 
ATOM 3698 C CD2 . PHE A 1 468 ? -16.975 10.817  167.443 1.00 39.54  ? 514 PHE A CD2 1 
ATOM 3699 C CE1 . PHE A 1 468 ? -18.215 8.417   167.958 1.00 40.61  ? 514 PHE A CE1 1 
ATOM 3700 C CE2 . PHE A 1 468 ? -17.719 10.202  166.461 1.00 42.01  ? 514 PHE A CE2 1 
ATOM 3701 C CZ  . PHE A 1 468 ? -18.339 9.001   166.719 1.00 41.34  ? 514 PHE A CZ  1 
ATOM 3702 N N   . GLY A 1 469 ? -13.997 9.369   167.917 1.00 40.11  ? 515 GLY A N   1 
ATOM 3703 C CA  . GLY A 1 469 ? -13.168 9.301   166.739 1.00 37.34  ? 515 GLY A CA  1 
ATOM 3704 C C   . GLY A 1 469 ? -13.401 10.463  165.799 1.00 37.79  ? 515 GLY A C   1 
ATOM 3705 O O   . GLY A 1 469 ? -13.909 11.518  166.190 1.00 44.49  ? 515 GLY A O   1 
ATOM 3706 N N   . PRO A 1 470 ? -13.030 10.290  164.530 1.00 30.10  ? 516 PRO A N   1 
ATOM 3707 C CA  . PRO A 1 470 ? -13.153 11.389  163.560 1.00 31.49  ? 516 PRO A CA  1 
ATOM 3708 C C   . PRO A 1 470 ? -14.611 11.753  163.329 1.00 38.09  ? 516 PRO A C   1 
ATOM 3709 O O   . PRO A 1 470 ? -15.430 10.901  162.981 1.00 40.54  ? 516 PRO A O   1 
ATOM 3710 C CB  . PRO A 1 470 ? -12.504 10.819  162.292 1.00 30.29  ? 516 PRO A CB  1 
ATOM 3711 C CG  . PRO A 1 470 ? -11.710 9.641   162.750 1.00 36.11  ? 516 PRO A CG  1 
ATOM 3712 C CD  . PRO A 1 470 ? -12.443 9.087   163.924 1.00 32.27  ? 516 PRO A CD  1 
ATOM 3713 N N   . PHE A 1 471 ? -14.932 13.031  163.528 1.00 30.96  ? 517 PHE A N   1 
ATOM 3714 C CA  . PHE A 1 471 ? -16.263 13.557  163.237 1.00 30.21  ? 517 PHE A CA  1 
ATOM 3715 C C   . PHE A 1 471 ? -16.232 14.130  161.825 1.00 31.01  ? 517 PHE A C   1 
ATOM 3716 O O   . PHE A 1 471 ? -16.173 15.340  161.611 1.00 39.73  ? 517 PHE A O   1 
ATOM 3717 C CB  . PHE A 1 471 ? -16.672 14.602  164.267 1.00 29.85  ? 517 PHE A CB  1 
ATOM 3718 C CG  . PHE A 1 471 ? -18.144 14.882  164.290 1.00 35.37  ? 517 PHE A CG  1 
ATOM 3719 C CD1 . PHE A 1 471 ? -18.991 14.137  165.090 1.00 33.90  ? 517 PHE A CD1 1 
ATOM 3720 C CD2 . PHE A 1 471 ? -18.683 15.881  163.498 1.00 32.71  ? 517 PHE A CD2 1 
ATOM 3721 C CE1 . PHE A 1 471 ? -20.346 14.391  165.108 1.00 32.94  ? 517 PHE A CE1 1 
ATOM 3722 C CE2 . PHE A 1 471 ? -20.037 16.137  163.511 1.00 35.47  ? 517 PHE A CE2 1 
ATOM 3723 C CZ  . PHE A 1 471 ? -20.870 15.392  164.317 1.00 36.13  ? 517 PHE A CZ  1 
ATOM 3724 N N   . ALA A 1 472 ? -16.270 13.232  160.845 1.00 27.83  ? 518 ALA A N   1 
ATOM 3725 C CA  . ALA A 1 472 ? -16.172 13.627  159.450 1.00 32.08  ? 518 ALA A CA  1 
ATOM 3726 C C   . ALA A 1 472 ? -16.905 12.609  158.591 1.00 37.46  ? 518 ALA A C   1 
ATOM 3727 O O   . ALA A 1 472 ? -17.195 11.491  159.022 1.00 44.53  ? 518 ALA A O   1 
ATOM 3728 C CB  . ALA A 1 472 ? -14.712 13.758  159.008 1.00 33.28  ? 518 ALA A CB  1 
ATOM 3729 N N   . GLN A 1 473 ? -17.205 13.015  157.361 1.00 32.58  ? 519 GLN A N   1 
ATOM 3730 C CA  . GLN A 1 473 ? -17.866 12.149  156.394 1.00 30.78  ? 519 GLN A CA  1 
ATOM 3731 C C   . GLN A 1 473 ? -16.795 11.380  155.633 1.00 33.07  ? 519 GLN A C   1 
ATOM 3732 O O   . GLN A 1 473 ? -16.064 11.957  154.822 1.00 36.57  ? 519 GLN A O   1 
ATOM 3733 C CB  . GLN A 1 473 ? -18.741 12.967  155.448 1.00 31.96  ? 519 GLN A CB  1 
ATOM 3734 C CG  . GLN A 1 473 ? -19.190 12.217  154.208 1.00 38.85  ? 519 GLN A CG  1 
ATOM 3735 C CD  . GLN A 1 473 ? -20.496 12.742  153.654 1.00 39.24  ? 519 GLN A CD  1 
ATOM 3736 O OE1 . GLN A 1 473 ? -21.164 13.565  154.279 1.00 36.95  ? 519 GLN A OE1 1 
ATOM 3737 N NE2 . GLN A 1 473 ? -20.867 12.271  152.470 1.00 37.09  ? 519 GLN A NE2 1 
ATOM 3738 N N   . LEU A 1 474 ? -16.696 10.081  155.898 1.00 38.63  ? 520 LEU A N   1 
ATOM 3739 C CA  . LEU A 1 474 ? -15.683 9.253   155.261 1.00 38.25  ? 520 LEU A CA  1 
ATOM 3740 C C   . LEU A 1 474 ? -16.134 8.854   153.862 1.00 41.38  ? 520 LEU A C   1 
ATOM 3741 O O   . LEU A 1 474 ? -17.239 8.334   153.681 1.00 42.56  ? 520 LEU A O   1 
ATOM 3742 C CB  . LEU A 1 474 ? -15.401 8.013   156.106 1.00 35.37  ? 520 LEU A CB  1 
ATOM 3743 C CG  . LEU A 1 474 ? -14.953 8.284   157.543 1.00 34.19  ? 520 LEU A CG  1 
ATOM 3744 C CD1 . LEU A 1 474 ? -14.632 6.991   158.261 1.00 34.97  ? 520 LEU A CD1 1 
ATOM 3745 C CD2 . LEU A 1 474 ? -13.756 9.215   157.568 1.00 32.83  ? 520 LEU A CD2 1 
ATOM 3746 N N   . ASN A 1 475 ? -15.273 9.095   152.874 1.00 38.36  ? 521 ASN A N   1 
ATOM 3747 C CA  . ASN A 1 475 ? -15.582 8.803   151.481 1.00 44.09  ? 521 ASN A CA  1 
ATOM 3748 C C   . ASN A 1 475 ? -14.719 7.676   150.929 1.00 44.77  ? 521 ASN A C   1 
ATOM 3749 O O   . ASN A 1 475 ? -15.246 6.677   150.431 1.00 46.27  ? 521 ASN A O   1 
ATOM 3750 C CB  . ASN A 1 475 ? -15.413 10.073  150.634 1.00 41.33  ? 521 ASN A CB  1 
ATOM 3751 C CG  . ASN A 1 475 ? -15.409 9.786   149.146 1.00 50.44  ? 521 ASN A CG  1 
ATOM 3752 O OD1 . ASN A 1 475 ? -16.463 9.644   148.526 1.00 51.08  ? 521 ASN A OD1 1 
ATOM 3753 N ND2 . ASN A 1 475 ? -14.219 9.705   148.562 1.00 47.04  ? 521 ASN A ND2 1 
ATOM 3754 N N   . ASP A 1 476 ? -13.398 7.809   151.007 1.00 39.97  ? 522 ASP A N   1 
ATOM 3755 C CA  . ASP A 1 476 ? -12.484 6.754   150.577 1.00 43.50  ? 522 ASP A CA  1 
ATOM 3756 C C   . ASP A 1 476 ? -11.232 6.885   151.428 1.00 42.14  ? 522 ASP A C   1 
ATOM 3757 O O   . ASP A 1 476 ? -10.359 7.702   151.124 1.00 44.82  ? 522 ASP A O   1 
ATOM 3758 C CB  . ASP A 1 476 ? -12.159 6.868   149.093 1.00 45.06  ? 522 ASP A CB  1 
ATOM 3759 C CG  . ASP A 1 476 ? -11.277 5.739   148.604 1.00 47.42  ? 522 ASP A CG  1 
ATOM 3760 O OD1 . ASP A 1 476 ? -11.334 4.642   149.195 1.00 46.69  ? 522 ASP A OD1 1 
ATOM 3761 O OD2 . ASP A 1 476 ? -10.528 5.947   147.629 1.00 49.80  ? 522 ASP A OD2 1 
ATOM 3762 N N   . TRP A 1 477 ? -11.142 6.081   152.481 1.00 28.01  ? 523 TRP A N   1 
ATOM 3763 C CA  . TRP A 1 477 ? -10.196 6.317   153.556 1.00 26.63  ? 523 TRP A CA  1 
ATOM 3764 C C   . TRP A 1 477 ? -9.253  5.134   153.707 1.00 28.16  ? 523 TRP A C   1 
ATOM 3765 O O   . TRP A 1 477 ? -9.457  4.062   153.134 1.00 34.06  ? 523 TRP A O   1 
ATOM 3766 C CB  . TRP A 1 477 ? -10.929 6.568   154.878 1.00 29.97  ? 523 TRP A CB  1 
ATOM 3767 C CG  . TRP A 1 477 ? -11.939 5.515   155.182 1.00 27.38  ? 523 TRP A CG  1 
ATOM 3768 C CD1 . TRP A 1 477 ? -13.228 5.468   154.748 1.00 31.92  ? 523 TRP A CD1 1 
ATOM 3769 C CD2 . TRP A 1 477 ? -11.739 4.344   155.977 1.00 31.96  ? 523 TRP A CD2 1 
ATOM 3770 N NE1 . TRP A 1 477 ? -13.848 4.341   155.228 1.00 34.55  ? 523 TRP A NE1 1 
ATOM 3771 C CE2 . TRP A 1 477 ? -12.953 3.634   155.987 1.00 32.12  ? 523 TRP A CE2 1 
ATOM 3772 C CE3 . TRP A 1 477 ? -10.651 3.828   156.686 1.00 31.21  ? 523 TRP A CE3 1 
ATOM 3773 C CZ2 . TRP A 1 477 ? -13.111 2.437   156.675 1.00 32.04  ? 523 TRP A CZ2 1 
ATOM 3774 C CZ3 . TRP A 1 477 ? -10.810 2.640   157.368 1.00 30.30  ? 523 TRP A CZ3 1 
ATOM 3775 C CH2 . TRP A 1 477 ? -12.029 1.957   157.358 1.00 32.73  ? 523 TRP A CH2 1 
ATOM 3776 N N   . THR A 1 478 ? -8.207  5.355   154.500 1.00 31.77  ? 524 THR A N   1 
ATOM 3777 C CA  . THR A 1 478 ? -7.269  4.314   154.886 1.00 31.56  ? 524 THR A CA  1 
ATOM 3778 C C   . THR A 1 478 ? -6.693  4.682   156.243 1.00 29.30  ? 524 THR A C   1 
ATOM 3779 O O   . THR A 1 478 ? -6.744  5.840   156.665 1.00 37.83  ? 524 THR A O   1 
ATOM 3780 C CB  . THR A 1 478 ? -6.144  4.139   153.861 1.00 27.02  ? 524 THR A CB  1 
ATOM 3781 O OG1 . THR A 1 478 ? -5.345  3.006   154.217 1.00 18.71  ? 524 THR A OG1 1 
ATOM 3782 C CG2 . THR A 1 478 ? -5.257  5.369   153.836 1.00 31.26  ? 524 THR A CG2 1 
ATOM 3783 N N   . ILE A 1 479 ? -6.149  3.685   156.930 1.00 23.62  ? 525 ILE A N   1 
ATOM 3784 C CA  . ILE A 1 479 ? -5.542  3.881   158.240 1.00 23.40  ? 525 ILE A CA  1 
ATOM 3785 C C   . ILE A 1 479 ? -4.050  4.100   158.041 1.00 27.86  ? 525 ILE A C   1 
ATOM 3786 O O   . ILE A 1 479 ? -3.352  3.231   157.505 1.00 30.79  ? 525 ILE A O   1 
ATOM 3787 C CB  . ILE A 1 479 ? -5.807  2.687   159.169 1.00 28.78  ? 525 ILE A CB  1 
ATOM 3788 C CG1 . ILE A 1 479 ? -7.296  2.596   159.501 1.00 33.19  ? 525 ILE A CG1 1 
ATOM 3789 C CG2 . ILE A 1 479 ? -4.994  2.816   160.440 1.00 25.99  ? 525 ILE A CG2 1 
ATOM 3790 C CD1 . ILE A 1 479 ? -7.687  1.314   160.196 1.00 28.42  ? 525 ILE A CD1 1 
ATOM 3791 N N   . LEU A 1 480 ? -3.561  5.256   158.473 1.00 38.34  ? 526 LEU A N   1 
ATOM 3792 C CA  . LEU A 1 480 ? -2.160  5.611   158.325 1.00 31.50  ? 526 LEU A CA  1 
ATOM 3793 C C   . LEU A 1 480 ? -1.399  5.317   159.609 1.00 29.95  ? 526 LEU A C   1 
ATOM 3794 O O   . LEU A 1 480 ? -1.913  5.493   160.716 1.00 35.75  ? 526 LEU A O   1 
ATOM 3795 C CB  . LEU A 1 480 ? -2.002  7.086   157.958 1.00 29.26  ? 526 LEU A CB  1 
ATOM 3796 C CG  . LEU A 1 480 ? -1.872  7.388   156.467 1.00 29.66  ? 526 LEU A CG  1 
ATOM 3797 C CD1 . LEU A 1 480 ? -1.637  8.868   156.247 1.00 33.53  ? 526 LEU A CD1 1 
ATOM 3798 C CD2 . LEU A 1 480 ? -0.748  6.573   155.862 1.00 35.15  ? 526 LEU A CD2 1 
ATOM 3799 N N   . THR A 1 481 ? -0.165  4.858   159.446 1.00 33.45  ? 527 THR A N   1 
ATOM 3800 C CA  . THR A 1 481 ? 0.703   4.513   160.557 1.00 35.42  ? 527 THR A CA  1 
ATOM 3801 C C   . THR A 1 481 ? 1.788   5.573   160.698 1.00 40.47  ? 527 THR A C   1 
ATOM 3802 O O   . THR A 1 481 ? 2.091   6.304   159.748 1.00 50.37  ? 527 THR A O   1 
ATOM 3803 C CB  . THR A 1 481 ? 1.329   3.131   160.347 1.00 42.78  ? 527 THR A CB  1 
ATOM 3804 O OG1 . THR A 1 481 ? 0.330   2.231   159.854 1.00 47.16  ? 527 THR A OG1 1 
ATOM 3805 C CG2 . THR A 1 481 ? 1.865   2.576   161.657 1.00 45.55  ? 527 THR A CG2 1 
ATOM 3806 N N   . GLY A 1 482 ? 2.357   5.661   161.901 1.00 36.00  ? 528 GLY A N   1 
ATOM 3807 C CA  . GLY A 1 482 ? 3.396   6.646   162.144 1.00 40.12  ? 528 GLY A CA  1 
ATOM 3808 C C   . GLY A 1 482 ? 4.590   6.476   161.226 1.00 39.80  ? 528 GLY A C   1 
ATOM 3809 O O   . GLY A 1 482 ? 5.178   7.457   160.772 1.00 41.07  ? 528 GLY A O   1 
ATOM 3810 N N   . GLU A 1 483 ? 4.955   5.227   160.928 1.00 34.41  ? 529 GLU A N   1 
ATOM 3811 C CA  . GLU A 1 483 ? 6.094   4.984   160.048 1.00 37.21  ? 529 GLU A CA  1 
ATOM 3812 C C   . GLU A 1 483 ? 5.804   5.426   158.618 1.00 39.66  ? 529 GLU A C   1 
ATOM 3813 O O   . GLU A 1 483 ? 6.665   6.023   157.961 1.00 49.98  ? 529 GLU A O   1 
ATOM 3814 C CB  . GLU A 1 483 ? 6.478   3.507   160.089 1.00 42.51  ? 529 GLU A CB  1 
ATOM 3815 C CG  . GLU A 1 483 ? 7.065   3.069   161.419 1.00 48.68  ? 529 GLU A CG  1 
ATOM 3816 C CD  . GLU A 1 483 ? 8.214   3.953   161.867 1.00 51.14  ? 529 GLU A CD  1 
ATOM 3817 O OE1 . GLU A 1 483 ? 9.216   4.051   161.129 1.00 46.49  ? 529 GLU A OE1 1 
ATOM 3818 O OE2 . GLU A 1 483 ? 8.115   4.551   162.959 1.00 48.59  ? 529 GLU A OE2 1 
ATOM 3819 N N   . THR A 1 484 ? 4.603   5.135   158.113 1.00 33.02  ? 530 THR A N   1 
ATOM 3820 C CA  . THR A 1 484 ? 4.240   5.592   156.775 1.00 30.63  ? 530 THR A CA  1 
ATOM 3821 C C   . THR A 1 484 ? 4.204   7.112   156.708 1.00 35.10  ? 530 THR A C   1 
ATOM 3822 O O   . THR A 1 484 ? 4.669   7.712   155.728 1.00 47.69  ? 530 THR A O   1 
ATOM 3823 C CB  . THR A 1 484 ? 2.890   5.008   156.365 1.00 36.27  ? 530 THR A CB  1 
ATOM 3824 O OG1 . THR A 1 484 ? 1.954   5.176   157.435 1.00 42.90  ? 530 THR A OG1 1 
ATOM 3825 C CG2 . THR A 1 484 ? 3.026   3.530   156.051 1.00 37.24  ? 530 THR A CG2 1 
ATOM 3826 N N   . LEU A 1 485 ? 3.658   7.753   157.743 1.00 30.01  ? 531 LEU A N   1 
ATOM 3827 C CA  . LEU A 1 485 ? 3.651   9.210   157.778 1.00 32.21  ? 531 LEU A CA  1 
ATOM 3828 C C   . LEU A 1 485 ? 5.067   9.765   157.813 1.00 38.74  ? 531 LEU A C   1 
ATOM 3829 O O   . LEU A 1 485 ? 5.359   10.768  157.156 1.00 44.68  ? 531 LEU A O   1 
ATOM 3830 C CB  . LEU A 1 485 ? 2.854   9.711   158.979 1.00 33.58  ? 531 LEU A CB  1 
ATOM 3831 C CG  . LEU A 1 485 ? 2.194   11.067  158.735 1.00 35.60  ? 531 LEU A CG  1 
ATOM 3832 C CD1 . LEU A 1 485 ? 1.161   10.950  157.634 1.00 37.22  ? 531 LEU A CD1 1 
ATOM 3833 C CD2 . LEU A 1 485 ? 1.579   11.623  160.003 1.00 35.91  ? 531 LEU A CD2 1 
ATOM 3834 N N   . ALA A 1 486 ? 5.957   9.135   158.581 1.00 35.02  ? 532 ALA A N   1 
ATOM 3835 C CA  . ALA A 1 486 ? 7.343   9.581   158.631 1.00 31.47  ? 532 ALA A CA  1 
ATOM 3836 C C   . ALA A 1 486 ? 8.015   9.447   157.272 1.00 31.61  ? 532 ALA A C   1 
ATOM 3837 O O   . ALA A 1 486 ? 8.760   10.339  156.855 1.00 41.30  ? 532 ALA A O   1 
ATOM 3838 C CB  . ALA A 1 486 ? 8.111   8.791   159.689 1.00 29.15  ? 532 ALA A CB  1 
ATOM 3839 N N   . ARG A 1 487 ? 7.770   8.338   156.570 1.00 23.24  ? 533 ARG A N   1 
ATOM 3840 C CA  . ARG A 1 487 ? 8.340   8.173   155.236 1.00 24.77  ? 533 ARG A CA  1 
ATOM 3841 C C   . ARG A 1 487 ? 7.837   9.252   154.285 1.00 26.42  ? 533 ARG A C   1 
ATOM 3842 O O   . ARG A 1 487 ? 8.623   9.852   153.539 1.00 36.83  ? 533 ARG A O   1 
ATOM 3843 C CB  . ARG A 1 487 ? 8.006   6.790   154.681 1.00 29.73  ? 533 ARG A CB  1 
ATOM 3844 C CG  . ARG A 1 487 ? 8.733   5.640   155.346 1.00 33.90  ? 533 ARG A CG  1 
ATOM 3845 C CD  . ARG A 1 487 ? 8.509   4.359   154.564 1.00 31.58  ? 533 ARG A CD  1 
ATOM 3846 N NE  . ARG A 1 487 ? 8.845   4.534   153.156 1.00 30.22  ? 533 ARG A NE  1 
ATOM 3847 C CZ  . ARG A 1 487 ? 8.684   3.605   152.224 1.00 31.74  ? 533 ARG A CZ  1 
ATOM 3848 N NH1 . ARG A 1 487 ? 8.176   2.419   152.512 1.00 34.19  ? 533 ARG A NH1 1 
ATOM 3849 N NH2 . ARG A 1 487 ? 9.041   3.873   150.972 1.00 30.40  ? 533 ARG A NH2 1 
ATOM 3850 N N   . MET A 1 488 ? 6.529   9.514   154.301 1.00 31.20  ? 534 MET A N   1 
ATOM 3851 C CA  . MET A 1 488 ? 5.975   10.525  153.406 1.00 30.04  ? 534 MET A CA  1 
ATOM 3852 C C   . MET A 1 488 ? 6.507   11.912  153.743 1.00 32.33  ? 534 MET A C   1 
ATOM 3853 O O   . MET A 1 488 ? 6.806   12.703  152.842 1.00 40.97  ? 534 MET A O   1 
ATOM 3854 C CB  . MET A 1 488 ? 4.450   10.500  153.464 1.00 25.09  ? 534 MET A CB  1 
ATOM 3855 C CG  . MET A 1 488 ? 3.833   9.366   152.667 1.00 32.36  ? 534 MET A CG  1 
ATOM 3856 S SD  . MET A 1 488 ? 2.071   9.577   152.374 1.00 57.62  ? 534 MET A SD  1 
ATOM 3857 C CE  . MET A 1 488 ? 1.407   8.236   153.356 1.00 28.89  ? 534 MET A CE  1 
ATOM 3858 N N   . HIS A 1 489 ? 6.634   12.224  155.034 1.00 30.92  ? 535 HIS A N   1 
ATOM 3859 C CA  . HIS A 1 489 ? 7.165   13.521  155.436 1.00 27.79  ? 535 HIS A CA  1 
ATOM 3860 C C   . HIS A 1 489 ? 8.627   13.667  155.041 1.00 32.84  ? 535 HIS A C   1 
ATOM 3861 O O   . HIS A 1 489 ? 9.050   14.741  154.604 1.00 32.61  ? 535 HIS A O   1 
ATOM 3862 C CB  . HIS A 1 489 ? 6.988   13.713  156.940 1.00 26.42  ? 535 HIS A CB  1 
ATOM 3863 C CG  . HIS A 1 489 ? 5.582   14.023  157.345 1.00 29.01  ? 535 HIS A CG  1 
ATOM 3864 N ND1 . HIS A 1 489 ? 4.731   14.769  156.559 1.00 26.22  ? 535 HIS A ND1 1 
ATOM 3865 C CD2 . HIS A 1 489 ? 4.878   13.689  158.451 1.00 29.47  ? 535 HIS A CD2 1 
ATOM 3866 C CE1 . HIS A 1 489 ? 3.563   14.881  157.164 1.00 32.11  ? 535 HIS A CE1 1 
ATOM 3867 N NE2 . HIS A 1 489 ? 3.625   14.235  158.314 1.00 30.59  ? 535 HIS A NE2 1 
ATOM 3868 N N   . GLU A 1 490 ? 9.416   12.602  155.197 1.00 37.56  ? 536 GLU A N   1 
ATOM 3869 C CA  . GLU A 1 490 ? 10.803  12.641  154.749 1.00 29.41  ? 536 GLU A CA  1 
ATOM 3870 C C   . GLU A 1 490 ? 10.883  12.905  153.254 1.00 28.57  ? 536 GLU A C   1 
ATOM 3871 O O   . GLU A 1 490 ? 11.670  13.747  152.805 1.00 38.50  ? 536 GLU A O   1 
ATOM 3872 C CB  . GLU A 1 490 ? 11.502  11.329  155.097 1.00 27.60  ? 536 GLU A CB  1 
ATOM 3873 C CG  . GLU A 1 490 ? 12.984  11.304  154.774 1.00 40.11  ? 536 GLU A CG  1 
ATOM 3874 C CD  . GLU A 1 490 ? 13.850  11.136  156.006 1.00 48.66  ? 536 GLU A CD  1 
ATOM 3875 O OE1 . GLU A 1 490 ? 13.291  11.037  157.118 1.00 48.60  ? 536 GLU A OE1 1 
ATOM 3876 O OE2 . GLU A 1 490 ? 15.090  11.094  155.861 1.00 43.99  ? 536 GLU A OE2 1 
ATOM 3877 N N   . VAL A 1 491 ? 10.054  12.211  152.470 1.00 29.27  ? 537 VAL A N   1 
ATOM 3878 C CA  . VAL A 1 491 ? 10.056  12.418  151.025 1.00 26.09  ? 537 VAL A CA  1 
ATOM 3879 C C   . VAL A 1 491 ? 9.688   13.857  150.691 1.00 25.80  ? 537 VAL A C   1 
ATOM 3880 O O   . VAL A 1 491 ? 10.359  14.516  149.885 1.00 32.08  ? 537 VAL A O   1 
ATOM 3881 C CB  . VAL A 1 491 ? 9.102   11.422  150.342 1.00 27.81  ? 537 VAL A CB  1 
ATOM 3882 C CG1 . VAL A 1 491 ? 8.793   11.870  148.925 1.00 28.85  ? 537 VAL A CG1 1 
ATOM 3883 C CG2 . VAL A 1 491 ? 9.697   10.028  150.349 1.00 32.55  ? 537 VAL A CG2 1 
ATOM 3884 N N   . CYS A 1 492 ? 8.629   14.374  151.318 1.00 31.70  ? 538 CYS A N   1 
ATOM 3885 C CA  . CYS A 1 492 ? 8.167   15.719  150.995 1.00 35.76  ? 538 CYS A CA  1 
ATOM 3886 C C   . CYS A 1 492 ? 9.197   16.773  151.382 1.00 34.37  ? 538 CYS A C   1 
ATOM 3887 O O   . CYS A 1 492 ? 9.467   17.692  150.603 1.00 42.59  ? 538 CYS A O   1 
ATOM 3888 C CB  . CYS A 1 492 ? 6.825   15.992  151.677 1.00 40.00  ? 538 CYS A CB  1 
ATOM 3889 S SG  . CYS A 1 492 ? 6.931   16.712  153.327 1.00 58.71  ? 538 CYS A SG  1 
ATOM 3890 N N   . VAL A 1 493 ? 9.799   16.650  152.567 1.00 27.41  ? 539 VAL A N   1 
ATOM 3891 C CA  . VAL A 1 493 ? 10.783  17.637  153.003 1.00 25.32  ? 539 VAL A CA  1 
ATOM 3892 C C   . VAL A 1 493 ? 12.029  17.584  152.126 1.00 27.52  ? 539 VAL A C   1 
ATOM 3893 O O   . VAL A 1 493 ? 12.574  18.626  151.737 1.00 30.29  ? 539 VAL A O   1 
ATOM 3894 C CB  . VAL A 1 493 ? 11.121  17.430  154.490 1.00 27.17  ? 539 VAL A CB  1 
ATOM 3895 C CG1 . VAL A 1 493 ? 12.304  18.289  154.887 1.00 30.08  ? 539 VAL A CG1 1 
ATOM 3896 C CG2 . VAL A 1 493 ? 9.918   17.759  155.352 1.00 28.23  ? 539 VAL A CG2 1 
ATOM 3897 N N   . THR A 1 494 ? 12.500  16.376  151.796 1.00 29.55  ? 540 THR A N   1 
ATOM 3898 C CA  . THR A 1 494 ? 13.649  16.256  150.907 1.00 22.83  ? 540 THR A CA  1 
ATOM 3899 C C   . THR A 1 494 ? 13.363  16.874  149.547 1.00 25.52  ? 540 THR A C   1 
ATOM 3900 O O   . THR A 1 494 ? 14.234  17.532  148.969 1.00 32.38  ? 540 THR A O   1 
ATOM 3901 C CB  . THR A 1 494 ? 14.039  14.786  150.750 1.00 27.47  ? 540 THR A CB  1 
ATOM 3902 O OG1 . THR A 1 494 ? 14.280  14.214  152.040 1.00 31.84  ? 540 THR A OG1 1 
ATOM 3903 C CG2 . THR A 1 494 ? 15.297  14.653  149.905 1.00 28.62  ? 540 THR A CG2 1 
ATOM 3904 N N   . SER A 1 495 ? 12.152  16.675  149.022 1.00 25.21  ? 541 SER A N   1 
ATOM 3905 C CA  . SER A 1 495 ? 11.794  17.270  147.739 1.00 26.36  ? 541 SER A CA  1 
ATOM 3906 C C   . SER A 1 495 ? 11.724  18.790  147.828 1.00 28.87  ? 541 SER A C   1 
ATOM 3907 O O   . SER A 1 495 ? 12.133  19.494  146.897 1.00 32.15  ? 541 SER A O   1 
ATOM 3908 C CB  . SER A 1 495 ? 10.466  16.698  147.254 1.00 33.94  ? 541 SER A CB  1 
ATOM 3909 O OG  . SER A 1 495 ? 9.381   17.328  147.907 1.00 44.36  ? 541 SER A OG  1 
ATOM 3910 N N   . MET A 1 496 ? 11.193  19.319  148.932 1.00 35.03  ? 542 MET A N   1 
ATOM 3911 C CA  . MET A 1 496 ? 11.124  20.765  149.108 1.00 30.50  ? 542 MET A CA  1 
ATOM 3912 C C   . MET A 1 496 ? 12.490  21.417  149.235 1.00 33.27  ? 542 MET A C   1 
ATOM 3913 O O   . MET A 1 496 ? 12.682  22.517  148.708 1.00 36.48  ? 542 MET A O   1 
ATOM 3914 C CB  . MET A 1 496 ? 10.302  21.123  150.348 1.00 25.23  ? 542 MET A CB  1 
ATOM 3915 C CG  . MET A 1 496 ? 8.877   20.626  150.338 1.00 36.39  ? 542 MET A CG  1 
ATOM 3916 S SD  . MET A 1 496 ? 7.736   21.875  149.733 1.00 48.55  ? 542 MET A SD  1 
ATOM 3917 C CE  . MET A 1 496 ? 7.734   23.002  151.125 1.00 44.96  ? 542 MET A CE  1 
ATOM 3918 N N   . PHE A 1 497 ? 13.434  20.776  149.911 1.00 37.07  ? 543 PHE A N   1 
ATOM 3919 C CA  . PHE A 1 497 ? 14.761  21.354  150.125 1.00 32.12  ? 543 PHE A CA  1 
ATOM 3920 C C   . PHE A 1 497 ? 15.732  20.916  149.037 1.00 36.77  ? 543 PHE A C   1 
ATOM 3921 O O   . PHE A 1 497 ? 16.810  20.397  149.319 1.00 42.94  ? 543 PHE A O   1 
ATOM 3922 C CB  . PHE A 1 497 ? 15.280  20.965  151.502 1.00 35.30  ? 543 PHE A CB  1 
ATOM 3923 C CG  . PHE A 1 497 ? 14.774  21.836  152.611 1.00 31.86  ? 543 PHE A CG  1 
ATOM 3924 C CD1 . PHE A 1 497 ? 13.418  21.975  152.834 1.00 39.17  ? 543 PHE A CD1 1 
ATOM 3925 C CD2 . PHE A 1 497 ? 15.653  22.514  153.432 1.00 33.97  ? 543 PHE A CD2 1 
ATOM 3926 C CE1 . PHE A 1 497 ? 12.949  22.773  153.855 1.00 39.41  ? 543 PHE A CE1 1 
ATOM 3927 C CE2 . PHE A 1 497 ? 15.187  23.315  154.453 1.00 37.59  ? 543 PHE A CE2 1 
ATOM 3928 C CZ  . PHE A 1 497 ? 13.835  23.442  154.665 1.00 37.63  ? 543 PHE A CZ  1 
ATOM 3929 N N   . ASP A 1 498 ? 15.362  21.117  147.776 1.00 40.19  ? 544 ASP A N   1 
ATOM 3930 C CA  . ASP A 1 498 ? 16.143  20.642  146.643 1.00 37.11  ? 544 ASP A CA  1 
ATOM 3931 C C   . ASP A 1 498 ? 16.533  21.815  145.759 1.00 41.28  ? 544 ASP A C   1 
ATOM 3932 O O   . ASP A 1 498 ? 15.769  22.775  145.622 1.00 51.55  ? 544 ASP A O   1 
ATOM 3933 C CB  . ASP A 1 498 ? 15.360  19.610  145.828 1.00 41.80  ? 544 ASP A CB  1 
ATOM 3934 C CG  . ASP A 1 498 ? 16.264  18.640  145.100 1.00 46.44  ? 544 ASP A CG  1 
ATOM 3935 O OD1 . ASP A 1 498 ? 17.137  18.038  145.758 1.00 49.93  ? 544 ASP A OD1 1 
ATOM 3936 O OD2 . ASP A 1 498 ? 16.103  18.476  143.873 1.00 47.18  ? 544 ASP A OD2 1 
ATOM 3937 N N   . VAL A 1 499 ? 17.716  21.732  145.161 1.00 37.31  ? 545 VAL A N   1 
ATOM 3938 C CA  . VAL A 1 499 ? 18.191  22.763  144.252 1.00 43.86  ? 545 VAL A CA  1 
ATOM 3939 C C   . VAL A 1 499 ? 18.357  22.191  142.849 1.00 43.50  ? 545 VAL A C   1 
ATOM 3940 O O   . VAL A 1 499 ? 17.544  22.448  141.962 1.00 39.14  ? 545 VAL A O   1 
ATOM 3941 C CB  . VAL A 1 499 ? 19.509  23.373  144.751 1.00 43.17  ? 545 VAL A CB  1 
ATOM 3942 C CG1 . VAL A 1 499 ? 20.198  24.134  143.630 1.00 43.17  ? 545 VAL A CG1 1 
ATOM 3943 C CG2 . VAL A 1 499 ? 19.250  24.285  145.938 1.00 39.58  ? 545 VAL A CG2 1 
ATOM 3944 N N   . VAL B 1 1   ? 8.890   18.885  142.826 1.00 89.89  ? 47  VAL B N   1 
ATOM 3945 C CA  . VAL B 1 1   ? 8.656   19.020  141.394 1.00 93.57  ? 47  VAL B CA  1 
ATOM 3946 C C   . VAL B 1 1   ? 9.572   18.087  140.615 1.00 91.89  ? 47  VAL B C   1 
ATOM 3947 O O   . VAL B 1 1   ? 9.172   16.985  140.235 1.00 91.87  ? 47  VAL B O   1 
ATOM 3948 C CB  . VAL B 1 1   ? 8.849   20.474  140.934 1.00 96.07  ? 47  VAL B CB  1 
ATOM 3949 C CG1 . VAL B 1 1   ? 8.115   20.715  139.624 1.00 92.46  ? 47  VAL B CG1 1 
ATOM 3950 C CG2 . VAL B 1 1   ? 8.365   21.437  142.007 1.00 92.33  ? 47  VAL B CG2 1 
ATOM 3951 N N   . ALA B 1 2   ? 10.806  18.533  140.374 1.00 74.85  ? 48  ALA B N   1 
ATOM 3952 C CA  . ALA B 1 2   ? 11.784  17.707  139.681 1.00 71.72  ? 48  ALA B CA  1 
ATOM 3953 C C   . ALA B 1 2   ? 12.240  16.517  140.512 1.00 77.21  ? 48  ALA B C   1 
ATOM 3954 O O   . ALA B 1 2   ? 12.595  15.483  139.938 1.00 77.67  ? 48  ALA B O   1 
ATOM 3955 C CB  . ALA B 1 2   ? 12.998  18.548  139.281 1.00 65.65  ? 48  ALA B CB  1 
ATOM 3956 N N   . TRP B 1 3   ? 12.235  16.638  141.840 1.00 63.17  ? 49  TRP B N   1 
ATOM 3957 C CA  . TRP B 1 3   ? 12.603  15.513  142.691 1.00 57.78  ? 49  TRP B CA  1 
ATOM 3958 C C   . TRP B 1 3   ? 11.610  14.365  142.569 1.00 59.12  ? 49  TRP B C   1 
ATOM 3959 O O   . TRP B 1 3   ? 12.015  13.197  142.575 1.00 65.81  ? 49  TRP B O   1 
ATOM 3960 C CB  . TRP B 1 3   ? 12.718  15.978  144.139 1.00 55.25  ? 49  TRP B CB  1 
ATOM 3961 C CG  . TRP B 1 3   ? 13.556  15.090  144.993 1.00 55.25  ? 49  TRP B CG  1 
ATOM 3962 C CD1 . TRP B 1 3   ? 14.903  15.167  145.180 1.00 58.58  ? 49  TRP B CD1 1 
ATOM 3963 C CD2 . TRP B 1 3   ? 13.099  14.002  145.799 1.00 57.48  ? 49  TRP B CD2 1 
ATOM 3964 N NE1 . TRP B 1 3   ? 15.316  14.185  146.046 1.00 57.93  ? 49  TRP B NE1 1 
ATOM 3965 C CE2 . TRP B 1 3   ? 14.225  13.457  146.441 1.00 58.12  ? 49  TRP B CE2 1 
ATOM 3966 C CE3 . TRP B 1 3   ? 11.846  13.433  146.036 1.00 60.74  ? 49  TRP B CE3 1 
ATOM 3967 C CZ2 . TRP B 1 3   ? 14.136  12.371  147.302 1.00 60.12  ? 49  TRP B CZ2 1 
ATOM 3968 C CZ3 . TRP B 1 3   ? 11.761  12.358  146.890 1.00 57.86  ? 49  TRP B CZ3 1 
ATOM 3969 C CH2 . TRP B 1 3   ? 12.897  11.841  147.516 1.00 59.77  ? 49  TRP B CH2 1 
ATOM 3970 N N   . TYR B 1 4   ? 10.314  14.669  142.468 1.00 59.64  ? 50  TYR B N   1 
ATOM 3971 C CA  . TYR B 1 4   ? 9.331   13.616  142.231 1.00 60.19  ? 50  TYR B CA  1 
ATOM 3972 C C   . TYR B 1 4   ? 9.569   12.938  140.890 1.00 64.67  ? 50  TYR B C   1 
ATOM 3973 O O   . TYR B 1 4   ? 9.479   11.709  140.782 1.00 70.07  ? 50  TYR B O   1 
ATOM 3974 C CB  . TYR B 1 4   ? 7.913   14.183  142.298 1.00 61.12  ? 50  TYR B CB  1 
ATOM 3975 C CG  . TYR B 1 4   ? 7.484   14.666  143.665 1.00 62.11  ? 50  TYR B CG  1 
ATOM 3976 C CD1 . TYR B 1 4   ? 8.213   14.345  144.801 1.00 61.13  ? 50  TYR B CD1 1 
ATOM 3977 C CD2 . TYR B 1 4   ? 6.339   15.433  143.819 1.00 64.82  ? 50  TYR B CD2 1 
ATOM 3978 C CE1 . TYR B 1 4   ? 7.817   14.781  146.049 1.00 62.53  ? 50  TYR B CE1 1 
ATOM 3979 C CE2 . TYR B 1 4   ? 5.937   15.874  145.062 1.00 64.60  ? 50  TYR B CE2 1 
ATOM 3980 C CZ  . TYR B 1 4   ? 6.679   15.546  146.173 1.00 63.72  ? 50  TYR B CZ  1 
ATOM 3981 O OH  . TYR B 1 4   ? 6.279   15.986  147.414 1.00 63.15  ? 50  TYR B OH  1 
ATOM 3982 N N   . ALA B 1 5   ? 9.874   13.720  139.856 1.00 63.93  ? 51  ALA B N   1 
ATOM 3983 C CA  . ALA B 1 5   ? 10.194  13.163  138.550 1.00 65.76  ? 51  ALA B CA  1 
ATOM 3984 C C   . ALA B 1 5   ? 11.562  12.501  138.512 1.00 65.67  ? 51  ALA B C   1 
ATOM 3985 O O   . ALA B 1 5   ? 11.884  11.838  137.521 1.00 67.48  ? 51  ALA B O   1 
ATOM 3986 C CB  . ALA B 1 5   ? 10.126  14.254  137.480 1.00 63.80  ? 51  ALA B CB  1 
ATOM 3987 N N   . ARG B 1 6   ? 12.370  12.665  139.558 1.00 60.84  ? 52  ARG B N   1 
ATOM 3988 C CA  . ARG B 1 6   ? 13.702  12.082  139.606 1.00 60.22  ? 52  ARG B CA  1 
ATOM 3989 C C   . ARG B 1 6   ? 13.775  10.826  140.464 1.00 63.74  ? 52  ARG B C   1 
ATOM 3990 O O   . ARG B 1 6   ? 14.653  9.988   140.231 1.00 62.94  ? 52  ARG B O   1 
ATOM 3991 C CB  . ARG B 1 6   ? 14.703  13.125  140.117 1.00 58.57  ? 52  ARG B CB  1 
ATOM 3992 C CG  . ARG B 1 6   ? 16.160  12.728  140.025 1.00 63.82  ? 52  ARG B CG  1 
ATOM 3993 C CD  . ARG B 1 6   ? 17.026  13.969  139.920 1.00 61.98  ? 52  ARG B CD  1 
ATOM 3994 N NE  . ARG B 1 6   ? 17.042  14.723  141.168 1.00 63.29  ? 52  ARG B NE  1 
ATOM 3995 C CZ  . ARG B 1 6   ? 17.751  15.824  141.369 1.00 63.64  ? 52  ARG B CZ  1 
ATOM 3996 N NH1 . ARG B 1 6   ? 18.517  16.336  140.420 1.00 67.43  ? 52  ARG B NH1 1 
ATOM 3997 N NH2 . ARG B 1 6   ? 17.687  16.430  142.551 1.00 61.18  ? 52  ARG B NH2 1 
ATOM 3998 N N   . TYR B 1 7   ? 12.875  10.665  141.433 1.00 58.55  ? 53  TYR B N   1 
ATOM 3999 C CA  . TYR B 1 7   ? 12.767  9.436   142.221 1.00 56.48  ? 53  TYR B CA  1 
ATOM 4000 C C   . TYR B 1 7   ? 11.315  8.963   142.261 1.00 60.13  ? 53  TYR B C   1 
ATOM 4001 O O   . TYR B 1 7   ? 10.726  8.777   143.339 1.00 63.76  ? 53  TYR B O   1 
ATOM 4002 C CB  . TYR B 1 7   ? 13.325  9.636   143.630 1.00 57.06  ? 53  TYR B CB  1 
ATOM 4003 C CG  . TYR B 1 7   ? 14.682  10.307  143.683 1.00 57.50  ? 53  TYR B CG  1 
ATOM 4004 C CD1 . TYR B 1 7   ? 14.807  11.685  143.583 1.00 57.69  ? 53  TYR B CD1 1 
ATOM 4005 C CD2 . TYR B 1 7   ? 15.839  9.556   143.838 1.00 60.66  ? 53  TYR B CD2 1 
ATOM 4006 C CE1 . TYR B 1 7   ? 16.046  12.293  143.632 1.00 60.37  ? 53  TYR B CE1 1 
ATOM 4007 C CE2 . TYR B 1 7   ? 17.080  10.157  143.888 1.00 56.07  ? 53  TYR B CE2 1 
ATOM 4008 C CZ  . TYR B 1 7   ? 17.177  11.525  143.786 1.00 57.16  ? 53  TYR B CZ  1 
ATOM 4009 O OH  . TYR B 1 7   ? 18.412  12.128  143.837 1.00 55.14  ? 53  TYR B OH  1 
ATOM 4010 N N   . PRO B 1 8   ? 10.720  8.700   141.092 1.00 58.32  ? 54  PRO B N   1 
ATOM 4011 C CA  . PRO B 1 8   ? 9.333   8.224   141.080 1.00 57.82  ? 54  PRO B CA  1 
ATOM 4012 C C   . PRO B 1 8   ? 9.185   6.817   141.617 1.00 60.14  ? 54  PRO B C   1 
ATOM 4013 O O   . PRO B 1 8   ? 8.120   6.491   142.152 1.00 63.99  ? 54  PRO B O   1 
ATOM 4014 C CB  . PRO B 1 8   ? 8.949   8.297   139.598 1.00 57.18  ? 54  PRO B CB  1 
ATOM 4015 C CG  . PRO B 1 8   ? 10.231  8.113   138.871 1.00 59.98  ? 54  PRO B CG  1 
ATOM 4016 C CD  . PRO B 1 8   ? 11.352  8.575   139.765 1.00 58.12  ? 54  PRO B CD  1 
ATOM 4017 N N   . HIS B 1 9   ? 10.217  5.981   141.504 1.00 59.85  ? 55  HIS B N   1 
ATOM 4018 C CA  . HIS B 1 9   ? 10.145  4.639   142.068 1.00 60.41  ? 55  HIS B CA  1 
ATOM 4019 C C   . HIS B 1 9   ? 9.991   4.690   143.582 1.00 62.93  ? 55  HIS B C   1 
ATOM 4020 O O   . HIS B 1 9   ? 9.148   3.987   144.154 1.00 69.68  ? 55  HIS B O   1 
ATOM 4021 C CB  . HIS B 1 9   ? 11.386  3.840   141.671 1.00 59.82  ? 55  HIS B CB  1 
ATOM 4022 C CG  . HIS B 1 9   ? 12.633  4.663   141.591 1.00 63.00  ? 55  HIS B CG  1 
ATOM 4023 N ND1 . HIS B 1 9   ? 13.460  4.868   142.674 1.00 64.56  ? 55  HIS B ND1 1 
ATOM 4024 C CD2 . HIS B 1 9   ? 13.193  5.335   140.558 1.00 64.68  ? 55  HIS B CD2 1 
ATOM 4025 C CE1 . HIS B 1 9   ? 14.476  5.630   142.312 1.00 64.86  ? 55  HIS B CE1 1 
ATOM 4026 N NE2 . HIS B 1 9   ? 14.338  5.927   141.032 1.00 66.85  ? 55  HIS B NE2 1 
ATOM 4027 N N   . ILE B 1 10  ? 10.790  5.523   144.254 1.00 54.82  ? 56  ILE B N   1 
ATOM 4028 C CA  . ILE B 1 10  ? 10.639  5.623   145.700 1.00 56.58  ? 56  ILE B CA  1 
ATOM 4029 C C   . ILE B 1 10  ? 9.344   6.341   146.051 1.00 54.65  ? 56  ILE B C   1 
ATOM 4030 O O   . ILE B 1 10  ? 8.731   6.046   147.084 1.00 65.66  ? 56  ILE B O   1 
ATOM 4031 C CB  . ILE B 1 10  ? 11.858  6.297   146.358 1.00 57.22  ? 56  ILE B CB  1 
ATOM 4032 C CG1 . ILE B 1 10  ? 11.821  7.809   146.193 1.00 48.72  ? 56  ILE B CG1 1 
ATOM 4033 C CG2 . ILE B 1 10  ? 13.154  5.744   145.788 1.00 58.90  ? 56  ILE B CG2 1 
ATOM 4034 C CD1 . ILE B 1 10  ? 12.761  8.503   147.126 1.00 53.16  ? 56  ILE B CD1 1 
ATOM 4035 N N   . LEU B 1 11  ? 8.885   7.271   145.204 1.00 47.91  ? 57  LEU B N   1 
ATOM 4036 C CA  . LEU B 1 11  ? 7.578   7.875   145.458 1.00 51.90  ? 57  LEU B CA  1 
ATOM 4037 C C   . LEU B 1 11  ? 6.470   6.824   145.451 1.00 51.76  ? 57  LEU B C   1 
ATOM 4038 O O   . LEU B 1 11  ? 5.623   6.797   146.354 1.00 49.75  ? 57  LEU B O   1 
ATOM 4039 C CB  . LEU B 1 11  ? 7.286   8.965   144.428 1.00 50.60  ? 57  LEU B CB  1 
ATOM 4040 C CG  . LEU B 1 11  ? 6.185   9.950   144.823 1.00 47.32  ? 57  LEU B CG  1 
ATOM 4041 C CD1 . LEU B 1 11  ? 6.573   10.703  146.080 1.00 47.80  ? 57  LEU B CD1 1 
ATOM 4042 C CD2 . LEU B 1 11  ? 5.881   10.916  143.688 1.00 48.66  ? 57  LEU B CD2 1 
ATOM 4043 N N   . GLU B 1 12  ? 6.471   5.941   144.449 1.00 51.74  ? 58  GLU B N   1 
ATOM 4044 C CA  . GLU B 1 12  ? 5.471   4.879   144.397 1.00 47.41  ? 58  GLU B CA  1 
ATOM 4045 C C   . GLU B 1 12  ? 5.617   3.913   145.565 1.00 49.59  ? 58  GLU B C   1 
ATOM 4046 O O   . GLU B 1 12  ? 4.615   3.508   146.164 1.00 58.06  ? 58  GLU B O   1 
ATOM 4047 C CB  . GLU B 1 12  ? 5.558   4.123   143.071 1.00 52.18  ? 58  GLU B CB  1 
ATOM 4048 C CG  . GLU B 1 12  ? 5.476   5.002   141.840 1.00 56.33  ? 58  GLU B CG  1 
ATOM 4049 C CD  . GLU B 1 12  ? 4.137   4.898   141.143 1.00 62.31  ? 58  GLU B CD  1 
ATOM 4050 O OE1 . GLU B 1 12  ? 3.942   5.585   140.119 1.00 61.32  ? 58  GLU B OE1 1 
ATOM 4051 O OE2 . GLU B 1 12  ? 3.279   4.121   141.616 1.00 64.53  ? 58  GLU B OE2 1 
ATOM 4052 N N   . GLU B 1 13  ? 6.849   3.526   145.906 1.00 46.36  ? 59  GLU B N   1 
ATOM 4053 C CA  . GLU B 1 13  ? 7.023   2.603   147.020 1.00 47.42  ? 59  GLU B CA  1 
ATOM 4054 C C   . GLU B 1 13  ? 6.592   3.213   148.345 1.00 48.08  ? 59  GLU B C   1 
ATOM 4055 O O   . GLU B 1 13  ? 6.162   2.477   149.239 1.00 55.16  ? 59  GLU B O   1 
ATOM 4056 C CB  . GLU B 1 13  ? 8.475   2.124   147.118 1.00 51.25  ? 59  GLU B CB  1 
ATOM 4057 C CG  . GLU B 1 13  ? 8.623   0.809   147.890 1.00 61.71  ? 59  GLU B CG  1 
ATOM 4058 C CD  . GLU B 1 13  ? 10.050  0.511   148.323 1.00 60.45  ? 59  GLU B CD  1 
ATOM 4059 O OE1 . GLU B 1 13  ? 10.337  0.580   149.537 1.00 49.08  ? 59  GLU B OE1 1 
ATOM 4060 O OE2 . GLU B 1 13  ? 10.884  0.195   147.449 1.00 60.58  ? 59  GLU B OE2 1 
ATOM 4061 N N   . ALA B 1 14  ? 6.687   4.533   148.491 1.00 45.70  ? 60  ALA B N   1 
ATOM 4062 C CA  . ALA B 1 14  ? 6.222   5.193   149.702 1.00 44.23  ? 60  ALA B CA  1 
ATOM 4063 C C   . ALA B 1 14  ? 4.722   5.439   149.713 1.00 48.09  ? 60  ALA B C   1 
ATOM 4064 O O   . ALA B 1 14  ? 4.132   5.510   150.796 1.00 49.98  ? 60  ALA B O   1 
ATOM 4065 C CB  . ALA B 1 14  ? 6.950   6.528   149.891 1.00 41.77  ? 60  ALA B CB  1 
ATOM 4066 N N   . THR B 1 15  ? 4.088   5.560   148.548 1.00 50.36  ? 61  THR B N   1 
ATOM 4067 C CA  . THR B 1 15  ? 2.673   5.907   148.459 1.00 42.54  ? 61  THR B CA  1 
ATOM 4068 C C   . THR B 1 15  ? 1.809   4.733   148.008 1.00 43.61  ? 61  THR B C   1 
ATOM 4069 O O   . THR B 1 15  ? 0.807   4.914   147.314 1.00 46.69  ? 61  THR B O   1 
ATOM 4070 C CB  . THR B 1 15  ? 2.467   7.088   147.520 1.00 41.46  ? 61  THR B CB  1 
ATOM 4071 O OG1 . THR B 1 15  ? 3.039   6.784   146.244 1.00 46.63  ? 61  THR B OG1 1 
ATOM 4072 C CG2 . THR B 1 15  ? 3.136   8.317   148.079 1.00 44.57  ? 61  THR B CG2 1 
ATOM 4073 N N   . ARG B 1 16  ? 2.180   3.517   148.396 1.00 42.36  ? 62  ARG B N   1 
ATOM 4074 C CA  . ARG B 1 16  ? 1.357   2.337   148.161 1.00 37.90  ? 62  ARG B CA  1 
ATOM 4075 C C   . ARG B 1 16  ? 0.553   2.067   149.430 1.00 43.71  ? 62  ARG B C   1 
ATOM 4076 O O   . ARG B 1 16  ? 1.109   1.668   150.458 1.00 54.04  ? 62  ARG B O   1 
ATOM 4077 C CB  . ARG B 1 16  ? 2.214   1.136   147.761 1.00 38.86  ? 62  ARG B CB  1 
ATOM 4078 C CG  . ARG B 1 16  ? 3.345   0.809   148.726 1.00 53.76  ? 62  ARG B CG  1 
ATOM 4079 C CD  . ARG B 1 16  ? 3.522   -0.695  148.902 1.00 47.89  ? 62  ARG B CD  1 
ATOM 4080 N NE  . ARG B 1 16  ? 4.729   -1.039  149.648 1.00 48.32  ? 62  ARG B NE  1 
ATOM 4081 C CZ  . ARG B 1 16  ? 4.986   -0.667  150.896 1.00 42.20  ? 62  ARG B CZ  1 
ATOM 4082 N NH1 . ARG B 1 16  ? 4.112   0.024   151.610 1.00 29.74  ? 62  ARG B NH1 1 
ATOM 4083 N NH2 . ARG B 1 16  ? 6.145   -1.014  151.448 1.00 37.79  ? 62  ARG B NH2 1 
ATOM 4084 N N   . LEU B 1 17  ? -0.753  2.311   149.369 1.00 34.26  ? 63  LEU B N   1 
ATOM 4085 C CA  . LEU B 1 17  ? -1.591  2.133   150.540 1.00 34.62  ? 63  LEU B CA  1 
ATOM 4086 C C   . LEU B 1 17  ? -2.852  1.364   150.174 1.00 42.47  ? 63  LEU B C   1 
ATOM 4087 O O   . LEU B 1 17  ? -3.356  1.490   149.051 1.00 46.90  ? 63  LEU B O   1 
ATOM 4088 C CB  . LEU B 1 17  ? -1.970  3.487   151.154 1.00 34.60  ? 63  LEU B CB  1 
ATOM 4089 C CG  . LEU B 1 17  ? -0.855  4.250   151.868 1.00 30.01  ? 63  LEU B CG  1 
ATOM 4090 C CD1 . LEU B 1 17  ? -1.292  5.674   152.152 1.00 39.96  ? 63  LEU B CD1 1 
ATOM 4091 C CD2 . LEU B 1 17  ? -0.457  3.545   153.151 1.00 31.51  ? 63  LEU B CD2 1 
ATOM 4092 N N   . PRO B 1 18  ? -3.385  0.564   151.095 1.00 32.76  ? 64  PRO B N   1 
ATOM 4093 C CA  . PRO B 1 18  ? -4.626  -0.172  150.824 1.00 30.38  ? 64  PRO B CA  1 
ATOM 4094 C C   . PRO B 1 18  ? -5.846  0.708   151.069 1.00 28.58  ? 64  PRO B C   1 
ATOM 4095 O O   . PRO B 1 18  ? -6.068  1.195   152.178 1.00 31.66  ? 64  PRO B O   1 
ATOM 4096 C CB  . PRO B 1 18  ? -4.556  -1.344  151.813 1.00 32.42  ? 64  PRO B CB  1 
ATOM 4097 C CG  . PRO B 1 18  ? -3.704  -0.857  152.930 1.00 31.52  ? 64  PRO B CG  1 
ATOM 4098 C CD  . PRO B 1 18  ? -2.824  0.251   152.420 1.00 25.34  ? 64  PRO B CD  1 
ATOM 4099 N N   . PHE B 1 19  ? -6.632  0.914   150.019 1.00 27.39  ? 65  PHE B N   1 
ATOM 4100 C CA  . PHE B 1 19  ? -7.844  1.710   150.091 1.00 29.56  ? 65  PHE B CA  1 
ATOM 4101 C C   . PHE B 1 19  ? -9.066  0.809   149.935 1.00 31.63  ? 65  PHE B C   1 
ATOM 4102 O O   . PHE B 1 19  ? -8.961  -0.416  149.843 1.00 35.22  ? 65  PHE B O   1 
ATOM 4103 C CB  . PHE B 1 19  ? -7.822  2.805   149.025 1.00 34.05  ? 65  PHE B CB  1 
ATOM 4104 C CG  . PHE B 1 19  ? -7.003  4.004   149.404 1.00 33.47  ? 65  PHE B CG  1 
ATOM 4105 C CD1 . PHE B 1 19  ? -7.436  4.869   150.391 1.00 31.70  ? 65  PHE B CD1 1 
ATOM 4106 C CD2 . PHE B 1 19  ? -5.796  4.261   148.779 1.00 33.95  ? 65  PHE B CD2 1 
ATOM 4107 C CE1 . PHE B 1 19  ? -6.687  5.971   150.740 1.00 27.67  ? 65  PHE B CE1 1 
ATOM 4108 C CE2 . PHE B 1 19  ? -5.042  5.361   149.129 1.00 32.37  ? 65  PHE B CE2 1 
ATOM 4109 C CZ  . PHE B 1 19  ? -5.488  6.215   150.111 1.00 28.79  ? 65  PHE B CZ  1 
ATOM 4110 N N   . ALA B 1 20  ? -10.243 1.436   149.907 1.00 30.88  ? 66  ALA B N   1 
ATOM 4111 C CA  . ALA B 1 20  ? -11.518 0.746   149.715 1.00 37.44  ? 66  ALA B CA  1 
ATOM 4112 C C   . ALA B 1 20  ? -11.735 -0.326  150.784 1.00 36.58  ? 66  ALA B C   1 
ATOM 4113 O O   . ALA B 1 20  ? -11.887 -1.514  150.496 1.00 39.56  ? 66  ALA B O   1 
ATOM 4114 C CB  . ALA B 1 20  ? -11.613 0.151   148.306 1.00 43.68  ? 66  ALA B CB  1 
ATOM 4115 N N   . TYR B 1 21  ? -11.746 0.119   152.031 1.00 29.59  ? 67  TYR B N   1 
ATOM 4116 C CA  . TYR B 1 21  ? -12.035 -0.785  153.136 1.00 35.72  ? 67  TYR B CA  1 
ATOM 4117 C C   . TYR B 1 21  ? -13.492 -1.226  153.061 1.00 36.71  ? 67  TYR B C   1 
ATOM 4118 O O   . TYR B 1 21  ? -14.390 -0.376  153.041 1.00 39.96  ? 67  TYR B O   1 
ATOM 4119 C CB  . TYR B 1 21  ? -11.761 -0.098  154.470 1.00 28.94  ? 67  TYR B CB  1 
ATOM 4120 C CG  . TYR B 1 21  ? -10.321 -0.161  154.922 1.00 28.82  ? 67  TYR B CG  1 
ATOM 4121 C CD1 . TYR B 1 21  ? -9.333  0.539   154.250 1.00 30.93  ? 67  TYR B CD1 1 
ATOM 4122 C CD2 . TYR B 1 21  ? -9.953  -0.914  156.026 1.00 37.14  ? 67  TYR B CD2 1 
ATOM 4123 C CE1 . TYR B 1 21  ? -8.018  0.488   154.661 1.00 34.72  ? 67  TYR B CE1 1 
ATOM 4124 C CE2 . TYR B 1 21  ? -8.640  -0.971  156.446 1.00 35.69  ? 67  TYR B CE2 1 
ATOM 4125 C CZ  . TYR B 1 21  ? -7.677  -0.268  155.759 1.00 36.07  ? 67  TYR B CZ  1 
ATOM 4126 O OH  . TYR B 1 21  ? -6.365  -0.320  156.171 1.00 37.39  ? 67  TYR B OH  1 
ATOM 4127 N N   . PRO B 1 22  ? -13.771 -2.528  153.010 1.00 32.79  ? 68  PRO B N   1 
ATOM 4128 C CA  . PRO B 1 22  ? -15.167 -2.981  152.929 1.00 36.79  ? 68  PRO B CA  1 
ATOM 4129 C C   . PRO B 1 22  ? -15.942 -2.594  154.180 1.00 37.46  ? 68  PRO B C   1 
ATOM 4130 O O   . PRO B 1 22  ? -15.522 -2.884  155.301 1.00 41.30  ? 68  PRO B O   1 
ATOM 4131 C CB  . PRO B 1 22  ? -15.043 -4.504  152.794 1.00 35.97  ? 68  PRO B CB  1 
ATOM 4132 C CG  . PRO B 1 22  ? -13.644 -4.740  152.336 1.00 40.25  ? 68  PRO B CG  1 
ATOM 4133 C CD  . PRO B 1 22  ? -12.823 -3.650  152.942 1.00 30.22  ? 68  PRO B CD  1 
ATOM 4134 N N   . ILE B 1 23  ? -17.082 -1.938  153.979 1.00 35.01  ? 69  ILE B N   1 
ATOM 4135 C CA  . ILE B 1 23  ? -17.921 -1.515  155.094 1.00 34.58  ? 69  ILE B CA  1 
ATOM 4136 C C   . ILE B 1 23  ? -18.717 -2.709  155.594 1.00 35.36  ? 69  ILE B C   1 
ATOM 4137 O O   . ILE B 1 23  ? -18.841 -3.722  154.899 1.00 39.74  ? 69  ILE B O   1 
ATOM 4138 C CB  . ILE B 1 23  ? -18.854 -0.359  154.695 1.00 29.30  ? 69  ILE B CB  1 
ATOM 4139 C CG1 . ILE B 1 23  ? -19.389 -0.569  153.280 1.00 30.39  ? 69  ILE B CG1 1 
ATOM 4140 C CG2 . ILE B 1 23  ? -18.123 0.965   154.793 1.00 40.55  ? 69  ILE B CG2 1 
ATOM 4141 C CD1 . ILE B 1 23  ? -20.286 0.546   152.804 1.00 28.66  ? 69  ILE B CD1 1 
ATOM 4142 N N   . GLY B 1 24  ? -19.267 -2.595  156.797 1.00 36.84  ? 70  GLY B N   1 
ATOM 4143 C CA  . GLY B 1 24  ? -20.015 -3.678  157.392 1.00 39.34  ? 70  GLY B CA  1 
ATOM 4144 C C   . GLY B 1 24  ? -19.290 -4.454  158.464 1.00 38.35  ? 70  GLY B C   1 
ATOM 4145 O O   . GLY B 1 24  ? -19.846 -5.433  158.976 1.00 43.05  ? 70  GLY B O   1 
ATOM 4146 N N   . GLN B 1 25  ? -18.070 -4.061  158.816 1.00 33.86  ? 71  GLN B N   1 
ATOM 4147 C CA  . GLN B 1 25  ? -17.324 -4.698  159.890 1.00 39.62  ? 71  GLN B CA  1 
ATOM 4148 C C   . GLN B 1 25  ? -16.638 -3.636  160.732 1.00 38.44  ? 71  GLN B C   1 
ATOM 4149 O O   . GLN B 1 25  ? -16.322 -2.549  160.241 1.00 38.75  ? 71  GLN B O   1 
ATOM 4150 C CB  . GLN B 1 25  ? -16.289 -5.682  159.348 1.00 33.56  ? 71  GLN B CB  1 
ATOM 4151 C CG  . GLN B 1 25  ? -15.512 -5.169  158.158 1.00 35.71  ? 71  GLN B CG  1 
ATOM 4152 C CD  . GLN B 1 25  ? -14.769 -6.272  157.444 1.00 44.68  ? 71  GLN B CD  1 
ATOM 4153 O OE1 . GLN B 1 25  ? -15.298 -6.893  156.528 1.00 45.66  ? 71  GLN B OE1 1 
ATOM 4154 N NE2 . GLN B 1 25  ? -13.538 -6.529  157.865 1.00 45.61  ? 71  GLN B NE2 1 
ATOM 4155 N N   . TYR B 1 26  ? -16.418 -3.956  162.002 1.00 38.47  ? 72  TYR B N   1 
ATOM 4156 C CA  . TYR B 1 26  ? -15.755 -3.031  162.909 1.00 34.20  ? 72  TYR B CA  1 
ATOM 4157 C C   . TYR B 1 26  ? -14.263 -2.981  162.606 1.00 36.31  ? 72  TYR B C   1 
ATOM 4158 O O   . TYR B 1 26  ? -13.604 -4.020  162.513 1.00 41.32  ? 72  TYR B O   1 
ATOM 4159 C CB  . TYR B 1 26  ? -15.997 -3.462  164.353 1.00 34.52  ? 72  TYR B CB  1 
ATOM 4160 C CG  . TYR B 1 26  ? -15.007 -2.912  165.347 1.00 37.86  ? 72  TYR B CG  1 
ATOM 4161 C CD1 . TYR B 1 26  ? -15.073 -1.593  165.764 1.00 38.01  ? 72  TYR B CD1 1 
ATOM 4162 C CD2 . TYR B 1 26  ? -14.007 -3.715  165.874 1.00 41.91  ? 72  TYR B CD2 1 
ATOM 4163 C CE1 . TYR B 1 26  ? -14.173 -1.090  166.676 1.00 43.22  ? 72  TYR B CE1 1 
ATOM 4164 C CE2 . TYR B 1 26  ? -13.101 -3.220  166.787 1.00 40.41  ? 72  TYR B CE2 1 
ATOM 4165 C CZ  . TYR B 1 26  ? -13.189 -1.906  167.184 1.00 43.68  ? 72  TYR B CZ  1 
ATOM 4166 O OH  . TYR B 1 26  ? -12.287 -1.405  168.094 1.00 43.61  ? 72  TYR B OH  1 
ATOM 4167 N N   . TYR B 1 27  ? -13.731 -1.772  162.452 1.00 33.80  ? 73  TYR B N   1 
ATOM 4168 C CA  . TYR B 1 27  ? -12.320 -1.560  162.156 1.00 30.17  ? 73  TYR B CA  1 
ATOM 4169 C C   . TYR B 1 27  ? -11.646 -0.906  163.351 1.00 34.67  ? 73  TYR B C   1 
ATOM 4170 O O   . TYR B 1 27  ? -12.142 0.096   163.877 1.00 44.23  ? 73  TYR B O   1 
ATOM 4171 C CB  . TYR B 1 27  ? -12.138 -0.693  160.911 1.00 29.99  ? 73  TYR B CB  1 
ATOM 4172 C CG  . TYR B 1 27  ? -12.492 -1.392  159.623 1.00 31.99  ? 73  TYR B CG  1 
ATOM 4173 C CD1 . TYR B 1 27  ? -11.720 -2.439  159.146 1.00 32.08  ? 73  TYR B CD1 1 
ATOM 4174 C CD2 . TYR B 1 27  ? -13.600 -1.008  158.885 1.00 38.64  ? 73  TYR B CD2 1 
ATOM 4175 C CE1 . TYR B 1 27  ? -12.040 -3.083  157.971 1.00 33.29  ? 73  TYR B CE1 1 
ATOM 4176 C CE2 . TYR B 1 27  ? -13.927 -1.646  157.708 1.00 36.73  ? 73  TYR B CE2 1 
ATOM 4177 C CZ  . TYR B 1 27  ? -13.144 -2.683  157.257 1.00 35.05  ? 73  TYR B CZ  1 
ATOM 4178 O OH  . TYR B 1 27  ? -13.468 -3.320  156.084 1.00 36.03  ? 73  TYR B OH  1 
ATOM 4179 N N   . ASP B 1 28  ? -10.518 -1.468  163.772 1.00 34.58  ? 74  ASP B N   1 
ATOM 4180 C CA  . ASP B 1 28  ? -9.742  -0.940  164.886 1.00 38.54  ? 74  ASP B CA  1 
ATOM 4181 C C   . ASP B 1 28  ? -8.513  -0.233  164.333 1.00 46.55  ? 74  ASP B C   1 
ATOM 4182 O O   . ASP B 1 28  ? -7.704  -0.846  163.628 1.00 53.62  ? 74  ASP B O   1 
ATOM 4183 C CB  . ASP B 1 28  ? -9.337  -2.057  165.845 1.00 45.32  ? 74  ASP B CB  1 
ATOM 4184 C CG  . ASP B 1 28  ? -8.851  -1.531  167.178 1.00 51.54  ? 74  ASP B CG  1 
ATOM 4185 O OD1 . ASP B 1 28  ? -9.700  -1.192  168.029 1.00 53.86  ? 74  ASP B OD1 1 
ATOM 4186 O OD2 . ASP B 1 28  ? -7.621  -1.458  167.377 1.00 49.10  ? 74  ASP B OD2 1 
ATOM 4187 N N   . THR B 1 29  ? -8.373  1.053   164.655 1.00 41.74  ? 75  THR B N   1 
ATOM 4188 C CA  . THR B 1 29  ? -7.281  1.848   164.113 1.00 36.45  ? 75  THR B CA  1 
ATOM 4189 C C   . THR B 1 29  ? -5.973  1.657   164.866 1.00 40.41  ? 75  THR B C   1 
ATOM 4190 O O   . THR B 1 29  ? -4.931  2.122   164.394 1.00 44.14  ? 75  THR B O   1 
ATOM 4191 C CB  . THR B 1 29  ? -7.656  3.330   164.115 1.00 41.66  ? 75  THR B CB  1 
ATOM 4192 O OG1 . THR B 1 29  ? -8.071  3.716   165.430 1.00 43.20  ? 75  THR B OG1 1 
ATOM 4193 C CG2 . THR B 1 29  ? -8.784  3.593   163.135 1.00 44.21  ? 75  THR B CG2 1 
ATOM 4194 N N   . GLY B 1 30  ? -5.997  0.991   166.014 1.00 44.96  ? 76  GLY B N   1 
ATOM 4195 C CA  . GLY B 1 30  ? -4.788  0.790   166.783 1.00 48.74  ? 76  GLY B CA  1 
ATOM 4196 C C   . GLY B 1 30  ? -4.380  2.037   167.541 1.00 50.57  ? 76  GLY B C   1 
ATOM 4197 O O   . GLY B 1 30  ? -5.080  3.049   167.579 1.00 52.86  ? 76  GLY B O   1 
ATOM 4198 N N   . TYR B 1 31  ? -3.208  1.953   168.160 1.00 44.65  ? 77  TYR B N   1 
ATOM 4199 C CA  . TYR B 1 31  ? -2.672  3.026   168.984 1.00 41.35  ? 77  TYR B CA  1 
ATOM 4200 C C   . TYR B 1 31  ? -1.404  3.568   168.341 1.00 46.27  ? 77  TYR B C   1 
ATOM 4201 O O   . TYR B 1 31  ? -0.471  2.807   168.066 1.00 52.10  ? 77  TYR B O   1 
ATOM 4202 C CB  . TYR B 1 31  ? -2.365  2.525   170.396 1.00 43.55  ? 77  TYR B CB  1 
ATOM 4203 C CG  . TYR B 1 31  ? -3.552  2.524   171.326 1.00 41.84  ? 77  TYR B CG  1 
ATOM 4204 C CD1 . TYR B 1 31  ? -4.111  3.709   171.770 1.00 44.20  ? 77  TYR B CD1 1 
ATOM 4205 C CD2 . TYR B 1 31  ? -4.110  1.332   171.764 1.00 48.00  ? 77  TYR B CD2 1 
ATOM 4206 C CE1 . TYR B 1 31  ? -5.195  3.708   172.622 1.00 53.41  ? 77  TYR B CE1 1 
ATOM 4207 C CE2 . TYR B 1 31  ? -5.193  1.322   172.615 1.00 47.43  ? 77  TYR B CE2 1 
ATOM 4208 C CZ  . TYR B 1 31  ? -5.732  2.512   173.041 1.00 50.43  ? 77  TYR B CZ  1 
ATOM 4209 O OH  . TYR B 1 31  ? -6.814  2.504   173.891 1.00 51.34  ? 77  TYR B OH  1 
ATOM 4210 N N   . SER B 1 32  ? -1.373  4.880   168.099 1.00 43.35  ? 78  SER B N   1 
ATOM 4211 C CA  . SER B 1 32  ? -0.143  5.500   167.616 1.00 42.65  ? 78  SER B CA  1 
ATOM 4212 C C   . SER B 1 32  ? 0.869   5.665   168.739 1.00 43.19  ? 78  SER B C   1 
ATOM 4213 O O   . SER B 1 32  ? 2.074   5.507   168.516 1.00 45.58  ? 78  SER B O   1 
ATOM 4214 C CB  . SER B 1 32  ? -0.445  6.850   166.970 1.00 44.10  ? 78  SER B CB  1 
ATOM 4215 O OG  . SER B 1 32  ? -0.563  7.864   167.950 1.00 50.02  ? 78  SER B OG  1 
ATOM 4216 N N   . VAL B 1 33  ? 0.403   5.980   169.943 1.00 43.87  ? 79  VAL B N   1 
ATOM 4217 C CA  . VAL B 1 33  ? 1.241   6.047   171.134 1.00 43.60  ? 79  VAL B CA  1 
ATOM 4218 C C   . VAL B 1 33  ? 0.985   4.782   171.939 1.00 51.87  ? 79  VAL B C   1 
ATOM 4219 O O   . VAL B 1 33  ? -0.136  4.556   172.411 1.00 54.43  ? 79  VAL B O   1 
ATOM 4220 C CB  . VAL B 1 33  ? 0.945   7.301   171.967 1.00 39.72  ? 79  VAL B CB  1 
ATOM 4221 C CG1 . VAL B 1 33  ? 1.735   7.274   173.262 1.00 46.09  ? 79  VAL B CG1 1 
ATOM 4222 C CG2 . VAL B 1 33  ? 1.259   8.554   171.170 1.00 41.22  ? 79  VAL B CG2 1 
ATOM 4223 N N   . ALA B 1 34  ? 2.021   3.958   172.096 1.00 54.25  ? 80  ALA B N   1 
