data_8PNS
# 
_entry.id   8PNS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   8PNS         pdb_00008pns 10.2210/pdb8pns/pdb 
WWPDB D_1292130036 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8PNS 
_pdbx_database_status.recvd_initial_deposition_date   2023-06-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              mw240@cam.ac.uk 
_pdbx_contact_author.name_first         Martin 
_pdbx_contact_author.name_last          Welch 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3646-1733 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, M.'  1 0000-0001-9286-8242 
'Brear, P.' 2 0000-0002-4045-0474 
'Welch, M.' 3 0000-0003-3646-1733 
# 
_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                     'Characterization of two acyl-CoA dehydrogenases from P. aeruginosa' 
_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 'Wang, M.'  1 0000-0001-9286-8242 
primary 'Brear, P.' 2 0000-0002-4045-0474 
primary 'Welch, M.' 3 0000-0003-3646-1733 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Acyl-CoA dehydrogenase'      65625.703 2   1.3.8.1 ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   2   ?       ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'       106.120   2   ?       ? ? ? 
4 non-polymer syn 'OCTANOYL-COENZYME A'         893.730   2   ?       ? ? ? 
5 water       nat water                         18.015    146 ?       ? ? ? 
# 
_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       
;GHMPDYKAPLRDIRFVRDELLGYEAHYQSLPGAEDATPDMVNAILEEGAKFCEQVIAPLNRVGDLEGCTWSADGVKTPTG
FKEAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGE
WTGTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEHDMADNIVHIVLARLPDAPQGTKGISLFIVPKFLPN
AEGNAGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYA
RERLQMRSLTGPKAPEKPADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIVQRSQDEEQKKAADSMLAFLTPIAK
AFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALDLLGRKVLMTQGEALKGFTKIVHKFCQAN
EANEAVKEFVAPLAQLNKEWGDLTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTGEEAFYK
AKLQTARFYFQRILPRTRAHVAAMLSGANNLMEMAEEDFALGY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GHMPDYKAPLRDIRFVRDELLGYEAHYQSLPGAEDATPDMVNAILEEGAKFCEQVIAPLNRVGDLEGCTWSADGVKTPTG
FKEAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGE
WTGTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEHDMADNIVHIVLARLPDAPQGTKGISLFIVPKFLPN
AEGNAGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYA
RERLQMRSLTGPKAPEKPADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIVQRSQDEEQKKAADSMLAFLTPIAK
AFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALDLLGRKVLMTQGEALKGFTKIVHKFCQAN
EANEAVKEFVAPLAQLNKEWGDLTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTGEEAFYK
AKLQTARFYFQRILPRTRAHVAAMLSGANNLMEMAEEDFALGY
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'DI(HYDROXYETHYL)ETHER'       PEG 
4 'OCTANOYL-COENZYME A'         CO8 
5 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   HIS n 
1 3   MET n 
1 4   PRO n 
1 5   ASP n 
1 6   TYR n 
1 7   LYS n 
1 8   ALA n 
1 9   PRO n 
1 10  LEU n 
1 11  ARG n 
1 12  ASP n 
1 13  ILE n 
1 14  ARG n 
1 15  PHE n 
1 16  VAL n 
1 17  ARG n 
1 18  ASP n 
1 19  GLU n 
1 20  LEU n 
1 21  LEU n 
1 22  GLY n 
1 23  TYR n 
1 24  GLU n 
1 25  ALA n 
1 26  HIS n 
1 27  TYR n 
1 28  GLN n 
1 29  SER n 
1 30  LEU n 
1 31  PRO n 
1 32  GLY n 
1 33  ALA n 
1 34  GLU n 
1 35  ASP n 
1 36  ALA n 
1 37  THR n 
1 38  PRO n 
1 39  ASP n 
1 40  MET n 
1 41  VAL n 
1 42  ASN n 
1 43  ALA n 
1 44  ILE n 
1 45  LEU n 
1 46  GLU n 
1 47  GLU n 
1 48  GLY n 
1 49  ALA n 
1 50  LYS n 
1 51  PHE n 
1 52  CYS n 
1 53  GLU n 
1 54  GLN n 
1 55  VAL n 
1 56  ILE n 
1 57  ALA n 
1 58  PRO n 
1 59  LEU n 
1 60  ASN n 
1 61  ARG n 
1 62  VAL n 
1 63  GLY n 
1 64  ASP n 
1 65  LEU n 
1 66  GLU n 
1 67  GLY n 
1 68  CYS n 
1 69  THR n 
1 70  TRP n 
1 71  SER n 
1 72  ALA n 
1 73  ASP n 
1 74  GLY n 
1 75  VAL n 
1 76  LYS n 
1 77  THR n 
1 78  PRO n 
1 79  THR n 
1 80  GLY n 
1 81  PHE n 
1 82  LYS n 
1 83  GLU n 
1 84  ALA n 
1 85  TYR n 
1 86  GLN n 
1 87  GLN n 
1 88  PHE n 
1 89  VAL n 
1 90  GLU n 
1 91  GLY n 
1 92  GLY n 
1 93  TRP n 
1 94  PRO n 
1 95  SER n 
1 96  LEU n 
1 97  ALA n 
1 98  HIS n 
1 99  ASP n 
1 100 VAL n 
1 101 GLU n 
1 102 HIS n 
1 103 GLY n 
1 104 GLY n 
1 105 GLN n 
1 106 GLY n 
1 107 LEU n 
1 108 PRO n 
1 109 GLU n 
1 110 SER n 
1 111 LEU n 
1 112 GLY n 
1 113 LEU n 
1 114 ALA n 
1 115 ILE n 
1 116 SER n 
1 117 GLU n 
1 118 MET n 
1 119 VAL n 
1 120 GLY n 
1 121 GLN n 
1 122 ALA n 
1 123 ASN n 
1 124 TRP n 
1 125 SER n 
1 126 TRP n 
1 127 GLY n 
1 128 MET n 
1 129 TYR n 
1 130 PRO n 
1 131 GLY n 
1 132 LEU n 
1 133 SER n 
1 134 HIS n 
1 135 GLY n 
1 136 ALA n 
1 137 MET n 
1 138 ASN n 
1 139 THR n 
1 140 LEU n 
1 141 HIS n 
1 142 ALA n 
1 143 HIS n 
1 144 GLY n 
1 145 THR n 
1 146 ALA n 
1 147 GLU n 
1 148 GLN n 
1 149 GLN n 
1 150 ALA n 
1 151 THR n 
1 152 TYR n 
1 153 LEU n 
1 154 THR n 
1 155 LYS n 
1 156 LEU n 
1 157 VAL n 
1 158 SER n 
1 159 GLY n 
1 160 GLU n 
1 161 TRP n 
1 162 THR n 
1 163 GLY n 
1 164 THR n 
1 165 MET n 
1 166 CYS n 
1 167 LEU n 
1 168 THR n 
1 169 GLU n 
1 170 PRO n 
1 171 HIS n 
1 172 CYS n 
1 173 GLY n 
1 174 THR n 
1 175 ASP n 
1 176 LEU n 
1 177 GLY n 
1 178 MET n 
1 179 LEU n 
1 180 ARG n 
1 181 THR n 
1 182 LYS n 
1 183 ALA n 
1 184 GLU n 
1 185 PRO n 
1 186 GLN n 
1 187 ALA n 
1 188 ASP n 
1 189 GLY n 
1 190 SER n 
1 191 TYR n 
1 192 LYS n 
1 193 VAL n 
1 194 THR n 
1 195 GLY n 
1 196 THR n 
1 197 LYS n 
1 198 ILE n 
1 199 PHE n 
1 200 ILE n 
1 201 SER n 
1 202 ALA n 
1 203 GLY n 
1 204 GLU n 
1 205 HIS n 
1 206 ASP n 
1 207 MET n 
1 208 ALA n 
1 209 ASP n 
1 210 ASN n 
1 211 ILE n 
1 212 VAL n 
1 213 HIS n 
1 214 ILE n 
1 215 VAL n 
1 216 LEU n 
1 217 ALA n 
1 218 ARG n 
1 219 LEU n 
1 220 PRO n 
1 221 ASP n 
1 222 ALA n 
1 223 PRO n 
1 224 GLN n 
1 225 GLY n 
1 226 THR n 
1 227 LYS n 
1 228 GLY n 
1 229 ILE n 
1 230 SER n 
1 231 LEU n 
1 232 PHE n 
1 233 ILE n 
1 234 VAL n 
1 235 PRO n 
1 236 LYS n 
1 237 PHE n 
1 238 LEU n 
1 239 PRO n 
1 240 ASN n 
1 241 ALA n 
1 242 GLU n 
1 243 GLY n 
1 244 ASN n 
1 245 ALA n 
1 246 GLY n 
1 247 GLU n 
1 248 ARG n 
1 249 ASN n 
1 250 ALA n 
1 251 VAL n 
1 252 SER n 
1 253 CYS n 
1 254 GLY n 
1 255 SER n 
1 256 ILE n 
1 257 GLU n 
1 258 HIS n 
1 259 LYS n 
1 260 MET n 
1 261 GLY n 
1 262 ILE n 
1 263 HIS n 
1 264 GLY n 
1 265 ASN n 
1 266 ALA n 
1 267 THR n 
1 268 CYS n 
1 269 VAL n 
1 270 MET n 
1 271 ASN n 
1 272 PHE n 
1 273 ASP n 
1 274 ALA n 
1 275 ALA n 
1 276 THR n 
1 277 GLY n 
1 278 PHE n 
1 279 LEU n 
1 280 ILE n 
1 281 GLY n 
1 282 PRO n 
1 283 PRO n 
1 284 ASN n 
1 285 LYS n 
1 286 GLY n 
1 287 LEU n 
1 288 ASN n 
1 289 CYS n 
1 290 MET n 
1 291 PHE n 
1 292 THR n 
1 293 PHE n 
1 294 MET n 
1 295 ASN n 
1 296 THR n 
1 297 ALA n 
1 298 ARG n 
1 299 LEU n 
1 300 GLY n 
1 301 THR n 
1 302 ALA n 
1 303 LEU n 
1 304 GLN n 
1 305 GLY n 
1 306 LEU n 
1 307 ALA n 
1 308 HIS n 
1 309 ALA n 
1 310 GLU n 
1 311 VAL n 
1 312 GLY n 
1 313 PHE n 
1 314 GLN n 
1 315 GLY n 
1 316 GLY n 
1 317 ILE n 
1 318 ALA n 
1 319 TYR n 
1 320 ALA n 
1 321 ARG n 
1 322 GLU n 
1 323 ARG n 
1 324 LEU n 
1 325 GLN n 
1 326 MET n 
1 327 ARG n 
1 328 SER n 
1 329 LEU n 
1 330 THR n 
1 331 GLY n 
1 332 PRO n 
1 333 LYS n 
1 334 ALA n 
1 335 PRO n 
1 336 GLU n 
1 337 LYS n 
1 338 PRO n 
1 339 ALA n 
1 340 ASP n 
1 341 PRO n 
1 342 ILE n 
1 343 ILE n 
1 344 VAL n 
1 345 HIS n 
1 346 PRO n 
1 347 ASP n 
1 348 VAL n 
1 349 ARG n 
1 350 ARG n 
1 351 MET n 
1 352 LEU n 
1 353 LEU n 
1 354 THR n 
1 355 MET n 
1 356 LYS n 
1 357 ALA n 
1 358 PHE n 
1 359 ALA n 
1 360 GLU n 
1 361 GLY n 
1 362 ASN n 
1 363 ARG n 
1 364 ALA n 
1 365 MET n 
1 366 LEU n 
1 367 TYR n 
1 368 PHE n 
1 369 ALA n 
1 370 ALA n 
1 371 LYS n 
1 372 GLN n 
1 373 VAL n 
1 374 ASP n 