ATOM 4224 C CA  . ALA B 1 34  ? 1.856   2.678   172.772 1.00 50.79  ? 80  ALA B CA  1 
ATOM 4225 C C   . ALA B 1 34  ? 1.510   2.837   174.245 1.00 56.40  ? 80  ALA B C   1 
ATOM 4226 O O   . ALA B 1 34  ? 0.992   1.894   174.852 1.00 56.92  ? 80  ALA B O   1 
ATOM 4227 C CB  . ALA B 1 34  ? 3.124   1.839   172.625 1.00 53.46  ? 80  ALA B CB  1 
ATOM 4228 N N   . SER B 1 35  ? 1.773   4.002   174.828 1.00 55.12  ? 81  SER B N   1 
ATOM 4229 C CA  . SER B 1 35  ? 1.500   4.252   176.235 1.00 51.19  ? 81  SER B CA  1 
ATOM 4230 C C   . SER B 1 35  ? 0.100   4.796   176.476 1.00 50.64  ? 81  SER B C   1 
ATOM 4231 O O   . SER B 1 35  ? -0.214  5.180   177.606 1.00 55.38  ? 81  SER B O   1 
ATOM 4232 C CB  . SER B 1 35  ? 2.535   5.223   176.806 1.00 50.85  ? 81  SER B CB  1 
ATOM 4233 O OG  . SER B 1 35  ? 2.180   5.632   178.114 1.00 56.98  ? 81  SER B OG  1 
ATOM 4234 N N   . ALA B 1 36  ? -0.743  4.839   175.449 1.00 50.02  ? 82  ALA B N   1 
ATOM 4235 C CA  . ALA B 1 36  ? -2.090  5.379   175.567 1.00 54.18  ? 82  ALA B CA  1 
ATOM 4236 C C   . ALA B 1 36  ? -3.081  4.373   176.135 1.00 54.95  ? 82  ALA B C   1 
ATOM 4237 O O   . ALA B 1 36  ? -4.242  4.726   176.363 1.00 56.45  ? 82  ALA B O   1 
ATOM 4238 C CB  . ALA B 1 36  ? -2.579  5.878   174.207 1.00 54.80  ? 82  ALA B CB  1 
ATOM 4239 N N   . THR B 1 37  ? -2.655  3.131   176.364 1.00 59.12  ? 83  THR B N   1 
ATOM 4240 C CA  . THR B 1 37  ? -3.551  2.125   176.918 1.00 59.83  ? 83  THR B CA  1 
ATOM 4241 C C   . THR B 1 37  ? -3.960  2.423   178.354 1.00 59.42  ? 83  THR B C   1 
ATOM 4242 O O   . THR B 1 37  ? -4.970  1.879   178.813 1.00 59.86  ? 83  THR B O   1 
ATOM 4243 C CB  . THR B 1 37  ? -2.901  0.741   176.845 1.00 59.03  ? 83  THR B CB  1 
ATOM 4244 O OG1 . THR B 1 37  ? -1.711  0.725   177.642 1.00 59.85  ? 83  THR B OG1 1 
ATOM 4245 C CG2 . THR B 1 37  ? -2.548  0.397   175.408 1.00 53.81  ? 83  THR B CG2 1 
ATOM 4246 N N   . GLU B 1 38  ? -3.205  3.258   179.075 1.00 56.30  ? 84  GLU B N   1 
ATOM 4247 C CA  . GLU B 1 38  ? -3.609  3.626   180.428 1.00 57.39  ? 84  GLU B CA  1 
ATOM 4248 C C   . GLU B 1 38  ? -4.912  4.411   180.415 1.00 59.29  ? 84  GLU B C   1 
ATOM 4249 O O   . GLU B 1 38  ? -5.801  4.167   181.239 1.00 63.59  ? 84  GLU B O   1 
ATOM 4250 C CB  . GLU B 1 38  ? -2.506  4.434   181.109 1.00 57.92  ? 84  GLU B CB  1 
ATOM 4251 C CG  . GLU B 1 38  ? -1.894  5.508   180.232 1.00 58.50  ? 84  GLU B CG  1 
ATOM 4252 C CD  . GLU B 1 38  ? -0.701  6.181   180.875 1.00 62.81  ? 84  GLU B CD  1 
ATOM 4253 O OE1 . GLU B 1 38  ? -0.637  6.216   182.121 1.00 65.43  ? 84  GLU B OE1 1 
ATOM 4254 O OE2 . GLU B 1 38  ? 0.172   6.678   180.134 1.00 63.97  ? 84  GLU B OE2 1 
ATOM 4255 N N   . TRP B 1 39  ? -5.044  5.354   179.487 1.00 55.04  ? 85  TRP B N   1 
ATOM 4256 C CA  . TRP B 1 39  ? -6.282  6.105   179.300 1.00 54.23  ? 85  TRP B CA  1 
ATOM 4257 C C   . TRP B 1 39  ? -7.229  5.210   178.515 1.00 56.09  ? 85  TRP B C   1 
ATOM 4258 O O   . TRP B 1 39  ? -7.217  5.201   177.282 1.00 56.70  ? 85  TRP B O   1 
ATOM 4259 C CB  . TRP B 1 39  ? -6.007  7.419   178.580 1.00 52.76  ? 85  TRP B CB  1 
ATOM 4260 C CG  . TRP B 1 39  ? -4.739  8.080   179.023 1.00 55.86  ? 85  TRP B CG  1 
ATOM 4261 C CD1 . TRP B 1 39  ? -4.300  8.230   180.306 1.00 57.51  ? 85  TRP B CD1 1 
ATOM 4262 C CD2 . TRP B 1 39  ? -3.736  8.667   178.186 1.00 56.62  ? 85  TRP B CD2 1 
ATOM 4263 N NE1 . TRP B 1 39  ? -3.093  8.883   180.320 1.00 55.90  ? 85  TRP B NE1 1 
ATOM 4264 C CE2 . TRP B 1 39  ? -2.725  9.162   179.031 1.00 55.60  ? 85  TRP B CE2 1 
ATOM 4265 C CE3 . TRP B 1 39  ? -3.599  8.826   176.805 1.00 55.30  ? 85  TRP B CE3 1 
ATOM 4266 C CZ2 . TRP B 1 39  ? -1.591  9.802   178.540 1.00 54.08  ? 85  TRP B CZ2 1 
ATOM 4267 C CZ3 . TRP B 1 39  ? -2.472  9.463   176.321 1.00 55.85  ? 85  TRP B CZ3 1 
ATOM 4268 C CH2 . TRP B 1 39  ? -1.484  9.942   177.185 1.00 55.30  ? 85  TRP B CH2 1 
ATOM 4269 N N   . SER B 1 40  ? -8.053  4.449   179.236 1.00 57.15  ? 86  SER B N   1 
ATOM 4270 C CA  . SER B 1 40  ? -8.840  3.391   178.613 1.00 60.37  ? 86  SER B CA  1 
ATOM 4271 C C   . SER B 1 40  ? -9.833  3.951   177.603 1.00 59.39  ? 86  SER B C   1 
ATOM 4272 O O   . SER B 1 40  ? -9.787  3.610   176.416 1.00 60.85  ? 86  SER B O   1 
ATOM 4273 C CB  . SER B 1 40  ? -9.568  2.582   179.689 1.00 62.89  ? 86  SER B CB  1 
ATOM 4274 O OG  . SER B 1 40  ? -10.250 3.435   180.591 1.00 64.42  ? 86  SER B OG  1 
ATOM 4275 N N   . LYS B 1 41  ? -10.733 4.820   178.055 1.00 52.66  ? 87  LYS B N   1 
ATOM 4276 C CA  . LYS B 1 41  ? -11.797 5.312   177.192 1.00 50.69  ? 87  LYS B CA  1 
ATOM 4277 C C   . LYS B 1 41  ? -11.491 6.671   176.581 1.00 52.81  ? 87  LYS B C   1 
ATOM 4278 O O   . LYS B 1 41  ? -12.312 7.182   175.813 1.00 50.50  ? 87  LYS B O   1 
ATOM 4279 C CB  . LYS B 1 41  ? -13.107 5.381   177.979 1.00 49.09  ? 87  LYS B CB  1 
ATOM 4280 C CG  . LYS B 1 41  ? -13.869 4.066   178.012 1.00 48.99  ? 87  LYS B CG  1 
ATOM 4281 C CD  . LYS B 1 41  ? -15.346 4.279   178.296 1.00 56.05  ? 87  LYS B CD  1 
ATOM 4282 C CE  . LYS B 1 41  ? -15.556 5.187   179.497 1.00 56.16  ? 87  LYS B CE  1 
ATOM 4283 N NZ  . LYS B 1 41  ? -16.941 5.730   179.547 1.00 52.69  ? 87  LYS B NZ  1 
ATOM 4284 N N   . TYR B 1 42  ? -10.332 7.256   176.880 1.00 50.38  ? 88  TYR B N   1 
ATOM 4285 C CA  . TYR B 1 42  ? -9.993  8.574   176.365 1.00 39.88  ? 88  TYR B CA  1 
ATOM 4286 C C   . TYR B 1 42  ? -9.450  8.537   174.944 1.00 42.85  ? 88  TYR B C   1 
ATOM 4287 O O   . TYR B 1 42  ? -9.222  9.601   174.360 1.00 46.44  ? 88  TYR B O   1 
ATOM 4288 C CB  . TYR B 1 42  ? -8.980  9.251   177.290 1.00 43.54  ? 88  TYR B CB  1 
ATOM 4289 C CG  . TYR B 1 42  ? -9.622  10.017  178.422 1.00 43.69  ? 88  TYR B CG  1 
ATOM 4290 C CD1 . TYR B 1 42  ? -10.418 11.123  178.170 1.00 43.22  ? 88  TYR B CD1 1 
ATOM 4291 C CD2 . TYR B 1 42  ? -9.450  9.622   179.740 1.00 48.74  ? 88  TYR B CD2 1 
ATOM 4292 C CE1 . TYR B 1 42  ? -11.012 11.824  179.198 1.00 44.82  ? 88  TYR B CE1 1 
ATOM 4293 C CE2 . TYR B 1 42  ? -10.041 10.316  180.776 1.00 51.92  ? 88  TYR B CE2 1 
ATOM 4294 C CZ  . TYR B 1 42  ? -10.822 11.416  180.498 1.00 49.82  ? 88  TYR B CZ  1 
ATOM 4295 O OH  . TYR B 1 42  ? -11.414 12.114  181.524 1.00 46.71  ? 88  TYR B OH  1 
ATOM 4296 N N   . VAL B 1 43  ? -9.234  7.353   174.379 1.00 47.09  ? 89  VAL B N   1 
ATOM 4297 C CA  . VAL B 1 43  ? -8.774  7.199   173.004 1.00 43.86  ? 89  VAL B CA  1 
ATOM 4298 C C   . VAL B 1 43  ? -9.805  6.361   172.263 1.00 47.20  ? 89  VAL B C   1 
ATOM 4299 O O   . VAL B 1 43  ? -10.114 5.237   172.676 1.00 52.73  ? 89  VAL B O   1 
ATOM 4300 C CB  . VAL B 1 43  ? -7.385  6.548   172.936 1.00 39.79  ? 89  VAL B CB  1 
ATOM 4301 C CG1 . VAL B 1 43  ? -6.793  6.714   171.549 1.00 40.32  ? 89  VAL B CG1 1 
ATOM 4302 C CG2 . VAL B 1 43  ? -6.466  7.136   173.990 1.00 35.49  ? 89  VAL B CG2 1 
ATOM 4303 N N   . ASP B 1 44  ? -10.343 6.905   171.175 1.00 44.35  ? 90  ASP B N   1 
ATOM 4304 C CA  . ASP B 1 44  ? -11.356 6.222   170.375 1.00 49.88  ? 90  ASP B CA  1 
ATOM 4305 C C   . ASP B 1 44  ? -10.671 5.570   169.181 1.00 49.46  ? 90  ASP B C   1 
ATOM 4306 O O   . ASP B 1 44  ? -10.487 6.198   168.136 1.00 51.74  ? 90  ASP B O   1 
ATOM 4307 C CB  . ASP B 1 44  ? -12.444 7.193   169.932 1.00 51.27  ? 90  ASP B CB  1 
ATOM 4308 C CG  . ASP B 1 44  ? -13.640 6.489   169.327 1.00 54.42  ? 90  ASP B CG  1 
ATOM 4309 O OD1 . ASP B 1 44  ? -14.560 6.122   170.088 1.00 58.63  ? 90  ASP B OD1 1 
ATOM 4310 O OD2 . ASP B 1 44  ? -13.660 6.298   168.094 1.00 50.91  ? 90  ASP B OD2 1 
ATOM 4311 N N   . THR B 1 45  ? -10.295 4.304   169.338 1.00 43.73  ? 91  THR B N   1 
ATOM 4312 C CA  . THR B 1 45  ? -9.705  3.528   168.258 1.00 46.50  ? 91  THR B CA  1 
ATOM 4313 C C   . THR B 1 45  ? -10.749 2.829   167.399 1.00 47.70  ? 91  THR B C   1 
ATOM 4314 O O   . THR B 1 45  ? -10.392 2.218   166.388 1.00 50.87  ? 91  THR B O   1 
ATOM 4315 C CB  . THR B 1 45  ? -8.730  2.492   168.822 1.00 50.52  ? 91  THR B CB  1 
ATOM 4316 O OG1 . THR B 1 45  ? -9.452  1.531   169.602 1.00 54.49  ? 91  THR B OG1 1 
ATOM 4317 C CG2 . THR B 1 45  ? -7.689  3.166   169.699 1.00 42.37  ? 91  THR B CG2 1 
ATOM 4318 N N   . SER B 1 46  ? -12.021 2.903   167.777 1.00 47.31  ? 92  SER B N   1 
ATOM 4319 C CA  . SER B 1 46  ? -13.086 2.265   167.022 1.00 43.58  ? 92  SER B CA  1 
ATOM 4320 C C   . SER B 1 46  ? -13.406 3.055   165.761 1.00 39.26  ? 92  SER B C   1 
ATOM 4321 O O   . SER B 1 46  ? -13.197 4.269   165.690 1.00 40.17  ? 92  SER B O   1 
ATOM 4322 C CB  . SER B 1 46  ? -14.344 2.136   167.881 1.00 46.17  ? 92  SER B CB  1 
ATOM 4323 O OG  . SER B 1 46  ? -14.038 1.596   169.154 1.00 52.14  ? 92  SER B OG  1 
ATOM 4324 N N   . LEU B 1 47  ? -13.922 2.349   164.755 1.00 31.88  ? 93  LEU B N   1 
ATOM 4325 C CA  . LEU B 1 47  ? -14.351 2.992   163.514 1.00 36.21  ? 93  LEU B CA  1 
ATOM 4326 C C   . LEU B 1 47  ? -15.435 2.119   162.887 1.00 34.46  ? 93  LEU B C   1 
ATOM 4327 O O   . LEU B 1 47  ? -15.130 1.094   162.271 1.00 33.96  ? 93  LEU B O   1 
ATOM 4328 C CB  . LEU B 1 47  ? -13.181 3.198   162.565 1.00 27.43  ? 93  LEU B CB  1 
ATOM 4329 C CG  . LEU B 1 47  ? -13.531 3.927   161.270 1.00 25.94  ? 93  LEU B CG  1 
ATOM 4330 C CD1 . LEU B 1 47  ? -13.810 5.388   161.549 1.00 26.74  ? 93  LEU B CD1 1 
ATOM 4331 C CD2 . LEU B 1 47  ? -12.403 3.789   160.278 1.00 28.82  ? 93  LEU B CD2 1 
ATOM 4332 N N   . THR B 1 48  ? -16.688 2.537   163.041 1.00 37.36  ? 94  THR B N   1 
ATOM 4333 C CA  . THR B 1 48  ? -17.839 1.822   162.507 1.00 41.92  ? 94  THR B CA  1 
ATOM 4334 C C   . THR B 1 48  ? -18.557 2.717   161.510 1.00 41.47  ? 94  THR B C   1 
ATOM 4335 O O   . THR B 1 48  ? -18.752 3.909   161.770 1.00 42.26  ? 94  THR B O   1 
ATOM 4336 C CB  . THR B 1 48  ? -18.796 1.401   163.625 1.00 45.90  ? 94  THR B CB  1 
ATOM 4337 O OG1 . THR B 1 48  ? -19.430 2.562   164.173 1.00 48.68  ? 94  THR B OG1 1 
ATOM 4338 C CG2 . THR B 1 48  ? -18.040 0.679   164.728 1.00 41.82  ? 94  THR B CG2 1 
ATOM 4339 N N   . ILE B 1 49  ? -18.946 2.148   160.377 1.00 36.15  ? 95  ILE B N   1 
ATOM 4340 C CA  . ILE B 1 49  ? -19.583 2.884   159.290 1.00 37.12  ? 95  ILE B CA  1 
ATOM 4341 C C   . ILE B 1 49  ? -20.996 2.341   159.110 1.00 37.98  ? 95  ILE B C   1 
ATOM 4342 O O   . ILE B 1 49  ? -21.163 1.136   158.882 1.00 42.67  ? 95  ILE B O   1 
ATOM 4343 C CB  . ILE B 1 49  ? -18.784 2.772   157.983 1.00 34.12  ? 95  ILE B CB  1 
ATOM 4344 C CG1 . ILE B 1 49  ? -17.323 3.146   158.221 1.00 32.05  ? 95  ILE B CG1 1 
ATOM 4345 C CG2 . ILE B 1 49  ? -19.387 3.669   156.918 1.00 31.84  ? 95  ILE B CG2 1 
ATOM 4346 C CD1 . ILE B 1 49  ? -17.148 4.507   158.834 1.00 36.16  ? 95  ILE B CD1 1 
ATOM 4347 N N   . PRO B 1 50  ? -22.028 3.174   159.204 1.00 29.26  ? 96  PRO B N   1 
ATOM 4348 C CA  . PRO B 1 50  ? -23.385 2.703   158.916 1.00 29.26  ? 96  PRO B CA  1 
ATOM 4349 C C   . PRO B 1 50  ? -23.552 2.414   157.434 1.00 39.17  ? 96  PRO B C   1 
ATOM 4350 O O   . PRO B 1 50  ? -22.841 2.953   156.584 1.00 41.34  ? 96  PRO B O   1 
ATOM 4351 C CB  . PRO B 1 50  ? -24.265 3.874   159.358 1.00 39.52  ? 96  PRO B CB  1 
ATOM 4352 C CG  . PRO B 1 50  ? -23.393 5.065   159.167 1.00 33.86  ? 96  PRO B CG  1 
ATOM 4353 C CD  . PRO B 1 50  ? -21.995 4.617   159.496 1.00 33.05  ? 96  PRO B CD  1 
ATOM 4354 N N   . GLY B 1 51  ? -24.510 1.545   157.127 1.00 35.52  ? 97  GLY B N   1 
ATOM 4355 C CA  . GLY B 1 51  ? -24.663 1.107   155.755 1.00 34.89  ? 97  GLY B CA  1 
ATOM 4356 C C   . GLY B 1 51  ? -26.046 1.231   155.152 1.00 31.17  ? 97  GLY B C   1 
ATOM 4357 O O   . GLY B 1 51  ? -26.190 1.152   153.929 1.00 35.52  ? 97  GLY B O   1 
ATOM 4358 N N   . VAL B 1 52  ? -27.072 1.423   155.978 1.00 28.73  ? 98  VAL B N   1 
ATOM 4359 C CA  . VAL B 1 52  ? -28.435 1.538   155.474 1.00 37.90  ? 98  VAL B CA  1 
ATOM 4360 C C   . VAL B 1 52  ? -29.238 2.434   156.407 1.00 41.76  ? 98  VAL B C   1 
ATOM 4361 O O   . VAL B 1 52  ? -28.996 2.484   157.616 1.00 44.77  ? 98  VAL B O   1 
ATOM 4362 C CB  . VAL B 1 52  ? -29.100 0.150   155.304 1.00 28.77  ? 98  VAL B CB  1 
ATOM 4363 C CG1 . VAL B 1 52  ? -29.619 -0.363  156.619 1.00 34.62  ? 98  VAL B CG1 1 
ATOM 4364 C CG2 . VAL B 1 52  ? -30.230 0.219   154.295 1.00 34.52  ? 98  VAL B CG2 1 
ATOM 4365 N N   . MET B 1 53  ? -30.184 3.167   155.823 1.00 36.03  ? 99  MET B N   1 
ATOM 4366 C CA  . MET B 1 53  ? -31.128 3.983   156.574 1.00 31.32  ? 99  MET B CA  1 
ATOM 4367 C C   . MET B 1 53  ? -32.514 3.774   155.990 1.00 40.91  ? 99  MET B C   1 
ATOM 4368 O O   . MET B 1 53  ? -32.710 3.932   154.782 1.00 45.38  ? 99  MET B O   1 
ATOM 4369 C CB  . MET B 1 53  ? -30.755 5.467   156.529 1.00 33.19  ? 99  MET B CB  1 
ATOM 4370 C CG  . MET B 1 53  ? -31.493 6.310   157.550 1.00 35.24  ? 99  MET B CG  1 
ATOM 4371 S SD  . MET B 1 53  ? -31.502 8.060   157.135 1.00 54.35  ? 99  MET B SD  1 
ATOM 4372 C CE  . MET B 1 53  ? -31.517 8.781   158.771 1.00 43.34  ? 99  MET B CE  1 
ATOM 4373 N N   . CYS B 1 54  ? -33.468 3.426   156.846 1.00 38.63  ? 100 CYS B N   1 
ATOM 4374 C CA  . CYS B 1 54  ? -34.822 3.101   156.425 1.00 27.99  ? 100 CYS B CA  1 
ATOM 4375 C C   . CYS B 1 54  ? -35.752 4.251   156.777 1.00 40.32  ? 100 CYS B C   1 
ATOM 4376 O O   . CYS B 1 54  ? -35.677 4.801   157.881 1.00 50.83  ? 100 CYS B O   1 
ATOM 4377 C CB  . CYS B 1 54  ? -35.303 1.808   157.084 1.00 33.09  ? 100 CYS B CB  1 
ATOM 4378 S SG  . CYS B 1 54  ? -36.628 0.983   156.189 1.00 51.69  ? 100 CYS B SG  1 
ATOM 4379 N N   . VAL B 1 55  ? -36.618 4.611   155.838 1.00 37.00  ? 101 VAL B N   1 
ATOM 4380 C CA  . VAL B 1 55  ? -37.582 5.690   156.013 1.00 25.74  ? 101 VAL B CA  1 
ATOM 4381 C C   . VAL B 1 55  ? -38.950 5.058   156.231 1.00 29.44  ? 101 VAL B C   1 
ATOM 4382 O O   . VAL B 1 55  ? -39.562 4.538   155.292 1.00 39.03  ? 101 VAL B O   1 
ATOM 4383 C CB  . VAL B 1 55  ? -37.588 6.637   154.807 1.00 23.72  ? 101 VAL B CB  1 
ATOM 4384 C CG1 . VAL B 1 55  ? -38.536 7.790   155.045 1.00 30.74  ? 101 VAL B CG1 1 
ATOM 4385 C CG2 . VAL B 1 55  ? -36.184 7.148   154.535 1.00 26.51  ? 101 VAL B CG2 1 
ATOM 4386 N N   . ASN B 1 56  ? -39.434 5.100   157.469 1.00 21.15  ? 102 ASN B N   1 
ATOM 4387 C CA  . ASN B 1 56  ? -40.717 4.497   157.822 1.00 23.45  ? 102 ASN B CA  1 
ATOM 4388 C C   . ASN B 1 56  ? -41.827 5.486   157.494 1.00 26.66  ? 102 ASN B C   1 
ATOM 4389 O O   . ASN B 1 56  ? -42.151 6.363   158.296 1.00 39.03  ? 102 ASN B O   1 
ATOM 4390 C CB  . ASN B 1 56  ? -40.738 4.112   159.296 1.00 28.57  ? 102 ASN B CB  1 
ATOM 4391 C CG  . ASN B 1 56  ? -39.699 3.068   159.639 1.00 33.85  ? 102 ASN B CG  1 
ATOM 4392 O OD1 . ASN B 1 56  ? -38.887 2.685   158.799 1.00 34.15  ? 102 ASN B OD1 1 
ATOM 4393 N ND2 . ASN B 1 56  ? -39.719 2.602   160.881 1.00 32.56  ? 102 ASN B ND2 1 
ATOM 4394 N N   . PHE B 1 57  ? -42.420 5.344   156.313 1.00 25.82  ? 103 PHE B N   1 
ATOM 4395 C CA  . PHE B 1 57  ? -43.443 6.259   155.839 1.00 31.71  ? 103 PHE B CA  1 
ATOM 4396 C C   . PHE B 1 57  ? -44.833 5.664   156.047 1.00 28.16  ? 103 PHE B C   1 
ATOM 4397 O O   . PHE B 1 57  ? -45.000 4.547   156.540 1.00 32.37  ? 103 PHE B O   1 
ATOM 4398 C CB  . PHE B 1 57  ? -43.206 6.604   154.368 1.00 29.67  ? 103 PHE B CB  1 
ATOM 4399 C CG  . PHE B 1 57  ? -43.687 5.551   153.412 1.00 34.59  ? 103 PHE B CG  1 
ATOM 4400 C CD1 . PHE B 1 57  ? -42.965 4.388   153.226 1.00 34.34  ? 103 PHE B CD1 1 
ATOM 4401 C CD2 . PHE B 1 57  ? -44.855 5.728   152.694 1.00 35.46  ? 103 PHE B CD2 1 
ATOM 4402 C CE1 . PHE B 1 57  ? -43.402 3.421   152.346 1.00 31.62  ? 103 PHE B CE1 1 
ATOM 4403 C CE2 . PHE B 1 57  ? -45.295 4.763   151.815 1.00 28.03  ? 103 PHE B CE2 1 
ATOM 4404 C CZ  . PHE B 1 57  ? -44.568 3.609   151.641 1.00 28.42  ? 103 PHE B CZ  1 
ATOM 4405 N N   . THR B 1 58  ? -45.846 6.435   155.662 1.00 28.42  ? 104 THR B N   1 
ATOM 4406 C CA  . THR B 1 58  ? -47.240 6.034   155.783 1.00 26.83  ? 104 THR B CA  1 
ATOM 4407 C C   . THR B 1 58  ? -48.056 6.670   154.664 1.00 35.52  ? 104 THR B C   1 
ATOM 4408 O O   . THR B 1 58  ? -48.056 7.898   154.522 1.00 50.67  ? 104 THR B O   1 
ATOM 4409 C CB  . THR B 1 58  ? -47.802 6.440   157.145 1.00 24.82  ? 104 THR B CB  1 
ATOM 4410 O OG1 . THR B 1 58  ? -47.351 5.517   158.143 1.00 38.03  ? 104 THR B OG1 1 
ATOM 4411 C CG2 . THR B 1 58  ? -49.319 6.442   157.114 1.00 23.95  ? 104 THR B CG2 1 
ATOM 4412 N N   . PRO B 1 59  ? -48.753 5.881   153.851 1.00 31.93  ? 105 PRO B N   1 
ATOM 4413 C CA  . PRO B 1 59  ? -49.574 6.466   152.786 1.00 40.13  ? 105 PRO B CA  1 
ATOM 4414 C C   . PRO B 1 59  ? -50.813 7.142   153.353 1.00 42.50  ? 105 PRO B C   1 
ATOM 4415 O O   . PRO B 1 59  ? -51.475 6.619   154.253 1.00 53.70  ? 105 PRO B O   1 
ATOM 4416 C CB  . PRO B 1 59  ? -49.944 5.257   151.921 1.00 36.39  ? 105 PRO B CB  1 
ATOM 4417 C CG  . PRO B 1 59  ? -49.900 4.104   152.856 1.00 30.05  ? 105 PRO B CG  1 
ATOM 4418 C CD  . PRO B 1 59  ? -48.870 4.414   153.905 1.00 28.12  ? 105 PRO B CD  1 
ATOM 4419 N N   . THR B 1 60  ? -51.124 8.318   152.817 1.00 32.25  ? 106 THR B N   1 
ATOM 4420 C CA  . THR B 1 60  ? -52.226 9.123   153.317 1.00 36.76  ? 106 THR B CA  1 
ATOM 4421 C C   . THR B 1 60  ? -53.020 9.700   152.155 1.00 45.09  ? 106 THR B C   1 
ATOM 4422 O O   . THR B 1 60  ? -52.468 9.926   151.072 1.00 45.49  ? 106 THR B O   1 
ATOM 4423 C CB  . THR B 1 60  ? -51.728 10.271  154.208 1.00 41.62  ? 106 THR B CB  1 
ATOM 4424 O OG1 . THR B 1 60  ? -50.608 10.909  153.584 1.00 41.80  ? 106 THR B OG1 1 
ATOM 4425 C CG2 . THR B 1 60  ? -51.304 9.744   155.567 1.00 38.45  ? 106 THR B CG2 1 
ATOM 4426 N N   . PRO B 1 61  ? -54.321 9.937   152.348 1.00 46.70  ? 107 PRO B N   1 
ATOM 4427 C CA  . PRO B 1 61  ? -55.102 10.634  151.315 1.00 39.15  ? 107 PRO B CA  1 
ATOM 4428 C C   . PRO B 1 61  ? -54.772 12.111  151.186 1.00 48.09  ? 107 PRO B C   1 
ATOM 4429 O O   . PRO B 1 61  ? -55.121 12.713  150.164 1.00 49.17  ? 107 PRO B O   1 
ATOM 4430 C CB  . PRO B 1 61  ? -56.553 10.434  151.772 1.00 34.98  ? 107 PRO B CB  1 
ATOM 4431 C CG  . PRO B 1 61  ? -56.506 9.290   152.720 1.00 42.60  ? 107 PRO B CG  1 
ATOM 4432 C CD  . PRO B 1 61  ? -55.182 9.375   153.398 1.00 46.24  ? 107 PRO B CD  1 
ATOM 4433 N N   . GLY B 1 62  ? -54.113 12.714  152.172 1.00 42.66  ? 108 GLY B N   1 
ATOM 4434 C CA  . GLY B 1 62  ? -53.738 14.110  152.060 1.00 40.25  ? 108 GLY B CA  1 
ATOM 4435 C C   . GLY B 1 62  ? -54.636 15.134  152.728 1.00 43.03  ? 108 GLY B C   1 
ATOM 4436 O O   . GLY B 1 62  ? -55.094 16.073  152.071 1.00 45.90  ? 108 GLY B O   1 
ATOM 4437 N N   . GLU B 1 63  ? -54.899 14.966  154.026 1.00 46.54  ? 109 GLU B N   1 
ATOM 4438 C CA  . GLU B 1 63  ? -55.490 16.011  154.867 1.00 45.55  ? 109 GLU B CA  1 
ATOM 4439 C C   . GLU B 1 63  ? -56.873 16.433  154.355 1.00 49.02  ? 109 GLU B C   1 
ATOM 4440 O O   . GLU B 1 63  ? -57.079 17.531  153.837 1.00 51.73  ? 109 GLU B O   1 
ATOM 4441 C CB  . GLU B 1 63  ? -54.546 17.216  154.972 1.00 50.31  ? 109 GLU B CB  1 
ATOM 4442 C CG  . GLU B 1 63  ? -54.983 18.314  155.944 1.00 50.23  ? 109 GLU B CG  1 
ATOM 4443 C CD  . GLU B 1 63  ? -55.064 17.849  157.386 1.00 56.95  ? 109 GLU B CD  1 
ATOM 4444 O OE1 . GLU B 1 63  ? -56.005 17.105  157.730 1.00 57.77  ? 109 GLU B OE1 1 
ATOM 4445 O OE2 . GLU B 1 63  ? -54.184 18.236  158.182 1.00 60.43  ? 109 GLU B OE2 1 
ATOM 4446 N N   . SER B 1 64  ? -57.814 15.505  154.486 1.00 48.32  ? 110 SER B N   1 
ATOM 4447 C CA  . SER B 1 64  ? -59.210 15.755  154.152 1.00 44.92  ? 110 SER B CA  1 
ATOM 4448 C C   . SER B 1 64  ? -60.012 15.981  155.426 1.00 46.10  ? 110 SER B C   1 
ATOM 4449 O O   . SER B 1 64  ? -60.006 15.134  156.325 1.00 54.57  ? 110 SER B O   1 
ATOM 4450 C CB  . SER B 1 64  ? -59.798 14.587  153.366 1.00 47.01  ? 110 SER B CB  1 
ATOM 4451 O OG  . SER B 1 64  ? -61.017 14.956  152.748 1.00 53.14  ? 110 SER B OG  1 
ATOM 4452 N N   . TYR B 1 65  ? -60.705 17.120  155.500 1.00 46.88  ? 111 TYR B N   1 
ATOM 4453 C CA  . TYR B 1 65  ? -61.679 17.334  156.563 1.00 49.55  ? 111 TYR B CA  1 
ATOM 4454 C C   . TYR B 1 65  ? -62.960 17.987  156.058 1.00 54.21  ? 111 TYR B C   1 
ATOM 4455 O O   . TYR B 1 65  ? -63.785 18.406  156.879 1.00 55.21  ? 111 TYR B O   1 
ATOM 4456 C CB  . TYR B 1 65  ? -61.092 18.171  157.708 1.00 50.91  ? 111 TYR B CB  1 
ATOM 4457 C CG  . TYR B 1 65  ? -60.039 19.172  157.298 1.00 53.70  ? 111 TYR B CG  1 
ATOM 4458 C CD1 . TYR B 1 65  ? -60.329 20.193  156.405 1.00 53.80  ? 111 TYR B CD1 1 
ATOM 4459 C CD2 . TYR B 1 65  ? -58.757 19.106  157.824 1.00 54.26  ? 111 TYR B CD2 1 
ATOM 4460 C CE1 . TYR B 1 65  ? -59.365 21.113  156.035 1.00 57.52  ? 111 TYR B CE1 1 
ATOM 4461 C CE2 . TYR B 1 65  ? -57.788 20.019  157.463 1.00 55.89  ? 111 TYR B CE2 1 
ATOM 4462 C CZ  . TYR B 1 65  ? -58.097 21.021  156.568 1.00 62.76  ? 111 TYR B CZ  1 
ATOM 4463 O OH  . TYR B 1 65  ? -57.131 21.932  156.207 1.00 60.51  ? 111 TYR B OH  1 
ATOM 4464 N N   . ASN B 1 66  ? -63.157 18.084  154.747 1.00 54.62  ? 112 ASN B N   1 
ATOM 4465 C CA  . ASN B 1 66  ? -64.375 18.637  154.171 1.00 49.29  ? 112 ASN B CA  1 
ATOM 4466 C C   . ASN B 1 66  ? -64.661 17.908  152.864 1.00 49.17  ? 112 ASN B C   1 
ATOM 4467 O O   . ASN B 1 66  ? -63.905 17.026  152.447 1.00 54.81  ? 112 ASN B O   1 
ATOM 4468 C CB  . ASN B 1 66  ? -64.242 20.151  153.960 1.00 51.04  ? 112 ASN B CB  1 
ATOM 4469 C CG  . ASN B 1 66  ? -64.558 20.945  155.209 1.00 58.48  ? 112 ASN B CG  1 
ATOM 4470 O OD1 . ASN B 1 66  ? -64.372 22.161  155.247 1.00 55.03  ? 112 ASN B OD1 1 
ATOM 4471 N ND2 . ASN B 1 66  ? -65.053 20.264  156.235 1.00 61.11  ? 112 ASN B ND2 1 
ATOM 4472 N N   . LYS B 1 67  ? -65.759 18.280  152.215 1.00 42.41  ? 113 LYS B N   1 
ATOM 4473 C CA  . LYS B 1 67  ? -66.080 17.777  150.887 1.00 45.57  ? 113 LYS B CA  1 
ATOM 4474 C C   . LYS B 1 67  ? -65.351 18.530  149.786 1.00 50.40  ? 113 LYS B C   1 
ATOM 4475 O O   . LYS B 1 67  ? -65.437 18.133  148.620 1.00 51.44  ? 113 LYS B O   1 
ATOM 4476 C CB  . LYS B 1 67  ? -67.590 17.846  150.643 1.00 45.34  ? 113 LYS B CB  1 
ATOM 4477 C CG  . LYS B 1 67  ? -68.124 16.726  149.769 1.00 46.97  ? 113 LYS B CG  1 
ATOM 4478 C CD  . LYS B 1 67  ? -69.404 16.140  150.333 1.00 51.30  ? 113 LYS B CD  1 
ATOM 4479 C CE  . LYS B 1 67  ? -69.854 14.936  149.524 1.00 52.85  ? 113 LYS B CE  1 
ATOM 4480 N NZ  . LYS B 1 67  ? -71.272 14.582  149.803 1.00 50.81  ? 113 LYS B NZ  1 
ATOM 4481 N N   . ASN B 1 68  ? -64.646 19.604  150.125 1.00 52.92  ? 114 ASN B N   1 
ATOM 4482 C CA  . ASN B 1 68  ? -63.900 20.394  149.159 1.00 50.24  ? 114 ASN B CA  1 
ATOM 4483 C C   . ASN B 1 68  ? -62.447 19.958  149.040 1.00 55.76  ? 114 ASN B C   1 
ATOM 4484 O O   . ASN B 1 68  ? -61.693 20.569  148.276 1.00 57.82  ? 114 ASN B O   1 
ATOM 4485 C CB  . ASN B 1 68  ? -63.962 21.875  149.539 1.00 51.42  ? 114 ASN B CB  1 
ATOM 4486 C CG  . ASN B 1 68  ? -65.290 22.510  149.189 1.00 57.96  ? 114 ASN B CG  1 
ATOM 4487 O OD1 . ASN B 1 68  ? -65.647 22.623  148.017 1.00 63.09  ? 114 ASN B OD1 1 
ATOM 4488 N ND2 . ASN B 1 68  ? -66.034 22.923  150.207 1.00 56.80  ? 114 ASN B ND2 1 
ATOM 4489 N N   . SER B 1 69  ? -62.041 18.925  149.774 1.00 48.97  ? 115 SER B N   1 
ATOM 4490 C CA  . SER B 1 69  ? -60.654 18.499  149.772 1.00 42.36  ? 115 SER B CA  1 
ATOM 4491 C C   . SER B 1 69  ? -60.277 17.897  148.420 1.00 40.07  ? 115 SER B C   1 
ATOM 4492 O O   . SER B 1 69  ? -61.138 17.388  147.697 1.00 48.07  ? 115 SER B O   1 
ATOM 4493 C CB  . SER B 1 69  ? -60.414 17.478  150.878 1.00 45.59  ? 115 SER B CB  1 
ATOM 4494 O OG  . SER B 1 69  ? -60.757 18.015  152.143 1.00 52.69  ? 115 SER B OG  1 
ATOM 4495 N N   . PRO B 1 70  ? -58.994 17.956  148.051 1.00 35.30  ? 116 PRO B N   1 
ATOM 4496 C CA  . PRO B 1 70  ? -58.580 17.386  146.760 1.00 38.67  ? 116 PRO B CA  1 
ATOM 4497 C C   . PRO B 1 70  ? -58.911 15.915  146.621 1.00 36.35  ? 116 PRO B C   1 
ATOM 4498 O O   . PRO B 1 70  ? -59.215 15.462  145.511 1.00 42.28  ? 116 PRO B O   1 
ATOM 4499 C CB  . PRO B 1 70  ? -57.065 17.628  146.742 1.00 43.63  ? 116 PRO B CB  1 
ATOM 4500 C CG  . PRO B 1 70  ? -56.856 18.773  147.668 1.00 44.99  ? 116 PRO B CG  1 
ATOM 4501 C CD  . PRO B 1 70  ? -57.872 18.603  148.751 1.00 41.45  ? 116 PRO B CD  1 
ATOM 4502 N N   . ILE B 1 71  ? -58.876 15.153  147.716 1.00 38.87  ? 117 ILE B N   1 
ATOM 4503 C CA  . ILE B 1 71  ? -59.245 13.743  147.636 1.00 44.64  ? 117 ILE B CA  1 
ATOM 4504 C C   . ILE B 1 71  ? -60.717 13.601  147.267 1.00 44.44  ? 117 ILE B C   1 
ATOM 4505 O O   . ILE B 1 71  ? -61.088 12.733  146.472 1.00 51.31  ? 117 ILE B O   1 
ATOM 4506 C CB  . ILE B 1 71  ? -58.901 13.015  148.951 1.00 43.24  ? 117 ILE B CB  1 
ATOM 4507 C CG1 . ILE B 1 71  ? -58.970 11.499  148.761 1.00 40.68  ? 117 ILE B CG1 1 
ATOM 4508 C CG2 . ILE B 1 71  ? -59.816 13.441  150.079 1.00 38.51  ? 117 ILE B CG2 1 
ATOM 4509 C CD1 . ILE B 1 71  ? -58.358 11.017  147.474 1.00 39.45  ? 117 ILE B CD1 1 
ATOM 4510 N N   . ASN B 1 72  ? -61.575 14.471  147.809 1.00 43.38  ? 118 ASN B N   1 
ATOM 4511 C CA  . ASN B 1 72  ? -62.993 14.411  147.471 1.00 33.03  ? 118 ASN B CA  1 
ATOM 4512 C C   . ASN B 1 72  ? -63.251 14.886  146.048 1.00 36.45  ? 118 ASN B C   1 
ATOM 4513 O O   . ASN B 1 72  ? -64.113 14.329  145.360 1.00 45.73  ? 118 ASN B O   1 
ATOM 4514 C CB  . ASN B 1 72  ? -63.806 15.235  148.465 1.00 39.15  ? 118 ASN B CB  1 
ATOM 4515 C CG  . ASN B 1 72  ? -63.876 14.591  149.832 1.00 39.62  ? 118 ASN B CG  1 
ATOM 4516 O OD1 . ASN B 1 72  ? -64.688 13.699  150.068 1.00 34.06  ? 118 ASN B OD1 1 
ATOM 4517 N ND2 . ASN B 1 72  ? -63.023 15.041  150.742 1.00 42.11  ? 118 ASN B ND2 1 
ATOM 4518 N N   . ILE B 1 73  ? -62.521 15.905  145.590 1.00 43.92  ? 119 ILE B N   1 
ATOM 4519 C CA  . ILE B 1 73  ? -62.651 16.332  144.199 1.00 43.62  ? 119 ILE B CA  1 
ATOM 4520 C C   . ILE B 1 73  ? -62.258 15.200  143.258 1.00 46.19  ? 119 ILE B C   1 
ATOM 4521 O O   . ILE B 1 73  ? -62.952 14.923  142.271 1.00 51.50  ? 119 ILE B O   1 
ATOM 4522 C CB  . ILE B 1 73  ? -61.810 17.595  143.941 1.00 44.64  ? 119 ILE B CB  1 
ATOM 4523 C CG1 . ILE B 1 73  ? -62.102 18.668  144.989 1.00 41.89  ? 119 ILE B CG1 1 
ATOM 4524 C CG2 . ILE B 1 73  ? -62.075 18.128  142.546 1.00 48.72  ? 119 ILE B CG2 1 
ATOM 4525 C CD1 . ILE B 1 73  ? -63.556 19.047  145.088 1.00 49.41  ? 119 ILE B CD1 1 
ATOM 4526 N N   . ALA B 1 74  ? -61.144 14.525  143.551 1.00 39.40  ? 120 ALA B N   1 
ATOM 4527 C CA  . ALA B 1 74  ? -60.717 13.398  142.732 1.00 37.17  ? 120 ALA B CA  1 
ATOM 4528 C C   . ALA B 1 74  ? -61.709 12.247  142.797 1.00 42.12  ? 120 ALA B C   1 
ATOM 4529 O O   . ALA B 1 74  ? -61.949 11.583  141.784 1.00 50.58  ? 120 ALA B O   1 
ATOM 4530 C CB  . ALA B 1 74  ? -59.334 12.926  143.169 1.00 40.90  ? 120 ALA B CB  1 
ATOM 4531 N N   . ALA B 1 75  ? -62.282 11.988  143.974 1.00 40.93  ? 121 ALA B N   1 
ATOM 4532 C CA  . ALA B 1 75  ? -63.285 10.938  144.100 1.00 38.78  ? 121 ALA B CA  1 
ATOM 4533 C C   . ALA B 1 75  ? -64.497 11.241  143.235 1.00 38.87  ? 121 ALA B C   1 
ATOM 4534 O O   . ALA B 1 75  ? -65.003 10.366  142.524 1.00 40.77  ? 121 ALA B O   1 
ATOM 4535 C CB  . ALA B 1 75  ? -63.698 10.784  145.563 1.00 38.40  ? 121 ALA B CB  1 
ATOM 4536 N N   . GLN B 1 76  ? -64.972 12.486  143.278 1.00 45.77  ? 122 GLN B N   1 
ATOM 4537 C CA  . GLN B 1 76  ? -66.110 12.870  142.451 1.00 40.89  ? 122 GLN B CA  1 
ATOM 4538 C C   . GLN B 1 76  ? -65.780 12.743  140.970 1.00 41.14  ? 122 GLN B C   1 
ATOM 4539 O O   . GLN B 1 76  ? -66.593 12.231  140.191 1.00 50.11  ? 122 GLN B O   1 
ATOM 4540 C CB  . GLN B 1 76  ? -66.545 14.295  142.791 1.00 42.29  ? 122 GLN B CB  1 
ATOM 4541 C CG  . GLN B 1 76  ? -67.198 15.042  141.644 1.00 43.36  ? 122 GLN B CG  1 
ATOM 4542 C CD  . GLN B 1 76  ? -67.234 16.539  141.874 1.00 48.60  ? 122 GLN B CD  1 
ATOM 4543 O OE1 . GLN B 1 76  ? -67.629 17.005  142.942 1.00 51.06  ? 122 GLN B OE1 1 
ATOM 4544 N NE2 . GLN B 1 76  ? -66.818 17.301  140.871 1.00 49.18  ? 122 GLN B NE2 1 
ATOM 4545 N N   . ASN B 1 77  ? -64.587 13.183  140.566 1.00 42.02  ? 123 ASN B N   1 
ATOM 4546 C CA  . ASN B 1 77  ? -64.209 13.100  139.158 1.00 43.79  ? 123 ASN B CA  1 
ATOM 4547 C C   . ASN B 1 77  ? -64.130 11.652  138.688 1.00 46.39  ? 123 ASN B C   1 
ATOM 4548 O O   . ASN B 1 77  ? -64.644 11.309  137.617 1.00 55.13  ? 123 ASN B O   1 
ATOM 4549 C CB  . ASN B 1 77  ? -62.877 13.812  138.930 1.00 49.77  ? 123 ASN B CB  1 
ATOM 4550 C CG  . ASN B 1 77  ? -63.020 15.319  138.907 1.00 57.68  ? 123 ASN B CG  1 
ATOM 4551 O OD1 . ASN B 1 77  ? -63.940 15.877  139.503 1.00 57.76  ? 123 ASN B OD1 1 
ATOM 4552 N ND2 . ASN B 1 77  ? -62.106 15.989  138.215 1.00 57.35  ? 123 ASN B ND2 1 
ATOM 4553 N N   . VAL B 1 78  ? -63.495 10.783  139.478 1.00 41.60  ? 124 VAL B N   1 
ATOM 4554 C CA  . VAL B 1 78  ? -63.334 9.395   139.058 1.00 43.05  ? 124 VAL B CA  1 
ATOM 4555 C C   . VAL B 1 78  ? -64.670 8.663   139.070 1.00 47.54  ? 124 VAL B C   1 
ATOM 4556 O O   . VAL B 1 78  ? -64.937 7.836   138.189 1.00 51.96  ? 124 VAL B O   1 
ATOM 4557 C CB  . VAL B 1 78  ? -62.268 8.686   139.920 1.00 42.97  ? 124 VAL B CB  1 
ATOM 4558 C CG1 . VAL B 1 78  ? -62.792 8.358   141.310 1.00 45.42  ? 124 VAL B CG1 1 
ATOM 4559 C CG2 . VAL B 1 78  ? -61.777 7.429   139.224 1.00 42.25  ? 124 VAL B CG2 1 
ATOM 4560 N N   . TYR B 1 79  ? -65.538 8.952   140.045 1.00 49.80  ? 125 TYR B N   1 
ATOM 4561 C CA  . TYR B 1 79  ? -66.858 8.337   140.055 1.00 40.93  ? 125 TYR B CA  1 
ATOM 4562 C C   . TYR B 1 79  ? -67.681 8.786   138.859 1.00 40.53  ? 125 TYR B C   1 
ATOM 4563 O O   . TYR B 1 79  ? -68.384 7.977   138.247 1.00 46.06  ? 125 TYR B O   1 
ATOM 4564 C CB  . TYR B 1 79  ? -67.583 8.670   141.353 1.00 44.55  ? 125 TYR B CB  1 
ATOM 4565 C CG  . TYR B 1 79  ? -68.959 8.059   141.460 1.00 42.91  ? 125 TYR B CG  1 
ATOM 4566 C CD1 . TYR B 1 79  ? -69.121 6.729   141.815 1.00 48.78  ? 125 TYR B CD1 1 
ATOM 4567 C CD2 . TYR B 1 79  ? -70.095 8.813   141.209 1.00 46.96  ? 125 TYR B CD2 1 
ATOM 4568 C CE1 . TYR B 1 79  ? -70.376 6.166   141.916 1.00 49.40  ? 125 TYR B CE1 1 
ATOM 4569 C CE2 . TYR B 1 79  ? -71.354 8.258   141.307 1.00 51.25  ? 125 TYR B CE2 1 
ATOM 4570 C CZ  . TYR B 1 79  ? -71.488 6.935   141.660 1.00 48.76  ? 125 TYR B CZ  1 
ATOM 4571 O OH  . TYR B 1 79  ? -72.741 6.377   141.759 1.00 48.87  ? 125 TYR B OH  1 
ATOM 4572 N N   . THR B 1 80  ? -67.614 10.075  138.517 1.00 50.85  ? 126 THR B N   1 
ATOM 4573 C CA  . THR B 1 80  ? -68.323 10.557  137.339 1.00 49.34  ? 126 THR B CA  1 
ATOM 4574 C C   . THR B 1 80  ? -67.799 9.887   136.079 1.00 52.46  ? 126 THR B C   1 
ATOM 4575 O O   . THR B 1 80  ? -68.582 9.477   135.216 1.00 58.21  ? 126 THR B O   1 
ATOM 4576 C CB  . THR B 1 80  ? -68.192 12.075  137.234 1.00 50.96  ? 126 THR B CB  1 
ATOM 4577 O OG1 . THR B 1 80  ? -68.511 12.669  138.497 1.00 56.69  ? 126 THR B OG1 1 
ATOM 4578 C CG2 . THR B 1 80  ? -69.135 12.618  136.174 1.00 53.08  ? 126 THR B CG2 1 
ATOM 4579 N N   . TYR B 1 81  ? -66.476 9.750   135.964 1.00 48.62  ? 127 TYR B N   1 
ATOM 4580 C CA  . TYR B 1 81  ? -65.894 9.072   134.811 1.00 46.57  ? 127 TYR B CA  1 
ATOM 4581 C C   . TYR B 1 81  ? -66.393 7.638   134.703 1.00 49.49  ? 127 TYR B C   1 
ATOM 4582 O O   . TYR B 1 81  ? -66.832 7.199   133.634 1.00 55.06  ? 127 TYR B O   1 
ATOM 4583 C CB  . TYR B 1 81  ? -64.370 9.102   134.909 1.00 50.34  ? 127 TYR B CB  1 
ATOM 4584 C CG  . TYR B 1 81  ? -63.664 8.494   133.721 1.00 52.70  ? 127 TYR B CG  1 
ATOM 4585 C CD1 . TYR B 1 81  ? -63.543 9.191   132.529 1.00 56.94  ? 127 TYR B CD1 1 
ATOM 4586 C CD2 . TYR B 1 81  ? -63.116 7.223   133.795 1.00 52.45  ? 127 TYR B CD2 1 
ATOM 4587 C CE1 . TYR B 1 81  ? -62.895 8.637   131.444 1.00 58.07  ? 127 TYR B CE1 1 
ATOM 4588 C CE2 . TYR B 1 81  ? -62.469 6.662   132.716 1.00 51.74  ? 127 TYR B CE2 1 
ATOM 4589 C CZ  . TYR B 1 81  ? -62.360 7.372   131.543 1.00 54.82  ? 127 TYR B CZ  1 
ATOM 4590 O OH  . TYR B 1 81  ? -61.714 6.815   130.465 1.00 55.72  ? 127 TYR B OH  1 
ATOM 4591 N N   . VAL B 1 82  ? -66.342 6.894   135.810 1.00 52.73  ? 128 VAL B N   1 
ATOM 4592 C CA  . VAL B 1 82  ? -66.734 5.488   135.781 1.00 50.04  ? 128 VAL B CA  1 
ATOM 4593 C C   . VAL B 1 82  ? -68.218 5.350   135.461 1.00 55.29  ? 128 VAL B C   1 
ATOM 4594 O O   . VAL B 1 82  ? -68.612 4.559   134.596 1.00 60.01  ? 128 VAL B O   1 
ATOM 4595 C CB  . VAL B 1 82  ? -66.375 4.807   137.113 1.00 44.05  ? 128 VAL B CB  1 
ATOM 4596 C CG1 . VAL B 1 82  ? -67.185 3.539   137.298 1.00 48.05  ? 128 VAL B CG1 1 
ATOM 4597 C CG2 . VAL B 1 82  ? -64.889 4.501   137.162 1.00 43.04  ? 128 VAL B CG2 1 
ATOM 4598 N N   . ARG B 1 83  ? -69.063 6.125   136.143 1.00 53.64  ? 129 ARG B N   1 
ATOM 4599 C CA  . ARG B 1 83  ? -70.501 6.048   135.931 1.00 45.00  ? 129 ARG B CA  1 
ATOM 4600 C C   . ARG B 1 83  ? -70.911 6.488   134.532 1.00 53.34  ? 129 ARG B C   1 
ATOM 4601 O O   . ARG B 1 83  ? -71.851 5.917   133.971 1.00 56.92  ? 129 ARG B O   1 
ATOM 4602 C CB  . ARG B 1 83  ? -71.225 6.883   136.992 1.00 51.43  ? 129 ARG B CB  1 
ATOM 4603 C CG  . ARG B 1 83  ? -72.700 7.132   136.725 1.00 55.21  ? 129 ARG B CG  1 
ATOM 4604 C CD  . ARG B 1 83  ? -73.080 8.575   137.026 1.00 55.46  ? 129 ARG B CD  1 
ATOM 4605 N NE  . ARG B 1 83  ? -72.429 9.517   136.124 1.00 61.60  ? 129 ARG B NE  1 
ATOM 4606 C CZ  . ARG B 1 83  ? -72.915 9.886   134.947 1.00 59.92  ? 129 ARG B CZ  1 
ATOM 4607 N NH1 . ARG B 1 83  ? -74.065 9.414   134.496 1.00 57.11  ? 129 ARG B NH1 1 
ATOM 4608 N NH2 . ARG B 1 83  ? -72.231 10.752  134.206 1.00 54.21  ? 129 ARG B NH2 1 
ATOM 4609 N N   . HIS B 1 84  ? -70.231 7.475   133.951 1.00 64.12  ? 130 HIS B N   1 
ATOM 4610 C CA  . HIS B 1 84  ? -70.514 7.905   132.591 1.00 63.30  ? 130 HIS B CA  1 
ATOM 4611 C C   . HIS B 1 84  ? -69.995 6.932   131.543 1.00 63.11  ? 130 HIS B C   1 
ATOM 4612 O O   . HIS B 1 84  ? -70.601 6.821   130.472 1.00 65.23  ? 130 HIS B O   1 
ATOM 4613 C CB  . HIS B 1 84  ? -69.914 9.295   132.350 1.00 62.12  ? 130 HIS B CB  1 
ATOM 4614 C CG  . HIS B 1 84  ? -69.780 9.655   130.904 1.00 68.81  ? 130 HIS B CG  1 
ATOM 4615 N ND1 . HIS B 1 84  ? -70.796 9.469   129.992 1.00 72.35  ? 130 HIS B ND1 1 
ATOM 4616 C CD2 . HIS B 1 84  ? -68.745 10.187  130.211 1.00 66.73  ? 130 HIS B CD2 1 
ATOM 4617 C CE1 . HIS B 1 84  ? -70.394 9.872   128.799 1.00 72.31  ? 130 HIS B CE1 1 
ATOM 4618 N NE2 . HIS B 1 84  ? -69.153 10.312  128.905 1.00 70.46  ? 130 HIS B NE2 1 
ATOM 4619 N N   . MET B 1 85  ? -68.901 6.224   131.818 1.00 60.25  ? 131 MET B N   1 
ATOM 4620 C CA  . MET B 1 85  ? -68.368 5.237   130.891 1.00 63.18  ? 131 MET B CA  1 
ATOM 4621 C C   . MET B 1 85  ? -69.077 3.891   131.014 1.00 66.51  ? 131 MET B C   1 
ATOM 4622 O O   . MET B 1 85  ? -69.010 3.074   130.090 1.00 66.62  ? 131 MET B O   1 
ATOM 4623 C CB  . MET B 1 85  ? -66.858 5.089   131.121 1.00 63.56  ? 131 MET B CB  1 
ATOM 4624 C CG  . MET B 1 85  ? -66.215 3.827   130.574 1.00 66.25  ? 131 MET B CG  1 
ATOM 4625 S SD  . MET B 1 85  ? -65.745 3.978   128.841 1.00 79.15  ? 131 MET B SD  1 
ATOM 4626 C CE  . MET B 1 85  ? -64.649 5.391   128.910 1.00 66.09  ? 131 MET B CE  1 
ATOM 4627 N N   . ASN B 1 86  ? -69.812 3.672   132.099 1.00 67.36  ? 132 ASN B N   1 
ATOM 4628 C CA  . ASN B 1 86  ? -70.448 2.392   132.373 1.00 63.76  ? 132 ASN B CA  1 
ATOM 4629 C C   . ASN B 1 86  ? -71.962 2.543   132.370 1.00 70.44  ? 132 ASN B C   1 
ATOM 4630 O O   . ASN B 1 86  ? -72.486 3.624   132.654 1.00 69.60  ? 132 ASN B O   1 
ATOM 4631 C CB  . ASN B 1 86  ? -69.992 1.830   133.717 1.00 58.97  ? 132 ASN B CB  1 
ATOM 4632 C CG  . ASN B 1 86  ? -68.773 0.955   133.591 1.00 65.67  ? 132 ASN B CG  1 
ATOM 4633 O OD1 . ASN B 1 86  ? -68.073 0.992   132.581 1.00 69.83  ? 132 ASN B OD1 1 
ATOM 4634 N ND2 . ASN B 1 86  ? -68.512 0.154   134.613 1.00 68.62  ? 132 ASN B ND2 1 
ATOM 4635 N N   . SER B 1 87  ? -72.655 1.460   132.035 1.00 81.35  ? 133 SER B N   1 
ATOM 4636 C CA  . SER B 1 87  ? -74.108 1.381   132.125 1.00 84.12  ? 133 SER B CA  1 
ATOM 4637 C C   . SER B 1 87  ? -74.453 0.095   132.864 1.00 84.98  ? 133 SER B C   1 
ATOM 4638 O O   . SER B 1 87  ? -74.089 -0.998  132.418 1.00 86.02  ? 133 SER B O   1 
ATOM 4639 C CB  . SER B 1 87  ? -74.745 1.416   130.737 1.00 85.05  ? 133 SER B CB  1 
ATOM 4640 O OG  . SER B 1 87  ? -74.170 2.440   129.945 1.00 82.27  ? 133 SER B OG  1 
ATOM 4641 N N   . GLY B 1 88  ? -75.142 0.223   133.994 1.00 86.84  ? 134 GLY B N   1 
ATOM 4642 C CA  . GLY B 1 88  ? -75.463 -0.941  134.796 1.00 87.77  ? 134 GLY B CA  1 
ATOM 4643 C C   . GLY B 1 88  ? -75.660 -0.654  136.270 1.00 88.52  ? 134 GLY B C   1 
ATOM 4644 O O   . GLY B 1 88  ? -76.452 0.220   136.639 1.00 85.53  ? 134 GLY B O   1 
ATOM 4645 N N   . HIS B 1 89  ? -74.949 -1.391  137.123 1.00 99.85  ? 135 HIS B N   1 
ATOM 4646 C CA  . HIS B 1 89  ? -75.141 -1.287  138.565 1.00 98.51  ? 135 HIS B CA  1 
ATOM 4647 C C   . HIS B 1 89  ? -74.828 0.124   139.044 1.00 97.90  ? 135 HIS B C   1 
ATOM 4648 O O   . HIS B 1 89  ? -73.748 0.659   138.771 1.00 96.87  ? 135 HIS B O   1 
ATOM 4649 C CB  . HIS B 1 89  ? -74.260 -2.297  139.298 1.00 97.29  ? 135 HIS B CB  1 
ATOM 4650 C CG  . HIS B 1 89  ? -73.972 -3.540  138.514 1.00 99.17  ? 135 HIS B CG  1 
ATOM 4651 N ND1 . HIS B 1 89  ? -72.746 -3.787  137.936 1.00 98.00  ? 135 HIS B ND1 1 
ATOM 4652 C CD2 . HIS B 1 89  ? -74.746 -4.613  138.226 1.00 96.60  ? 135 HIS B CD2 1 
ATOM 4653 C CE1 . HIS B 1 89  ? -72.779 -4.954  137.319 1.00 96.17  ? 135 HIS B CE1 1 
ATOM 4654 N NE2 . HIS B 1 89  ? -73.981 -5.476  137.480 1.00 96.58  ? 135 HIS B NE2 1 
ATOM 4655 N N   . ALA B 1 90  ? -75.777 0.726   139.761 1.00 91.72  ? 136 ALA B N   1 
ATOM 4656 C CA  . ALA B 1 90  ? -75.582 2.009   140.434 1.00 92.27  ? 136 ALA B CA  1 
ATOM 4657 C C   . ALA B 1 90  ? -75.934 1.776   141.899 1.00 92.05  ? 136 ALA B C   1 
ATOM 4658 O O   . ALA B 1 90  ? -77.065 2.011   142.331 1.00 94.16  ? 136 ALA B O   1 
ATOM 4659 C CB  . ALA B 1 90  ? -76.432 3.110   139.801 1.00 91.38  ? 136 ALA B CB  1 
ATOM 4660 N N   . ASN B 1 91  ? -74.951 1.307   142.664 1.00 73.83  ? 137 ASN B N   1 
ATOM 4661 C CA  . ASN B 1 91  ? -75.172 0.957   144.058 1.00 74.39  ? 137 ASN B CA  1 
ATOM 4662 C C   . ASN B 1 91  ? -74.039 1.381   144.980 1.00 73.99  ? 137 ASN B C   1 
ATOM 4663 O O   . ASN B 1 91  ? -74.095 1.073   146.174 1.00 75.96  ? 137 ASN B O   1 
ATOM 4664 C CB  . ASN B 1 91  ? -75.404 -0.556  144.192 1.00 76.70  ? 137 ASN B CB  1 
ATOM 4665 C CG  . ASN B 1 91  ? -74.434 -1.366  143.357 1.00 77.98  ? 137 ASN B CG  1 
ATOM 4666 O OD1 . ASN B 1 91  ? -73.503 -0.822  142.764 1.00 79.54  ? 137 ASN B OD1 1 
ATOM 4667 N ND2 . ASN B 1 91  ? -74.649 -2.675  143.304 1.00 72.36  ? 137 ASN B ND2 1 
ATOM 4668 N N   . TYR B 1 92  ? -73.023 2.070   144.474 1.00 54.16  ? 138 TYR B N   1 
ATOM 4669 C CA  . TYR B 1 92  ? -71.960 2.629   145.292 1.00 56.90  ? 138 TYR B CA  1 
ATOM 4670 C C   . TYR B 1 92  ? -71.796 4.105   144.958 1.00 55.19  ? 138 TYR B C   1 
ATOM 4671 O O   . TYR B 1 92  ? -72.373 4.617   143.996 1.00 57.53  ? 138 TYR B O   1 
ATOM 4672 C CB  . TYR B 1 92  ? -70.640 1.876   145.084 1.00 57.79  ? 138 TYR B CB  1 
ATOM 4673 C CG  . TYR B 1 92  ? -70.233 1.725   143.639 1.00 54.30  ? 138 TYR B CG  1 
ATOM 4674 C CD1 . TYR B 1 92  ? -69.521 2.724   142.993 1.00 55.74  ? 138 TYR B CD1 1 
ATOM 4675 C CD2 . TYR B 1 92  ? -70.555 0.584   142.921 1.00 49.55  ? 138 TYR B CD2 1 
ATOM 4676 C CE1 . TYR B 1 92  ? -69.144 2.593   141.676 1.00 51.41  ? 138 TYR B CE1 1 
ATOM 4677 C CE2 . TYR B 1 92  ? -70.181 0.444   141.601 1.00 53.05  ? 138 TYR B CE2 1 
ATOM 4678 C CZ  . TYR B 1 92  ? -69.476 1.452   140.986 1.00 51.86  ? 138 TYR B CZ  1 
ATOM 4679 O OH  . TYR B 1 92  ? -69.100 1.326   139.672 1.00 53.00  ? 138 TYR B OH  1 
ATOM 4680 N N   . GLU B 1 93  ? -70.997 4.791   145.765 1.00 55.97  ? 139 GLU B N   1 
ATOM 4681 C CA  . GLU B 1 93  ? -70.808 6.225   145.632 1.00 56.99  ? 139 GLU B CA  1 
ATOM 4682 C C   . GLU B 1 93  ? -69.348 6.545   145.342 1.00 56.73  ? 139 GLU B C   1 
ATOM 4683 O O   . GLU B 1 93  ? -68.483 5.664   145.291 1.00 60.13  ? 139 GLU B O   1 
ATOM 4684 C CB  . GLU B 1 93  ? -71.266 6.960   146.898 1.00 56.68  ? 139 GLU B CB  1 
ATOM 4685 C CG  . GLU B 1 93  ? -72.303 6.204   147.708 1.00 58.13  ? 139 GLU B CG  1 
ATOM 4686 C CD  . GLU B 1 93  ? -73.711 6.426   147.196 1.00 63.64  ? 139 GLU B CD  1 
ATOM 4687 O OE1 . GLU B 1 93  ? -73.891 7.265   146.289 1.00 60.44  ? 139 GLU B OE1 1 
ATOM 4688 O OE2 . GLU B 1 93  ? -74.639 5.760   147.700 1.00 65.96  ? 139 GLU B OE2 1 
ATOM 4689 N N   . GLN B 1 94  ? -69.089 7.840   145.151 1.00 49.75  ? 140 GLN B N   1 
ATOM 4690 C CA  . GLN B 1 94  ? -67.723 8.296   144.936 1.00 52.13  ? 140 GLN B CA  1 
ATOM 4691 C C   . GLN B 1 94  ? -66.848 7.963   146.132 1.00 54.86  ? 140 GLN B C   1 
ATOM 4692 O O   . GLN B 1 94  ? -65.695 7.551   145.972 1.00 61.64  ? 140 GLN B O   1 
ATOM 4693 C CB  . GLN B 1 94  ? -67.704 9.800   144.670 1.00 49.87  ? 140 GLN B CB  1 
ATOM 4694 C CG  . GLN B 1 94  ? -68.706 10.583  145.487 1.00 52.48  ? 140 GLN B CG  1 
ATOM 4695 C CD  . GLN B 1 94  ? -68.683 12.058  145.164 1.00 53.26  ? 140 GLN B CD  1 
ATOM 4696 O OE1 . GLN B 1 94  ? -68.975 12.462  144.040 1.00 57.78  ? 140 GLN B OE1 1 
ATOM 4697 N NE2 . GLN B 1 94  ? -68.331 12.874  146.148 1.00 50.24  ? 140 GLN B NE2 1 
ATOM 4698 N N   . ALA B 1 95  ? -67.382 8.137   147.341 1.00 48.76  ? 141 ALA B N   1 
ATOM 4699 C CA  . ALA B 1 95  ? -66.626 7.799   148.540 1.00 53.56  ? 141 ALA B CA  1 
ATOM 4700 C C   . ALA B 1 95  ? -66.300 6.312   148.581 1.00 55.65  ? 141 ALA B C   1 
ATOM 4701 O O   . ALA B 1 95  ? -65.172 5.922   148.904 1.00 64.96  ? 141 ALA B O   1 
ATOM 4702 C CB  . ALA B 1 95  ? -67.410 8.218   149.781 1.00 50.63  ? 141 ALA B CB  1 
ATOM 4703 N N   . ASP B 1 96  ? -67.277 5.463   148.253 1.00 47.87  ? 142 ASP B N   1 
ATOM 4704 C CA  . ASP B 1 96  ? -67.032 4.024   148.256 1.00 51.48  ? 142 ASP B CA  1 
ATOM 4705 C C   . ASP B 1 96  ? -65.953 3.649   147.249 1.00 52.40  ? 142 ASP B C   1 
ATOM 4706 O O   . ASP B 1 96  ? -65.033 2.884   147.568 1.00 59.89  ? 142 ASP B O   1 
ATOM 4707 C CB  . ASP B 1 96  ? -68.327 3.272   147.957 1.00 56.35  ? 142 ASP B CB  1 
ATOM 4708 C CG  . ASP B 1 96  ? -69.356 3.425   149.056 1.00 63.95  ? 142 ASP B CG  1 
ATOM 4709 O OD1 . ASP B 1 96  ? -68.963 3.478   150.240 1.00 63.94  ? 142 ASP B OD1 1 
ATOM 4710 O OD2 . ASP B 1 96  ? -70.561 3.493   148.736 1.00 60.55  ? 142 ASP B OD2 1 
ATOM 4711 N N   . LEU B 1 97  ? -66.037 4.197   146.035 1.00 37.30  ? 143 LEU B N   1 
ATOM 4712 C CA  . LEU B 1 97  ? -65.023 3.909   145.027 1.00 38.70  ? 143 LEU B CA  1 
ATOM 4713 C C   . LEU B 1 97  ? -63.652 4.415   145.460 1.00 46.78  ? 143 LEU B C   1 
ATOM 4714 O O   . LEU B 1 97  ? -62.633 3.760   145.215 1.00 53.30  ? 143 LEU B O   1 
ATOM 4715 C CB  . LEU B 1 97  ? -65.427 4.523   143.688 1.00 36.51  ? 143 LEU B CB  1 
ATOM 4716 C CG  . LEU B 1 97  ? -64.596 4.107   142.475 1.00 40.26  ? 143 LEU B CG  1 
ATOM 4717 C CD1 . LEU B 1 97  ? -64.390 2.603   142.464 1.00 41.15  ? 143 LEU B CD1 1 
ATOM 4718 C CD2 . LEU B 1 97  ? -65.267 4.562   141.193 1.00 44.56  ? 143 LEU B CD2 1 
ATOM 4719 N N   . MET B 1 98  ? -63.605 5.575   146.117 1.00 39.70  ? 144 MET B N   1 
ATOM 4720 C CA  . MET B 1 98  ? -62.321 6.125   146.528 1.00 34.69  ? 144 MET B CA  1 
ATOM 4721 C C   . MET B 1 98  ? -61.677 5.307   147.638 1.00 40.79  ? 144 MET B C   1 
ATOM 4722 O O   . MET B 1 98  ? -60.462 5.081   147.608 1.00 52.78  ? 144 MET B O   1 
ATOM 4723 C CB  . MET B 1 98  ? -62.482 7.573   146.982 1.00 39.82  ? 144 MET B CB  1 
ATOM 4724 C CG  . MET B 1 98  ? -61.275 8.415   146.653 1.00 47.32  ? 144 MET B CG  1 
ATOM 4725 S SD  . MET B 1 98  ? -60.730 8.033   144.980 1.00 51.49  ? 144 MET B SD  1 
ATOM 4726 C CE  . MET B 1 98  ? -58.981 8.344   145.105 1.00 39.32  ? 144 MET B CE  1 
ATOM 4727 N N   . MET B 1 99  ? -62.459 4.854   148.621 1.00 34.98  ? 145 MET B N   1 
ATOM 4728 C CA  . MET B 1 99  ? -61.882 3.970   149.630 1.00 41.27  ? 145 MET B CA  1 
ATOM 4729 C C   . MET B 1 99  ? -61.486 2.627   149.032 1.00 42.37  ? 145 MET B C   1 
ATOM 4730 O O   . MET B 1 99  ? -60.508 2.019   149.482 1.00 50.84  ? 145 MET B O   1 
ATOM 4731 C CB  . MET B 1 99  ? -62.835 3.777   150.810 1.00 35.64  ? 145 MET B CB  1 
ATOM 4732 C CG  . MET B 1 99  ? -63.582 5.023   151.216 1.00 38.97  ? 145 MET B CG  1 
ATOM 4733 S SD  . MET B 1 99  ? -62.646 6.076   152.336 1.00 60.81  ? 145 MET B SD  1 
ATOM 4734 C CE  . MET B 1 99  ? -62.963 5.279   153.902 1.00 48.27  ? 145 MET B CE  1 
ATOM 4735 N N   . TYR B 1 100 ? -62.208 2.155   148.014 1.00 32.93  ? 146 TYR B N   1 
ATOM 4736 C CA  . TYR B 1 100 ? -61.763 0.962   147.299 1.00 32.29  ? 146 TYR B CA  1 
ATOM 4737 C C   . TYR B 1 100 ? -60.398 1.189   146.662 1.00 36.78  ? 146 TYR B C   1 
ATOM 4738 O O   . TYR B 1 100 ? -59.513 0.327   146.732 1.00 51.61  ? 146 TYR B O   1 
ATOM 4739 C CB  . TYR B 1 100 ? -62.792 0.570   146.241 1.00 31.40  ? 146 TYR B CB  1 
ATOM 4740 C CG  . TYR B 1 100 ? -62.240 -0.314  145.148 1.00 30.35  ? 146 TYR B CG  1 
ATOM 4741 C CD1 . TYR B 1 100 ? -61.975 -1.655  145.379 1.00 35.53  ? 146 TYR B CD1 1 
ATOM 4742 C CD2 . TYR B 1 100 ? -61.981 0.195   143.885 1.00 35.15  ? 146 TYR B CD2 1 
ATOM 4743 C CE1 . TYR B 1 100 ? -61.473 -2.464  144.380 1.00 32.36  ? 146 TYR B CE1 1 
ATOM 4744 C CE2 . TYR B 1 100 ? -61.478 -0.605  142.883 1.00 34.11  ? 146 TYR B CE2 1 
ATOM 4745 C CZ  . TYR B 1 100 ? -61.226 -1.932  143.136 1.00 33.24  ? 146 TYR B CZ  1 
ATOM 4746 O OH  . TYR B 1 100 ? -60.723 -2.731  142.137 1.00 44.11  ? 146 TYR B OH  1 
ATOM 4747 N N   . LEU B 1 101 ? -60.210 2.350   146.034 1.00 27.45  ? 147 LEU B N   1 
ATOM 4748 C CA  . LEU B 1 101 ? -58.920 2.670   145.430 1.00 30.74  ? 147 LEU B CA  1 
ATOM 4749 C C   . LEU B 1 101 ? -57.815 2.762   146.476 1.00 35.84  ? 147 LEU B C   1 
ATOM 4750 O O   . LEU B 1 101 ? -56.692 2.302   146.236 1.00 48.59  ? 147 LEU B O   1 
ATOM 4751 C CB  . LEU B 1 101 ? -59.021 3.975   144.644 1.00 32.52  ? 147 LEU B CB  1 
ATOM 4752 C CG  . LEU B 1 101 ? -59.898 3.926   143.394 1.00 35.25  ? 147 LEU B CG  1 
ATOM 4753 C CD1 . LEU B 1 101 ? -59.716 5.179   142.563 1.00 38.46  ? 147 LEU B CD1 1 
ATOM 4754 C CD2 . LEU B 1 101 ? -59.584 2.693   142.571 1.00 36.95  ? 147 LEU B CD2 1 
ATOM 4755 N N   . LEU B 1 102 ? -58.112 3.351   147.635 1.00 31.15  ? 148 LEU B N   1 
ATOM 4756 C CA  . LEU B 1 102 ? -57.122 3.418   148.707 1.00 36.40  ? 148 LEU B CA  1 
ATOM 4757 C C   . LEU B 1 102 ? -56.751 2.031   149.223 1.00 43.22  ? 148 LEU B C   1 
ATOM 4758 O O   . LEU B 1 102 ? -55.572 1.759   149.484 1.00 43.84  ? 148 LEU B O   1 
ATOM 4759 C CB  . LEU B 1 102 ? -57.644 4.291   149.846 1.00 32.63  ? 148 LEU B CB  1 
ATOM 4760 C CG  . LEU B 1 102 ? -57.902 5.760   149.503 1.00 33.18  ? 148 LEU B CG  1 
ATOM 4761 C CD1 . LEU B 1 102 ? -58.353 6.528   150.733 1.00 32.01  ? 148 LEU B CD1 1 
ATOM 4762 C CD2 . LEU B 1 102 ? -56.665 6.398   148.897 1.00 38.84  ? 148 LEU B CD2 1 
ATOM 4763 N N   . ALA B 1 103 ? -57.735 1.142   149.374 1.00 34.34  ? 149 ALA B N   1 
ATOM 4764 C CA  . ALA B 1 103 ? -57.439 -0.224  149.793 1.00 22.77  ? 149 ALA B CA  1 
ATOM 4765 C C   . ALA B 1 103 ? -56.603 -0.952  148.748 1.00 29.22  ? 149 ALA B C   1 
ATOM 4766 O O   . ALA B 1 103 ? -55.710 -1.736  149.092 1.00 42.33  ? 149 ALA B O   1 
ATOM 4767 C CB  . ALA B 1 103 ? -58.735 -0.982  150.068 1.00 38.23  ? 149 ALA B CB  1 
ATOM 4768 N N   . MET B 1 104 ? -56.886 -0.714  147.466 1.00 29.07  ? 150 MET B N   1 
ATOM 4769 C CA  . MET B 1 104 ? -56.069 -1.303  146.410 1.00 35.37  ? 150 MET B CA  1 
ATOM 4770 C C   . MET B 1 104 ? -54.633 -0.799  146.491 1.00 40.41  ? 150 MET B C   1 
ATOM 4771 O O   . MET B 1 104 ? -53.681 -1.564  146.291 1.00 49.67  ? 150 MET B O   1 
ATOM 4772 C CB  . MET B 1 104 ? -56.673 -0.986  145.044 1.00 32.02  ? 150 MET B CB  1 
ATOM 4773 C CG  . MET B 1 104 ? -57.711 -1.986  144.581 1.00 36.54  ? 150 MET B CG  1 
ATOM 4774 S SD  . MET B 1 104 ? -57.359 -3.673  145.094 1.00 53.19  ? 150 MET B SD  1 
ATOM 4775 C CE  . MET B 1 104 ? -55.994 -4.084  144.022 1.00 40.81  ? 150 MET B CE  1 
ATOM 4776 N N   . ASP B 1 105 ? -54.461 0.493   146.777 1.00 32.41  ? 151 ASP B N   1 
ATOM 4777 C CA  . ASP B 1 105 ? -53.120 1.037   146.968 1.00 30.35  ? 151 ASP B CA  1 
ATOM 4778 C C   . ASP B 1 105 ? -52.416 0.362   148.137 1.00 35.39  ? 151 ASP B C   1 
ATOM 4779 O O   . ASP B 1 105 ? -51.216 0.073   148.066 1.00 47.33  ? 151 ASP B O   1 
ATOM 4780 C CB  . ASP B 1 105 ? -53.188 2.545   147.197 1.00 44.10  ? 151 ASP B CB  1 
ATOM 4781 C CG  . ASP B 1 105 ? -51.952 3.083   147.889 1.00 50.12  ? 151 ASP B CG  1 
ATOM 4782 O OD1 . ASP B 1 105 ? -50.836 2.840   147.386 1.00 46.42  ? 151 ASP B OD1 1 
ATOM 4783 O OD2 . ASP B 1 105 ? -52.098 3.753   148.933 1.00 52.00  ? 151 ASP B OD2 1 
ATOM 4784 N N   . SER B 1 106 ? -53.141 0.123   149.231 1.00 33.87  ? 152 SER B N   1 
ATOM 4785 C CA  . SER B 1 106 ? -52.542 -0.566  150.371 1.00 34.50  ? 152 SER B CA  1 
ATOM 4786 C C   . SER B 1 106 ? -52.106 -1.979  149.995 1.00 37.02  ? 152 SER B C   1 
ATOM 4787 O O   . SER B 1 106 ? -51.015 -2.424  150.373 1.00 43.07  ? 152 SER B O   1 
ATOM 4788 C CB  . SER B 1 106 ? -53.523 -0.602  151.540 1.00 40.82  ? 152 SER B CB  1 
ATOM 4789 O OG  . SER B 1 106 ? -54.405 -1.704  151.426 1.00 47.98  ? 152 SER B OG  1 
ATOM 4790 N N   . LEU B 1 107 ? -52.946 -2.701  149.251 1.00 30.15  ? 153 LEU B N   1 
ATOM 4791 C CA  . LEU B 1 107 ? -52.559 -4.034  148.794 1.00 26.73  ? 153 LEU B CA  1 
ATOM 4792 C C   . LEU B 1 107 ? -51.315 -3.991  147.922 1.00 29.85  ? 153 LEU B C   1 
ATOM 4793 O O   . LEU B 1 107 ? -50.431 -4.844  148.061 1.00 38.85  ? 153 LEU B O   1 
ATOM 4794 C CB  . LEU B 1 107 ? -53.688 -4.694  148.005 1.00 29.40  ? 153 LEU B CB  1 
ATOM 4795 C CG  . LEU B 1 107 ? -54.736 -5.544  148.721 1.00 38.21  ? 153 LEU B CG  1 
ATOM 4796 C CD1 . LEU B 1 107 ? -55.158 -4.941  150.051 1.00 37.20  ? 153 LEU B CD1 1 
ATOM 4797 C CD2 . LEU B 1 107 ? -55.921 -5.755  147.805 1.00 39.42  ? 153 LEU B CD2 1 
ATOM 4798 N N   . TYR B 1 108 ? -51.240 -3.016  147.018 1.00 23.01  ? 154 TYR B N   1 
ATOM 4799 C CA  . TYR B 1 108 ? -50.074 -2.893  146.153 1.00 22.91  ? 154 TYR B CA  1 
ATOM 4800 C C   . TYR B 1 108 ? -48.821 -2.576  146.958 1.00 28.09  ? 154 TYR B C   1 
ATOM 4801 O O   . TYR B 1 108 ? -47.741 -3.102  146.670 1.00 32.08  ? 154 TYR B O   1 
ATOM 4802 C CB  . TYR B 1 108 ? -50.335 -1.826  145.096 1.00 27.96  ? 154 TYR B CB  1 
ATOM 4803 C CG  . TYR B 1 108 ? -51.365 -2.252  144.080 1.00 32.44  ? 154 TYR B CG  1 
ATOM 4804 C CD1 . TYR B 1 108 ? -51.786 -3.571  144.008 1.00 38.91  ? 154 TYR B CD1 1 
ATOM 4805 C CD2 . TYR B 1 108 ? -51.938 -1.336  143.215 1.00 32.00  ? 154 TYR B CD2 1 
ATOM 4806 C CE1 . TYR B 1 108 ? -52.725 -3.970  143.088 1.00 36.66  ? 154 TYR B CE1 1 
ATOM 4807 C CE2 . TYR B 1 108 ? -52.885 -1.725  142.297 1.00 35.15  ? 154 TYR B CE2 1 
ATOM 4808 C CZ  . TYR B 1 108 ? -53.275 -3.043  142.235 1.00 31.43  ? 154 TYR B CZ  1 
ATOM 4809 O OH  . TYR B 1 108 ? -54.219 -3.439  141.318 1.00 33.73  ? 154 TYR B OH  1 
ATOM 4810 N N   . ILE B 1 109 ? -48.950 -1.723  147.976 1.00 25.80  ? 155 ILE B N   1 
ATOM 4811 C CA  . ILE B 1 109 ? -47.813 -1.416  148.839 1.00 22.57  ? 155 ILE B CA  1 
ATOM 4812 C C   . ILE B 1 109 ? -47.343 -2.670  149.563 1.00 32.68  ? 155 ILE B C   1 
ATOM 4813 O O   . ILE B 1 109 ? -46.139 -2.929  149.663 1.00 37.23  ? 155 ILE B O   1 
ATOM 4814 C CB  . ILE B 1 109 ? -48.177 -0.292  149.826 1.00 25.36  ? 155 ILE B CB  1 
ATOM 4815 C CG1 . ILE B 1 109 ? -48.001 1.075   149.168 1.00 28.93  ? 155 ILE B CG1 1 
ATOM 4816 C CG2 . ILE B 1 109 ? -47.333 -0.381  151.087 1.00 25.95  ? 155 ILE B CG2 1 
ATOM 4817 C CD1 . ILE B 1 109 ? -48.536 2.214   149.996 1.00 27.74  ? 155 ILE B CD1 1 
ATOM 4818 N N   . PHE B 1 110 ? -48.282 -3.467  150.078 1.00 29.97  ? 156 PHE B N   1 
ATOM 4819 C CA  . PHE B 1 110 ? -47.898 -4.691  150.778 1.00 22.41  ? 156 PHE B CA  1 
ATOM 4820 C C   . PHE B 1 110 ? -47.212 -5.677  149.840 1.00 20.69  ? 156 PHE B C   1 
ATOM 4821 O O   . PHE B 1 110 ? -46.220 -6.320  150.216 1.00 34.79  ? 156 PHE B O   1 
ATOM 4822 C CB  . PHE B 1 110 ? -49.121 -5.336  151.423 1.00 24.65  ? 156 PHE B CB  1 
ATOM 4823 C CG  . PHE B 1 110 ? -48.831 -6.654  152.077 1.00 31.12  ? 156 PHE B CG  1 
ATOM 4824 C CD1 . PHE B 1 110 ? -48.202 -6.705  153.307 1.00 32.73  ? 156 PHE B CD1 1 
ATOM 4825 C CD2 . PHE B 1 110 ? -49.179 -7.841  151.461 1.00 31.59  ? 156 PHE B CD2 1 
ATOM 4826 C CE1 . PHE B 1 110 ? -47.932 -7.914  153.913 1.00 26.10  ? 156 PHE B CE1 1 
ATOM 4827 C CE2 . PHE B 1 110 ? -48.909 -9.053  152.062 1.00 30.05  ? 156 PHE B CE2 1 
ATOM 4828 C CZ  . PHE B 1 110 ? -48.285 -9.088  153.290 1.00 30.25  ? 156 PHE B CZ  1 
ATOM 4829 N N   . HIS B 1 111 ? -47.735 -5.824  148.621 1.00 19.59  ? 157 HIS B N   1 
ATOM 4830 C CA  . HIS B 1 111 ? -47.100 -6.722  147.663 1.00 19.56  ? 157 HIS B CA  1 
ATOM 4831 C C   . HIS B 1 111 ? -45.699 -6.249  147.307 1.00 28.01  ? 157 HIS B C   1 
ATOM 4832 O O   . HIS B 1 111 ? -44.773 -7.059  147.210 1.00 29.95  ? 157 HIS B O   1 
ATOM 4833 C CB  . HIS B 1 111 ? -47.942 -6.850  146.399 1.00 23.07  ? 157 HIS B CB  1 
ATOM 4834 C CG  . HIS B 1 111 ? -47.204 -7.478  145.260 1.00 26.04  ? 157 HIS B CG  1 
ATOM 4835 N ND1 . HIS B 1 111 ? -46.688 -6.745  144.214 1.00 27.13  ? 157 HIS B ND1 1 
ATOM 4836 C CD2 . HIS B 1 111 ? -46.869 -8.767  145.017 1.00 27.18  ? 157 HIS B CD2 1 
ATOM 4837 C CE1 . HIS B 1 111 ? -46.080 -7.557  143.368 1.00 29.55  ? 157 HIS B CE1 1 
ATOM 4838 N NE2 . HIS B 1 111 ? -46.176 -8.789  143.832 1.00 25.85  ? 157 HIS B NE2 1 
ATOM 4839 N N   . SER B 1 112 ? -45.525 -4.942  147.098 1.00 27.26  ? 158 SER B N   1 
ATOM 4840 C CA  . SER B 1 112 ? -44.192 -4.417  146.832 1.00 24.07  ? 158 SER B CA  1 
ATOM 4841 C C   . SER B 1 112 ? -43.262 -4.650  148.012 1.00 25.24  ? 158 SER B C   1 
ATOM 4842 O O   . SER B 1 112 ? -42.085 -4.968  147.818 1.00 34.04  ? 158 SER B O   1 
ATOM 4843 C CB  . SER B 1 112 ? -44.271 -2.928  146.501 1.00 34.32  ? 158 SER B CB  1 
ATOM 4844 O OG  . SER B 1 112 ? -44.598 -2.729  145.138 1.00 39.72  ? 158 SER B OG  1 
ATOM 4845 N N   . TYR B 1 113 ? -43.776 -4.508  149.233 1.00 22.99  ? 159 TYR B N   1 
ATOM 4846 C CA  . TYR B 1 113 ? -42.975 -4.746  150.428 1.00 28.23  ? 159 TYR B CA  1 
ATOM 4847 C C   . TYR B 1 113 ? -42.462 -6.180  150.471 1.00 28.41  ? 159 TYR B C   1 
ATOM 4848 O O   . TYR B 1 113 ? -41.262 -6.417  150.653 1.00 32.16  ? 159 TYR B O   1 
ATOM 4849 C CB  . TYR B 1 113 ? -43.814 -4.434  151.666 1.00 26.23  ? 159 TYR B CB  1 
ATOM 4850 C CG  . TYR B 1 113 ? -43.128 -4.679  152.986 1.00 21.43  ? 159 TYR B CG  1 
ATOM 4851 C CD1 . TYR B 1 113 ? -41.825 -4.263  153.207 1.00 30.46  ? 159 TYR B CD1 1 
ATOM 4852 C CD2 . TYR B 1 113 ? -43.789 -5.331  154.014 1.00 18.55  ? 159 TYR B CD2 1 
ATOM 4853 C CE1 . TYR B 1 113 ? -41.205 -4.485  154.419 1.00 30.61  ? 159 TYR B CE1 1 
ATOM 4854 C CE2 . TYR B 1 113 ? -43.178 -5.557  155.225 1.00 23.24  ? 159 TYR B CE2 1 
ATOM 4855 C CZ  . TYR B 1 113 ? -41.888 -5.134  155.423 1.00 27.55  ? 159 TYR B CZ  1 
ATOM 4856 O OH  . TYR B 1 113 ? -41.278 -5.365  156.633 1.00 33.76  ? 159 TYR B OH  1 
ATOM 4857 N N   . VAL B 1 114 ? -43.359 -7.154  150.296 1.00 29.19  ? 160 VAL B N   1 
ATOM 4858 C CA  . VAL B 1 114 ? -42.920 -8.548  150.370 1.00 17.16  ? 160 VAL B CA  1 
ATOM 4859 C C   . VAL B 1 114 ? -42.026 -8.905  149.186 1.00 22.71  ? 160 VAL B C   1 
ATOM 4860 O O   . VAL B 1 114 ? -41.069 -9.677  149.335 1.00 37.29  ? 160 VAL B O   1 
ATOM 4861 C CB  . VAL B 1 114 ? -44.119 -9.509  150.489 1.00 23.64  ? 160 VAL B CB  1 
ATOM 4862 C CG1 . VAL B 1 114 ? -44.813 -9.321  151.827 1.00 27.38  ? 160 VAL B CG1 1 
ATOM 4863 C CG2 . VAL B 1 114 ? -45.092 -9.317  149.348 1.00 33.10  ? 160 VAL B CG2 1 
ATOM 4864 N N   . ARG B 1 115 ? -42.307 -8.361  147.999 1.00 25.06  ? 161 ARG B N   1 
ATOM 4865 C CA  . ARG B 1 115 ? -41.448 -8.624  146.849 1.00 23.24  ? 161 ARG B CA  1 
ATOM 4866 C C   . ARG B 1 115 ? -40.045 -8.081  147.073 1.00 33.83  ? 161 ARG B C   1 
ATOM 4867 O O   . ARG B 1 115 ? -39.058 -8.738  146.724 1.00 36.62  ? 161 ARG B O   1 
ATOM 4868 C CB  . ARG B 1 115 ? -42.059 -8.020  145.587 1.00 28.58  ? 161 ARG B CB  1 
ATOM 4869 C CG  . ARG B 1 115 ? -41.482 -8.570  144.300 1.00 31.24  ? 161 ARG B CG  1 
ATOM 4870 C CD  . ARG B 1 115 ? -41.949 -7.766  143.101 1.00 36.44  ? 161 ARG B CD  1 
ATOM 4871 N NE  . ARG B 1 115 ? -40.936 -6.823  142.645 1.00 35.38  ? 161 ARG B NE  1 
ATOM 4872 C CZ  . ARG B 1 115 ? -40.020 -7.094  141.726 1.00 37.53  ? 161 ARG B CZ  1 
ATOM 4873 N NH1 . ARG B 1 115 ? -39.961 -8.277  141.138 1.00 39.11  ? 161 ARG B NH1 1 
ATOM 4874 N NH2 . ARG B 1 115 ? -39.143 -6.155  141.388 1.00 37.16  ? 161 ARG B NH2 1 
ATOM 4875 N N   . LYS B 1 116 ? -39.933 -6.883  147.648 1.00 38.03  ? 162 LYS B N   1 
ATOM 4876 C CA  . LYS B 1 116 ? -38.620 -6.339  147.966 1.00 30.20  ? 162 LYS B CA  1 
ATOM 4877 C C   . LYS B 1 116 ? -37.930 -7.170  149.036 1.00 29.31  ? 162 LYS B C   1 
ATOM 4878 O O   . LYS B 1 116 ? -36.715 -7.376  148.977 1.00 40.13  ? 162 LYS B O   1 
ATOM 4879 C CB  . LYS B 1 116 ? -38.745 -4.885  148.415 1.00 32.96  ? 162 LYS B CB  1 
ATOM 4880 C CG  . LYS B 1 116 ? -37.427 -4.135  148.446 1.00 34.77  ? 162 LYS B CG  1 
ATOM 4881 C CD  . LYS B 1 116 ? -37.625 -2.715  148.935 1.00 38.37  ? 162 LYS B CD  1 
ATOM 4882 C CE  . LYS B 1 116 ? -38.223 -2.702  150.329 1.00 43.07  ? 162 LYS B CE  1 
ATOM 4883 N NZ  . LYS B 1 116 ? -38.653 -1.339  150.734 1.00 44.67  ? 162 LYS B NZ  1 
ATOM 4884 N N   . ILE B 1 117 ? -38.687 -7.657  150.021 1.00 31.60  ? 163 ILE B N   1 
ATOM 4885 C CA  . ILE B 1 117 ? -38.104 -8.531  151.036 1.00 31.56  ? 163 ILE B CA  1 
ATOM 4886 C C   . ILE B 1 117 ? -37.488 -9.758  150.382 1.00 29.49  ? 163 ILE B C   1 
ATOM 4887 O O   . ILE B 1 117 ? -36.371 -10.169 150.718 1.00 39.02  ? 163 ILE B O   1 
ATOM 4888 C CB  . ILE B 1 117 ? -39.166 -8.925  152.077 1.00 30.06  ? 163 ILE B CB  1 
ATOM 4889 C CG1 . ILE B 1 117 ? -39.461 -7.752  153.006 1.00 36.54  ? 163 ILE B CG1 1 
ATOM 4890 C CG2 . ILE B 1 117 ? -38.709 -10.130 152.877 1.00 21.97  ? 163 ILE B CG2 1 
ATOM 4891 C CD1 . ILE B 1 117 ? -40.674 -7.966  153.859 1.00 39.45  ? 163 ILE B CD1 1 
ATOM 4892 N N   . LEU B 1 118 ? -38.206 -10.361 149.435 1.00 36.61  ? 164 LEU B N   1 
ATOM 4893 C CA  . LEU B 1 118 ? -37.678 -11.534 148.745 1.00 34.12  ? 164 LEU B CA  1 
ATOM 4894 C C   . LEU B 1 118 ? -36.466 -11.184 147.888 1.00 32.06  ? 164 LEU B C   1 
ATOM 4895 O O   . LEU B 1 118 ? -35.471 -11.917 147.886 1.00 37.15  ? 164 LEU B O   1 
ATOM 4896 C CB  . LEU B 1 118 ? -38.768 -12.175 147.891 1.00 39.85  ? 164 LEU B CB  1 
ATOM 4897 C CG  . LEU B 1 118 ? -38.360 -13.440 147.139 1.00 38.04  ? 164 LEU B CG  1 
ATOM 4898 C CD1 . LEU B 1 118 ? -38.224 -14.611 148.094 1.00 41.37  ? 164 LEU B CD1 1 
ATOM 4899 C CD2 . LEU B 1 118 ? -39.359 -13.752 146.044 1.00 38.24  ? 164 LEU B CD2 1 
ATOM 4900 N N   . ALA B 1 119 ? -36.525 -10.069 147.157 1.00 34.34  ? 165 ALA B N   1 
ATOM 4901 C CA  . ALA B 1 119 ? -35.473 -9.745  146.199 1.00 41.14  ? 165 ALA B CA  1 
ATOM 4902 C C   . ALA B 1 119 ? -34.194 -9.252  146.864 1.00 44.40  ? 165 ALA B C   1 
ATOM 4903 O O   . ALA B 1 119 ? -33.111 -9.430  146.298 1.00 39.81  ? 165 ALA B O   1 
ATOM 4904 C CB  . ALA B 1 119 ? -35.974 -8.697  145.206 1.00 31.50  ? 165 ALA B CB  1 
ATOM 4905 N N   . ILE B 1 120 ? -34.292 -8.632  148.040 1.00 43.89  ? 166 ILE B N   1 
ATOM 4906 C CA  . ILE B 1 120 ? -33.103 -8.141  148.728 1.00 32.60  ? 166 ILE B CA  1 
ATOM 4907 C C   . ILE B 1 120 ? -32.221 -9.298  149.178 1.00 41.03  ? 166 ILE B C   1 
ATOM 4908 O O   . ILE B 1 120 ? -30.989 -9.211  149.130 1.00 50.61  ? 166 ILE B O   1 
ATOM 4909 C CB  . ILE B 1 120 ? -33.515 -7.242  149.908 1.00 30.38  ? 166 ILE B CB  1 
ATOM 4910 C CG1 . ILE B 1 120 ? -34.062 -5.907  149.399 1.00 38.81  ? 166 ILE B CG1 1 
ATOM 4911 C CG2 . ILE B 1 120 ? -32.357 -7.036  150.855 1.00 38.28  ? 166 ILE B CG2 1 
ATOM 4912 C CD1 . ILE B 1 120 ? -34.072 -4.811  150.436 1.00 41.93  ? 166 ILE B CD1 1 
ATOM 4913 N N   . SER B 1 121 ? -32.832 -10.410 149.586 1.00 34.57  ? 167 SER B N   1 
ATOM 4914 C CA  . SER B 1 121 ? -32.092 -11.517 150.180 1.00 37.58  ? 167 SER B CA  1 
ATOM 4915 C C   . SER B 1 121 ? -31.087 -12.149 149.226 1.00 43.75  ? 167 SER B C   1 
ATOM 4916 O O   . SER B 1 121 ? -30.221 -12.903 149.680 1.00 48.15  ? 167 SER B O   1 
ATOM 4917 C CB  . SER B 1 121 ? -33.066 -12.582 150.683 1.00 37.98  ? 167 SER B CB  1 
ATOM 4918 O OG  . SER B 1 121 ? -33.876 -13.064 149.628 1.00 43.73  ? 167 SER B OG  1 
ATOM 4919 N N   . LYS B 1 122 ? -31.177 -11.867 147.927 1.00 45.58  ? 168 LYS B N   1 
ATOM 4920 C CA  . LYS B 1 122 ? -30.257 -12.416 146.942 1.00 44.14  ? 168 LYS B CA  1 
ATOM 4921 C C   . LYS B 1 122 ? -29.125 -11.454 146.596 1.00 45.69  ? 168 LYS B C   1 
ATOM 4922 O O   . LYS B 1 122 ? -28.405 -11.683 145.620 1.00 52.86  ? 168 LYS B O   1 
ATOM 4923 C CB  . LYS B 1 122 ? -31.019 -12.809 145.677 1.00 46.39  ? 168 LYS B CB  1 
ATOM 4924 C CG  . LYS B 1 122 ? -32.038 -13.914 145.892 1.00 47.80  ? 168 LYS B CG  1 
ATOM 4925 C CD  . LYS B 1 122 ? -33.292 -13.671 145.074 1.00 47.58  ? 168 LYS B CD  1 
ATOM 4926 C CE  . LYS B 1 122 ? -32.981 -13.656 143.588 1.00 50.99  ? 168 LYS B CE  1 
ATOM 4927 N NZ  . LYS B 1 122 ? -32.666 -15.015 143.072 1.00 58.25  ? 168 LYS B NZ  1 
ATOM 4928 N N   . LEU B 1 123 ? -28.944 -10.395 147.381 1.00 40.04  ? 169 LEU B N   1 
ATOM 4929 C CA  . LEU B 1 123 ? -27.917 -9.392  147.126 1.00 40.65  ? 169 LEU B CA  1 
ATOM 4930 C C   . LEU B 1 123 ? -26.678 -9.713  147.949 1.00 41.98  ? 169 LEU B C   1 
ATOM 4931 O O   . LEU B 1 123 ? -26.770 -9.917  149.164 1.00 45.30  ? 169 LEU B O   1 
ATOM 4932 C CB  . LEU B 1 123 ? -28.426 -7.991  147.462 1.00 38.25  ? 169 LEU B CB  1 
ATOM 4933 C CG  . LEU B 1 123 ? -29.197 -7.257  146.368 1.00 42.31  ? 169 LEU B CG  1 
ATOM 4934 C CD1 . LEU B 1 123 ? -29.480 -5.828  146.790 1.00 41.19  ? 169 LEU B CD1 1 
ATOM 4935 C CD2 . LEU B 1 123 ? -28.413 -7.287  145.071 1.00 44.23  ? 169 LEU B CD2 1 
ATOM 4936 N N   . TYR B 1 124 ? -25.523 -9.755  147.288 1.00 38.96  ? 170 TYR B N   1 
ATOM 4937 C CA  . TYR B 1 124 ? -24.249 -9.975  147.962 1.00 38.15  ? 170 TYR B CA  1 
ATOM 4938 C C   . TYR B 1 124 ? -23.157 -9.275  147.172 1.00 39.32  ? 170 TYR B C   1 
ATOM 4939 O O   . TYR B 1 124 ? -23.073 -9.435  145.952 1.00 41.74  ? 170 TYR B O   1 
ATOM 4940 C CB  . TYR B 1 124 ? -23.941 -11.472 148.107 1.00 41.91  ? 170 TYR B CB  1 
ATOM 4941 C CG  . TYR B 1 124 ? -22.464 -11.809 148.212 1.00 42.88  ? 170 TYR B CG  1 
ATOM 4942 C CD1 . TYR B 1 124 ? -21.685 -12.006 147.076 1.00 39.72  ? 170 TYR B CD1 1 
ATOM 4943 C CD2 . TYR B 1 124 ? -21.862 -11.976 149.451 1.00 42.73  ? 170 TYR B CD2 1 
ATOM 4944 C CE1 . TYR B 1 124 ? -20.346 -12.319 147.175 1.00 42.72  ? 170 TYR B CE1 1 
ATOM 4945 C CE2 . TYR B 1 124 ? -20.522 -12.291 149.558 1.00 42.41  ? 170 TYR B CE2 1 
ATOM 4946 C CZ  . TYR B 1 124 ? -19.770 -12.461 148.418 1.00 45.35  ? 170 TYR B CZ  1 
ATOM 4947 O OH  . TYR B 1 124 ? -18.437 -12.778 148.520 1.00 48.08  ? 170 TYR B OH  1 
ATOM 4948 N N   . THR B 1 125 ? -22.330 -8.503  147.866 1.00 42.35  ? 171 THR B N   1 
ATOM 4949 C CA  . THR B 1 125 ? -21.139 -7.901  147.295 1.00 45.67  ? 171 THR B CA  1 
ATOM 4950 C C   . THR B 1 125 ? -20.001 -7.986  148.300 1.00 44.03  ? 171 THR B C   1 
ATOM 4951 O O   . THR B 1 125 ? -20.230 -7.904  149.511 1.00 44.36  ? 171 THR B O   1 
ATOM 4952 C CB  . THR B 1 125 ? -21.394 -6.439  146.893 1.00 42.66  ? 171 THR B CB  1 
ATOM 4953 O OG1 . THR B 1 125 ? -20.224 -5.889  146.275 1.00 43.69  ? 171 THR B OG1 1 
ATOM 4954 C CG2 . THR B 1 125 ? -21.782 -5.602  148.094 1.00 41.96  ? 171 THR B CG2 1 
ATOM 4955 N N   . PRO B 1 126 ? -18.764 -8.177  147.830 1.00 33.64  ? 172 PRO B N   1 
ATOM 4956 C CA  . PRO B 1 126 ? -17.644 -8.341  148.770 1.00 34.12  ? 172 PRO B CA  1 
ATOM 4957 C C   . PRO B 1 126 ? -17.264 -7.075  149.515 1.00 43.03  ? 172 PRO B C   1 
ATOM 4958 O O   . PRO B 1 126 ? -16.611 -7.173  150.563 1.00 42.06  ? 172 PRO B O   1 
ATOM 4959 C CB  . PRO B 1 126 ? -16.489 -8.811  147.869 1.00 34.21  ? 172 PRO B CB  1 
ATOM 4960 C CG  . PRO B 1 126 ? -17.130 -9.215  146.575 1.00 35.06  ? 172 PRO B CG  1 
ATOM 4961 C CD  . PRO B 1 126 ? -18.332 -8.349  146.436 1.00 34.78  ? 172 PRO B CD  1 
ATOM 4962 N N   . VAL B 1 127 ? -17.644 -5.896  149.017 1.00 41.07  ? 173 VAL B N   1 
ATOM 4963 C CA  . VAL B 1 127 ? -17.228 -4.645  149.647 1.00 31.78  ? 173 VAL B CA  1 
ATOM 4964 C C   . VAL B 1 127 ? -18.251 -4.101  150.627 1.00 36.65  ? 173 VAL B C   1 
ATOM 4965 O O   . VAL B 1 127 ? -17.997 -3.067  151.255 1.00 41.01  ? 173 VAL B O   1 
ATOM 4966 C CB  . VAL B 1 127 ? -16.934 -3.572  148.584 1.00 25.32  ? 173 VAL B CB  1 
ATOM 4967 C CG1 . VAL B 1 127 ? -15.935 -4.097  147.572 1.00 29.43  ? 173 VAL B CG1 1 
ATOM 4968 C CG2 . VAL B 1 127 ? -18.215 -3.150  147.897 1.00 34.07  ? 173 VAL B CG2 1 
ATOM 4969 N N   . ASN B 1 128 ? -19.398 -4.758  150.774 1.00 32.35  ? 174 ASN B N   1 
ATOM 4970 C CA  . ASN B 1 128 ? -20.441 -4.312  151.691 1.00 25.43  ? 174 ASN B CA  1 
ATOM 4971 C C   . ASN B 1 128 ? -21.017 -5.525  152.402 1.00 34.21  ? 174 ASN B C   1 
ATOM 4972 O O   . ASN B 1 128 ? -21.761 -6.302  151.798 1.00 42.93  ? 174 ASN B O   1 
ATOM 4973 C CB  . ASN B 1 128 ? -21.542 -3.552  150.947 1.00 26.52  ? 174 ASN B CB  1 
ATOM 4974 C CG  . ASN B 1 128 ? -22.279 -2.577  151.835 1.00 36.94  ? 174 ASN B CG  1 
ATOM 4975 O OD1 . ASN B 1 128 ? -22.502 -2.842  153.015 1.00 40.30  ? 174 ASN B OD1 1 
ATOM 4976 N ND2 . ASN B 1 128 ? -22.668 -1.441  151.270 1.00 38.92  ? 174 ASN B ND2 1 
ATOM 4977 N N   . LYS B 1 129 ? -20.678 -5.682  153.681 1.00 31.76  ? 175 LYS B N   1 
ATOM 4978 C CA  . LYS B 1 129 ? -21.186 -6.797  154.471 1.00 38.94  ? 175 LYS B CA  1 
ATOM 4979 C C   . LYS B 1 129 ? -22.603 -6.570  154.976 1.00 40.45  ? 175 LYS B C   1 
ATOM 4980 O O   . LYS B 1 129 ? -23.172 -7.471  155.601 1.00 39.05  ? 175 LYS B O   1 
ATOM 4981 C CB  . LYS B 1 129 ? -20.257 -7.074  155.655 1.00 34.58  ? 175 LYS B CB  1 
ATOM 4982 C CG  . LYS B 1 129 ? -18.783 -6.920  155.337 1.00 40.57  ? 175 LYS B CG  1 
ATOM 4983 C CD  . LYS B 1 129 ? -18.380 -7.857  154.210 1.00 42.02  ? 175 LYS B CD  1 
ATOM 4984 C CE  . LYS B 1 129 ? -16.889 -8.119  154.213 1.00 41.68  ? 175 LYS B CE  1 
ATOM 4985 N NZ  . LYS B 1 129 ? -16.537 -9.337  154.993 1.00 35.15  ? 175 LYS B NZ  1 
ATOM 4986 N N   . TYR B 1 130 ? -23.180 -5.394  154.732 1.00 35.57  ? 176 TYR B N   1 
ATOM 4987 C CA  . TYR B 1 130 ? -24.564 -5.148  155.113 1.00 30.38  ? 176 TYR B CA  1 
ATOM 4988 C C   . TYR B 1 130 ? -25.546 -5.841  154.179 1.00 34.76  ? 176 TYR B C   1 
ATOM 4989 O O   . TYR B 1 130 ? -26.748 -5.851  154.460 1.00 41.21  ? 176 TYR B O   1 
ATOM 4990 C CB  . TYR B 1 130 ? -24.831 -3.645  155.141 1.00 24.98  ? 176 TYR B CB  1 
ATOM 4991 C CG  . TYR B 1 130 ? -24.185 -2.938  156.309 1.00 27.66  ? 176 TYR B CG  1 
ATOM 4992 C CD1 . TYR B 1 130 ? -24.560 -3.222  157.612 1.00 28.23  ? 176 TYR B CD1 1 
ATOM 4993 C CD2 . TYR B 1 130 ? -23.186 -2.000  156.107 1.00 32.09  ? 176 TYR B CD2 1 
ATOM 4994 C CE1 . TYR B 1 130 ? -23.969 -2.583  158.680 1.00 29.66  ? 176 TYR B CE1 1 
ATOM 4995 C CE2 . TYR B 1 130 ? -22.590 -1.355  157.168 1.00 32.49  ? 176 TYR B CE2 1 
ATOM 4996 C CZ  . TYR B 1 130 ? -22.984 -1.651  158.452 1.00 35.40  ? 176 TYR B CZ  1 
ATOM 4997 O OH  . TYR B 1 130 ? -22.389 -1.010  159.512 1.00 42.84  ? 176 TYR B OH  1 
ATOM 4998 N N   . PHE B 1 131 ? -25.064 -6.408  153.080 1.00 34.60  ? 177 PHE B N   1 
ATOM 4999 C CA  . PHE B 1 131 ? -25.930 -7.077  152.118 1.00 30.58  ? 177 PHE B CA  1 
ATOM 5000 C C   . PHE B 1 131 ? -25.958 -8.573  152.401 1.00 34.02  ? 177 PHE B C   1 
ATOM 5001 O O   . PHE B 1 131 ? -24.896 -9.204  152.435 1.00 42.54  ? 177 PHE B O   1 
ATOM 5002 C CB  . PHE B 1 131 ? -25.440 -6.839  150.697 1.00 30.40  ? 177 PHE B CB  1 
ATOM 5003 C CG  . PHE B 1 131 ? -25.742 -5.469  150.161 1.00 33.16  ? 177 PHE B CG  1 
ATOM 5004 C CD1 . PHE B 1 131 ? -26.028 -4.416  151.009 1.00 33.55  ? 177 PHE B CD1 1 
ATOM 5005 C CD2 . PHE B 1 131 ? -25.725 -5.235  148.799 1.00 39.32  ? 177 PHE B CD2 1 
ATOM 5006 C CE1 . PHE B 1 131 ? -26.295 -3.161  150.509 1.00 35.47  ? 177 PHE B CE1 1 
ATOM 5007 C CE2 . PHE B 1 131 ? -25.993 -3.983  148.295 1.00 35.28  ? 177 PHE B CE2 1 
ATOM 5008 C CZ  . PHE B 1 131 ? -26.278 -2.946  149.150 1.00 37.03  ? 177 PHE B CZ  1 
ATOM 5009 N N   . PRO B 1 132 ? -27.130 -9.178  152.609 1.00 32.78  ? 178 PRO B N   1 
ATOM 5010 C CA  . PRO B 1 132 ? -28.450 -8.563  152.710 1.00 34.64  ? 178 PRO B CA  1 
ATOM 5011 C C   . PRO B 1 132 ? -29.015 -8.649  154.119 1.00 33.06  ? 178 PRO B C   1 
ATOM 5012 O O   . PRO B 1 132 ? -30.172 -8.310  154.350 1.00 38.40  ? 178 PRO B O   1 
ATOM 5013 C CB  . PRO B 1 132 ? -29.264 -9.397  151.725 1.00 34.25  ? 178 PRO B CB  1 
ATOM 5014 C CG  . PRO B 1 132 ? -28.676 -10.796 151.870 1.00 36.87  ? 178 PRO B CG  1 
ATOM 5015 C CD  . PRO B 1 132 ? -27.256 -10.629 152.394 1.00 33.63  ? 178 PRO B CD  1 
ATOM 5016 N N   . ARG B 1 133 ? -28.212 -9.117  155.075 1.00 32.56  ? 179 ARG B N   1 
ATOM 5017 C CA  . ARG B 1 133 ? -28.718 -9.362  156.420 1.00 33.78  ? 179 ARG B CA  1 
ATOM 5018 C C   . ARG B 1 133 ? -29.184 -8.073  157.084 1.00 34.89  ? 179 ARG B C   1 
ATOM 5019 O O   . ARG B 1 133 ? -30.250 -8.043  157.708 1.00 43.77  ? 179 ARG B O   1 
ATOM 5020 C CB  . ARG B 1 133 ? -27.641 -10.045 157.261 1.00 34.81  ? 179 ARG B CB  1 
ATOM 5021 C CG  . ARG B 1 133 ? -27.574 -11.550 157.071 1.00 34.85  ? 179 ARG B CG  1 
ATOM 5022 C CD  . ARG B 1 133 ? -26.877 -12.219 158.237 1.00 31.27  ? 179 ARG B CD  1 
ATOM 5023 N NE  . ARG B 1 133 ? -27.813 -12.587 159.291 1.00 38.49  ? 179 ARG B NE  1 
ATOM 5024 C CZ  . ARG B 1 133 ? -27.996 -11.888 160.402 1.00 42.83  ? 179 ARG B CZ  1 
ATOM 5025 N NH1 . ARG B 1 133 ? -27.328 -10.771 160.633 1.00 37.06  ? 179 ARG B NH1 1 
ATOM 5026 N NH2 . ARG B 1 133 ? -28.872 -12.321 161.304 1.00 45.81  ? 179 ARG B NH2 1 
ATOM 5027 N N   . ALA B 1 134 ? -28.407 -6.997  156.954 1.00 29.89  ? 180 ALA B N   1 
ATOM 5028 C CA  . ALA B 1 134 ? -28.803 -5.725  157.549 1.00 31.64  ? 180 ALA B CA  1 
ATOM 5029 C C   . ALA B 1 134 ? -30.063 -5.176  156.896 1.00 36.92  ? 180 ALA B C   1 
ATOM 5030 O O   . ALA B 1 134 ? -30.939 -4.636  157.580 1.00 45.10  ? 180 ALA B O   1 
ATOM 5031 C CB  . ALA B 1 134 ? -27.665 -4.715  157.441 1.00 36.15  ? 180 ALA B CB  1 
ATOM 5032 N N   . LEU B 1 135 ? -30.166 -5.292  155.571 1.00 37.59  ? 181 LEU B N   1 
ATOM 5033 C CA  . LEU B 1 135 ? -31.351 -4.803  154.875 1.00 31.04  ? 181 LEU B CA  1 
ATOM 5034 C C   . LEU B 1 135 ? -32.594 -5.573  155.300 1.00 33.07  ? 181 LEU B C   1 
ATOM 5035 O O   . LEU B 1 135 ? -33.650 -4.977  155.541 1.00 37.08  ? 181 LEU B O   1 
ATOM 5036 C CB  . LEU B 1 135 ? -31.140 -4.898  153.365 1.00 27.85  ? 181 LEU B CB  1 
ATOM 5037 C CG  . LEU B 1 135 ? -30.501 -3.715  152.630 1.00 30.37  ? 181 LEU B CG  1 
ATOM 5038 C CD1 . LEU B 1 135 ? -29.228 -3.244  153.310 1.00 35.94  ? 181 LEU B CD1 1 
ATOM 5039 C CD2 . LEU B 1 135 ? -30.208 -4.095  151.192 1.00 31.72  ? 181 LEU B CD2 1 
ATOM 5040 N N   . LEU B 1 136 ? -32.485 -6.899  155.412 1.00 40.44  ? 182 LEU B N   1 
ATOM 5041 C CA  . LEU B 1 136 ? -33.610 -7.696  155.889 1.00 32.15  ? 182 LEU B CA  1 
ATOM 5042 C C   . LEU B 1 136 ? -33.968 -7.358  157.330 1.00 29.30  ? 182 LEU B C   1 
ATOM 5043 O O   . LEU B 1 136 ? -35.153 -7.286  157.673 1.00 39.55  ? 182 LEU B O   1 
ATOM 5044 C CB  . LEU B 1 136 ? -33.291 -9.184  155.755 1.00 31.32  ? 182 LEU B CB  1 
ATOM 5045 C CG  . LEU B 1 136 ? -33.088 -9.704  154.332 1.00 25.96  ? 182 LEU B CG  1 
ATOM 5046 C CD1 . LEU B 1 136 ? -32.873 -11.206 154.340 1.00 35.19  ? 182 LEU B CD1 1 
ATOM 5047 C CD2 . LEU B 1 136 ? -34.262 -9.333  153.447 1.00 27.00  ? 182 LEU B CD2 1 
ATOM 5048 N N   . VAL B 1 137 ? -32.964 -7.147  158.184 1.00 24.82  ? 183 VAL B N   1 
ATOM 5049 C CA  . VAL B 1 137 ? -33.228 -6.783  159.572 1.00 25.78  ? 183 VAL B CA  1 
ATOM 5050 C C   . VAL B 1 137 ? -33.964 -5.451  159.641 1.00 29.52  ? 183 VAL B C   1 
ATOM 5051 O O   . VAL B 1 137 ? -34.904 -5.283  160.427 1.00 34.57  ? 183 VAL B O   1 
ATOM 5052 C CB  . VAL B 1 137 ? -31.909 -6.753  160.366 1.00 21.94  ? 183 VAL B CB  1 
ATOM 5053 C CG1 . VAL B 1 137 ? -32.006 -5.798  161.539 1.00 25.08  ? 183 VAL B CG1 1 
ATOM 5054 C CG2 . VAL B 1 137 ? -31.545 -8.149  160.839 1.00 30.59  ? 183 VAL B CG2 1 
ATOM 5055 N N   . ALA B 1 138 ? -33.549 -4.483  158.821 1.00 30.73  ? 184 ALA B N   1 
ATOM 5056 C CA  . ALA B 1 138 ? -34.250 -3.205  158.763 1.00 30.59  ? 184 ALA B CA  1 
ATOM 5057 C C   . ALA B 1 138 ? -35.679 -3.380  158.270 1.00 35.38  ? 184 ALA B C   1 
ATOM 5058 O O   . ALA B 1 138 ? -36.604 -2.748  158.793 1.00 38.78  ? 184 ALA B O   1 
ATOM 5059 C CB  . ALA B 1 138 ? -33.490 -2.230  157.865 1.00 27.55  ? 184 ALA B CB  1 
ATOM 5060 N N   . LEU B 1 139 ? -35.881 -4.233  157.263 1.00 38.21  ? 185 LEU B N   1 
ATOM 5061 C CA  . LEU B 1 139 ? -37.230 -4.488  156.771 1.00 31.12  ? 185 LEU B CA  1 
ATOM 5062 C C   . LEU B 1 139 ? -38.081 -5.214  157.805 1.00 29.03  ? 185 LEU B C   1 
ATOM 5063 O O   . LEU B 1 139 ? -39.312 -5.189  157.719 1.00 40.21  ? 185 LEU B O   1 
ATOM 5064 C CB  . LEU B 1 139 ? -37.176 -5.291  155.474 1.00 28.12  ? 185 LEU B CB  1 
ATOM 5065 C CG  . LEU B 1 139 ? -36.803 -4.489  154.230 1.00 31.02  ? 185 LEU B CG  1 
ATOM 5066 C CD1 . LEU B 1 139 ? -36.694 -5.398  153.022 1.00 36.07  ? 185 LEU B CD1 1 
ATOM 5067 C CD2 . LEU B 1 139 ? -37.815 -3.386  153.988 1.00 34.39  ? 185 LEU B CD2 1 
ATOM 5068 N N   . GLY B 1 140 ? -37.453 -5.867  158.773 1.00 29.94  ? 186 GLY B N   1 
ATOM 5069 C CA  . GLY B 1 140 ? -38.165 -6.510  159.849 1.00 29.11  ? 186 GLY B CA  1 
ATOM 5070 C C   . GLY B 1 140 ? -38.497 -7.969  159.644 1.00 32.42  ? 186 GLY B C   1 
ATOM 5071 O O   . GLY B 1 140 ? -39.543 -8.418  160.124 1.00 45.99  ? 186 GLY B O   1 
ATOM 5072 N N   . VAL B 1 141 ? -37.648 -8.722  158.949 1.00 32.27  ? 187 VAL B N   1 
ATOM 5073 C CA  . VAL B 1 141 ? -37.886 -10.144 158.729 1.00 34.61  ? 187 VAL B CA  1 
ATOM 5074 C C   . VAL B 1 141 ? -36.758 -10.943 159.362 1.00 45.39  ? 187 VAL B C   1 
ATOM 5075 O O   . VAL B 1 141 ? -35.835 -10.377 159.956 1.00 49.16  ? 187 VAL B O   1 
ATOM 5076 C CB  . VAL B 1 141 ? -38.012 -10.470 157.231 1.00 33.20  ? 187 VAL B CB  1 
ATOM 5077 C CG1 . VAL B 1 141 ? -39.041 -9.578  156.586 1.00 43.86  ? 187 VAL B CG1 1 
ATOM 5078 C CG2 . VAL B 1 141 ? -36.671 -10.315 156.541 1.00 33.35  ? 187 VAL B CG2 1 
ATOM 5079 N N   . ASP B 1 142 ? -36.832 -12.267 159.245 1.00 49.88  ? 188 ASP B N   1 
ATOM 5080 C CA  . ASP B 1 142 ? -35.777 -13.137 159.735 1.00 47.89  ? 188 ASP B CA  1 
ATOM 5081 C C   . ASP B 1 142 ? -34.983 -13.657 158.549 1.00 53.53  ? 188 ASP B C   1 
ATOM 5082 O O   . ASP B 1 142 ? -35.513 -14.464 157.767 1.00 62.49  ? 188 ASP B O   1 
ATOM 5083 C CB  . ASP B 1 142 ? -36.365 -14.295 160.536 1.00 51.87  ? 188 ASP B CB  1 
ATOM 5084 C CG  . ASP B 1 142 ? -35.400 -14.838 161.567 1.00 57.15  ? 188 ASP B CG  1 
ATOM 5085 O OD1 . ASP B 1 142 ? -34.422 -14.136 161.893 1.00 57.84  ? 188 ASP B OD1 1 
ATOM 5086 O OD2 . ASP B 1 142 ? -35.622 -15.966 162.053 1.00 54.18  ? 188 ASP B OD2 1 
ATOM 5087 N N   . PRO B 1 143 ? -33.735 -13.221 158.357 1.00 44.31  ? 189 PRO B N   1 
ATOM 5088 C CA  . PRO B 1 143 ? -32.952 -13.729 157.220 1.00 45.18  ? 189 PRO B CA  1 
ATOM 5089 C C   . PRO B 1 143 ? -32.782 -15.234 157.246 1.00 47.06  ? 189 PRO B C   1 
ATOM 5090 O O   . PRO B 1 143 ? -32.777 -15.870 156.183 1.00 50.82  ? 189 PRO B O   1 
ATOM 5091 C CB  . PRO B 1 143 ? -31.607 -13.003 157.366 1.00 48.73  ? 189 PRO B CB  1 
ATOM 5092 C CG  . PRO B 1 143 ? -31.886 -11.834 158.258 1.00 42.21  ? 189 PRO B CG  1 
ATOM 5093 C CD  . PRO B 1 143 ? -32.970 -12.274 159.182 1.00 40.76  ? 189 PRO B CD  1 
ATOM 5094 N N   . GLU B 1 144 ? -32.651 -15.825 158.434 1.00 46.50  ? 190 GLU B N   1 
ATOM 5095 C CA  . GLU B 1 144 ? -32.600 -17.278 158.531 1.00 47.55  ? 190 GLU B CA  1 
ATOM 5096 C C   . GLU B 1 144 ? -33.880 -17.902 157.996 1.00 55.97  ? 190 GLU B C   1 
ATOM 5097 O O   . GLU B 1 144 ? -33.832 -18.896 157.264 1.00 61.22  ? 190 GLU B O   1 
ATOM 5098 C CB  . GLU B 1 144 ? -32.364 -17.697 159.981 1.00 51.22  ? 190 GLU B CB  1 
ATOM 5099 C CG  . GLU B 1 144 ? -31.063 -17.182 160.569 1.00 56.83  ? 190 GLU B CG  1 
ATOM 5100 C CD  . GLU B 1 144 ? -31.226 -15.839 161.251 1.00 58.46  ? 190 GLU B CD  1 
ATOM 5101 O OE1 . GLU B 1 144 ? -31.807 -15.795 162.355 1.00 57.42  ? 190 GLU B OE1 1 
ATOM 5102 O OE2 . GLU B 1 144 ? -30.769 -14.826 160.682 1.00 55.40  ? 190 GLU B OE2 1 
ATOM 5103 N N   . ASP B 1 145 ? -35.032 -17.322 158.341 1.00 51.13  ? 191 ASP B N   1 
ATOM 5104 C CA  . ASP B 1 145 ? -36.299 -17.836 157.835 1.00 45.91  ? 191 ASP B CA  1 
ATOM 5105 C C   . ASP B 1 145 ? -36.381 -17.713 156.320 1.00 43.71  ? 191 ASP B C   1 
ATOM 5106 O O   . ASP B 1 145 ? -36.846 -18.637 155.642 1.00 53.09  ? 191 ASP B O   1 
ATOM 5107 C CB  . ASP B 1 145 ? -37.463 -17.099 158.493 1.00 46.94  ? 191 ASP B CB  1 
ATOM 5108 C CG  . ASP B 1 145 ? -38.794 -17.430 157.856 1.00 56.38  ? 191 ASP B CG  1 
ATOM 5109 O OD1 . ASP B 1 145 ? -39.389 -18.464 158.225 1.00 58.88  ? 191 ASP B OD1 1 
ATOM 5110 O OD2 . ASP B 1 145 ? -39.244 -16.661 156.982 1.00 54.85  ? 191 ASP B OD2 1 
ATOM 5111 N N   . VAL B 1 146 ? -35.935 -16.581 155.772 1.00 33.67  ? 192 VAL B N   1 
ATOM 5112 C CA  . VAL B 1 146 ? -35.975 -16.400 154.324 1.00 36.64  ? 192 VAL B CA  1 
ATOM 5113 C C   . VAL B 1 146 ? -35.093 -17.429 153.628 1.00 41.53  ? 192 VAL B C   1 
ATOM 5114 O O   . VAL B 1 146 ? -35.504 -18.060 152.646 1.00 45.64  ? 192 VAL B O   1 
ATOM 5115 C CB  . VAL B 1 146 ? -35.571 -14.963 153.949 1.00 35.57  ? 192 VAL B CB  1 
ATOM 5116 C CG1 . VAL B 1 146 ? -35.695 -14.756 152.453 1.00 33.95  ? 192 VAL B CG1 1 
ATOM 5117 C CG2 . VAL B 1 146 ? -36.431 -13.961 154.694 1.00 38.68  ? 192 VAL B CG2 1 
ATOM 5118 N N   . PHE B 1 147 ? -33.873 -17.627 154.125 1.00 41.06  ? 193 PHE B N   1 
ATOM 5119 C CA  . PHE B 1 147 ? -32.971 -18.566 153.467 1.00 42.98  ? 193 PHE B CA  1 
ATOM 5120 C C   . PHE B 1 147 ? -33.413 -20.010 153.670 1.00 45.91  ? 193 PHE B C   1 
ATOM 5121 O O   . PHE B 1 147 ? -33.101 -20.872 152.842 1.00 46.41  ? 193 PHE B O   1 
ATOM 5122 C CB  . PHE B 1 147 ? -31.543 -18.359 153.966 1.00 41.91  ? 193 PHE B CB  1 
ATOM 5123 C CG  . PHE B 1 147 ? -31.012 -16.980 153.708 1.00 44.83  ? 193 PHE B CG  1 
ATOM 5124 C CD1 . PHE B 1 147 ? -31.319 -16.318 152.532 1.00 39.11  ? 193 PHE B CD1 1 
ATOM 5125 C CD2 . PHE B 1 147 ? -30.205 -16.347 154.636 1.00 48.81  ? 193 PHE B CD2 1 
ATOM 5126 C CE1 . PHE B 1 147 ? -30.835 -15.050 152.288 1.00 38.50  ? 193 PHE B CE1 1 
ATOM 5127 C CE2 . PHE B 1 147 ? -29.719 -15.077 154.398 1.00 44.40  ? 193 PHE B CE2 1 
ATOM 5128 C CZ  . PHE B 1 147 ? -30.034 -14.428 153.222 1.00 36.50  ? 193 PHE B CZ  1 
ATOM 5129 N N   . ALA B 1 148 ? -34.135 -20.296 154.755 1.00 48.54  ? 194 ALA B N   1 
ATOM 5130 C CA  . ALA B 1 148 ? -34.630 -21.650 154.968 1.00 46.05  ? 194 ALA B CA  1 
ATOM 5131 C C   . ALA B 1 148 ? -35.838 -21.948 154.088 1.00 49.41  ? 194 ALA B C   1 
ATOM 5132 O O   . ALA B 1 148 ? -35.968 -23.060 153.565 1.00 53.89  ? 194 ALA B O   1 
ATOM 5133 C CB  . ALA B 1 148 ? -34.977 -21.855 156.442 1.00 44.11  ? 194 ALA B CB  1 
ATOM 5134 N N   . ASN B 1 149 ? -36.729 -20.976 153.910 1.00 43.18  ? 195 ASN B N   1 
ATOM 5135 C CA  . ASN B 1 149 ? -37.980 -21.184 153.192 1.00 33.12  ? 195 ASN B CA  1 
ATOM 5136 C C   . ASN B 1 149 ? -38.094 -20.256 151.991 1.00 37.41  ? 195 ASN B C   1 
ATOM 5137 O O   . ASN B 1 149 ? -39.124 -19.621 151.778 1.00 49.01  ? 195 ASN B O   1 
ATOM 5138 C CB  . ASN B 1 149 ? -39.173 -20.996 154.125 1.00 38.75  ? 195 ASN B CB  1 
ATOM 5139 C CG  . ASN B 1 149 ? -38.912 -21.526 155.517 1.00 47.35  ? 195 ASN B CG  1 
ATOM 5140 O OD1 . ASN B 1 149 ? -39.081 -20.814 156.506 1.00 49.60  ? 195 ASN B OD1 1 
ATOM 5141 N ND2 . ASN B 1 149 ? -38.497 -22.784 155.604 1.00 47.85  ? 195 ASN B ND2 1 
ATOM 5142 N N   . GLN B 1 150 ? -37.005 -20.120 151.232 1.00 39.25  ? 196 GLN B N   1 
ATOM 5143 C CA  . GLN B 1 150 ? -37.051 -19.383 149.971 1.00 41.49  ? 196 GLN B CA  1 
ATOM 5144 C C   . GLN B 1 150 ? -38.191 -19.844 149.069 1.00 43.90  ? 196 GLN B C   1 
ATOM 5145 O O   . GLN B 1 150 ? -38.897 -19.014 148.489 1.00 52.07  ? 196 GLN B O   1 
ATOM 5146 C CB  . GLN B 1 150 ? -35.714 -19.519 149.247 1.00 39.59  ? 196 GLN B CB  1 
ATOM 5147 C CG  . GLN B 1 150 ? -35.592 -18.676 147.996 1.00 41.82  ? 196 GLN B CG  1 
ATOM 5148 C CD  . GLN B 1 150 ? -34.295 -18.927 147.259 1.00 51.16  ? 196 GLN B CD  1 
ATOM 5149 O OE1 . GLN B 1 150 ? -33.259 -19.180 147.873 1.00 52.89  ? 196 GLN B OE1 1 
ATOM 5150 N NE2 . GLN B 1 150 ? -34.344 -18.864 145.935 1.00 51.94  ? 196 GLN B NE2 1 
ATOM 5151 N N   . ALA B 1 151 ? -38.372 -21.157 148.910 1.00 41.55  ? 197 ALA B N   1 
ATOM 5152 C CA  . ALA B 1 151 ? -39.419 -21.645 148.015 1.00 38.08  ? 197 ALA B CA  1 
ATOM 5153 C C   . ALA B 1 151 ? -40.804 -21.241 148.506 1.00 38.28  ? 197 ALA B C   1 
ATOM 5154 O O   . ALA B 1 151 ? -41.645 -20.785 147.718 1.00 42.63  ? 197 ALA B O   1 
ATOM 5155 C CB  . ALA B 1 151 ? -39.323 -23.162 147.870 1.00 39.63  ? 197 ALA B CB  1 
ATOM 5156 N N   . GLN B 1 152 ? -41.055 -21.394 149.807 1.00 38.26  ? 198 GLN B N   1 
ATOM 5157 C CA  . GLN B 1 152 ? -42.332 -20.976 150.369 1.00 35.90  ? 198 GLN B CA  1 
ATOM 5158 C C   . GLN B 1 152 ? -42.528 -19.473 150.225 1.00 37.68  ? 198 GLN B C   1 
ATOM 5159 O O   . GLN B 1 152 ? -43.643 -19.012 149.964 1.00 43.45  ? 198 GLN B O   1 
ATOM 5160 C CB  . GLN B 1 152 ? -42.420 -21.393 151.836 1.00 31.63  ? 198 GLN B CB  1 
ATOM 5161 C CG  . GLN B 1 152 ? -42.739 -22.858 152.051 1.00 35.20  ? 198 GLN B CG  1 
ATOM 5162 C CD  . GLN B 1 152 ? -41.497 -23.721 152.099 1.00 44.54  ? 198 GLN B CD  1 
ATOM 5163 O OE1 . GLN B 1 152 ? -40.690 -23.719 151.170 1.00 48.79  ? 198 GLN B OE1 1 
ATOM 5164 N NE2 . GLN B 1 152 ? -41.334 -24.464 153.186 1.00 45.85  ? 198 GLN B NE2 1 
ATOM 5165 N N   . TRP B 1 153 ? -41.459 -18.693 150.399 1.00 33.89  ? 199 TRP B N   1 
ATOM 5166 C CA  . TRP B 1 153 ? -41.561 -17.246 150.247 1.00 31.14  ? 199 TRP B CA  1 
ATOM 5167 C C   . TRP B 1 153 ? -41.922 -16.864 148.818 1.00 37.06  ? 199 TRP B C   1 
ATOM 5168 O O   . TRP B 1 153 ? -42.771 -15.991 148.599 1.00 49.49  ? 199 TRP B O   1 
ATOM 5169 C CB  . TRP B 1 153 ? -40.250 -16.580 150.663 1.00 32.16  ? 199 TRP B CB  1 
ATOM 5170 C CG  . TRP B 1 153 ? -40.192 -16.220 152.115 1.00 33.57  ? 199 TRP B CG  1 
ATOM 5171 C CD1 . TRP B 1 153 ? -39.760 -17.010 153.137 1.00 34.77  ? 199 TRP B CD1 1 
ATOM 5172 C CD2 . TRP B 1 153 ? -40.586 -14.978 152.706 1.00 35.19  ? 199 TRP B CD2 1 
ATOM 5173 N NE1 . TRP B 1 153 ? -39.857 -16.337 154.329 1.00 36.39  ? 199 TRP B NE1 1 
ATOM 5174 C CE2 . TRP B 1 153 ? -40.362 -15.087 154.092 1.00 37.19  ? 199 TRP B CE2 1 
ATOM 5175 C CE3 . TRP B 1 153 ? -41.104 -13.784 152.199 1.00 35.48  ? 199 TRP B CE3 1 
ATOM 5176 C CZ2 . TRP B 1 153 ? -40.640 -14.049 154.975 1.00 35.36  ? 199 TRP B CZ2 1 
ATOM 5177 C CZ3 . TRP B 1 153 ? -41.378 -12.755 153.078 1.00 38.79  ? 199 TRP B CZ3 1 
ATOM 5178 C CH2 . TRP B 1 153 ? -41.146 -12.894 154.450 1.00 36.95  ? 199 TRP B CH2 1 
ATOM 5179 N N   . GLU B 1 154 ? -41.286 -17.504 147.833 1.00 36.74  ? 200 GLU B N   1 
ATOM 5180 C CA  . GLU B 1 154 ? -41.622 -17.226 146.440 1.00 34.95  ? 200 GLU B CA  1 
ATOM 5181 C C   . GLU B 1 154 ? -43.064 -17.603 146.137 1.00 40.82  ? 200 GLU B C   1 
ATOM 5182 O O   . GLU B 1 154 ? -43.781 -16.849 145.470 1.00 48.49  ? 200 GLU B O   1 
ATOM 5183 C CB  . GLU B 1 154 ? -40.673 -17.961 145.494 1.00 42.05  ? 200 GLU B CB  1 
ATOM 5184 C CG  . GLU B 1 154 ? -39.202 -17.724 145.755 1.00 55.67  ? 200 GLU B CG  1 
ATOM 5185 C CD  . GLU B 1 154 ? -38.365 -17.835 144.499 1.00 61.13  ? 200 GLU B CD  1 
ATOM 5186 O OE1 . GLU B 1 154 ? -38.761 -18.588 143.585 1.00 58.37  ? 200 GLU B OE1 1 
ATOM 5187 O OE2 . GLU B 1 154 ? -37.310 -17.172 144.423 1.00 58.15  ? 200 GLU B OE2 1 
ATOM 5188 N N   . TYR B 1 155 ? -43.512 -18.762 146.624 1.00 35.46  ? 201 TYR B N   1 
ATOM 5189 C CA  . TYR B 1 155 ? -44.902 -19.143 146.394 1.00 28.30  ? 201 TYR B CA  1 
ATOM 5190 C C   . TYR B 1 155 ? -45.863 -18.160 147.048 1.00 34.35  ? 201 TYR B C   1 
ATOM 5191 O O   . TYR B 1 155 ? -46.873 -17.786 146.442 1.00 45.21  ? 201 TYR B O   1 
ATOM 5192 C CB  . TYR B 1 155 ? -45.161 -20.558 146.908 1.00 35.13  ? 201 TYR B CB  1 
ATOM 5193 C CG  . TYR B 1 155 ? -46.627 -20.931 146.972 1.00 38.86  ? 201 TYR B CG  1 
ATOM 5194 C CD1 . TYR B 1 155 ? -47.298 -21.379 145.842 1.00 37.23  ? 201 TYR B CD1 1 
ATOM 5195 C CD2 . TYR B 1 155 ? -47.337 -20.844 148.161 1.00 38.74  ? 201 TYR B CD2 1 
ATOM 5196 C CE1 . TYR B 1 155 ? -48.632 -21.723 145.893 1.00 32.19  ? 201 TYR B CE1 1 
ATOM 5197 C CE2 . TYR B 1 155 ? -48.672 -21.184 148.221 1.00 41.21  ? 201 TYR B CE2 1 
ATOM 5198 C CZ  . TYR B 1 155 ? -49.314 -21.624 147.085 1.00 39.16  ? 201 TYR B CZ  1 
ATOM 5199 O OH  . TYR B 1 155 ? -50.645 -21.964 147.142 1.00 42.24  ? 201 TYR B OH  1 
ATOM 5200 N N   . PHE B 1 156 ? -45.563 -17.726 148.274 1.00 35.72  ? 202 PHE B N   1 
ATOM 5201 C CA  . PHE B 1 156 ? -46.444 -16.803 148.979 1.00 31.51  ? 202 PHE B CA  1 
ATOM 5202 C C   . PHE B 1 156 ? -46.530 -15.464 148.263 1.00 32.66  ? 202 PHE B C   1 
ATOM 5203 O O   . PHE B 1 156 ? -47.620 -14.910 148.097 1.00 40.69  ? 202 PHE B O   1 
ATOM 5204 C CB  . PHE B 1 156 ? -45.959 -16.609 150.414 1.00 31.05  ? 202 PHE B CB  1 
ATOM 5205 C CG  . PHE B 1 156 ? -46.473 -15.357 151.063 1.00 32.03  ? 202 PHE B CG  1 
ATOM 5206 C CD1 . PHE B 1 156 ? -47.797 -15.256 151.450 1.00 34.70  ? 202 PHE B CD1 1 
ATOM 5207 C CD2 . PHE B 1 156 ? -45.634 -14.280 151.284 1.00 31.28  ? 202 PHE B CD2 1 
ATOM 5208 C CE1 . PHE B 1 156 ? -48.271 -14.109 152.051 1.00 34.68  ? 202 PHE B CE1 1 
ATOM 5209 C CE2 . PHE B 1 156 ? -46.104 -13.130 151.884 1.00 38.64  ? 202 PHE B CE2 1 
ATOM 5210 C CZ  . PHE B 1 156 ? -47.425 -13.045 152.266 1.00 35.82  ? 202 PHE B CZ  1 
ATOM 5211 N N   . VAL B 1 157 ? -45.388 -14.921 147.836 1.00 32.13  ? 203 VAL B N   1 
ATOM 5212 C CA  . VAL B 1 157 ? -45.422 -13.628 147.162 1.00 33.91  ? 203 VAL B CA  1 
ATOM 5213 C C   . VAL B 1 157 ? -46.085 -13.746 145.793 1.00 37.03  ? 203 VAL B C   1 
ATOM 5214 O O   . VAL B 1 157 ? -46.797 -12.829 145.362 1.00 45.35  ? 203 VAL B O   1 
ATOM 5215 C CB  . VAL B 1 157 ? -44.009 -13.019 147.079 1.00 31.72  ? 203 VAL B CB  1 
ATOM 5216 C CG1 . VAL B 1 157 ? -43.091 -13.880 146.248 1.00 41.30  ? 203 VAL B CG1 1 
ATOM 5217 C CG2 . VAL B 1 157 ? -44.072 -11.610 146.520 1.00 38.92  ? 203 VAL B CG2 1 
ATOM 5218 N N   . ASN B 1 158 ? -45.891 -14.868 145.094 1.00 28.94  ? 204 ASN B N   1 
ATOM 5219 C CA  . ASN B 1 158 ? -46.576 -15.060 143.820 1.00 25.56  ? 204 ASN B CA  1 
ATOM 5220 C C   . ASN B 1 158 ? -48.084 -15.145 144.010 1.00 33.84  ? 204 ASN B C   1 
ATOM 5221 O O   . ASN B 1 158 ? -48.846 -14.567 143.228 1.00 35.01  ? 204 ASN B O   1 
ATOM 5222 C CB  . ASN B 1 158 ? -46.046 -16.312 143.128 1.00 31.60  ? 204 ASN B CB  1 
ATOM 5223 C CG  . ASN B 1 158 ? -44.860 -16.021 142.239 1.00 36.66  ? 204 ASN B CG  1 
ATOM 5224 O OD1 . ASN B 1 158 ? -44.795 -14.975 141.597 1.00 38.22  ? 204 ASN B OD1 1 
ATOM 5225 N ND2 . ASN B 1 158 ? -43.911 -16.946 142.198 1.00 43.29  ? 204 ASN B ND2 1 
ATOM 5226 N N   . MET B 1 159 ? -48.537 -15.858 145.045 1.00 39.44  ? 205 MET B N   1 
ATOM 5227 C CA  . MET B 1 159 ? -49.966 -15.905 145.333 1.00 32.13  ? 205 MET B CA  1 
ATOM 5228 C C   . MET B 1 159 ? -50.500 -14.543 145.750 1.00 40.26  ? 205 MET B C   1 
ATOM 5229 O O   . MET B 1 159 ? -51.636 -14.198 145.414 1.00 53.73  ? 205 MET B O   1 
ATOM 5230 C CB  . MET B 1 159 ? -50.258 -16.944 146.414 1.00 36.15  ? 205 MET B CB  1 
ATOM 5231 C CG  . MET B 1 159 ? -50.277 -18.372 145.905 1.00 45.72  ? 205 MET B CG  1 
ATOM 5232 S SD  . MET B 1 159 ? -51.882 -18.830 145.224 1.00 64.13  ? 205 MET B SD  1 
ATOM 5233 C CE  . MET B 1 159 ? -51.445 -19.168 143.521 1.00 47.56  ? 205 MET B CE  1 
ATOM 5234 N N   . VAL B 1 160 ? -49.702 -13.762 146.479 1.00 31.79  ? 206 VAL B N   1 
ATOM 5235 C CA  . VAL B 1 160 ? -50.119 -12.413 146.850 1.00 31.14  ? 206 VAL B CA  1 
ATOM 5236 C C   . VAL B 1 160 ? -50.316 -11.561 145.604 1.00 31.94  ? 206 VAL B C   1 
ATOM 5237 O O   . VAL B 1 160 ? -51.318 -10.848 145.473 1.00 42.02  ? 206 VAL B O   1 
ATOM 5238 C CB  . VAL B 1 160 ? -49.095 -11.783 147.811 1.00 31.79  ? 206 VAL B CB  1 
ATOM 5239 C CG1 . VAL B 1 160 ? -49.152 -10.270 147.734 1.00 33.09  ? 206 VAL B CG1 1 
ATOM 5240 C CG2 . VAL B 1 160 ? -49.345 -12.253 149.230 1.00 34.23  ? 206 VAL B CG2 1 
ATOM 5241 N N   . ALA B 1 161 ? -49.371 -11.631 144.665 1.00 30.48  ? 207 ALA B N   1 
ATOM 5242 C CA  . ALA B 1 161 ? -49.517 -10.889 143.417 1.00 29.88  ? 207 ALA B CA  1 
ATOM 5243 C C   . ALA B 1 161 ? -50.731 -11.363 142.630 1.00 32.28  ? 207 ALA B C   1 
ATOM 5244 O O   . ALA B 1 161 ? -51.484 -10.547 142.087 1.00 41.99  ? 207 ALA B O   1 
ATOM 5245 C CB  . ALA B 1 161 ? -48.251 -11.020 142.573 1.00 32.02  ? 207 ALA B CB  1 
ATOM 5246 N N   . TYR B 1 162 ? -50.939 -12.680 142.562 1.00 30.78  ? 208 TYR B N   1 
ATOM 5247 C CA  . TYR B 1 162 ? -52.065 -13.223 141.810 1.00 32.11  ? 208 TYR B CA  1 
ATOM 5248 C C   . TYR B 1 162 ? -53.396 -12.779 142.402 1.00 34.69  ? 208 TYR B C   1 
ATOM 5249 O O   . TYR B 1 162 ? -54.317 -12.409 141.666 1.00 42.24  ? 208 TYR B O   1 
ATOM 5250 C CB  . TYR B 1 162 ? -51.974 -14.748 141.772 1.00 30.51  ? 208 TYR B CB  1 
ATOM 5251 C CG  . TYR B 1 162 ? -53.099 -15.420 141.023 1.00 33.64  ? 208 TYR B CG  1 
ATOM 5252 C CD1 . TYR B 1 162 ? -53.214 -15.294 139.647 1.00 35.52  ? 208 TYR B CD1 1 
ATOM 5253 C CD2 . TYR B 1 162 ? -54.039 -16.191 141.691 1.00 37.90  ? 208 TYR B CD2 1 
ATOM 5254 C CE1 . TYR B 1 162 ? -54.239 -15.910 138.958 1.00 39.94  ? 208 TYR B CE1 1 
ATOM 5255 C CE2 . TYR B 1 162 ? -55.068 -16.808 141.011 1.00 37.96  ? 208 TYR B CE2 1 
ATOM 5256 C CZ  . TYR B 1 162 ? -55.162 -16.666 139.645 1.00 39.03  ? 208 TYR B CZ  1 
ATOM 5257 O OH  . TYR B 1 162 ? -56.184 -17.280 138.962 1.00 36.74  ? 208 TYR B OH  1 
ATOM 5258 N N   . ARG B 1 163 ? -53.516 -12.805 143.729 1.00 26.01  ? 209 ARG B N   1 
ATOM 5259 C CA  . ARG B 1 163 ? -54.765 -12.433 144.377 1.00 32.75  ? 209 ARG B CA  1 
ATOM 5260 C C   . ARG B 1 163 ? -54.991 -10.929 144.401 1.00 36.95  ? 209 ARG B C   1 
ATOM 5261 O O   . ARG B 1 163 ? -56.147 -10.492 144.390 1.00 40.55  ? 209 ARG B O   1 
ATOM 5262 C CB  . ARG B 1 163 ? -54.801 -12.988 145.800 1.00 31.04  ? 209 ARG B CB  1 
ATOM 5263 C CG  . ARG B 1 163 ? -54.921 -14.501 145.853 1.00 35.61  ? 209 ARG B CG  1 
ATOM 5264 C CD  . ARG B 1 163 ? -56.224 -14.964 145.223 1.00 38.69  ? 209 ARG B CD  1 
ATOM 5265 N NE  . ARG B 1 163 ? -56.163 -16.348 144.772 1.00 39.30  ? 209 ARG B NE  1 
ATOM 5266 C CZ  . ARG B 1 163 ? -56.243 -17.402 145.572 1.00 41.54  ? 209 ARG B CZ  1 
ATOM 5267 N NH1 . ARG B 1 163 ? -56.393 -17.268 146.879 1.00 41.93  ? 209 ARG B NH1 1 
ATOM 5268 N NH2 . ARG B 1 163 ? -56.174 -18.622 145.047 1.00 41.04  ? 209 ARG B NH2 1 
ATOM 5269 N N   . ALA B 1 164 ? -53.927 -10.127 144.437 1.00 33.73  ? 210 ALA B N   1 
ATOM 5270 C CA  . ALA B 1 164 ? -54.086 -8.683  144.352 1.00 32.90  ? 210 ALA B CA  1 
ATOM 5271 C C   . ALA B 1 164 ? -54.367 -8.214  142.935 1.00 34.76  ? 210 ALA B C   1 
ATOM 5272 O O   . ALA B 1 164 ? -54.999 -7.169  142.757 1.00 44.29  ? 210 ALA B O   1 
ATOM 5273 C CB  . ALA B 1 164 ? -52.841 -7.981  144.892 1.00 34.07  ? 210 ALA B CB  1 
ATOM 5274 N N   . GLY B 1 165 ? -53.919 -8.957  141.928 1.00 30.63  ? 211 GLY B N   1 