1 375 ILE n 
1 376 VAL n 
1 377 GLN n 
1 378 ARG n 
1 379 SER n 
1 380 GLN n 
1 381 ASP n 
1 382 GLU n 
1 383 GLU n 
1 384 GLN n 
1 385 LYS n 
1 386 LYS n 
1 387 ALA n 
1 388 ALA n 
1 389 ASP n 
1 390 SER n 
1 391 MET n 
1 392 LEU n 
1 393 ALA n 
1 394 PHE n 
1 395 LEU n 
1 396 THR n 
1 397 PRO n 
1 398 ILE n 
1 399 ALA n 
1 400 LYS n 
1 401 ALA n 
1 402 PHE n 
1 403 MET n 
1 404 THR n 
1 405 GLU n 
1 406 VAL n 
1 407 GLY n 
1 408 PHE n 
1 409 GLU n 
1 410 SER n 
1 411 ALA n 
1 412 ASN n 
1 413 HIS n 
1 414 GLY n 
1 415 VAL n 
1 416 GLN n 
1 417 ILE n 
1 418 PHE n 
1 419 GLY n 
1 420 GLY n 
1 421 HIS n 
1 422 GLY n 
1 423 PHE n 
1 424 ILE n 
1 425 ALA n 
1 426 GLU n 
1 427 HIS n 
1 428 GLY n 
1 429 MET n 
1 430 GLU n 
1 431 GLN n 
1 432 ASN n 
1 433 VAL n 
1 434 ARG n 
1 435 ASP n 
1 436 SER n 
1 437 ARG n 
1 438 ILE n 
1 439 SER n 
1 440 MET n 
1 441 LEU n 
1 442 TYR n 
1 443 GLU n 
1 444 GLY n 
1 445 THR n 
1 446 THR n 
1 447 GLY n 
1 448 VAL n 
1 449 GLN n 
1 450 ALA n 
1 451 LEU n 
1 452 ASP n 
1 453 LEU n 
1 454 LEU n 
1 455 GLY n 
1 456 ARG n 
1 457 LYS n 
1 458 VAL n 
1 459 LEU n 
1 460 MET n 
1 461 THR n 
1 462 GLN n 
1 463 GLY n 
1 464 GLU n 
1 465 ALA n 
1 466 LEU n 
1 467 LYS n 
1 468 GLY n 
1 469 PHE n 
1 470 THR n 
1 471 LYS n 
1 472 ILE n 
1 473 VAL n 
1 474 HIS n 
1 475 LYS n 
1 476 PHE n 
1 477 CYS n 
1 478 GLN n 
1 479 ALA n 
1 480 ASN n 
1 481 GLU n 
1 482 ALA n 
1 483 ASN n 
1 484 GLU n 
1 485 ALA n 
1 486 VAL n 
1 487 LYS n 
1 488 GLU n 
1 489 PHE n 
1 490 VAL n 
1 491 ALA n 
1 492 PRO n 
1 493 LEU n 
1 494 ALA n 
1 495 GLN n 
1 496 LEU n 
1 497 ASN n 
1 498 LYS n 
1 499 GLU n 
1 500 TRP n 
1 501 GLY n 
1 502 ASP n 
1 503 LEU n 
1 504 THR n 
1 505 MET n 
1 506 LYS n 
1 507 VAL n 
1 508 GLY n 
1 509 MET n 
1 510 ALA n 
1 511 ALA n 
1 512 MET n 
1 513 LYS n 
1 514 ASP n 
1 515 ARG n 
1 516 GLU n 
1 517 GLU n 
1 518 VAL n 
1 519 GLY n 
1 520 ALA n 
1 521 ALA n 
1 522 SER n 
1 523 VAL n 
1 524 ASP n 
1 525 TYR n 
1 526 LEU n 
1 527 MET n 
1 528 TYR n 
1 529 SER n 
1 530 GLY n 
1 531 TYR n 
1 532 ALA n 
1 533 CYS n 
1 534 LEU n 
1 535 ALA n 
1 536 TYR n 
1 537 PHE n 
1 538 TRP n 
1 539 ALA n 
1 540 ASP n 
1 541 MET n 
1 542 ALA n 
1 543 ARG n 
1 544 LEU n 
1 545 ALA n 
1 546 ALA n 
1 547 GLU n 
1 548 LYS n 
1 549 LEU n 
1 550 ALA n 
1 551 ALA n 
1 552 GLY n 
1 553 THR n 
1 554 GLY n 
1 555 GLU n 
1 556 GLU n 
1 557 ALA n 
1 558 PHE n 
1 559 TYR n 
1 560 LYS n 
1 561 ALA n 
1 562 LYS n 
1 563 LEU n 
1 564 GLN n 
1 565 THR n 
1 566 ALA n 
1 567 ARG n 
1 568 PHE n 
1 569 TYR n 
1 570 PHE n 
1 571 GLN n 
1 572 ARG n 
1 573 ILE n 
1 574 LEU n 
1 575 PRO n 
1 576 ARG n 
1 577 THR n 
1 578 ARG n 
1 579 ALA n 
1 580 HIS n 
1 581 VAL n 
1 582 ALA n 
1 583 ALA n 
1 584 MET n 
1 585 LEU n 
1 586 SER n 
1 587 GLY n 
1 588 ALA n 
1 589 ASN n 
1 590 ASN n 
1 591 LEU n 
1 592 MET n 
1 593 GLU n 
1 594 MET n 
1 595 ALA n 
1 596 GLU n 
1 597 GLU n 
1 598 ASP n 
1 599 PHE n 
1 600 ALA n 
1 601 LEU n 
1 602 GLY n 
1 603 TYR 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                   603 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 
'mmgC10, ALP65_01436, CAZ10_18495, CGU42_20105, GNQ48_07395, GUL26_18035, NCTC13621_06274, PA52Ts2_5823' 
_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      'Pseudomonas aeruginosa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     287 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
CO8 non-polymer         . 'OCTANOYL-COENZYME A'         ? 'C29 H50 N7 O17 P3 S' 893.730 
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'        121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2'   785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                         ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'       149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'       ? 'C4 H10 O3'           106.120 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'         117.146 
# 
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   GLY 1   -1  ?   ?   ?   A . n 
A 1 2   HIS 2   0   ?   ?   ?   A . n 
A 1 3   MET 3   1   ?   ?   ?   A . n 
A 1 4   PRO 4   2   2   PRO PRO A . n 
A 1 5   ASP 5   3   3   ASP ASP A . n 
A 1 6   TYR 6   4   4   TYR TYR A . n 
A 1 7   LYS 7   5   5   LYS LYS A . n 
A 1 8   ALA 8   6   6   ALA ALA A . n 
A 1 9   PRO 9   7   7   PRO PRO A . n 
A 1 10  LEU 10  8   8   LEU LEU A . n 
A 1 11  ARG 11  9   9   ARG ARG A . n 
A 1 12  ASP 12  10  10  ASP ASP A . n 
A 1 13  ILE 13  11  11  ILE ILE A . n 
A 1 14  ARG 14  12  12  ARG ARG A . n 
A 1 15  PHE 15  13  13  PHE PHE A . n 
A 1 16  VAL 16  14  14  VAL VAL A . n 
A 1 17  ARG 17  15  15  ARG ARG A . n 
A 1 18  ASP 18  16  16  ASP ASP A . n 
A 1 19  GLU 19  17  17  GLU GLU A . n 
A 1 20  LEU 20  18  18  LEU LEU A . n 
A 1 21  LEU 21  19  19  LEU LEU A . n 
A 1 22  GLY 22  20  20  GLY GLY A . n 
A 1 23  TYR 23  21  21  TYR TYR A . n 
A 1 24  GLU 24  22  22  GLU GLU A . n 
A 1 25  ALA 25  23  23  ALA ALA A . n 
A 1 26  HIS 26  24  24  HIS HIS A . n 
A 1 27  TYR 27  25  25  TYR TYR A . n 
A 1 28  GLN 28  26  26  GLN GLN A . n 
A 1 29  SER 29  27  27  SER SER A . n 
A 1 30  LEU 30  28  28  LEU LEU A . n 
A 1 31  PRO 31  29  29  PRO PRO A . n 
A 1 32  GLY 32  30  30  GLY GLY A . n 
A 1 33  ALA 33  31  31  ALA ALA A . n 
A 1 34  GLU 34  32  32  GLU GLU A . n 
A 1 35  ASP 35  33  33  ASP ASP A . n 
A 1 36  ALA 36  34  34  ALA ALA A . n 
A 1 37  THR 37  35  35  THR THR A . n 
A 1 38  PRO 38  36  36  PRO PRO A . n 
A 1 39  ASP 39  37  37  ASP ASP A . n 
A 1 40  MET 40  38  38  MET MET A . n 
A 1 41  VAL 41  39  39  VAL VAL A . n 
A 1 42  ASN 42  40  40  ASN ASN A . n 
A 1 43  ALA 43  41  41  ALA ALA A . n 
A 1 44  ILE 44  42  42  ILE ILE A . n 
A 1 45  LEU 45  43  43  LEU LEU A . n 
A 1 46  GLU 46  44  44  GLU GLU A . n 
A 1 47  GLU 47  45  45  GLU GLU A . n 
A 1 48  GLY 48  46  46  GLY GLY A . n 
A 1 49  ALA 49  47  47  ALA ALA A . n 
A 1 50  LYS 50  48  48  LYS LYS A . n 
A 1 51  PHE 51  49  49  PHE PHE A . n 
A 1 52  CYS 52  50  50  CYS CYS A . n 
A 1 53  GLU 53  51  51  GLU GLU A . n 
A 1 54  GLN 54  52  52  GLN GLN A . n 
A 1 55  VAL 55  53  53  VAL VAL A . n 
A 1 56  ILE 56  54  54  ILE ILE A . n 
A 1 57  ALA 57  55  55  ALA ALA A . n 
A 1 58  PRO 58  56  56  PRO PRO A . n 
A 1 59  LEU 59  57  57  LEU LEU A . n 
A 1 60  ASN 60  58  58  ASN ASN A . n 
A 1 61  ARG 61  59  59  ARG ARG A . n 
A 1 62  VAL 62  60  60  VAL VAL A . n 
A 1 63  GLY 63  61  61  GLY GLY A . n 
A 1 64  ASP 64  62  62  ASP ASP A . n 
A 1 65  LEU 65  63  63  LEU LEU A . n 
A 1 66  GLU 66  64  64  GLU GLU A . n 
A 1 67  GLY 67  65  65  GLY GLY A . n 
A 1 68  CYS 68  66  66  CYS CYS A . n 
A 1 69  THR 69  67  67  THR THR A . n 
A 1 70  TRP 70  68  68  TRP TRP A . n 
A 1 71  SER 71  69  69  SER SER A . n 
A 1 72  ALA 72  70  70  ALA ALA A . n 
A 1 73  ASP 73  71  71  ASP ASP A . n 
A 1 74  GLY 74  72  72  GLY GLY A . n 
A 1 75  VAL 75  73  73  VAL VAL A . n 
A 1 76  LYS 76  74  74  LYS LYS A . n 
A 1 77  THR 77  75  75  THR THR A . n 
A 1 78  PRO 78  76  76  PRO PRO A . n 
A 1 79  THR 79  77  77  THR THR A . n 
A 1 80  GLY 80  78  78  GLY GLY A . n 
A 1 81  PHE 81  79  79  PHE PHE A . n 
A 1 82  LYS 82  80  80  LYS LYS A . n 
A 1 83  GLU 83  81  81  GLU GLU A . n 
A 1 84  ALA 84  82  82  ALA ALA A . n 
A 1 85  TYR 85  83  83  TYR TYR A . n 
A 1 86  GLN 86  84  84  GLN GLN A . n 
A 1 87  GLN 87  85  85  GLN GLN A . n 
A 1 88  PHE 88  86  86  PHE PHE A . n 
A 1 89  VAL 89  87  87  VAL VAL A . n 
A 1 90  GLU 90  88  88  GLU GLU A . n 
A 1 91  GLY 91  89  89  GLY GLY A . n 
A 1 92  GLY 92  90  90  GLY GLY A . n 
A 1 93  TRP 93  91  91  TRP TRP A . n 
A 1 94  PRO 94  92  92  PRO PRO A . n 
A 1 95  SER 95  93  93  SER SER A . n 
A 1 96  LEU 96  94  94  LEU LEU A . n 
A 1 97  ALA 97  95  95  ALA ALA A . n 