ATOM 5275 C CA  . GLY B 1 165 ? -54.195 -8.593  140.557 1.00 29.33  ? 211 GLY B CA  1 
ATOM 5276 C C   . GLY B 1 165 ? -55.601 -8.874  140.089 1.00 36.29  ? 211 GLY B C   1 
ATOM 5277 O O   . GLY B 1 165 ? -55.971 -8.454  138.990 1.00 42.06  ? 211 GLY B O   1 
ATOM 5278 N N   . ALA B 1 166 ? -56.399 -9.584  140.890 1.00 40.45  ? 212 ALA B N   1 
ATOM 5279 C CA  . ALA B 1 166 ? -57.790 -9.825  140.525 1.00 39.62  ? 212 ALA B CA  1 
ATOM 5280 C C   . ALA B 1 166 ? -58.574 -8.520  140.471 1.00 41.14  ? 212 ALA B C   1 
ATOM 5281 O O   . ALA B 1 166 ? -59.336 -8.281  139.528 1.00 43.69  ? 212 ALA B O   1 
ATOM 5282 C CB  . ALA B 1 166 ? -58.432 -10.799 141.513 1.00 35.87  ? 212 ALA B CB  1 
ATOM 5283 N N   . PHE B 1 167 ? -58.392 -7.662  141.469 1.00 37.80  ? 213 PHE B N   1 
ATOM 5284 C CA  . PHE B 1 167 ? -59.041 -6.363  141.492 1.00 34.56  ? 213 PHE B CA  1 
ATOM 5285 C C   . PHE B 1 167 ? -58.312 -5.391  140.571 1.00 37.49  ? 213 PHE B C   1 
ATOM 5286 O O   . PHE B 1 167 ? -57.142 -5.573  140.229 1.00 39.92  ? 213 PHE B O   1 
ATOM 5287 C CB  . PHE B 1 167 ? -59.099 -5.814  142.916 1.00 30.32  ? 213 PHE B CB  1 
ATOM 5288 C CG  . PHE B 1 167 ? -59.394 -6.853  143.955 1.00 36.66  ? 213 PHE B CG  1 
ATOM 5289 C CD1 . PHE B 1 167 ? -60.699 -7.227  144.225 1.00 37.00  ? 213 PHE B CD1 1 
ATOM 5290 C CD2 . PHE B 1 167 ? -58.370 -7.450  144.669 1.00 38.48  ? 213 PHE B CD2 1 
ATOM 5291 C CE1 . PHE B 1 167 ? -60.976 -8.181  145.182 1.00 37.97  ? 213 PHE B CE1 1 
ATOM 5292 C CE2 . PHE B 1 167 ? -58.642 -8.404  145.627 1.00 42.76  ? 213 PHE B CE2 1 
ATOM 5293 C CZ  . PHE B 1 167 ? -59.947 -8.769  145.884 1.00 43.85  ? 213 PHE B CZ  1 
ATOM 5294 N N   . ALA B 1 168 ? -59.021 -4.339  140.174 1.00 43.92  ? 214 ALA B N   1 
ATOM 5295 C CA  . ALA B 1 168 ? -58.524 -3.398  139.185 1.00 36.30  ? 214 ALA B CA  1 
ATOM 5296 C C   . ALA B 1 168 ? -58.391 -2.014  139.800 1.00 40.64  ? 214 ALA B C   1 
ATOM 5297 O O   . ALA B 1 168 ? -59.251 -1.566  140.562 1.00 44.99  ? 214 ALA B O   1 
ATOM 5298 C CB  . ALA B 1 168 ? -59.442 -3.334  137.961 1.00 38.27  ? 214 ALA B CB  1 
ATOM 5299 N N   . ALA B 1 169 ? -57.292 -1.349  139.462 1.00 42.83  ? 215 ALA B N   1 
ATOM 5300 C CA  . ALA B 1 169 ? -57.025 0.023   139.855 1.00 37.97  ? 215 ALA B CA  1 
ATOM 5301 C C   . ALA B 1 169 ? -56.460 0.762   138.654 1.00 40.53  ? 215 ALA B C   1 
ATOM 5302 O O   . ALA B 1 169 ? -55.733 0.172   137.847 1.00 44.86  ? 215 ALA B O   1 
ATOM 5303 C CB  . ALA B 1 169 ? -56.039 0.097   141.030 1.00 35.74  ? 215 ALA B CB  1 
ATOM 5304 N N   . PRO B 1 170 ? -56.779 2.046   138.502 1.00 29.86  ? 216 PRO B N   1 
ATOM 5305 C CA  . PRO B 1 170 ? -56.318 2.779   137.318 1.00 26.69  ? 216 PRO B CA  1 
ATOM 5306 C C   . PRO B 1 170 ? -54.816 2.997   137.343 1.00 33.45  ? 216 PRO B C   1 
ATOM 5307 O O   . PRO B 1 170 ? -54.240 3.366   138.368 1.00 40.36  ? 216 PRO B O   1 
ATOM 5308 C CB  . PRO B 1 170 ? -57.072 4.112   137.406 1.00 31.56  ? 216 PRO B CB  1 
ATOM 5309 C CG  . PRO B 1 170 ? -58.144 3.901   138.417 1.00 35.98  ? 216 PRO B CG  1 
ATOM 5310 C CD  . PRO B 1 170 ? -57.629 2.879   139.365 1.00 31.57  ? 216 PRO B CD  1 
ATOM 5311 N N   . ALA B 1 171 ? -54.179 2.767   136.197 1.00 38.85  ? 217 ALA B N   1 
ATOM 5312 C CA  . ALA B 1 171 ? -52.766 3.076   136.043 1.00 38.42  ? 217 ALA B CA  1 
ATOM 5313 C C   . ALA B 1 171 ? -52.522 4.530   135.679 1.00 36.99  ? 217 ALA B C   1 
ATOM 5314 O O   . ALA B 1 171 ? -51.389 5.004   135.807 1.00 40.34  ? 217 ALA B O   1 
ATOM 5315 C CB  . ALA B 1 171 ? -52.128 2.179   134.981 1.00 42.21  ? 217 ALA B CB  1 
ATOM 5316 N N   . SER B 1 172 ? -53.551 5.252   135.239 1.00 47.40  ? 218 SER B N   1 
ATOM 5317 C CA  . SER B 1 172 ? -53.372 6.672   134.959 1.00 46.49  ? 218 SER B CA  1 
ATOM 5318 C C   . SER B 1 172 ? -53.276 7.476   136.246 1.00 44.07  ? 218 SER B C   1 
ATOM 5319 O O   . SER B 1 172 ? -52.725 8.583   136.254 1.00 47.76  ? 218 SER B O   1 
ATOM 5320 C CB  . SER B 1 172 ? -54.513 7.193   134.097 1.00 49.65  ? 218 SER B CB  1 
ATOM 5321 O OG  . SER B 1 172 ? -54.429 8.600   133.967 1.00 52.81  ? 218 SER B OG  1 
ATOM 5322 N N   . MET B 1 173 ? -53.826 6.954   137.338 1.00 40.21  ? 219 MET B N   1 
ATOM 5323 C CA  . MET B 1 173 ? -53.606 7.580   138.632 1.00 37.04  ? 219 MET B CA  1 
ATOM 5324 C C   . MET B 1 173 ? -52.177 7.317   139.074 1.00 42.75  ? 219 MET B C   1 
ATOM 5325 O O   . MET B 1 173 ? -51.812 6.176   139.362 1.00 49.87  ? 219 MET B O   1 
ATOM 5326 C CB  . MET B 1 173 ? -54.579 7.032   139.672 1.00 33.84  ? 219 MET B CB  1 
ATOM 5327 C CG  . MET B 1 173 ? -55.919 7.722   139.658 1.00 43.28  ? 219 MET B CG  1 
ATOM 5328 S SD  . MET B 1 173 ? -57.017 7.256   141.001 1.00 59.04  ? 219 MET B SD  1 
ATOM 5329 C CE  . MET B 1 173 ? -55.836 6.842   142.278 1.00 42.24  ? 219 MET B CE  1 
ATOM 5330 N N   . THR B 1 174 ? -51.372 8.369   139.146 1.00 40.16  ? 220 THR B N   1 
ATOM 5331 C CA  . THR B 1 174 ? -49.963 8.228   139.476 1.00 42.48  ? 220 THR B CA  1 
ATOM 5332 C C   . THR B 1 174 ? -49.727 7.956   140.959 1.00 42.67  ? 220 THR B C   1 
ATOM 5333 O O   . THR B 1 174 ? -48.577 7.778   141.364 1.00 51.33  ? 220 THR B O   1 
ATOM 5334 C CB  . THR B 1 174 ? -49.186 9.467   139.005 1.00 42.57  ? 220 THR B CB  1 
ATOM 5335 O OG1 . THR B 1 174 ? -49.263 10.515  139.981 1.00 48.10  ? 220 THR B OG1 1 
ATOM 5336 C CG2 . THR B 1 174 ? -49.716 9.962   137.669 1.00 46.76  ? 220 THR B CG2 1 
ATOM 5337 N N   . TYR B 1 175 ? -50.787 7.870   141.763 1.00 32.56  ? 221 TYR B N   1 
ATOM 5338 C CA  . TYR B 1 175 ? -50.641 7.462   143.158 1.00 30.54  ? 221 TYR B CA  1 
ATOM 5339 C C   . TYR B 1 175 ? -49.937 6.114   143.265 1.00 36.77  ? 221 TYR B C   1 
ATOM 5340 O O   . TYR B 1 175 ? -48.931 5.971   143.976 1.00 43.85  ? 221 TYR B O   1 
ATOM 5341 C CB  . TYR B 1 175 ? -52.022 7.382   143.804 1.00 34.04  ? 221 TYR B CB  1 
ATOM 5342 C CG  . TYR B 1 175 ? -52.030 7.414   145.308 1.00 37.33  ? 221 TYR B CG  1 
ATOM 5343 C CD1 . TYR B 1 175 ? -51.025 8.048   146.010 1.00 46.86  ? 221 TYR B CD1 1 
ATOM 5344 C CD2 . TYR B 1 175 ? -53.038 6.794   146.026 1.00 39.92  ? 221 TYR B CD2 1 
ATOM 5345 C CE1 . TYR B 1 175 ? -51.034 8.090   147.385 1.00 53.33  ? 221 TYR B CE1 1 
ATOM 5346 C CE2 . TYR B 1 175 ? -53.056 6.821   147.409 1.00 38.67  ? 221 TYR B CE2 1 
ATOM 5347 C CZ  . TYR B 1 175 ? -52.053 7.469   148.084 1.00 43.54  ? 221 TYR B CZ  1 
ATOM 5348 O OH  . TYR B 1 175 ? -52.045 7.514   149.456 1.00 40.93  ? 221 TYR B OH  1 
ATOM 5349 N N   . TYR B 1 176 ? -50.456 5.112   142.553 1.00 37.73  ? 222 TYR B N   1 
ATOM 5350 C CA  . TYR B 1 176 ? -49.891 3.771   142.614 1.00 34.62  ? 222 TYR B CA  1 
ATOM 5351 C C   . TYR B 1 176 ? -48.473 3.745   142.070 1.00 34.70  ? 222 TYR B C   1 
ATOM 5352 O O   . TYR B 1 176 ? -47.606 3.060   142.620 1.00 44.13  ? 222 TYR B O   1 
ATOM 5353 C CB  . TYR B 1 176 ? -50.773 2.803   141.833 1.00 39.77  ? 222 TYR B CB  1 
ATOM 5354 C CG  . TYR B 1 176 ? -52.228 2.888   142.212 1.00 30.86  ? 222 TYR B CG  1 
ATOM 5355 C CD1 . TYR B 1 176 ? -52.637 2.642   143.510 1.00 33.46  ? 222 TYR B CD1 1 
ATOM 5356 C CD2 . TYR B 1 176 ? -53.191 3.216   141.274 1.00 31.60  ? 222 TYR B CD2 1 
ATOM 5357 C CE1 . TYR B 1 176 ? -53.962 2.716   143.862 1.00 33.76  ? 222 TYR B CE1 1 
ATOM 5358 C CE2 . TYR B 1 176 ? -54.519 3.293   141.617 1.00 37.61  ? 222 TYR B CE2 1 
ATOM 5359 C CZ  . TYR B 1 176 ? -54.899 3.040   142.914 1.00 36.01  ? 222 TYR B CZ  1 
ATOM 5360 O OH  . TYR B 1 176 ? -56.225 3.115   143.262 1.00 42.29  ? 222 TYR B OH  1 
ATOM 5361 N N   . GLU B 1 177 ? -48.223 4.470   140.981 1.00 35.51  ? 223 GLU B N   1 
ATOM 5362 C CA  . GLU B 1 177 ? -46.884 4.483   140.408 1.00 37.84  ? 223 GLU B CA  1 
ATOM 5363 C C   . GLU B 1 177 ? -45.881 5.106   141.369 1.00 39.20  ? 223 GLU B C   1 
ATOM 5364 O O   . GLU B 1 177 ? -44.782 4.571   141.553 1.00 48.88  ? 223 GLU B O   1 
ATOM 5365 C CB  . GLU B 1 177 ? -46.893 5.221   139.073 1.00 40.10  ? 223 GLU B CB  1 
ATOM 5366 C CG  . GLU B 1 177 ? -45.561 5.836   138.700 1.00 44.87  ? 223 GLU B CG  1 
ATOM 5367 C CD  . GLU B 1 177 ? -45.566 6.429   137.306 1.00 51.49  ? 223 GLU B CD  1 
ATOM 5368 O OE1 . GLU B 1 177 ? -44.641 6.119   136.525 1.00 54.71  ? 223 GLU B OE1 1 
ATOM 5369 O OE2 . GLU B 1 177 ? -46.497 7.197   136.988 1.00 50.35  ? 223 GLU B OE2 1 
ATOM 5370 N N   . ARG B 1 178 ? -46.247 6.223   142.003 1.00 33.10  ? 224 ARG B N   1 
ATOM 5371 C CA  . ARG B 1 178 ? -45.359 6.840   142.982 1.00 35.31  ? 224 ARG B CA  1 
ATOM 5372 C C   . ARG B 1 178 ? -45.083 5.901   144.145 1.00 38.53  ? 224 ARG B C   1 
ATOM 5373 O O   . ARG B 1 178 ? -43.926 5.720   144.542 1.00 46.40  ? 224 ARG B O   1 
ATOM 5374 C CB  . ARG B 1 178 ? -45.957 8.151   143.490 1.00 36.79  ? 224 ARG B CB  1 
ATOM 5375 C CG  . ARG B 1 178 ? -45.280 8.690   144.742 1.00 39.13  ? 224 ARG B CG  1 
ATOM 5376 C CD  . ARG B 1 178 ? -44.243 9.750   144.406 1.00 38.33  ? 224 ARG B CD  1 
ATOM 5377 N NE  . ARG B 1 178 ? -43.373 10.044  145.539 1.00 41.82  ? 224 ARG B NE  1 
ATOM 5378 C CZ  . ARG B 1 178 ? -43.742 10.750  146.598 1.00 43.30  ? 224 ARG B CZ  1 
ATOM 5379 N NH1 . ARG B 1 178 ? -44.955 11.265  146.695 1.00 43.14  ? 224 ARG B NH1 1 
ATOM 5380 N NH2 . ARG B 1 178 ? -42.872 10.945  147.585 1.00 42.56  ? 224 ARG B NH2 1 
ATOM 5381 N N   . HIS B 1 179 ? -46.127 5.278   144.694 1.00 37.98  ? 225 HIS B N   1 
ATOM 5382 C CA  . HIS B 1 179 ? -45.915 4.392   145.833 1.00 29.91  ? 225 HIS B CA  1 
ATOM 5383 C C   . HIS B 1 179 ? -45.066 3.183   145.454 1.00 34.25  ? 225 HIS B C   1 
ATOM 5384 O O   . HIS B 1 179 ? -44.191 2.768   146.222 1.00 46.75  ? 225 HIS B O   1 
ATOM 5385 C CB  . HIS B 1 179 ? -47.254 3.952   146.415 1.00 34.06  ? 225 HIS B CB  1 
ATOM 5386 C CG  . HIS B 1 179 ? -47.795 4.888   147.448 1.00 40.93  ? 225 HIS B CG  1 
ATOM 5387 N ND1 . HIS B 1 179 ? -47.023 5.386   148.474 1.00 43.12  ? 225 HIS B ND1 1 
ATOM 5388 C CD2 . HIS B 1 179 ? -49.032 5.407   147.621 1.00 44.46  ? 225 HIS B CD2 1 
ATOM 5389 C CE1 . HIS B 1 179 ? -47.760 6.178   149.232 1.00 40.21  ? 225 HIS B CE1 1 
ATOM 5390 N NE2 . HIS B 1 179 ? -48.984 6.206   148.737 1.00 37.32  ? 225 HIS B NE2 1 
ATOM 5391 N N   . ALA B 1 180 ? -45.305 2.604   144.275 1.00 34.59  ? 226 ALA B N   1 
ATOM 5392 C CA  . ALA B 1 180 ? -44.531 1.444   143.848 1.00 34.77  ? 226 ALA B CA  1 
ATOM 5393 C C   . ALA B 1 180 ? -43.072 1.807   143.607 1.00 41.91  ? 226 ALA B C   1 
ATOM 5394 O O   . ALA B 1 180 ? -42.171 1.057   143.997 1.00 49.18  ? 226 ALA B O   1 
ATOM 5395 C CB  . ALA B 1 180 ? -45.146 0.836   142.590 1.00 40.99  ? 226 ALA B CB  1 
ATOM 5396 N N   . TRP B 1 181 ? -42.816 2.947   142.963 1.00 43.93  ? 227 TRP B N   1 
ATOM 5397 C CA  . TRP B 1 181 ? -41.438 3.363   142.735 1.00 42.96  ? 227 TRP B CA  1 
ATOM 5398 C C   . TRP B 1 181 ? -40.742 3.723   144.040 1.00 34.17  ? 227 TRP B C   1 
ATOM 5399 O O   . TRP B 1 181 ? -39.519 3.580   144.151 1.00 32.07  ? 227 TRP B O   1 
ATOM 5400 C CB  . TRP B 1 181 ? -41.410 4.537   141.757 1.00 44.00  ? 227 TRP B CB  1 
ATOM 5401 C CG  . TRP B 1 181 ? -40.257 5.464   141.929 1.00 46.36  ? 227 TRP B CG  1 
ATOM 5402 C CD1 . TRP B 1 181 ? -38.990 5.295   141.454 1.00 51.47  ? 227 TRP B CD1 1 
ATOM 5403 C CD2 . TRP B 1 181 ? -40.262 6.715   142.621 1.00 48.27  ? 227 TRP B CD2 1 
ATOM 5404 N NE1 . TRP B 1 181 ? -38.205 6.364   141.809 1.00 52.11  ? 227 TRP B NE1 1 
ATOM 5405 C CE2 . TRP B 1 181 ? -38.964 7.249   142.528 1.00 54.60  ? 227 TRP B CE2 1 
ATOM 5406 C CE3 . TRP B 1 181 ? -41.239 7.433   143.314 1.00 43.07  ? 227 TRP B CE3 1 
ATOM 5407 C CZ2 . TRP B 1 181 ? -38.617 8.468   143.101 1.00 48.43  ? 227 TRP B CZ2 1 
ATOM 5408 C CZ3 . TRP B 1 181 ? -40.894 8.641   143.882 1.00 44.45  ? 227 TRP B CZ3 1 
ATOM 5409 C CH2 . TRP B 1 181 ? -39.596 9.148   143.772 1.00 44.05  ? 227 TRP B CH2 1 
ATOM 5410 N N   . MET B 1 182 ? -41.497 4.181   145.039 1.00 38.08  ? 228 MET B N   1 
ATOM 5411 C CA  . MET B 1 182 ? -40.901 4.471   146.337 1.00 37.82  ? 228 MET B CA  1 
ATOM 5412 C C   . MET B 1 182 ? -40.560 3.193   147.091 1.00 36.19  ? 228 MET B C   1 
ATOM 5413 O O   . MET B 1 182 ? -39.488 3.091   147.697 1.00 43.40  ? 228 MET B O   1 
ATOM 5414 C CB  . MET B 1 182 ? -41.850 5.336   147.163 1.00 43.16  ? 228 MET B CB  1 
ATOM 5415 C CG  . MET B 1 182 ? -41.179 6.451   147.939 1.00 46.39  ? 228 MET B CG  1 
ATOM 5416 S SD  . MET B 1 182 ? -42.320 7.215   149.102 1.00 53.34  ? 228 MET B SD  1 
ATOM 5417 C CE  . MET B 1 182 ? -43.853 7.037   148.203 1.00 36.34  ? 228 MET B CE  1 
ATOM 5418 N N   . SER B 1 183 ? -41.454 2.208   147.068 1.00 37.61  ? 229 SER B N   1 
ATOM 5419 C CA  . SER B 1 183 ? -41.303 1.009   147.881 1.00 41.55  ? 229 SER B CA  1 
ATOM 5420 C C   . SER B 1 183 ? -40.686 -0.165  147.133 1.00 44.24  ? 229 SER B C   1 
ATOM 5421 O O   . SER B 1 183 ? -40.612 -1.262  147.694 1.00 43.87  ? 229 SER B O   1 
ATOM 5422 C CB  . SER B 1 183 ? -42.660 0.587   148.449 1.00 38.73  ? 229 SER B CB  1 
ATOM 5423 O OG  . SER B 1 183 ? -42.517 -0.498  149.347 1.00 47.66  ? 229 SER B OG  1 
ATOM 5424 N N   . ASN B 1 184 ? -40.247 0.025   145.893 1.00 40.88  ? 230 ASN B N   1 
ATOM 5425 C CA  . ASN B 1 184 ? -39.705 -1.058  145.078 1.00 36.24  ? 230 ASN B CA  1 
ATOM 5426 C C   . ASN B 1 184 ? -38.327 -0.696  144.547 1.00 41.86  ? 230 ASN B C   1 
ATOM 5427 O O   . ASN B 1 184 ? -38.027 -0.861  143.363 1.00 46.39  ? 230 ASN B O   1 
ATOM 5428 C CB  . ASN B 1 184 ? -40.647 -1.392  143.927 1.00 36.28  ? 230 ASN B CB  1 
ATOM 5429 C CG  . ASN B 1 184 ? -41.559 -2.557  144.242 1.00 47.22  ? 230 ASN B CG  1 
ATOM 5430 O OD1 . ASN B 1 184 ? -42.535 -2.805  143.535 1.00 46.98  ? 230 ASN B OD1 1 
ATOM 5431 N ND2 . ASN B 1 184 ? -41.244 -3.283  145.309 1.00 45.46  ? 230 ASN B ND2 1 
ATOM 5432 N N   . GLY B 1 185 ? -37.462 -0.192  145.421 1.00 39.26  ? 231 GLY B N   1 
ATOM 5433 C CA  . GLY B 1 185 ? -36.119 0.147   144.995 1.00 36.18  ? 231 GLY B CA  1 
ATOM 5434 C C   . GLY B 1 185 ? -35.198 0.422   146.158 1.00 38.95  ? 231 GLY B C   1 
ATOM 5435 O O   . GLY B 1 185 ? -35.632 0.786   147.255 1.00 41.42  ? 231 GLY B O   1 
ATOM 5436 N N   . LEU B 1 186 ? -33.906 0.244   145.899 1.00 36.49  ? 232 LEU B N   1 
ATOM 5437 C CA  . LEU B 1 186 ? -32.842 0.580   146.834 1.00 30.07  ? 232 LEU B CA  1 
ATOM 5438 C C   . LEU B 1 186 ? -32.045 1.742   146.262 1.00 35.50  ? 232 LEU B C   1 
ATOM 5439 O O   . LEU B 1 186 ? -31.715 1.745   145.072 1.00 43.38  ? 232 LEU B O   1 
ATOM 5440 C CB  . LEU B 1 186 ? -31.931 -0.621  147.081 1.00 32.64  ? 232 LEU B CB  1 
ATOM 5441 C CG  . LEU B 1 186 ? -32.591 -1.811  147.772 1.00 36.90  ? 232 LEU B CG  1 
ATOM 5442 C CD1 . LEU B 1 186 ? -31.585 -2.926  147.968 1.00 37.49  ? 232 LEU B CD1 1 
ATOM 5443 C CD2 . LEU B 1 186 ? -33.175 -1.378  149.100 1.00 42.28  ? 232 LEU B CD2 1 
ATOM 5444 N N   . TYR B 1 187 ? -31.742 2.725   147.104 1.00 27.56  ? 233 TYR B N   1 
ATOM 5445 C CA  . TYR B 1 187 ? -31.156 3.977   146.650 1.00 30.77  ? 233 TYR B CA  1 
ATOM 5446 C C   . TYR B 1 187 ? -29.865 4.249   147.404 1.00 38.65  ? 233 TYR B C   1 
ATOM 5447 O O   . TYR B 1 187 ? -29.829 4.155   148.634 1.00 42.59  ? 233 TYR B O   1 
ATOM 5448 C CB  . TYR B 1 187 ? -32.147 5.128   146.836 1.00 28.36  ? 233 TYR B CB  1 
ATOM 5449 C CG  . TYR B 1 187 ? -33.455 4.887   146.121 1.00 32.47  ? 233 TYR B CG  1 
ATOM 5450 C CD1 . TYR B 1 187 ? -33.528 4.931   144.736 1.00 31.36  ? 233 TYR B CD1 1 
ATOM 5451 C CD2 . TYR B 1 187 ? -34.608 4.582   146.828 1.00 37.43  ? 233 TYR B CD2 1 
ATOM 5452 C CE1 . TYR B 1 187 ? -34.716 4.699   144.078 1.00 34.85  ? 233 TYR B CE1 1 
ATOM 5453 C CE2 . TYR B 1 187 ? -35.801 4.347   146.178 1.00 36.18  ? 233 TYR B CE2 1 
ATOM 5454 C CZ  . TYR B 1 187 ? -35.849 4.407   144.804 1.00 38.64  ? 233 TYR B CZ  1 
ATOM 5455 O OH  . TYR B 1 187 ? -37.036 4.174   144.150 1.00 45.30  ? 233 TYR B OH  1 
ATOM 5456 N N   . VAL B 1 188 ? -28.815 4.584   146.664 1.00 35.68  ? 234 VAL B N   1 
ATOM 5457 C CA  . VAL B 1 188 ? -27.506 4.881   147.230 1.00 27.90  ? 234 VAL B CA  1 
ATOM 5458 C C   . VAL B 1 188 ? -27.367 6.386   147.399 1.00 30.99  ? 234 VAL B C   1 
ATOM 5459 O O   . VAL B 1 188 ? -27.850 7.174   146.579 1.00 44.38  ? 234 VAL B O   1 
ATOM 5460 C CB  . VAL B 1 188 ? -26.375 4.316   146.346 1.00 28.39  ? 234 VAL B CB  1 
ATOM 5461 C CG1 . VAL B 1 188 ? -26.224 2.825   146.570 1.00 36.65  ? 234 VAL B CG1 1 
ATOM 5462 C CG2 . VAL B 1 188 ? -26.655 4.608   144.884 1.00 31.77  ? 234 VAL B CG2 1 
ATOM 5463 N N   . ASP B 1 189 ? -26.697 6.792   148.480 1.00 28.16  ? 235 ASP B N   1 
ATOM 5464 C CA  . ASP B 1 189 ? -26.456 8.211   148.716 1.00 31.48  ? 235 ASP B CA  1 
ATOM 5465 C C   . ASP B 1 189 ? -25.439 8.787   147.741 1.00 36.16  ? 235 ASP B C   1 
ATOM 5466 O O   . ASP B 1 189 ? -25.495 9.981   147.428 1.00 42.02  ? 235 ASP B O   1 
ATOM 5467 C CB  . ASP B 1 189 ? -25.991 8.435   150.155 1.00 32.66  ? 235 ASP B CB  1 
ATOM 5468 C CG  . ASP B 1 189 ? -24.720 7.681   150.479 1.00 42.25  ? 235 ASP B CG  1 
ATOM 5469 O OD1 . ASP B 1 189 ? -24.564 6.543   149.991 1.00 49.00  ? 235 ASP B OD1 1 
ATOM 5470 O OD2 . ASP B 1 189 ? -23.876 8.223   151.223 1.00 41.12  ? 235 ASP B OD2 1 
ATOM 5471 N N   . GLN B 1 190 ? -24.507 7.968   147.262 1.00 38.19  ? 236 GLN B N   1 
ATOM 5472 C CA  . GLN B 1 190 ? -23.531 8.376   146.264 1.00 37.67  ? 236 GLN B CA  1 
ATOM 5473 C C   . GLN B 1 190 ? -23.417 7.293   145.204 1.00 45.22  ? 236 GLN B C   1 
ATOM 5474 O O   . GLN B 1 190 ? -23.758 6.132   145.442 1.00 53.99  ? 236 GLN B O   1 
ATOM 5475 C CB  . GLN B 1 190 ? -22.153 8.632   146.882 1.00 42.99  ? 236 GLN B CB  1 
ATOM 5476 C CG  . GLN B 1 190 ? -22.107 9.790   147.856 1.00 48.89  ? 236 GLN B CG  1 
ATOM 5477 C CD  . GLN B 1 190 ? -20.797 9.857   148.608 1.00 51.05  ? 236 GLN B CD  1 
ATOM 5478 O OE1 . GLN B 1 190 ? -19.760 10.199  148.041 1.00 47.28  ? 236 GLN B OE1 1 
ATOM 5479 N NE2 . GLN B 1 190 ? -20.834 9.527   149.894 1.00 51.30  ? 236 GLN B NE2 1 
ATOM 5480 N N   . ASP B 1 191 ? -22.929 7.679   144.029 1.00 51.59  ? 237 ASP B N   1 
ATOM 5481 C CA  . ASP B 1 191 ? -22.731 6.731   142.934 1.00 54.17  ? 237 ASP B CA  1 
ATOM 5482 C C   . ASP B 1 191 ? -21.366 6.051   143.058 1.00 57.25  ? 237 ASP B C   1 
ATOM 5483 O O   . ASP B 1 191 ? -20.552 6.033   142.136 1.00 62.12  ? 237 ASP B O   1 
ATOM 5484 C CB  . ASP B 1 191 ? -22.883 7.434   141.591 1.00 54.23  ? 237 ASP B CB  1 
ATOM 5485 C CG  . ASP B 1 191 ? -23.535 6.554   140.547 1.00 58.27  ? 237 ASP B CG  1 
ATOM 5486 O OD1 . ASP B 1 191 ? -23.263 5.336   140.542 1.00 57.85  ? 237 ASP B OD1 1 
ATOM 5487 O OD2 . ASP B 1 191 ? -24.320 7.078   139.729 1.00 60.26  ? 237 ASP B OD2 1 
ATOM 5488 N N   . VAL B 1 192 ? -21.129 5.480   144.238 1.00 47.19  ? 238 VAL B N   1 
ATOM 5489 C CA  . VAL B 1 192 ? -19.898 4.765   144.543 1.00 44.35  ? 238 VAL B CA  1 
ATOM 5490 C C   . VAL B 1 192 ? -20.259 3.351   144.980 1.00 49.86  ? 238 VAL B C   1 
ATOM 5491 O O   . VAL B 1 192 ? -21.412 3.045   145.286 1.00 53.61  ? 238 VAL B O   1 
ATOM 5492 C CB  . VAL B 1 192 ? -19.057 5.475   145.624 1.00 45.37  ? 238 VAL B CB  1 
ATOM 5493 C CG1 . VAL B 1 192 ? -19.010 6.971   145.365 1.00 46.81  ? 238 VAL B CG1 1 
ATOM 5494 C CG2 . VAL B 1 192 ? -19.615 5.191   147.005 1.00 47.50  ? 238 VAL B CG2 1 
ATOM 5495 N N   . THR B 1 193 ? -19.248 2.480   144.992 1.00 47.52  ? 239 THR B N   1 
ATOM 5496 C CA  . THR B 1 193 ? -19.489 1.074   145.303 1.00 42.57  ? 239 THR B CA  1 
ATOM 5497 C C   . THR B 1 193 ? -19.838 0.882   146.774 1.00 44.38  ? 239 THR B C   1 
ATOM 5498 O O   . THR B 1 193 ? -20.790 0.169   147.109 1.00 43.00  ? 239 THR B O   1 
ATOM 5499 C CB  . THR B 1 193 ? -18.268 0.237   144.930 1.00 43.70  ? 239 THR B CB  1 
ATOM 5500 O OG1 . THR B 1 193 ? -17.656 0.781   143.755 1.00 46.77  ? 239 THR B OG1 1 
ATOM 5501 C CG2 . THR B 1 193 ? -18.678 -1.200  144.658 1.00 44.79  ? 239 THR B CG2 1 
ATOM 5502 N N   . ARG B 1 194 ? -19.077 1.506   147.667 1.00 40.04  ? 240 ARG B N   1 
ATOM 5503 C CA  . ARG B 1 194 ? -19.317 1.384   149.104 1.00 37.96  ? 240 ARG B CA  1 
ATOM 5504 C C   . ARG B 1 194 ? -20.229 2.495   149.610 1.00 39.38  ? 240 ARG B C   1 
ATOM 5505 O O   . ARG B 1 194 ? -19.913 3.203   150.564 1.00 43.22  ? 240 ARG B O   1 
ATOM 5506 C CB  . ARG B 1 194 ? -17.991 1.383   149.852 1.00 33.99  ? 240 ARG B CB  1 
ATOM 5507 C CG  . ARG B 1 194 ? -17.073 0.229   149.496 1.00 33.14  ? 240 ARG B CG  1 
ATOM 5508 C CD  . ARG B 1 194 ? -15.633 0.694   149.399 1.00 39.86  ? 240 ARG B CD  1 
ATOM 5509 N NE  . ARG B 1 194 ? -15.141 1.184   150.681 1.00 43.25  ? 240 ARG B NE  1 
ATOM 5510 C CZ  . ARG B 1 194 ? -14.890 2.458   150.948 1.00 41.76  ? 240 ARG B CZ  1 
ATOM 5511 N NH1 . ARG B 1 194 ? -15.069 3.402   150.040 1.00 39.75  ? 240 ARG B NH1 1 
ATOM 5512 N NH2 . ARG B 1 194 ? -14.449 2.792   152.157 1.00 38.81  ? 240 ARG B NH2 1 
ATOM 5513 N N   . ALA B 1 195 ? -21.380 2.648   148.968 1.00 32.96  ? 241 ALA B N   1 
ATOM 5514 C CA  . ALA B 1 195 ? -22.330 3.687   149.325 1.00 26.63  ? 241 ALA B CA  1 
ATOM 5515 C C   . ALA B 1 195 ? -23.298 3.186   150.390 1.00 31.14  ? 241 ALA B C   1 
ATOM 5516 O O   . ALA B 1 195 ? -23.340 2.002   150.727 1.00 42.17  ? 241 ALA B O   1 
ATOM 5517 C CB  . ALA B 1 195 ? -23.095 4.160   148.090 1.00 29.93  ? 241 ALA B CB  1 
ATOM 5518 N N   . GLN B 1 196 ? -24.086 4.112   150.922 1.00 26.91  ? 242 GLN B N   1 
ATOM 5519 C CA  . GLN B 1 196 ? -25.092 3.803   151.925 1.00 31.56  ? 242 GLN B CA  1 
ATOM 5520 C C   . GLN B 1 196 ? -26.460 3.705   151.266 1.00 36.93  ? 242 GLN B C   1 
ATOM 5521 O O   . GLN B 1 196 ? -26.805 4.515   150.403 1.00 47.96  ? 242 GLN B O   1 
ATOM 5522 C CB  . GLN B 1 196 ? -25.102 4.862   153.025 1.00 32.21  ? 242 GLN B CB  1 
ATOM 5523 C CG  . GLN B 1 196 ? -24.032 4.645   154.075 1.00 26.69  ? 242 GLN B CG  1 
ATOM 5524 C CD  . GLN B 1 196 ? -22.786 5.457   153.810 1.00 33.82  ? 242 GLN B CD  1 
ATOM 5525 O OE1 . GLN B 1 196 ? -22.597 5.988   152.717 1.00 45.54  ? 242 GLN B OE1 1 
ATOM 5526 N NE2 . GLN B 1 196 ? -21.919 5.549   154.809 1.00 34.79  ? 242 GLN B NE2 1 
ATOM 5527 N N   . ILE B 1 197 ? -27.235 2.708   151.680 1.00 30.34  ? 243 ILE B N   1 
ATOM 5528 C CA  . ILE B 1 197 ? -28.490 2.357   151.029 1.00 23.52  ? 243 ILE B CA  1 
ATOM 5529 C C   . ILE B 1 197 ? -29.630 3.098   151.711 1.00 26.27  ? 243 ILE B C   1 
ATOM 5530 O O   . ILE B 1 197 ? -29.718 3.122   152.944 1.00 29.42  ? 243 ILE B O   1 
ATOM 5531 C CB  . ILE B 1 197 ? -28.723 0.838   151.062 1.00 29.24  ? 243 ILE B CB  1 
ATOM 5532 C CG1 . ILE B 1 197 ? -27.631 0.120   150.275 1.00 31.66  ? 243 ILE B CG1 1 
ATOM 5533 C CG2 . ILE B 1 197 ? -30.090 0.492   150.508 1.00 36.43  ? 243 ILE B CG2 1 
ATOM 5534 C CD1 . ILE B 1 197 ? -27.696 0.366   148.794 1.00 27.56  ? 243 ILE B CD1 1 
ATOM 5535 N N   . TYR B 1 198 ? -30.495 3.710   150.909 1.00 34.93  ? 244 TYR B N   1 
ATOM 5536 C CA  . TYR B 1 198 ? -31.716 4.335   151.394 1.00 34.15  ? 244 TYR B CA  1 
ATOM 5537 C C   . TYR B 1 198 ? -32.895 3.433   151.057 1.00 35.59  ? 244 TYR B C   1 
ATOM 5538 O O   . TYR B 1 198 ? -32.988 2.919   149.938 1.00 38.01  ? 244 TYR B O   1 
ATOM 5539 C CB  . TYR B 1 198 ? -31.902 5.718   150.774 1.00 28.88  ? 244 TYR B CB  1 
ATOM 5540 C CG  . TYR B 1 198 ? -31.254 6.825   151.567 1.00 31.83  ? 244 TYR B CG  1 
ATOM 5541 C CD1 . TYR B 1 198 ? -31.681 7.124   152.851 1.00 34.48  ? 244 TYR B CD1 1 
ATOM 5542 C CD2 . TYR B 1 198 ? -30.211 7.568   151.033 1.00 27.36  ? 244 TYR B CD2 1 
ATOM 5543 C CE1 . TYR B 1 198 ? -31.091 8.134   153.579 1.00 25.47  ? 244 TYR B CE1 1 
ATOM 5544 C CE2 . TYR B 1 198 ? -29.616 8.578   151.753 1.00 25.41  ? 244 TYR B CE2 1 
ATOM 5545 C CZ  . TYR B 1 198 ? -30.060 8.857   153.024 1.00 25.83  ? 244 TYR B CZ  1 
ATOM 5546 O OH  . TYR B 1 198 ? -29.470 9.864   153.746 1.00 41.47  ? 244 TYR B OH  1 
ATOM 5547 N N   . MET B 1 199 ? -33.788 3.241   152.023 1.00 38.87  ? 245 MET B N   1 
ATOM 5548 C CA  . MET B 1 199 ? -34.879 2.289   151.895 1.00 38.79  ? 245 MET B CA  1 
ATOM 5549 C C   . MET B 1 199 ? -36.173 2.908   152.398 1.00 41.70  ? 245 MET B C   1 
ATOM 5550 O O   . MET B 1 199 ? -36.162 3.827   153.221 1.00 49.35  ? 245 MET B O   1 
ATOM 5551 C CB  . MET B 1 199 ? -34.579 1.003   152.669 1.00 37.21  ? 245 MET B CB  1 
ATOM 5552 C CG  . MET B 1 199 ? -35.175 -0.251  152.066 1.00 42.53  ? 245 MET B CG  1 
ATOM 5553 S SD  . MET B 1 199 ? -34.249 -1.717  152.546 1.00 62.81  ? 245 MET B SD  1 
ATOM 5554 C CE  . MET B 1 199 ? -34.358 -1.602  154.328 1.00 44.17  ? 245 MET B CE  1 
ATOM 5555 N N   . PHE B 1 200 ? -37.292 2.392   151.894 1.00 31.57  ? 246 PHE B N   1 
ATOM 5556 C CA  . PHE B 1 200 ? -38.619 2.848   152.286 1.00 24.09  ? 246 PHE B CA  1 
ATOM 5557 C C   . PHE B 1 200 ? -39.418 1.661   152.803 1.00 35.66  ? 246 PHE B C   1 
ATOM 5558 O O   . PHE B 1 200 ? -39.547 0.649   152.108 1.00 46.34  ? 246 PHE B O   1 
ATOM 5559 C CB  . PHE B 1 200 ? -39.349 3.499   151.108 1.00 33.12  ? 246 PHE B CB  1 
ATOM 5560 C CG  . PHE B 1 200 ? -38.939 4.920   150.851 1.00 33.62  ? 246 PHE B CG  1 
ATOM 5561 C CD1 . PHE B 1 200 ? -39.553 5.963   151.517 1.00 35.18  ? 246 PHE B CD1 1 
ATOM 5562 C CD2 . PHE B 1 200 ? -37.943 5.211   149.935 1.00 31.90  ? 246 PHE B CD2 1 
ATOM 5563 C CE1 . PHE B 1 200 ? -39.179 7.269   151.280 1.00 32.15  ? 246 PHE B CE1 1 
ATOM 5564 C CE2 . PHE B 1 200 ? -37.566 6.514   149.694 1.00 30.44  ? 246 PHE B CE2 1 
ATOM 5565 C CZ  . PHE B 1 200 ? -38.184 7.544   150.367 1.00 30.09  ? 246 PHE B CZ  1 
ATOM 5566 N N   . LYS B 1 201 ? -39.957 1.789   154.014 1.00 32.84  ? 247 LYS B N   1 
ATOM 5567 C CA  . LYS B 1 201 ? -40.743 0.729   154.626 1.00 37.45  ? 247 LYS B CA  1 
ATOM 5568 C C   . LYS B 1 201 ? -42.063 1.310   155.117 1.00 36.96  ? 247 LYS B C   1 
ATOM 5569 O O   . LYS B 1 201 ? -42.061 2.304   155.863 1.00 45.18  ? 247 LYS B O   1 
ATOM 5570 C CB  . LYS B 1 201 ? -39.986 0.071   155.787 1.00 28.98  ? 247 LYS B CB  1 
ATOM 5571 C CG  . LYS B 1 201 ? -40.373 -1.374  156.037 1.00 29.42  ? 247 LYS B CG  1 
ATOM 5572 C CD  . LYS B 1 201 ? -41.255 -1.510  157.262 1.00 28.48  ? 247 LYS B CD  1 
ATOM 5573 C CE  . LYS B 1 201 ? -40.476 -1.275  158.537 1.00 35.56  ? 247 LYS B CE  1 
ATOM 5574 N NZ  . LYS B 1 201 ? -41.345 -1.413  159.733 1.00 39.77  ? 247 LYS B NZ  1 
ATOM 5575 N N   . PRO B 1 202 ? -43.201 0.735   154.730 1.00 25.76  ? 248 PRO B N   1 
ATOM 5576 C CA  . PRO B 1 202 ? -44.497 1.253   155.194 1.00 26.33  ? 248 PRO B CA  1 
ATOM 5577 C C   . PRO B 1 202 ? -44.720 0.931   156.664 1.00 30.60  ? 248 PRO B C   1 
ATOM 5578 O O   . PRO B 1 202 ? -44.702 -0.233  157.067 1.00 42.19  ? 248 PRO B O   1 
ATOM 5579 C CB  . PRO B 1 202 ? -45.510 0.532   154.299 1.00 32.34  ? 248 PRO B CB  1 
ATOM 5580 C CG  . PRO B 1 202 ? -44.806 -0.695  153.839 1.00 26.76  ? 248 PRO B CG  1 
ATOM 5581 C CD  . PRO B 1 202 ? -43.355 -0.343  153.739 1.00 23.39  ? 248 PRO B CD  1 
ATOM 5582 N N   . THR B 1 203 ? -44.930 1.973   157.468 1.00 31.03  ? 249 THR B N   1 
ATOM 5583 C CA  . THR B 1 203 ? -45.225 1.771   158.881 1.00 32.06  ? 249 THR B CA  1 
ATOM 5584 C C   . THR B 1 203 ? -46.657 1.311   159.110 1.00 40.25  ? 249 THR B C   1 
ATOM 5585 O O   . THR B 1 203 ? -46.935 0.637   160.106 1.00 46.13  ? 249 THR B O   1 
ATOM 5586 C CB  . THR B 1 203 ? -44.978 3.057   159.667 1.00 31.72  ? 249 THR B CB  1 
ATOM 5587 O OG1 . THR B 1 203 ? -43.874 3.764   159.094 1.00 35.17  ? 249 THR B OG1 1 
ATOM 5588 C CG2 . THR B 1 203 ? -44.666 2.736   161.117 1.00 34.17  ? 249 THR B CG2 1 
ATOM 5589 N N   . MET B 1 204 ? -47.574 1.662   158.214 1.00 42.79  ? 250 MET B N   1 
ATOM 5590 C CA  . MET B 1 204 ? -48.985 1.396   158.434 1.00 37.05  ? 250 MET B CA  1 
ATOM 5591 C C   . MET B 1 204 ? -49.650 1.093   157.103 1.00 45.31  ? 250 MET B C   1 
ATOM 5592 O O   . MET B 1 204 ? -49.327 1.693   156.075 1.00 52.72  ? 250 MET B O   1 
ATOM 5593 C CB  . MET B 1 204 ? -49.673 2.588   159.108 1.00 35.47  ? 250 MET B CB  1 
ATOM 5594 C CG  . MET B 1 204 ? -51.107 2.811   158.665 1.00 46.55  ? 250 MET B CG  1 
ATOM 5595 S SD  . MET B 1 204 ? -51.999 3.900   159.771 1.00 68.05  ? 250 MET B SD  1 
ATOM 5596 C CE  . MET B 1 204 ? -50.694 5.048   160.154 1.00 53.27  ? 250 MET B CE  1 
ATOM 5597 N N   . LEU B 1 205 ? -50.590 0.153   157.134 1.00 44.03  ? 251 LEU B N   1 
ATOM 5598 C CA  . LEU B 1 205 ? -51.422 -0.155  155.983 1.00 40.90  ? 251 LEU B CA  1 
ATOM 5599 C C   . LEU B 1 205 ? -52.867 0.191   156.322 1.00 44.23  ? 251 LEU B C   1 
ATOM 5600 O O   . LEU B 1 205 ? -53.183 0.613   157.438 1.00 51.62  ? 251 LEU B O   1 
ATOM 5601 C CB  . LEU B 1 205 ? -51.273 -1.620  155.557 1.00 45.41  ? 251 LEU B CB  1 
ATOM 5602 C CG  . LEU B 1 205 ? -50.118 -1.941  154.600 1.00 43.11  ? 251 LEU B CG  1 
ATOM 5603 C CD1 . LEU B 1 205 ? -50.429 -1.407  153.229 1.00 46.26  ? 251 LEU B CD1 1 
ATOM 5604 C CD2 . LEU B 1 205 ? -48.791 -1.392  155.066 1.00 42.41  ? 251 LEU B CD2 1 
ATOM 5605 N N   . TRP B 1 206 ? -53.757 -0.004  155.351 1.00 34.94  ? 252 TRP B N   1 
ATOM 5606 C CA  . TRP B 1 206 ? -55.105 0.558   155.387 1.00 37.93  ? 252 TRP B CA  1 
ATOM 5607 C C   . TRP B 1 206 ? -56.151 -0.543  155.207 1.00 46.21  ? 252 TRP B C   1 
ATOM 5608 O O   . TRP B 1 206 ? -56.971 -0.499  154.292 1.00 57.60  ? 252 TRP B O   1 
ATOM 5609 C CB  . TRP B 1 206 ? -55.277 1.661   154.345 1.00 45.31  ? 252 TRP B CB  1 
ATOM 5610 C CG  . TRP B 1 206 ? -54.578 2.937   154.707 1.00 44.89  ? 252 TRP B CG  1 
ATOM 5611 C CD1 . TRP B 1 206 ? -53.631 3.590   153.977 1.00 43.50  ? 252 TRP B CD1 1 
ATOM 5612 C CD2 . TRP B 1 206 ? -54.780 3.720   155.891 1.00 41.16  ? 252 TRP B CD2 1 
ATOM 5613 N NE1 . TRP B 1 206 ? -53.227 4.726   154.633 1.00 42.39  ? 252 TRP B NE1 1 
ATOM 5614 C CE2 . TRP B 1 206 ? -53.918 4.828   155.811 1.00 40.92  ? 252 TRP B CE2 1 
ATOM 5615 C CE3 . TRP B 1 206 ? -55.605 3.589   157.012 1.00 40.84  ? 252 TRP B CE3 1 
ATOM 5616 C CZ2 . TRP B 1 206 ? -53.857 5.798   156.806 1.00 40.03  ? 252 TRP B CZ2 1 
ATOM 5617 C CZ3 . TRP B 1 206 ? -55.542 4.551   157.997 1.00 39.29  ? 252 TRP B CZ3 1 
ATOM 5618 C CH2 . TRP B 1 206 ? -54.675 5.642   157.889 1.00 37.62  ? 252 TRP B CH2 1 
ATOM 5619 N N   . LYS B 1 207 ? -56.067 -1.573  156.053 1.00 42.89  ? 253 LYS B N   1 
ATOM 5620 C CA  . LYS B 1 207 ? -57.105 -2.597  156.129 1.00 39.41  ? 253 LYS B CA  1 
ATOM 5621 C C   . LYS B 1 207 ? -58.493 -1.983  156.013 1.00 44.09  ? 253 LYS B C   1 
ATOM 5622 O O   . LYS B 1 207 ? -58.800 -0.982  156.663 1.00 51.31  ? 253 LYS B O   1 
ATOM 5623 C CB  . LYS B 1 207 ? -56.992 -3.358  157.449 1.00 40.79  ? 253 LYS B CB  1 
ATOM 5624 C CG  . LYS B 1 207 ? -57.722 -4.682  157.456 1.00 44.66  ? 253 LYS B CG  1 
ATOM 5625 C CD  . LYS B 1 207 ? -58.156 -5.051  158.861 1.00 47.11  ? 253 LYS B CD  1 
ATOM 5626 C CE  . LYS B 1 207 ? -59.216 -6.140  158.839 1.00 50.79  ? 253 LYS B CE  1 
ATOM 5627 N NZ  . LYS B 1 207 ? -59.948 -6.182  157.543 1.00 50.25  ? 253 LYS B NZ  1 
ATOM 5628 N N   . TYR B 1 208 ? -59.336 -2.598  155.185 1.00 54.11  ? 254 TYR B N   1 
ATOM 5629 C CA  . TYR B 1 208 ? -60.611 -1.984  154.839 1.00 60.02  ? 254 TYR B CA  1 
ATOM 5630 C C   . TYR B 1 208 ? -61.600 -2.015  155.998 1.00 59.96  ? 254 TYR B C   1 
ATOM 5631 O O   . TYR B 1 208 ? -62.032 -0.958  156.464 1.00 64.93  ? 254 TYR B O   1 
ATOM 5632 C CB  . TYR B 1 208 ? -61.202 -2.662  153.600 1.00 57.34  ? 254 TYR B CB  1 
ATOM 5633 C CG  . TYR B 1 208 ? -62.181 -1.792  152.841 1.00 57.87  ? 254 TYR B CG  1 
ATOM 5634 C CD1 . TYR B 1 208 ? -63.335 -1.314  153.444 1.00 60.00  ? 254 TYR B CD1 1 
ATOM 5635 C CD2 . TYR B 1 208 ? -61.926 -1.413  151.534 1.00 56.87  ? 254 TYR B CD2 1 
ATOM 5636 C CE1 . TYR B 1 208 ? -64.222 -0.514  152.756 1.00 66.29  ? 254 TYR B CE1 1 
ATOM 5637 C CE2 . TYR B 1 208 ? -62.806 -0.609  150.838 1.00 61.71  ? 254 TYR B CE2 1 
ATOM 5638 C CZ  . TYR B 1 208 ? -63.952 -0.163  151.454 1.00 68.16  ? 254 TYR B CZ  1 
ATOM 5639 O OH  . TYR B 1 208 ? -64.832 0.638   150.764 1.00 67.32  ? 254 TYR B OH  1 
ATOM 5640 N N   . GLU B 1 209 ? -61.971 -3.206  156.467 1.00 65.93  ? 255 GLU B N   1 
ATOM 5641 C CA  . GLU B 1 209 ? -62.899 -3.361  157.588 1.00 71.96  ? 255 GLU B CA  1 
ATOM 5642 C C   . GLU B 1 209 ? -64.220 -2.638  157.291 1.00 72.66  ? 255 GLU B C   1 
ATOM 5643 O O   . GLU B 1 209 ? -64.607 -1.662  157.936 1.00 68.59  ? 255 GLU B O   1 
ATOM 5644 C CB  . GLU B 1 209 ? -62.246 -2.878  158.892 1.00 68.24  ? 255 GLU B CB  1 
ATOM 5645 C CG  . GLU B 1 209 ? -63.089 -3.040  160.149 1.00 73.81  ? 255 GLU B CG  1 
ATOM 5646 C CD  . GLU B 1 209 ? -63.444 -1.710  160.783 1.00 74.07  ? 255 GLU B CD  1 
ATOM 5647 O OE1 . GLU B 1 209 ? -63.225 -0.665  160.136 1.00 73.55  ? 255 GLU B OE1 1 
ATOM 5648 O OE2 . GLU B 1 209 ? -63.942 -1.707  161.928 1.00 75.86  ? 255 GLU B OE2 1 
ATOM 5649 N N   . ASN B 1 210 ? -64.887 -3.134  156.251 1.00 80.77  ? 256 ASN B N   1 
ATOM 5650 C CA  . ASN B 1 210 ? -66.178 -2.594  155.838 1.00 80.15  ? 256 ASN B CA  1 
ATOM 5651 C C   . ASN B 1 210 ? -67.285 -3.237  156.663 1.00 81.54  ? 256 ASN B C   1 
ATOM 5652 O O   . ASN B 1 210 ? -67.430 -4.464  156.670 1.00 77.05  ? 256 ASN B O   1 
ATOM 5653 C CB  . ASN B 1 210 ? -66.400 -2.838  154.349 1.00 80.53  ? 256 ASN B CB  1 
ATOM 5654 C CG  . ASN B 1 210 ? -67.763 -2.372  153.878 1.00 80.04  ? 256 ASN B CG  1 
ATOM 5655 O OD1 . ASN B 1 210 ? -67.959 -1.198  153.574 1.00 80.31  ? 256 ASN B OD1 1 
ATOM 5656 N ND2 . ASN B 1 210 ? -68.714 -3.296  153.815 1.00 77.21  ? 256 ASN B ND2 1 
ATOM 5657 N N   . LEU B 1 211 ? -68.068 -2.414  157.356 1.00 89.64  ? 257 LEU B N   1 
ATOM 5658 C CA  . LEU B 1 211 ? -69.147 -2.917  158.191 1.00 89.03  ? 257 LEU B CA  1 
ATOM 5659 C C   . LEU B 1 211 ? -70.150 -1.803  158.450 1.00 87.40  ? 257 LEU B C   1 
ATOM 5660 O O   . LEU B 1 211 ? -69.824 -0.617  158.352 1.00 85.77  ? 257 LEU B O   1 
ATOM 5661 C CB  . LEU B 1 211 ? -68.611 -3.480  159.515 1.00 89.75  ? 257 LEU B CB  1 
ATOM 5662 C CG  . LEU B 1 211 ? -67.753 -2.561  160.393 1.00 88.76  ? 257 LEU B CG  1 
ATOM 5663 C CD1 . LEU B 1 211 ? -68.594 -1.765  161.387 1.00 85.86  ? 257 LEU B CD1 1 
ATOM 5664 C CD2 . LEU B 1 211 ? -66.683 -3.365  161.116 1.00 85.26  ? 257 LEU B CD2 1 
ATOM 5665 N N   . GLY B 1 212 ? -71.376 -2.202  158.779 1.00 88.84  ? 258 GLY B N   1 
ATOM 5666 C CA  . GLY B 1 212 ? -72.400 -1.266  159.197 1.00 90.32  ? 258 GLY B CA  1 
ATOM 5667 C C   . GLY B 1 212 ? -72.952 -0.387  158.095 1.00 90.65  ? 258 GLY B C   1 
ATOM 5668 O O   . GLY B 1 212 ? -72.317 -0.201  157.052 1.00 93.26  ? 258 GLY B O   1 
ATOM 5669 N N   . THR B 1 213 ? -74.149 0.161   158.319 1.00 89.77  ? 259 THR B N   1 
ATOM 5670 C CA  . THR B 1 213 ? -74.719 1.119   157.381 1.00 93.02  ? 259 THR B CA  1 
ATOM 5671 C C   . THR B 1 213 ? -74.012 2.465   157.437 1.00 93.05  ? 259 THR B C   1 
ATOM 5672 O O   . THR B 1 213 ? -74.224 3.301   156.551 1.00 88.02  ? 259 THR B O   1 
ATOM 5673 C CB  . THR B 1 213 ? -76.211 1.311   157.661 1.00 92.81  ? 259 THR B CB  1 
ATOM 5674 O OG1 . THR B 1 213 ? -76.757 2.253   156.730 1.00 92.54  ? 259 THR B OG1 1 
ATOM 5675 C CG2 . THR B 1 213 ? -76.423 1.827   159.075 1.00 91.62  ? 259 THR B CG2 1 
ATOM 5676 N N   . THR B 1 214 ? -73.183 2.693   158.450 1.00 90.95  ? 260 THR B N   1 
ATOM 5677 C CA  . THR B 1 214 ? -72.477 3.962   158.620 1.00 90.14  ? 260 THR B CA  1 
ATOM 5678 C C   . THR B 1 214 ? -71.207 4.016   157.777 1.00 90.29  ? 260 THR B C   1 
ATOM 5679 O O   . THR B 1 214 ? -70.125 4.337   158.265 1.00 88.57  ? 260 THR B O   1 
ATOM 5680 C CB  . THR B 1 214 ? -72.162 4.181   160.094 1.00 87.90  ? 260 THR B CB  1 
ATOM 5681 O OG1 . THR B 1 214 ? -71.469 3.038   160.610 1.00 82.94  ? 260 THR B OG1 1 
ATOM 5682 C CG2 . THR B 1 214 ? -73.443 4.390   160.884 1.00 85.99  ? 260 THR B CG2 1 
ATOM 5683 N N   . GLY B 1 215 ? -71.340 3.700   156.493 1.00 82.31  ? 261 GLY B N   1 
ATOM 5684 C CA  . GLY B 1 215 ? -70.228 3.795   155.575 1.00 80.76  ? 261 GLY B CA  1 
ATOM 5685 C C   . GLY B 1 215 ? -69.100 2.828   155.899 1.00 78.51  ? 261 GLY B C   1 
ATOM 5686 O O   . GLY B 1 215 ? -69.270 1.807   156.565 1.00 77.22  ? 261 GLY B O   1 
ATOM 5687 N N   . THR B 1 216 ? -67.920 3.186   155.405 1.00 65.52  ? 262 THR B N   1 
ATOM 5688 C CA  . THR B 1 216 ? -66.703 2.413   155.587 1.00 63.96  ? 262 THR B CA  1 
ATOM 5689 C C   . THR B 1 216 ? -65.716 3.197   156.448 1.00 67.91  ? 262 THR B C   1 
ATOM 5690 O O   . THR B 1 216 ? -65.907 4.382   156.733 1.00 70.19  ? 262 THR B O   1 
ATOM 5691 C CB  . THR B 1 216 ? -66.088 2.054   154.234 1.00 63.31  ? 262 THR B CB  1 
ATOM 5692 O OG1 . THR B 1 216 ? -65.200 3.097   153.821 1.00 67.72  ? 262 THR B OG1 1 
ATOM 5693 C CG2 . THR B 1 216 ? -67.171 1.889   153.182 1.00 61.33  ? 262 THR B CG2 1 
ATOM 5694 N N   . LYS B 1 217 ? -64.647 2.519   156.863 1.00 49.51  ? 263 LYS B N   1 
ATOM 5695 C CA  . LYS B 1 217 ? -63.644 3.132   157.732 1.00 42.17  ? 263 LYS B CA  1 
ATOM 5696 C C   . LYS B 1 217 ? -62.351 2.341   157.595 1.00 47.99  ? 263 LYS B C   1 
ATOM 5697 O O   . LYS B 1 217 ? -62.294 1.183   158.017 1.00 61.45  ? 263 LYS B O   1 
ATOM 5698 C CB  . LYS B 1 217 ? -64.126 3.152   159.177 1.00 47.87  ? 263 LYS B CB  1 
ATOM 5699 C CG  . LYS B 1 217 ? -63.031 3.404   160.197 1.00 51.38  ? 263 LYS B CG  1 
ATOM 5700 C CD  . LYS B 1 217 ? -63.612 3.848   161.528 1.00 53.45  ? 263 LYS B CD  1 
ATOM 5701 C CE  . LYS B 1 217 ? -64.698 2.898   162.002 1.00 50.94  ? 263 LYS B CE  1 
ATOM 5702 N NZ  . LYS B 1 217 ? -64.212 1.494   162.084 1.00 51.43  ? 263 LYS B NZ  1 
ATOM 5703 N N   . LEU B 1 218 ? -61.318 2.966   157.033 1.00 45.69  ? 264 LEU B N   1 
ATOM 5704 C CA  . LEU B 1 218 ? -60.033 2.304   156.800 1.00 41.43  ? 264 LEU B CA  1 
ATOM 5705 C C   . LEU B 1 218 ? -59.211 2.372   158.079 1.00 41.57  ? 264 LEU B C   1 
ATOM 5706 O O   . LEU B 1 218 ? -58.568 3.378   158.381 1.00 48.41  ? 264 LEU B O   1 
ATOM 5707 C CB  . LEU B 1 218 ? -59.295 2.953   155.636 1.00 37.07  ? 264 LEU B CB  1 
ATOM 5708 C CG  . LEU B 1 218 ? -59.888 2.803   154.235 1.00 39.50  ? 264 LEU B CG  1 
ATOM 5709 C CD1 . LEU B 1 218 ? -58.796 2.890   153.189 1.00 35.52  ? 264 LEU B CD1 1 
ATOM 5710 C CD2 . LEU B 1 218 ? -60.658 1.509   154.098 1.00 43.83  ? 264 LEU B CD2 1 
ATOM 5711 N N   . VAL B 1 219 ? -59.227 1.287   158.841 1.00 42.75  ? 265 VAL B N   1 
ATOM 5712 C CA  . VAL B 1 219 ? -58.509 1.266   160.121 1.00 45.91  ? 265 VAL B CA  1 
ATOM 5713 C C   . VAL B 1 219 ? -57.027 1.017   159.867 1.00 51.51  ? 265 VAL B C   1 
ATOM 5714 O O   . VAL B 1 219 ? -56.673 0.376   158.862 1.00 51.74  ? 265 VAL B O   1 
ATOM 5715 C CB  . VAL B 1 219 ? -59.096 0.199   161.044 1.00 51.65  ? 265 VAL B CB  1 
ATOM 5716 C CG1 . VAL B 1 219 ? -60.412 0.677   161.631 1.00 50.58  ? 265 VAL B CG1 1 
ATOM 5717 C CG2 . VAL B 1 219 ? -59.288 -1.103  160.289 1.00 55.48  ? 265 VAL B CG2 1 
ATOM 5718 N N   . PRO B 1 220 ? -56.138 1.509   160.726 1.00 56.82  ? 266 PRO B N   1 
ATOM 5719 C CA  . PRO B 1 220 ? -54.708 1.221   160.566 1.00 47.02  ? 266 PRO B CA  1 
ATOM 5720 C C   . PRO B 1 220 ? -54.416 -0.269  160.671 1.00 49.31  ? 266 PRO B C   1 
ATOM 5721 O O   . PRO B 1 220 ? -55.093 -1.005  161.392 1.00 55.02  ? 266 PRO B O   1 
ATOM 5722 C CB  . PRO B 1 220 ? -54.054 1.987   161.723 1.00 40.53  ? 266 PRO B CB  1 
ATOM 5723 C CG  . PRO B 1 220 ? -55.125 2.779   162.385 1.00 52.02  ? 266 PRO B CG  1 
ATOM 5724 C CD  . PRO B 1 220 ? -56.391 2.648   161.620 1.00 54.51  ? 266 PRO B CD  1 
ATOM 5725 N N   . LEU B 1 221 ? -53.394 -0.710  159.943 1.00 40.99  ? 267 LEU B N   1 
ATOM 5726 C CA  . LEU B 1 221 ? -52.835 -2.049  160.092 1.00 35.96  ? 267 LEU B CA  1 
ATOM 5727 C C   . LEU B 1 221 ? -51.340 -1.915  160.329 1.00 47.63  ? 267 LEU B C   1 
ATOM 5728 O O   . LEU B 1 221 ? -50.629 -1.329  159.505 1.00 52.73  ? 267 LEU B O   1 
ATOM 5729 C CB  . LEU B 1 221 ? -53.105 -2.912  158.858 1.00 39.29  ? 267 LEU B CB  1 
ATOM 5730 C CG  . LEU B 1 221 ? -52.528 -4.328  158.931 1.00 38.76  ? 267 LEU B CG  1 
ATOM 5731 C CD1 . LEU B 1 221 ? -53.360 -5.193  159.863 1.00 38.25  ? 267 LEU B CD1 1 
ATOM 5732 C CD2 . LEU B 1 221 ? -52.429 -4.959  157.555 1.00 41.56  ? 267 LEU B CD2 1 
ATOM 5733 N N   . MET B 1 222 ? -50.864 -2.460  161.443 1.00 45.91  ? 268 MET B N   1 
ATOM 5734 C CA  . MET B 1 222 ? -49.461 -2.341  161.797 1.00 34.60  ? 268 MET B CA  1 
ATOM 5735 C C   . MET B 1 222 ? -48.605 -3.231  160.901 1.00 39.21  ? 268 MET B C   1 
ATOM 5736 O O   . MET B 1 222 ? -49.090 -4.171  160.267 1.00 45.47  ? 268 MET B O   1 
ATOM 5737 C CB  . MET B 1 222 ? -49.245 -2.717  163.263 1.00 41.08  ? 268 MET B CB  1 
ATOM 5738 C CG  . MET B 1 222 ? -49.334 -1.558  164.253 1.00 47.39  ? 268 MET B CG  1 
ATOM 5739 S SD  . MET B 1 222 ? -49.120 0.095   163.561 1.00 40.81  ? 268 MET B SD  1 
ATOM 5740 C CE  . MET B 1 222 ? -47.363 0.107   163.213 1.00 41.58  ? 268 MET B CE  1 
ATOM 5741 N N   . MET B 1 223 ? -47.315 -2.919  160.853 1.00 46.74  ? 269 MET B N   1 
ATOM 5742 C CA  . MET B 1 223 ? -46.348 -3.706  160.106 1.00 46.67  ? 269 MET B CA  1 
ATOM 5743 C C   . MET B 1 223 ? -45.127 -3.988  160.965 1.00 50.38  ? 269 MET B C   1 
ATOM 5744 O O   . MET B 1 223 ? -44.853 -3.253  161.919 1.00 53.57  ? 269 MET B O   1 
ATOM 5745 C CB  . MET B 1 223 ? -45.920 -2.993  158.816 1.00 39.95  ? 269 MET B CB  1 
ATOM 5746 C CG  . MET B 1 223 ? -47.066 -2.698  157.884 1.00 42.57  ? 269 MET B CG  1 
ATOM 5747 S SD  . MET B 1 223 ? -47.621 -4.199  157.060 1.00 53.05  ? 269 MET B SD  1 
ATOM 5748 C CE  . MET B 1 223 ? -46.635 -4.151  155.571 1.00 48.52  ? 269 MET B CE  1 
ATOM 5749 N N   . PRO B 1 224 ? -44.385 -5.056  160.663 1.00 47.46  ? 270 PRO B N   1 
ATOM 5750 C CA  . PRO B 1 224 ? -43.217 -5.399  161.485 1.00 43.98  ? 270 PRO B CA  1 
ATOM 5751 C C   . PRO B 1 224 ? -42.181 -4.285  161.472 1.00 46.82  ? 270 PRO B C   1 
ATOM 5752 O O   . PRO B 1 224 ? -41.789 -3.793  160.412 1.00 47.64  ? 270 PRO B O   1 
ATOM 5753 C CB  . PRO B 1 224 ? -42.679 -6.674  160.826 1.00 40.01  ? 270 PRO B CB  1 
ATOM 5754 C CG  . PRO B 1 224 ? -43.826 -7.222  160.057 1.00 39.69  ? 270 PRO B CG  1 
ATOM 5755 C CD  . PRO B 1 224 ? -44.598 -6.037  159.586 1.00 48.62  ? 270 PRO B CD  1 
ATOM 5756 N N   . LYS B 1 225 ? -41.739 -3.896  162.663 1.00 49.24  ? 271 LYS B N   1 
ATOM 5757 C CA  . LYS B 1 225 ? -40.677 -2.915  162.799 1.00 46.20  ? 271 LYS B CA  1 
ATOM 5758 C C   . LYS B 1 225 ? -39.323 -3.595  162.623 1.00 48.12  ? 271 LYS B C   1 
ATOM 5759 O O   . LYS B 1 225 ? -39.216 -4.822  162.570 1.00 54.84  ? 271 LYS B O   1 
ATOM 5760 C CB  . LYS B 1 225 ? -40.773 -2.214  164.151 1.00 44.48  ? 271 LYS B CB  1 
ATOM 5761 C CG  . LYS B 1 225 ? -42.179 -1.785  164.523 1.00 46.99  ? 271 LYS B CG  1 
ATOM 5762 C CD  . LYS B 1 225 ? -42.159 -0.793  165.670 1.00 44.85  ? 271 LYS B CD  1 
ATOM 5763 C CE  . LYS B 1 225 ? -43.197 0.296   165.472 1.00 47.48  ? 271 LYS B CE  1 
ATOM 5764 N NZ  . LYS B 1 225 ? -43.332 0.669   164.038 1.00 51.75  ? 271 LYS B NZ  1 
ATOM 5765 N N   . ALA B 1 226 ? -38.272 -2.789  162.521 1.00 44.02  ? 272 ALA B N   1 
ATOM 5766 C CA  . ALA B 1 226 ? -36.934 -3.343  162.421 1.00 46.69  ? 272 ALA B CA  1 
ATOM 5767 C C   . ALA B 1 226 ? -36.537 -4.006  163.735 1.00 50.33  ? 272 ALA B C   1 
ATOM 5768 O O   . ALA B 1 226 ? -36.948 -3.591  164.821 1.00 58.09  ? 272 ALA B O   1 
ATOM 5769 C CB  . ALA B 1 226 ? -35.924 -2.261  162.048 1.00 41.75  ? 272 ALA B CB  1 
ATOM 5770 N N   . GLY B 1 227 ? -35.725 -5.052  163.622 1.00 45.34  ? 273 GLY B N   1 
ATOM 5771 C CA  . GLY B 1 227 ? -35.362 -5.819  164.795 1.00 51.37  ? 273 GLY B CA  1 
ATOM 5772 C C   . GLY B 1 227 ? -36.416 -6.797  165.253 1.00 52.17  ? 273 GLY B C   1 
ATOM 5773 O O   . GLY B 1 227 ? -36.321 -7.320  166.366 1.00 53.61  ? 273 GLY B O   1 
ATOM 5774 N N   . ASP B 1 228 ? -37.426 -7.056  164.428 1.00 54.07  ? 274 ASP B N   1 
ATOM 5775 C CA  . ASP B 1 228 ? -38.440 -8.064  164.706 1.00 57.24  ? 274 ASP B CA  1 
ATOM 5776 C C   . ASP B 1 228 ? -38.230 -9.223  163.746 1.00 57.39  ? 274 ASP B C   1 
ATOM 5777 O O   . ASP B 1 228 ? -38.239 -9.031  162.526 1.00 59.29  ? 274 ASP B O   1 
ATOM 5778 C CB  . ASP B 1 228 ? -39.851 -7.492  164.558 1.00 53.20  ? 274 ASP B CB  1 
ATOM 5779 C CG  . ASP B 1 228 ? -40.215 -6.547  165.683 1.00 61.46  ? 274 ASP B CG  1 
ATOM 5780 O OD1 . ASP B 1 228 ? -39.613 -6.659  166.771 1.00 67.05  ? 274 ASP B OD1 1 
ATOM 5781 O OD2 . ASP B 1 228 ? -41.105 -5.695  165.482 1.00 59.75  ? 274 ASP B OD2 1 
ATOM 5782 N N   . ASN B 1 229 ? -38.037 -10.422 164.296 1.00 49.84  ? 275 ASN B N   1 
ATOM 5783 C CA  . ASN B 1 229 ? -37.773 -11.608 163.483 1.00 47.64  ? 275 ASN B CA  1 
ATOM 5784 C C   . ASN B 1 229 ? -39.101 -12.239 163.065 1.00 52.17  ? 275 ASN B C   1 
ATOM 5785 O O   . ASN B 1 229 ? -39.445 -13.366 163.427 1.00 60.52  ? 275 ASN B O   1 
ATOM 5786 C CB  . ASN B 1 229 ? -36.894 -12.588 164.244 1.00 55.41  ? 275 ASN B CB  1 
ATOM 5787 C CG  . ASN B 1 229 ? -35.560 -11.989 164.632 1.00 56.18  ? 275 ASN B CG  1 
ATOM 5788 O OD1 . ASN B 1 229 ? -35.254 -10.850 164.282 1.00 47.04  ? 275 ASN B OD1 1 
ATOM 5789 N ND2 . ASN B 1 229 ? -34.757 -12.752 165.363 1.00 56.24  ? 275 ASN B ND2 1 
ATOM 5790 N N   . ARG B 1 230 ? -39.858 -11.478 162.283 1.00 50.63  ? 276 ARG B N   1 
ATOM 5791 C CA  . ARG B 1 230 ? -41.113 -11.957 161.732 1.00 51.02  ? 276 ARG B CA  1 
ATOM 5792 C C   . ARG B 1 230 ? -40.840 -12.918 160.585 1.00 55.23  ? 276 ARG B C   1 
ATOM 5793 O O   . ARG B 1 230 ? -39.914 -12.725 159.794 1.00 58.86  ? 276 ARG B O   1 
ATOM 5794 C CB  . ARG B 1 230 ? -41.976 -10.792 161.249 1.00 47.99  ? 276 ARG B CB  1 
ATOM 5795 C CG  . ARG B 1 230 ? -42.610 -9.993  162.371 1.00 53.64  ? 276 ARG B CG  1 
ATOM 5796 C CD  . ARG B 1 230 ? -43.360 -10.899 163.330 1.00 55.12  ? 276 ARG B CD  1 
ATOM 5797 N NE  . ARG B 1 230 ? -42.725 -10.950 164.640 1.00 57.23  ? 276 ARG B NE  1 
ATOM 5798 C CZ  . ARG B 1 230 ? -42.959 -10.085 165.617 1.00 58.93  ? 276 ARG B CZ  1 
ATOM 5799 N NH1 . ARG B 1 230 ? -43.819 -9.090  165.467 1.00 55.45  ? 276 ARG B NH1 1 
ATOM 5800 N NH2 . ARG B 1 230 ? -42.317 -10.222 166.773 1.00 57.39  ? 276 ARG B NH2 1 