A 1 98  HIS 98  96  96  HIS HIS A . n 
A 1 99  ASP 99  97  97  ASP ASP A . n 
A 1 100 VAL 100 98  98  VAL VAL A . n 
A 1 101 GLU 101 99  99  GLU GLU A . n 
A 1 102 HIS 102 100 100 HIS HIS A . n 
A 1 103 GLY 103 101 101 GLY GLY A . n 
A 1 104 GLY 104 102 102 GLY GLY A . n 
A 1 105 GLN 105 103 103 GLN GLN A . n 
A 1 106 GLY 106 104 104 GLY GLY A . n 
A 1 107 LEU 107 105 105 LEU LEU A . n 
A 1 108 PRO 108 106 106 PRO PRO A . n 
A 1 109 GLU 109 107 107 GLU GLU A . n 
A 1 110 SER 110 108 108 SER SER A . n 
A 1 111 LEU 111 109 109 LEU LEU A . n 
A 1 112 GLY 112 110 110 GLY GLY A . n 
A 1 113 LEU 113 111 111 LEU LEU A . n 
A 1 114 ALA 114 112 112 ALA ALA A . n 
A 1 115 ILE 115 113 113 ILE ILE A . n 
A 1 116 SER 116 114 114 SER SER A . n 
A 1 117 GLU 117 115 115 GLU GLU A . n 
A 1 118 MET 118 116 116 MET MET A . n 
A 1 119 VAL 119 117 117 VAL VAL A . n 
A 1 120 GLY 120 118 118 GLY GLY A . n 
A 1 121 GLN 121 119 119 GLN GLN A . n 
A 1 122 ALA 122 120 120 ALA ALA A . n 
A 1 123 ASN 123 121 121 ASN ASN A . n 
A 1 124 TRP 124 122 122 TRP TRP A . n 
A 1 125 SER 125 123 123 SER SER A . n 
A 1 126 TRP 126 124 124 TRP TRP A . n 
A 1 127 GLY 127 125 125 GLY GLY A . n 
A 1 128 MET 128 126 126 MET MET A . n 
A 1 129 TYR 129 127 127 TYR TYR A . n 
A 1 130 PRO 130 128 128 PRO PRO A . n 
A 1 131 GLY 131 129 129 GLY GLY A . n 
A 1 132 LEU 132 130 130 LEU LEU A . n 
A 1 133 SER 133 131 131 SER SER A . n 
A 1 134 HIS 134 132 132 HIS HIS A . n 
A 1 135 GLY 135 133 133 GLY GLY A . n 
A 1 136 ALA 136 134 134 ALA ALA A . n 
A 1 137 MET 137 135 135 MET MET A . n 
A 1 138 ASN 138 136 136 ASN ASN A . n 
A 1 139 THR 139 137 137 THR THR A . n 
A 1 140 LEU 140 138 138 LEU LEU A . n 
A 1 141 HIS 141 139 139 HIS HIS A . n 
A 1 142 ALA 142 140 140 ALA ALA A . n 
A 1 143 HIS 143 141 141 HIS HIS A . n 
A 1 144 GLY 144 142 142 GLY GLY A . n 
A 1 145 THR 145 143 143 THR THR A . n 
A 1 146 ALA 146 144 144 ALA ALA A . n 
A 1 147 GLU 147 145 145 GLU GLU A . n 
A 1 148 GLN 148 146 146 GLN GLN A . n 
A 1 149 GLN 149 147 147 GLN GLN A . n 
A 1 150 ALA 150 148 148 ALA ALA A . n 
A 1 151 THR 151 149 149 THR THR A . n 
A 1 152 TYR 152 150 150 TYR TYR A . n 
A 1 153 LEU 153 151 151 LEU LEU A . n 
A 1 154 THR 154 152 152 THR THR A . n 
A 1 155 LYS 155 153 153 LYS LYS A . n 
A 1 156 LEU 156 154 154 LEU LEU A . n 
A 1 157 VAL 157 155 155 VAL VAL A . n 
A 1 158 SER 158 156 156 SER SER A . n 
A 1 159 GLY 159 157 157 GLY GLY A . n 
A 1 160 GLU 160 158 158 GLU GLU A . n 
A 1 161 TRP 161 159 159 TRP TRP A . n 
A 1 162 THR 162 160 160 THR THR A . n 
A 1 163 GLY 163 161 161 GLY GLY A . n 
A 1 164 THR 164 162 162 THR THR A . n 
A 1 165 MET 165 163 163 MET MET A . n 
A 1 166 CYS 166 164 164 CYS CYS A . n 
A 1 167 LEU 167 165 165 LEU LEU A . n 
A 1 168 THR 168 166 166 THR THR A . n 
A 1 169 GLU 169 167 167 GLU GLU A . n 
A 1 170 PRO 170 168 168 PRO PRO A . n 
A 1 171 HIS 171 169 169 HIS HIS A . n 
A 1 172 CYS 172 170 170 CYS CYS A . n 
A 1 173 GLY 173 171 171 GLY GLY A . n 
A 1 174 THR 174 172 172 THR THR A . n 
A 1 175 ASP 175 173 173 ASP ASP A . n 
A 1 176 LEU 176 174 174 LEU LEU A . n 
A 1 177 GLY 177 175 175 GLY GLY A . n 
A 1 178 MET 178 176 176 MET MET A . n 
A 1 179 LEU 179 177 177 LEU LEU A . n 
A 1 180 ARG 180 178 178 ARG ARG A . n 
A 1 181 THR 181 179 179 THR THR A . n 
A 1 182 LYS 182 180 180 LYS LYS A . n 
A 1 183 ALA 183 181 181 ALA ALA A . n 
A 1 184 GLU 184 182 182 GLU GLU A . n 
A 1 185 PRO 185 183 183 PRO PRO A . n 
A 1 186 GLN 186 184 184 GLN GLN A . n 
A 1 187 ALA 187 185 185 ALA ALA A . n 
A 1 188 ASP 188 186 186 ASP ASP A . n 
A 1 189 GLY 189 187 187 GLY GLY A . n 
A 1 190 SER 190 188 188 SER SER A . n 
A 1 191 TYR 191 189 189 TYR TYR A . n 
A 1 192 LYS 192 190 190 LYS LYS A . n 
A 1 193 VAL 193 191 191 VAL VAL A . n 
A 1 194 THR 194 192 192 THR THR A . n 
A 1 195 GLY 195 193 193 GLY GLY A . n 
A 1 196 THR 196 194 194 THR THR A . n 
A 1 197 LYS 197 195 195 LYS LYS A . n 
A 1 198 ILE 198 196 196 ILE ILE A . n 
A 1 199 PHE 199 197 197 PHE PHE A . n 
A 1 200 ILE 200 198 198 ILE ILE A . n 
A 1 201 SER 201 199 199 SER SER A . n 
A 1 202 ALA 202 200 200 ALA ALA A . n 
A 1 203 GLY 203 201 201 GLY GLY A . n 
A 1 204 GLU 204 202 202 GLU GLU A . n 
A 1 205 HIS 205 203 203 HIS HIS A . n 
A 1 206 ASP 206 204 204 ASP ASP A . n 
A 1 207 MET 207 205 205 MET MET A . n 
A 1 208 ALA 208 206 206 ALA ALA A . n 
A 1 209 ASP 209 207 207 ASP ASP A . n 
A 1 210 ASN 210 208 208 ASN ASN A . n 
A 1 211 ILE 211 209 209 ILE ILE A . n 
A 1 212 VAL 212 210 210 VAL VAL A . n 
A 1 213 HIS 213 211 211 HIS HIS A . n 
A 1 214 ILE 214 212 212 ILE ILE A . n 
A 1 215 VAL 215 213 213 VAL VAL A . n 
A 1 216 LEU 216 214 214 LEU LEU A . n 
A 1 217 ALA 217 215 215 ALA ALA A . n 
A 1 218 ARG 218 216 216 ARG ARG A . n 
A 1 219 LEU 219 217 217 LEU LEU A . n 
A 1 220 PRO 220 218 218 PRO PRO A . n 
A 1 221 ASP 221 219 219 ASP ASP A . n 
A 1 222 ALA 222 220 220 ALA ALA A . n 
A 1 223 PRO 223 221 221 PRO PRO A . n 
A 1 224 GLN 224 222 222 GLN GLN A . n 
A 1 225 GLY 225 223 223 GLY GLY A . n 
A 1 226 THR 226 224 224 THR THR A . n 
A 1 227 LYS 227 225 225 LYS LYS A . n 
A 1 228 GLY 228 226 226 GLY GLY A . n 
A 1 229 ILE 229 227 227 ILE ILE A . n 
A 1 230 SER 230 228 228 SER SER A . n 
A 1 231 LEU 231 229 229 LEU LEU A . n 
A 1 232 PHE 232 230 230 PHE PHE A . n 
A 1 233 ILE 233 231 231 ILE ILE A . n 
A 1 234 VAL 234 232 232 VAL VAL A . n 
A 1 235 PRO 235 233 233 PRO PRO A . n 
A 1 236 LYS 236 234 234 LYS LYS A . n 
A 1 237 PHE 237 235 235 PHE PHE A . n 
A 1 238 LEU 238 236 236 LEU LEU A . n 
A 1 239 PRO 239 237 237 PRO PRO A . n 
A 1 240 ASN 240 238 238 ASN ASN A . n 
A 1 241 ALA 241 239 239 ALA ALA A . n 
A 1 242 GLU 242 240 240 GLU GLU A . n 
A 1 243 GLY 243 241 241 GLY GLY A . n 
A 1 244 ASN 244 242 242 ASN ASN A . n 
A 1 245 ALA 245 243 243 ALA ALA A . n 
A 1 246 GLY 246 244 244 GLY GLY A . n 
A 1 247 GLU 247 245 245 GLU GLU A . n 
A 1 248 ARG 248 246 246 ARG ARG A . n 
A 1 249 ASN 249 247 247 ASN ASN A . n 
A 1 250 ALA 250 248 248 ALA ALA A . n 
A 1 251 VAL 251 249 249 VAL VAL A . n 
A 1 252 SER 252 250 250 SER SER A . n 
A 1 253 CYS 253 251 251 CYS CYS A . n 
A 1 254 GLY 254 252 252 GLY GLY A . n 
A 1 255 SER 255 253 253 SER SER A . n 
A 1 256 ILE 256 254 254 ILE ILE A . n 
A 1 257 GLU 257 255 255 GLU GLU A . n 
A 1 258 HIS 258 256 256 HIS HIS A . n 
A 1 259 LYS 259 257 257 LYS LYS A . n 
A 1 260 MET 260 258 258 MET MET A . n 
A 1 261 GLY 261 259 259 GLY GLY A . n 
A 1 262 ILE 262 260 260 ILE ILE A . n 
A 1 263 HIS 263 261 261 HIS HIS A . n 
A 1 264 GLY 264 262 262 GLY GLY A . n 
A 1 265 ASN 265 263 263 ASN ASN A . n 
A 1 266 ALA 266 264 264 ALA ALA A . n 
A 1 267 THR 267 265 265 THR THR A . n 
A 1 268 CYS 268 266 266 CYS CYS A . n 
A 1 269 VAL 269 267 267 VAL VAL A . n 
A 1 270 MET 270 268 268 MET MET A . n 
A 1 271 ASN 271 269 269 ASN ASN A . n 
A 1 272 PHE 272 270 270 PHE PHE A . n 
A 1 273 ASP 273 271 271 ASP ASP A . n 
A 1 274 ALA 274 272 272 ALA ALA A . n 
A 1 275 ALA 275 273 273 ALA ALA A . n 
A 1 276 THR 276 274 274 THR THR A . n 
A 1 277 GLY 277 275 275 GLY GLY A . n 
A 1 278 PHE 278 276 276 PHE PHE A . n 
A 1 279 LEU 279 277 277 LEU LEU A . n 
A 1 280 ILE 280 278 278 ILE ILE A . n 
A 1 281 GLY 281 279 279 GLY GLY A . n 
A 1 282 PRO 282 280 280 PRO PRO A . n 
A 1 283 PRO 283 281 281 PRO PRO A . n 
A 1 284 ASN 284 282 282 ASN ASN A . n 
A 1 285 LYS 285 283 283 LYS LYS A . n 
A 1 286 GLY 286 284 284 GLY GLY A . n 
A 1 287 LEU 287 285 285 LEU LEU A . n 
A 1 288 ASN 288 286 286 ASN ASN A . n 
A 1 289 CYS 289 287 287 CYS CYS A . n 
A 1 290 MET 290 288 288 MET MET A . n 
A 1 291 PHE 291 289 289 PHE PHE A . n 
A 1 292 THR 292 290 290 THR THR A . n 
A 1 293 PHE 293 291 291 PHE PHE A . n 
A 1 294 MET 294 292 292 MET MET A . n 
A 1 295 ASN 295 293 293 ASN ASN A . n 
A 1 296 THR 296 294 294 THR THR A . n 
A 1 297 ALA 297 295 295 ALA ALA A . n 
A 1 298 ARG 298 296 296 ARG ARG A . n 
A 1 299 LEU 299 297 297 LEU LEU A . n 
A 1 300 GLY 300 298 298 GLY GLY A . n 
A 1 301 THR 301 299 299 THR THR A . n 
A 1 302 ALA 302 300 300 ALA ALA A . n 
A 1 303 LEU 303 301 301 LEU LEU A . n 
A 1 304 GLN 304 302 302 GLN GLN A . n 
A 1 305 GLY 305 303 303 GLY GLY A . n 
A 1 306 LEU 306 304 304 LEU LEU A . n 
A 1 307 ALA 307 305 305 ALA ALA A . n 
A 1 308 HIS 308 306 306 HIS HIS A . n 
A 1 309 ALA 309 307 307 ALA ALA A . n 
A 1 310 GLU 310 308 308 GLU GLU A . n 
A 1 311 VAL 311 309 309 VAL VAL A . n 
A 1 312 GLY 312 310 310 GLY GLY A . n 
A 1 313 PHE 313 311 311 PHE PHE A . n 
A 1 314 GLN 314 312 312 GLN GLN A . n 
A 1 315 GLY 315 313 313 GLY GLY A . n 
A 1 316 GLY 316 314 314 GLY GLY A . n 
A 1 317 ILE 317 315 315 ILE ILE A . n 
A 1 318 ALA 318 316 316 ALA ALA A . n 
A 1 319 TYR 319 317 317 TYR TYR A . n 
A 1 320 ALA 320 318 318 ALA ALA A . n 
A 1 321 ARG 321 319 319 ARG ARG A . n 
A 1 322 GLU 322 320 320 GLU GLU A . n 
A 1 323 ARG 323 321 321 ARG ARG A . n 
A 1 324 LEU 324 322 322 LEU LEU A . n 
A 1 325 GLN 325 323 323 GLN GLN A . n 
A 1 326 MET 326 324 324 MET MET A . n 
A 1 327 ARG 327 325 325 ARG ARG A . n 
A 1 328 SER 328 326 326 SER SER A . n 
A 1 329 LEU 329 327 327 LEU LEU A . n 
A 1 330 THR 330 328 328 THR THR A . n 
A 1 331 GLY 331 329 329 GLY GLY A . n 
A 1 332 PRO 332 330 330 PRO PRO A . n 
A 1 333 LYS 333 331 331 LYS LYS A . n 
A 1 334 ALA 334 332 332 ALA ALA A . n 
A 1 335 PRO 335 333 333 PRO PRO A . n 
A 1 336 GLU 336 334 334 GLU GLU A . n 
A 1 337 LYS 337 335 335 LYS LYS A . n 
A 1 338 PRO 338 336 336 PRO PRO A . n 
A 1 339 ALA 339 337 337 ALA ALA A . n 
A 1 340 ASP 340 338 338 ASP ASP A . n 
A 1 341 PRO 341 339 339 PRO PRO A . n 
A 1 342 ILE 342 340 340 ILE ILE A . n 
A 1 343 ILE 343 341 341 ILE ILE A . n 
A 1 344 VAL 344 342 342 VAL VAL A . n 
A 1 345 HIS 345 343 343 HIS HIS A . n 
A 1 346 PRO 346 344 344 PRO PRO A . n 
A 1 347 ASP 347 345 345 ASP ASP A . n 
A 1 348 VAL 348 346 346 VAL VAL A . n 
A 1 349 ARG 349 347 347 ARG ARG A . n 
A 1 350 ARG 350 348 348 ARG ARG A . n 
A 1 351 MET 351 349 349 MET MET A . n 
A 1 352 LEU 352 350 350 LEU LEU A . n 
A 1 353 LEU 353 351 351 LEU LEU A . n 
A 1 354 THR 354 352 352 THR THR A . n 
A 1 355 MET 355 353 353 MET MET A . n 
A 1 356 LYS 356 354 354 LYS LYS A . n 
A 1 357 ALA 357 355 355 ALA ALA A . n 
A 1 358 PHE 358 356 356 PHE PHE A . n 
A 1 359 ALA 359 357 357 ALA ALA A . n 
A 1 360 GLU 360 358 358 GLU GLU A . n 
A 1 361 GLY 361 359 359 GLY GLY A . n 
A 1 362 ASN 362 360 360 ASN ASN A . n 
A 1 363 ARG 363 361 361 ARG ARG A . n 
A 1 364 ALA 364 362 362 ALA ALA A . n 
A 1 365 MET 365 363 363 MET MET A . n 
A 1 366 LEU 366 364 364 LEU LEU A . n 
A 1 367 TYR 367 365 365 TYR TYR A . n 
A 1 368 PHE 368 366 366 PHE PHE A . n 
A 1 369 ALA 369 367 367 ALA ALA A . n 
A 1 370 ALA 370 368 368 ALA ALA A . n 
A 1 371 LYS 371 369 369 LYS LYS A . n 
A 1 372 GLN 372 370 370 GLN GLN A . n 
A 1 373 VAL 373 371 371 VAL VAL A . n 
A 1 374 ASP 374 372 372 ASP ASP A . n 
A 1 375 ILE 375 373 373 ILE ILE A . n 
A 1 376 VAL 376 374 374 VAL VAL A . n 
A 1 377 GLN 377 375 375 GLN GLN A . n 
A 1 378 ARG 378 376 376 ARG ARG A . n 
A 1 379 SER 379 377 377 SER SER A . n 
A 1 380 GLN 380 378 378 GLN GLN A . n 
A 1 381 ASP 381 379 379 ASP ASP A . n 
A 1 382 GLU 382 380 380 GLU GLU A . n 
A 1 383 GLU 383 381 381 GLU GLU A . n 
A 1 384 GLN 384 382 382 GLN GLN A . n 
A 1 385 LYS 385 383 383 LYS LYS A . n 
A 1 386 LYS 386 384 384 LYS LYS A . n 
A 1 387 ALA 387 385 385 ALA ALA A . n 
A 1 388 ALA 388 386 386 ALA ALA A . n 
A 1 389 ASP 389 387 387 ASP ASP A . n 
A 1 390 SER 390 388 388 SER SER A . n 
A 1 391 MET 391 389 389 MET MET A . n 
A 1 392 LEU 392 390 390 LEU LEU A . n 
A 1 393 ALA 393 391 391 ALA ALA A . n 
A 1 394 PHE 394 392 392 PHE PHE A . n 
A 1 395 LEU 395 393 393 LEU LEU A . n 
A 1 396 THR 396 394 394 THR THR A . n 
A 1 397 PRO 397 395 395 PRO PRO A . n 
A 1 398 ILE 398 396 396 ILE ILE A . n 
A 1 399 ALA 399 397 397 ALA ALA A . n 
A 1 400 LYS 400 398 398 LYS LYS A . n 
A 1 401 ALA 401 399 399 ALA ALA A . n 
A 1 402 PHE 402 400 400 PHE PHE A . n 
A 1 403 MET 403 401 401 MET MET A . n 
A 1 404 THR 404 402 402 THR THR A . n 
A 1 405 GLU 405 403 403 GLU GLU A . n 
A 1 406 VAL 406 404 404 VAL VAL A . n 
A 1 407 GLY 407 405 405 GLY GLY A . n 
A 1 408 PHE 408 406 406 PHE PHE A . n 
A 1 409 GLU 409 407 407 GLU GLU A . n 
A 1 410 SER 410 408 408 SER SER A . n 
A 1 411 ALA 411 409 409 ALA ALA A . n 
A 1 412 ASN 412 410 410 ASN ASN A . n 
A 1 413 HIS 413 411 411 HIS HIS A . n 
A 1 414 GLY 414 412 412 GLY GLY A . n 
A 1 415 VAL 415 413 413 VAL VAL A . n 
A 1 416 GLN 416 414 414 GLN GLN A . n 
A 1 417 ILE 417 415 415 ILE ILE A . n 
A 1 418 PHE 418 416 416 PHE PHE A . n 
A 1 419 GLY 419 417 417 GLY GLY A . n 
A 1 420 GLY 420 418 418 GLY GLY A . n 
A 1 421 HIS 421 419 419 HIS HIS A . n 
A 1 422 GLY 422 420 420 GLY GLY A . n 
A 1 423 PHE 423 421 421 PHE PHE A . n 
A 1 424 ILE 424 422 422 ILE ILE A . n 
A 1 425 ALA 425 423 423 ALA ALA A . n 
A 1 426 GLU 426 424 424 GLU GLU A . n 
A 1 427 HIS 427 425 425 HIS HIS A . n 
A 1 428 GLY 428 426 426 GLY GLY A . n 
A 1 429 MET 429 427 427 MET MET A . n 
A 1 430 GLU 430 428 428 GLU GLU A . n 
A 1 431 GLN 431 429 429 GLN GLN A . n 
A 1 432 ASN 432 430 430 ASN ASN A . n 
A 1 433 VAL 433 431 431 VAL VAL A . n 
A 1 434 ARG 434 432 432 ARG ARG A . n 
A 1 435 ASP 435 433 433 ASP ASP A . n 
A 1 436 SER 436 434 434 SER SER A . n 
A 1 437 ARG 437 435 435 ARG ARG A . n 
A 1 438 ILE 438 436 436 ILE ILE A . n 
A 1 439 SER 439 437 437 SER SER A . n 
A 1 440 MET 440 438 438 MET MET A . n 
A 1 441 LEU 441 439 439 LEU LEU A . n 
A 1 442 TYR 442 440 440 TYR TYR A . n 
A 1 443 GLU 443 441 441 GLU GLU A . n 
A 1 444 GLY 444 442 442 GLY GLY A . n 
A 1 445 THR 445 443 443 THR THR A . n 
A 1 446 THR 446 444 444 THR THR A . n 
A 1 447 GLY 447 445 445 GLY GLY A . n 
A 1 448 VAL 448 446 446 VAL VAL A . n 
A 1 449 GLN 449 447 447 GLN GLN A . n 
A 1 450 ALA 450 448 448 ALA ALA A . n 
A 1 451 LEU 451 449 449 LEU LEU A . n 
A 1 452 ASP 452 450 450 ASP ASP A . n 
A 1 453 LEU 453 451 451 LEU LEU A . n 
A 1 454 LEU 454 452 452 LEU LEU A . n 
A 1 455 GLY 455 453 453 GLY GLY A . n 
A 1 456 ARG 456 454 454 ARG ARG A . n 
A 1 457 LYS 457 455 455 LYS LYS A . n 
A 1 458 VAL 458 456 456 VAL VAL A . n 
A 1 459 LEU 459 457 457 LEU LEU A . n 
A 1 460 MET 460 458 458 MET MET A . n 
A 1 461 THR 461 459 459 THR THR A . n 
A 1 462 GLN 462 460 460 GLN GLN A . n 
A 1 463 GLY 463 461 461 GLY GLY A . n 
A 1 464 GLU 464 462 462 GLU GLU A . n 
A 1 465 ALA 465 463 463 ALA ALA A . n 
A 1 466 LEU 466 464 464 LEU LEU A . n 
A 1 467 LYS 467 465 465 LYS LYS A . n 
A 1 468 GLY 468 466 466 GLY GLY A . n 
A 1 469 PHE 469 467 467 PHE PHE A . n 
A 1 470 THR 470 468 468 THR THR A . n 
A 1 471 LYS 471 469 469 LYS LYS A . n 
A 1 472 ILE 472 470 470 ILE ILE A . n 
A 1 473 VAL 473 471 471 VAL VAL A . n 
A 1 474 HIS 474 472 472 HIS HIS A . n 
A 1 475 LYS 475 473 473 LYS LYS A . n 
A 1 476 PHE 476 474 474 PHE PHE A . n 
A 1 477 CYS 477 475 475 CYS CYS A . n 
A 1 478 GLN 478 476 476 GLN GLN A . n 
A 1 479 ALA 479 477 477 ALA ALA A . n 
A 1 480 ASN 480 478 478 ASN ASN A . n 
A 1 481 GLU 481 479 479 GLU GLU A . n 
A 1 482 ALA 482 480 480 ALA ALA A . n 
A 1 483 ASN 483 481 481 ASN ASN A . n 
A 1 484 GLU 484 482 482 GLU GLU A . n 
A 1 485 ALA 485 483 483 ALA ALA A . n 
A 1 486 VAL 486 484 484 VAL VAL A . n 
A 1 487 LYS 487 485 485 LYS LYS A . n 
A 1 488 GLU 488 486 486 GLU GLU A . n 
A 1 489 PHE 489 487 487 PHE PHE A . n 
A 1 490 VAL 490 488 488 VAL VAL A . n 
A 1 491 ALA 491 489 489 ALA ALA A . n 
A 1 492 PRO 492 490 490 PRO PRO A . n 
A 1 493 LEU 493 491 491 LEU LEU A . n 
A 1 494 ALA 494 492 492 ALA ALA A . n 
A 1 495 GLN 495 493 493 GLN GLN A . n 
A 1 496 LEU 496 494 494 LEU LEU A . n 