ATOM 5801 N N   . LYS B 1 231 ? -41.656 -13.960 160.503 1.00 50.48  ? 277 LYS B N   1 
ATOM 5802 C CA  . LYS B 1 231 ? -41.444 -15.036 159.549 1.00 44.83  ? 277 LYS B CA  1 
ATOM 5803 C C   . LYS B 1 231 ? -42.598 -15.098 158.549 1.00 49.83  ? 277 LYS B C   1 
ATOM 5804 O O   . LYS B 1 231 ? -43.514 -14.261 158.550 1.00 54.70  ? 277 LYS B O   1 
ATOM 5805 C CB  . LYS B 1 231 ? -41.264 -16.367 160.282 1.00 44.99  ? 277 LYS B CB  1 
ATOM 5806 C CG  . LYS B 1 231 ? -40.064 -16.404 161.212 1.00 48.93  ? 277 LYS B CG  1 
ATOM 5807 C CD  . LYS B 1 231 ? -40.007 -17.709 161.986 1.00 49.85  ? 277 LYS B CD  1 
ATOM 5808 C CE  . LYS B 1 231 ? -38.873 -17.700 162.996 1.00 49.45  ? 277 LYS B CE  1 
ATOM 5809 N NZ  . LYS B 1 231 ? -38.985 -16.557 163.942 1.00 51.75  ? 277 LYS B NZ  1 
ATOM 5810 N N   . LEU B 1 232 ? -42.541 -16.114 157.687 1.00 40.33  ? 278 LEU B N   1 
ATOM 5811 C CA  . LEU B 1 232 ? -43.536 -16.254 156.635 1.00 39.52  ? 278 LEU B CA  1 
ATOM 5812 C C   . LEU B 1 232 ? -44.931 -16.470 157.200 1.00 43.43  ? 278 LEU B C   1 
ATOM 5813 O O   . LEU B 1 232 ? -45.910 -16.030 156.594 1.00 46.78  ? 278 LEU B O   1 
ATOM 5814 C CB  . LEU B 1 232 ? -43.160 -17.402 155.703 1.00 40.26  ? 278 LEU B CB  1 
ATOM 5815 C CG  . LEU B 1 232 ? -43.993 -17.464 154.427 1.00 36.24  ? 278 LEU B CG  1 
ATOM 5816 C CD1 . LEU B 1 232 ? -44.067 -16.092 153.798 1.00 43.72  ? 278 LEU B CD1 1 
ATOM 5817 C CD2 . LEU B 1 232 ? -43.399 -18.453 153.458 1.00 37.45  ? 278 LEU B CD2 1 
ATOM 5818 N N   . VAL B 1 233 ? -45.050 -17.138 158.349 1.00 52.54  ? 279 VAL B N   1 
ATOM 5819 C CA  . VAL B 1 233 ? -46.375 -17.313 158.935 1.00 48.08  ? 279 VAL B CA  1 
ATOM 5820 C C   . VAL B 1 233 ? -46.931 -15.975 159.407 1.00 48.17  ? 279 VAL B C   1 
ATOM 5821 O O   . VAL B 1 233 ? -48.127 -15.703 159.245 1.00 54.56  ? 279 VAL B O   1 
ATOM 5822 C CB  . VAL B 1 233 ? -46.340 -18.370 160.058 1.00 48.19  ? 279 VAL B CB  1 
ATOM 5823 C CG1 . VAL B 1 233 ? -45.531 -19.576 159.613 1.00 48.07  ? 279 VAL B CG1 1 
ATOM 5824 C CG2 . VAL B 1 233 ? -45.775 -17.805 161.351 1.00 49.11  ? 279 VAL B CG2 1 
ATOM 5825 N N   . ASP B 1 234 ? -46.083 -15.103 159.960 1.00 44.70  ? 280 ASP B N   1 
ATOM 5826 C CA  . ASP B 1 234 ? -46.543 -13.776 160.354 1.00 48.04  ? 280 ASP B CA  1 
ATOM 5827 C C   . ASP B 1 234 ? -46.953 -12.953 159.141 1.00 50.76  ? 280 ASP B C   1 
ATOM 5828 O O   . ASP B 1 234 ? -47.965 -12.243 159.177 1.00 53.90  ? 280 ASP B O   1 
ATOM 5829 C CB  . ASP B 1 234 ? -45.456 -13.056 161.149 1.00 47.18  ? 280 ASP B CB  1 
ATOM 5830 C CG  . ASP B 1 234 ? -44.857 -13.925 162.234 1.00 60.45  ? 280 ASP B CG  1 
ATOM 5831 O OD1 . ASP B 1 234 ? -45.590 -14.286 163.177 1.00 60.48  ? 280 ASP B OD1 1 
ATOM 5832 O OD2 . ASP B 1 234 ? -43.654 -14.251 162.143 1.00 66.46  ? 280 ASP B OD2 1 
ATOM 5833 N N   . PHE B 1 235 ? -46.186 -13.040 158.053 1.00 41.04  ? 281 PHE B N   1 
ATOM 5834 C CA  . PHE B 1 235 ? -46.556 -12.287 156.858 1.00 35.39  ? 281 PHE B CA  1 
ATOM 5835 C C   . PHE B 1 235 ? -47.827 -12.829 156.213 1.00 37.88  ? 281 PHE B C   1 
ATOM 5836 O O   . PHE B 1 235 ? -48.637 -12.053 155.695 1.00 38.43  ? 281 PHE B O   1 
ATOM 5837 C CB  . PHE B 1 235 ? -45.399 -12.281 155.866 1.00 35.25  ? 281 PHE B CB  1 
ATOM 5838 C CG  . PHE B 1 235 ? -44.377 -11.226 156.154 1.00 37.59  ? 281 PHE B CG  1 
ATOM 5839 C CD1 . PHE B 1 235 ? -43.477 -11.381 157.192 1.00 43.60  ? 281 PHE B CD1 1 
ATOM 5840 C CD2 . PHE B 1 235 ? -44.332 -10.068 155.403 1.00 39.29  ? 281 PHE B CD2 1 
ATOM 5841 C CE1 . PHE B 1 235 ? -42.542 -10.408 157.466 1.00 40.59  ? 281 PHE B CE1 1 
ATOM 5842 C CE2 . PHE B 1 235 ? -43.401 -9.092  155.673 1.00 41.78  ? 281 PHE B CE2 1 
ATOM 5843 C CZ  . PHE B 1 235 ? -42.505 -9.262  156.705 1.00 36.81  ? 281 PHE B CZ  1 
ATOM 5844 N N   . GLN B 1 236 ? -48.024 -14.148 156.240 1.00 42.64  ? 282 GLN B N   1 
ATOM 5845 C CA  . GLN B 1 236 ? -49.272 -14.722 155.752 1.00 40.33  ? 282 GLN B CA  1 
ATOM 5846 C C   . GLN B 1 236 ? -50.447 -14.280 156.611 1.00 45.45  ? 282 GLN B C   1 
ATOM 5847 O O   . GLN B 1 236 ? -51.532 -14.002 156.091 1.00 53.38  ? 282 GLN B O   1 
ATOM 5848 C CB  . GLN B 1 236 ? -49.173 -16.245 155.724 1.00 36.00  ? 282 GLN B CB  1 
ATOM 5849 C CG  . GLN B 1 236 ? -48.435 -16.793 154.520 1.00 41.40  ? 282 GLN B CG  1 
ATOM 5850 C CD  . GLN B 1 236 ? -48.165 -18.277 154.630 1.00 48.03  ? 282 GLN B CD  1 
ATOM 5851 O OE1 . GLN B 1 236 ? -48.155 -18.838 155.725 1.00 48.02  ? 282 GLN B OE1 1 
ATOM 5852 N NE2 . GLN B 1 236 ? -47.944 -18.923 153.492 1.00 49.06  ? 282 GLN B NE2 1 
ATOM 5853 N N   . VAL B 1 237 ? -50.248 -14.214 157.929 1.00 39.50  ? 283 VAL B N   1 
ATOM 5854 C CA  . VAL B 1 237 ? -51.292 -13.709 158.814 1.00 41.88  ? 283 VAL B CA  1 
ATOM 5855 C C   . VAL B 1 237 ? -51.627 -12.267 158.463 1.00 42.74  ? 283 VAL B C   1 
ATOM 5856 O O   . VAL B 1 237 ? -52.801 -11.883 158.407 1.00 44.19  ? 283 VAL B O   1 
ATOM 5857 C CB  . VAL B 1 237 ? -50.855 -13.852 160.284 1.00 41.97  ? 283 VAL B CB  1 
ATOM 5858 C CG1 . VAL B 1 237 ? -51.611 -12.872 161.166 1.00 44.27  ? 283 VAL B CG1 1 
ATOM 5859 C CG2 . VAL B 1 237 ? -51.059 -15.279 160.759 1.00 41.28  ? 283 VAL B CG2 1 
ATOM 5860 N N   . LEU B 1 238 ? -50.602 -11.449 158.214 1.00 43.33  ? 284 LEU B N   1 
ATOM 5861 C CA  . LEU B 1 238 ? -50.837 -10.057 157.841 1.00 41.35  ? 284 LEU B CA  1 
ATOM 5862 C C   . LEU B 1 238 ? -51.616 -9.954  156.535 1.00 43.18  ? 284 LEU B C   1 
ATOM 5863 O O   . LEU B 1 238 ? -52.559 -9.162  156.431 1.00 46.89  ? 284 LEU B O   1 
ATOM 5864 C CB  . LEU B 1 238 ? -49.511 -9.308  157.728 1.00 39.72  ? 284 LEU B CB  1 
ATOM 5865 C CG  . LEU B 1 238 ? -48.903 -8.799  159.034 1.00 43.40  ? 284 LEU B CG  1 
ATOM 5866 C CD1 . LEU B 1 238 ? -47.514 -8.238  158.788 1.00 42.29  ? 284 LEU B CD1 1 
ATOM 5867 C CD2 . LEU B 1 238 ? -49.799 -7.755  159.675 1.00 49.17  ? 284 LEU B CD2 1 
ATOM 5868 N N   . PHE B 1 239 ? -51.241 -10.746 155.528 1.00 36.35  ? 285 PHE B N   1 
ATOM 5869 C CA  . PHE B 1 239 ? -51.953 -10.696 154.253 1.00 29.62  ? 285 PHE B CA  1 
ATOM 5870 C C   . PHE B 1 239 ? -53.399 -11.148 154.402 1.00 39.06  ? 285 PHE B C   1 
ATOM 5871 O O   . PHE B 1 239 ? -54.314 -10.510 153.866 1.00 44.91  ? 285 PHE B O   1 
ATOM 5872 C CB  . PHE B 1 239 ? -51.237 -11.550 153.212 1.00 33.50  ? 285 PHE B CB  1 
ATOM 5873 C CG  . PHE B 1 239 ? -51.870 -11.501 151.853 1.00 41.41  ? 285 PHE B CG  1 
ATOM 5874 C CD1 . PHE B 1 239 ? -52.018 -10.299 151.186 1.00 37.87  ? 285 PHE B CD1 1 
ATOM 5875 C CD2 . PHE B 1 239 ? -52.319 -12.658 151.242 1.00 40.06  ? 285 PHE B CD2 1 
ATOM 5876 C CE1 . PHE B 1 239 ? -52.600 -10.250 149.935 1.00 35.32  ? 285 PHE B CE1 1 
ATOM 5877 C CE2 . PHE B 1 239 ? -52.903 -12.616 149.992 1.00 41.96  ? 285 PHE B CE2 1 
ATOM 5878 C CZ  . PHE B 1 239 ? -53.043 -11.411 149.338 1.00 40.38  ? 285 PHE B CZ  1 
ATOM 5879 N N   . ASN B 1 240 ? -53.626 -12.247 155.125 1.00 45.56  ? 286 ASN B N   1 
ATOM 5880 C CA  . ASN B 1 240 ? -54.984 -12.739 155.320 1.00 45.05  ? 286 ASN B CA  1 
ATOM 5881 C C   . ASN B 1 240 ? -55.828 -11.741 156.096 1.00 44.61  ? 286 ASN B C   1 
ATOM 5882 O O   . ASN B 1 240 ? -57.018 -11.583 155.806 1.00 46.96  ? 286 ASN B O   1 
ATOM 5883 C CB  . ASN B 1 240 ? -54.953 -14.086 156.040 1.00 41.11  ? 286 ASN B CB  1 
ATOM 5884 C CG  . ASN B 1 240 ? -54.246 -15.156 155.237 1.00 48.99  ? 286 ASN B CG  1 
ATOM 5885 O OD1 . ASN B 1 240 ? -54.249 -15.127 154.007 1.00 50.41  ? 286 ASN B OD1 1 
ATOM 5886 N ND2 . ASN B 1 240 ? -53.629 -16.106 155.929 1.00 45.41  ? 286 ASN B ND2 1 
ATOM 5887 N N   . ASN B 1 241 ? -55.233 -11.066 157.080 1.00 43.22  ? 287 ASN B N   1 
ATOM 5888 C CA  . ASN B 1 241 ? -55.934 -10.007 157.791 1.00 35.82  ? 287 ASN B CA  1 
ATOM 5889 C C   . ASN B 1 241 ? -56.256 -8.849  156.853 1.00 38.13  ? 287 ASN B C   1 
ATOM 5890 O O   . ASN B 1 241 ? -57.344 -8.269  156.934 1.00 45.91  ? 287 ASN B O   1 
ATOM 5891 C CB  . ASN B 1 241 ? -55.073 -9.564  158.981 1.00 41.41  ? 287 ASN B CB  1 
ATOM 5892 C CG  . ASN B 1 241 ? -55.715 -8.478  159.833 1.00 46.54  ? 287 ASN B CG  1 
ATOM 5893 O OD1 . ASN B 1 241 ? -56.386 -7.579  159.338 1.00 51.09  ? 287 ASN B OD1 1 
ATOM 5894 N ND2 . ASN B 1 241 ? -55.500 -8.567  161.139 1.00 46.95  ? 287 ASN B ND2 1 
ATOM 5895 N N   . LEU B 1 242 ? -55.334 -8.516  155.948 1.00 35.66  ? 288 LEU B N   1 
ATOM 5896 C CA  . LEU B 1 242 ? -55.566 -7.420  155.012 1.00 38.73  ? 288 LEU B CA  1 
ATOM 5897 C C   . LEU B 1 242 ? -56.715 -7.722  154.058 1.00 42.31  ? 288 LEU B C   1 
ATOM 5898 O O   . LEU B 1 242 ? -57.552 -6.851  153.795 1.00 41.08  ? 288 LEU B O   1 
ATOM 5899 C CB  . LEU B 1 242 ? -54.286 -7.126  154.230 1.00 38.43  ? 288 LEU B CB  1 
ATOM 5900 C CG  . LEU B 1 242 ? -54.182 -5.763  153.546 1.00 38.43  ? 288 LEU B CG  1 
ATOM 5901 C CD1 . LEU B 1 242 ? -54.405 -4.641  154.541 1.00 39.15  ? 288 LEU B CD1 1 
ATOM 5902 C CD2 . LEU B 1 242 ? -52.832 -5.613  152.868 1.00 40.69  ? 288 LEU B CD2 1 
ATOM 5903 N N   . VAL B 1 243 ? -56.778 -8.940  153.528 1.00 51.92  ? 289 VAL B N   1 
ATOM 5904 C CA  . VAL B 1 243 ? -57.779 -9.288  152.522 1.00 45.04  ? 289 VAL B CA  1 
ATOM 5905 C C   . VAL B 1 243 ? -58.865 -10.206 153.090 1.00 44.29  ? 289 VAL B C   1 
ATOM 5906 O O   . VAL B 1 243 ? -59.522 -10.921 152.336 1.00 45.90  ? 289 VAL B O   1 
ATOM 5907 C CB  . VAL B 1 243 ? -57.134 -9.902  151.271 1.00 38.36  ? 289 VAL B CB  1 
ATOM 5908 C CG1 . VAL B 1 243 ? -56.163 -8.924  150.647 1.00 39.72  ? 289 VAL B CG1 1 
ATOM 5909 C CG2 . VAL B 1 243 ? -56.433 -11.203 151.617 1.00 42.86  ? 289 VAL B CG2 1 
ATOM 5910 N N   . SER B 1 244 ? -59.068 -10.193 154.408 1.00 52.38  ? 290 SER B N   1 
ATOM 5911 C CA  . SER B 1 244 ? -60.107 -11.029 155.002 1.00 50.55  ? 290 SER B CA  1 
ATOM 5912 C C   . SER B 1 244 ? -61.492 -10.604 154.530 1.00 58.26  ? 290 SER B C   1 
ATOM 5913 O O   . SER B 1 244 ? -62.331 -11.447 154.191 1.00 58.06  ? 290 SER B O   1 
ATOM 5914 C CB  . SER B 1 244 ? -60.019 -10.972 156.526 1.00 49.41  ? 290 SER B CB  1 
ATOM 5915 O OG  . SER B 1 244 ? -60.942 -10.037 157.055 1.00 60.18  ? 290 SER B OG  1 
ATOM 5916 N N   . THR B 1 245 ? -61.746 -9.298  154.497 1.00 57.43  ? 291 THR B N   1 
ATOM 5917 C CA  . THR B 1 245 ? -63.032 -8.751  154.094 1.00 53.07  ? 291 THR B CA  1 
ATOM 5918 C C   . THR B 1 245 ? -63.021 -8.218  152.669 1.00 54.47  ? 291 THR B C   1 
ATOM 5919 O O   . THR B 1 245 ? -63.934 -7.479  152.286 1.00 59.27  ? 291 THR B O   1 
ATOM 5920 C CB  . THR B 1 245 ? -63.456 -7.640  155.056 1.00 54.27  ? 291 THR B CB  1 
ATOM 5921 O OG1 . THR B 1 245 ? -64.737 -7.130  154.666 1.00 56.17  ? 291 THR B OG1 1 
ATOM 5922 C CG2 . THR B 1 245 ? -62.439 -6.512  155.036 1.00 56.71  ? 291 THR B CG2 1 
ATOM 5923 N N   . MET B 1 246 ? -62.010 -8.566  151.882 1.00 53.58  ? 292 MET B N   1 
ATOM 5924 C CA  . MET B 1 246 ? -61.821 -7.985  150.560 1.00 53.65  ? 292 MET B CA  1 
ATOM 5925 C C   . MET B 1 246 ? -61.850 -9.012  149.438 1.00 51.53  ? 292 MET B C   1 
ATOM 5926 O O   . MET B 1 246 ? -62.256 -8.685  148.321 1.00 48.40  ? 292 MET B O   1 
ATOM 5927 C CB  . MET B 1 246 ? -60.497 -7.213  150.534 1.00 53.54  ? 292 MET B CB  1 
ATOM 5928 C CG  . MET B 1 246 ? -60.049 -6.714  149.183 1.00 54.87  ? 292 MET B CG  1 
ATOM 5929 S SD  . MET B 1 246 ? -58.967 -5.293  149.396 1.00 64.31  ? 292 MET B SD  1 
ATOM 5930 C CE  . MET B 1 246 ? -59.253 -4.420  147.866 1.00 54.45  ? 292 MET B CE  1 
ATOM 5931 N N   . LEU B 1 247 ? -61.453 -10.251 149.710 1.00 55.47  ? 293 LEU B N   1 
ATOM 5932 C CA  . LEU B 1 247 ? -61.465 -11.312 148.714 1.00 51.24  ? 293 LEU B CA  1 
ATOM 5933 C C   . LEU B 1 247 ? -62.810 -12.028 148.711 1.00 55.61  ? 293 LEU B C   1 
ATOM 5934 O O   . LEU B 1 247 ? -63.375 -12.336 149.763 1.00 55.81  ? 293 LEU B O   1 
ATOM 5935 C CB  . LEU B 1 247 ? -60.349 -12.323 148.980 1.00 44.98  ? 293 LEU B CB  1 
ATOM 5936 C CG  . LEU B 1 247 ? -59.010 -12.125 148.268 1.00 46.98  ? 293 LEU B CG  1 
ATOM 5937 C CD1 . LEU B 1 247 ? -57.971 -13.073 148.835 1.00 46.82  ? 293 LEU B CD1 1 
ATOM 5938 C CD2 . LEU B 1 247 ? -59.153 -12.327 146.773 1.00 44.91  ? 293 LEU B CD2 1 
ATOM 5939 N N   . GLY B 1 248 ? -63.320 -12.288 147.510 1.00 58.78  ? 294 GLY B N   1 
ATOM 5940 C CA  . GLY B 1 248 ? -64.566 -13.010 147.360 1.00 53.29  ? 294 GLY B CA  1 
ATOM 5941 C C   . GLY B 1 248 ? -65.815 -12.231 147.701 1.00 58.47  ? 294 GLY B C   1 
ATOM 5942 O O   . GLY B 1 248 ? -66.859 -12.846 147.942 1.00 56.51  ? 294 GLY B O   1 
ATOM 5943 N N   . ASP B 1 249 ? -65.747 -10.904 147.729 1.00 66.85  ? 295 ASP B N   1 
ATOM 5944 C CA  . ASP B 1 249 ? -66.889 -10.066 148.068 1.00 66.82  ? 295 ASP B CA  1 
ATOM 5945 C C   . ASP B 1 249 ? -67.568 -9.614  146.782 1.00 68.01  ? 295 ASP B C   1 
ATOM 5946 O O   . ASP B 1 249 ? -66.900 -9.148  145.853 1.00 69.10  ? 295 ASP B O   1 
ATOM 5947 C CB  . ASP B 1 249 ? -66.457 -8.860  148.901 1.00 68.78  ? 295 ASP B CB  1 
ATOM 5948 C CG  . ASP B 1 249 ? -67.499 -8.457  149.921 1.00 73.82  ? 295 ASP B CG  1 
ATOM 5949 O OD1 . ASP B 1 249 ? -68.597 -8.025  149.514 1.00 72.67  ? 295 ASP B OD1 1 
ATOM 5950 O OD2 . ASP B 1 249 ? -67.229 -8.591  151.132 1.00 73.70  ? 295 ASP B OD2 1 
ATOM 5951 N N   . GLU B 1 250 ? -68.893 -9.763  146.727 1.00 68.28  ? 296 GLU B N   1 
ATOM 5952 C CA  . GLU B 1 250 ? -69.623 -9.459  145.501 1.00 69.52  ? 296 GLU B CA  1 
ATOM 5953 C C   . GLU B 1 250 ? -69.570 -7.978  145.148 1.00 68.55  ? 296 GLU B C   1 
ATOM 5954 O O   . GLU B 1 250 ? -69.380 -7.635  143.977 1.00 74.75  ? 296 GLU B O   1 
ATOM 5955 C CB  . GLU B 1 250 ? -71.071 -9.937  145.621 1.00 68.91  ? 296 GLU B CB  1 
ATOM 5956 C CG  . GLU B 1 250 ? -71.240 -11.443 145.872 1.00 72.73  ? 296 GLU B CG  1 
ATOM 5957 C CD  . GLU B 1 250 ? -70.232 -12.325 145.135 1.00 73.76  ? 296 GLU B CD  1 
ATOM 5958 O OE1 . GLU B 1 250 ? -69.863 -13.384 145.680 1.00 68.34  ? 296 GLU B OE1 1 
ATOM 5959 O OE2 . GLU B 1 250 ? -69.857 -12.004 143.984 1.00 74.05  ? 296 GLU B OE2 1 
ATOM 5960 N N   . ASP B 1 251 ? -69.741 -7.087  146.129 1.00 65.85  ? 297 ASP B N   1 
ATOM 5961 C CA  . ASP B 1 251 ? -69.675 -5.660  145.827 1.00 66.08  ? 297 ASP B CA  1 
ATOM 5962 C C   . ASP B 1 251 ? -68.279 -5.266  145.364 1.00 66.83  ? 297 ASP B C   1 
ATOM 5963 O O   . ASP B 1 251 ? -68.125 -4.423  144.472 1.00 67.69  ? 297 ASP B O   1 
ATOM 5964 C CB  . ASP B 1 251 ? -70.083 -4.833  147.045 1.00 63.55  ? 297 ASP B CB  1 
ATOM 5965 C CG  . ASP B 1 251 ? -69.563 -5.409  148.340 1.00 68.70  ? 297 ASP B CG  1 
ATOM 5966 O OD1 . ASP B 1 251 ? -68.327 -5.503  148.487 1.00 71.07  ? 297 ASP B OD1 1 
ATOM 5967 O OD2 . ASP B 1 251 ? -70.384 -5.748  149.216 1.00 70.97  ? 297 ASP B OD2 1 
ATOM 5968 N N   . PHE B 1 252 ? -67.250 -5.861  145.968 1.00 61.12  ? 298 PHE B N   1 
ATOM 5969 C CA  . PHE B 1 252 ? -65.883 -5.583  145.547 1.00 54.97  ? 298 PHE B CA  1 
ATOM 5970 C C   . PHE B 1 252 ? -65.637 -6.067  144.126 1.00 54.90  ? 298 PHE B C   1 
ATOM 5971 O O   . PHE B 1 252 ? -64.968 -5.387  143.340 1.00 54.65  ? 298 PHE B O   1 
ATOM 5972 C CB  . PHE B 1 252 ? -64.900 -6.236  146.511 1.00 58.75  ? 298 PHE B CB  1 
ATOM 5973 C CG  . PHE B 1 252 ? -64.313 -5.284  147.498 1.00 59.37  ? 298 PHE B CG  1 
ATOM 5974 C CD1 . PHE B 1 252 ? -64.967 -5.015  148.686 1.00 57.91  ? 298 PHE B CD1 1 
ATOM 5975 C CD2 . PHE B 1 252 ? -63.120 -4.641  147.232 1.00 57.58  ? 298 PHE B CD2 1 
ATOM 5976 C CE1 . PHE B 1 252 ? -64.435 -4.135  149.596 1.00 60.11  ? 298 PHE B CE1 1 
ATOM 5977 C CE2 . PHE B 1 252 ? -62.587 -3.758  148.139 1.00 57.76  ? 298 PHE B CE2 1 
ATOM 5978 C CZ  . PHE B 1 252 ? -63.243 -3.508  149.321 1.00 60.62  ? 298 PHE B CZ  1 
ATOM 5979 N N   . GLY B 1 253 ? -66.157 -7.246  143.784 1.00 53.20  ? 299 GLY B N   1 
ATOM 5980 C CA  . GLY B 1 253 ? -66.058 -7.713  142.412 1.00 53.84  ? 299 GLY B CA  1 
ATOM 5981 C C   . GLY B 1 253 ? -66.787 -6.805  141.442 1.00 58.68  ? 299 GLY B C   1 
ATOM 5982 O O   . GLY B 1 253 ? -66.314 -6.559  140.331 1.00 60.61  ? 299 GLY B O   1 
ATOM 5983 N N   . ILE B 1 254 ? -67.946 -6.288  141.856 1.00 59.57  ? 300 ILE B N   1 
ATOM 5984 C CA  . ILE B 1 254 ? -68.687 -5.341  141.026 1.00 54.13  ? 300 ILE B CA  1 
ATOM 5985 C C   . ILE B 1 254 ? -67.858 -4.088  140.778 1.00 56.18  ? 300 ILE B C   1 
ATOM 5986 O O   . ILE B 1 254 ? -67.754 -3.607  139.642 1.00 57.72  ? 300 ILE B O   1 
ATOM 5987 C CB  . ILE B 1 254 ? -70.037 -5.000  141.685 1.00 48.63  ? 300 ILE B CB  1 
ATOM 5988 C CG1 . ILE B 1 254 ? -71.007 -6.182  141.594 1.00 53.41  ? 300 ILE B CG1 1 
ATOM 5989 C CG2 . ILE B 1 254 ? -70.644 -3.763  141.050 1.00 57.81  ? 300 ILE B CG2 1 
ATOM 5990 C CD1 . ILE B 1 254 ? -70.835 -7.040  140.359 1.00 56.73  ? 300 ILE B CD1 1 
ATOM 5991 N N   . MET B 1 255 ? -67.255 -3.540  141.835 1.00 54.45  ? 301 MET B N   1 
ATOM 5992 C CA  . MET B 1 255 ? -66.441 -2.338  141.683 1.00 47.43  ? 301 MET B CA  1 
ATOM 5993 C C   . MET B 1 255 ? -65.220 -2.598  140.810 1.00 50.14  ? 301 MET B C   1 
ATOM 5994 O O   . MET B 1 255 ? -64.859 -1.763  139.972 1.00 56.87  ? 301 MET B O   1 
ATOM 5995 C CB  . MET B 1 255 ? -66.021 -1.806  143.052 1.00 43.07  ? 301 MET B CB  1 
ATOM 5996 C CG  . MET B 1 255 ? -67.018 -0.834  143.657 1.00 48.53  ? 301 MET B CG  1 
ATOM 5997 S SD  . MET B 1 255 ? -66.393 0.011   145.118 1.00 64.24  ? 301 MET B SD  1 
ATOM 5998 C CE  . MET B 1 255 ? -65.936 -1.380  146.145 1.00 53.30  ? 301 MET B CE  1 
ATOM 5999 N N   . SER B 1 256 ? -64.564 -3.746  140.995 1.00 46.44  ? 302 SER B N   1 
ATOM 6000 C CA  . SER B 1 256 ? -63.400 -4.070  140.176 1.00 47.16  ? 302 SER B CA  1 
ATOM 6001 C C   . SER B 1 256 ? -63.783 -4.230  138.711 1.00 49.05  ? 302 SER B C   1 
ATOM 6002 O O   . SER B 1 256 ? -63.058 -3.772  137.822 1.00 52.41  ? 302 SER B O   1 
ATOM 6003 C CB  . SER B 1 256 ? -62.724 -5.336  140.698 1.00 49.92  ? 302 SER B CB  1 
ATOM 6004 O OG  . SER B 1 256 ? -63.638 -6.415  140.755 1.00 61.50  ? 302 SER B OG  1 
ATOM 6005 N N   . GLY B 1 257 ? -64.920 -4.872  138.436 1.00 46.25  ? 303 GLY B N   1 
ATOM 6006 C CA  . GLY B 1 257 ? -65.378 -4.978  137.062 1.00 51.35  ? 303 GLY B CA  1 
ATOM 6007 C C   . GLY B 1 257 ? -65.714 -3.630  136.456 1.00 55.87  ? 303 GLY B C   1 
ATOM 6008 O O   . GLY B 1 257 ? -65.395 -3.365  135.294 1.00 55.16  ? 303 GLY B O   1 
ATOM 6009 N N   . ASP B 1 258 ? -66.362 -2.760  137.234 1.00 58.84  ? 304 ASP B N   1 
ATOM 6010 C CA  . ASP B 1 258 ? -66.676 -1.423  136.743 1.00 51.93  ? 304 ASP B CA  1 
ATOM 6011 C C   . ASP B 1 258 ? -65.409 -0.646  136.419 1.00 48.18  ? 304 ASP B C   1 
ATOM 6012 O O   . ASP B 1 258 ? -65.332 0.029   135.385 1.00 49.06  ? 304 ASP B O   1 
ATOM 6013 C CB  . ASP B 1 258 ? -67.515 -0.670  137.774 1.00 53.59  ? 304 ASP B CB  1 
ATOM 6014 C CG  . ASP B 1 258 ? -68.987 -1.016  137.692 1.00 64.54  ? 304 ASP B CG  1 
ATOM 6015 O OD1 . ASP B 1 258 ? -69.431 -1.484  136.623 1.00 65.79  ? 304 ASP B OD1 1 
ATOM 6016 O OD2 . ASP B 1 258 ? -69.702 -0.816  138.696 1.00 67.00  ? 304 ASP B OD2 1 
ATOM 6017 N N   . VAL B 1 259 ? -64.402 -0.736  137.289 1.00 45.03  ? 305 VAL B N   1 
ATOM 6018 C CA  . VAL B 1 259 ? -63.119 -0.102  137.015 1.00 45.75  ? 305 VAL B CA  1 
ATOM 6019 C C   . VAL B 1 259 ? -62.448 -0.710  135.790 1.00 49.20  ? 305 VAL B C   1 
ATOM 6020 O O   . VAL B 1 259 ? -61.798 0.012   135.029 1.00 55.79  ? 305 VAL B O   1 
ATOM 6021 C CB  . VAL B 1 259 ? -62.211 -0.195  138.253 1.00 44.32  ? 305 VAL B CB  1 
ATOM 6022 C CG1 . VAL B 1 259 ? -60.769 0.122   137.899 1.00 46.41  ? 305 VAL B CG1 1 
ATOM 6023 C CG2 . VAL B 1 259 ? -62.713 0.733   139.346 1.00 43.16  ? 305 VAL B CG2 1 
ATOM 6024 N N   . PHE B 1 260 ? -62.595 -2.019  135.572 1.00 47.85  ? 306 PHE B N   1 
ATOM 6025 C CA  . PHE B 1 260 ? -62.069 -2.641  134.360 1.00 47.54  ? 306 PHE B CA  1 
ATOM 6026 C C   . PHE B 1 260 ? -62.716 -2.060  133.108 1.00 51.55  ? 306 PHE B C   1 
ATOM 6027 O O   . PHE B 1 260 ? -62.016 -1.678  132.159 1.00 52.42  ? 306 PHE B O   1 
ATOM 6028 C CB  . PHE B 1 260 ? -62.289 -4.153  134.417 1.00 50.65  ? 306 PHE B CB  1 
ATOM 6029 C CG  . PHE B 1 260 ? -61.373 -4.937  133.524 1.00 51.96  ? 306 PHE B CG  1 
ATOM 6030 C CD1 . PHE B 1 260 ? -61.608 -5.009  132.162 1.00 52.35  ? 306 PHE B CD1 1 
ATOM 6031 C CD2 . PHE B 1 260 ? -60.293 -5.621  134.048 1.00 49.51  ? 306 PHE B CD2 1 
ATOM 6032 C CE1 . PHE B 1 260 ? -60.772 -5.731  131.339 1.00 53.39  ? 306 PHE B CE1 1 
ATOM 6033 C CE2 . PHE B 1 260 ? -59.453 -6.346  133.229 1.00 49.66  ? 306 PHE B CE2 1 
ATOM 6034 C CZ  . PHE B 1 260 ? -59.694 -6.402  131.872 1.00 52.63  ? 306 PHE B CZ  1 
ATOM 6035 N N   . LYS B 1 261 ? -64.051 -1.990  133.084 1.00 49.05  ? 307 LYS B N   1 
ATOM 6036 C CA  . LYS B 1 261 ? -64.730 -1.417  131.923 1.00 49.59  ? 307 LYS B CA  1 
ATOM 6037 C C   . LYS B 1 261 ? -64.331 0.037   131.713 1.00 54.71  ? 307 LYS B C   1 
ATOM 6038 O O   . LYS B 1 261 ? -64.130 0.470   130.573 1.00 62.14  ? 307 LYS B O   1 
ATOM 6039 C CB  . LYS B 1 261 ? -66.252 -1.523  132.049 1.00 51.16  ? 307 LYS B CB  1 
ATOM 6040 C CG  . LYS B 1 261 ? -66.861 -2.890  131.745 1.00 55.58  ? 307 LYS B CG  1 
ATOM 6041 C CD  . LYS B 1 261 ? -67.279 -3.622  133.002 1.00 60.82  ? 307 LYS B CD  1 
ATOM 6042 C CE  . LYS B 1 261 ? -68.285 -4.723  132.710 1.00 55.63  ? 307 LYS B CE  1 
ATOM 6043 N NZ  . LYS B 1 261 ? -68.388 -5.682  133.841 1.00 49.73  ? 307 LYS B NZ  1 
ATOM 6044 N N   . ALA B 1 262 ? -64.217 0.807   132.797 1.00 45.86  ? 308 ALA B N   1 
ATOM 6045 C CA  . ALA B 1 262 ? -63.778 2.194   132.678 1.00 41.94  ? 308 ALA B CA  1 
ATOM 6046 C C   . ALA B 1 262 ? -62.382 2.271   132.072 1.00 40.61  ? 308 ALA B C   1 
ATOM 6047 O O   . ALA B 1 262 ? -62.184 2.859   131.003 1.00 37.90  ? 308 ALA B O   1 
ATOM 6048 C CB  . ALA B 1 262 ? -63.819 2.873   134.046 1.00 46.92  ? 308 ALA B CB  1 
ATOM 6049 N N   . PHE B 1 263 ? -61.401 1.674   132.741 1.00 48.04  ? 309 PHE B N   1 
ATOM 6050 C CA  . PHE B 1 263 ? -60.030 1.585   132.252 1.00 46.45  ? 309 PHE B CA  1 
ATOM 6051 C C   . PHE B 1 263 ? -59.776 0.122   131.909 1.00 54.99  ? 309 PHE B C   1 
ATOM 6052 O O   . PHE B 1 263 ? -59.466 -0.684  132.788 1.00 62.02  ? 309 PHE B O   1 
ATOM 6053 C CB  . PHE B 1 263 ? -59.040 2.076   133.303 1.00 44.50  ? 309 PHE B CB  1 
ATOM 6054 C CG  . PHE B 1 263 ? -59.499 3.288   134.058 1.00 49.18  ? 309 PHE B CG  1 
ATOM 6055 C CD1 . PHE B 1 263 ? -60.234 3.155   135.223 1.00 46.21  ? 309 PHE B CD1 1 
ATOM 6056 C CD2 . PHE B 1 263 ? -59.189 4.559   133.611 1.00 52.01  ? 309 PHE B CD2 1 
ATOM 6057 C CE1 . PHE B 1 263 ? -60.657 4.263   135.923 1.00 44.18  ? 309 PHE B CE1 1 
ATOM 6058 C CE2 . PHE B 1 263 ? -59.608 5.672   134.310 1.00 49.93  ? 309 PHE B CE2 1 
ATOM 6059 C CZ  . PHE B 1 263 ? -60.343 5.523   135.467 1.00 44.06  ? 309 PHE B CZ  1 
ATOM 6060 N N   . GLY B 1 264 ? -59.944 -0.228  130.640 1.00 56.46  ? 310 GLY B N   1 
ATOM 6061 C CA  . GLY B 1 264 ? -59.612 -1.559  130.165 1.00 56.17  ? 310 GLY B CA  1 
ATOM 6062 C C   . GLY B 1 264 ? -58.195 -1.977  130.524 1.00 56.66  ? 310 GLY B C   1 
ATOM 6063 O O   . GLY B 1 264 ? -57.370 -1.200  131.003 1.00 59.30  ? 310 GLY B O   1 
ATOM 6064 N N   . ALA B 1 265 ? -57.914 -3.256  130.257 1.00 61.87  ? 311 ALA B N   1 
ATOM 6065 C CA  . ALA B 1 265 ? -56.698 -3.893  130.754 1.00 60.64  ? 311 ALA B CA  1 
ATOM 6066 C C   . ALA B 1 265 ? -55.427 -3.180  130.316 1.00 62.56  ? 311 ALA B C   1 
ATOM 6067 O O   . ALA B 1 265 ? -54.413 -3.263  131.018 1.00 63.63  ? 311 ALA B O   1 
ATOM 6068 C CB  . ALA B 1 265 ? -56.649 -5.351  130.299 1.00 57.82  ? 311 ALA B CB  1 
ATOM 6069 N N   . ASP B 1 266 ? -55.449 -2.490  129.174 1.00 72.20  ? 312 ASP B N   1 
ATOM 6070 C CA  . ASP B 1 266 ? -54.267 -1.752  128.743 1.00 71.10  ? 312 ASP B CA  1 
ATOM 6071 C C   . ASP B 1 266 ? -53.943 -0.614  129.703 1.00 66.61  ? 312 ASP B C   1 
ATOM 6072 O O   . ASP B 1 266 ? -52.772 -0.369  130.011 1.00 66.48  ? 312 ASP B O   1 
ATOM 6073 C CB  . ASP B 1 266 ? -54.472 -1.219  127.326 1.00 75.85  ? 312 ASP B CB  1 
ATOM 6074 C CG  . ASP B 1 266 ? -54.029 -2.205  126.266 1.00 78.59  ? 312 ASP B CG  1 
ATOM 6075 O OD1 . ASP B 1 266 ? -52.954 -2.817  126.435 1.00 74.40  ? 312 ASP B OD1 1 
ATOM 6076 O OD2 . ASP B 1 266 ? -54.756 -2.367  125.263 1.00 78.65  ? 312 ASP B OD2 1 
ATOM 6077 N N   . GLY B 1 267 ? -54.963 0.087   130.184 1.00 56.34  ? 313 GLY B N   1 
ATOM 6078 C CA  . GLY B 1 267 ? -54.800 1.212   131.078 1.00 54.22  ? 313 GLY B CA  1 
ATOM 6079 C C   . GLY B 1 267 ? -54.815 0.879   132.552 1.00 53.64  ? 313 GLY B C   1 
ATOM 6080 O O   . GLY B 1 267 ? -54.868 1.795   133.379 1.00 55.30  ? 313 GLY B O   1 
ATOM 6081 N N   . LEU B 1 268 ? -54.781 -0.398  132.911 1.00 48.44  ? 314 LEU B N   1 
ATOM 6082 C CA  . LEU B 1 268 ? -54.800 -0.807  134.305 1.00 43.23  ? 314 LEU B CA  1 
ATOM 6083 C C   . LEU B 1 268 ? -53.382 -0.978  134.837 1.00 46.16  ? 314 LEU B C   1 
ATOM 6084 O O   . LEU B 1 268 ? -52.433 -1.211  134.087 1.00 52.97  ? 314 LEU B O   1 
ATOM 6085 C CB  . LEU B 1 268 ? -55.575 -2.112  134.471 1.00 42.58  ? 314 LEU B CB  1 
ATOM 6086 C CG  . LEU B 1 268 ? -57.095 -1.992  134.452 1.00 49.14  ? 314 LEU B CG  1 
ATOM 6087 C CD1 . LEU B 1 268 ? -57.723 -3.366  134.451 1.00 52.34  ? 314 LEU B CD1 1 
ATOM 6088 C CD2 . LEU B 1 268 ? -57.585 -1.179  135.630 1.00 47.11  ? 314 LEU B CD2 1 
ATOM 6089 N N   . VAL B 1 269 ? -53.251 -0.860  136.150 1.00 37.00  ? 315 VAL B N   1 
ATOM 6090 C CA  . VAL B 1 269 ? -51.968 -1.032  136.821 1.00 40.48  ? 315 VAL B CA  1 
ATOM 6091 C C   . VAL B 1 269 ? -51.781 -2.507  137.143 1.00 46.25  ? 315 VAL B C   1 
ATOM 6092 O O   . VAL B 1 269 ? -52.723 -3.196  137.553 1.00 52.06  ? 315 VAL B O   1 
ATOM 6093 C CB  . VAL B 1 269 ? -51.882 -0.151  138.083 1.00 36.01  ? 315 VAL B CB  1 
ATOM 6094 C CG1 . VAL B 1 269 ? -52.919 -0.563  139.101 1.00 31.83  ? 315 VAL B CG1 1 
ATOM 6095 C CG2 . VAL B 1 269 ? -50.490 -0.214  138.684 1.00 39.38  ? 315 VAL B CG2 1 
ATOM 6096 N N   . LYS B 1 270 ? -50.566 -3.004  136.929 1.00 40.52  ? 316 LYS B N   1 
ATOM 6097 C CA  . LYS B 1 270 ? -50.274 -4.425  137.048 1.00 42.01  ? 316 LYS B CA  1 
ATOM 6098 C C   . LYS B 1 270 ? -49.051 -4.630  137.928 1.00 46.92  ? 316 LYS B C   1 
ATOM 6099 O O   . LYS B 1 270 ? -48.140 -3.797  137.936 1.00 46.16  ? 316 LYS B O   1 
ATOM 6100 C CB  . LYS B 1 270 ? -50.048 -5.055  135.672 1.00 44.34  ? 316 LYS B CB  1 
ATOM 6101 C CG  . LYS B 1 270 ? -49.074 -4.294  134.796 1.00 44.95  ? 316 LYS B CG  1 
ATOM 6102 C CD  . LYS B 1 270 ? -49.275 -4.645  133.336 1.00 48.70  ? 316 LYS B CD  1 
ATOM 6103 C CE  . LYS B 1 270 ? -50.590 -4.093  132.813 1.00 44.50  ? 316 LYS B CE  1 
ATOM 6104 N NZ  . LYS B 1 270 ? -50.538 -2.617  132.622 1.00 49.78  ? 316 LYS B NZ  1 
ATOM 6105 N N   . LEU B 1 271 ? -49.042 -5.736  138.667 1.00 47.91  ? 317 LEU B N   1 
ATOM 6106 C CA  . LEU B 1 271 ? -47.923 -6.080  139.534 1.00 45.07  ? 317 LEU B CA  1 
ATOM 6107 C C   . LEU B 1 271 ? -46.981 -7.027  138.805 1.00 47.61  ? 317 LEU B C   1 
ATOM 6108 O O   . LEU B 1 271 ? -47.416 -8.045  138.255 1.00 50.25  ? 317 LEU B O   1 
ATOM 6109 C CB  . LEU B 1 271 ? -48.431 -6.715  140.826 1.00 43.51  ? 317 LEU B CB  1 
ATOM 6110 C CG  . LEU B 1 271 ? -49.700 -6.076  141.378 1.00 44.72  ? 317 LEU B CG  1 
ATOM 6111 C CD1 . LEU B 1 271 ? -50.219 -6.851  142.571 1.00 42.28  ? 317 LEU B CD1 1 
ATOM 6112 C CD2 . LEU B 1 271 ? -49.417 -4.636  141.753 1.00 43.53  ? 317 LEU B CD2 1 
ATOM 6113 N N   . LEU B 1 272 ? -45.694 -6.693  138.800 1.00 45.43  ? 318 LEU B N   1 
ATOM 6114 C CA  . LEU B 1 272 ? -44.707 -7.526  138.130 1.00 54.70  ? 318 LEU B CA  1 
ATOM 6115 C C   . LEU B 1 272 ? -44.393 -8.759  138.969 1.00 55.78  ? 318 LEU B C   1 
ATOM 6116 O O   . LEU B 1 272 ? -44.135 -8.666  140.172 1.00 54.29  ? 318 LEU B O   1 
ATOM 6117 C CB  . LEU B 1 272 ? -43.426 -6.733  137.849 1.00 51.95  ? 318 LEU B CB  1 
ATOM 6118 C CG  . LEU B 1 272 ? -42.589 -6.065  138.948 1.00 51.68  ? 318 LEU B CG  1 
ATOM 6119 C CD1 . LEU B 1 272 ? -41.311 -5.517  138.338 1.00 53.99  ? 318 LEU B CD1 1 
ATOM 6120 C CD2 . LEU B 1 272 ? -43.321 -4.949  139.679 1.00 51.80  ? 318 LEU B CD2 1 
ATOM 6121 N N   . ALA B 1 273 ? -44.418 -9.922  138.323 1.00 59.27  ? 319 ALA B N   1 
ATOM 6122 C CA  . ALA B 1 273 ? -44.196 -11.177 139.025 1.00 59.88  ? 319 ALA B CA  1 
ATOM 6123 C C   . ALA B 1 273 ? -42.736 -11.315 139.440 1.00 62.34  ? 319 ALA B C   1 
ATOM 6124 O O   . ALA B 1 273 ? -41.836 -10.710 138.851 1.00 61.69  ? 319 ALA B O   1 
ATOM 6125 C CB  . ALA B 1 273 ? -44.605 -12.360 138.149 1.00 56.75  ? 319 ALA B CB  1 
ATOM 6126 N N   . VAL B 1 274 ? -42.508 -12.128 140.471 1.00 66.32  ? 320 VAL B N   1 
ATOM 6127 C CA  . VAL B 1 274 ? -41.181 -12.337 141.027 1.00 67.08  ? 320 VAL B CA  1 
ATOM 6128 C C   . VAL B 1 274 ? -40.919 -13.834 141.143 1.00 68.46  ? 320 VAL B C   1 
ATOM 6129 O O   . VAL B 1 274 ? -41.796 -14.622 141.503 1.00 62.88  ? 320 VAL B O   1 
ATOM 6130 C CB  . VAL B 1 274 ? -41.015 -11.642 142.397 1.00 64.16  ? 320 VAL B CB  1 
ATOM 6131 C CG1 . VAL B 1 274 ? -42.080 -12.115 143.366 1.00 59.95  ? 320 VAL B CG1 1 
ATOM 6132 C CG2 . VAL B 1 274 ? -39.623 -11.874 142.961 1.00 62.31  ? 320 VAL B CG2 1 
ATOM 6133 N N   . ASP B 1 275 ? -39.688 -14.217 140.814 1.00 79.83  ? 321 ASP B N   1 
ATOM 6134 C CA  . ASP B 1 275 ? -39.236 -15.599 140.883 1.00 77.86  ? 321 ASP B CA  1 
ATOM 6135 C C   . ASP B 1 275 ? -37.744 -15.592 141.211 1.00 78.08  ? 321 ASP B C   1 
ATOM 6136 O O   . ASP B 1 275 ? -37.186 -14.575 141.634 1.00 77.59  ? 321 ASP B O   1 
ATOM 6137 C CB  . ASP B 1 275 ? -39.585 -16.344 139.585 1.00 75.56  ? 321 ASP B CB  1 
ATOM 6138 C CG  . ASP B 1 275 ? -38.973 -15.705 138.349 1.00 78.26  ? 321 ASP B CG  1 
ATOM 6139 O OD1 . ASP B 1 275 ? -38.110 -14.816 138.481 1.00 77.79  ? 321 ASP B OD1 1 
ATOM 6140 O OD2 . ASP B 1 275 ? -39.373 -16.088 137.229 1.00 78.87  ? 321 ASP B OD2 1 
ATOM 6141 N N   . SER B 1 276 ? -37.093 -16.739 141.022 1.00 73.77  ? 322 SER B N   1 
ATOM 6142 C CA  . SER B 1 276 ? -35.701 -16.894 141.429 1.00 71.13  ? 322 SER B CA  1 
ATOM 6143 C C   . SER B 1 276 ? -34.732 -16.035 140.624 1.00 71.11  ? 322 SER B C   1 
ATOM 6144 O O   . SER B 1 276 ? -33.608 -15.806 141.083 1.00 70.60  ? 322 SER B O   1 
ATOM 6145 C CB  . SER B 1 276 ? -35.288 -18.363 141.332 1.00 71.23  ? 322 SER B CB  1 
ATOM 6146 O OG  . SER B 1 276 ? -35.848 -19.117 142.393 1.00 73.41  ? 322 SER B OG  1 
ATOM 6147 N N   . THR B 1 277 ? -35.125 -15.561 139.440 1.00 84.17  ? 323 THR B N   1 
ATOM 6148 C CA  . THR B 1 277 ? -34.237 -14.781 138.585 1.00 84.49  ? 323 THR B CA  1 
ATOM 6149 C C   . THR B 1 277 ? -34.590 -13.295 138.558 1.00 84.44  ? 323 THR B C   1 
ATOM 6150 O O   . THR B 1 277 ? -34.393 -12.630 137.534 1.00 84.50  ? 323 THR B O   1 
ATOM 6151 C CB  . THR B 1 277 ? -34.224 -15.351 137.165 1.00 84.73  ? 323 THR B CB  1 
ATOM 6152 O OG1 . THR B 1 277 ? -33.326 -14.588 136.349 1.00 82.85  ? 323 THR B OG1 1 
ATOM 6153 C CG2 . THR B 1 277 ? -35.619 -15.336 136.551 1.00 83.24  ? 323 THR B CG2 1 
ATOM 6154 N N   . THR B 1 278 ? -35.090 -12.750 139.664 1.00 78.31  ? 324 THR B N   1 
ATOM 6155 C CA  . THR B 1 278 ? -35.334 -11.317 139.785 1.00 79.56  ? 324 THR B CA  1 
ATOM 6156 C C   . THR B 1 278 ? -34.294 -10.711 140.717 1.00 78.60  ? 324 THR B C   1 
ATOM 6157 O O   . THR B 1 278 ? -34.189 -11.106 141.883 1.00 76.67  ? 324 THR B O   1 
ATOM 6158 C CB  . THR B 1 278 ? -36.742 -11.017 140.296 1.00 79.66  ? 324 THR B CB  1 
ATOM 6159 O OG1 . THR B 1 278 ? -36.749 -11.025 141.730 1.00 78.23  ? 324 THR B OG1 1 
ATOM 6160 C CG2 . THR B 1 278 ? -37.731 -12.017 139.761 1.00 76.71  ? 324 THR B CG2 1 
ATOM 6161 N N   . MET B 1 279 ? -33.532 -9.757  140.196 1.00 79.80  ? 325 MET B N   1 
ATOM 6162 C CA  . MET B 1 279 ? -32.458 -9.104  140.926 1.00 78.80  ? 325 MET B CA  1 
ATOM 6163 C C   . MET B 1 279 ? -32.772 -7.622  141.061 1.00 79.15  ? 325 MET B C   1 
ATOM 6164 O O   . MET B 1 279 ? -33.005 -6.940  140.058 1.00 77.09  ? 325 MET B O   1 
ATOM 6165 C CB  . MET B 1 279 ? -31.125 -9.294  140.202 1.00 79.35  ? 325 MET B CB  1 
ATOM 6166 C CG  . MET B 1 279 ? -29.912 -8.908  141.018 1.00 81.11  ? 325 MET B CG  1 
ATOM 6167 S SD  . MET B 1 279 ? -29.981 -9.577  142.686 1.00 88.29  ? 325 MET B SD  1 
ATOM 6168 C CE  . MET B 1 279 ? -28.731 -10.853 142.563 1.00 77.07  ? 325 MET B CE  1 
ATOM 6169 N N   . THR B 1 280 ? -32.786 -7.128  142.293 1.00 70.71  ? 326 THR B N   1 
ATOM 6170 C CA  . THR B 1 280 ? -32.890 -5.697  142.523 1.00 68.00  ? 326 THR B CA  1 
ATOM 6171 C C   . THR B 1 280 ? -31.501 -5.102  142.744 1.00 68.40  ? 326 THR B C   1 
ATOM 6172 O O   . THR B 1 280 ? -30.631 -5.700  143.381 1.00 70.20  ? 326 THR B O   1 
ATOM 6173 C CB  . THR B 1 280 ? -33.812 -5.395  143.709 1.00 65.86  ? 326 THR B CB  1 
ATOM 6174 O OG1 . THR B 1 280 ? -34.159 -4.004  143.709 1.00 61.54  ? 326 THR B OG1 1 
ATOM 6175 C CG2 . THR B 1 280 ? -33.160 -5.760  145.033 1.00 68.54  ? 326 THR B CG2 1 
ATOM 6176 N N   . LEU B 1 281 ? -31.291 -3.917  142.171 1.00 56.04  ? 327 LEU B N   1 
ATOM 6177 C CA  . LEU B 1 281 ? -29.992 -3.273  142.193 1.00 51.65  ? 327 LEU B CA  1 
ATOM 6178 C C   . LEU B 1 281 ? -30.135 -1.883  142.786 1.00 55.65  ? 327 LEU B C   1 
ATOM 6179 O O   . LEU B 1 281 ? -31.093 -1.172  142.448 1.00 61.42  ? 327 LEU B O   1 
ATOM 6180 C CB  . LEU B 1 281 ? -29.384 -3.173  140.790 1.00 52.97  ? 327 LEU B CB  1 
ATOM 6181 C CG  . LEU B 1 281 ? -28.872 -4.438  140.098 1.00 58.33  ? 327 LEU B CG  1 
ATOM 6182 C CD1 . LEU B 1 281 ? -27.700 -4.097  139.195 1.00 61.24  ? 327 LEU B CD1 1 
ATOM 6183 C CD2 . LEU B 1 281 ? -28.460 -5.490  141.111 1.00 55.26  ? 327 LEU B CD2 1 
ATOM 6184 N N   . PRO B 1 282 ? -29.229 -1.475  143.670 1.00 40.86  ? 328 PRO B N   1 
ATOM 6185 C CA  . PRO B 1 282 ? -29.239 -0.090  144.146 1.00 40.07  ? 328 PRO B CA  1 
ATOM 6186 C C   . PRO B 1 282 ? -29.025 0.885   143.000 1.00 40.41  ? 328 PRO B C   1 
ATOM 6187 O O   . PRO B 1 282 ? -28.234 0.645   142.086 1.00 42.01  ? 328 PRO B O   1 
ATOM 6188 C CB  . PRO B 1 282 ? -28.075 -0.046  145.142 1.00 35.11  ? 328 PRO B CB  1 
ATOM 6189 C CG  . PRO B 1 282 ? -27.847 -1.468  145.528 1.00 35.72  ? 328 PRO B CG  1 
ATOM 6190 C CD  . PRO B 1 282 ? -28.180 -2.277  144.319 1.00 38.45  ? 328 PRO B CD  1 
ATOM 6191 N N   . THR B 1 283 ? -29.748 2.000   143.060 1.00 39.17  ? 329 THR B N   1 
ATOM 6192 C CA  . THR B 1 283 ? -29.701 3.004   142.008 1.00 41.22  ? 329 THR B CA  1 
ATOM 6193 C C   . THR B 1 283 ? -29.555 4.383   142.632 1.00 43.06  ? 329 THR B C   1 
ATOM 6194 O O   . THR B 1 283 ? -29.977 4.625   143.764 1.00 51.00  ? 329 THR B O   1 
ATOM 6195 C CB  . THR B 1 283 ? -30.952 2.959   141.123 1.00 46.59  ? 329 THR B CB  1 
ATOM 6196 O OG1 . THR B 1 283 ? -32.099 2.678   141.933 1.00 43.63  ? 329 THR B OG1 1 
ATOM 6197 C CG2 . THR B 1 283 ? -30.811 1.883   140.061 1.00 44.03  ? 329 THR B CG2 1 
ATOM 6198 N N   . TYR B 1 284 ? -28.950 5.291   141.874 1.00 42.06  ? 330 TYR B N   1 
ATOM 6199 C CA  . TYR B 1 284 ? -28.712 6.657   142.320 1.00 45.36  ? 330 TYR B CA  1 
ATOM 6200 C C   . TYR B 1 284 ? -29.793 7.561   141.742 1.00 51.75  ? 330 TYR B C   1 
ATOM 6201 O O   . TYR B 1 284 ? -29.923 7.673   140.518 1.00 53.84  ? 330 TYR B O   1 
ATOM 6202 C CB  . TYR B 1 284 ? -27.323 7.127   141.891 1.00 44.13  ? 330 TYR B CB  1 
ATOM 6203 C CG  . TYR B 1 284 ? -26.960 8.514   142.364 1.00 48.66  ? 330 TYR B CG  1 
ATOM 6204 C CD1 . TYR B 1 284 ? -26.619 8.748   143.686 1.00 49.19  ? 330 TYR B CD1 1 
ATOM 6205 C CD2 . TYR B 1 284 ? -26.946 9.586   141.485 1.00 50.43  ? 330 TYR B CD2 1 
ATOM 6206 C CE1 . TYR B 1 284 ? -26.282 10.010  144.123 1.00 52.02  ? 330 TYR B CE1 1 
ATOM 6207 C CE2 . TYR B 1 284 ? -26.609 10.854  141.914 1.00 50.48  ? 330 TYR B CE2 1 
ATOM 6208 C CZ  . TYR B 1 284 ? -26.279 11.059  143.234 1.00 52.91  ? 330 TYR B CZ  1 
ATOM 6209 O OH  . TYR B 1 284 ? -25.943 12.319  143.670 1.00 52.74  ? 330 TYR B OH  1 
ATOM 6210 N N   . ASP B 1 285 ? -30.564 8.201   142.618 1.00 51.25  ? 331 ASP B N   1 
ATOM 6211 C CA  . ASP B 1 285 ? -31.638 9.078   142.170 1.00 49.79  ? 331 ASP B CA  1 
ATOM 6212 C C   . ASP B 1 285 ? -31.640 10.376  142.969 1.00 55.88  ? 331 ASP B C   1 
ATOM 6213 O O   . ASP B 1 285 ? -32.057 10.398  144.138 1.00 62.83  ? 331 ASP B O   1 
ATOM 6214 C CB  . ASP B 1 285 ? -32.988 8.370   142.281 1.00 49.57  ? 331 ASP B CB  1 
ATOM 6215 C CG  . ASP B 1 285 ? -33.977 8.837   141.234 1.00 56.47  ? 331 ASP B CG  1 
ATOM 6216 O OD1 . ASP B 1 285 ? -33.607 9.695   140.406 1.00 56.94  ? 331 ASP B OD1 1 
ATOM 6217 O OD2 . ASP B 1 285 ? -35.124 8.345   141.235 1.00 56.49  ? 331 ASP B OD2 1 
ATOM 6218 N N   . PRO B 1 286 ? -31.178 11.477  142.372 1.00 48.95  ? 332 PRO B N   1 
ATOM 6219 C CA  . PRO B 1 286 ? -31.135 12.751  143.105 1.00 42.19  ? 332 PRO B CA  1 
ATOM 6220 C C   . PRO B 1 286 ? -32.497 13.255  143.548 1.00 46.47  ? 332 PRO B C   1 
ATOM 6221 O O   . PRO B 1 286 ? -32.571 13.926  144.581 1.00 51.21  ? 332 PRO B O   1 
ATOM 6222 C CB  . PRO B 1 286 ? -30.482 13.717  142.106 1.00 48.85  ? 332 PRO B CB  1 
ATOM 6223 C CG  . PRO B 1 286 ? -29.878 12.853  141.044 1.00 49.40  ? 332 PRO B CG  1 
ATOM 6224 C CD  . PRO B 1 286 ? -30.695 11.611  140.990 1.00 50.59  ? 332 PRO B CD  1 
ATOM 6225 N N   . LEU B 1 287 ? -33.572 12.957  142.816 1.00 47.16  ? 333 LEU B N   1 
ATOM 6226 C CA  . LEU B 1 287 ? -34.893 13.426  143.228 1.00 50.43  ? 333 LEU B CA  1 
ATOM 6227 C C   . LEU B 1 287 ? -35.325 12.773  144.536 1.00 53.62  ? 333 LEU B C   1 
ATOM 6228 O O   . LEU B 1 287 ? -35.753 13.458  145.477 1.00 57.86  ? 333 LEU B O   1 
ATOM 6229 C CB  . LEU B 1 287 ? -35.924 13.150  142.130 1.00 51.30  ? 333 LEU B CB  1 
ATOM 6230 C CG  . LEU B 1 287 ? -35.841 13.861  140.775 1.00 52.33  ? 333 LEU B CG  1 
ATOM 6231 C CD1 . LEU B 1 287 ? -34.685 13.361  139.916 1.00 55.19  ? 333 LEU B CD1 1 
ATOM 6232 C CD2 . LEU B 1 287 ? -37.159 13.718  140.031 1.00 47.54  ? 333 LEU B CD2 1 
ATOM 6233 N N   . ILE B 1 288 ? -35.226 11.443  144.612 1.00 37.59  ? 334 ILE B N   1 
ATOM 6234 C CA  . ILE B 1 288 ? -35.581 10.763  145.850 1.00 35.90  ? 334 ILE B CA  1 
ATOM 6235 C C   . ILE B 1 288 ? -34.608 11.143  146.954 1.00 39.96  ? 334 ILE B C   1 
ATOM 6236 O O   . ILE B 1 288 ? -34.998 11.237  148.122 1.00 47.03  ? 334 ILE B O   1 
ATOM 6237 C CB  . ILE B 1 288 ? -35.654 9.237   145.648 1.00 38.55  ? 334 ILE B CB  1 
ATOM 6238 C CG1 . ILE B 1 288 ? -36.362 8.577   146.831 1.00 46.85  ? 334 ILE B CG1 1 
ATOM 6239 C CG2 . ILE B 1 288 ? -34.279 8.633   145.514 1.00 46.86  ? 334 ILE B CG2 1 
ATOM 6240 C CD1 . ILE B 1 288 ? -37.865 8.714   146.803 1.00 48.12  ? 334 ILE B CD1 1 
ATOM 6241 N N   . LEU B 1 289 ? -33.341 11.396  146.614 1.00 42.59  ? 335 LEU B N   1 
ATOM 6242 C CA  . LEU B 1 289 ? -32.395 11.842  147.632 1.00 46.69  ? 335 LEU B CA  1 
ATOM 6243 C C   . LEU B 1 289 ? -32.803 13.190  148.214 1.00 47.15  ? 335 LEU B C   1 
ATOM 6244 O O   . LEU B 1 289 ? -32.762 13.388  149.433 1.00 48.24  ? 335 LEU B O   1 
ATOM 6245 C CB  . LEU B 1 289 ? -30.988 11.914  147.045 1.00 47.00  ? 335 LEU B CB  1 
ATOM 6246 C CG  . LEU B 1 289 ? -30.238 10.584  147.007 1.00 43.80  ? 335 LEU B CG  1 
ATOM 6247 C CD1 . LEU B 1 289 ? -28.863 10.765  146.400 1.00 42.61  ? 335 LEU B CD1 1 
ATOM 6248 C CD2 . LEU B 1 289 ? -30.140 9.998   148.400 1.00 44.36  ? 335 LEU B CD2 1 
ATOM 6249 N N   . ALA B 1 290 ? -33.213 14.126  147.357 1.00 38.31  ? 336 ALA B N   1 
ATOM 6250 C CA  . ALA B 1 290 ? -33.632 15.439  147.833 1.00 37.54  ? 336 ALA B CA  1 
ATOM 6251 C C   . ALA B 1 290 ? -34.889 15.345  148.686 1.00 36.03  ? 336 ALA B C   1 
ATOM 6252 O O   . ALA B 1 290 ? -34.970 15.968  149.753 1.00 41.36  ? 336 ALA B O   1 
ATOM 6253 C CB  . ALA B 1 290 ? -33.858 16.379  146.650 1.00 34.67  ? 336 ALA B CB  1 
ATOM 6254 N N   . GLN B 1 291 ? -35.880 14.574  148.238 1.00 36.12  ? 337 GLN B N   1 
ATOM 6255 C CA  . GLN B 1 291 ? -37.104 14.465  149.024 1.00 36.04  ? 337 GLN B CA  1 
ATOM 6256 C C   . GLN B 1 291 ? -36.911 13.650  150.297 1.00 35.35  ? 337 GLN B C   1 
ATOM 6257 O O   . GLN B 1 291 ? -37.718 13.778  151.223 1.00 32.58  ? 337 GLN B O   1 
ATOM 6258 C CB  . GLN B 1 291 ? -38.238 13.884  148.177 1.00 31.49  ? 337 GLN B CB  1 
ATOM 6259 C CG  . GLN B 1 291 ? -38.193 12.394  147.959 1.00 36.06  ? 337 GLN B CG  1 
ATOM 6260 C CD  . GLN B 1 291 ? -39.356 11.918  147.116 1.00 41.38  ? 337 GLN B CD  1 
ATOM 6261 O OE1 . GLN B 1 291 ? -40.289 11.295  147.621 1.00 42.60  ? 337 GLN B OE1 1 
ATOM 6262 N NE2 . GLN B 1 291 ? -39.316 12.227  145.826 1.00 42.11  ? 337 GLN B NE2 1 
ATOM 6263 N N   . ILE B 1 292 ? -35.871 12.817  150.364 1.00 38.36  ? 338 ILE B N   1 
ATOM 6264 C CA  . ILE B 1 292 ? -35.471 12.229  151.638 1.00 35.11  ? 338 ILE B CA  1 
ATOM 6265 C C   . ILE B 1 292 ? -34.841 13.288  152.530 1.00 35.03  ? 338 ILE B C   1 
ATOM 6266 O O   . ILE B 1 292 ? -35.117 13.355  153.733 1.00 41.69  ? 338 ILE B O   1 
ATOM 6267 C CB  . ILE B 1 292 ? -34.510 11.050  151.400 1.00 34.24  ? 338 ILE B CB  1 
ATOM 6268 C CG1 . ILE B 1 292 ? -35.286 9.783   151.047 1.00 32.85  ? 338 ILE B CG1 1 
ATOM 6269 C CG2 . ILE B 1 292 ? -33.639 10.812  152.620 1.00 29.55  ? 338 ILE B CG2 1 
ATOM 6270 C CD1 . ILE B 1 292 ? -34.404 8.634   150.623 1.00 33.69  ? 338 ILE B CD1 1 
ATOM 6271 N N   . HIS B 1 293 ? -33.988 14.135  151.950 1.00 36.09  ? 339 HIS B N   1 
ATOM 6272 C CA  . HIS B 1 293 ? -33.276 15.145  152.725 1.00 34.72  ? 339 HIS B CA  1 
ATOM 6273 C C   . HIS B 1 293 ? -34.238 16.141  153.356 1.00 37.30  ? 339 HIS B C   1 
ATOM 6274 O O   . HIS B 1 293 ? -34.053 16.546  154.508 1.00 40.29  ? 339 HIS B O   1 
ATOM 6275 C CB  . HIS B 1 293 ? -32.266 15.859  151.828 1.00 36.99  ? 339 HIS B CB  1 
ATOM 6276 C CG  . HIS B 1 293 ? -31.477 16.922  152.526 1.00 40.94  ? 339 HIS B CG  1 
ATOM 6277 N ND1 . HIS B 1 293 ? -31.032 16.788  153.823 1.00 48.55  ? 339 HIS B ND1 1 
ATOM 6278 C CD2 . HIS B 1 293 ? -31.038 18.129  152.101 1.00 40.09  ? 339 HIS B CD2 1 
ATOM 6279 C CE1 . HIS B 1 293 ? -30.360 17.871  154.170 1.00 40.84  ? 339 HIS B CE1 1 
ATOM 6280 N NE2 . HIS B 1 293 ? -30.350 18.701  153.143 1.00 41.17  ? 339 HIS B NE2 1 
ATOM 6281 N N   . SER B 1 294 ? -35.276 16.540  152.622 1.00 41.92  ? 340 SER B N   1 
ATOM 6282 C CA  . SER B 1 294 ? -36.241 17.522  153.103 1.00 36.08  ? 340 SER B CA  1 
ATOM 6283 C C   . SER B 1 294 ? -37.455 16.872  153.758 1.00 34.80  ? 340 SER B C   1 
ATOM 6284 O O   . SER B 1 294 ? -38.562 17.414  153.684 1.00 45.14  ? 340 SER B O   1 
ATOM 6285 C CB  . SER B 1 294 ? -36.683 18.435  151.961 1.00 41.55  ? 340 SER B CB  1 
ATOM 6286 O OG  . SER B 1 294 ? -35.568 18.979  151.279 1.00 49.97  ? 340 SER B OG  1 
ATOM 6287 N N   . ALA B 1 295 ? -37.272 15.720  154.394 1.00 33.18  ? 341 ALA B N   1 
ATOM 6288 C CA  . ALA B 1 295 ? -38.360 14.997  155.032 1.00 29.78  ? 341 ALA B CA  1 
ATOM 6289 C C   . ALA B 1 295 ? -38.358 15.243  156.535 1.00 31.18  ? 341 ALA B C   1 
ATOM 6290 O O   . ALA B 1 295 ? -37.313 15.201  157.188 1.00 38.62  ? 341 ALA B O   1 
ATOM 6291 C CB  . ALA B 1 295 ? -38.255 13.497  154.756 1.00 31.20  ? 341 ALA B CB  1 
ATOM 6292 N N   . ARG B 1 296 ? -39.545 15.497  157.080 1.00 31.94  ? 342 ARG B N   1 
ATOM 6293 C CA  . ARG B 1 296 ? -39.712 15.761  158.503 1.00 34.92  ? 342 ARG B CA  1 
ATOM 6294 C C   . ARG B 1 296 ? -40.582 14.674  159.110 1.00 38.43  ? 342 ARG B C   1 
ATOM 6295 O O   . ARG B 1 296 ? -41.691 14.422  158.630 1.00 46.46  ? 342 ARG B O   1 
ATOM 6296 C CB  . ARG B 1 296 ? -40.332 17.141  158.739 1.00 33.14  ? 342 ARG B CB  1 
ATOM 6297 C CG  . ARG B 1 296 ? -39.417 18.292  158.359 1.00 38.62  ? 342 ARG B CG  1 
ATOM 6298 C CD  . ARG B 1 296 ? -40.171 19.607  158.270 1.00 40.38  ? 342 ARG B CD  1 
ATOM 6299 N NE  . ARG B 1 296 ? -40.558 20.119  159.578 1.00 36.47  ? 342 ARG B NE  1 
ATOM 6300 C CZ  . ARG B 1 296 ? -39.780 20.869  160.345 1.00 40.55  ? 342 ARG B CZ  1 
ATOM 6301 N NH1 . ARG B 1 296 ? -38.557 21.202  159.971 1.00 40.39  ? 342 ARG B NH1 1 
ATOM 6302 N NH2 . ARG B 1 296 ? -40.240 21.294  161.518 1.00 39.96  ? 342 ARG B NH2 1 
ATOM 6303 N N   . ALA B 1 297 ? -40.077 14.031  160.158 1.00 31.64  ? 343 ALA B N   1 
ATOM 6304 C CA  . ALA B 1 297 ? -40.807 12.960  160.817 1.00 21.31  ? 343 ALA B CA  1 
ATOM 6305 C C   . ALA B 1 297 ? -41.989 13.519  161.594 1.00 38.08  ? 343 ALA B C   1 
ATOM 6306 O O   . ALA B 1 297 ? -41.899 14.584  162.210 1.00 42.22  ? 343 ALA B O   1 
ATOM 6307 C CB  . ALA B 1 297 ? -39.885 12.183  161.755 1.00 24.79  ? 343 ALA B CB  1 
ATOM 6308 N N   . VAL B 1 298 ? -43.103 12.789  161.564 1.00 40.24  ? 344 VAL B N   1 
ATOM 6309 C CA  . VAL B 1 298 ? -44.333 13.220  162.221 1.00 35.05  ? 344 VAL B CA  1 
ATOM 6310 C C   . VAL B 1 298 ? -44.654 12.415  163.468 1.00 36.59  ? 344 VAL B C   1 
ATOM 6311 O O   . VAL B 1 298 ? -45.621 12.753  164.170 1.00 36.84  ? 344 VAL B O   1 
ATOM 6312 C CB  . VAL B 1 298 ? -45.532 13.181  161.252 1.00 36.09  ? 344 VAL B CB  1 
ATOM 6313 C CG1 . VAL B 1 298 ? -45.182 13.883  159.954 1.00 38.03  ? 344 VAL B CG1 1 
ATOM 6314 C CG2 . VAL B 1 298 ? -45.947 11.748  160.986 1.00 36.87  ? 344 VAL B CG2 1 
ATOM 6315 N N   . GLY B 1 299 ? -43.892 11.372  163.771 1.00 44.64  ? 345 GLY B N   1 
ATOM 6316 C CA  . GLY B 1 299 ? -44.109 10.579  164.961 1.00 45.10  ? 345 GLY B CA  1 
ATOM 6317 C C   . GLY B 1 299 ? -44.877 9.299   164.679 1.00 46.12  ? 345 GLY B C   1 
ATOM 6318 O O   . GLY B 1 299 ? -45.332 9.029   163.564 1.00 43.75  ? 345 GLY B O   1 
ATOM 6319 N N   . ALA B 1 300 ? -45.014 8.497   165.731 1.00 56.61  ? 346 ALA B N   1 
ATOM 6320 C CA  . ALA B 1 300 ? -45.676 7.211   165.611 1.00 57.12  ? 346 ALA B CA  1 
ATOM 6321 C C   . ALA B 1 300 ? -47.178 7.392   165.401 1.00 57.96  ? 346 ALA B C   1 
ATOM 6322 O O   . ALA B 1 300 ? -47.773 8.348   165.904 1.00 57.25  ? 346 ALA B O   1 
ATOM 6323 C CB  . ALA B 1 300 ? -45.424 6.364   166.855 1.00 55.50  ? 346 ALA B CB  1 
ATOM 6324 N N   . PRO B 1 301 ? -47.809 6.491   164.654 1.00 56.69  ? 347 PRO B N   1 
ATOM 6325 C CA  . PRO B 1 301 ? -49.259 6.575   164.459 1.00 52.37  ? 347 PRO B CA  1 