A 1 497 ASN 497 495 495 ASN ASN A . n 
A 1 498 LYS 498 496 496 LYS LYS A . n 
A 1 499 GLU 499 497 497 GLU GLU A . n 
A 1 500 TRP 500 498 498 TRP TRP A . n 
A 1 501 GLY 501 499 499 GLY GLY A . n 
A 1 502 ASP 502 500 500 ASP ASP A . n 
A 1 503 LEU 503 501 501 LEU LEU A . n 
A 1 504 THR 504 502 502 THR THR A . n 
A 1 505 MET 505 503 503 MET MET A . n 
A 1 506 LYS 506 504 504 LYS LYS A . n 
A 1 507 VAL 507 505 505 VAL VAL A . n 
A 1 508 GLY 508 506 506 GLY GLY A . n 
A 1 509 MET 509 507 507 MET MET A . n 
A 1 510 ALA 510 508 508 ALA ALA A . n 
A 1 511 ALA 511 509 509 ALA ALA A . n 
A 1 512 MET 512 510 510 MET MET A . n 
A 1 513 LYS 513 511 511 LYS LYS A . n 
A 1 514 ASP 514 512 512 ASP ASP A . n 
A 1 515 ARG 515 513 513 ARG ARG A . n 
A 1 516 GLU 516 514 514 GLU GLU A . n 
A 1 517 GLU 517 515 515 GLU GLU A . n 
A 1 518 VAL 518 516 516 VAL VAL A . n 
A 1 519 GLY 519 517 517 GLY GLY A . n 
A 1 520 ALA 520 518 518 ALA ALA A . n 
A 1 521 ALA 521 519 519 ALA ALA A . n 
A 1 522 SER 522 520 520 SER SER A . n 
A 1 523 VAL 523 521 521 VAL VAL A . n 
A 1 524 ASP 524 522 522 ASP ASP A . n 
A 1 525 TYR 525 523 523 TYR TYR A . n 
A 1 526 LEU 526 524 524 LEU LEU A . n 
A 1 527 MET 527 525 525 MET MET A . n 
A 1 528 TYR 528 526 526 TYR TYR A . n 
A 1 529 SER 529 527 527 SER SER A . n 
A 1 530 GLY 530 528 528 GLY GLY A . n 
A 1 531 TYR 531 529 529 TYR TYR A . n 
A 1 532 ALA 532 530 530 ALA ALA A . n 
A 1 533 CYS 533 531 531 CYS CYS A . n 
A 1 534 LEU 534 532 532 LEU LEU A . n 
A 1 535 ALA 535 533 533 ALA ALA A . n 
A 1 536 TYR 536 534 534 TYR TYR A . n 
A 1 537 PHE 537 535 535 PHE PHE A . n 
A 1 538 TRP 538 536 536 TRP TRP A . n 
A 1 539 ALA 539 537 537 ALA ALA A . n 
A 1 540 ASP 540 538 538 ASP ASP A . n 
A 1 541 MET 541 539 539 MET MET A . n 
A 1 542 ALA 542 540 540 ALA ALA A . n 
A 1 543 ARG 543 541 541 ARG ARG A . n 
A 1 544 LEU 544 542 542 LEU LEU A . n 
A 1 545 ALA 545 543 543 ALA ALA A . n 
A 1 546 ALA 546 544 544 ALA ALA A . n 
A 1 547 GLU 547 545 545 GLU GLU A . n 
A 1 548 LYS 548 546 546 LYS LYS A . n 
A 1 549 LEU 549 547 547 LEU LEU A . n 
A 1 550 ALA 550 548 548 ALA ALA A . n 
A 1 551 ALA 551 549 549 ALA ALA A . n 
A 1 552 GLY 552 550 550 GLY GLY A . n 
A 1 553 THR 553 551 551 THR THR A . n 
A 1 554 GLY 554 552 552 GLY GLY A . n 
A 1 555 GLU 555 553 553 GLU GLU A . n 
A 1 556 GLU 556 554 554 GLU GLU A . n 
A 1 557 ALA 557 555 555 ALA ALA A . n 
A 1 558 PHE 558 556 556 PHE PHE A . n 
A 1 559 TYR 559 557 557 TYR TYR A . n 
A 1 560 LYS 560 558 558 LYS LYS A . n 
A 1 561 ALA 561 559 559 ALA ALA A . n 
A 1 562 LYS 562 560 560 LYS LYS A . n 
A 1 563 LEU 563 561 561 LEU LEU A . n 
A 1 564 GLN 564 562 562 GLN GLN A . n 
A 1 565 THR 565 563 563 THR THR A . n 
A 1 566 ALA 566 564 564 ALA ALA A . n 
A 1 567 ARG 567 565 565 ARG ARG A . n 
A 1 568 PHE 568 566 566 PHE PHE A . n 
A 1 569 TYR 569 567 567 TYR TYR A . n 
A 1 570 PHE 570 568 568 PHE PHE A . n 
A 1 571 GLN 571 569 569 GLN GLN A . n 
A 1 572 ARG 572 570 570 ARG ARG A . n 
A 1 573 ILE 573 571 571 ILE ILE A . n 
A 1 574 LEU 574 572 572 LEU LEU A . n 
A 1 575 PRO 575 573 573 PRO PRO A . n 
A 1 576 ARG 576 574 574 ARG ARG A . n 
A 1 577 THR 577 575 575 THR THR A . n 
A 1 578 ARG 578 576 576 ARG ARG A . n 
A 1 579 ALA 579 577 577 ALA ALA A . n 
A 1 580 HIS 580 578 578 HIS HIS A . n 
A 1 581 VAL 581 579 579 VAL VAL A . n 
A 1 582 ALA 582 580 580 ALA ALA A . n 
A 1 583 ALA 583 581 581 ALA ALA A . n 
A 1 584 MET 584 582 582 MET MET A . n 
A 1 585 LEU 585 583 583 LEU LEU A . n 
A 1 586 SER 586 584 584 SER SER A . n 
A 1 587 GLY 587 585 585 GLY GLY A . n 
A 1 588 ALA 588 586 586 ALA ALA A . n 
A 1 589 ASN 589 587 587 ASN ASN A . n 
A 1 590 ASN 590 588 588 ASN ASN A . n 
A 1 591 LEU 591 589 589 LEU LEU A . n 
A 1 592 MET 592 590 590 MET MET A . n 
A 1 593 GLU 593 591 591 GLU GLU A . n 
A 1 594 MET 594 592 592 MET MET A . n 
A 1 595 ALA 595 593 593 ALA ALA A . n 
A 1 596 GLU 596 594 594 GLU GLU A . n 
A 1 597 GLU 597 595 595 GLU GLU A . n 
A 1 598 ASP 598 596 596 ASP ASP A . n 
A 1 599 PHE 599 597 597 PHE PHE A . n 
A 1 600 ALA 600 598 598 ALA ALA A . n 
A 1 601 LEU 601 599 599 LEU LEU A . n 
A 1 602 GLY 602 600 600 GLY GLY A . n 
A 1 603 TYR 603 601 601 TYR TYR A . n 
B 1 1   GLY 1   -1  ?   ?   ?   B . n 
B 1 2   HIS 2   0   ?   ?   ?   B . n 
B 1 3   MET 3   1   ?   ?   ?   B . n 
B 1 4   PRO 4   2   ?   ?   ?   B . n 
B 1 5   ASP 5   3   3   ASP ASP B . n 
B 1 6   TYR 6   4   4   TYR TYR B . n 
B 1 7   LYS 7   5   5   LYS LYS B . n 
B 1 8   ALA 8   6   6   ALA ALA B . n 
B 1 9   PRO 9   7   7   PRO PRO B . n 
B 1 10  LEU 10  8   8   LEU LEU B . n 
B 1 11  ARG 11  9   9   ARG ARG B . n 
B 1 12  ASP 12  10  10  ASP ASP B . n 
B 1 13  ILE 13  11  11  ILE ILE B . n 
B 1 14  ARG 14  12  12  ARG ARG B . n 
B 1 15  PHE 15  13  13  PHE PHE B . n 
B 1 16  VAL 16  14  14  VAL VAL B . n 
B 1 17  ARG 17  15  15  ARG ARG B . n 
B 1 18  ASP 18  16  16  ASP ASP B . n 
B 1 19  GLU 19  17  17  GLU GLU B . n 
B 1 20  LEU 20  18  18  LEU LEU B . n 
B 1 21  LEU 21  19  19  LEU LEU B . n 
B 1 22  GLY 22  20  20  GLY GLY B . n 
B 1 23  TYR 23  21  21  TYR TYR B . n 
B 1 24  GLU 24  22  22  GLU GLU B . n 
B 1 25  ALA 25  23  23  ALA ALA B . n 
B 1 26  HIS 26  24  24  HIS HIS B . n 
B 1 27  TYR 27  25  25  TYR TYR B . n 
B 1 28  GLN 28  26  26  GLN GLN B . n 
B 1 29  SER 29  27  27  SER SER B . n 
B 1 30  LEU 30  28  28  LEU LEU B . n 
B 1 31  PRO 31  29  29  PRO PRO B . n 
B 1 32  GLY 32  30  30  GLY GLY B . n 
B 1 33  ALA 33  31  31  ALA ALA B . n 
B 1 34  GLU 34  32  32  GLU GLU B . n 
B 1 35  ASP 35  33  33  ASP ASP B . n 
B 1 36  ALA 36  34  34  ALA ALA B . n 
B 1 37  THR 37  35  35  THR THR B . n 
B 1 38  PRO 38  36  36  PRO PRO B . n 
B 1 39  ASP 39  37  37  ASP ASP B . n 
B 1 40  MET 40  38  38  MET MET B . n 
B 1 41  VAL 41  39  39  VAL VAL B . n 
B 1 42  ASN 42  40  40  ASN ASN B . n 
B 1 43  ALA 43  41  41  ALA ALA B . n 
B 1 44  ILE 44  42  42  ILE ILE B . n 
B 1 45  LEU 45  43  43  LEU LEU B . n 
B 1 46  GLU 46  44  44  GLU GLU B . n 
B 1 47  GLU 47  45  45  GLU GLU B . n 
B 1 48  GLY 48  46  46  GLY GLY B . n 
B 1 49  ALA 49  47  47  ALA ALA B . n 
B 1 50  LYS 50  48  48  LYS LYS B . n 
B 1 51  PHE 51  49  49  PHE PHE B . n 
B 1 52  CYS 52  50  50  CYS CYS B . n 
B 1 53  GLU 53  51  51  GLU GLU B . n 
B 1 54  GLN 54  52  52  GLN GLN B . n 
B 1 55  VAL 55  53  53  VAL VAL B . n 
B 1 56  ILE 56  54  54  ILE ILE B . n 
B 1 57  ALA 57  55  55  ALA ALA B . n 
B 1 58  PRO 58  56  56  PRO PRO B . n 
B 1 59  LEU 59  57  57  LEU LEU B . n 
B 1 60  ASN 60  58  58  ASN ASN B . n 
B 1 61  ARG 61  59  59  ARG ARG B . n 
B 1 62  VAL 62  60  60  VAL VAL B . n 
B 1 63  GLY 63  61  61  GLY GLY B . n 
B 1 64  ASP 64  62  62  ASP ASP B . n 
B 1 65  LEU 65  63  63  LEU LEU B . n 
B 1 66  GLU 66  64  64  GLU GLU B . n 
B 1 67  GLY 67  65  65  GLY GLY B . n 
B 1 68  CYS 68  66  66  CYS CYS B . n 
B 1 69  THR 69  67  67  THR THR B . n 
B 1 70  TRP 70  68  68  TRP TRP B . n 
B 1 71  SER 71  69  69  SER SER B . n 
B 1 72  ALA 72  70  70  ALA ALA B . n 
B 1 73  ASP 73  71  71  ASP ASP B . n 
B 1 74  GLY 74  72  72  GLY GLY B . n 
B 1 75  VAL 75  73  73  VAL VAL B . n 
B 1 76  LYS 76  74  74  LYS LYS B . n 
B 1 77  THR 77  75  75  THR THR B . n 
B 1 78  PRO 78  76  76  PRO PRO B . n 
B 1 79  THR 79  77  77  THR THR B . n 
B 1 80  GLY 80  78  78  GLY GLY B . n 
B 1 81  PHE 81  79  79  PHE PHE B . n 
B 1 82  LYS 82  80  80  LYS LYS B . n 
B 1 83  GLU 83  81  81  GLU GLU B . n 
B 1 84  ALA 84  82  82  ALA ALA B . n 
B 1 85  TYR 85  83  83  TYR TYR B . n 
B 1 86  GLN 86  84  84  GLN GLN B . n 
B 1 87  GLN 87  85  85  GLN GLN B . n 
B 1 88  PHE 88  86  86  PHE PHE B . n 
B 1 89  VAL 89  87  87  VAL VAL B . n 
B 1 90  GLU 90  88  88  GLU GLU B . n 
B 1 91  GLY 91  89  89  GLY GLY B . n 
B 1 92  GLY 92  90  90  GLY GLY B . n 
B 1 93  TRP 93  91  91  TRP TRP B . n 
B 1 94  PRO 94  92  92  PRO PRO B . n 
B 1 95  SER 95  93  93  SER SER B . n 
B 1 96  LEU 96  94  94  LEU LEU B . n 
B 1 97  ALA 97  95  95  ALA ALA B . n 
B 1 98  HIS 98  96  96  HIS HIS B . n 
B 1 99  ASP 99  97  97  ASP ASP B . n 
B 1 100 VAL 100 98  98  VAL VAL B . n 
B 1 101 GLU 101 99  99  GLU GLU B . n 
B 1 102 HIS 102 100 100 HIS HIS B . n 
B 1 103 GLY 103 101 101 GLY GLY B . n 
B 1 104 GLY 104 102 102 GLY GLY B . n 
B 1 105 GLN 105 103 103 GLN GLN B . n 
B 1 106 GLY 106 104 104 GLY GLY B . n 
B 1 107 LEU 107 105 105 LEU LEU B . n 
B 1 108 PRO 108 106 106 PRO PRO B . n 
B 1 109 GLU 109 107 107 GLU GLU B . n 
B 1 110 SER 110 108 108 SER SER B . n 
B 1 111 LEU 111 109 109 LEU LEU B . n 
B 1 112 GLY 112 110 110 GLY GLY B . n 
B 1 113 LEU 113 111 111 LEU LEU B . n 
B 1 114 ALA 114 112 112 ALA ALA B . n 
B 1 115 ILE 115 113 113 ILE ILE B . n 
B 1 116 SER 116 114 114 SER SER B . n 
B 1 117 GLU 117 115 115 GLU GLU B . n 
B 1 118 MET 118 116 116 MET MET B . n 
B 1 119 VAL 119 117 117 VAL VAL B . n 
B 1 120 GLY 120 118 118 GLY GLY B . n 
B 1 121 GLN 121 119 119 GLN GLN B . n 
B 1 122 ALA 122 120 120 ALA ALA B . n 
B 1 123 ASN 123 121 121 ASN ASN B . n 
B 1 124 TRP 124 122 122 TRP TRP B . n 
B 1 125 SER 125 123 123 SER SER B . n 
B 1 126 TRP 126 124 124 TRP TRP B . n 
B 1 127 GLY 127 125 125 GLY GLY B . n 
B 1 128 MET 128 126 126 MET MET B . n 
B 1 129 TYR 129 127 127 TYR TYR B . n 
B 1 130 PRO 130 128 128 PRO PRO B . n 
B 1 131 GLY 131 129 129 GLY GLY B . n 
B 1 132 LEU 132 130 130 LEU LEU B . n 
B 1 133 SER 133 131 131 SER SER B . n 
B 1 134 HIS 134 132 132 HIS HIS B . n 
B 1 135 GLY 135 133 133 GLY GLY B . n 
B 1 136 ALA 136 134 134 ALA ALA B . n 
B 1 137 MET 137 135 135 MET MET B . n 
B 1 138 ASN 138 136 136 ASN ASN B . n 
B 1 139 THR 139 137 137 THR THR B . n 
B 1 140 LEU 140 138 138 LEU LEU B . n 
B 1 141 HIS 141 139 139 HIS HIS B . n 
B 1 142 ALA 142 140 140 ALA ALA B . n 
B 1 143 HIS 143 141 141 HIS HIS B . n 
B 1 144 GLY 144 142 142 GLY GLY B . n 
B 1 145 THR 145 143 143 THR THR B . n 
B 1 146 ALA 146 144 144 ALA ALA B . n 
B 1 147 GLU 147 145 145 GLU GLU B . n 
B 1 148 GLN 148 146 146 GLN GLN B . n 
B 1 149 GLN 149 147 147 GLN GLN B . n 
B 1 150 ALA 150 148 148 ALA ALA B . n 
B 1 151 THR 151 149 149 THR THR B . n 
B 1 152 TYR 152 150 150 TYR TYR B . n 
B 1 153 LEU 153 151 151 LEU LEU B . n 
B 1 154 THR 154 152 152 THR THR B . n 
B 1 155 LYS 155 153 153 LYS LYS B . n 
B 1 156 LEU 156 154 154 LEU LEU B . n 
B 1 157 VAL 157 155 155 VAL VAL B . n 
B 1 158 SER 158 156 156 SER SER B . n 
B 1 159 GLY 159 157 157 GLY GLY B . n 
B 1 160 GLU 160 158 158 GLU GLU B . n 
B 1 161 TRP 161 159 159 TRP TRP B . n 
B 1 162 THR 162 160 160 THR THR B . n 
B 1 163 GLY 163 161 161 GLY GLY B . n 
B 1 164 THR 164 162 162 THR THR B . n 
B 1 165 MET 165 163 163 MET MET B . n 
B 1 166 CYS 166 164 164 CYS CYS B . n 
B 1 167 LEU 167 165 165 LEU LEU B . n 
B 1 168 THR 168 166 166 THR THR B . n 
B 1 169 GLU 169 167 167 GLU GLU B . n 
B 1 170 PRO 170 168 168 PRO PRO B . n 
B 1 171 HIS 171 169 169 HIS HIS B . n 
B 1 172 CYS 172 170 170 CYS CYS B . n 
B 1 173 GLY 173 171 171 GLY GLY B . n 
B 1 174 THR 174 172 172 THR THR B . n 
B 1 175 ASP 175 173 173 ASP ASP B . n 
B 1 176 LEU 176 174 174 LEU LEU B . n 
B 1 177 GLY 177 175 175 GLY GLY B . n 
B 1 178 MET 178 176 176 MET MET B . n 
B 1 179 LEU 179 177 177 LEU LEU B . n 
B 1 180 ARG 180 178 178 ARG ARG B . n 
B 1 181 THR 181 179 179 THR THR B . n 
B 1 182 LYS 182 180 180 LYS LYS B . n 
B 1 183 ALA 183 181 181 ALA ALA B . n 
B 1 184 GLU 184 182 182 GLU GLU B . n 
B 1 185 PRO 185 183 183 PRO PRO B . n 
B 1 186 GLN 186 184 184 GLN GLN B . n 
B 1 187 ALA 187 185 185 ALA ALA B . n 
B 1 188 ASP 188 186 186 ASP ASP B . n 
B 1 189 GLY 189 187 187 GLY GLY B . n 
B 1 190 SER 190 188 188 SER SER B . n 
B 1 191 TYR 191 189 189 TYR TYR B . n 
B 1 192 LYS 192 190 190 LYS LYS B . n 
B 1 193 VAL 193 191 191 VAL VAL B . n 
B 1 194 THR 194 192 192 THR THR B . n 
B 1 195 GLY 195 193 193 GLY GLY B . n 
B 1 196 THR 196 194 194 THR THR B . n 
B 1 197 LYS 197 195 195 LYS LYS B . n 
B 1 198 ILE 198 196 196 ILE ILE B . n 
B 1 199 PHE 199 197 197 PHE PHE B . n 
B 1 200 ILE 200 198 198 ILE ILE B . n 
B 1 201 SER 201 199 199 SER SER B . n 
B 1 202 ALA 202 200 200 ALA ALA B . n 
B 1 203 GLY 203 201 201 GLY GLY B . n 
B 1 204 GLU 204 202 202 GLU GLU B . n 
B 1 205 HIS 205 203 203 HIS HIS B . n 
B 1 206 ASP 206 204 204 ASP ASP B . n 
B 1 207 MET 207 205 205 MET MET B . n 
B 1 208 ALA 208 206 206 ALA ALA B . n 
B 1 209 ASP 209 207 207 ASP ASP B . n 
B 1 210 ASN 210 208 208 ASN ASN B . n 
B 1 211 ILE 211 209 209 ILE ILE B . n 
B 1 212 VAL 212 210 210 VAL VAL B . n 
B 1 213 HIS 213 211 211 HIS HIS B . n 
B 1 214 ILE 214 212 212 ILE ILE B . n 
B 1 215 VAL 215 213 213 VAL VAL B . n 
B 1 216 LEU 216 214 214 LEU LEU B . n 
B 1 217 ALA 217 215 215 ALA ALA B . n 
B 1 218 ARG 218 216 216 ARG ARG B . n 
B 1 219 LEU 219 217 217 LEU LEU B . n 
B 1 220 PRO 220 218 218 PRO PRO B . n 
B 1 221 ASP 221 219 219 ASP ASP B . n 
B 1 222 ALA 222 220 220 ALA ALA B . n 
B 1 223 PRO 223 221 221 PRO PRO B . n 
B 1 224 GLN 224 222 222 GLN GLN B . n 
B 1 225 GLY 225 223 223 GLY GLY B . n 
B 1 226 THR 226 224 224 THR THR B . n 
B 1 227 LYS 227 225 225 LYS LYS B . n 
B 1 228 GLY 228 226 226 GLY GLY B . n 
B 1 229 ILE 229 227 227 ILE ILE B . n 
B 1 230 SER 230 228 228 SER SER B . n 
B 1 231 LEU 231 229 229 LEU LEU B . n 
B 1 232 PHE 232 230 230 PHE PHE B . n 
B 1 233 ILE 233 231 231 ILE ILE B . n 
B 1 234 VAL 234 232 232 VAL VAL B . n 
B 1 235 PRO 235 233 233 PRO PRO B . n 
B 1 236 LYS 236 234 234 LYS LYS B . n 
B 1 237 PHE 237 235 235 PHE PHE B . n 
B 1 238 LEU 238 236 236 LEU LEU B . n 
B 1 239 PRO 239 237 237 PRO PRO B . n 
B 1 240 ASN 240 238 238 ASN ASN B . n 
B 1 241 ALA 241 239 239 ALA ALA B . n 
B 1 242 GLU 242 240 240 GLU GLU B . n 
B 1 243 GLY 243 241 241 GLY GLY B . n 
B 1 244 ASN 244 242 242 ASN ASN B . n 
B 1 245 ALA 245 243 243 ALA ALA B . n 
B 1 246 GLY 246 244 244 GLY GLY B . n 
B 1 247 GLU 247 245 245 GLU GLU B . n 
B 1 248 ARG 248 246 246 ARG ARG B . n 
B 1 249 ASN 249 247 247 ASN ASN B . n 
B 1 250 ALA 250 248 248 ALA ALA B . n 
B 1 251 VAL 251 249 249 VAL VAL B . n 
B 1 252 SER 252 250 250 SER SER B . n 
B 1 253 CYS 253 251 251 CYS CYS B . n 
B 1 254 GLY 254 252 252 GLY GLY B . n 
B 1 255 SER 255 253 253 SER SER B . n 
B 1 256 ILE 256 254 254 ILE ILE B . n 
B 1 257 GLU 257 255 255 GLU GLU B . n 
B 1 258 HIS 258 256 256 HIS HIS B . n 
B 1 259 LYS 259 257 257 LYS LYS B . n 
B 1 260 MET 260 258 258 MET MET B . n 
B 1 261 GLY 261 259 259 GLY GLY B . n 
B 1 262 ILE 262 260 260 ILE ILE B . n 
B 1 263 HIS 263 261 261 HIS HIS B . n 
B 1 264 GLY 264 262 262 GLY GLY B . n 
B 1 265 ASN 265 263 263 ASN ASN B . n 
B 1 266 ALA 266 264 264 ALA ALA B . n 
B 1 267 THR 267 265 265 THR THR B . n 
B 1 268 CYS 268 266 266 CYS CYS B . n 
B 1 269 VAL 269 267 267 VAL VAL B . n 
B 1 270 MET 270 268 268 MET MET B . n 
B 1 271 ASN 271 269 269 ASN ASN B . n 
B 1 272 PHE 272 270 270 PHE PHE B . n 
B 1 273 ASP 273 271 271 ASP ASP B . n 
B 1 274 ALA 274 272 272 ALA ALA B . n 
B 1 275 ALA 275 273 273 ALA ALA B . n 
B 1 276 THR 276 274 274 THR THR B . n 
B 1 277 GLY 277 275 275 GLY GLY B . n 
B 1 278 PHE 278 276 276 PHE PHE B . n 
B 1 279 LEU 279 277 277 LEU LEU B . n 
B 1 280 ILE 280 278 278 ILE ILE B . n 
B 1 281 GLY 281 279 279 GLY GLY B . n 
B 1 282 PRO 282 280 280 PRO PRO B . n 
B 1 283 PRO 283 281 281 PRO PRO B . n 
B 1 284 ASN 284 282 282 ASN ASN B . n 
B 1 285 LYS 285 283 283 LYS LYS B . n 
B 1 286 GLY 286 284 284 GLY GLY B . n 
B 1 287 LEU 287 285 285 LEU LEU B . n 
B 1 288 ASN 288 286 286 ASN ASN B . n 
B 1 289 CYS 289 287 287 CYS CYS B . n 
B 1 290 MET 290 288 288 MET MET B . n 
B 1 291 PHE 291 289 289 PHE PHE B . n 
B 1 292 THR 292 290 290 THR THR B . n 