ATOM 6326 C C   . PRO B 1 301 ? -50.019 6.310   165.747 1.00 52.47  ? 347 PRO B C   1 
ATOM 6327 O O   . PRO B 1 301 ? -49.533 5.640   166.660 1.00 56.18  ? 347 PRO B O   1 
ATOM 6328 C CB  . PRO B 1 301 ? -49.540 5.481   163.423 1.00 46.17  ? 347 PRO B CB  1 
ATOM 6329 C CG  . PRO B 1 301 ? -48.226 5.225   162.765 1.00 48.90  ? 347 PRO B CG  1 
ATOM 6330 C CD  . PRO B 1 301 ? -47.204 5.434   163.829 1.00 51.39  ? 347 PRO B CD  1 
ATOM 6331 N N   . ILE B 1 302 ? -51.235 6.847   165.808 1.00 48.74  ? 348 ILE B N   1 
ATOM 6332 C CA  . ILE B 1 302 ? -52.129 6.651   166.942 1.00 51.83  ? 348 ILE B CA  1 
ATOM 6333 C C   . ILE B 1 302 ? -53.158 5.595   166.570 1.00 54.80  ? 348 ILE B C   1 
ATOM 6334 O O   . ILE B 1 302 ? -53.872 5.737   165.570 1.00 62.18  ? 348 ILE B O   1 
ATOM 6335 C CB  . ILE B 1 302 ? -52.817 7.966   167.346 1.00 50.16  ? 348 ILE B CB  1 
ATOM 6336 C CG1 . ILE B 1 302 ? -51.809 9.113   167.358 1.00 53.78  ? 348 ILE B CG1 1 
ATOM 6337 C CG2 . ILE B 1 302 ? -53.471 7.824   168.707 1.00 50.16  ? 348 ILE B CG2 1 
ATOM 6338 C CD1 . ILE B 1 302 ? -52.440 10.468  167.550 1.00 50.84  ? 348 ILE B CD1 1 
ATOM 6339 N N   . LEU B 1 303 ? -53.234 4.538   167.369 1.00 62.93  ? 349 LEU B N   1 
ATOM 6340 C CA  . LEU B 1 303 ? -54.196 3.465   167.173 1.00 64.24  ? 349 LEU B CA  1 
ATOM 6341 C C   . LEU B 1 303 ? -55.301 3.556   168.216 1.00 66.85  ? 349 LEU B C   1 
ATOM 6342 O O   . LEU B 1 303 ? -55.221 4.318   169.183 1.00 70.15  ? 349 LEU B O   1 
ATOM 6343 C CB  . LEU B 1 303 ? -53.509 2.096   167.240 1.00 61.86  ? 349 LEU B CB  1 
ATOM 6344 C CG  . LEU B 1 303 ? -52.107 1.997   166.640 1.00 60.73  ? 349 LEU B CG  1 
ATOM 6345 C CD1 . LEU B 1 303 ? -51.395 0.766   167.165 1.00 60.89  ? 349 LEU B CD1 1 
ATOM 6346 C CD2 . LEU B 1 303 ? -52.178 1.967   165.125 1.00 60.71  ? 349 LEU B CD2 1 
ATOM 6347 N N   . GLU B 1 304 ? -56.350 2.759   168.002 1.00 72.84  ? 350 GLU B N   1 
ATOM 6348 C CA  . GLU B 1 304 ? -57.468 2.739   168.939 1.00 73.68  ? 350 GLU B CA  1 
ATOM 6349 C C   . GLU B 1 304 ? -57.036 2.210   170.299 1.00 73.85  ? 350 GLU B C   1 
ATOM 6350 O O   . GLU B 1 304 ? -57.522 2.675   171.337 1.00 75.98  ? 350 GLU B O   1 
ATOM 6351 C CB  . GLU B 1 304 ? -58.619 1.898   168.381 1.00 75.30  ? 350 GLU B CB  1 
ATOM 6352 C CG  . GLU B 1 304 ? -58.908 2.089   166.894 1.00 78.06  ? 350 GLU B CG  1 
ATOM 6353 C CD  . GLU B 1 304 ? -57.949 1.329   165.995 1.00 82.23  ? 350 GLU B CD  1 
ATOM 6354 O OE1 . GLU B 1 304 ? -57.160 0.516   166.518 1.00 81.59  ? 350 GLU B OE1 1 
ATOM 6355 O OE2 . GLU B 1 304 ? -57.984 1.550   164.766 1.00 80.15  ? 350 GLU B OE2 1 
ATOM 6356 N N   . THR B 1 305 ? -56.127 1.236   170.315 1.00 71.39  ? 351 THR B N   1 
ATOM 6357 C CA  . THR B 1 305 ? -55.642 0.660   171.561 1.00 72.91  ? 351 THR B CA  1 
ATOM 6358 C C   . THR B 1 305 ? -54.598 1.525   172.252 1.00 72.84  ? 351 THR B C   1 
ATOM 6359 O O   . THR B 1 305 ? -54.312 1.297   173.431 1.00 74.02  ? 351 THR B O   1 
ATOM 6360 C CB  . THR B 1 305 ? -55.052 -0.729  171.304 1.00 73.37  ? 351 THR B CB  1 
ATOM 6361 O OG1 . THR B 1 305 ? -53.667 -0.603  170.962 1.00 70.82  ? 351 THR B OG1 1 
ATOM 6362 C CG2 . THR B 1 305 ? -55.789 -1.414  170.162 1.00 72.75  ? 351 THR B CG2 1 
ATOM 6363 N N   . SER B 1 306 ? -54.026 2.504   171.556 1.00 71.80  ? 352 SER B N   1 
ATOM 6364 C CA  . SER B 1 306 ? -52.992 3.352   172.135 1.00 70.36  ? 352 SER B CA  1 
ATOM 6365 C C   . SER B 1 306 ? -53.625 4.334   173.111 1.00 72.46  ? 352 SER B C   1 
ATOM 6366 O O   . SER B 1 306 ? -54.515 5.105   172.736 1.00 73.03  ? 352 SER B O   1 
ATOM 6367 C CB  . SER B 1 306 ? -52.238 4.095   171.036 1.00 68.28  ? 352 SER B CB  1 
ATOM 6368 O OG  . SER B 1 306 ? -53.130 4.841   170.226 1.00 71.50  ? 352 SER B OG  1 
ATOM 6369 N N   . THR B 1 307 ? -53.168 4.308   174.358 1.00 74.26  ? 353 THR B N   1 
ATOM 6370 C CA  . THR B 1 307 ? -53.706 5.197   175.376 1.00 75.96  ? 353 THR B CA  1 
ATOM 6371 C C   . THR B 1 307 ? -53.137 6.601   175.221 1.00 74.45  ? 353 THR B C   1 
ATOM 6372 O O   . THR B 1 307 ? -51.943 6.784   174.964 1.00 72.11  ? 353 THR B O   1 
ATOM 6373 C CB  . THR B 1 307 ? -53.409 4.653   176.776 1.00 76.43  ? 353 THR B CB  1 
ATOM 6374 O OG1 . THR B 1 307 ? -53.879 5.580   177.763 1.00 76.08  ? 353 THR B OG1 1 
ATOM 6375 C CG2 . THR B 1 307 ? -51.918 4.411   176.966 1.00 74.83  ? 353 THR B CG2 1 
ATOM 6376 N N   . LEU B 1 308 ? -54.009 7.596   175.364 1.00 68.46  ? 354 LEU B N   1 
ATOM 6377 C CA  . LEU B 1 308 ? -53.609 8.997   175.261 1.00 65.30  ? 354 LEU B CA  1 
ATOM 6378 C C   . LEU B 1 308 ? -54.422 9.776   176.283 1.00 67.14  ? 354 LEU B C   1 
ATOM 6379 O O   . LEU B 1 308 ? -55.637 9.924   176.124 1.00 71.97  ? 354 LEU B O   1 
ATOM 6380 C CB  . LEU B 1 308 ? -53.837 9.533   173.851 1.00 63.67  ? 354 LEU B CB  1 
ATOM 6381 C CG  . LEU B 1 308 ? -52.686 9.348   172.863 1.00 62.38  ? 354 LEU B CG  1 
ATOM 6382 C CD1 . LEU B 1 308 ? -52.962 10.097  171.574 1.00 64.01  ? 354 LEU B CD1 1 
ATOM 6383 C CD2 . LEU B 1 308 ? -51.382 9.806   173.479 1.00 67.63  ? 354 LEU B CD2 1 
ATOM 6384 N N   . THR B 1 309 ? -53.759 10.268  177.325 1.00 70.61  ? 355 THR B N   1 
ATOM 6385 C CA  . THR B 1 309 ? -54.449 10.949  178.414 1.00 72.07  ? 355 THR B CA  1 
ATOM 6386 C C   . THR B 1 309 ? -54.770 12.374  177.982 1.00 73.78  ? 355 THR B C   1 
ATOM 6387 O O   . THR B 1 309 ? -53.864 13.178  177.744 1.00 77.20  ? 355 THR B O   1 
ATOM 6388 C CB  . THR B 1 309 ? -53.597 10.937  179.678 1.00 74.80  ? 355 THR B CB  1 
ATOM 6389 O OG1 . THR B 1 309 ? -52.925 9.676   179.786 1.00 76.64  ? 355 THR B OG1 1 
ATOM 6390 C CG2 . THR B 1 309 ? -54.477 11.122  180.897 1.00 73.88  ? 355 THR B CG2 1 
ATOM 6391 N N   . GLY B 1 310 ? -56.057 12.690  177.884 1.00 71.71  ? 356 GLY B N   1 
ATOM 6392 C CA  . GLY B 1 310 ? -56.491 13.994  177.435 1.00 71.97  ? 356 GLY B CA  1 
ATOM 6393 C C   . GLY B 1 310 ? -56.734 14.110  175.948 1.00 73.24  ? 356 GLY B C   1 
ATOM 6394 O O   . GLY B 1 310 ? -57.224 15.153  175.499 1.00 77.23  ? 356 GLY B O   1 
ATOM 6395 N N   . PHE B 1 311 ? -56.412 13.078  175.170 1.00 62.42  ? 357 PHE B N   1 
ATOM 6396 C CA  . PHE B 1 311 ? -56.639 13.064  173.726 1.00 60.16  ? 357 PHE B CA  1 
ATOM 6397 C C   . PHE B 1 311 ? -57.377 11.782  173.367 1.00 64.27  ? 357 PHE B C   1 
ATOM 6398 O O   . PHE B 1 311 ? -56.795 10.857  172.785 1.00 65.64  ? 357 PHE B O   1 
ATOM 6399 C CB  . PHE B 1 311 ? -55.324 13.175  172.955 1.00 59.66  ? 357 PHE B CB  1 
ATOM 6400 C CG  . PHE B 1 311 ? -54.658 14.511  173.085 1.00 61.37  ? 357 PHE B CG  1 
ATOM 6401 C CD1 . PHE B 1 311 ? -54.936 15.527  172.191 1.00 64.06  ? 357 PHE B CD1 1 
ATOM 6402 C CD2 . PHE B 1 311 ? -53.751 14.750  174.102 1.00 61.26  ? 357 PHE B CD2 1 
ATOM 6403 C CE1 . PHE B 1 311 ? -54.324 16.756  172.308 1.00 64.37  ? 357 PHE B CE1 1 
ATOM 6404 C CE2 . PHE B 1 311 ? -53.137 15.978  174.224 1.00 62.07  ? 357 PHE B CE2 1 
ATOM 6405 C CZ  . PHE B 1 311 ? -53.423 16.981  173.326 1.00 64.51  ? 357 PHE B CZ  1 
ATOM 6406 N N   . PRO B 1 312 ? -58.665 11.690  173.700 1.00 68.56  ? 358 PRO B N   1 
ATOM 6407 C CA  . PRO B 1 312 ? -59.421 10.473  173.392 1.00 67.89  ? 358 PRO B CA  1 
ATOM 6408 C C   . PRO B 1 312 ? -59.977 10.483  171.978 1.00 68.02  ? 358 PRO B C   1 
ATOM 6409 O O   . PRO B 1 312 ? -60.377 11.517  171.440 1.00 66.50  ? 358 PRO B O   1 
ATOM 6410 C CB  . PRO B 1 312 ? -60.553 10.505  174.428 1.00 67.84  ? 358 PRO B CB  1 
ATOM 6411 C CG  . PRO B 1 312 ? -60.752 11.960  174.733 1.00 66.09  ? 358 PRO B CG  1 
ATOM 6412 C CD  . PRO B 1 312 ? -59.503 12.714  174.346 1.00 67.34  ? 358 PRO B CD  1 
ATOM 6413 N N   . GLY B 1 313 ? -60.002 9.301   171.372 1.00 59.08  ? 359 GLY B N   1 
ATOM 6414 C CA  . GLY B 1 313 ? -60.547 9.152   170.034 1.00 58.09  ? 359 GLY B CA  1 
ATOM 6415 C C   . GLY B 1 313 ? -59.793 9.893   168.951 1.00 59.32  ? 359 GLY B C   1 
ATOM 6416 O O   . GLY B 1 313 ? -60.416 10.568  168.121 1.00 58.44  ? 359 GLY B O   1 
ATOM 6417 N N   . ARG B 1 314 ? -58.467 9.791   168.938 1.00 61.05  ? 360 ARG B N   1 
ATOM 6418 C CA  . ARG B 1 314 ? -57.633 10.419  167.920 1.00 58.98  ? 360 ARG B CA  1 
ATOM 6419 C C   . ARG B 1 314 ? -56.950 9.375   167.042 1.00 59.96  ? 360 ARG B C   1 
ATOM 6420 O O   . ARG B 1 314 ? -55.840 9.584   166.550 1.00 67.49  ? 360 ARG B O   1 
ATOM 6421 C CB  . ARG B 1 314 ? -56.595 11.338  168.558 1.00 58.37  ? 360 ARG B CB  1 
ATOM 6422 C CG  . ARG B 1 314 ? -57.091 12.074  169.789 1.00 60.08  ? 360 ARG B CG  1 
ATOM 6423 C CD  . ARG B 1 314 ? -58.193 13.057  169.440 1.00 61.23  ? 360 ARG B CD  1 
ATOM 6424 N NE  . ARG B 1 314 ? -57.719 14.124  168.568 1.00 61.71  ? 360 ARG B NE  1 
ATOM 6425 C CZ  . ARG B 1 314 ? -57.610 15.393  168.934 1.00 63.85  ? 360 ARG B CZ  1 
ATOM 6426 N NH1 . ARG B 1 314 ? -57.929 15.790  170.154 1.00 60.98  ? 360 ARG B NH1 1 
ATOM 6427 N NH2 . ARG B 1 314 ? -57.170 16.286  168.052 1.00 65.35  ? 360 ARG B NH2 1 
ATOM 6428 N N   . GLN B 1 315 ? -57.611 8.240   166.836 1.00 52.96  ? 361 GLN B N   1 
ATOM 6429 C CA  . GLN B 1 315 ? -57.043 7.172   166.031 1.00 54.14  ? 361 GLN B CA  1 
ATOM 6430 C C   . GLN B 1 315 ? -56.914 7.605   164.573 1.00 56.89  ? 361 GLN B C   1 
ATOM 6431 O O   . GLN B 1 315 ? -57.691 8.416   164.063 1.00 55.55  ? 361 GLN B O   1 
ATOM 6432 C CB  . GLN B 1 315 ? -57.901 5.912   166.132 1.00 60.13  ? 361 GLN B CB  1 
ATOM 6433 C CG  . GLN B 1 315 ? -59.395 6.179   166.118 1.00 58.60  ? 361 GLN B CG  1 
ATOM 6434 C CD  . GLN B 1 315 ? -59.998 6.175   167.507 1.00 62.04  ? 361 GLN B CD  1 
ATOM 6435 O OE1 . GLN B 1 315 ? -59.282 6.181   168.507 1.00 64.28  ? 361 GLN B OE1 1 
ATOM 6436 N NE2 . GLN B 1 315 ? -61.324 6.166   167.576 1.00 58.44  ? 361 GLN B NE2 1 
ATOM 6437 N N   . TRP B 1 316 ? -55.907 7.047   163.900 1.00 49.10  ? 362 TRP B N   1 
ATOM 6438 C CA  . TRP B 1 316 ? -55.600 7.405   162.515 1.00 48.75  ? 362 TRP B CA  1 
ATOM 6439 C C   . TRP B 1 316 ? -56.471 6.581   161.567 1.00 53.37  ? 362 TRP B C   1 
ATOM 6440 O O   . TRP B 1 316 ? -56.016 5.672   160.872 1.00 53.33  ? 362 TRP B O   1 
ATOM 6441 C CB  . TRP B 1 316 ? -54.123 7.191   162.224 1.00 47.88  ? 362 TRP B CB  1 
ATOM 6442 C CG  . TRP B 1 316 ? -53.226 8.222   162.812 1.00 45.25  ? 362 TRP B CG  1 
ATOM 6443 C CD1 . TRP B 1 316 ? -53.452 8.967   163.929 1.00 48.03  ? 362 TRP B CD1 1 
ATOM 6444 C CD2 . TRP B 1 316 ? -51.948 8.625   162.312 1.00 44.03  ? 362 TRP B CD2 1 
ATOM 6445 N NE1 . TRP B 1 316 ? -52.393 9.809   164.157 1.00 48.36  ? 362 TRP B NE1 1 
ATOM 6446 C CE2 . TRP B 1 316 ? -51.456 9.618   163.177 1.00 48.01  ? 362 TRP B CE2 1 
ATOM 6447 C CE3 . TRP B 1 316 ? -51.173 8.242   161.215 1.00 40.65  ? 362 TRP B CE3 1 
ATOM 6448 C CZ2 . TRP B 1 316 ? -50.225 10.232  162.980 1.00 48.39  ? 362 TRP B CZ2 1 
ATOM 6449 C CZ3 . TRP B 1 316 ? -49.953 8.851   161.022 1.00 44.49  ? 362 TRP B CZ3 1 
ATOM 6450 C CH2 . TRP B 1 316 ? -49.489 9.835   161.899 1.00 49.62  ? 362 TRP B CH2 1 
ATOM 6451 N N   . GLN B 1 317 ? -57.752 6.926   161.538 1.00 53.31  ? 363 GLN B N   1 
ATOM 6452 C CA  . GLN B 1 317 ? -58.718 6.243   160.695 1.00 49.64  ? 363 GLN B CA  1 
ATOM 6453 C C   . GLN B 1 317 ? -59.222 7.178   159.605 1.00 47.90  ? 363 GLN B C   1 
ATOM 6454 O O   . GLN B 1 317 ? -59.187 8.404   159.738 1.00 51.23  ? 363 GLN B O   1 
ATOM 6455 C CB  . GLN B 1 317 ? -59.897 5.720   161.521 1.00 48.61  ? 363 GLN B CB  1 
ATOM 6456 C CG  . GLN B 1 317 ? -60.796 6.811   162.063 1.00 49.82  ? 363 GLN B CG  1 
ATOM 6457 C CD  . GLN B 1 317 ? -61.627 6.347   163.238 1.00 57.06  ? 363 GLN B CD  1 
ATOM 6458 O OE1 . GLN B 1 317 ? -61.469 5.227   163.720 1.00 56.48  ? 363 GLN B OE1 1 
ATOM 6459 N NE2 . GLN B 1 317 ? -62.519 7.210   163.708 1.00 57.62  ? 363 GLN B NE2 1 
ATOM 6460 N N   . ILE B 1 318 ? -59.684 6.581   158.514 1.00 37.32  ? 364 ILE B N   1 
ATOM 6461 C CA  . ILE B 1 318 ? -60.291 7.309   157.409 1.00 39.34  ? 364 ILE B CA  1 
ATOM 6462 C C   . ILE B 1 318 ? -61.792 7.071   157.502 1.00 47.77  ? 364 ILE B C   1 
ATOM 6463 O O   . ILE B 1 318 ? -62.316 6.093   156.958 1.00 51.06  ? 364 ILE B O   1 
ATOM 6464 C CB  . ILE B 1 318 ? -59.730 6.869   156.054 1.00 31.70  ? 364 ILE B CB  1 
ATOM 6465 C CG1 . ILE B 1 318 ? -58.204 6.852   156.099 1.00 38.52  ? 364 ILE B CG1 1 
ATOM 6466 C CG2 . ILE B 1 318 ? -60.215 7.793   154.954 1.00 35.63  ? 364 ILE B CG2 1 
ATOM 6467 C CD1 . ILE B 1 318 ? -57.561 6.556   154.771 1.00 39.86  ? 364 ILE B CD1 1 
ATOM 6468 N N   . THR B 1 319 ? -62.490 7.967   158.191 1.00 59.56  ? 365 THR B N   1 
ATOM 6469 C CA  . THR B 1 319 ? -63.918 7.806   158.410 1.00 60.16  ? 365 THR B CA  1 
ATOM 6470 C C   . THR B 1 319 ? -64.703 8.295   157.203 1.00 63.60  ? 365 THR B C   1 
ATOM 6471 O O   . THR B 1 319 ? -64.367 9.315   156.594 1.00 62.87  ? 365 THR B O   1 
ATOM 6472 C CB  . THR B 1 319 ? -64.356 8.567   159.661 1.00 65.06  ? 365 THR B CB  1 
ATOM 6473 O OG1 . THR B 1 319 ? -63.349 8.445   160.673 1.00 64.81  ? 365 THR B OG1 1 
ATOM 6474 C CG2 . THR B 1 319 ? -65.667 8.010   160.191 1.00 62.81  ? 365 THR B CG2 1 
ATOM 6475 N N   . GLN B 1 320 ? -65.751 7.552   156.852 1.00 71.25  ? 366 GLN B N   1 
ATOM 6476 C CA  . GLN B 1 320 ? -66.673 7.924   155.781 1.00 67.69  ? 366 GLN B CA  1 
ATOM 6477 C C   . GLN B 1 320 ? -68.081 7.555   156.233 1.00 68.84  ? 366 GLN B C   1 
ATOM 6478 O O   . GLN B 1 320 ? -68.551 6.443   155.981 1.00 68.37  ? 366 GLN B O   1 
ATOM 6479 C CB  . GLN B 1 320 ? -66.307 7.236   154.477 1.00 66.53  ? 366 GLN B CB  1 
ATOM 6480 C CG  . GLN B 1 320 ? -67.021 7.811   153.277 1.00 68.11  ? 366 GLN B CG  1 
ATOM 6481 C CD  . GLN B 1 320 ? -68.244 7.007   152.891 1.00 66.92  ? 366 GLN B CD  1 
ATOM 6482 O OE1 . GLN B 1 320 ? -68.210 5.777   152.865 1.00 65.66  ? 366 GLN B OE1 1 
ATOM 6483 N NE2 . GLN B 1 320 ? -69.334 7.699   152.587 1.00 66.28  ? 366 GLN B NE2 1 
ATOM 6484 N N   . ASN B 1 321 ? -68.754 8.490   156.897 1.00 76.15  ? 367 ASN B N   1 
ATOM 6485 C CA  . ASN B 1 321 ? -70.111 8.281   157.383 1.00 78.05  ? 367 ASN B CA  1 
ATOM 6486 C C   . ASN B 1 321 ? -71.048 9.230   156.651 1.00 79.81  ? 367 ASN B C   1 
ATOM 6487 O O   . ASN B 1 321 ? -70.817 10.452  156.666 1.00 79.59  ? 367 ASN B O   1 
ATOM 6488 C CB  . ASN B 1 321 ? -70.190 8.505   158.892 1.00 79.28  ? 367 ASN B CB  1 
ATOM 6489 C CG  . ASN B 1 321 ? -71.201 7.606   159.561 1.00 79.46  ? 367 ASN B CG  1 
ATOM 6490 O OD1 . ASN B 1 321 ? -72.236 7.280   158.983 1.00 78.57  ? 367 ASN B OD1 1 
ATOM 6491 N ND2 . ASN B 1 321 ? -70.911 7.204   160.792 1.00 80.30  ? 367 ASN B ND2 1 
ATOM 6492 N N   . PRO B 1 322 ? -72.102 8.733   155.997 1.00 76.49  ? 368 PRO B N   1 
ATOM 6493 C CA  . PRO B 1 322 ? -72.982 9.632   155.234 1.00 77.42  ? 368 PRO B CA  1 
ATOM 6494 C C   . PRO B 1 322 ? -73.699 10.667  156.083 1.00 76.76  ? 368 PRO B C   1 
ATOM 6495 O O   . PRO B 1 322 ? -74.161 11.674  155.533 1.00 75.80  ? 368 PRO B O   1 
ATOM 6496 C CB  . PRO B 1 322 ? -73.980 8.671   154.571 1.00 72.54  ? 368 PRO B CB  1 
ATOM 6497 C CG  . PRO B 1 322 ? -73.300 7.342   154.580 1.00 72.37  ? 368 PRO B CG  1 
ATOM 6498 C CD  . PRO B 1 322 ? -72.466 7.318   155.820 1.00 72.26  ? 368 PRO B CD  1 
ATOM 6499 N N   . ASP B 1 323 ? -73.813 10.462  157.393 1.00 80.36  ? 369 ASP B N   1 
ATOM 6500 C CA  . ASP B 1 323 ? -74.554 11.381  158.244 1.00 81.23  ? 369 ASP B CA  1 
ATOM 6501 C C   . ASP B 1 323 ? -73.688 12.481  158.847 1.00 82.24  ? 369 ASP B C   1 
ATOM 6502 O O   . ASP B 1 323 ? -74.221 13.347  159.549 1.00 82.46  ? 369 ASP B O   1 
ATOM 6503 C CB  . ASP B 1 323 ? -75.263 10.609  159.363 1.00 81.23  ? 369 ASP B CB  1 
ATOM 6504 C CG  . ASP B 1 323 ? -74.320 10.180  160.470 1.00 81.57  ? 369 ASP B CG  1 
ATOM 6505 O OD1 . ASP B 1 323 ? -74.070 10.987  161.389 1.00 81.61  ? 369 ASP B OD1 1 
ATOM 6506 O OD2 . ASP B 1 323 ? -73.846 9.027   160.434 1.00 80.77  ? 369 ASP B OD2 1 
ATOM 6507 N N   . VAL B 1 324 ? -72.380 12.477  158.601 1.00 81.10  ? 370 VAL B N   1 
ATOM 6508 C CA  . VAL B 1 324 ? -71.486 13.521  159.094 1.00 80.28  ? 370 VAL B CA  1 
ATOM 6509 C C   . VAL B 1 324 ? -70.733 14.109  157.908 1.00 77.90  ? 370 VAL B C   1 
ATOM 6510 O O   . VAL B 1 324 ? -70.288 13.372  157.018 1.00 77.36  ? 370 VAL B O   1 
ATOM 6511 C CB  . VAL B 1 324 ? -70.511 13.000  160.164 1.00 79.02  ? 370 VAL B CB  1 
ATOM 6512 C CG1 . VAL B 1 324 ? -71.271 12.516  161.387 1.00 79.77  ? 370 VAL B CG1 1 
ATOM 6513 C CG2 . VAL B 1 324 ? -69.630 11.896  159.612 1.00 75.16  ? 370 VAL B CG2 1 
ATOM 6514 N N   . ASN B 1 325 ? -70.618 15.437  157.887 1.00 71.55  ? 371 ASN B N   1 
ATOM 6515 C CA  . ASN B 1 325 ? -69.869 16.161  156.858 1.00 72.38  ? 371 ASN B CA  1 
ATOM 6516 C C   . ASN B 1 325 ? -70.360 15.811  155.455 1.00 73.97  ? 371 ASN B C   1 
ATOM 6517 O O   . ASN B 1 325 ? -69.579 15.746  154.504 1.00 73.40  ? 371 ASN B O   1 
ATOM 6518 C CB  . ASN B 1 325 ? -68.366 15.908  156.988 1.00 74.97  ? 371 ASN B CB  1 
ATOM 6519 C CG  . ASN B 1 325 ? -67.755 16.638  158.166 1.00 78.02  ? 371 ASN B CG  1 
ATOM 6520 O OD1 . ASN B 1 325 ? -68.267 16.573  159.284 1.00 80.35  ? 371 ASN B OD1 1 
ATOM 6521 N ND2 . ASN B 1 325 ? -66.661 17.348  157.920 1.00 74.47  ? 371 ASN B ND2 1 
ATOM 6522 N N   . ASN B 1 326 ? -71.669 15.585  155.331 1.00 73.41  ? 372 ASN B N   1 
ATOM 6523 C CA  . ASN B 1 326 ? -72.318 15.323  154.047 1.00 72.45  ? 372 ASN B CA  1 
ATOM 6524 C C   . ASN B 1 326 ? -71.705 14.117  153.337 1.00 73.19  ? 372 ASN B C   1 
ATOM 6525 O O   . ASN B 1 326 ? -71.610 14.083  152.108 1.00 72.27  ? 372 ASN B O   1 
ATOM 6526 C CB  . ASN B 1 326 ? -72.273 16.564  153.148 1.00 72.74  ? 372 ASN B CB  1 
ATOM 6527 C CG  . ASN B 1 326 ? -73.257 16.493  151.996 1.00 76.11  ? 372 ASN B CG  1 
ATOM 6528 O OD1 . ASN B 1 326 ? -74.368 15.982  152.143 1.00 77.22  ? 372 ASN B OD1 1 
ATOM 6529 N ND2 . ASN B 1 326 ? -72.854 17.008  150.841 1.00 77.97  ? 372 ASN B ND2 1 
ATOM 6530 N N   . GLY B 1 327 ? -71.279 13.116  154.103 1.00 71.96  ? 373 GLY B N   1 
ATOM 6531 C CA  . GLY B 1 327 ? -70.732 11.907  153.524 1.00 69.97  ? 373 GLY B CA  1 
ATOM 6532 C C   . GLY B 1 327 ? -69.338 12.031  152.957 1.00 69.94  ? 373 GLY B C   1 
ATOM 6533 O O   . GLY B 1 327 ? -68.889 11.118  152.255 1.00 67.54  ? 373 GLY B O   1 
ATOM 6534 N N   . ALA B 1 328 ? -68.639 13.127  153.233 1.00 60.92  ? 374 ALA B N   1 
ATOM 6535 C CA  . ALA B 1 328 ? -67.308 13.325  152.685 1.00 57.10  ? 374 ALA B CA  1 
ATOM 6536 C C   . ALA B 1 328 ? -66.289 12.444  153.399 1.00 63.22  ? 374 ALA B C   1 
ATOM 6537 O O   . ALA B 1 328 ? -66.474 12.032  154.547 1.00 70.45  ? 374 ALA B O   1 
ATOM 6538 C CB  . ALA B 1 328 ? -66.898 14.792  152.797 1.00 61.79  ? 374 ALA B CB  1 
ATOM 6539 N N   . ILE B 1 329 ? -65.194 12.158  152.695 1.00 54.20  ? 375 ILE B N   1 
ATOM 6540 C CA  . ILE B 1 329 ? -64.097 11.391  153.276 1.00 48.83  ? 375 ILE B CA  1 
ATOM 6541 C C   . ILE B 1 329 ? -63.364 12.275  154.275 1.00 50.11  ? 375 ILE B C   1 
ATOM 6542 O O   . ILE B 1 329 ? -62.951 13.394  153.950 1.00 54.53  ? 375 ILE B O   1 
ATOM 6543 C CB  . ILE B 1 329 ? -63.150 10.880  152.184 1.00 44.35  ? 375 ILE B CB  1 
ATOM 6544 C CG1 . ILE B 1 329 ? -63.813 9.758   151.387 1.00 39.10  ? 375 ILE B CG1 1 
ATOM 6545 C CG2 . ILE B 1 329 ? -61.847 10.400  152.793 1.00 46.91  ? 375 ILE B CG2 1 
ATOM 6546 C CD1 . ILE B 1 329 ? -63.152 9.495   150.059 1.00 42.57  ? 375 ILE B CD1 1 
ATOM 6547 N N   . ILE B 1 330 ? -63.196 11.777  155.496 1.00 43.63  ? 376 ILE B N   1 
ATOM 6548 C CA  . ILE B 1 330 ? -62.639 12.551  156.598 1.00 44.99  ? 376 ILE B CA  1 
ATOM 6549 C C   . ILE B 1 330 ? -61.339 11.891  157.032 1.00 48.70  ? 376 ILE B C   1 
ATOM 6550 O O   . ILE B 1 330 ? -61.322 10.701  157.369 1.00 58.61  ? 376 ILE B O   1 
ATOM 6551 C CB  . ILE B 1 330 ? -63.624 12.644  157.772 1.00 51.06  ? 376 ILE B CB  1 
ATOM 6552 C CG1 . ILE B 1 330 ? -64.769 13.598  157.436 1.00 47.75  ? 376 ILE B CG1 1 
ATOM 6553 C CG2 . ILE B 1 330 ? -62.909 13.108  159.029 1.00 51.20  ? 376 ILE B CG2 1 
ATOM 6554 C CD1 . ILE B 1 330 ? -64.345 15.030  157.303 1.00 50.98  ? 376 ILE B CD1 1 
ATOM 6555 N N   . PHE B 1 331 ? -60.249 12.660  157.026 1.00 41.75  ? 377 PHE B N   1 
ATOM 6556 C CA  . PHE B 1 331 ? -58.963 12.157  157.507 1.00 42.79  ? 377 PHE B CA  1 
ATOM 6557 C C   . PHE B 1 331 ? -58.140 13.351  157.981 1.00 49.33  ? 377 PHE B C   1 
ATOM 6558 O O   . PHE B 1 331 ? -57.503 14.029  157.170 1.00 50.85  ? 377 PHE B O   1 
ATOM 6559 C CB  . PHE B 1 331 ? -58.237 11.376  156.422 1.00 40.82  ? 377 PHE B CB  1 
ATOM 6560 C CG  . PHE B 1 331 ? -56.868 10.917  156.824 1.00 44.22  ? 377 PHE B CG  1 
ATOM 6561 C CD1 . PHE B 1 331 ? -56.703 10.019  157.863 1.00 48.90  ? 377 PHE B CD1 1 
ATOM 6562 C CD2 . PHE B 1 331 ? -55.747 11.383  156.165 1.00 42.83  ? 377 PHE B CD2 1 
ATOM 6563 C CE1 . PHE B 1 331 ? -55.445 9.594   158.236 1.00 45.35  ? 377 PHE B CE1 1 
ATOM 6564 C CE2 . PHE B 1 331 ? -54.487 10.961  156.533 1.00 46.41  ? 377 PHE B CE2 1 
ATOM 6565 C CZ  . PHE B 1 331 ? -54.336 10.066  157.571 1.00 43.16  ? 377 PHE B CZ  1 
ATOM 6566 N N   . HIS B 1 332 ? -58.155 13.598  159.289 1.00 48.09  ? 378 HIS B N   1 
ATOM 6567 C CA  . HIS B 1 332 ? -57.365 14.665  159.894 1.00 45.26  ? 378 HIS B CA  1 
ATOM 6568 C C   . HIS B 1 332 ? -56.658 14.093  161.113 1.00 50.26  ? 378 HIS B C   1 
ATOM 6569 O O   . HIS B 1 332 ? -57.244 14.075  162.215 1.00 52.02  ? 378 HIS B O   1 
ATOM 6570 C CB  . HIS B 1 332 ? -58.240 15.860  160.275 1.00 42.44  ? 378 HIS B CB  1 
ATOM 6571 C CG  . HIS B 1 332 ? -59.564 15.478  160.860 1.00 50.71  ? 378 HIS B CG  1 
ATOM 6572 N ND1 . HIS B 1 332 ? -59.697 14.508  161.829 1.00 53.43  ? 378 HIS B ND1 1 
ATOM 6573 C CD2 . HIS B 1 332 ? -60.813 15.939  160.615 1.00 53.49  ? 378 HIS B CD2 1 
ATOM 6574 C CE1 . HIS B 1 332 ? -60.971 14.386  162.155 1.00 54.02  ? 378 HIS B CE1 1 
ATOM 6575 N NE2 . HIS B 1 332 ? -61.669 15.243  161.432 1.00 56.09  ? 378 HIS B NE2 1 
ATOM 6576 N N   . PRO B 1 333 ? -55.421 13.620  160.982 1.00 46.15  ? 379 PRO B N   1 
ATOM 6577 C CA  . PRO B 1 333 ? -54.739 13.017  162.131 1.00 41.81  ? 379 PRO B CA  1 
ATOM 6578 C C   . PRO B 1 333 ? -54.000 14.042  162.972 1.00 49.57  ? 379 PRO B C   1 
ATOM 6579 O O   . PRO B 1 333 ? -53.736 15.158  162.515 1.00 59.27  ? 379 PRO B O   1 
ATOM 6580 C CB  . PRO B 1 333 ? -53.772 12.027  161.476 1.00 41.52  ? 379 PRO B CB  1 
ATOM 6581 C CG  . PRO B 1 333 ? -53.498 12.603  160.111 1.00 40.19  ? 379 PRO B CG  1 
ATOM 6582 C CD  . PRO B 1 333 ? -54.580 13.605  159.774 1.00 43.81  ? 379 PRO B CD  1 
ATOM 6583 N N   . SER B 1 334 ? -53.659 13.673  164.202 1.00 50.44  ? 380 SER B N   1 
ATOM 6584 C CA  . SER B 1 334 ? -52.901 14.529  165.105 1.00 47.09  ? 380 SER B CA  1 
ATOM 6585 C C   . SER B 1 334 ? -51.489 13.975  165.222 1.00 43.05  ? 380 SER B C   1 
ATOM 6586 O O   . SER B 1 334 ? -51.303 12.816  165.604 1.00 49.93  ? 380 SER B O   1 
ATOM 6587 C CB  . SER B 1 334 ? -53.567 14.609  166.477 1.00 46.70  ? 380 SER B CB  1 
ATOM 6588 O OG  . SER B 1 334 ? -54.907 15.054  166.370 1.00 53.61  ? 380 SER B OG  1 
ATOM 6589 N N   . PHE B 1 335 ? -50.504 14.802  164.895 1.00 42.14  ? 381 PHE B N   1 
ATOM 6590 C CA  . PHE B 1 335 ? -49.112 14.387  164.901 1.00 45.55  ? 381 PHE B CA  1 
ATOM 6591 C C   . PHE B 1 335 ? -48.479 14.660  166.262 1.00 47.81  ? 381 PHE B C   1 
ATOM 6592 O O   . PHE B 1 335 ? -49.068 15.300  167.135 1.00 51.48  ? 381 PHE B O   1 
ATOM 6593 C CB  . PHE B 1 335 ? -48.344 15.107  163.796 1.00 45.96  ? 381 PHE B CB  1 
ATOM 6594 C CG  . PHE B 1 335 ? -48.746 14.695  162.412 1.00 43.89  ? 381 PHE B CG  1 
ATOM 6595 C CD1 . PHE B 1 335 ? -49.399 13.496  162.196 1.00 43.66  ? 381 PHE B CD1 1 
ATOM 6596 C CD2 . PHE B 1 335 ? -48.479 15.508  161.327 1.00 48.34  ? 381 PHE B CD2 1 
ATOM 6597 C CE1 . PHE B 1 335 ? -49.772 13.114  160.924 1.00 40.72  ? 381 PHE B CE1 1 
ATOM 6598 C CE2 . PHE B 1 335 ? -48.851 15.131  160.054 1.00 48.46  ? 381 PHE B CE2 1 
ATOM 6599 C CZ  . PHE B 1 335 ? -49.497 13.931  159.853 1.00 43.62  ? 381 PHE B CZ  1 
ATOM 6600 N N   . GLY B 1 336 ? -47.257 14.165  166.437 1.00 47.92  ? 382 GLY B N   1 
ATOM 6601 C CA  . GLY B 1 336 ? -46.531 14.342  167.677 1.00 48.43  ? 382 GLY B CA  1 
ATOM 6602 C C   . GLY B 1 336 ? -46.575 13.168  168.628 1.00 51.54  ? 382 GLY B C   1 
ATOM 6603 O O   . GLY B 1 336 ? -46.181 13.322  169.790 1.00 52.88  ? 382 GLY B O   1 
ATOM 6604 N N   . TYR B 1 337 ? -47.047 12.009  168.182 1.00 57.67  ? 383 TYR B N   1 
ATOM 6605 C CA  . TYR B 1 337 ? -47.104 10.830  169.032 1.00 57.50  ? 383 TYR B CA  1 
ATOM 6606 C C   . TYR B 1 337 ? -45.870 9.964   168.816 1.00 61.73  ? 383 TYR B C   1 
ATOM 6607 O O   . TYR B 1 337 ? -45.499 9.661   167.680 1.00 65.09  ? 383 TYR B O   1 
ATOM 6608 C CB  . TYR B 1 337 ? -48.370 10.027  168.735 1.00 56.27  ? 383 TYR B CB  1 
ATOM 6609 C CG  . TYR B 1 337 ? -48.624 8.884   169.688 1.00 55.67  ? 383 TYR B CG  1 
ATOM 6610 C CD1 . TYR B 1 337 ? -48.546 9.068   171.060 1.00 58.37  ? 383 TYR B CD1 1 
ATOM 6611 C CD2 . TYR B 1 337 ? -48.952 7.622   169.214 1.00 56.15  ? 383 TYR B CD2 1 
ATOM 6612 C CE1 . TYR B 1 337 ? -48.781 8.026   171.932 1.00 59.96  ? 383 TYR B CE1 1 
ATOM 6613 C CE2 . TYR B 1 337 ? -49.189 6.575   170.078 1.00 60.76  ? 383 TYR B CE2 1 
ATOM 6614 C CZ  . TYR B 1 337 ? -49.103 6.782   171.436 1.00 63.29  ? 383 TYR B CZ  1 
ATOM 6615 O OH  . TYR B 1 337 ? -49.338 5.741   172.304 1.00 67.10  ? 383 TYR B OH  1 
ATOM 6616 N N   . ASP B 1 338 ? -45.229 9.567   169.915 1.00 69.10  ? 384 ASP B N   1 
ATOM 6617 C CA  . ASP B 1 338 ? -44.041 8.727   169.849 1.00 68.88  ? 384 ASP B CA  1 
ATOM 6618 C C   . ASP B 1 338 ? -44.305 7.267   170.174 1.00 69.09  ? 384 ASP B C   1 
ATOM 6619 O O   . ASP B 1 338 ? -43.593 6.398   169.667 1.00 66.75  ? 384 ASP B O   1 
ATOM 6620 C CB  . ASP B 1 338 ? -42.962 9.249   170.803 1.00 66.71  ? 384 ASP B CB  1 
ATOM 6621 C CG  . ASP B 1 338 ? -43.506 9.559   172.177 1.00 73.25  ? 384 ASP B CG  1 
ATOM 6622 O OD1 . ASP B 1 338 ? -44.737 9.467   172.364 1.00 75.25  ? 384 ASP B OD1 1 
ATOM 6623 O OD2 . ASP B 1 338 ? -42.702 9.879   173.075 1.00 75.31  ? 384 ASP B OD2 1 
ATOM 6624 N N   . GLY B 1 339 ? -45.301 6.976   171.005 1.00 68.05  ? 385 GLY B N   1 
ATOM 6625 C CA  . GLY B 1 339 ? -45.609 5.609   171.369 1.00 65.31  ? 385 GLY B CA  1 
ATOM 6626 C C   . GLY B 1 339 ? -45.959 5.458   172.834 1.00 65.72  ? 385 GLY B C   1 
ATOM 6627 O O   . GLY B 1 339 ? -46.695 4.542   173.212 1.00 66.62  ? 385 GLY B O   1 
ATOM 6628 N N   . GLN B 1 340 ? -45.442 6.353   173.667 1.00 70.11  ? 386 GLN B N   1 
ATOM 6629 C CA  . GLN B 1 340 ? -45.722 6.356   175.093 1.00 69.46  ? 386 GLN B CA  1 
ATOM 6630 C C   . GLN B 1 340 ? -46.547 7.581   175.463 1.00 73.60  ? 386 GLN B C   1 
ATOM 6631 O O   . GLN B 1 340 ? -46.636 8.553   174.709 1.00 75.80  ? 386 GLN B O   1 
ATOM 6632 C CB  . GLN B 1 340 ? -44.427 6.326   175.911 1.00 72.62  ? 386 GLN B CB  1 
ATOM 6633 C CG  . GLN B 1 340 ? -43.280 5.599   175.231 1.00 75.73  ? 386 GLN B CG  1 
ATOM 6634 C CD  . GLN B 1 340 ? -41.938 5.931   175.849 1.00 79.76  ? 386 GLN B CD  1 
ATOM 6635 O OE1 . GLN B 1 340 ? -41.844 6.214   177.043 1.00 79.87  ? 386 GLN B OE1 1 
ATOM 6636 N NE2 . GLN B 1 340 ? -40.888 5.896   175.037 1.00 79.30  ? 386 GLN B NE2 1 
ATOM 6637 N N   . ASP B 1 341 ? -47.153 7.520   176.646 1.00 77.91  ? 387 ASP B N   1 
ATOM 6638 C CA  . ASP B 1 341 ? -48.077 8.557   177.100 1.00 77.39  ? 387 ASP B CA  1 
ATOM 6639 C C   . ASP B 1 341 ? -47.346 9.554   177.998 1.00 77.28  ? 387 ASP B C   1 
ATOM 6640 O O   . ASP B 1 341 ? -47.557 9.626   179.209 1.00 76.81  ? 387 ASP B O   1 
ATOM 6641 C CB  . ASP B 1 341 ? -49.264 7.921   177.818 1.00 77.70  ? 387 ASP B CB  1 
ATOM 6642 C CG  . ASP B 1 341 ? -50.498 8.796   177.791 1.00 79.97  ? 387 ASP B CG  1 
ATOM 6643 O OD1 . ASP B 1 341 ? -50.539 9.740   176.976 1.00 82.69  ? 387 ASP B OD1 1 
ATOM 6644 O OD2 . ASP B 1 341 ? -51.428 8.537   178.583 1.00 79.83  ? 387 ASP B OD2 1 
ATOM 6645 N N   . HIS B 1 342 ? -46.467 10.336  177.374 1.00 73.48  ? 388 HIS B N   1 
ATOM 6646 C CA  . HIS B 1 342 ? -45.741 11.388  178.076 1.00 71.09  ? 388 HIS B CA  1 
ATOM 6647 C C   . HIS B 1 342 ? -45.516 12.549  177.111 1.00 73.12  ? 388 HIS B C   1 
ATOM 6648 O O   . HIS B 1 342 ? -46.020 12.555  175.984 1.00 76.11  ? 388 HIS B O   1 
ATOM 6649 C CB  . HIS B 1 342 ? -44.432 10.852  178.669 1.00 70.15  ? 388 HIS B CB  1 
ATOM 6650 C CG  . HIS B 1 342 ? -43.414 10.465  177.644 1.00 71.24  ? 388 HIS B CG  1 
ATOM 6651 N ND1 . HIS B 1 342 ? -43.602 9.421   176.765 1.00 72.67  ? 388 HIS B ND1 1 
ATOM 6652 C CD2 . HIS B 1 342 ? -42.196 10.982  177.359 1.00 72.43  ? 388 HIS B CD2 1 
ATOM 6653 C CE1 . HIS B 1 342 ? -42.543 9.310   175.984 1.00 71.07  ? 388 HIS B CE1 1 
ATOM 6654 N NE2 . HIS B 1 342 ? -41.676 10.246  176.322 1.00 72.17  ? 388 HIS B NE2 1 
ATOM 6655 N N   . GLU B 1 343 ? -44.745 13.540  177.564 1.00 72.08  ? 389 GLU B N   1 
ATOM 6656 C CA  . GLU B 1 343 ? -44.626 14.803  176.839 1.00 69.89  ? 389 GLU B CA  1 
ATOM 6657 C C   . GLU B 1 343 ? -43.876 14.654  175.520 1.00 71.77  ? 389 GLU B C   1 
ATOM 6658 O O   . GLU B 1 343 ? -44.292 15.229  174.508 1.00 72.50  ? 389 GLU B O   1 
ATOM 6659 C CB  . GLU B 1 343 ? -43.935 15.845  177.718 1.00 69.41  ? 389 GLU B CB  1 
ATOM 6660 C CG  . GLU B 1 343 ? -44.575 17.221  177.665 1.00 73.25  ? 389 GLU B CG  1 
ATOM 6661 C CD  . GLU B 1 343 ? -44.207 17.987  176.410 1.00 74.83  ? 389 GLU B CD  1 
ATOM 6662 O OE1 . GLU B 1 343 ? -43.176 17.655  175.790 1.00 76.50  ? 389 GLU B OE1 1 
ATOM 6663 O OE2 . GLU B 1 343 ? -44.943 18.927  176.048 1.00 70.37  ? 389 GLU B OE2 1 
ATOM 6664 N N   . GLU B 1 344 ? -42.773 13.901  175.510 1.00 69.94  ? 390 GLU B N   1 
ATOM 6665 C CA  . GLU B 1 344 ? -41.894 13.783  174.344 1.00 69.33  ? 390 GLU B CA  1 
ATOM 6666 C C   . GLU B 1 344 ? -41.383 15.172  173.937 1.00 69.56  ? 390 GLU B C   1 
ATOM 6667 O O   . GLU B 1 344 ? -41.766 15.758  172.922 1.00 67.45  ? 390 GLU B O   1 
ATOM 6668 C CB  . GLU B 1 344 ? -42.602 13.050  173.195 1.00 66.18  ? 390 GLU B CB  1 
ATOM 6669 C CG  . GLU B 1 344 ? -41.866 13.042  171.859 1.00 67.11  ? 390 GLU B CG  1 
ATOM 6670 C CD  . GLU B 1 344 ? -40.474 12.450  171.963 1.00 70.42  ? 390 GLU B CD  1 
ATOM 6671 O OE1 . GLU B 1 344 ? -40.348 11.209  171.900 1.00 73.76  ? 390 GLU B OE1 1 
ATOM 6672 O OE2 . GLU B 1 344 ? -39.505 13.223  172.109 1.00 66.16  ? 390 GLU B OE2 1 
ATOM 6673 N N   . LEU B 1 345 ? -40.541 15.712  174.821 1.00 58.73  ? 391 LEU B N   1 
ATOM 6674 C CA  . LEU B 1 345 ? -40.065 17.088  174.731 1.00 54.76  ? 391 LEU B CA  1 
ATOM 6675 C C   . LEU B 1 345 ? -39.365 17.407  173.418 1.00 53.62  ? 391 LEU B C   1 
ATOM 6676 O O   . LEU B 1 345 ? -39.355 18.575  173.015 1.00 52.38  ? 391 LEU B O   1 
ATOM 6677 C CB  . LEU B 1 345 ? -39.110 17.376  175.889 1.00 54.94  ? 391 LEU B CB  1 
ATOM 6678 C CG  . LEU B 1 345 ? -39.733 17.827  177.208 1.00 55.84  ? 391 LEU B CG  1 
ATOM 6679 C CD1 . LEU B 1 345 ? -38.703 17.788  178.321 1.00 55.18  ? 391 LEU B CD1 1 
ATOM 6680 C CD2 . LEU B 1 345 ? -40.310 19.216  177.065 1.00 53.96  ? 391 LEU B CD2 1 
ATOM 6681 N N   . SER B 1 346 ? -38.787 16.412  172.744 1.00 57.99  ? 392 SER B N   1 
ATOM 6682 C CA  . SER B 1 346 ? -38.002 16.675  171.543 1.00 53.95  ? 392 SER B CA  1 
ATOM 6683 C C   . SER B 1 346 ? -38.831 17.254  170.406 1.00 52.02  ? 392 SER B C   1 
ATOM 6684 O O   . SER B 1 346 ? -38.261 17.834  169.477 1.00 56.78  ? 392 SER B O   1 
ATOM 6685 C CB  . SER B 1 346 ? -37.318 15.393  171.070 1.00 55.52  ? 392 SER B CB  1 
ATOM 6686 O OG  . SER B 1 346 ? -38.168 14.651  170.213 1.00 58.56  ? 392 SER B OG  1 
ATOM 6687 N N   . PHE B 1 347 ? -40.154 17.110  170.449 1.00 49.47  ? 393 PHE B N   1 
ATOM 6688 C CA  . PHE B 1 347 ? -40.990 17.563  169.347 1.00 47.75  ? 393 PHE B CA  1 
ATOM 6689 C C   . PHE B 1 347 ? -41.234 19.065  169.359 1.00 53.91  ? 393 PHE B C   1 
ATOM 6690 O O   . PHE B 1 347 ? -41.779 19.592  168.383 1.00 58.40  ? 393 PHE B O   1 
ATOM 6691 C CB  . PHE B 1 347 ? -42.323 16.815  169.361 1.00 48.44  ? 393 PHE B CB  1 
ATOM 6692 C CG  . PHE B 1 347 ? -42.410 15.728  168.331 1.00 53.99  ? 393 PHE B CG  1 
ATOM 6693 C CD1 . PHE B 1 347 ? -42.403 16.033  166.983 1.00 53.09  ? 393 PHE B CD1 1 
ATOM 6694 C CD2 . PHE B 1 347 ? -42.475 14.400  168.710 1.00 51.30  ? 393 PHE B CD2 1 
ATOM 6695 C CE1 . PHE B 1 347 ? -42.472 15.038  166.035 1.00 50.02  ? 393 PHE B CE1 1 
ATOM 6696 C CE2 . PHE B 1 347 ? -42.545 13.400  167.766 1.00 47.55  ? 393 PHE B CE2 1 
ATOM 6697 C CZ  . PHE B 1 347 ? -42.544 13.720  166.426 1.00 50.67  ? 393 PHE B CZ  1 
ATOM 6698 N N   . ARG B 1 348 ? -40.851 19.765  170.430 1.00 57.34  ? 394 ARG B N   1 
ATOM 6699 C CA  . ARG B 1 348 ? -40.962 21.218  170.450 1.00 50.73  ? 394 ARG B CA  1 
ATOM 6700 C C   . ARG B 1 348 ? -40.051 21.881  169.428 1.00 52.65  ? 394 ARG B C   1 
ATOM 6701 O O   . ARG B 1 348 ? -40.359 22.983  168.965 1.00 58.22  ? 394 ARG B O   1 
ATOM 6702 C CB  . ARG B 1 348 ? -40.645 21.757  171.845 1.00 51.40  ? 394 ARG B CB  1 
ATOM 6703 C CG  . ARG B 1 348 ? -41.585 21.275  172.932 1.00 52.50  ? 394 ARG B CG  1 
ATOM 6704 C CD  . ARG B 1 348 ? -41.253 21.915  174.269 1.00 53.18  ? 394 ARG B CD  1 
ATOM 6705 N NE  . ARG B 1 348 ? -42.175 21.493  175.316 1.00 55.61  ? 394 ARG B NE  1 
ATOM 6706 C CZ  . ARG B 1 348 ? -42.161 21.955  176.558 1.00 56.95  ? 394 ARG B CZ  1 
ATOM 6707 N NH1 . ARG B 1 348 ? -41.274 22.854  176.951 1.00 54.02  ? 394 ARG B NH1 1 
ATOM 6708 N NH2 . ARG B 1 348 ? -43.053 21.496  177.431 1.00 58.45  ? 394 ARG B NH2 1 
ATOM 6709 N N   . ALA B 1 349 ? -38.939 21.238  169.068 1.00 48.06  ? 395 ALA B N   1 
ATOM 6710 C CA  . ALA B 1 349 ? -38.001 21.808  168.110 1.00 46.80  ? 395 ALA B CA  1 
ATOM 6711 C C   . ALA B 1 349 ? -38.575 21.911  166.705 1.00 49.73  ? 395 ALA B C   1 
ATOM 6712 O O   . ALA B 1 349 ? -38.001 22.620  165.873 1.00 50.67  ? 395 ALA B O   1 
ATOM 6713 C CB  . ALA B 1 349 ? -36.718 20.978  168.078 1.00 43.68  ? 395 ALA B CB  1 
ATOM 6714 N N   . MET B 1 350 ? -39.678 21.227  166.420 1.00 45.22  ? 396 MET B N   1 
ATOM 6715 C CA  . MET B 1 350 ? -40.294 21.250  165.101 1.00 50.35  ? 396 MET B CA  1 
ATOM 6716 C C   . MET B 1 350 ? -41.266 22.405  164.915 1.00 50.20  ? 396 MET B C   1 
ATOM 6717 O O   . MET B 1 350 ? -41.877 22.515  163.847 1.00 48.90  ? 396 MET B O   1 
ATOM 6718 C CB  . MET B 1 350 ? -41.013 19.928  164.832 1.00 47.88  ? 396 MET B CB  1 
ATOM 6719 C CG  . MET B 1 350 ? -40.086 18.806  164.429 1.00 40.72  ? 396 MET B CG  1 
ATOM 6720 S SD  . MET B 1 350 ? -38.887 19.365  163.214 1.00 58.88  ? 396 MET B SD  1 
ATOM 6721 C CE  . MET B 1 350 ? -38.567 17.836  162.354 1.00 43.24  ? 396 MET B CE  1 
ATOM 6722 N N   . CYS B 1 351 ? -41.435 23.258  165.924 1.00 42.68  ? 397 CYS B N   1 
ATOM 6723 C CA  . CYS B 1 351 ? -42.303 24.419  165.799 1.00 44.83  ? 397 CYS B CA  1 
ATOM 6724 C C   . CYS B 1 351 ? -41.691 25.527  164.954 1.00 48.36  ? 397 CYS B C   1 
ATOM 6725 O O   . CYS B 1 351 ? -42.399 26.474  164.599 1.00 46.14  ? 397 CYS B O   1 
ATOM 6726 C CB  . CYS B 1 351 ? -42.649 24.958  167.186 1.00 47.43  ? 397 CYS B CB  1 
ATOM 6727 S SG  . CYS B 1 351 ? -43.748 23.888  168.134 1.00 50.00  ? 397 CYS B SG  1 
ATOM 6728 N N   . SER B 1 352 ? -40.405 25.436  164.631 1.00 46.49  ? 398 SER B N   1 
ATOM 6729 C CA  . SER B 1 352 ? -39.765 26.406  163.760 1.00 42.40  ? 398 SER B CA  1 
ATOM 6730 C C   . SER B 1 352 ? -40.018 26.061  162.295 1.00 46.11  ? 398 SER B C   1 
ATOM 6731 O O   . SER B 1 352 ? -40.359 24.930  161.944 1.00 53.51  ? 398 SER B O   1 
ATOM 6732 C CB  . SER B 1 352 ? -38.264 26.463  164.032 1.00 44.08  ? 398 SER B CB  1 
ATOM 6733 O OG  . SER B 1 352 ? -37.569 25.526  163.229 1.00 52.53  ? 398 SER B OG  1 
ATOM 6734 N N   . ASN B 1 353 ? -39.849 27.062  161.437 1.00 38.06  ? 399 ASN B N   1 
ATOM 6735 C CA  . ASN B 1 353 ? -40.053 26.869  160.009 1.00 34.65  ? 399 ASN B CA  1 
ATOM 6736 C C   . ASN B 1 353 ? -38.981 25.954  159.436 1.00 45.65  ? 399 ASN B C   1 
ATOM 6737 O O   . ASN B 1 353 ? -37.809 26.031  159.813 1.00 53.79  ? 399 ASN B O   1 
ATOM 6738 C CB  . ASN B 1 353 ? -40.033 28.214  159.286 1.00 40.17  ? 399 ASN B CB  1 
ATOM 6739 C CG  . ASN B 1 353 ? -41.283 29.029  159.538 1.00 52.56  ? 399 ASN B CG  1 
ATOM 6740 O OD1 . ASN B 1 353 ? -42.399 28.528  159.422 1.00 51.39  ? 399 ASN B OD1 1 
ATOM 6741 N ND2 . ASN B 1 353 ? -41.100 30.293  159.898 1.00 49.75  ? 399 ASN B ND2 1 
ATOM 6742 N N   . MET B 1 354 ? -39.385 25.078  158.522 1.00 42.60  ? 400 MET B N   1 
ATOM 6743 C CA  . MET B 1 354 ? -38.427 24.185  157.894 1.00 38.24  ? 400 MET B CA  1 
ATOM 6744 C C   . MET B 1 354 ? -37.597 24.937  156.861 1.00 41.12  ? 400 MET B C   1 
ATOM 6745 O O   . MET B 1 354 ? -37.989 25.990  156.354 1.00 47.77  ? 400 MET B O   1 
ATOM 6746 C CB  . MET B 1 354 ? -39.130 22.999  157.235 1.00 41.68  ? 400 MET B CB  1 
ATOM 6747 C CG  . MET B 1 354 ? -39.781 23.319  155.905 1.00 43.44  ? 400 MET B CG  1 
ATOM 6748 S SD  . MET B 1 354 ? -39.776 21.922  154.767 1.00 55.44  ? 400 MET B SD  1 
ATOM 6749 C CE  . MET B 1 354 ? -38.080 21.372  154.906 1.00 47.55  ? 400 MET B CE  1 
ATOM 6750 N N   . ILE B 1 355 ? -36.429 24.380  156.557 1.00 38.74  ? 401 ILE B N   1 
ATOM 6751 C CA  . ILE B 1 355 ? -35.511 24.947  155.579 1.00 38.09  ? 401 ILE B CA  1 
ATOM 6752 C C   . ILE B 1 355 ? -35.374 23.952  154.439 1.00 41.90  ? 401 ILE B C   1 
ATOM 6753 O O   . ILE B 1 355 ? -34.944 22.813  154.655 1.00 46.14  ? 401 ILE B O   1 
ATOM 6754 C CB  . ILE B 1 355 ? -34.138 25.258  156.194 1.00 32.19  ? 401 ILE B CB  1 
ATOM 6755 C CG1 . ILE B 1 355 ? -34.263 26.372  157.230 1.00 37.83  ? 401 ILE B CG1 1 
ATOM 6756 C CG2 . ILE B 1 355 ? -33.147 25.644  155.117 1.00 38.10  ? 401 ILE B CG2 1 
ATOM 6757 C CD1 . ILE B 1 355 ? -33.027 26.559  158.059 1.00 37.92  ? 401 ILE B CD1 1 
ATOM 6758 N N   . LEU B 1 356 ? -35.735 24.375  153.232 1.00 40.70  ? 402 LEU B N   1 
ATOM 6759 C CA  . LEU B 1 356 ? -35.656 23.511  152.062 1.00 42.37  ? 402 LEU B CA  1 
ATOM 6760 C C   . LEU B 1 356 ? -34.283 23.674  151.423 1.00 45.70  ? 402 LEU B C   1 
ATOM 6761 O O   . LEU B 1 356 ? -34.001 24.698  150.793 1.00 49.29  ? 402 LEU B O   1 
ATOM 6762 C CB  . LEU B 1 356 ? -36.771 23.837  151.069 1.00 42.42  ? 402 LEU B CB  1 
ATOM 6763 C CG  . LEU B 1 356 ? -36.722 23.161  149.698 1.00 40.37  ? 402 LEU B CG  1 
ATOM 6764 C CD1 . LEU B 1 356 ? -38.077 22.575  149.353 1.00 44.25  ? 402 LEU B CD1 1 
ATOM 6765 C CD2 . LEU B 1 356 ? -36.294 24.144  148.625 1.00 42.31  ? 402 LEU B CD2 1 
ATOM 6766 N N   . ASN B 1 357 ? -33.431 22.670  151.594 1.00 45.66  ? 403 ASN B N   1 
ATOM 6767 C CA  . ASN B 1 357 ? -32.079 22.681  151.058 1.00 37.70  ? 403 ASN B CA  1 
ATOM 6768 C C   . ASN B 1 357 ? -32.045 21.893  149.758 1.00 45.38  ? 403 ASN B C   1 
ATOM 6769 O O   . ASN B 1 357 ? -32.552 20.769  149.697 1.00 56.43  ? 403 ASN B O   1 
ATOM 6770 C CB  . ASN B 1 357 ? -31.093 22.087  152.064 1.00 39.38  ? 403 ASN B CB  1 
ATOM 6771 C CG  . ASN B 1 357 ? -29.657 22.217  151.616 1.00 45.92  ? 403 ASN B CG  1 
ATOM 6772 O OD1 . ASN B 1 357 ? -29.348 22.975  150.698 1.00 55.50  ? 403 ASN B OD1 1 
ATOM 6773 N ND2 . ASN B 1 357 ? -28.767 21.474  152.260 1.00 45.96  ? 403 ASN B ND2 1 
ATOM 6774 N N   . LEU B 1 358 ? -31.454 22.484  148.723 1.00 40.55  ? 404 LEU B N   1 
ATOM 6775 C CA  . LEU B 1 358 ? -31.383 21.837  147.426 1.00 45.51  ? 404 LEU B CA  1 
ATOM 6776 C C   . LEU B 1 358 ? -29.972 21.929  146.862 1.00 50.55  ? 404 LEU B C   1 
ATOM 6777 O O   . LEU B 1 358 ? -29.273 22.924  147.086 1.00 51.28  ? 404 LEU B O   1 
ATOM 6778 C CB  . LEU B 1 358 ? -32.372 22.473  146.441 1.00 44.87  ? 404 LEU B CB  1 
ATOM 6779 C CG  . LEU B 1 358 ? -33.849 22.159  146.669 1.00 40.81  ? 404 LEU B CG  1 
ATOM 6780 C CD1 . LEU B 1 358 ? -34.697 22.737  145.552 1.00 44.22  ? 404 LEU B CD1 1 
ATOM 6781 C CD2 . LEU B 1 358 ? -34.054 20.663  146.777 1.00 47.50  ? 404 LEU B CD2 1 
ATOM 6782 N N   . PRO B 1 359 ? -29.528 20.913  146.131 1.00 53.12  ? 405 PRO B N   1 
ATOM 6783 C CA  . PRO B 1 359 ? -28.221 20.985  145.477 1.00 50.77  ? 405 PRO B CA  1 
ATOM 6784 C C   . PRO B 1 359 ? -28.270 21.853  144.229 1.00 53.82  ? 405 PRO B C   1 
ATOM 6785 O O   . PRO B 1 359 ? -29.333 22.169  143.693 1.00 57.69  ? 405 PRO B O   1 
ATOM 6786 C CB  . PRO B 1 359 ? -27.928 19.526  145.118 1.00 49.66  ? 405 PRO B CB  1 
ATOM 6787 C CG  . PRO B 1 359 ? -29.277 18.926  144.930 1.00 53.58  ? 405 PRO B CG  1 
ATOM 6788 C CD  . PRO B 1 359 ? -30.178 19.607  145.926 1.00 52.79  ? 405 PRO B CD  1 
ATOM 6789 N N   . GLY B 1 360 ? -27.085 22.228  143.765 1.00 55.01  ? 406 GLY B N   1 
ATOM 6790 C CA  . GLY B 1 360 ? -26.986 23.044  142.576 1.00 56.80  ? 406 GLY B CA  1 
ATOM 6791 C C   . GLY B 1 360 ? -27.304 24.505  142.849 1.00 58.05  ? 406 GLY B C   1 
ATOM 6792 O O   . GLY B 1 360 ? -27.400 24.959  143.989 1.00 58.83  ? 406 GLY B O   1 
ATOM 6793 N N   . GLU B 1 361 ? -27.471 25.246  141.756 1.00 66.05  ? 407 GLU B N   1 
ATOM 6794 C CA  . GLU B 1 361 ? -27.737 26.677  141.813 1.00 66.18  ? 407 GLU B CA  1 
ATOM 6795 C C   . GLU B 1 361 ? -29.118 27.041  141.291 1.00 68.15  ? 407 GLU B C   1 
ATOM 6796 O O   . GLU B 1 361 ? -29.836 27.816  141.930 1.00 66.15  ? 407 GLU B O   1 
ATOM 6797 C CB  . GLU B 1 361 ? -26.665 27.441  141.023 1.00 67.56  ? 407 GLU B CB  1 
ATOM 6798 C CG  . GLU B 1 361 ? -26.344 28.818  141.584 1.00 71.02  ? 407 GLU B CG  1 
ATOM 6799 C CD  . GLU B 1 361 ? -25.488 28.754  142.837 1.00 74.76  ? 407 GLU B CD  1 
ATOM 6800 O OE1 . GLU B 1 361 ? -25.937 29.246  143.893 1.00 77.69  ? 407 GLU B OE1 1 
ATOM 6801 O OE2 . GLU B 1 361 ? -24.365 28.213  142.763 1.00 68.84  ? 407 GLU B OE2 1 
ATOM 6802 N N   . ALA B 1 362 ? -29.512 26.502  140.142 1.00 65.25  ? 408 ALA B N   1 
ATOM 6803 C CA  . ALA B 1 362 ? -30.820 26.766  139.557 1.00 61.83  ? 408 ALA B CA  1 
ATOM 6804 C C   . ALA B 1 362 ? -31.717 25.552  139.749 1.00 63.27  ? 408 ALA B C   1 
ATOM 6805 O O   . ALA B 1 362 ? -31.362 24.442  139.339 1.00 64.25  ? 408 ALA B O   1 
ATOM 6806 C CB  . ALA B 1 362 ? -30.695 27.103  138.071 1.00 60.14  ? 408 ALA B CB  1 
ATOM 6807 N N   . HIS B 1 363 ? -32.876 25.765  140.366 1.00 56.45  ? 409 HIS B N   1 
ATOM 6808 C CA  . HIS B 1 363 ? -33.818 24.698  140.672 1.00 55.55  ? 409 HIS B CA  1 
ATOM 6809 C C   . HIS B 1 363 ? -35.098 24.905  139.880 1.00 56.37  ? 409 HIS B C   1 
ATOM 6810 O O   . HIS B 1 363 ? -35.702 25.980  139.939 1.00 58.32  ? 409 HIS B O   1 
ATOM 6811 C CB  . HIS B 1 363 ? -34.134 24.653  142.167 1.00 52.22  ? 409 HIS B CB  1 
ATOM 6812 C CG  . HIS B 1 363 ? -32.965 24.976  143.041 1.00 52.60  ? 409 HIS B CG  1 
ATOM 6813 N ND1 . HIS B 1 363 ? -31.816 24.216  143.054 1.00 53.84  ? 409 HIS B ND1 1 
ATOM 6814 C CD2 . HIS B 1 363 ? -32.767 25.975  143.932 1.00 51.63  ? 409 HIS B CD2 1 
ATOM 6815 C CE1 . HIS B 1 363 ? -30.960 24.734  143.916 1.00 54.03  ? 409 HIS B CE1 1 
ATOM 6816 N NE2 . HIS B 1 363 ? -31.512 25.801  144.463 1.00 57.66  ? 409 HIS B NE2 1 
ATOM 6817 N N   . SER B 1 364 ? -35.512 23.876  139.149 1.00 55.95  ? 410 SER B N   1 
ATOM 6818 C CA  . SER B 1 364 ? -36.757 23.953  138.407 1.00 52.55  ? 410 SER B CA  1 
ATOM 6819 C C   . SER B 1 364 ? -37.947 23.745  139.339 1.00 55.01  ? 410 SER B C   1 
ATOM 6820 O O   . SER B 1 364 ? -37.818 23.234  140.455 1.00 59.70  ? 410 SER B O   1 
ATOM 6821 C CB  . SER B 1 364 ? -36.779 22.918  137.284 1.00 57.46  ? 410 SER B CB  1 
ATOM 6822 O OG  . SER B 1 364 ? -36.231 21.685  137.713 1.00 59.73  ? 410 SER B OG  1 
ATOM 6823 N N   . ALA B 1 365 ? -39.122 24.159  138.862 1.00 55.07  ? 411 ALA B N   1 
ATOM 6824 C CA  . ALA B 1 365 ? -40.342 23.968  139.638 1.00 48.17  ? 411 ALA B CA  1 
ATOM 6825 C C   . ALA B 1 365 ? -40.622 22.489  139.866 1.00 48.48  ? 411 ALA B C   1 
ATOM 6826 O O   . ALA B 1 365 ? -41.129 22.105  140.926 1.00 48.15  ? 411 ALA B O   1 
ATOM 6827 C CB  . ALA B 1 365 ? -41.520 24.640  138.936 1.00 47.55  ? 411 ALA B CB  1 
ATOM 6828 N N   . GLU B 1 366 ? -40.287 21.644  138.885 1.00 56.85  ? 412 GLU B N   1 
ATOM 6829 C CA  . GLU B 1 366 ? -40.399 20.201  139.067 1.00 54.82  ? 412 GLU B CA  1 
ATOM 6830 C C   . GLU B 1 366 ? -39.607 19.732  140.281 1.00 57.74  ? 412 GLU B C   1 
ATOM 6831 O O   . GLU B 1 366 ? -40.145 19.035  141.149 1.00 58.58  ? 412 GLU B O   1 
ATOM 6832 C CB  . GLU B 1 366 ? -39.913 19.477  137.808 1.00 59.02  ? 412 GLU B CB  1 
ATOM 6833 C CG  . GLU B 1 366 ? -40.470 19.962  136.451 1.00 63.23  ? 412 GLU B CG  1 
ATOM 6834 C CD  . GLU B 1 366 ? -41.923 20.433  136.470 1.00 64.96  ? 412 GLU B CD  1 
ATOM 6835 O OE1 . GLU B 1 366 ? -42.726 19.920  137.274 1.00 66.81  ? 412 GLU B OE1 1 
ATOM 6836 O OE2 . GLU B 1 366 ? -42.259 21.329  135.666 1.00 62.68  ? 412 GLU B OE2 1 
ATOM 6837 N N   . MET B 1 367 ? -38.331 20.114  140.366 1.00 57.50  ? 413 MET B N   1 
ATOM 6838 C CA  . MET B 1 367 ? -37.500 19.675  141.481 1.00 51.05  ? 413 MET B CA  1 
ATOM 6839 C C   . MET B 1 367 ? -37.971 20.289  142.793 1.00 51.45  ? 413 MET B C   1 
ATOM 6840 O O   . MET B 1 367 ? -37.977 19.618  143.831 1.00 58.58  ? 413 MET B O   1 
ATOM 6841 C CB  . MET B 1 367 ? -36.037 20.023  141.205 1.00 55.19  ? 413 MET B CB  1 
ATOM 6842 C CG  . MET B 1 367 ? -35.240 20.482  142.414 1.00 61.43  ? 413 MET B CG  1 
ATOM 6843 S SD  . MET B 1 367 ? -34.845 19.122  143.530 1.00 80.98  ? 413 MET B SD  1 
ATOM 6844 C CE  . MET B 1 367 ? -33.982 18.014  142.419 1.00 60.92  ? 413 MET B CE  1 
ATOM 6845 N N   . ILE B 1 368 ? -38.386 21.555  142.765 1.00 42.38  ? 414 ILE B N   1 
ATOM 6846 C CA  . ILE B 1 368 ? -38.826 22.209  143.992 1.00 41.99  ? 414 ILE B CA  1 
ATOM 6847 C C   . ILE B 1 368 ? -40.076 21.532  144.541 1.00 43.50  ? 414 ILE B C   1 
ATOM 6848 O O   . ILE B 1 368 ? -40.212 21.342  145.755 1.00 49.09  ? 414 ILE B O   1 
ATOM 6849 C CB  . ILE B 1 368 ? -39.050 23.712  143.748 1.00 46.28  ? 414 ILE B CB  1 
ATOM 6850 C CG1 . ILE B 1 368 ? -37.717 24.421  143.514 1.00 48.83  ? 414 ILE B CG1 1 
ATOM 6851 C CG2 . ILE B 1 368 ? -39.741 24.343  144.934 1.00 42.25  ? 414 ILE B CG2 1 