B 1 293 PHE 293 291 291 PHE PHE B . n 
B 1 294 MET 294 292 292 MET MET B . n 
B 1 295 ASN 295 293 293 ASN ASN B . n 
B 1 296 THR 296 294 294 THR THR B . n 
B 1 297 ALA 297 295 295 ALA ALA B . n 
B 1 298 ARG 298 296 296 ARG ARG B . n 
B 1 299 LEU 299 297 297 LEU LEU B . n 
B 1 300 GLY 300 298 298 GLY GLY B . n 
B 1 301 THR 301 299 299 THR THR B . n 
B 1 302 ALA 302 300 300 ALA ALA B . n 
B 1 303 LEU 303 301 301 LEU LEU B . n 
B 1 304 GLN 304 302 302 GLN GLN B . n 
B 1 305 GLY 305 303 303 GLY GLY B . n 
B 1 306 LEU 306 304 304 LEU LEU B . n 
B 1 307 ALA 307 305 305 ALA ALA B . n 
B 1 308 HIS 308 306 306 HIS HIS B . n 
B 1 309 ALA 309 307 307 ALA ALA B . n 
B 1 310 GLU 310 308 308 GLU GLU B . n 
B 1 311 VAL 311 309 309 VAL VAL B . n 
B 1 312 GLY 312 310 310 GLY GLY B . n 
B 1 313 PHE 313 311 311 PHE PHE B . n 
B 1 314 GLN 314 312 312 GLN GLN B . n 
B 1 315 GLY 315 313 313 GLY GLY B . n 
B 1 316 GLY 316 314 314 GLY GLY B . n 
B 1 317 ILE 317 315 315 ILE ILE B . n 
B 1 318 ALA 318 316 316 ALA ALA B . n 
B 1 319 TYR 319 317 317 TYR TYR B . n 
B 1 320 ALA 320 318 318 ALA ALA B . n 
B 1 321 ARG 321 319 319 ARG ARG B . n 
B 1 322 GLU 322 320 320 GLU GLU B . n 
B 1 323 ARG 323 321 321 ARG ARG B . n 
B 1 324 LEU 324 322 322 LEU LEU B . n 
B 1 325 GLN 325 323 323 GLN GLN B . n 
B 1 326 MET 326 324 324 MET MET B . n 
B 1 327 ARG 327 325 325 ARG ARG B . n 
B 1 328 SER 328 326 326 SER SER B . n 
B 1 329 LEU 329 327 327 LEU LEU B . n 
B 1 330 THR 330 328 328 THR THR B . n 
B 1 331 GLY 331 329 329 GLY GLY B . n 
B 1 332 PRO 332 330 330 PRO PRO B . n 
B 1 333 LYS 333 331 331 LYS LYS B . n 
B 1 334 ALA 334 332 332 ALA ALA B . n 
B 1 335 PRO 335 333 333 PRO PRO B . n 
B 1 336 GLU 336 334 334 GLU GLU B . n 
B 1 337 LYS 337 335 335 LYS LYS B . n 
B 1 338 PRO 338 336 336 PRO PRO B . n 
B 1 339 ALA 339 337 337 ALA ALA B . n 
B 1 340 ASP 340 338 338 ASP ASP B . n 
B 1 341 PRO 341 339 339 PRO PRO B . n 
B 1 342 ILE 342 340 340 ILE ILE B . n 
B 1 343 ILE 343 341 341 ILE ILE B . n 
B 1 344 VAL 344 342 342 VAL VAL B . n 
B 1 345 HIS 345 343 343 HIS HIS B . n 
B 1 346 PRO 346 344 344 PRO PRO B . n 
B 1 347 ASP 347 345 345 ASP ASP B . n 
B 1 348 VAL 348 346 346 VAL VAL B . n 
B 1 349 ARG 349 347 347 ARG ARG B . n 
B 1 350 ARG 350 348 348 ARG ARG B . n 
B 1 351 MET 351 349 349 MET MET B . n 
B 1 352 LEU 352 350 350 LEU LEU B . n 
B 1 353 LEU 353 351 351 LEU LEU B . n 
B 1 354 THR 354 352 352 THR THR B . n 
B 1 355 MET 355 353 353 MET MET B . n 
B 1 356 LYS 356 354 354 LYS LYS B . n 
B 1 357 ALA 357 355 355 ALA ALA B . n 
B 1 358 PHE 358 356 356 PHE PHE B . n 
B 1 359 ALA 359 357 357 ALA ALA B . n 
B 1 360 GLU 360 358 358 GLU GLU B . n 
B 1 361 GLY 361 359 359 GLY GLY B . n 
B 1 362 ASN 362 360 360 ASN ASN B . n 
B 1 363 ARG 363 361 361 ARG ARG B . n 
B 1 364 ALA 364 362 362 ALA ALA B . n 
B 1 365 MET 365 363 363 MET MET B . n 
B 1 366 LEU 366 364 364 LEU LEU B . n 
B 1 367 TYR 367 365 365 TYR TYR B . n 
B 1 368 PHE 368 366 366 PHE PHE B . n 
B 1 369 ALA 369 367 367 ALA ALA B . n 
B 1 370 ALA 370 368 368 ALA ALA B . n 
B 1 371 LYS 371 369 369 LYS LYS B . n 
B 1 372 GLN 372 370 370 GLN GLN B . n 
B 1 373 VAL 373 371 371 VAL VAL B . n 
B 1 374 ASP 374 372 372 ASP ASP B . n 
B 1 375 ILE 375 373 373 ILE ILE B . n 
B 1 376 VAL 376 374 374 VAL VAL B . n 
B 1 377 GLN 377 375 375 GLN GLN B . n 
B 1 378 ARG 378 376 376 ARG ARG B . n 
B 1 379 SER 379 377 377 SER SER B . n 
B 1 380 GLN 380 378 378 GLN GLN B . n 
B 1 381 ASP 381 379 379 ASP ASP B . n 
B 1 382 GLU 382 380 380 GLU GLU B . n 
B 1 383 GLU 383 381 381 GLU GLU B . n 
B 1 384 GLN 384 382 382 GLN GLN B . n 
B 1 385 LYS 385 383 383 LYS LYS B . n 
B 1 386 LYS 386 384 384 LYS LYS B . n 
B 1 387 ALA 387 385 385 ALA ALA B . n 
B 1 388 ALA 388 386 386 ALA ALA B . n 
B 1 389 ASP 389 387 387 ASP ASP B . n 
B 1 390 SER 390 388 388 SER SER B . n 
B 1 391 MET 391 389 389 MET MET B . n 
B 1 392 LEU 392 390 390 LEU LEU B . n 
B 1 393 ALA 393 391 391 ALA ALA B . n 
B 1 394 PHE 394 392 392 PHE PHE B . n 
B 1 395 LEU 395 393 393 LEU LEU B . n 
B 1 396 THR 396 394 394 THR THR B . n 
B 1 397 PRO 397 395 395 PRO PRO B . n 
B 1 398 ILE 398 396 396 ILE ILE B . n 
B 1 399 ALA 399 397 397 ALA ALA B . n 
B 1 400 LYS 400 398 398 LYS LYS B . n 
B 1 401 ALA 401 399 399 ALA ALA B . n 
B 1 402 PHE 402 400 400 PHE PHE B . n 
B 1 403 MET 403 401 401 MET MET B . n 
B 1 404 THR 404 402 402 THR THR B . n 
B 1 405 GLU 405 403 403 GLU GLU B . n 
B 1 406 VAL 406 404 404 VAL VAL B . n 
B 1 407 GLY 407 405 405 GLY GLY B . n 
B 1 408 PHE 408 406 406 PHE PHE B . n 
B 1 409 GLU 409 407 407 GLU GLU B . n 
B 1 410 SER 410 408 408 SER SER B . n 
B 1 411 ALA 411 409 409 ALA ALA B . n 
B 1 412 ASN 412 410 410 ASN ASN B . n 
B 1 413 HIS 413 411 411 HIS HIS B . n 
B 1 414 GLY 414 412 412 GLY GLY B . n 
B 1 415 VAL 415 413 413 VAL VAL B . n 
B 1 416 GLN 416 414 414 GLN GLN B . n 
B 1 417 ILE 417 415 415 ILE ILE B . n 
B 1 418 PHE 418 416 416 PHE PHE B . n 
B 1 419 GLY 419 417 417 GLY GLY B . n 
B 1 420 GLY 420 418 418 GLY GLY B . n 
B 1 421 HIS 421 419 419 HIS HIS B . n 
B 1 422 GLY 422 420 420 GLY GLY B . n 
B 1 423 PHE 423 421 421 PHE PHE B . n 
B 1 424 ILE 424 422 422 ILE ILE B . n 
B 1 425 ALA 425 423 423 ALA ALA B . n 
B 1 426 GLU 426 424 424 GLU GLU B . n 
B 1 427 HIS 427 425 425 HIS HIS B . n 
B 1 428 GLY 428 426 426 GLY GLY B . n 
B 1 429 MET 429 427 427 MET MET B . n 
B 1 430 GLU 430 428 428 GLU GLU B . n 
B 1 431 GLN 431 429 429 GLN GLN B . n 
B 1 432 ASN 432 430 430 ASN ASN B . n 
B 1 433 VAL 433 431 431 VAL VAL B . n 
B 1 434 ARG 434 432 432 ARG ARG B . n 
B 1 435 ASP 435 433 433 ASP ASP B . n 
B 1 436 SER 436 434 434 SER SER B . n 
B 1 437 ARG 437 435 435 ARG ARG B . n 
B 1 438 ILE 438 436 436 ILE ILE B . n 
B 1 439 SER 439 437 437 SER SER B . n 
B 1 440 MET 440 438 438 MET MET B . n 
B 1 441 LEU 441 439 439 LEU LEU B . n 
B 1 442 TYR 442 440 440 TYR TYR B . n 
B 1 443 GLU 443 441 441 GLU GLU B . n 
B 1 444 GLY 444 442 442 GLY GLY B . n 
B 1 445 THR 445 443 443 THR THR B . n 
B 1 446 THR 446 444 444 THR THR B . n 
B 1 447 GLY 447 445 445 GLY GLY B . n 
B 1 448 VAL 448 446 446 VAL VAL B . n 
B 1 449 GLN 449 447 447 GLN GLN B . n 
B 1 450 ALA 450 448 448 ALA ALA B . n 
B 1 451 LEU 451 449 449 LEU LEU B . n 
B 1 452 ASP 452 450 450 ASP ASP B . n 
B 1 453 LEU 453 451 451 LEU LEU B . n 
B 1 454 LEU 454 452 452 LEU LEU B . n 
B 1 455 GLY 455 453 453 GLY GLY B . n 
B 1 456 ARG 456 454 454 ARG ARG B . n 
B 1 457 LYS 457 455 455 LYS LYS B . n 
B 1 458 VAL 458 456 456 VAL VAL B . n 
B 1 459 LEU 459 457 457 LEU LEU B . n 
B 1 460 MET 460 458 458 MET MET B . n 
B 1 461 THR 461 459 459 THR THR B . n 
B 1 462 GLN 462 460 460 GLN GLN B . n 
B 1 463 GLY 463 461 461 GLY GLY B . n 
B 1 464 GLU 464 462 462 GLU GLU B . n 
B 1 465 ALA 465 463 463 ALA ALA B . n 
B 1 466 LEU 466 464 464 LEU LEU B . n 
B 1 467 LYS 467 465 465 LYS LYS B . n 
B 1 468 GLY 468 466 466 GLY GLY B . n 
B 1 469 PHE 469 467 467 PHE PHE B . n 
B 1 470 THR 470 468 468 THR THR B . n 
B 1 471 LYS 471 469 469 LYS LYS B . n 
B 1 472 ILE 472 470 470 ILE ILE B . n 
B 1 473 VAL 473 471 471 VAL VAL B . n 
B 1 474 HIS 474 472 472 HIS HIS B . n 
B 1 475 LYS 475 473 473 LYS LYS B . n 
B 1 476 PHE 476 474 474 PHE PHE B . n 
B 1 477 CYS 477 475 475 CYS CYS B . n 
B 1 478 GLN 478 476 476 GLN GLN B . n 
B 1 479 ALA 479 477 477 ALA ALA B . n 
B 1 480 ASN 480 478 478 ASN ASN B . n 
B 1 481 GLU 481 479 479 GLU GLU B . n 
B 1 482 ALA 482 480 480 ALA ALA B . n 
B 1 483 ASN 483 481 481 ASN ASN B . n 
B 1 484 GLU 484 482 482 GLU GLU B . n 
B 1 485 ALA 485 483 483 ALA ALA B . n 
B 1 486 VAL 486 484 484 VAL VAL B . n 
B 1 487 LYS 487 485 485 LYS LYS B . n 
B 1 488 GLU 488 486 486 GLU GLU B . n 
B 1 489 PHE 489 487 487 PHE PHE B . n 
B 1 490 VAL 490 488 488 VAL VAL B . n 
B 1 491 ALA 491 489 489 ALA ALA B . n 
B 1 492 PRO 492 490 490 PRO PRO B . n 