ATOM 6852 C CD1 . ILE B 1 368 ? -37.869 25.801  142.920 1.00 44.72  ? 414 ILE B CD1 1 
ATOM 6853 N N   . ILE B 1 369 ? -41.007 21.153  143.661 1.00 49.57  ? 415 ILE B N   1 
ATOM 6854 C CA  . ILE B 1 369 ? -42.227 20.492  144.111 1.00 49.23  ? 415 ILE B CA  1 
ATOM 6855 C C   . ILE B 1 369 ? -41.991 19.033  144.487 1.00 52.15  ? 415 ILE B C   1 
ATOM 6856 O O   . ILE B 1 369 ? -42.658 18.524  145.395 1.00 51.40  ? 415 ILE B O   1 
ATOM 6857 C CB  . ILE B 1 369 ? -43.332 20.626  143.042 1.00 46.27  ? 415 ILE B CB  1 
ATOM 6858 C CG1 . ILE B 1 369 ? -44.710 20.678  143.700 1.00 43.31  ? 415 ILE B CG1 1 
ATOM 6859 C CG2 . ILE B 1 369 ? -43.268 19.504  142.027 1.00 48.39  ? 415 ILE B CG2 1 
ATOM 6860 C CD1 . ILE B 1 369 ? -45.055 22.023  144.278 1.00 50.60  ? 415 ILE B CD1 1 
ATOM 6861 N N   . GLU B 1 370 ? -41.060 18.339  143.827 1.00 51.04  ? 416 GLU B N   1 
ATOM 6862 C CA  . GLU B 1 370 ? -40.782 16.949  144.160 1.00 43.71  ? 416 GLU B CA  1 
ATOM 6863 C C   . GLU B 1 370 ? -39.881 16.797  145.374 1.00 44.05  ? 416 GLU B C   1 
ATOM 6864 O O   . GLU B 1 370 ? -39.805 15.701  145.938 1.00 53.02  ? 416 GLU B O   1 
ATOM 6865 C CB  . GLU B 1 370 ? -40.132 16.232  142.971 1.00 51.02  ? 416 GLU B CB  1 
ATOM 6866 C CG  . GLU B 1 370 ? -41.002 16.120  141.724 1.00 53.89  ? 416 GLU B CG  1 
ATOM 6867 C CD  . GLU B 1 370 ? -42.042 15.018  141.807 1.00 56.95  ? 416 GLU B CD  1 
ATOM 6868 O OE1 . GLU B 1 370 ? -42.323 14.529  142.919 1.00 56.73  ? 416 GLU B OE1 1 
ATOM 6869 O OE2 . GLU B 1 370 ? -42.579 14.637  140.747 1.00 59.39  ? 416 GLU B OE2 1 
ATOM 6870 N N   . ALA B 1 371 ? -39.206 17.862  145.794 1.00 39.80  ? 417 ALA B N   1 
ATOM 6871 C CA  . ALA B 1 371 ? -38.276 17.782  146.908 1.00 44.59  ? 417 ALA B CA  1 
ATOM 6872 C C   . ALA B 1 371 ? -38.941 17.975  148.260 1.00 42.60  ? 417 ALA B C   1 
ATOM 6873 O O   . ALA B 1 371 ? -38.275 17.814  149.286 1.00 42.96  ? 417 ALA B O   1 
ATOM 6874 C CB  . ALA B 1 371 ? -37.164 18.820  146.741 1.00 40.17  ? 417 ALA B CB  1 
ATOM 6875 N N   . THR B 1 372 ? -40.230 18.303  148.293 1.00 44.33  ? 418 THR B N   1 
ATOM 6876 C CA  . THR B 1 372 ? -40.905 18.625  149.542 1.00 46.11  ? 418 THR B CA  1 
ATOM 6877 C C   . THR B 1 372 ? -42.190 17.823  149.708 1.00 44.92  ? 418 THR B C   1 
ATOM 6878 O O   . THR B 1 372 ? -43.139 18.285  150.345 1.00 51.33  ? 418 THR B O   1 
ATOM 6879 C CB  . THR B 1 372 ? -41.200 20.121  149.626 1.00 46.89  ? 418 THR B CB  1 
ATOM 6880 O OG1 . THR B 1 372 ? -41.981 20.389  150.795 1.00 51.06  ? 418 THR B OG1 1 
ATOM 6881 C CG2 . THR B 1 372 ? -41.969 20.578  148.399 1.00 42.25  ? 418 THR B CG2 1 
ATOM 6882 N N   . ARG B 1 373 ? -42.236 16.614  149.145 1.00 42.32  ? 419 ARG B N   1 
ATOM 6883 C CA  . ARG B 1 373 ? -43.435 15.795  149.273 1.00 42.56  ? 419 ARG B CA  1 
ATOM 6884 C C   . ARG B 1 373 ? -43.549 15.176  150.659 1.00 46.96  ? 419 ARG B C   1 
ATOM 6885 O O   . ARG B 1 373 ? -44.662 15.012  151.171 1.00 52.87  ? 419 ARG B O   1 
ATOM 6886 C CB  . ARG B 1 373 ? -43.445 14.707  148.203 1.00 42.66  ? 419 ARG B CB  1 
ATOM 6887 C CG  . ARG B 1 373 ? -43.172 15.227  146.811 1.00 45.57  ? 419 ARG B CG  1 
ATOM 6888 C CD  . ARG B 1 373 ? -43.740 14.303  145.757 1.00 48.82  ? 419 ARG B CD  1 
ATOM 6889 N NE  . ARG B 1 373 ? -45.135 14.603  145.463 1.00 43.99  ? 419 ARG B NE  1 
ATOM 6890 C CZ  . ARG B 1 373 ? -45.637 14.681  144.239 1.00 49.76  ? 419 ARG B CZ  1 
ATOM 6891 N NH1 . ARG B 1 373 ? -44.882 14.498  143.169 1.00 50.24  ? 419 ARG B NH1 1 
ATOM 6892 N NH2 . ARG B 1 373 ? -46.930 14.952  144.084 1.00 49.14  ? 419 ARG B NH2 1 
ATOM 6893 N N   . LEU B 1 374 ? -42.425 14.825  151.276 1.00 45.41  ? 420 LEU B N   1 
ATOM 6894 C CA  . LEU B 1 374 ? -42.419 14.235  152.606 1.00 40.58  ? 420 LEU B CA  1 
ATOM 6895 C C   . LEU B 1 374 ? -42.344 15.272  153.717 1.00 41.59  ? 420 LEU B C   1 
ATOM 6896 O O   . LEU B 1 374 ? -42.470 14.911  154.891 1.00 41.64  ? 420 LEU B O   1 
ATOM 6897 C CB  . LEU B 1 374 ? -41.253 13.251  152.742 1.00 33.82  ? 420 LEU B CB  1 
ATOM 6898 C CG  . LEU B 1 374 ? -41.102 12.208  151.635 1.00 35.12  ? 420 LEU B CG  1 
ATOM 6899 C CD1 . LEU B 1 374 ? -39.915 11.306  151.910 1.00 38.09  ? 420 LEU B CD1 1 
ATOM 6900 C CD2 . LEU B 1 374 ? -42.369 11.391  151.499 1.00 36.28  ? 420 LEU B CD2 1 
ATOM 6901 N N   . ALA B 1 375 ? -42.138 16.543  153.381 1.00 32.84  ? 421 ALA B N   1 
ATOM 6902 C CA  . ALA B 1 375 ? -42.052 17.583  154.395 1.00 31.21  ? 421 ALA B CA  1 
ATOM 6903 C C   . ALA B 1 375 ? -43.405 17.800  155.060 1.00 38.31  ? 421 ALA B C   1 
ATOM 6904 O O   . ALA B 1 375 ? -44.458 17.700  154.427 1.00 46.71  ? 421 ALA B O   1 
ATOM 6905 C CB  . ALA B 1 375 ? -41.556 18.889  153.779 1.00 31.50  ? 421 ALA B CB  1 
ATOM 6906 N N   . THR B 1 376 ? -43.369 18.098  156.357 1.00 39.82  ? 422 THR B N   1 
ATOM 6907 C CA  . THR B 1 376 ? -44.593 18.321  157.123 1.00 44.73  ? 422 THR B CA  1 
ATOM 6908 C C   . THR B 1 376 ? -44.247 19.133  158.358 1.00 44.57  ? 422 THR B C   1 
ATOM 6909 O O   . THR B 1 376 ? -43.429 18.695  159.173 1.00 50.10  ? 422 THR B O   1 
ATOM 6910 C CB  . THR B 1 376 ? -45.242 16.994  157.518 1.00 43.87  ? 422 THR B CB  1 
ATOM 6911 O OG1 . THR B 1 376 ? -45.780 16.356  156.355 1.00 41.78  ? 422 THR B OG1 1 
ATOM 6912 C CG2 . THR B 1 376 ? -46.361 17.228  158.518 1.00 41.19  ? 422 THR B CG2 1 
ATOM 6913 N N   . MET B 1 377 ? -44.867 20.301  158.504 1.00 41.55  ? 423 MET B N   1 
ATOM 6914 C CA  . MET B 1 377 ? -44.678 21.140  159.676 1.00 47.37  ? 423 MET B CA  1 
ATOM 6915 C C   . MET B 1 377 ? -45.983 21.264  160.446 1.00 44.49  ? 423 MET B C   1 
ATOM 6916 O O   . MET B 1 377 ? -47.072 21.240  159.867 1.00 42.85  ? 423 MET B O   1 
ATOM 6917 C CB  . MET B 1 377 ? -44.178 22.539  159.309 1.00 44.13  ? 423 MET B CB  1 
ATOM 6918 C CG  . MET B 1 377 ? -43.356 22.612  158.048 1.00 41.67  ? 423 MET B CG  1 
ATOM 6919 S SD  . MET B 1 377 ? -42.471 24.175  157.959 1.00 48.89  ? 423 MET B SD  1 
ATOM 6920 C CE  . MET B 1 377 ? -43.819 25.293  157.606 1.00 46.46  ? 423 MET B CE  1 
ATOM 6921 N N   . PHE B 1 378 ? -45.857 21.399  161.760 1.00 50.12  ? 424 PHE B N   1 
ATOM 6922 C CA  . PHE B 1 378 ? -47.013 21.585  162.615 1.00 49.57  ? 424 PHE B CA  1 
ATOM 6923 C C   . PHE B 1 378 ? -47.488 23.032  162.553 1.00 51.03  ? 424 PHE B C   1 
ATOM 6924 O O   . PHE B 1 378 ? -46.709 23.961  162.326 1.00 57.08  ? 424 PHE B O   1 
ATOM 6925 C CB  . PHE B 1 378 ? -46.682 21.199  164.055 1.00 49.46  ? 424 PHE B CB  1 
ATOM 6926 C CG  . PHE B 1 378 ? -46.046 19.846  164.189 1.00 52.27  ? 424 PHE B CG  1 
ATOM 6927 C CD1 . PHE B 1 378 ? -46.422 18.802  163.361 1.00 48.66  ? 424 PHE B CD1 1 
ATOM 6928 C CD2 . PHE B 1 378 ? -45.077 19.616  165.149 1.00 51.17  ? 424 PHE B CD2 1 
ATOM 6929 C CE1 . PHE B 1 378 ? -45.837 17.560  163.483 1.00 48.91  ? 424 PHE B CE1 1 
ATOM 6930 C CE2 . PHE B 1 378 ? -44.491 18.373  165.277 1.00 49.72  ? 424 PHE B CE2 1 
ATOM 6931 C CZ  . PHE B 1 378 ? -44.872 17.345  164.443 1.00 51.51  ? 424 PHE B CZ  1 
ATOM 6932 N N   . GLN B 1 379 ? -48.790 23.215  162.755 1.00 47.18  ? 425 GLN B N   1 
ATOM 6933 C CA  . GLN B 1 379 ? -49.397 24.539  162.731 1.00 48.67  ? 425 GLN B CA  1 
ATOM 6934 C C   . GLN B 1 379 ? -49.918 24.966  164.092 1.00 50.20  ? 425 GLN B C   1 
ATOM 6935 O O   . GLN B 1 379 ? -49.548 26.039  164.583 1.00 56.45  ? 425 GLN B O   1 
ATOM 6936 C CB  . GLN B 1 379 ? -50.534 24.578  161.700 1.00 46.87  ? 425 GLN B CB  1 
ATOM 6937 C CG  . GLN B 1 379 ? -51.447 25.780  161.840 1.00 53.24  ? 425 GLN B CG  1 
ATOM 6938 C CD  . GLN B 1 379 ? -52.225 26.069  160.576 1.00 57.20  ? 425 GLN B CD  1 
ATOM 6939 O OE1 . GLN B 1 379 ? -51.655 26.457  159.558 1.00 59.22  ? 425 GLN B OE1 1 
ATOM 6940 N NE2 . GLN B 1 379 ? -53.537 25.877  160.633 1.00 54.52  ? 425 GLN B NE2 1 
ATOM 6941 N N   . VAL B 1 380 ? -50.770 24.160  164.717 1.00 44.03  ? 426 VAL B N   1 
ATOM 6942 C CA  . VAL B 1 380 ? -51.336 24.484  166.021 1.00 47.66  ? 426 VAL B CA  1 
ATOM 6943 C C   . VAL B 1 380 ? -51.421 23.205  166.838 1.00 47.27  ? 426 VAL B C   1 
ATOM 6944 O O   . VAL B 1 380 ? -51.678 22.125  166.299 1.00 50.96  ? 426 VAL B O   1 
ATOM 6945 C CB  . VAL B 1 380 ? -52.723 25.149  165.894 1.00 52.37  ? 426 VAL B CB  1 
ATOM 6946 C CG1 . VAL B 1 380 ? -52.585 26.611  165.505 1.00 52.09  ? 426 VAL B CG1 1 
ATOM 6947 C CG2 . VAL B 1 380 ? -53.575 24.405  164.882 1.00 48.77  ? 426 VAL B CG2 1 
ATOM 6948 N N   . LYS B 1 381 ? -51.196 23.330  168.141 1.00 52.16  ? 427 LYS B N   1 
ATOM 6949 C CA  . LYS B 1 381 ? -51.349 22.192  169.034 1.00 51.96  ? 427 LYS B CA  1 
ATOM 6950 C C   . LYS B 1 381 ? -52.813 21.784  169.122 1.00 56.21  ? 427 LYS B C   1 
ATOM 6951 O O   . LYS B 1 381 ? -53.704 22.630  169.230 1.00 58.59  ? 427 LYS B O   1 
ATOM 6952 C CB  . LYS B 1 381 ? -50.823 22.531  170.427 1.00 50.83  ? 427 LYS B CB  1 
ATOM 6953 C CG  . LYS B 1 381 ? -49.356 22.895  170.473 1.00 59.65  ? 427 LYS B CG  1 
ATOM 6954 C CD  . LYS B 1 381 ? -48.884 23.047  171.907 1.00 62.02  ? 427 LYS B CD  1 
ATOM 6955 C CE  . LYS B 1 381 ? -49.670 24.123  172.636 1.00 59.48  ? 427 LYS B CE  1 
ATOM 6956 N NZ  . LYS B 1 381 ? -49.288 24.210  174.071 1.00 56.13  ? 427 LYS B NZ  1 
ATOM 6957 N N   . ALA B 1 382 ? -53.061 20.479  169.072 1.00 56.73  ? 428 ALA B N   1 
ATOM 6958 C CA  . ALA B 1 382 ? -54.410 19.978  169.279 1.00 57.84  ? 428 ALA B CA  1 
ATOM 6959 C C   . ALA B 1 382 ? -54.823 20.191  170.729 1.00 62.70  ? 428 ALA B C   1 
ATOM 6960 O O   . ALA B 1 382 ? -54.033 19.981  171.653 1.00 60.39  ? 428 ALA B O   1 
ATOM 6961 C CB  . ALA B 1 382 ? -54.493 18.497  168.915 1.00 55.69  ? 428 ALA B CB  1 
ATOM 6962 N N   . VAL B 1 383 ? -56.062 20.619  170.926 1.00 68.00  ? 429 VAL B N   1 
ATOM 6963 C CA  . VAL B 1 383 ? -56.523 20.934  172.282 1.00 65.50  ? 429 VAL B CA  1 
ATOM 6964 C C   . VAL B 1 383 ? -56.668 19.642  173.080 1.00 68.08  ? 429 VAL B C   1 
ATOM 6965 O O   . VAL B 1 383 ? -57.100 18.615  172.525 1.00 69.10  ? 429 VAL B O   1 
ATOM 6966 C CB  . VAL B 1 383 ? -57.838 21.722  172.232 1.00 65.24  ? 429 VAL B CB  1 
ATOM 6967 C CG1 . VAL B 1 383 ? -57.737 22.840  171.208 1.00 64.93  ? 429 VAL B CG1 1 
ATOM 6968 C CG2 . VAL B 1 383 ? -59.019 20.819  171.905 1.00 65.37  ? 429 VAL B CG2 1 
ATOM 6969 N N   . PRO B 1 384 ? -56.269 19.621  174.353 1.00 73.57  ? 430 PRO B N   1 
ATOM 6970 C CA  . PRO B 1 384 ? -56.439 18.415  175.176 1.00 72.12  ? 430 PRO B CA  1 
ATOM 6971 C C   . PRO B 1 384 ? -57.804 18.413  175.848 1.00 70.75  ? 430 PRO B C   1 
ATOM 6972 O O   . PRO B 1 384 ? -58.169 19.365  176.541 1.00 70.33  ? 430 PRO B O   1 
ATOM 6973 C CB  . PRO B 1 384 ? -55.307 18.528  176.200 1.00 74.01  ? 430 PRO B CB  1 
ATOM 6974 C CG  . PRO B 1 384 ? -55.094 20.000  176.344 1.00 72.54  ? 430 PRO B CG  1 
ATOM 6975 C CD  . PRO B 1 384 ? -55.425 20.631  175.014 1.00 70.87  ? 430 PRO B CD  1 
ATOM 6976 N N   . ALA B 1 385 ? -58.561 17.339  175.643 1.00 83.92  ? 431 ALA B N   1 
ATOM 6977 C CA  . ALA B 1 385 ? -59.855 17.191  176.294 1.00 86.06  ? 431 ALA B CA  1 
ATOM 6978 C C   . ALA B 1 385 ? -59.640 16.821  177.756 1.00 89.01  ? 431 ALA B C   1 
ATOM 6979 O O   . ALA B 1 385 ? -59.110 15.748  178.060 1.00 88.44  ? 431 ALA B O   1 
ATOM 6980 C CB  . ALA B 1 385 ? -60.694 16.131  175.584 1.00 83.72  ? 431 ALA B CB  1 
ATOM 6981 N N   . GLY B 1 386 ? -60.055 17.703  178.658 1.00 94.86  ? 432 GLY B N   1 
ATOM 6982 C CA  . GLY B 1 386 ? -59.839 17.510  180.079 1.00 95.74  ? 432 GLY B CA  1 
ATOM 6983 C C   . GLY B 1 386 ? -58.674 18.332  180.595 1.00 98.70  ? 432 GLY B C   1 
ATOM 6984 O O   . GLY B 1 386 ? -57.996 19.059  179.861 1.00 97.15  ? 432 GLY B O   1 
ATOM 6985 N N   . ASP B 1 387 ? -58.445 18.203  181.900 1.00 111.09 ? 433 ASP B N   1 
ATOM 6986 C CA  . ASP B 1 387 ? -57.433 18.985  182.596 1.00 109.93 ? 433 ASP B CA  1 
ATOM 6987 C C   . ASP B 1 387 ? -56.059 18.328  182.605 1.00 108.28 ? 433 ASP B C   1 
ATOM 6988 O O   . ASP B 1 387 ? -55.092 18.961  183.041 1.00 107.50 ? 433 ASP B O   1 
ATOM 6989 C CB  . ASP B 1 387 ? -57.875 19.249  184.038 1.00 110.07 ? 433 ASP B CB  1 
ATOM 6990 C CG  . ASP B 1 387 ? -58.019 17.973  184.844 1.00 111.97 ? 433 ASP B CG  1 
ATOM 6991 O OD1 . ASP B 1 387 ? -58.864 17.128  184.479 1.00 109.84 ? 433 ASP B OD1 1 
ATOM 6992 O OD2 . ASP B 1 387 ? -57.284 17.813  185.842 1.00 111.84 ? 433 ASP B OD2 1 
ATOM 6993 N N   . THR B 1 388 ? -55.940 17.087  182.142 1.00 98.04  ? 434 THR B N   1 
ATOM 6994 C CA  . THR B 1 388 ? -54.670 16.372  182.134 1.00 98.23  ? 434 THR B CA  1 
ATOM 6995 C C   . THR B 1 388 ? -54.212 16.211  180.690 1.00 99.37  ? 434 THR B C   1 
ATOM 6996 O O   . THR B 1 388 ? -54.965 15.714  179.847 1.00 97.41  ? 434 THR B O   1 
ATOM 6997 C CB  . THR B 1 388 ? -54.794 15.012  182.818 1.00 95.99  ? 434 THR B CB  1 
ATOM 6998 O OG1 . THR B 1 388 ? -54.869 15.197  184.236 1.00 93.31  ? 434 THR B OG1 1 
ATOM 6999 C CG2 . THR B 1 388 ? -53.580 14.156  182.506 1.00 94.31  ? 434 THR B CG2 1 
ATOM 7000 N N   . SER B 1 389 ? -52.982 16.633  180.413 1.00 89.44  ? 435 SER B N   1 
ATOM 7001 C CA  . SER B 1 389 ? -52.461 16.706  179.053 1.00 86.92  ? 435 SER B CA  1 
ATOM 7002 C C   . SER B 1 389 ? -51.047 16.137  178.997 1.00 87.36  ? 435 SER B C   1 
ATOM 7003 O O   . SER B 1 389 ? -50.119 16.771  178.493 1.00 87.23  ? 435 SER B O   1 
ATOM 7004 C CB  . SER B 1 389 ? -52.494 18.145  178.547 1.00 86.79  ? 435 SER B CB  1 
ATOM 7005 O OG  . SER B 1 389 ? -53.691 18.788  178.945 1.00 86.36  ? 435 SER B OG  1 
ATOM 7006 N N   . LYS B 1 390 ? -50.866 14.936  179.550 1.00 80.88  ? 436 LYS B N   1 
ATOM 7007 C CA  . LYS B 1 390 ? -49.535 14.333  179.575 1.00 81.22  ? 436 LYS B CA  1 
ATOM 7008 C C   . LYS B 1 390 ? -48.886 14.239  178.197 1.00 80.26  ? 436 LYS B C   1 
ATOM 7009 O O   . LYS B 1 390 ? -47.701 14.596  178.085 1.00 82.73  ? 436 LYS B O   1 
ATOM 7010 C CB  . LYS B 1 390 ? -49.599 12.958  180.255 1.00 77.94  ? 436 LYS B CB  1 
ATOM 7011 C CG  . LYS B 1 390 ? -49.866 13.027  181.748 1.00 81.74  ? 436 LYS B CG  1 
ATOM 7012 C CD  . LYS B 1 390 ? -49.124 11.934  182.493 1.00 79.59  ? 436 LYS B CD  1 
ATOM 7013 C CE  . LYS B 1 390 ? -49.817 10.594  182.332 1.00 80.92  ? 436 LYS B CE  1 
ATOM 7014 N NZ  . LYS B 1 390 ? -51.144 10.582  183.006 1.00 81.66  ? 436 LYS B NZ  1 
ATOM 7015 N N   . PRO B 1 391 ? -49.557 13.794  177.137 1.00 69.71  ? 437 PRO B N   1 
ATOM 7016 C CA  . PRO B 1 391 ? -48.989 13.930  175.796 1.00 68.58  ? 437 PRO B CA  1 
ATOM 7017 C C   . PRO B 1 391 ? -49.355 15.278  175.186 1.00 70.98  ? 437 PRO B C   1 
ATOM 7018 O O   . PRO B 1 391 ? -50.255 15.980  175.649 1.00 75.12  ? 437 PRO B O   1 
ATOM 7019 C CB  . PRO B 1 391 ? -49.648 12.782  175.027 1.00 65.73  ? 437 PRO B CB  1 
ATOM 7020 C CG  . PRO B 1 391 ? -50.987 12.691  175.639 1.00 69.69  ? 437 PRO B CG  1 
ATOM 7021 C CD  . PRO B 1 391 ? -50.802 13.004  177.105 1.00 68.75  ? 437 PRO B CD  1 
ATOM 7022 N N   . VAL B 1 392 ? -48.629 15.632  174.130 1.00 62.71  ? 438 VAL B N   1 
ATOM 7023 C CA  . VAL B 1 392 ? -48.891 16.846  173.367 1.00 61.41  ? 438 VAL B CA  1 
ATOM 7024 C C   . VAL B 1 392 ? -48.952 16.481  171.893 1.00 63.85  ? 438 VAL B C   1 
ATOM 7025 O O   . VAL B 1 392 ? -47.992 15.927  171.346 1.00 62.00  ? 438 VAL B O   1 
ATOM 7026 C CB  . VAL B 1 392 ? -47.821 17.925  173.617 1.00 61.10  ? 438 VAL B CB  1 
ATOM 7027 C CG1 . VAL B 1 392 ? -47.965 19.052  172.613 1.00 58.32  ? 438 VAL B CG1 1 
ATOM 7028 C CG2 . VAL B 1 392 ? -47.943 18.461  175.031 1.00 63.33  ? 438 VAL B CG2 1 
ATOM 7029 N N   . LEU B 1 393 ? -50.074 16.795  171.253 1.00 55.11  ? 439 LEU B N   1 
ATOM 7030 C CA  . LEU B 1 393 ? -50.298 16.481  169.851 1.00 51.92  ? 439 LEU B CA  1 
ATOM 7031 C C   . LEU B 1 393 ? -50.414 17.768  169.048 1.00 53.05  ? 439 LEU B C   1 
ATOM 7032 O O   . LEU B 1 393 ? -51.026 18.740  169.499 1.00 54.95  ? 439 LEU B O   1 
ATOM 7033 C CB  . LEU B 1 393 ? -51.558 15.633  169.666 1.00 49.78  ? 439 LEU B CB  1 
ATOM 7034 C CG  . LEU B 1 393 ? -51.523 14.240  170.292 1.00 48.17  ? 439 LEU B CG  1 
ATOM 7035 C CD1 . LEU B 1 393 ? -52.751 13.446  169.889 1.00 55.70  ? 439 LEU B CD1 1 
ATOM 7036 C CD2 . LEU B 1 393 ? -50.258 13.511  169.885 1.00 47.69  ? 439 LEU B CD2 1 
ATOM 7037 N N   . TYR B 1 394 ? -49.822 17.765  167.859 1.00 51.62  ? 440 TYR B N   1 
ATOM 7038 C CA  . TYR B 1 394 ? -49.785 18.930  166.987 1.00 51.06  ? 440 TYR B CA  1 
ATOM 7039 C C   . TYR B 1 394 ? -50.597 18.651  165.731 1.00 50.20  ? 440 TYR B C   1 
ATOM 7040 O O   . TYR B 1 394 ? -50.438 17.598  165.106 1.00 59.87  ? 440 TYR B O   1 
ATOM 7041 C CB  . TYR B 1 394 ? -48.346 19.286  166.616 1.00 50.60  ? 440 TYR B CB  1 
ATOM 7042 C CG  . TYR B 1 394 ? -47.443 19.525  167.803 1.00 51.76  ? 440 TYR B CG  1 
ATOM 7043 C CD1 . TYR B 1 394 ? -47.320 20.788  168.362 1.00 48.50  ? 440 TYR B CD1 1 
ATOM 7044 C CD2 . TYR B 1 394 ? -46.713 18.487  168.364 1.00 55.56  ? 440 TYR B CD2 1 
ATOM 7045 C CE1 . TYR B 1 394 ? -46.498 21.010  169.446 1.00 53.23  ? 440 TYR B CE1 1 
ATOM 7046 C CE2 . TYR B 1 394 ? -45.889 18.700  169.447 1.00 56.03  ? 440 TYR B CE2 1 
ATOM 7047 C CZ  . TYR B 1 394 ? -45.785 19.963  169.984 1.00 59.16  ? 440 TYR B CZ  1 
ATOM 7048 O OH  . TYR B 1 394 ? -44.963 20.180  171.065 1.00 60.97  ? 440 TYR B OH  1 
ATOM 7049 N N   . LEU B 1 395 ? -51.461 19.588  165.371 1.00 45.74  ? 441 LEU B N   1 
ATOM 7050 C CA  . LEU B 1 395 ? -52.268 19.461  164.162 1.00 45.30  ? 441 LEU B CA  1 
ATOM 7051 C C   . LEU B 1 395 ? -51.480 19.955  162.956 1.00 46.54  ? 441 LEU B C   1 
ATOM 7052 O O   . LEU B 1 395 ? -50.982 21.086  162.972 1.00 56.36  ? 441 LEU B O   1 
ATOM 7053 C CB  . LEU B 1 395 ? -53.560 20.253  164.287 1.00 52.37  ? 441 LEU B CB  1 
ATOM 7054 C CG  . LEU B 1 395 ? -54.520 19.798  165.385 1.00 57.72  ? 441 LEU B CG  1 
ATOM 7055 C CD1 . LEU B 1 395 ? -55.747 20.691  165.425 1.00 53.70  ? 441 LEU B CD1 1 
ATOM 7056 C CD2 . LEU B 1 395 ? -54.914 18.349  165.171 1.00 52.48  ? 441 LEU B CD2 1 
ATOM 7057 N N   . PRO B 1 396 ? -51.341 19.150  161.910 1.00 44.36  ? 442 PRO B N   1 
ATOM 7058 C CA  . PRO B 1 396 ? -50.615 19.597  160.721 1.00 42.47  ? 442 PRO B CA  1 
ATOM 7059 C C   . PRO B 1 396 ? -51.401 20.633  159.932 1.00 50.77  ? 442 PRO B C   1 
ATOM 7060 O O   . PRO B 1 396 ? -52.627 20.722  160.008 1.00 54.37  ? 442 PRO B O   1 
ATOM 7061 C CB  . PRO B 1 396 ? -50.444 18.309  159.912 1.00 45.29  ? 442 PRO B CB  1 
ATOM 7062 C CG  . PRO B 1 396 ? -51.631 17.494  160.285 1.00 51.68  ? 442 PRO B CG  1 
ATOM 7063 C CD  . PRO B 1 396 ? -51.925 17.810  161.730 1.00 51.95  ? 442 PRO B CD  1 
ATOM 7064 N N   . ASN B 1 397 ? -50.660 21.425  159.162 1.00 56.33  ? 443 ASN B N   1 
ATOM 7065 C CA  . ASN B 1 397 ? -51.255 22.397  158.257 1.00 54.23  ? 443 ASN B CA  1 
ATOM 7066 C C   . ASN B 1 397 ? -51.651 21.786  156.921 1.00 51.60  ? 443 ASN B C   1 
ATOM 7067 O O   . ASN B 1 397 ? -52.359 22.432  156.141 1.00 55.69  ? 443 ASN B O   1 
ATOM 7068 C CB  . ASN B 1 397 ? -50.282 23.560  158.028 1.00 57.03  ? 443 ASN B CB  1 
ATOM 7069 C CG  . ASN B 1 397 ? -50.892 24.683  157.213 1.00 60.18  ? 443 ASN B CG  1 
ATOM 7070 O OD1 . ASN B 1 397 ? -50.267 25.208  156.294 1.00 65.03  ? 443 ASN B OD1 1 
ATOM 7071 N ND2 . ASN B 1 397 ? -52.123 25.053  157.544 1.00 52.61  ? 443 ASN B ND2 1 
ATOM 7072 N N   . GLY B 1 398 ? -51.232 20.554  156.651 1.00 47.57  ? 444 GLY B N   1 
ATOM 7073 C CA  . GLY B 1 398 ? -51.503 19.903  155.387 1.00 47.28  ? 444 GLY B CA  1 
ATOM 7074 C C   . GLY B 1 398 ? -50.303 19.110  154.920 1.00 50.14  ? 444 GLY B C   1 
ATOM 7075 O O   . GLY B 1 398 ? -49.188 19.637  154.867 1.00 57.39  ? 444 GLY B O   1 
ATOM 7076 N N   . PHE B 1 399 ? -50.513 17.843  154.580 1.00 38.23  ? 445 PHE B N   1 
ATOM 7077 C CA  . PHE B 1 399 ? -49.426 16.950  154.214 1.00 38.46  ? 445 PHE B CA  1 
ATOM 7078 C C   . PHE B 1 399 ? -49.700 16.342  152.848 1.00 39.70  ? 445 PHE B C   1 
ATOM 7079 O O   . PHE B 1 399 ? -50.809 16.421  152.313 1.00 39.91  ? 445 PHE B O   1 
ATOM 7080 C CB  . PHE B 1 399 ? -49.234 15.843  155.257 1.00 41.65  ? 445 PHE B CB  1 
ATOM 7081 C CG  . PHE B 1 399 ? -50.518 15.245  155.751 1.00 40.97  ? 445 PHE B CG  1 
ATOM 7082 C CD1 . PHE B 1 399 ? -51.149 14.243  155.038 1.00 38.70  ? 445 PHE B CD1 1 
ATOM 7083 C CD2 . PHE B 1 399 ? -51.089 15.679  156.933 1.00 39.38  ? 445 PHE B CD2 1 
ATOM 7084 C CE1 . PHE B 1 399 ? -52.326 13.692  155.490 1.00 38.90  ? 445 PHE B CE1 1 
ATOM 7085 C CE2 . PHE B 1 399 ? -52.266 15.130  157.390 1.00 35.26  ? 445 PHE B CE2 1 
ATOM 7086 C CZ  . PHE B 1 399 ? -52.886 14.135  156.668 1.00 37.94  ? 445 PHE B CZ  1 
ATOM 7087 N N   . GLY B 1 400 ? -48.666 15.731  152.285 1.00 40.86  ? 446 GLY B N   1 
ATOM 7088 C CA  . GLY B 1 400 ? -48.770 15.070  151.004 1.00 43.95  ? 446 GLY B CA  1 
ATOM 7089 C C   . GLY B 1 400 ? -49.329 13.672  151.148 1.00 45.06  ? 446 GLY B C   1 
ATOM 7090 O O   . GLY B 1 400 ? -49.907 13.300  152.171 1.00 47.83  ? 446 GLY B O   1 
ATOM 7091 N N   . THR B 1 401 ? -49.145 12.882  150.092 1.00 38.21  ? 447 THR B N   1 
ATOM 7092 C CA  . THR B 1 401 ? -49.672 11.525  150.080 1.00 40.00  ? 447 THR B CA  1 
ATOM 7093 C C   . THR B 1 401 ? -48.943 10.602  151.048 1.00 44.43  ? 447 THR B C   1 
ATOM 7094 O O   . THR B 1 401 ? -49.482 9.548   151.399 1.00 48.60  ? 447 THR B O   1 
ATOM 7095 C CB  . THR B 1 401 ? -49.608 10.956  148.665 1.00 39.73  ? 447 THR B CB  1 
ATOM 7096 O OG1 . THR B 1 401 ? -48.327 11.240  148.092 1.00 37.32  ? 447 THR B OG1 1 
ATOM 7097 C CG2 . THR B 1 401 ? -50.691 11.579  147.801 1.00 41.64  ? 447 THR B CG2 1 
ATOM 7098 N N   . GLU B 1 402 ? -47.742 10.967  151.487 1.00 47.40  ? 448 GLU B N   1 
ATOM 7099 C CA  . GLU B 1 402 ? -46.968 10.161  152.419 1.00 40.65  ? 448 GLU B CA  1 
ATOM 7100 C C   . GLU B 1 402 ? -46.520 11.013  153.596 1.00 37.44  ? 448 GLU B C   1 
ATOM 7101 O O   . GLU B 1 402 ? -46.209 12.197  153.435 1.00 47.24  ? 448 GLU B O   1 
ATOM 7102 C CB  . GLU B 1 402 ? -45.743 9.549   151.741 1.00 38.26  ? 448 GLU B CB  1 
ATOM 7103 C CG  . GLU B 1 402 ? -46.038 8.871   150.423 1.00 45.34  ? 448 GLU B CG  1 
ATOM 7104 C CD  . GLU B 1 402 ? -45.752 9.768   149.239 1.00 53.83  ? 448 GLU B CD  1 
ATOM 7105 O OE1 . GLU B 1 402 ? -45.195 10.865  149.448 1.00 57.83  ? 448 GLU B OE1 1 
ATOM 7106 O OE2 . GLU B 1 402 ? -46.080 9.379   148.099 1.00 58.13  ? 448 GLU B OE2 1 
ATOM 7107 N N   . VAL B 1 403 ? -46.490 10.407  154.777 1.00 19.36  ? 449 VAL B N   1 
ATOM 7108 C CA  . VAL B 1 403 ? -45.939 11.030  155.971 1.00 26.93  ? 449 VAL B CA  1 
ATOM 7109 C C   . VAL B 1 403 ? -44.918 10.078  156.573 1.00 26.78  ? 449 VAL B C   1 
ATOM 7110 O O   . VAL B 1 403 ? -45.186 8.882   156.725 1.00 34.11  ? 449 VAL B O   1 
ATOM 7111 C CB  . VAL B 1 403 ? -47.036 11.391  156.995 1.00 30.25  ? 449 VAL B CB  1 
ATOM 7112 C CG1 . VAL B 1 403 ? -47.817 12.605  156.523 1.00 34.56  ? 449 VAL B CG1 1 
ATOM 7113 C CG2 . VAL B 1 403 ? -47.974 10.222  157.214 1.00 37.12  ? 449 VAL B CG2 1 
ATOM 7114 N N   . VAL B 1 404 ? -43.742 10.603  156.896 1.00 37.73  ? 450 VAL B N   1 
ATOM 7115 C CA  . VAL B 1 404 ? -42.652 9.809   157.449 1.00 32.80  ? 450 VAL B CA  1 
ATOM 7116 C C   . VAL B 1 404 ? -42.822 9.767   158.959 1.00 38.94  ? 450 VAL B C   1 
ATOM 7117 O O   . VAL B 1 404 ? -42.892 10.813  159.613 1.00 48.20  ? 450 VAL B O   1 
ATOM 7118 C CB  . VAL B 1 404 ? -41.283 10.388  157.065 1.00 30.60  ? 450 VAL B CB  1 
ATOM 7119 C CG1 . VAL B 1 404 ? -40.177 9.612   157.747 1.00 33.55  ? 450 VAL B CG1 1 
ATOM 7120 C CG2 . VAL B 1 404 ? -41.104 10.366  155.560 1.00 33.08  ? 450 VAL B CG2 1 
ATOM 7121 N N   . ASN B 1 405 ? -42.888 8.560   159.517 1.00 30.27  ? 451 ASN B N   1 
ATOM 7122 C CA  . ASN B 1 405 ? -43.054 8.406   160.958 1.00 29.63  ? 451 ASN B CA  1 
ATOM 7123 C C   . ASN B 1 405 ? -41.707 8.302   161.667 1.00 36.70  ? 451 ASN B C   1 
ATOM 7124 O O   . ASN B 1 405 ? -41.399 9.106   162.551 1.00 41.39  ? 451 ASN B O   1 
ATOM 7125 C CB  . ASN B 1 405 ? -43.915 7.176   161.265 1.00 32.71  ? 451 ASN B CB  1 
ATOM 7126 C CG  . ASN B 1 405 ? -45.055 7.006   160.288 1.00 41.08  ? 451 ASN B CG  1 
ATOM 7127 O OD1 . ASN B 1 405 ? -44.869 6.504   159.182 1.00 43.13  ? 451 ASN B OD1 1 
ATOM 7128 N ND2 . ASN B 1 405 ? -46.247 7.423   160.693 1.00 44.59  ? 451 ASN B ND2 1 
ATOM 7129 N N   . ASP B 1 406 ? -40.894 7.325   161.279 1.00 42.18  ? 452 ASP B N   1 
ATOM 7130 C CA  . ASP B 1 406 ? -39.662 7.002   161.978 1.00 35.68  ? 452 ASP B CA  1 
ATOM 7131 C C   . ASP B 1 406 ? -38.530 6.847   160.973 1.00 37.09  ? 452 ASP B C   1 
ATOM 7132 O O   . ASP B 1 406 ? -38.748 6.722   159.766 1.00 43.62  ? 452 ASP B O   1 
ATOM 7133 C CB  . ASP B 1 406 ? -39.814 5.713   162.799 1.00 43.51  ? 452 ASP B CB  1 
ATOM 7134 C CG  . ASP B 1 406 ? -40.471 5.949   164.143 1.00 47.74  ? 452 ASP B CG  1 
ATOM 7135 O OD1 . ASP B 1 406 ? -41.080 7.021   164.329 1.00 51.57  ? 452 ASP B OD1 1 
ATOM 7136 O OD2 . ASP B 1 406 ? -40.392 5.058   165.012 1.00 44.49  ? 452 ASP B OD2 1 
ATOM 7137 N N   . TYR B 1 407 ? -37.306 6.865   161.492 1.00 33.24  ? 453 TYR B N   1 
ATOM 7138 C CA  . TYR B 1 407 ? -36.110 6.536   160.730 1.00 32.74  ? 453 TYR B CA  1 
ATOM 7139 C C   . TYR B 1 407 ? -35.386 5.405   161.440 1.00 39.01  ? 453 TYR B C   1 
ATOM 7140 O O   . TYR B 1 407 ? -35.267 5.420   162.669 1.00 42.16  ? 453 TYR B O   1 
ATOM 7141 C CB  . TYR B 1 407 ? -35.180 7.742   160.591 1.00 34.78  ? 453 TYR B CB  1 
ATOM 7142 C CG  . TYR B 1 407 ? -35.750 8.874   159.777 1.00 36.00  ? 453 TYR B CG  1 
ATOM 7143 C CD1 . TYR B 1 407 ? -35.629 8.889   158.397 1.00 36.44  ? 453 TYR B CD1 1 
ATOM 7144 C CD2 . TYR B 1 407 ? -36.401 9.931   160.390 1.00 38.16  ? 453 TYR B CD2 1 
ATOM 7145 C CE1 . TYR B 1 407 ? -36.147 9.924   157.651 1.00 42.52  ? 453 TYR B CE1 1 
ATOM 7146 C CE2 . TYR B 1 407 ? -36.922 10.967  159.653 1.00 35.11  ? 453 TYR B CE2 1 
ATOM 7147 C CZ  . TYR B 1 407 ? -36.792 10.960  158.285 1.00 36.61  ? 453 TYR B CZ  1 
ATOM 7148 O OH  . TYR B 1 407 ? -37.310 11.995  157.547 1.00 34.91  ? 453 TYR B OH  1 
ATOM 7149 N N   . THR B 1 408 ? -34.914 4.426   160.676 1.00 37.37  ? 454 THR B N   1 
ATOM 7150 C CA  . THR B 1 408 ? -34.158 3.308   161.219 1.00 36.51  ? 454 THR B CA  1 
ATOM 7151 C C   . THR B 1 408 ? -32.799 3.244   160.543 1.00 38.57  ? 454 THR B C   1 
ATOM 7152 O O   . THR B 1 408 ? -32.711 3.287   159.312 1.00 42.84  ? 454 THR B O   1 
ATOM 7153 C CB  . THR B 1 408 ? -34.900 1.985   161.030 1.00 38.65  ? 454 THR B CB  1 
ATOM 7154 O OG1 . THR B 1 408 ? -36.260 2.136   161.451 1.00 39.88  ? 454 THR B OG1 1 
ATOM 7155 C CG2 . THR B 1 408 ? -34.244 0.894   161.849 1.00 35.99  ? 454 THR B CG2 1 
ATOM 7156 N N   . MET B 1 409 ? -31.747 3.139   161.347 1.00 36.67  ? 455 MET B N   1 
ATOM 7157 C CA  . MET B 1 409 ? -30.388 3.021   160.846 1.00 33.13  ? 455 MET B CA  1 
ATOM 7158 C C   . MET B 1 409 ? -29.760 1.753   161.397 1.00 39.05  ? 455 MET B C   1 
ATOM 7159 O O   . MET B 1 409 ? -29.843 1.480   162.597 1.00 48.09  ? 455 MET B O   1 
ATOM 7160 C CB  . MET B 1 409 ? -29.540 4.222   161.241 1.00 36.56  ? 455 MET B CB  1 
ATOM 7161 C CG  . MET B 1 409 ? -28.322 4.431   160.370 1.00 36.27  ? 455 MET B CG  1 
ATOM 7162 S SD  . MET B 1 409 ? -27.480 5.939   160.848 1.00 53.26  ? 455 MET B SD  1 
ATOM 7163 C CE  . MET B 1 409 ? -27.490 5.723   162.621 1.00 41.40  ? 455 MET B CE  1 
ATOM 7164 N N   . ILE B 1 410 ? -29.127 0.984   160.517 1.00 34.26  ? 456 ILE B N   1 
ATOM 7165 C CA  . ILE B 1 410 ? -28.472 -0.265  160.881 1.00 36.46  ? 456 ILE B CA  1 
ATOM 7166 C C   . ILE B 1 410 ? -26.970 -0.079  160.734 1.00 36.37  ? 456 ILE B C   1 
ATOM 7167 O O   . ILE B 1 410 ? -26.494 0.368   159.685 1.00 42.07  ? 456 ILE B O   1 
ATOM 7168 C CB  . ILE B 1 410 ? -28.969 -1.442  160.022 1.00 36.06  ? 456 ILE B CB  1 
ATOM 7169 C CG1 . ILE B 1 410 ? -30.489 -1.386  159.843 1.00 42.62  ? 456 ILE B CG1 1 
ATOM 7170 C CG2 . ILE B 1 410 ? -28.550 -2.764  160.635 1.00 35.08  ? 456 ILE B CG2 1 
ATOM 7171 C CD1 . ILE B 1 410 ? -31.268 -1.359  161.133 1.00 41.80  ? 456 ILE B CD1 1 
ATOM 7172 N N   . SER B 1 411 ? -26.230 -0.417  161.787 1.00 32.82  ? 457 SER B N   1 
ATOM 7173 C CA  . SER B 1 411 ? -24.782 -0.284  161.793 1.00 31.38  ? 457 SER B CA  1 
ATOM 7174 C C   . SER B 1 411 ? -24.198 -1.341  162.717 1.00 35.59  ? 457 SER B C   1 
ATOM 7175 O O   . SER B 1 411 ? -24.894 -1.900  163.568 1.00 45.22  ? 457 SER B O   1 
ATOM 7176 C CB  . SER B 1 411 ? -24.348 1.118   162.232 1.00 34.29  ? 457 SER B CB  1 
ATOM 7177 O OG  . SER B 1 411 ? -22.948 1.180   162.425 1.00 44.81  ? 457 SER B OG  1 
ATOM 7178 N N   . VAL B 1 412 ? -22.910 -1.611  162.540 1.00 33.52  ? 458 VAL B N   1 
ATOM 7179 C CA  . VAL B 1 412 ? -22.235 -2.647  163.314 1.00 36.93  ? 458 VAL B CA  1 
ATOM 7180 C C   . VAL B 1 412 ? -21.972 -2.144  164.725 1.00 35.93  ? 458 VAL B C   1 
ATOM 7181 O O   . VAL B 1 412 ? -21.840 -0.938  164.963 1.00 38.85  ? 458 VAL B O   1 
ATOM 7182 C CB  . VAL B 1 412 ? -20.931 -3.079  162.622 1.00 38.07  ? 458 VAL B CB  1 
ATOM 7183 C CG1 . VAL B 1 412 ? -21.211 -3.505  161.198 1.00 37.05  ? 458 VAL B CG1 1 
ATOM 7184 C CG2 . VAL B 1 412 ? -19.917 -1.954  162.650 1.00 37.82  ? 458 VAL B CG2 1 
ATOM 7185 N N   . ASP B 1 413 ? -21.911 -3.076  165.670 1.00 42.00  ? 459 ASP B N   1 
ATOM 7186 C CA  . ASP B 1 413 ? -21.631 -2.726  167.054 1.00 45.98  ? 459 ASP B CA  1 
ATOM 7187 C C   . ASP B 1 413 ? -20.131 -2.604  167.284 1.00 50.02  ? 459 ASP B C   1 
ATOM 7188 O O   . ASP B 1 413 ? -19.329 -3.284  166.640 1.00 56.46  ? 459 ASP B O   1 
ATOM 7189 C CB  . ASP B 1 413 ? -22.223 -3.777  167.992 1.00 50.43  ? 459 ASP B CB  1 
ATOM 7190 C CG  . ASP B 1 413 ? -22.304 -3.299  169.424 1.00 57.85  ? 459 ASP B CG  1 
ATOM 7191 O OD1 . ASP B 1 413 ? -22.171 -2.078  169.652 1.00 61.27  ? 459 ASP B OD1 1 
ATOM 7192 O OD2 . ASP B 1 413 ? -22.501 -4.142  170.322 1.00 57.32  ? 459 ASP B OD2 1 
ATOM 7193 N N   . LYS B 1 414 ? -19.752 -1.723  168.212 1.00 51.63  ? 460 LYS B N   1 
ATOM 7194 C CA  . LYS B 1 414 ? -18.339 -1.561  168.538 1.00 47.33  ? 460 LYS B CA  1 
ATOM 7195 C C   . LYS B 1 414 ? -17.817 -2.719  169.377 1.00 52.73  ? 460 LYS B C   1 
ATOM 7196 O O   . LYS B 1 414 ? -16.623 -3.033  169.322 1.00 56.54  ? 460 LYS B O   1 
ATOM 7197 C CB  . LYS B 1 414 ? -18.115 -0.241  169.273 1.00 49.11  ? 460 LYS B CB  1 
ATOM 7198 C CG  . LYS B 1 414 ? -18.991 0.901   168.788 1.00 57.02  ? 460 LYS B CG  1 
ATOM 7199 C CD  . LYS B 1 414 ? -18.246 2.226   168.829 1.00 56.71  ? 460 LYS B CD  1 
ATOM 7200 C CE  . LYS B 1 414 ? -17.511 2.414   170.148 1.00 51.42  ? 460 LYS B CE  1 
ATOM 7201 N NZ  . LYS B 1 414 ? -18.433 2.380   171.317 1.00 52.52  ? 460 LYS B NZ  1 
ATOM 7202 N N   . ALA B 1 415 ? -18.681 -3.357  170.158 1.00 53.84  ? 461 ALA B N   1 
ATOM 7203 C CA  . ALA B 1 415 ? -18.268 -4.424  171.053 1.00 52.66  ? 461 ALA B CA  1 
ATOM 7204 C C   . ALA B 1 415 ? -18.355 -5.781  170.360 1.00 53.49  ? 461 ALA B C   1 
ATOM 7205 O O   . ALA B 1 415 ? -18.986 -5.941  169.314 1.00 54.67  ? 461 ALA B O   1 
ATOM 7206 C CB  . ALA B 1 415 ? -19.123 -4.416  172.319 1.00 48.04  ? 461 ALA B CB  1 
ATOM 7207 N N   . THR B 1 416 ? -17.699 -6.766  170.964 1.00 52.68  ? 462 THR B N   1 
ATOM 7208 C CA  . THR B 1 416 ? -17.737 -8.126  170.448 1.00 53.96  ? 462 THR B CA  1 
ATOM 7209 C C   . THR B 1 416 ? -19.161 -8.674  170.545 1.00 56.03  ? 462 THR B C   1 
ATOM 7210 O O   . THR B 1 416 ? -19.838 -8.463  171.555 1.00 54.97  ? 462 THR B O   1 
ATOM 7211 C CB  . THR B 1 416 ? -16.769 -9.006  171.243 1.00 52.09  ? 462 THR B CB  1 
ATOM 7212 O OG1 . THR B 1 416 ? -15.523 -8.317  171.399 1.00 49.07  ? 462 THR B OG1 1 
ATOM 7213 C CG2 . THR B 1 416 ? -16.508 -10.326 170.539 1.00 50.52  ? 462 THR B CG2 1 
ATOM 7214 N N   . PRO B 1 417 ? -19.651 -9.378  169.511 1.00 53.72  ? 463 PRO B N   1 
ATOM 7215 C CA  . PRO B 1 417 ? -19.003 -9.750  168.251 1.00 50.66  ? 463 PRO B CA  1 
ATOM 7216 C C   . PRO B 1 417 ? -19.328 -8.824  167.087 1.00 54.58  ? 463 PRO B C   1 
ATOM 7217 O O   . PRO B 1 417 ? -19.330 -9.261  165.940 1.00 56.00  ? 463 PRO B O   1 
ATOM 7218 C CB  . PRO B 1 417 ? -19.546 -11.163 168.007 1.00 46.83  ? 463 PRO B CB  1 
ATOM 7219 C CG  . PRO B 1 417 ? -20.905 -11.195 168.703 1.00 48.18  ? 463 PRO B CG  1 
ATOM 7220 C CD  . PRO B 1 417 ? -20.990 -9.979  169.604 1.00 51.95  ? 463 PRO B CD  1 
ATOM 7221 N N   . HIS B 1 418 ? -19.608 -7.549  167.360 1.00 50.24  ? 464 HIS B N   1 
ATOM 7222 C CA  . HIS B 1 418 ? -19.864 -6.543  166.329 1.00 46.99  ? 464 HIS B CA  1 
ATOM 7223 C C   . HIS B 1 418 ? -21.045 -6.945  165.443 1.00 44.93  ? 464 HIS B C   1 
ATOM 7224 O O   . HIS B 1 418 ? -20.926 -7.100  164.227 1.00 47.92  ? 464 HIS B O   1 
ATOM 7225 C CB  . HIS B 1 418 ? -18.608 -6.290  165.490 1.00 46.94  ? 464 HIS B CB  1 
ATOM 7226 C CG  . HIS B 1 418 ? -17.344 -6.273  166.289 1.00 46.94  ? 464 HIS B CG  1 
ATOM 7227 N ND1 . HIS B 1 418 ? -17.160 -5.442  167.372 1.00 44.14  ? 464 HIS B ND1 1 
ATOM 7228 C CD2 . HIS B 1 418 ? -16.201 -6.988  166.164 1.00 50.13  ? 464 HIS B CD2 1 
ATOM 7229 C CE1 . HIS B 1 418 ? -15.958 -5.645  167.880 1.00 45.25  ? 464 HIS B CE1 1 
ATOM 7230 N NE2 . HIS B 1 418 ? -15.355 -6.578  167.165 1.00 49.67  ? 464 HIS B NE2 1 
ATOM 7231 N N   . ASP B 1 419 ? -22.199 -7.110  166.083 1.00 48.24  ? 465 ASP B N   1 
ATOM 7232 C CA  . ASP B 1 419 ? -23.426 -7.422  165.374 1.00 48.43  ? 465 ASP B CA  1 
ATOM 7233 C C   . ASP B 1 419 ? -24.125 -6.129  164.955 1.00 46.82  ? 465 ASP B C   1 
ATOM 7234 O O   . ASP B 1 419 ? -23.705 -5.023  165.303 1.00 52.26  ? 465 ASP B O   1 
ATOM 7235 C CB  . ASP B 1 419 ? -24.336 -8.290  166.241 1.00 48.00  ? 465 ASP B CB  1 
ATOM 7236 C CG  . ASP B 1 419 ? -24.989 -9.411  165.458 1.00 53.79  ? 465 ASP B CG  1 
ATOM 7237 O OD1 . ASP B 1 419 ? -24.660 -9.575  164.264 1.00 49.10  ? 465 ASP B OD1 1 
ATOM 7238 O OD2 . ASP B 1 419 ? -25.833 -10.127 166.036 1.00 58.42  ? 465 ASP B OD2 1 
ATOM 7239 N N   . LEU B 1 420 ? -25.206 -6.267  164.196 1.00 40.34  ? 466 LEU B N   1 
ATOM 7240 C CA  . LEU B 1 420 ? -25.953 -5.108  163.742 1.00 43.66  ? 466 LEU B CA  1 
ATOM 7241 C C   . LEU B 1 420 ? -26.672 -4.443  164.912 1.00 40.91  ? 466 LEU B C   1 
ATOM 7242 O O   . LEU B 1 420 ? -26.996 -5.076  165.919 1.00 47.35  ? 466 LEU B O   1 
ATOM 7243 C CB  . LEU B 1 420 ? -26.959 -5.505  162.663 1.00 36.56  ? 466 LEU B CB  1 
ATOM 7244 C CG  . LEU B 1 420 ? -26.383 -6.292  161.487 1.00 37.79  ? 466 LEU B CG  1 
ATOM 7245 C CD1 . LEU B 1 420 ? -27.477 -7.056  160.769 1.00 37.05  ? 466 LEU B CD1 1 
ATOM 7246 C CD2 . LEU B 1 420 ? -25.661 -5.367  160.528 1.00 41.28  ? 466 LEU B CD2 1 
ATOM 7247 N N   . THR B 1 421 ? -26.915 -3.144  164.768 1.00 37.30  ? 467 THR B N   1 
ATOM 7248 C CA  . THR B 1 421 ? -27.576 -2.351  165.791 1.00 43.00  ? 467 THR B CA  1 
ATOM 7249 C C   . THR B 1 421 ? -28.781 -1.636  165.197 1.00 51.19  ? 467 THR B C   1 
ATOM 7250 O O   . THR B 1 421 ? -28.785 -1.260  164.022 1.00 47.78  ? 467 THR B O   1 
ATOM 7251 C CB  . THR B 1 421 ? -26.621 -1.325  166.408 1.00 45.32  ? 467 THR B CB  1 
ATOM 7252 O OG1 . THR B 1 421 ? -25.920 -0.637  165.367 1.00 48.62  ? 467 THR B OG1 1 
ATOM 7253 C CG2 . THR B 1 421 ? -25.621 -2.012  167.318 1.00 43.27  ? 467 THR B CG2 1 
ATOM 7254 N N   . ILE B 1 422 ? -29.803 -1.447  166.025 1.00 54.33  ? 468 ILE B N   1 
ATOM 7255 C CA  . ILE B 1 422 ? -31.053 -0.817  165.617 1.00 44.61  ? 468 ILE B CA  1 
ATOM 7256 C C   . ILE B 1 422 ? -31.109 0.558   166.265 1.00 49.64  ? 468 ILE B C   1 
ATOM 7257 O O   . ILE B 1 422 ? -30.945 0.683   167.485 1.00 53.61  ? 468 ILE B O   1 
ATOM 7258 C CB  . ILE B 1 422 ? -32.274 -1.659  166.017 1.00 48.90  ? 468 ILE B CB  1 
ATOM 7259 C CG1 . ILE B 1 422 ? -32.120 -3.110  165.552 1.00 51.34  ? 468 ILE B CG1 1 
ATOM 7260 C CG2 . ILE B 1 422 ? -33.545 -1.052  165.446 1.00 46.25  ? 468 ILE B CG2 1 
ATOM 7261 C CD1 . ILE B 1 422 ? -31.673 -3.262  164.123 1.00 46.63  ? 468 ILE B CD1 1 
ATOM 7262 N N   . HIS B 1 423 ? -31.339 1.589   165.455 1.00 46.22  ? 469 HIS B N   1 
ATOM 7263 C CA  . HIS B 1 423 ? -31.396 2.966   165.947 1.00 39.25  ? 469 HIS B CA  1 
ATOM 7264 C C   . HIS B 1 423 ? -32.608 3.641   165.315 1.00 44.34  ? 469 HIS B C   1 
ATOM 7265 O O   . HIS B 1 423 ? -32.547 4.092   164.168 1.00 45.87  ? 469 HIS B O   1 
ATOM 7266 C CB  . HIS B 1 423 ? -30.109 3.716   165.631 1.00 42.81  ? 469 HIS B CB  1 
ATOM 7267 C CG  . HIS B 1 423 ? -28.958 3.330   166.506 1.00 54.51  ? 469 HIS B CG  1 
ATOM 7268 N ND1 . HIS B 1 423 ? -27.694 3.090   166.010 1.00 58.56  ? 469 HIS B ND1 1 
ATOM 7269 C CD2 . HIS B 1 423 ? -28.880 3.137   167.843 1.00 52.30  ? 469 HIS B CD2 1 
ATOM 7270 C CE1 . HIS B 1 423 ? -26.888 2.768   167.005 1.00 53.02  ? 469 HIS B CE1 1 
ATOM 7271 N NE2 . HIS B 1 423 ? -27.582 2.789   168.128 1.00 51.16  ? 469 HIS B NE2 1 
ATOM 7272 N N   . THR B 1 424 ? -33.701 3.709   166.067 1.00 42.41  ? 470 THR B N   1 
ATOM 7273 C CA  . THR B 1 424 ? -34.939 4.322   165.607 1.00 41.09  ? 470 THR B CA  1 
ATOM 7274 C C   . THR B 1 424 ? -35.059 5.721   166.195 1.00 38.08  ? 470 THR B C   1 
ATOM 7275 O O   . THR B 1 424 ? -34.926 5.903   167.409 1.00 41.31  ? 470 THR B O   1 
ATOM 7276 C CB  . THR B 1 424 ? -36.148 3.474   166.003 1.00 45.90  ? 470 THR B CB  1 
ATOM 7277 O OG1 . THR B 1 424 ? -36.158 2.265   165.235 1.00 43.26  ? 470 THR B OG1 1 
ATOM 7278 C CG2 . THR B 1 424 ? -37.434 4.232   165.752 1.00 45.99  ? 470 THR B CG2 1 
ATOM 7279 N N   . PHE B 1 425 ? -35.309 6.703   165.333 1.00 36.53  ? 471 PHE B N   1 
ATOM 7280 C CA  . PHE B 1 425 ? -35.341 8.095   165.753 1.00 43.28  ? 471 PHE B CA  1 
ATOM 7281 C C   . PHE B 1 425 ? -36.172 8.905   164.770 1.00 43.35  ? 471 PHE B C   1 
ATOM 7282 O O   . PHE B 1 425 ? -36.319 8.530   163.604 1.00 44.35  ? 471 PHE B O   1 
ATOM 7283 C CB  . PHE B 1 425 ? -33.925 8.673   165.848 1.00 39.54  ? 471 PHE B CB  1 
ATOM 7284 C CG  . PHE B 1 425 ? -33.122 8.522   164.584 1.00 41.59  ? 471 PHE B CG  1 
ATOM 7285 C CD1 . PHE B 1 425 ? -32.398 7.369   164.341 1.00 42.41  ? 471 PHE B CD1 1 
ATOM 7286 C CD2 . PHE B 1 425 ? -33.089 9.533   163.641 1.00 38.37  ? 471 PHE B CD2 1 
ATOM 7287 C CE1 . PHE B 1 425 ? -31.661 7.228   163.182 1.00 39.03  ? 471 PHE B CE1 1 
ATOM 7288 C CE2 . PHE B 1 425 ? -32.355 9.396   162.482 1.00 34.02  ? 471 PHE B CE2 1 
ATOM 7289 C CZ  . PHE B 1 425 ? -31.640 8.243   162.254 1.00 32.28  ? 471 PHE B CZ  1 
ATOM 7290 N N   . PHE B 1 426 ? -36.716 10.018  165.255 1.00 36.24  ? 472 PHE B N   1 
ATOM 7291 C CA  . PHE B 1 426 ? -37.346 11.002  164.390 1.00 39.10  ? 472 PHE B CA  1 
ATOM 7292 C C   . PHE B 1 426 ? -36.281 11.984  163.909 1.00 36.31  ? 472 PHE B C   1 
ATOM 7293 O O   . PHE B 1 426 ? -35.084 11.793  164.136 1.00 45.89  ? 472 PHE B O   1 
ATOM 7294 C CB  . PHE B 1 426 ? -38.478 11.729  165.114 1.00 39.21  ? 472 PHE B CB  1 
ATOM 7295 C CG  . PHE B 1 426 ? -39.263 10.863  166.049 1.00 40.08  ? 472 PHE B CG  1 
ATOM 7296 C CD1 . PHE B 1 426 ? -40.269 10.043  165.573 1.00 36.96  ? 472 PHE B CD1 1 
ATOM 7297 C CD2 . PHE B 1 426 ? -39.007 10.882  167.407 1.00 40.84  ? 472 PHE B CD2 1 
ATOM 7298 C CE1 . PHE B 1 426 ? -40.997 9.251   166.433 1.00 38.97  ? 472 PHE B CE1 1 
ATOM 7299 C CE2 . PHE B 1 426 ? -39.731 10.091  168.271 1.00 44.63  ? 472 PHE B CE2 1 
ATOM 7300 C CZ  . PHE B 1 426 ? -40.728 9.274   167.783 1.00 43.25  ? 472 PHE B CZ  1 
ATOM 7301 N N   . ASN B 1 427 ? -36.707 13.059  163.243 1.00 34.92  ? 473 ASN B N   1 
ATOM 7302 C CA  . ASN B 1 427 ? -35.774 14.123  162.896 1.00 29.65  ? 473 ASN B CA  1 
ATOM 7303 C C   . ASN B 1 427 ? -35.248 14.844  164.127 1.00 33.01  ? 473 ASN B C   1 
ATOM 7304 O O   . ASN B 1 427 ? -34.200 15.493  164.051 1.00 45.29  ? 473 ASN B O   1 
ATOM 7305 C CB  . ASN B 1 427 ? -36.442 15.128  161.961 1.00 27.62  ? 473 ASN B CB  1 
ATOM 7306 C CG  . ASN B 1 427 ? -36.290 14.763  160.505 1.00 31.79  ? 473 ASN B CG  1 
ATOM 7307 O OD1 . ASN B 1 427 ? -37.096 14.019  159.954 1.00 44.48  ? 473 ASN B OD1 1 
ATOM 7308 N ND2 . ASN B 1 427 ? -35.260 15.299  159.866 1.00 38.92  ? 473 ASN B ND2 1 
ATOM 7309 N N   . ASN B 1 428 ? -35.943 14.742  165.255 1.00 35.72  ? 474 ASN B N   1 
ATOM 7310 C CA  . ASN B 1 428 ? -35.542 15.385  166.496 1.00 40.06  ? 474 ASN B CA  1 
ATOM 7311 C C   . ASN B 1 428 ? -35.108 14.326  167.498 1.00 46.79  ? 474 ASN B C   1 
ATOM 7312 O O   . ASN B 1 428 ? -35.797 13.317  167.680 1.00 55.00  ? 474 ASN B O   1 
ATOM 7313 C CB  . ASN B 1 428 ? -36.685 16.223  167.070 1.00 36.68  ? 474 ASN B CB  1 
ATOM 7314 C CG  . ASN B 1 428 ? -38.011 15.498  167.029 1.00 41.78  ? 474 ASN B CG  1 
ATOM 7315 O OD1 . ASN B 1 428 ? -38.297 14.655  167.879 1.00 48.66  ? 474 ASN B OD1 1 
ATOM 7316 N ND2 . ASN B 1 428 ? -38.827 15.814  166.033 1.00 46.45  ? 474 ASN B ND2 1 
ATOM 7317 N N   . ILE B 1 429 ? -33.969 14.556  168.145 1.00 36.14  ? 475 ILE B N   1 
ATOM 7318 C CA  . ILE B 1 429 ? -33.409 13.631  169.121 1.00 37.16  ? 475 ILE B CA  1 
ATOM 7319 C C   . ILE B 1 429 ? -33.270 14.358  170.449 1.00 42.89  ? 475 ILE B C   1 
ATOM 7320 O O   . ILE B 1 429 ? -32.745 15.475  170.499 1.00 49.42  ? 475 ILE B O   1 
ATOM 7321 C CB  . ILE B 1 429 ? -32.052 13.066  168.661 1.00 45.07  ? 475 ILE B CB  1 
ATOM 7322 C CG1 . ILE B 1 429 ? -32.166 12.482  167.252 1.00 44.59  ? 475 ILE B CG1 1 
ATOM 7323 C CG2 . ILE B 1 429 ? -31.550 12.015  169.638 1.00 45.91  ? 475 ILE B CG2 1 
ATOM 7324 C CD1 . ILE B 1 429 ? -31.564 13.352  166.184 1.00 45.89  ? 475 ILE B CD1 1 
ATOM 7325 N N   . LEU B 1 430 ? -33.748 13.728  171.516 1.00 42.69  ? 476 LEU B N   1 
ATOM 7326 C CA  . LEU B 1 430 ? -33.668 14.276  172.862 1.00 45.48  ? 476 LEU B CA  1 
ATOM 7327 C C   . LEU B 1 430 ? -32.670 13.466  173.673 1.00 52.37  ? 476 LEU B C   1 
ATOM 7328 O O   . LEU B 1 430 ? -32.741 12.233  173.697 1.00 56.12  ? 476 LEU B O   1 
ATOM 7329 C CB  . LEU B 1 430 ? -35.037 14.254  173.545 1.00 42.82  ? 476 LEU B CB  1 
ATOM 7330 C CG  . LEU B 1 430 ? -35.044 14.356  175.071 1.00 45.96  ? 476 LEU B CG  1 
ATOM 7331 C CD1 . LEU B 1 430 ? -34.805 15.787  175.520 1.00 46.97  ? 476 LEU B CD1 1 
ATOM 7332 C CD2 . LEU B 1 430 ? -36.346 13.819  175.636 1.00 46.80  ? 476 LEU B CD2 1 
ATOM 7333 N N   . VAL B 1 431 ? -31.742 14.154  174.328 1.00 49.33  ? 477 VAL B N   1 
ATOM 7334 C CA  . VAL B 1 431 ? -30.776 13.520  175.213 1.00 50.41  ? 477 VAL B CA  1 
ATOM 7335 C C   . VAL B 1 431 ? -30.980 14.067  176.623 1.00 51.30  ? 477 VAL B C   1 
ATOM 7336 O O   . VAL B 1 431 ? -31.016 15.286  176.821 1.00 55.68  ? 477 VAL B O   1 
ATOM 7337 C CB  . VAL B 1 431 ? -29.324 13.704  174.731 1.00 46.55  ? 477 VAL B CB  1 
ATOM 7338 C CG1 . VAL B 1 431 ? -29.236 13.462  173.237 1.00 48.85  ? 477 VAL B CG1 1 
ATOM 7339 C CG2 . VAL B 1 431 ? -28.786 15.085  175.033 1.00 48.28  ? 477 VAL B CG2 1 
ATOM 7340 N N   . PRO B 1 432 ? -31.228 13.217  177.612 1.00 56.53  ? 478 PRO B N   1 
ATOM 7341 C CA  . PRO B 1 432 ? -31.266 13.684  179.003 1.00 59.07  ? 478 PRO B CA  1 
ATOM 7342 C C   . PRO B 1 432 ? -29.901 13.592  179.664 1.00 64.11  ? 478 PRO B C   1 
ATOM 7343 O O   . PRO B 1 432 ? -28.923 13.199  179.021 1.00 66.98  ? 478 PRO B O   1 
ATOM 7344 C CB  . PRO B 1 432 ? -32.278 12.738  179.655 1.00 60.95  ? 478 PRO B CB  1 
ATOM 7345 C CG  . PRO B 1 432 ? -32.135 11.464  178.879 1.00 61.88  ? 478 PRO B CG  1 
ATOM 7346 C CD  . PRO B 1 432 ? -31.667 11.817  177.485 1.00 55.73  ? 478 PRO B CD  1 
ATOM 7347 N N   . ASN B 1 433 ? -29.819 13.946  180.944 1.00 69.65  ? 479 ASN B N   1 
ATOM 7348 C CA  . ASN B 1 433 ? -28.571 13.825  181.692 1.00 69.78  ? 479 ASN B CA  1 
ATOM 7349 C C   . ASN B 1 433 ? -28.276 12.354  181.952 1.00 69.50  ? 479 ASN B C   1 
ATOM 7350 O O   . ASN B 1 433 ? -29.002 11.688  182.697 1.00 71.45  ? 479 ASN B O   1 
ATOM 7351 C CB  . ASN B 1 433 ? -28.644 14.598  183.003 1.00 69.41  ? 479 ASN B CB  1 
ATOM 7352 C CG  . ASN B 1 433 ? -27.692 15.769  183.037 1.00 69.26  ? 479 ASN B CG  1 
ATOM 7353 O OD1 . ASN B 1 433 ? -27.225 16.232  181.997 1.00 71.93  ? 479 ASN B OD1 1 
ATOM 7354 N ND2 . ASN B 1 433 ? -27.384 16.247  184.236 1.00 68.36  ? 479 ASN B ND2 1 
ATOM 7355 N N   . ALA B 1 434 ? -27.206 11.850  181.344 1.00 70.53  ? 480 ALA B N   1 
ATOM 7356 C CA  . ALA B 1 434 ? -26.749 10.491  181.586 1.00 73.71  ? 480 ALA B CA  1 
ATOM 7357 C C   . ALA B 1 434 ? -25.290 10.387  181.172 1.00 71.95  ? 480 ALA B C   1 
ATOM 7358 O O   . ALA B 1 434 ? -24.789 11.180  180.372 1.00 70.40  ? 480 ALA B O   1 
ATOM 7359 C CB  . ALA B 1 434 ? -27.606 9.466   180.837 1.00 71.95  ? 480 ALA B CB  1 
ATOM 7360 N N   . LYS B 1 435 ? -24.607 9.389   181.733 1.00 72.30  ? 481 LYS B N   1 
ATOM 7361 C CA  . LYS B 1 435 ? -23.199 9.184   181.415 1.00 73.11  ? 481 LYS B CA  1 
ATOM 7362 C C   . LYS B 1 435 ? -23.000 8.787   179.957 1.00 74.72  ? 481 LYS B C   1 
ATOM 7363 O O   . LYS B 1 435 ? -22.047 9.246   179.318 1.00 75.81  ? 481 LYS B O   1 
ATOM 7364 C CB  . LYS B 1 435 ? -22.607 8.122   182.341 1.00 75.38  ? 481 LYS B CB  1 
ATOM 7365 C CG  . LYS B 1 435 ? -22.015 8.670   183.628 1.00 74.21  ? 481 LYS B CG  1 
ATOM 7366 C CD  . LYS B 1 435 ? -20.549 9.015   183.454 1.00 73.99  ? 481 LYS B CD  1 
ATOM 7367 C CE  . LYS B 1 435 ? -19.741 7.775   183.111 1.00 74.50  ? 481 LYS B CE  1 
ATOM 7368 N NZ  . LYS B 1 435 ? -18.302 7.925   183.459 1.00 75.50  ? 481 LYS B NZ  1 
ATOM 7369 N N   . GLU B 1 436 ? -23.883 7.948   179.414 1.00 74.46  ? 482 GLU B N   1 
ATOM 7370 C CA  . GLU B 1 436 ? -23.704 7.392   178.081 1.00 75.24  ? 482 GLU B CA  1 
ATOM 7371 C C   . GLU B 1 436 ? -24.515 8.101   177.008 1.00 72.18  ? 482 GLU B C   1 
ATOM 7372 O O   . GLU B 1 436 ? -24.273 7.865   175.817 1.00 73.11  ? 482 GLU B O   1 
ATOM 7373 C CB  . GLU B 1 436 ? -24.072 5.896   178.061 1.00 75.20  ? 482 GLU B CB  1 
ATOM 7374 C CG  . GLU B 1 436 ? -25.441 5.518   178.655 1.00 74.13  ? 482 GLU B CG  1 
ATOM 7375 C CD  . GLU B 1 436 ? -25.537 5.654   180.169 1.00 74.48  ? 482 GLU B CD  1 
ATOM 7376 O OE1 . GLU B 1 436 ? -26.552 5.199   180.737 1.00 75.31  ? 482 GLU B OE1 1 
ATOM 7377 O OE2 . GLU B 1 436 ? -24.605 6.196   180.795 1.00 74.54  ? 482 GLU B OE2 1 
ATOM 7378 N N   . ASN B 1 437 ? -25.467 8.955   177.387 1.00 61.73  ? 483 ASN B N   1 
ATOM 7379 C CA  . ASN B 1 437 ? -26.327 9.581   176.390 1.00 63.96  ? 483 ASN B CA  1 
ATOM 7380 C C   . ASN B 1 437 ? -25.551 10.503  175.461 1.00 65.84  ? 483 ASN B C   1 
ATOM 7381 O O   . ASN B 1 437 ? -25.825 10.532  174.259 1.00 67.49  ? 483 ASN B O   1 
ATOM 7382 C CB  . ASN B 1 437 ? -27.463 10.341  177.071 1.00 64.65  ? 483 ASN B CB  1 
ATOM 7383 C CG  . ASN B 1 437 ? -28.740 9.531   177.137 1.00 66.78  ? 483 ASN B CG  1 
ATOM 7384 O OD1 . ASN B 1 437 ? -28.953 8.758   178.070 1.00 67.85  ? 483 ASN B OD1 1 
ATOM 7385 N ND2 . ASN B 1 437 ? -29.592 9.691   176.133 1.00 65.71  ? 483 ASN B ND2 1 
ATOM 7386 N N   . TYR B 1 438 ? -24.582 11.255  175.984 1.00 63.34  ? 484 TYR B N   1 
ATOM 7387 C CA  . TYR B 1 438 ? -23.854 12.202  175.145 1.00 62.18  ? 484 TYR B CA  1 
ATOM 7388 C C   . TYR B 1 438 ? -22.973 11.490  174.123 1.00 62.28  ? 484 TYR B C   1 
ATOM 7389 O O   . TYR B 1 438 ? -22.958 11.862  172.942 1.00 62.65  ? 484 TYR B O   1 
ATOM 7390 C CB  . TYR B 1 438 ? -23.031 13.140  176.024 1.00 59.99  ? 484 TYR B CB  1 
ATOM 7391 C CG  . TYR B 1 438 ? -23.874 13.866  177.044 1.00 60.46  ? 484 TYR B CG  1 
ATOM 7392 C CD1 . TYR B 1 438 ? -24.685 14.928  176.670 1.00 58.65  ? 484 TYR B CD1 1 
ATOM 7393 C CD2 . TYR B 1 438 ? -23.880 13.477  178.374 1.00 61.30  ? 484 TYR B CD2 1 
ATOM 7394 C CE1 . TYR B 1 438 ? -25.465 15.589  177.594 1.00 57.30  ? 484 TYR B CE1 1 
ATOM 7395 C CE2 . TYR B 1 438 ? -24.659 14.132  179.305 1.00 61.33  ? 484 TYR B CE2 1 
ATOM 7396 C CZ  . TYR B 1 438 ? -25.448 15.188  178.910 1.00 59.93  ? 484 TYR B CZ  1 
ATOM 7397 O OH  . TYR B 1 438 ? -26.223 15.844  179.836 1.00 64.00  ? 484 TYR B OH  1 
ATOM 7398 N N   . VAL B 1 439 ? -22.241 10.460  174.548 1.00 64.69  ? 485 VAL B N   1 
ATOM 7399 C CA  . VAL B 1 439 ? -21.408 9.719   173.605 1.00 64.19  ? 485 VAL B CA  1 
ATOM 7400 C C   . VAL B 1 439 ? -22.276 8.951   172.614 1.00 63.81  ? 485 VAL B C   1 
ATOM 7401 O O   . VAL B 1 439 ? -21.932 8.831   171.432 1.00 62.59  ? 485 VAL B O   1 
ATOM 7402 C CB  . VAL B 1 439 ? -20.433 8.792   174.353 1.00 66.18  ? 485 VAL B CB  1 
ATOM 7403 C CG1 . VAL B 1 439 ? -19.280 9.596   174.927 1.00 61.52  ? 485 VAL B CG1 1 
ATOM 7404 C CG2 . VAL B 1 439 ? -21.148 8.031   175.454 1.00 65.37  ? 485 VAL B CG2 1 
ATOM 7405 N N   . ALA B 1 440 ? -23.415 8.423   173.072 1.00 60.21  ? 486 ALA B N   1 
ATOM 7406 C CA  . ALA B 1 440 ? -24.333 7.760   172.152 1.00 59.92  ? 486 ALA B CA  1 
ATOM 7407 C C   . ALA B 1 440 ? -24.872 8.735   171.113 1.00 61.11  ? 486 ALA B C   1 
ATOM 7408 O O   . ALA B 1 440 ? -24.989 8.391   169.931 1.00 64.55  ? 486 ALA B O   1 
ATOM 7409 C CB  . ALA B 1 440 ? -25.478 7.113   172.929 1.00 62.17  ? 486 ALA B CB  1 
ATOM 7410 N N   . ASN B 1 441 ? -25.205 9.955   171.535 1.00 54.98  ? 487 ASN B N   1 
ATOM 7411 C CA  . ASN B 1 441 ? -25.689 10.963  170.600 1.00 51.12  ? 487 ASN B CA  1 
ATOM 7412 C C   . ASN B 1 441 ? -24.606 11.358  169.607 1.00 55.65  ? 487 ASN B C   1 
ATOM 7413 O O   . ASN B 1 441 ? -24.894 11.588  168.427 1.00 56.28  ? 487 ASN B O   1 
ATOM 7414 C CB  . ASN B 1 441 ? -26.189 12.186  171.364 1.00 53.16  ? 487 ASN B CB  1 
ATOM 7415 C CG  . ASN B 1 441 ? -26.575 13.323  170.448 1.00 61.50  ? 487 ASN B CG  1 
ATOM 7416 O OD1 . ASN B 1 441 ? -27.264 13.121  169.450 1.00 66.22  ? 487 ASN B OD1 1 
ATOM 7417 N ND2 . ASN B 1 441 ? -26.130 14.529  170.779 1.00 58.66  ? 487 ASN B ND2 1 
ATOM 7418 N N   . LEU B 1 442 ? -23.357 11.459  170.066 1.00 54.86  ? 488 LEU B N   1 
ATOM 7419 C CA  . LEU B 1 442 ? -22.264 11.744  169.142 1.00 49.38  ? 488 LEU B CA  1 
ATOM 7420 C C   . LEU B 1 442 ? -22.087 10.620  168.130 1.00 49.49  ? 488 LEU B C   1 
ATOM 7421 O O   . LEU B 1 442 ? -21.842 10.879  166.946 1.00 51.12  ? 488 LEU B O   1 
ATOM 7422 C CB  . LEU B 1 442 ? -20.966 11.981  169.907 1.00 49.51  ? 488 LEU B CB  1 
ATOM 7423 C CG  . LEU B 1 442 ? -20.551 13.442  170.053 1.00 48.05  ? 488 LEU B CG  1 
ATOM 7424 C CD1 . LEU B 1 442 ? -19.149 13.522  170.614 1.00 48.11  ? 488 LEU B CD1 1 
ATOM 7425 C CD2 . LEU B 1 442 ? -20.637 14.153  168.715 1.00 47.22  ? 488 LEU B CD2 1 
ATOM 7426 N N   . GLU B 1 443 ? -22.193 9.367   168.578 1.00 52.98  ? 489 GLU B N   1 
ATOM 7427 C CA  . GLU B 1 443 ? -22.135 8.245   167.646 1.00 54.14  ? 489 GLU B CA  1 
ATOM 7428 C C   . GLU B 1 443 ? -23.262 8.329   166.625 1.00 56.98  ? 489 GLU B C   1 
ATOM 7429 O O   . GLU B 1 443 ? -23.045 8.108   165.427 1.00 58.19  ? 489 GLU B O   1 
ATOM 7430 C CB  . GLU B 1 443 ? -22.205 6.923   168.408 1.00 52.33  ? 489 GLU B CB  1 
ATOM 7431 C CG  . GLU B 1 443 ? -20.925 6.543   169.130 1.00 59.93  ? 489 GLU B CG  1 
ATOM 7432 C CD  . GLU B 1 443 ? -20.971 5.135   169.692 1.00 64.09  ? 489 GLU B CD  1 
ATOM 7433 O OE1 . GLU B 1 443 ? -21.957 4.418   169.421 1.00 61.47  ? 489 GLU B OE1 1 
ATOM 7434 O OE2 . GLU B 1 443 ? -20.023 4.746   170.407 1.00 60.17  ? 489 GLU B OE2 1 
ATOM 7435 N N   . LEU B 1 444 ? -24.471 8.657   167.085 1.00 50.05  ? 490 LEU B N   1 
ATOM 7436 C CA  . LEU B 1 444 ? -25.605 8.815   166.180 1.00 45.22  ? 490 LEU B CA  1 
ATOM 7437 C C   . LEU B 1 444 ? -25.337 9.902   165.147 1.00 46.19  ? 490 LEU B C   1 
ATOM 7438 O O   . LEU B 1 444 ? -25.586 9.716   163.950 1.00 49.40  ? 490 LEU B O   1 
ATOM 7439 C CB  . LEU B 1 444 ? -26.863 9.145   166.984 1.00 41.63  ? 490 LEU B CB  1 
ATOM 7440 C CG  . LEU B 1 444 ? -28.213 9.058   166.273 1.00 43.92  ? 490 LEU B CG  1 
ATOM 7441 C CD1 . LEU B 1 444 ? -28.261 7.865   165.341 1.00 44.03  ? 490 LEU B CD1 1 
ATOM 7442 C CD2 . LEU B 1 444 ? -29.340 8.997   167.286 1.00 48.01  ? 490 LEU B CD2 1 
ATOM 7443 N N   . LEU B 1 445 ? -24.831 11.049  165.599 1.00 46.93  ? 491 LEU B N   1 
ATOM 7444 C CA  . LEU B 1 445 ? -24.579 12.165  164.694 1.00 47.04  ? 491 LEU B CA  1 
ATOM 7445 C C   . LEU B 1 445 ? -23.512 11.809  163.671 1.00 44.13  ? 491 LEU B C   1 
ATOM 7446 O O   . LEU B 1 445 ? -23.654 12.105  162.481 1.00 46.19  ? 491 LEU B O   1 
ATOM 7447 C CB  . LEU B 1 445 ? -24.167 13.400  165.492 1.00 46.03  ? 491 LEU B CB  1 
ATOM 7448 C CG  . LEU B 1 445 ? -25.270 14.423  165.742 1.00 43.14  ? 491 LEU B CG  1 
ATOM 7449 C CD1 . LEU B 1 445 ? -26.475 13.742  166.350 1.00 48.91  ? 491 LEU B CD1 1 
ATOM 7450 C CD2 . LEU B 1 445 ? -24.761 15.525  166.650 1.00 41.09  ? 491 LEU B CD2 1 
ATOM 7451 N N   . ASN B 1 446 ? -22.433 11.166  164.119 1.00 47.16  ? 492 ASN B N   1 
ATOM 7452 C CA  . ASN B 1 446 ? -21.377 10.777  163.194 1.00 45.27  ? 492 ASN B CA  1 
ATOM 7453 C C   . ASN B 1 446 ? -21.867 9.745   162.190 1.00 47.95  ? 492 ASN B C   1 
ATOM 7454 O O   . ASN B 1 446 ? -21.450 9.769   161.027 1.00 49.58  ? 492 ASN B O   1 
ATOM 7455 C CB  . ASN B 1 446 ? -20.174 10.237  163.962 1.00 41.25  ? 492 ASN B CB  1 
ATOM 7456 C CG  . ASN B 1 446 ? -18.964 10.042  163.078 1.00 46.51  ? 492 ASN B CG  1 
ATOM 7457 O OD1 . ASN B 1 446 ? -18.804 10.728  162.070 1.00 48.55  ? 492 ASN B OD1 1 
ATOM 7458 N ND2 . ASN B 1 446 ? -18.104 9.103   163.449 1.00 52.24  ? 492 ASN B ND2 1 
ATOM 7459 N N   . ASN B 1 447 ? -22.741 8.831   162.617 1.00 47.65  ? 493 ASN B N   1 
ATOM 7460 C CA  . ASN B 1 447 ? -23.317 7.875   161.679 1.00 42.76  ? 493 ASN B CA  1 
ATOM 7461 C C   . ASN B 1 447 ? -24.203 8.572   160.655 1.00 41.85  ? 493 ASN B C   1 
ATOM 7462 O O   . ASN B 1 447 ? -24.173 8.234   159.467 1.00 46.08  ? 493 ASN B O   1 
ATOM 7463 C CB  . ASN B 1 447 ? -24.108 6.814   162.440 1.00 38.46  ? 493 ASN B CB  1 
ATOM 7464 C CG  . ASN B 1 447 ? -23.215 5.818   163.146 1.00 48.60  ? 493 ASN B CG  1 
ATOM 7465 O OD1 . ASN B 1 447 ? -22.059 5.630   162.772 1.00 51.96  ? 493 ASN B OD1 1 
ATOM 7466 N ND2 . ASN B 1 447 ? -23.747 5.176   164.178 1.00 53.57  ? 493 ASN B ND2 1 
ATOM 7467 N N   . ILE B 1 448 ? -24.996 9.549   161.097 1.00 38.70  ? 494 ILE B N   1 
ATOM 7468 C CA  . ILE B 1 448 ? -25.898 10.242  160.181 1.00 37.41  ? 494 ILE B CA  1 
ATOM 7469 C C   . ILE B 1 448 ? -25.111 11.086  159.185 1.00 37.87  ? 494 ILE B C   1 
ATOM 7470 O O   . ILE B 1 448 ? -25.484 11.191  158.011 1.00 41.89  ? 494 ILE B O   1 
ATOM 7471 C CB  . ILE B 1 448 ? -26.919 11.081  160.972 1.00 33.97  ? 494 ILE B CB  1 
ATOM 7472 C CG1 . ILE B 1 448 ? -27.915 10.164  161.679 1.00 35.05  ? 494 ILE B CG1 1 
ATOM 7473 C CG2 . ILE B 1 448 ? -27.659 12.040  160.059 1.00 34.70  ? 494 ILE B CG2 1 
ATOM 7474 C CD1 . ILE B 1 448 ? -28.496 10.748  162.940 1.00 39.02  ? 494 ILE B CD1 1 
ATOM 7475 N N   . ILE B 1 449 ? -24.005 11.689  159.628 1.00 41.90  ? 495 ILE B N   1 
ATOM 7476 C CA  . ILE B 1 449 ? -23.177 12.494  158.734 1.00 40.43  ? 495 ILE B CA  1 
ATOM 7477 C C   . ILE B 1 449 ? -22.652 11.672  157.562 1.00 42.14  ? 495 ILE B C   1 
ATOM 7478 O O   . ILE B 1 449 ? -22.449 12.214  156.470 1.00 39.21  ? 495 ILE B O   1 
ATOM 7479 C CB  . ILE B 1 449 ? -22.023 13.146  159.525 1.00 42.22  ? 495 ILE B CB  1 
ATOM 7480 C CG1 . ILE B 1 449 ? -22.553 14.196  160.504 1.00 42.88  ? 495 ILE B CG1 1 
ATOM 7481 C CG2 . ILE B 1 449 ? -21.009 13.791  158.600 1.00 36.72  ? 495 ILE B CG2 1 
ATOM 7482 C CD1 . ILE B 1 449 ? -23.820 14.898  160.055 1.00 40.53  ? 495 ILE B CD1 1 
ATOM 7483 N N   . GLN B 1 450 ? -22.453 10.364  157.752 1.00 43.20  ? 496 GLN B N   1 
ATOM 7484 C CA  . GLN B 1 450 ? -21.986 9.517   156.660 1.00 35.79  ? 496 GLN B CA  1 
ATOM 7485 C C   . GLN B 1 450 ? -22.957 9.522   155.488 1.00 38.81  ? 496 GLN B C   1 
ATOM 7486 O O   . GLN B 1 450 ? -22.529 9.562   154.329 1.00 37.58  ? 496 GLN B O   1 
ATOM 7487 C CB  . GLN B 1 450 ? -21.770 8.090   157.160 1.00 31.01  ? 496 GLN B CB  1 
ATOM 7488 C CG  . GLN B 1 450 ? -20.835 7.988   158.348 1.00 28.50  ? 496 GLN B CG  1 
ATOM 7489 C CD  . GLN B 1 450 ? -19.531 8.715   158.120 1.00 35.91  ? 496 GLN B CD  1 
ATOM 7490 O OE1 . GLN B 1 450 ? -18.853 8.494   157.119 1.00 43.00  ? 496 GLN B OE1 1 
ATOM 7491 N NE2 . GLN B 1 450 ? -19.172 9.592   159.048 1.00 38.80  ? 496 GLN B NE2 1 
ATOM 7492 N N   . PHE B 1 451 ? -24.258 9.470   155.762 1.00 37.75  ? 497 PHE B N   1 
ATOM 7493 C CA  . PHE B 1 451 ? -25.250 9.579   154.702 1.00 33.37  ? 497 PHE B CA  1 
ATOM 7494 C C   . PHE B 1 451 ? -25.198 10.968  154.081 1.00 35.29  ? 497 PHE B C   1 
ATOM 7495 O O   . PHE B 1 451 ? -25.121 11.977  154.787 1.00 37.53  ? 497 PHE B O   1 
ATOM 7496 C CB  . PHE B 1 451 ? -26.647 9.297   155.249 1.00 28.17  ? 497 PHE B CB  1 
ATOM 7497 C CG  . PHE B 1 451 ? -26.816 7.907   155.787 1.00 28.12  ? 497 PHE B CG  1 
ATOM 7498 C CD1 . PHE B 1 451 ? -26.517 7.620   157.105 1.00 34.98  ? 497 PHE B CD1 1 
ATOM 7499 C CD2 . PHE B 1 451 ? -27.273 6.887   154.973 1.00 33.81  ? 497 PHE B CD2 1 
ATOM 7500 C CE1 . PHE B 1 451 ? -26.669 6.345   157.599 1.00 31.77  ? 497 PHE B CE1 1 
ATOM 7501 C CE2 . PHE B 1 451 ? -27.426 5.610   155.466 1.00 32.95  ? 497 PHE B CE2 1 
ATOM 7502 C CZ  . PHE B 1 451 ? -27.126 5.340   156.781 1.00 27.83  ? 497 PHE B CZ  1 
ATOM 7503 N N   . ASP B 1 452 ? -25.243 11.018  152.750 1.00 39.28  ? 498 ASP B N   1 
ATOM 7504 C CA  . ASP B 1 452 ? -25.048 12.288  152.059 1.00 42.71  ? 498 ASP B CA  1 
ATOM 7505 C C   . ASP B 1 452 ? -26.240 13.219  152.249 1.00 52.71  ? 498 ASP B C   1 
ATOM 7506 O O   . ASP B 1 452 ? -26.131 14.257  152.910 1.00 62.04  ? 498 ASP B O   1 
ATOM 7507 C CB  . ASP B 1 452 ? -24.794 12.043  150.571 1.00 46.26  ? 498 ASP B CB  1 
ATOM 7508 C CG  . ASP B 1 452 ? -23.779 13.004  149.992 1.00 54.82  ? 498 ASP B CG  1 
ATOM 7509 O OD1 . ASP B 1 452 ? -23.657 14.127  150.522 1.00 60.15  ? 498 ASP B OD1 1 
ATOM 7510 O OD2 . ASP B 1 452 ? -23.106 12.639  149.007 1.00 54.29  ? 498 ASP B OD2 1 
ATOM 7511 N N   . TRP B 1 453 ? -27.386 12.865  151.681 1.00 42.69  ? 499 TRP B N   1 
ATOM 7512 C CA  . TRP B 1 453 ? -28.587 13.690  151.798 1.00 39.04  ? 499 TRP B CA  1 
ATOM 7513 C C   . TRP B 1 453 ? -29.450 13.213  152.964 1.00 41.28  ? 499 TRP B C   1 
ATOM 7514 O O   . TRP B 1 453 ? -30.618 12.861  152.815 1.00 50.34  ? 499 TRP B O   1 
ATOM 7515 C CB  . TRP B 1 453 ? -29.364 13.682  150.487 1.00 44.66  ? 499 TRP B CB  1 
ATOM 7516 C CG  . TRP B 1 453 ? -28.592 14.261  149.351 1.00 51.78  ? 499 TRP B CG  1 
ATOM 7517 C CD1 . TRP B 1 453 ? -28.106 13.594  148.266 1.00 50.86  ? 499 TRP B CD1 1 
ATOM 7518 C CD2 . TRP B 1 453 ? -28.208 15.630  149.186 1.00 55.64  ? 499 TRP B CD2 1 
ATOM 7519 N NE1 . TRP B 1 453 ? -27.445 14.463  147.434 1.00 55.52  ? 499 TRP B NE1 1 
ATOM 7520 C CE2 . TRP B 1 453 ? -27.493 15.720  147.977 1.00 56.56  ? 499 TRP B CE2 1 
ATOM 7521 C CE3 . TRP B 1 453 ? -28.401 16.789  149.943 1.00 51.85  ? 499 TRP B CE3 1 
ATOM 7522 C CZ2 . TRP B 1 453 ? -26.970 16.921  147.507 1.00 54.44  ? 499 TRP B CZ2 1 
ATOM 7523 C CZ3 . TRP B 1 453 ? -27.882 17.981  149.475 1.00 50.82  ? 499 TRP B CZ3 1 
ATOM 7524 C CH2 . TRP B 1 453 ? -27.175 18.038  148.269 1.00 52.01  ? 499 TRP B CH2 1 
ATOM 7525 N N   . ALA B 1 454 ? -28.846 13.208  154.139 1.00 35.01  ? 500 ALA B N   1 
ATOM 7526 C CA  . ALA B 1 454 ? -29.562 12.809  155.335 1.00 35.60  ? 500 ALA B CA  1 
ATOM 7527 C C   . ALA B 1 454 ? -30.553 13.893  155.748 1.00 40.35  ? 500 ALA B C   1 
ATOM 7528 O O   . ALA B 1 454 ? -30.320 15.080  155.507 1.00 48.98  ? 500 ALA B O   1 
ATOM 7529 C CB  . ALA B 1 454 ? -28.586 12.539  156.474 1.00 37.30  ? 500 ALA B CB  1 
ATOM 7530 N N   . PRO B 1 455 ? -31.669 13.510  156.362 1.00 32.27  ? 501 PRO B N   1 
ATOM 7531 C CA  . PRO B 1 455 ? -32.628 14.511  156.836 1.00 33.45  ? 501 PRO B CA  1 
ATOM 7532 C C   . PRO B 1 455 ? -32.022 15.402  157.908 1.00 40.72  ? 501 PRO B C   1 
ATOM 7533 O O   . PRO B 1 455 ? -31.131 14.998  158.657 1.00 46.98  ? 501 PRO B O   1 
ATOM 7534 C CB  . PRO B 1 455 ? -33.775 13.665  157.401 1.00 34.10  ? 501 PRO B CB  1 
ATOM 7535 C CG  . PRO B 1 455 ? -33.175 12.323  157.650 1.00 33.16  ? 501 PRO B CG  1 
ATOM 7536 C CD  . PRO B 1 455 ? -32.153 12.139  156.582 1.00 32.88  ? 501 PRO B CD  1 
ATOM 7537 N N   . GLN B 1 456 ? -32.514 16.636  157.962 1.00 35.91  ? 502 GLN B N   1 
ATOM 7538 C CA  . GLN B 1 456 ? -32.007 17.603  158.925 1.00 36.32  ? 502 GLN B CA  1 
ATOM 7539 C C   . GLN B 1 456 ? -32.402 17.209  160.343 1.00 35.67  ? 502 GLN B C   1 
ATOM 7540 O O   . GLN B 1 456 ? -33.494 16.687  160.580 1.00 42.60  ? 502 GLN B O   1 
ATOM 7541 C CB  . GLN B 1 456 ? -32.530 18.997  158.591 1.00 38.38  ? 502 GLN B CB  1 
ATOM 7542 C CG  . GLN B 1 456 ? -32.144 19.460  157.199 1.00 35.02  ? 502 GLN B CG  1 
ATOM 7543 C CD  . GLN B 1 456 ? -33.132 20.442  156.618 1.00 43.16  ? 502 GLN B CD  1 
ATOM 7544 O OE1 . GLN B 1 456 ? -34.015 20.939  157.315 1.00 44.75  ? 502 GLN B OE1 1 
ATOM 7545 N NE2 . GLN B 1 456 ? -32.996 20.723  155.329 1.00 43.16  ? 502 GLN B NE2 1 
ATOM 7546 N N   . LEU B 1 457 ? -31.505 17.468  161.288 1.00 35.81  ? 503 LEU B N   1 
ATOM 7547 C CA  . LEU B 1 457 ? -31.656 17.028  162.666 1.00 36.90  ? 503 LEU B CA  1 
ATOM 7548 C C   . LEU B 1 457 ? -31.983 18.206  163.575 1.00 35.38  ? 503 LEU B C   1 
ATOM 7549 O O   . LEU B 1 457 ? -31.573 19.341  163.323 1.00 46.93  ? 503 LEU B O   1 
ATOM 7550 C CB  . LEU B 1 457 ? -30.379 16.341  163.151 1.00 37.04  ? 503 LEU B CB  1 
ATOM 7551 C CG  . LEU B 1 457 ? -30.343 14.814  163.142 1.00 38.26  ? 503 LEU B CG  1 
ATOM 7552 C CD1 . LEU B 1 457 ? -30.815 14.262  161.810 1.00 36.18  ? 503 LEU B CD1 1 
ATOM 7553 C CD2 . LEU B 1 457 ? -28.941 14.326  163.460 1.00 40.82  ? 503 LEU B CD2 1 
ATOM 7554 N N   . TYR B 1 458 ? -32.731 17.923  164.643 1.00 35.16  ? 504 TYR B N   1 
ATOM 7555 C CA  . TYR B 1 458 ? -33.124 18.927  165.635 1.00 42.83  ? 504 TYR B CA  1 
ATOM 7556 C C   . TYR B 1 458 ? -32.874 18.345  167.024 1.00 45.20  ? 504 TYR B C   1 
ATOM 7557 O O   . TYR B 1 458 ? -33.755 17.713  167.610 1.00 51.74  ? 504 TYR B O   1 
ATOM 7558 C CB  . TYR B 1 458 ? -34.582 19.336  165.459 1.00 42.79  ? 504 TYR B CB  1 
ATOM 7559 C CG  . TYR B 1 458 ? -34.848 20.212  164.258 1.00 44.12  ? 504 TYR B CG  1 
ATOM 7560 C CD1 . TYR B 1 458 ? -34.966 19.666  162.989 1.00 44.66  ? 504 TYR B CD1 1 
ATOM 7561 C CD2 . TYR B 1 458 ? -34.992 21.584  164.395 1.00 43.04  ? 504 TYR B CD2 1 
ATOM 7562 C CE1 . TYR B 1 458 ? -35.214 20.463  161.890 1.00 46.56  ? 504 TYR B CE1 1 
ATOM 7563 C CE2 . TYR B 1 458 ? -35.240 22.388  163.302 1.00 45.60  ? 504 TYR B CE2 1 
ATOM 7564 C CZ  . TYR B 1 458 ? -35.350 21.822  162.052 1.00 49.38  ? 504 TYR B CZ  1 
ATOM 7565 O OH  . TYR B 1 458 ? -35.597 22.619  160.959 1.00 52.85  ? 504 TYR B OH  1 
ATOM 7566 N N   . LEU B 1 459 ? -31.680 18.571  167.557 1.00 42.58  ? 505 LEU B N   1 
ATOM 7567 C CA  . LEU B 1 459 ? -31.323 18.024  168.856 1.00 36.66  ? 505 LEU B CA  1 
ATOM 7568 C C   . LEU B 1 459 ? -31.742 18.958  169.982 1.00 43.41  ? 505 LEU B C   1 
ATOM 7569 O O   . LEU B 1 459 ? -31.699 20.183  169.852 1.00 51.36  ? 505 LEU B O   1 
ATOM 7570 C CB  . LEU B 1 459 ? -29.820 17.774  168.941 1.00 40.75  ? 505 LEU B CB  1 
ATOM 7571 C CG  . LEU B 1 459 ? -29.163 17.021  167.789 1.00 44.76  ? 505 LEU B CG  1 
ATOM 7572 C CD1 . LEU B 1 459 ? -28.615 17.974  166.741 1.00 44.55  ? 505 LEU B CD1 1 
ATOM 7573 C CD2 . LEU B 1 459 ? -28.064 16.154  168.349 1.00 46.84  ? 505 LEU B CD2 1 
ATOM 7574 N N   . THR B 1 460 ? -32.139 18.360  171.103 1.00 42.92  ? 506 THR B N   1 
ATOM 7575 C CA  . THR B 1 460 ? -32.467 19.101  172.311 1.00 46.12  ? 506 THR B CA  1 
ATOM 7576 C C   . THR B 1 460 ? -31.791 18.426  173.495 1.00 48.69  ? 506 THR B C   1 
ATOM 7577 O O   . THR B 1 460 ? -31.531 17.221  173.483 1.00 52.16  ? 506 THR B O   1 
ATOM 7578 C CB  . THR B 1 460 ? -33.980 19.184  172.536 1.00 46.30  ? 506 THR B CB  1 
ATOM 7579 O OG1 . THR B 1 460 ? -34.244 19.672  173.856 1.00 50.70  ? 506 THR B OG1 1 
ATOM 7580 C CG2 . THR B 1 460 ? -34.613 17.819  172.374 1.00 51.29  ? 506 THR B CG2 1 
ATOM 7581 N N   . TYR B 1 461 ? -31.508 19.218  174.526 1.00 54.48  ? 507 TYR B N   1 
ATOM 7582 C CA  . TYR B 1 461 ? -30.761 18.749  175.682 1.00 49.69  ? 507 TYR B CA  1 
ATOM 7583 C C   . TYR B 1 461 ? -31.600 18.897  176.943 1.00 55.27  ? 507 TYR B C   1 
ATOM 7584 O O   . TYR B 1 461 ? -32.407 19.819  177.075 1.00 60.82  ? 507 TYR B O   1 
ATOM 7585 C CB  . TYR B 1 461 ? -29.438 19.508  175.830 1.00 47.12  ? 507 TYR B CB  1 
ATOM 7586 C CG  . TYR B 1 461 ? -28.332 18.939  174.978 1.00 51.28  ? 507 TYR B CG  1 
ATOM 7587 C CD1 . TYR B 1 461 ? -28.291 19.180  173.614 1.00 46.10  ? 507 TYR B CD1 1 
ATOM 7588 C CD2 . TYR B 1 461 ? -27.327 18.163  175.537 1.00 59.47  ? 507 TYR B CD2 1 
ATOM 7589 C CE1 . TYR B 1 461 ? -27.286 18.659  172.829 1.00 49.44  ? 507 TYR B CE1 1 
ATOM 7590 C CE2 . TYR B 1 461 ? -26.316 17.638  174.758 1.00 58.43  ? 507 TYR B CE2 1 
ATOM 7591 C CZ  . TYR B 1 461 ? -26.301 17.891  173.404 1.00 56.24  ? 507 TYR B CZ  1 
ATOM 7592 O OH  . TYR B 1 461 ? -25.295 17.373  172.622 1.00 56.29  ? 507 TYR B OH  1 
ATOM 7593 N N   . GLY B 1 462 ? -31.389 17.972  177.875 1.00 60.19  ? 508 GLY B N   1 
ATOM 7594 C CA  . GLY B 1 462 ? -32.175 17.930  179.091 1.00 61.28  ? 508 GLY B CA  1 
ATOM 7595 C C   . GLY B 1 462 ? -31.799 18.979  180.115 1.00 63.81  ? 508 GLY B C   1 
ATOM 7596 O O   . GLY B 1 462 ? -32.676 19.595  180.727 1.00 63.00  ? 508 GLY B O   1 
ATOM 7597 N N   . ILE B 1 463 ? -30.498 19.192  180.319 1.00 65.64  ? 509 ILE B N   1 
ATOM 7598 C CA  . ILE B 1 463 ? -30.072 20.195  181.288 1.00 66.44  ? 509 ILE B CA  1 
ATOM 7599 C C   . ILE B 1 463 ? -30.032 21.579  180.667 1.00 67.51  ? 509 ILE B C   1 
ATOM 7600 O O   . ILE B 1 463 ? -30.191 22.582  181.371 1.00 68.75  ? 509 ILE B O   1 
ATOM 7601 C CB  . ILE B 1 463 ? -28.709 19.830  181.893 1.00 64.28  ? 509 ILE B CB  1 
ATOM 7602 C CG1 . ILE B 1 463 ? -27.778 19.279  180.812 1.00 61.67  ? 509 ILE B CG1 1 
ATOM 7603 C CG2 . ILE B 1 463 ? -28.892 18.873  183.051 1.00 66.50  ? 509 ILE B CG2 1 
ATOM 7604 C CD1 . ILE B 1 463 ? -26.327 19.255  181.223 1.00 61.64  ? 509 ILE B CD1 1 
ATOM 7605 N N   . ALA B 1 464 ? -29.798 21.672  179.363 1.00 65.49  ? 510 ALA B N   1 
ATOM 7606 C CA  . ALA B 1 464 ? -29.846 22.964  178.704 1.00 64.21  ? 510 ALA B CA  1 
ATOM 7607 C C   . ALA B 1 464 ? -31.266 23.455  178.479 1.00 67.30  ? 510 ALA B C   1 
ATOM 7608 O O   . ALA B 1 464 ? -31.473 24.667  178.398 1.00 67.54  ? 510 ALA B O   1 
ATOM 7609 C CB  . ALA B 1 464 ? -29.109 22.908  177.363 1.00 61.64  ? 510 ALA B CB  1 
ATOM 7610 N N   . GLN B 1 465 ? -32.245 22.550  178.407 1.00 63.70  ? 511 GLN B N   1 
ATOM 7611 C CA  . GLN B 1 465 ? -33.620 22.902  178.044 1.00 61.91  ? 511 GLN B CA  1 
ATOM 7612 C C   . GLN B 1 465 ? -33.646 23.759  176.783 1.00 63.40  ? 511 GLN B C   1 
ATOM 7613 O O   . GLN B 1 465 ? -34.383 24.741  176.686 1.00 69.37  ? 511 GLN B O   1 
ATOM 7614 C CB  . GLN B 1 465 ? -34.352 23.604  179.193 1.00 62.22  ? 511 GLN B CB  1 
ATOM 7615 C CG  . GLN B 1 465 ? -34.315 22.877  180.527 1.00 63.42  ? 511 GLN B CG  1 
ATOM 7616 C CD  . GLN B 1 465 ? -33.099 23.219  181.359 1.00 66.09  ? 511 GLN B CD  1 
ATOM 7617 O OE1 . GLN B 1 465 ? -32.464 24.254  181.155 1.00 69.37  ? 511 GLN B OE1 1 
ATOM 7618 N NE2 . GLN B 1 465 ? -32.770 22.353  182.308 1.00 65.04  ? 511 GLN B NE2 1 
ATOM 7619 N N   . GLU B 1 466 ? -32.824 23.384  175.808 1.00 52.63  ? 512 GLU B N   1 
ATOM 7620 C CA  . GLU B 1 466 ? -32.659 24.164  174.593 1.00 55.82  ? 512 GLU B CA  1 
ATOM 7621 C C   . GLU B 1 466 ? -32.510 23.220  173.413 1.00 54.33  ? 512 GLU B C   1 
ATOM 7622 O O   . GLU B 1 466 ? -31.784 22.226  173.498 1.00 52.30  ? 512 GLU B O   1 
ATOM 7623 C CB  . GLU B 1 466 ? -31.440 25.080  174.694 1.00 58.61  ? 512 GLU B CB  1 
ATOM 7624 C CG  . GLU B 1 466 ? -31.045 25.744  173.394 1.00 60.20  ? 512 GLU B CG  1 
ATOM 7625 C CD  . GLU B 1 466 ? -30.040 26.855  173.591 1.00 61.91  ? 512 GLU B CD  1 
ATOM 7626 O OE1 . GLU B 1 466 ? -29.451 26.934  174.691 1.00 60.31  ? 512 GLU B OE1 1 
ATOM 7627 O OE2 . GLU B 1 466 ? -29.835 27.647  172.651 1.00 64.40  ? 512 GLU B OE2 1 
ATOM 7628 N N   . SER B 1 467 ? -33.190 23.530  172.315 1.00 53.27  ? 513 SER B N   1 
ATOM 7629 C CA  . SER B 1 467 ? -33.071 22.743  171.099 1.00 51.83  ? 513 SER B CA  1 
ATOM 7630 C C   . SER B 1 467 ? -32.032 23.382  170.182 1.00 55.47  ? 513 SER B C   1 
ATOM 7631 O O   . SER B 1 467 ? -31.482 24.445  170.476 1.00 59.59  ? 513 SER B O   1 
ATOM 7632 C CB  . SER B 1 467 ? -34.429 22.613  170.414 1.00 55.86  ? 513 SER B CB  1 
ATOM 7633 O OG  . SER B 1 467 ? -35.427 22.212  171.334 1.00 58.63  ? 513 SER B OG  1 
ATOM 7634 N N   . PHE B 1 468 ? -31.753 22.737  169.056 1.00 55.80  ? 514 PHE B N   1 
ATOM 7635 C CA  . PHE B 1 468 ? -30.809 23.266  168.089 1.00 55.14  ? 514 PHE B CA  1 
ATOM 7636 C C   . PHE B 1 468 ? -31.400 23.149  166.693 1.00 56.23  ? 514 PHE B C   1 
ATOM 7637 O O   . PHE B 1 468 ? -32.217 22.267  166.419 1.00 55.36  ? 514 PHE B O   1 
ATOM 7638 C CB  . PHE B 1 468 ? -29.460 22.542  168.158 1.00 41.39  ? 514 PHE B CB  1 
ATOM 7639 C CG  . PHE B 1 468 ? -28.375 23.229  167.392 1.00 48.48  ? 514 PHE B CG  1 
ATOM 7640 C CD1 . PHE B 1 468 ? -27.869 24.441  167.823 1.00 53.12  ? 514 PHE B CD1 1 
ATOM 7641 C CD2 . PHE B 1 468 ? -27.865 22.670  166.237 1.00 52.72  ? 514 PHE B CD2 1 
ATOM 7642 C CE1 . PHE B 1 468 ? -26.876 25.080  167.116 1.00 55.90  ? 514 PHE B CE1 1 
ATOM 7643 C CE2 . PHE B 1 468 ? -26.870 23.304  165.530 1.00 53.51  ? 514 PHE B CE2 1 
ATOM 7644 C CZ  . PHE B 1 468 ? -26.374 24.511  165.967 1.00 54.39  ? 514 PHE B CZ  1 
ATOM 7645 N N   . GLY B 1 469 ? -30.976 24.052  165.813 1.00 51.67  ? 515 GLY B N   1 
ATOM 7646 C CA  . GLY B 1 469 ? -31.513 24.133  164.477 1.00 49.90  ? 515 GLY B CA  1 
ATOM 7647 C C   . GLY B 1 469 ? -31.120 22.959  163.608 1.00 50.52  ? 515 GLY B C   1 
ATOM 7648 O O   . GLY B 1 469 ? -30.649 21.925  164.090 1.00 50.15  ? 515 GLY B O   1 
ATOM 7649 N N   . PRO B 1 470 ? -31.303 23.103  162.295 1.00 42.82  ? 516 PRO B N   1 
ATOM 7650 C CA  . PRO B 1 470 ? -31.015 21.994  161.373 1.00 40.37  ? 516 PRO B CA  1 
ATOM 7651 C C   . PRO B 1 470 ? -29.541 21.622  161.417 1.00 47.08  ? 516 PRO B C   1 
ATOM 7652 O O   . PRO B 1 470 ? -28.672 22.430  161.085 1.00 56.80  ? 516 PRO B O   1 
ATOM 7653 C CB  . PRO B 1 470 ? -31.419 22.553  160.002 1.00 36.43  ? 516 PRO B CB  1 
ATOM 7654 C CG  . PRO B 1 470 ? -32.283 23.733  160.301 1.00 44.85  ? 516 PRO B CG  1 
ATOM 7655 C CD  . PRO B 1 470 ? -31.769 24.299  161.581 1.00 42.99  ? 516 PRO B CD  1 
ATOM 7656 N N   . PHE B 1 471 ? -29.265 20.389  161.837 1.00 35.37  ? 517 PHE B N   1 
ATOM 7657 C CA  . PHE B 1 471 ? -27.902 19.876  161.932 1.00 29.77  ? 517 PHE B CA  1 
ATOM 7658 C C   . PHE B 1 471 ? -27.545 19.244  160.590 1.00 32.59  ? 517 PHE B C   1 
ATOM 7659 O O   . PHE B 1 471 ? -27.404 18.029  160.457 1.00 49.97  ? 517 PHE B O   1 
ATOM 7660 C CB  . PHE B 1 471 ? -27.787 18.886  163.084 1.00 36.03  ? 517 PHE B CB  1 
ATOM 7661 C CG  . PHE B 1 471 ? -26.380 18.612  163.514 1.00 38.77  ? 517 PHE B CG  1 
ATOM 7662 C CD1 . PHE B 1 471 ? -25.747 19.442  164.421 1.00 39.86  ? 517 PHE B CD1 1 
ATOM 7663 C CD2 . PHE B 1 471 ? -25.691 17.517  163.023 1.00 37.00  ? 517 PHE B CD2 1 
ATOM 7664 C CE1 . PHE B 1 471 ? -24.453 19.190  164.824 1.00 43.54  ? 517 PHE B CE1 1 
ATOM 7665 C CE2 . PHE B 1 471 ? -24.398 17.259  163.422 1.00 40.56  ? 517 PHE B CE2 1 
ATOM 7666 C CZ  . PHE B 1 471 ? -23.777 18.097  164.325 1.00 42.18  ? 517 PHE B CZ  1 
ATOM 7667 N N   . ALA B 1 472 ? -27.405 20.096  159.578 1.00 31.21  ? 518 ALA B N   1 
ATOM 7668 C CA  . ALA B 1 472 ? -27.125 19.634  158.229 1.00 38.26  ? 518 ALA B CA  1 
ATOM 7669 C C   . ALA B 1 472 ? -26.267 20.665  157.513 1.00 42.78  ? 518 ALA B C   1 
ATOM 7670 O O   . ALA B 1 472 ? -26.195 21.829  157.911 1.00 42.34  ? 518 ALA B O   1 
ATOM 7671 C CB  . ALA B 1 472 ? -28.414 19.375  157.443 1.00 44.32  ? 518 ALA B CB  1 
ATOM 7672 N N   . GLN B 1 473 ? -25.612 20.217  156.445 1.00 43.44  ? 519 GLN B N   1 
ATOM 7673 C CA  . GLN B 1 473 ? -24.760 21.075  155.631 1.00 40.96  ? 519 GLN B CA  1 
ATOM 7674 C C   . GLN B 1 473 ? -25.623 21.758  154.577 1.00 43.30  ? 519 GLN B C   1 
ATOM 7675 O O   . GLN B 1 473 ? -25.996 21.141  153.575 1.00 46.18  ? 519 GLN B O   1 
ATOM 7676 C CB  . GLN B 1 473 ? -23.642 20.264  154.983 1.00 36.82  ? 519 GLN B CB  1 
ATOM 7677 C CG  . GLN B 1 473 ? -22.590 21.106  154.287 1.00 44.42  ? 519 GLN B CG  1 
ATOM 7678 C CD  . GLN B 1 473 ? -21.793 20.316  153.272 1.00 48.29  ? 519 GLN B CD  1 
ATOM 7679 O OE1 . GLN B 1 473 ? -20.858 19.597  153.624 1.00 47.87  ? 519 GLN B OE1 1 
ATOM 7680 N NE2 . GLN B 1 473 ? -22.156 20.447  152.002 1.00 44.64  ? 519 GLN B NE2 1 
ATOM 7681 N N   . LEU B 1 474 ? -25.942 23.029  154.805 1.00 46.16  ? 520 LEU B N   1 
ATOM 7682 C CA  . LEU B 1 474 ? -26.763 23.788  153.872 1.00 47.14  ? 520 LEU B CA  1 
ATOM 7683 C C   . LEU B 1 474 ? -25.927 24.240  152.682 1.00 45.63  ? 520 LEU B C   1 
ATOM 7684 O O   . LEU B 1 474 ? -24.812 24.743  152.851 1.00 47.55  ? 520 LEU B O   1 
ATOM 7685 C CB  . LEU B 1 474 ? -27.381 24.994  154.574 1.00 42.13  ? 520 LEU B CB  1 
ATOM 7686 C CG  . LEU B 1 474 ? -28.135 24.696  155.870 1.00 42.58  ? 520 LEU B CG  1 
ATOM 7687 C CD1 . LEU B 1 474 ? -28.692 25.973  156.466 1.00 38.96  ? 520 LEU B CD1 1 
ATOM 7688 C CD2 . LEU B 1 474 ? -29.245 23.691  155.621 1.00 45.85  ? 520 LEU B CD2 1 
ATOM 7689 N N   . ASN B 1 475 ? -26.465 24.059  151.476 1.00 39.24  ? 521 ASN B N   1 
ATOM 7690 C CA  . ASN B 1 475 ? -25.795 24.472  150.250 1.00 43.74  ? 521 ASN B CA  1 
ATOM 7691 C C   . ASN B 1 475 ? -26.537 25.602  149.548 1.00 49.56  ? 521 ASN B C   1 
ATOM 7692 O O   . ASN B 1 475 ? -25.972 26.677  149.331 1.00 54.25  ? 521 ASN B O   1 
ATOM 7693 C CB  . ASN B 1 475 ? -25.639 23.273  149.305 1.00 43.47  ? 521 ASN B CB  1 
ATOM 7694 C CG  . ASN B 1 475 ? -25.467 21.966  150.046 1.00 53.75  ? 521 ASN B CG  1 
ATOM 7695 O OD1 . ASN B 1 475 ? -24.412 21.700  150.621 1.00 58.01  ? 521 ASN B OD1 1 
ATOM 7696 N ND2 . ASN B 1 475 ? -26.504 21.138  150.036 1.00 52.64  ? 521 ASN B ND2 1 
ATOM 7697 N N   . ASP B 1 476 ? -27.799 25.384  149.191 1.00 50.02  ? 522 ASP B N   1 
ATOM 7698 C CA  . ASP B 1 476 ? -28.619 26.418  148.565 1.00 49.61  ? 522 ASP B CA  1 
ATOM 7699 C C   . ASP B 1 476 ? -30.020 26.264  149.134 1.00 48.64  ? 522 ASP B C   1 
ATOM 7700 O O   . ASP B 1 476 ? -30.771 25.385  148.704 1.00 52.72  ? 522 ASP B O   1 
ATOM 7701 C CB  . ASP B 1 476 ? -28.618 26.288  147.046 1.00 49.87  ? 522 ASP B CB  1 
ATOM 7702 C CG  . ASP B 1 476 ? -29.312 27.448  146.365 1.00 53.41  ? 522 ASP B CG  1 
ATOM 7703 O OD1 . ASP B 1 476 ? -29.341 28.549  146.952 1.00 53.67  ? 522 ASP B OD1 1 
ATOM 7704 O OD2 . ASP B 1 476 ? -29.822 27.262  145.242 1.00 58.91  ? 522 ASP B OD2 1 
ATOM 7705 N N   . TRP B 1 477 ? -30.370 27.121  150.086 1.00 31.36  ? 523 TRP B N   1 
ATOM 7706 C CA  . TRP B 1 477 ? -31.503 26.883  150.961 1.00 32.59  ? 523 TRP B CA  1 
ATOM 7707 C C   . TRP B 1 477 ? -32.457 28.066  150.933 1.00 37.56  ? 523 TRP B C   1 
ATOM 7708 O O   . TRP B 1 477 ? -32.088 29.191  150.591 1.00 44.50  ? 523 TRP B O   1 
ATOM 7709 C CB  . TRP B 1 477 ? -31.033 26.634  152.397 1.00 38.67  ? 523 TRP B CB  1 
ATOM 7710 C CG  . TRP B 1 477 ? -30.074 27.674  152.865 1.00 39.35  ? 523 TRP B CG  1 
ATOM 7711 C CD1 . TRP B 1 477 ? -28.722 27.674  152.703 1.00 45.83  ? 523 TRP B CD1 1 
ATOM 7712 C CD2 . TRP B 1 477 ? -30.395 28.888  153.552 1.00 37.81  ? 523 TRP B CD2 1 
ATOM 7713 N NE1 . TRP B 1 477 ? -28.178 28.806  153.256 1.00 45.42  ? 523 TRP B NE1 1 
ATOM 7714 C CE2 . TRP B 1 477 ? -29.186 29.568  153.784 1.00 39.35  ? 523 TRP B CE2 1 
ATOM 7715 C CE3 . TRP B 1 477 ? -31.587 29.461  154.001 1.00 34.66  ? 523 TRP B CE3 1 
ATOM 7716 C CZ2 . TRP B 1 477 ? -29.134 30.791  154.443 1.00 38.98  ? 523 TRP B CZ2 1 
ATOM 7717 C CZ3 . TRP B 1 477 ? -31.533 30.675  154.652 1.00 38.00  ? 523 TRP B CZ3 1 
ATOM 7718 C CH2 . TRP B 1 477 ? -30.316 31.327  154.868 1.00 40.52  ? 523 TRP B CH2 1 
ATOM 7719 N N   . THR B 1 478 ? -33.702 27.787  151.311 1.00 42.61  ? 524 THR B N   1 
ATOM 7720 C CA  . THR B 1 478 ? -34.701 28.820  151.526 1.00 43.92  ? 524 THR B CA  1 
ATOM 7721 C C   . THR B 1 478 ? -35.534 28.427  152.734 1.00 45.95  ? 524 THR B C   1 
ATOM 7722 O O   . THR B 1 478 ? -35.627 27.251  153.093 1.00 49.77  ? 524 THR B O   1 
ATOM 7723 C CB  . THR B 1 478 ? -35.598 29.019  150.300 1.00 39.60  ? 524 THR B CB  1 
ATOM 7724 O OG1 . THR B 1 478 ? -36.454 30.147  150.514 1.00 39.54  ? 524 THR B OG1 1 
ATOM 7725 C CG2 . THR B 1 478 ? -36.454 27.790  150.061 1.00 40.42  ? 524 THR B CG2 1 
ATOM 7726 N N   . ILE B 1 479 ? -36.134 29.428  153.367 1.00 37.17  ? 525 ILE B N   1 
ATOM 7727 C CA  . ILE B 1 479 ? -36.978 29.220  154.536 1.00 39.81  ? 525 ILE B CA  1 
ATOM 7728 C C   . ILE B 1 479 ? -38.410 29.054  154.053 1.00 41.67  ? 525 ILE B C   1 
ATOM 7729 O O   . ILE B 1 479 ? -38.957 29.942  153.389 1.00 44.52  ? 525 ILE B O   1 
ATOM 7730 C CB  . ILE B 1 479 ? -36.858 30.383  155.531 1.00 41.48  ? 525 ILE B CB  1 
ATOM 7731 C CG1 . ILE B 1 479 ? -35.445 30.439  156.110 1.00 37.31  ? 525 ILE B CG1 1 
ATOM 7732 C CG2 . ILE B 1 479 ? -37.880 30.237  156.641 1.00 43.84  ? 525 ILE B CG2 1 
ATOM 7733 C CD1 . ILE B 1 479 ? -35.150 31.708  156.875 1.00 39.98  ? 525 ILE B CD1 1 
ATOM 7734 N N   . LEU B 1 480 ? -39.018 27.919  154.380 1.00 43.33  ? 526 LEU B N   1 
ATOM 7735 C CA  . LEU B 1 480 ? -40.366 27.608  153.937 1.00 45.05  ? 526 LEU B CA  1 
ATOM 7736 C C   . LEU B 1 480 ? -41.385 28.056  154.975 1.00 45.19  ? 526 LEU B C   1 
ATOM 7737 O O   . LEU B 1 480 ? -41.135 28.011  156.182 1.00 49.38  ? 526 LEU B O   1 
ATOM 7738 C CB  . LEU B 1 480 ? -40.522 26.112  153.667 1.00 43.53  ? 526 LEU B CB  1 
ATOM 7739 C CG  . LEU B 1 480 ? -40.244 25.689  152.226 1.00 44.98  ? 526 LEU B CG  1 
ATOM 7740 C CD1 . LEU B 1 480 ? -40.482 24.204  152.050 1.00 42.50  ? 526 LEU B CD1 1 
ATOM 7741 C CD2 . LEU B 1 480 ? -41.103 26.489  151.266 1.00 42.99  ? 526 LEU B CD2 1 
ATOM 7742 N N   . THR B 1 481 ? -42.540 28.493  154.488 1.00 49.16  ? 527 THR B N   1 
ATOM 7743 C CA  . THR B 1 481 ? -43.619 28.989  155.324 1.00 49.18  ? 527 THR B CA  1 
ATOM 7744 C C   . THR B 1 481 ? -44.778 28.001  155.295 1.00 54.57  ? 527 THR B C   1 
ATOM 7745 O O   . THR B 1 481 ? -44.912 27.205  154.360 1.00 60.00  ? 527 THR B O   1 
ATOM 7746 C CB  . THR B 1 481 ? -44.084 30.370  154.848 1.00 55.02  ? 527 THR B CB  1 
ATOM 7747 O OG1 . THR B 1 481 ? -42.940 31.171  154.530 1.00 52.84  ? 527 THR B OG1 1 
ATOM 7748 C CG2 . THR B 1 481 ? -44.879 31.080  155.934 1.00 53.13  ? 527 THR B CG2 1 
ATOM 7749 N N   . GLY B 1 482 ? -45.606 28.048  156.340 1.00 55.69  ? 528 GLY B N   1 
ATOM 7750 C CA  . GLY B 1 482 ? -46.732 27.133  156.420 1.00 49.78  ? 528 GLY B CA  1 
ATOM 7751 C C   . GLY B 1 482 ? -47.694 27.273  155.257 1.00 47.06  ? 528 GLY B C   1 
ATOM 7752 O O   . GLY B 1 482 ? -48.173 26.276  154.716 1.00 53.66  ? 528 GLY B O   1 
ATOM 7753 N N   . GLU B 1 483 ? -47.989 28.510  154.855 1.00 42.49  ? 529 GLU B N   1 
ATOM 7754 C CA  . GLU B 1 483 ? -48.907 28.724  153.740 1.00 50.55  ? 529 GLU B CA  1 
ATOM 7755 C C   . GLU B 1 483 ? -48.328 28.195  152.434 1.00 54.20  ? 529 GLU B C   1 
ATOM 7756 O O   . GLU B 1 483 ? -49.039 27.558  151.644 1.00 60.44  ? 529 GLU B O   1 
ATOM 7757 C CB  . GLU B 1 483 ? -49.243 30.208  153.620 1.00 55.51  ? 529 GLU B CB  1 
ATOM 7758 C CG  . GLU B 1 483 ? -50.378 30.654  154.524 1.00 59.95  ? 529 GLU B CG  1 
ATOM 7759 C CD  . GLU B 1 483 ? -49.957 30.760  155.976 1.00 63.04  ? 529 GLU B CD  1 
ATOM 7760 O OE1 . GLU B 1 483 ? -48.742 30.867  156.240 1.00 58.78  ? 529 GLU B OE1 1 
ATOM 7761 O OE2 . GLU B 1 483 ? -50.844 30.735  156.856 1.00 61.38  ? 529 GLU B OE2 1 
ATOM 7762 N N   . THR B 1 484 ? -47.042 28.451  152.188 1.00 37.92  ? 530 THR B N   1 
ATOM 7763 C CA  . THR B 1 484 ? -46.411 27.941  150.977 1.00 38.56  ? 530 THR B CA  1 
ATOM 7764 C C   . THR B 1 484 ? -46.396 26.419  150.967 1.00 44.46  ? 530 THR B C   1 
ATOM 7765 O O   . THR B 1 484 ? -46.649 25.798  149.929 1.00 52.41  ? 530 THR B O   1 
ATOM 7766 C CB  . THR B 1 484 ? -44.993 28.493  150.848 1.00 43.88  ? 530 THR B CB  1 
ATOM 7767 O OG1 . THR B 1 484 ? -45.013 29.911  151.053 1.00 51.64  ? 530 THR B OG1 1 
ATOM 7768 C CG2 . THR B 1 484 ? -44.436 28.201  149.467 1.00 46.59  ? 530 THR B CG2 1 
ATOM 7769 N N   . LEU B 1 485 ? -46.116 25.799  152.115 1.00 41.53  ? 531 LEU B N   1 
ATOM 7770 C CA  . LEU B 1 485 ? -46.126 24.342  152.178 1.00 38.95  ? 531 LEU B CA  1 
ATOM 7771 C C   . LEU B 1 485 ? -47.532 23.785  151.989 1.00 41.09  ? 531 LEU B C   1 
ATOM 7772 O O   . LEU B 1 485 ? -47.704 22.728  151.375 1.00 46.19  ? 531 LEU B O   1 
ATOM 7773 C CB  . LEU B 1 485 ? -45.530 23.860  153.497 1.00 38.50  ? 531 LEU B CB  1 
ATOM 7774 C CG  . LEU B 1 485 ? -44.864 22.489  153.381 1.00 34.54  ? 531 LEU B CG  1 
ATOM 7775 C CD1 . LEU B 1 485 ? -43.792 22.517  152.314 1.00 37.32  ? 531 LEU B CD1 1 
ATOM 7776 C CD2 . LEU B 1 485 ? -44.280 22.055  154.706 1.00 43.67  ? 531 LEU B CD2 1 
ATOM 7777 N N   . ALA B 1 486 ? -48.548 24.470  152.516 1.00 37.91  ? 532 ALA B N   1 
ATOM 7778 C CA  . ALA B 1 486 ? -49.920 24.017  152.313 1.00 38.01  ? 532 ALA B CA  1 
ATOM 7779 C C   . ALA B 1 486 ? -50.311 24.088  150.844 1.00 42.61  ? 532 ALA B C   1 
ATOM 7780 O O   . ALA B 1 486 ? -50.934 23.160  150.317 1.00 44.35  ? 532 ALA B O   1 
ATOM 7781 C CB  . ALA B 1 486 ? -50.879 24.844  153.165 1.00 40.62  ? 532 ALA B CB  1 
ATOM 7782 N N   . ARG B 1 487 ? -49.952 25.181  150.168 1.00 40.02  ? 533 ARG B N   1 
ATOM 7783 C CA  . ARG B 1 487 ? -50.200 25.276  148.732 1.00 40.87  ? 533 ARG B CA  1 
ATOM 7784 C C   . ARG B 1 487 ? -49.455 24.184  147.975 1.00 38.84  ? 533 ARG B C   1 
ATOM 7785 O O   . ARG B 1 487 ? -50.007 23.561  147.057 1.00 43.55  ? 533 ARG B O   1 
ATOM 7786 C CB  . ARG B 1 487 ? -49.791 26.659  148.227 1.00 36.99  ? 533 ARG B CB  1 
ATOM 7787 C CG  . ARG B 1 487 ? -50.069 26.909  146.757 1.00 45.34  ? 533 ARG B CG  1 
ATOM 7788 C CD  . ARG B 1 487 ? -51.556 27.051  146.472 1.00 52.86  ? 533 ARG B CD  1 
ATOM 7789 N NE  . ARG B 1 487 ? -51.816 28.105  145.499 1.00 49.62  ? 533 ARG B NE  1 
ATOM 7790 C CZ  . ARG B 1 487 ? -52.056 27.897  144.212 1.00 40.89  ? 533 ARG B CZ  1 
ATOM 7791 N NH1 . ARG B 1 487 ? -52.077 26.677  143.702 1.00 37.39  ? 533 ARG B NH1 1 
ATOM 7792 N NH2 . ARG B 1 487 ? -52.268 28.940  143.416 1.00 30.18  ? 533 ARG B NH2 1 
ATOM 7793 N N   . MET B 1 488 ? -48.202 23.933  148.356 1.00 38.62  ? 534 MET B N   1 
ATOM 7794 C CA  . MET B 1 488 ? -47.408 22.902  147.701 1.00 36.42  ? 534 MET B CA  1 
ATOM 7795 C C   . MET B 1 488 ? -48.039 21.527  147.875 1.00 43.67  ? 534 MET B C   1 
ATOM 7796 O O   . MET B 1 488 ? -48.101 20.743  146.923 1.00 49.47  ? 534 MET B O   1 
ATOM 7797 C CB  . MET B 1 488 ? -45.988 22.914  148.263 1.00 35.08  ? 534 MET B CB  1 
ATOM 7798 C CG  . MET B 1 488 ? -44.989 23.679  147.422 1.00 39.52  ? 534 MET B CG  1 
ATOM 7799 S SD  . MET B 1 488 ? -43.682 24.410  148.422 1.00 56.79  ? 534 MET B SD  1 
ATOM 7800 C CE  . MET B 1 488 ? -42.509 24.855  147.151 1.00 47.31  ? 534 MET B CE  1 
ATOM 7801 N N   . HIS B 1 489 ? -48.517 21.221  149.082 1.00 45.14  ? 535 HIS B N   1 
ATOM 7802 C CA  . HIS B 1 489 ? -49.135 19.923  149.330 1.00 39.81  ? 535 HIS B CA  1 
ATOM 7803 C C   . HIS B 1 489 ? -50.473 19.798  148.620 1.00 41.98  ? 535 HIS B C   1 
ATOM 7804 O O   . HIS B 1 489 ? -50.823 18.715  148.138 1.00 46.68  ? 535 HIS B O   1 
ATOM 7805 C CB  . HIS B 1 489 ? -49.302 19.690  150.828 1.00 35.18  ? 535 HIS B CB  1 
ATOM 7806 C CG  . HIS B 1 489 ? -48.019 19.397  151.535 1.00 38.05  ? 535 HIS B CG  1 
ATOM 7807 N ND1 . HIS B 1 489 ? -47.774 19.796  152.830 1.00 47.61  ? 535 HIS B ND1 1 
ATOM 7808 C CD2 . HIS B 1 489 ? -46.904 18.749  151.123 1.00 33.27  ? 535 HIS B CD2 1 
ATOM 7809 C CE1 . HIS B 1 489 ? -46.566 19.402  153.189 1.00 43.75  ? 535 HIS B CE1 1 
ATOM 7810 N NE2 . HIS B 1 489 ? -46.017 18.765  152.171 1.00 37.72  ? 535 HIS B NE2 1 
ATOM 7811 N N   . GLU B 1 490 ? -51.242 20.885  148.550 1.00 45.38  ? 536 GLU B N   1 
ATOM 7812 C CA  . GLU B 1 490 ? -52.485 20.835  147.791 1.00 43.87  ? 536 GLU B CA  1 
ATOM 7813 C C   . GLU B 1 490 ? -52.211 20.528  146.326 1.00 41.86  ? 536 GLU B C   1 
ATOM 7814 O O   . GLU B 1 490 ? -52.858 19.654  145.735 1.00 47.73  ? 536 GLU B O   1 
ATOM 7815 C CB  . GLU B 1 490 ? -53.247 22.152  147.934 1.00 48.06  ? 536 GLU B CB  1 
ATOM 7816 C CG  . GLU B 1 490 ? -54.369 22.102  148.957 1.00 53.29  ? 536 GLU B CG  1 
ATOM 7817 C CD  . GLU B 1 490 ? -55.218 23.356  148.949 1.00 57.92  ? 536 GLU B CD  1 
ATOM 7818 O OE1 . GLU B 1 490 ? -55.062 24.172  148.018 1.00 56.09  ? 536 GLU B OE1 1 
ATOM 7819 O OE2 . GLU B 1 490 ? -56.038 23.528  149.876 1.00 57.74  ? 536 GLU B OE2 1 
ATOM 7820 N N   . VAL B 1 491 ? -51.225 21.209  145.736 1.00 38.49  ? 537 VAL B N   1 
ATOM 7821 C CA  . VAL B 1 491 ? -50.881 20.951  144.340 1.00 37.01  ? 537 VAL B CA  1 
ATOM 7822 C C   . VAL B 1 491 ? -50.391 19.520  144.165 1.00 41.59  ? 537 VAL B C   1 
ATOM 7823 O O   . VAL B 1 491 ? -50.765 18.832  143.206 1.00 47.05  ? 537 VAL B O   1 
ATOM 7824 C CB  . VAL B 1 491 ? -49.839 21.972  143.848 1.00 37.81  ? 537 VAL B CB  1 
ATOM 7825 C CG1 . VAL B 1 491 ? -49.227 21.513  142.538 1.00 37.99  ? 537 VAL B CG1 1 
ATOM 7826 C CG2 . VAL B 1 491 ? -50.481 23.335  143.680 1.00 45.91  ? 537 VAL B CG2 1 
ATOM 7827 N N   . CYS B 1 492 ? -49.547 19.047  145.086 1.00 41.15  ? 538 CYS B N   1 
ATOM 7828 C CA  . CYS B 1 492 ? -48.979 17.709  144.959 1.00 37.32  ? 538 CYS B CA  1 
ATOM 7829 C C   . CYS B 1 492 ? -50.054 16.632  145.051 1.00 39.25  ? 538 CYS B C   1 
ATOM 7830 O O   . CYS B 1 492 ? -50.054 15.684  144.261 1.00 46.87  ? 538 CYS B O   1 
ATOM 7831 C CB  . CYS B 1 492 ? -47.900 17.494  146.020 1.00 43.02  ? 538 CYS B CB  1 
ATOM 7832 S SG  . CYS B 1 492 ? -48.464 16.725  147.553 1.00 55.12  ? 538 CYS B SG  1 
ATOM 7833 N N   . VAL B 1 493 ? -50.990 16.768  145.995 1.00 39.04  ? 539 VAL B N   1 
ATOM 7834 C CA  . VAL B 1 493 ? -52.060 15.783  146.132 1.00 34.28  ? 539 VAL B CA  1 
ATOM 7835 C C   . VAL B 1 493 ? -52.993 15.826  144.927 1.00 32.30  ? 539 VAL B C   1 
ATOM 7836 O O   . VAL B 1 493 ? -53.390 14.780  144.395 1.00 40.14  ? 539 VAL B O   1 
ATOM 7837 C CB  . VAL B 1 493 ? -52.818 16.007  147.452 1.00 38.15  ? 539 VAL B CB  1 
ATOM 7838 C CG1 . VAL B 1 493 ? -54.067 15.140  147.511 1.00 34.25  ? 539 VAL B CG1 1 
ATOM 7839 C CG2 . VAL B 1 493 ? -51.908 15.713  148.630 1.00 36.30  ? 539 VAL B CG2 1 
ATOM 7840 N N   . THR B 1 494 ? -53.358 17.030  144.473 1.00 33.28  ? 540 THR B N   1 
ATOM 7841 C CA  . THR B 1 494 ? -54.216 17.143  143.299 1.00 33.86  ? 540 THR B CA  1 
ATOM 7842 C C   . THR B 1 494 ? -53.569 16.499  142.079 1.00 28.50  ? 540 THR B C   1 
ATOM 7843 O O   . THR B 1 494 ? -54.246 15.820  141.298 1.00 29.69  ? 540 THR B O   1 
ATOM 7844 C CB  . THR B 1 494 ? -54.528 18.617  143.030 1.00 35.05  ? 540 THR B CB  1 
ATOM 7845 O OG1 . THR B 1 494 ? -55.123 19.204  144.193 1.00 35.28  ? 540 THR B OG1 1 
ATOM 7846 C CG2 . THR B 1 494 ? -55.495 18.758  141.878 1.00 32.61  ? 540 THR B CG2 1 
ATOM 7847 N N   . SER B 1 495 ? -52.259 16.679  141.914 1.00 31.78  ? 541 SER B N   1 
ATOM 7848 C CA  . SER B 1 495 ? -51.548 16.053  140.804 1.00 34.81  ? 541 SER B CA  1 
ATOM 7849 C C   . SER B 1 495 ? -51.461 14.541  140.988 1.00 40.89  ? 541 SER B C   1 
ATOM 7850 O O   . SER B 1 495 ? -51.499 13.778  140.012 1.00 46.19  ? 541 SER B O   1 
ATOM 7851 C CB  . SER B 1 495 ? -50.165 16.696  140.665 1.00 43.45  ? 541 SER B CB  1 
ATOM 7852 O OG  . SER B 1 495 ? -49.259 16.237  141.649 1.00 46.28  ? 541 SER B OG  1 
ATOM 7853 N N   . MET B 1 496 ? -51.367 14.095  142.241 1.00 48.90  ? 542 MET B N   1 
ATOM 7854 C CA  . MET B 1 496 ? -51.294 12.686  142.591 1.00 42.24  ? 542 MET B CA  1 
ATOM 7855 C C   . MET B 1 496 ? -52.577 11.932  142.269 1.00 38.92  ? 542 MET B C   1 
ATOM 7856 O O   . MET B 1 496 ? -52.508 10.793  141.794 1.00 42.32  ? 542 MET B O   1 
ATOM 7857 C CB  . MET B 1 496 ? -51.006 12.568  144.091 1.00 40.36  ? 542 MET B CB  1 
ATOM 7858 C CG  . MET B 1 496 ? -49.530 12.545  144.518 1.00 46.36  ? 542 MET B CG  1 
ATOM 7859 S SD  . MET B 1 496 ? -48.264 12.115  143.314 1.00 53.13  ? 542 MET B SD  1 
ATOM 7860 C CE  . MET B 1 496 ? -48.719 10.427  142.997 1.00 44.55  ? 542 MET B CE  1 
ATOM 7861 N N   . PHE B 1 497 ? -53.737 12.517  142.533 1.00 44.52  ? 543 PHE B N   1 
ATOM 7862 C CA  . PHE B 1 497 ? -54.993 11.789  142.355 1.00 36.28  ? 543 PHE B CA  1 
ATOM 7863 C C   . PHE B 1 497 ? -55.694 12.173  141.055 1.00 45.19  ? 543 PHE B C   1 
ATOM 7864 O O   . PHE B 1 497 ? -56.848 12.601  141.064 1.00 50.81  ? 543 PHE B O   1 
ATOM 7865 C CB  . PHE B 1 497 ? -55.892 12.031  143.554 1.00 35.06  ? 543 PHE B CB  1 
ATOM 7866 C CG  . PHE B 1 497 ? -55.597 11.142  144.725 1.00 37.98  ? 543 PHE B CG  1 
ATOM 7867 C CD1 . PHE B 1 497 ? -55.872 9.792   144.664 1.00 46.45  ? 543 PHE B CD1 1 
ATOM 7868 C CD2 . PHE B 1 497 ? -55.083 11.663  145.901 1.00 43.30  ? 543 PHE B CD2 1 
ATOM 7869 C CE1 . PHE B 1 497 ? -55.629 8.975   145.739 1.00 45.90  ? 543 PHE B CE1 1 
ATOM 7870 C CE2 . PHE B 1 497 ? -54.836 10.846  146.985 1.00 50.46  ? 543 PHE B CE2 1 
ATOM 7871 C CZ  . PHE B 1 497 ? -55.113 9.499   146.902 1.00 45.91  ? 543 PHE B CZ  1 
ATOM 7872 N N   . ASP B 1 498 ? -55.030 12.002  139.913 1.00 59.33  ? 544 ASP B N   1 
ATOM 7873 C CA  . ASP B 1 498 ? -55.515 12.521  138.640 1.00 57.45  ? 544 ASP B CA  1 
ATOM 7874 C C   . ASP B 1 498 ? -56.135 11.400  137.822 1.00 60.05  ? 544 ASP B C   1 
ATOM 7875 O O   . ASP B 1 498 ? -55.634 10.273  137.820 1.00 70.87  ? 544 ASP B O   1 
ATOM 7876 C CB  . ASP B 1 498 ? -54.389 13.182  137.846 1.00 61.29  ? 544 ASP B CB  1 
ATOM 7877 C CG  . ASP B 1 498 ? -54.880 14.342  137.001 1.00 65.68  ? 544 ASP B CG  1 
ATOM 7878 O OD1 . ASP B 1 498 ? -55.570 15.222  137.554 1.00 65.32  ? 544 ASP B OD1 1 
ATOM 7879 O OD2 . ASP B 1 498 ? -54.578 14.382  135.790 1.00 69.42  ? 544 ASP B OD2 1 
ATOM 7880 N N   . VAL B 1 499 ? -57.211 11.725  137.114 1.00 65.55  ? 545 VAL B N   1 
ATOM 7881 C CA  . VAL B 1 499 ? -57.971 10.761  136.323 1.00 66.91  ? 545 VAL B CA  1 
ATOM 7882 C C   . VAL B 1 499 ? -58.130 11.306  134.907 1.00 72.10  ? 545 VAL B C   1 
ATOM 7883 O O   . VAL B 1 499 ? -58.417 12.499  134.730 1.00 70.49  ? 545 VAL B O   1 
ATOM 7884 C CB  . VAL B 1 499 ? -59.330 10.477  136.983 1.00 66.88  ? 545 VAL B CB  1 
ATOM 7885 C CG1 . VAL B 1 499 ? -60.007 11.784  137.345 1.00 69.76  ? 545 VAL B CG1 1 
ATOM 7886 C CG2 . VAL B 1 499 ? -60.228 9.650   136.070 1.00 63.36  ? 545 VAL B CG2 1 
ATOM 7887 N N   . PRO B 1 500 ? -57.931 10.487  133.877 1.00 74.65  ? 546 PRO B N   1 
ATOM 7888 C CA  . PRO B 1 500 ? -58.105 10.971  132.505 1.00 72.60  ? 546 PRO B CA  1 
ATOM 7889 C C   . PRO B 1 500 ? -59.561 11.280  132.201 1.00 71.46  ? 546 PRO B C   1 
ATOM 7890 O O   . PRO B 1 500 ? -60.480 10.708  132.790 1.00 69.25  ? 546 PRO B O   1 
ATOM 7891 C CB  . PRO B 1 500 ? -57.597 9.804   131.652 1.00 70.46  ? 546 PRO B CB  1 
ATOM 7892 C CG  . PRO B 1 500 ? -57.808 8.608   132.512 1.00 71.87  ? 546 PRO B CG  1 
ATOM 7893 C CD  . PRO B 1 500 ? -57.542 9.068   133.915 1.00 72.33  ? 546 PRO B CD  1 
ATOM 7894 N N   . GLN B 1 501 ? -59.762 12.203  131.268 1.00 78.44  ? 547 GLN B N   1 
ATOM 7895 C CA  . GLN B 1 501 ? -61.108 12.570  130.847 1.00 80.50  ? 547 GLN B CA  1 
ATOM 7896 C C   . GLN B 1 501 ? -61.100 13.126  129.428 1.00 80.12  ? 547 GLN B C   1 
ATOM 7897 O O   . GLN B 1 501 ? -60.723 12.432  128.485 1.00 80.41  ? 547 GLN B O   1 
ATOM 7898 C CB  . GLN B 1 501 ? -61.717 13.591  131.810 1.00 78.07  ? 547 GLN B CB  1 
ATOM 7899 C CG  . GLN B 1 501 ? -63.164 13.979  131.510 1.00 78.46  ? 547 GLN B CG  1 
ATOM 7900 C CD  . GLN B 1 501 ? -64.052 12.789  131.174 1.00 81.88  ? 547 GLN B CD  1 
ATOM 7901 O OE1 . GLN B 1 501 ? -64.059 12.295  130.045 1.00 80.44  ? 547 GLN B OE1 1 
ATOM 7902 N NE2 . GLN B 1 501 ? -64.806 12.321  132.162 1.00 80.14  ? 547 GLN B NE2 1 
# 