B 1 493 LEU 493 491 491 LEU LEU B . n 
B 1 494 ALA 494 492 492 ALA ALA B . n 
B 1 495 GLN 495 493 493 GLN GLN B . n 
B 1 496 LEU 496 494 494 LEU LEU B . n 
B 1 497 ASN 497 495 495 ASN ASN B . n 
B 1 498 LYS 498 496 496 LYS LYS B . n 
B 1 499 GLU 499 497 497 GLU GLU B . n 
B 1 500 TRP 500 498 498 TRP TRP B . n 
B 1 501 GLY 501 499 499 GLY GLY B . n 
B 1 502 ASP 502 500 500 ASP ASP B . n 
B 1 503 LEU 503 501 501 LEU LEU B . n 
B 1 504 THR 504 502 502 THR THR B . n 
B 1 505 MET 505 503 503 MET MET B . n 
B 1 506 LYS 506 504 504 LYS LYS B . n 
B 1 507 VAL 507 505 505 VAL VAL B . n 
B 1 508 GLY 508 506 506 GLY GLY B . n 
B 1 509 MET 509 507 507 MET MET B . n 
B 1 510 ALA 510 508 508 ALA ALA B . n 
B 1 511 ALA 511 509 509 ALA ALA B . n 
B 1 512 MET 512 510 510 MET MET B . n 
B 1 513 LYS 513 511 511 LYS LYS B . n 
B 1 514 ASP 514 512 512 ASP ASP B . n 
B 1 515 ARG 515 513 513 ARG ARG B . n 
B 1 516 GLU 516 514 514 GLU GLU B . n 
B 1 517 GLU 517 515 515 GLU GLU B . n 
B 1 518 VAL 518 516 516 VAL VAL B . n 
B 1 519 GLY 519 517 517 GLY GLY B . n 
B 1 520 ALA 520 518 518 ALA ALA B . n 
B 1 521 ALA 521 519 519 ALA ALA B . n 
B 1 522 SER 522 520 520 SER SER B . n 
B 1 523 VAL 523 521 521 VAL VAL B . n 
B 1 524 ASP 524 522 522 ASP ASP B . n 
B 1 525 TYR 525 523 523 TYR TYR B . n 
B 1 526 LEU 526 524 524 LEU LEU B . n 
B 1 527 MET 527 525 525 MET MET B . n 
B 1 528 TYR 528 526 526 TYR TYR B . n 
B 1 529 SER 529 527 527 SER SER B . n 
B 1 530 GLY 530 528 528 GLY GLY B . n 
B 1 531 TYR 531 529 529 TYR TYR B . n 
B 1 532 ALA 532 530 530 ALA ALA B . n 
B 1 533 CYS 533 531 531 CYS CYS B . n 
B 1 534 LEU 534 532 532 LEU LEU B . n 
B 1 535 ALA 535 533 533 ALA ALA B . n 
B 1 536 TYR 536 534 534 TYR TYR B . n 
B 1 537 PHE 537 535 535 PHE PHE B . n 
B 1 538 TRP 538 536 536 TRP TRP B . n 
B 1 539 ALA 539 537 537 ALA ALA B . n 
B 1 540 ASP 540 538 538 ASP ASP B . n 
B 1 541 MET 541 539 539 MET MET B . n 
B 1 542 ALA 542 540 540 ALA ALA B . n 
B 1 543 ARG 543 541 541 ARG ARG B . n 
B 1 544 LEU 544 542 542 LEU LEU B . n 
B 1 545 ALA 545 543 543 ALA ALA B . n 
B 1 546 ALA 546 544 544 ALA ALA B . n 
B 1 547 GLU 547 545 545 GLU GLU B . n 
B 1 548 LYS 548 546 546 LYS LYS B . n 
B 1 549 LEU 549 547 547 LEU LEU B . n 
B 1 550 ALA 550 548 548 ALA ALA B . n 
B 1 551 ALA 551 549 549 ALA ALA B . n 
B 1 552 GLY 552 550 550 GLY GLY B . n 
B 1 553 THR 553 551 551 THR THR B . n 
B 1 554 GLY 554 552 552 GLY GLY B . n 
B 1 555 GLU 555 553 553 GLU GLU B . n 
B 1 556 GLU 556 554 554 GLU GLU B . n 
B 1 557 ALA 557 555 555 ALA ALA B . n 
B 1 558 PHE 558 556 556 PHE PHE B . n 
B 1 559 TYR 559 557 557 TYR TYR B . n 
B 1 560 LYS 560 558 558 LYS LYS B . n 
B 1 561 ALA 561 559 559 ALA ALA B . n 
B 1 562 LYS 562 560 560 LYS LYS B . n 
B 1 563 LEU 563 561 561 LEU LEU B . n 
B 1 564 GLN 564 562 562 GLN GLN B . n 
B 1 565 THR 565 563 563 THR THR B . n 
B 1 566 ALA 566 564 564 ALA ALA B . n 
B 1 567 ARG 567 565 565 ARG ARG B . n 
B 1 568 PHE 568 566 566 PHE PHE B . n 
B 1 569 TYR 569 567 567 TYR TYR B . n 
B 1 570 PHE 570 568 568 PHE PHE B . n 
B 1 571 GLN 571 569 569 GLN GLN B . n 
B 1 572 ARG 572 570 570 ARG ARG B . n 
B 1 573 ILE 573 571 571 ILE ILE B . n 
B 1 574 LEU 574 572 572 LEU LEU B . n 
B 1 575 PRO 575 573 573 PRO PRO B . n 
B 1 576 ARG 576 574 574 ARG ARG B . n 
B 1 577 THR 577 575 575 THR THR B . n 
B 1 578 ARG 578 576 576 ARG ARG B . n 
B 1 579 ALA 579 577 577 ALA ALA B . n 
B 1 580 HIS 580 578 578 HIS HIS B . n 
B 1 581 VAL 581 579 579 VAL VAL B . n 
B 1 582 ALA 582 580 580 ALA ALA B . n 
B 1 583 ALA 583 581 581 ALA ALA B . n 
B 1 584 MET 584 582 582 MET MET B . n 
B 1 585 LEU 585 583 583 LEU LEU B . n 
B 1 586 SER 586 584 584 SER SER B . n 
B 1 587 GLY 587 585 585 GLY GLY B . n 
B 1 588 ALA 588 586 586 ALA ALA B . n 
B 1 589 ASN 589 587 587 ASN ASN B . n 
B 1 590 ASN 590 588 588 ASN ASN B . n 
B 1 591 LEU 591 589 589 LEU LEU B . n 
B 1 592 MET 592 590 590 MET MET B . n 
B 1 593 GLU 593 591 591 GLU GLU B . n 
B 1 594 MET 594 592 592 MET MET B . n 
B 1 595 ALA 595 593 593 ALA ALA B . n 
B 1 596 GLU 596 594 594 GLU GLU B . n 
B 1 597 GLU 597 595 595 GLU GLU B . n 
B 1 598 ASP 598 596 596 ASP ASP B . n 
B 1 599 PHE 599 597 597 PHE PHE B . n 
B 1 600 ALA 600 598 598 ALA ALA B . n 
B 1 601 LEU 601 599 599 LEU LEU B . n 
B 1 602 GLY 602 600 600 GLY GLY B . n 
B 1 603 TYR 603 601 601 TYR TYR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CO8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CO8 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 FAD 1  701 700 FAD FAD A . 
D 3 PEG 1  702 702 PEG PEG A . 
E 4 CO8 1  703 703 CO8 CO8 A . 
F 3 PEG 1  704 709 PEG PEG A . 
G 2 FAD 1  701 699 FAD FAD B . 
H 4 CO8 1  702 710 CO8 CO8 B . 
I 5 HOH 1  801 128 HOH HOH A . 
I 5 HOH 2  802 144 HOH HOH A . 
I 5 HOH 3  803 120 HOH HOH A . 
I 5 HOH 4  804 133 HOH HOH A . 
I 5 HOH 5  805 110 HOH HOH A . 
I 5 HOH 6  806 40  HOH HOH A . 
I 5 HOH 7  807 2   HOH HOH A . 
I 5 HOH 8  808 138 HOH HOH A . 
I 5 HOH 9  809 56  HOH HOH A . 
I 5 HOH 10 810 122 HOH HOH A . 
I 5 HOH 11 811 48  HOH HOH A . 
I 5 HOH 12 812 79  HOH HOH A . 
I 5 HOH 13 813 6   HOH HOH A . 
I 5 HOH 14 814 69  HOH HOH A . 
I 5 HOH 15 815 91  HOH HOH A . 
I 5 HOH 16 816 29  HOH HOH A . 
I 5 HOH 17 817 103 HOH HOH A . 
I 5 HOH 18 818 1   HOH HOH A . 
I 5 HOH 19 819 141 HOH HOH A . 
I 5 HOH 20 820 147 HOH HOH A . 
I 5 HOH 21 821 95  HOH HOH A . 
I 5 HOH 22 822 57  HOH HOH A . 
I 5 HOH 23 823 163 HOH HOH A . 
I 5 HOH 24 824 89  HOH HOH A . 
I 5 HOH 25 825 10  HOH HOH A . 
I 5 HOH 26 826 13  HOH HOH A . 
I 5 HOH 27 827 127 HOH HOH A . 
I 5 HOH 28 828 108 HOH HOH A . 
I 5 HOH 29 829 35  HOH HOH A . 
I 5 HOH 30 830 12  HOH HOH A . 
I 5 HOH 31 831 131 HOH HOH A . 
I 5 HOH 32 832 106 HOH HOH A . 
I 5 HOH 33 833 158 HOH HOH A . 
I 5 HOH 34 834 24  HOH HOH A . 
I 5 HOH 35 835 165 HOH HOH A . 
I 5 HOH 36 836 135 HOH HOH A . 
I 5 HOH 37 837 111 HOH HOH A . 
I 5 HOH 38 838 82  HOH HOH A . 
I 5 HOH 39 839 8   HOH HOH A . 
I 5 HOH 40 840 49  HOH HOH A . 
I 5 HOH 41 841 78  HOH HOH A . 
I 5 HOH 42 842 22  HOH HOH A . 
I 5 HOH 43 843 114 HOH HOH A . 
I 5 HOH 44 844 99  HOH HOH A . 
I 5 HOH 45 845 113 HOH HOH A . 
I 5 HOH 46 846 159 HOH HOH A . 
I 5 HOH 47 847 19  HOH HOH A . 
I 5 HOH 48 848 33  HOH HOH A . 
I 5 HOH 49 849 9   HOH HOH A . 
I 5 HOH 50 850 148 HOH HOH A . 
I 5 HOH 51 851 54  HOH HOH A . 
I 5 HOH 52 852 100 HOH HOH A . 
I 5 HOH 53 853 59  HOH HOH A . 
I 5 HOH 54 854 94  HOH HOH A . 
I 5 HOH 55 855 156 HOH HOH A . 
I 5 HOH 56 856 44  HOH HOH A . 
I 5 HOH 57 857 101 HOH HOH A . 
I 5 HOH 58 858 142 HOH HOH A . 
I 5 HOH 59 859 153 HOH HOH A . 
I 5 HOH 60 860 118 HOH HOH A . 
I 5 HOH 61 861 64  HOH HOH A . 
I 5 HOH 62 862 71  HOH HOH A . 
I 5 HOH 63 863 168 HOH HOH A . 
I 5 HOH 64 864 139 HOH HOH A . 
I 5 HOH 65 865 116 HOH HOH A . 
I 5 HOH 66 866 112 HOH HOH A . 
I 5 HOH 67 867 60  HOH HOH A . 
I 5 HOH 68 868 34  HOH HOH A . 
I 5 HOH 69 869 105 HOH HOH A . 
I 5 HOH 70 870 137 HOH HOH A . 
I 5 HOH 71 871 72  HOH HOH A . 
I 5 HOH 72 872 53  HOH HOH A . 
I 5 HOH 73 873 75  HOH HOH A . 
I 5 HOH 74 874 27  HOH HOH A . 
I 5 HOH 75 875 145 HOH HOH A . 
I 5 HOH 76 876 161 HOH HOH A . 
I 5 HOH 77 877 162 HOH HOH A . 
I 5 HOH 78 878 170 HOH HOH A . 
J 5 HOH 1  801 121 HOH HOH B . 
J 5 HOH 2  802 169 HOH HOH B . 
J 5 HOH 3  803 55  HOH HOH B . 
J 5 HOH 4  804 155 HOH HOH B . 
J 5 HOH 5  805 136 HOH HOH B . 
J 5 HOH 6  806 80  HOH HOH B . 
J 5 HOH 7  807 4   HOH HOH B . 
J 5 HOH 8  808 77  HOH HOH B . 
J 5 HOH 9  809 154 HOH HOH B . 
J 5 HOH 10 810 123 HOH HOH B . 
J 5 HOH 11 811 51  HOH HOH B . 
J 5 HOH 12 812 3   HOH HOH B . 
J 5 HOH 13 813 149 HOH HOH B . 
J 5 HOH 14 814 88  HOH HOH B . 
J 5 HOH 15 815 28  HOH HOH B . 
J 5 HOH 16 816 167 HOH HOH B . 
J 5 HOH 17 817 58  HOH HOH B . 
J 5 HOH 18 818 90  HOH HOH B . 
J 5 HOH 19 819 140 HOH HOH B . 
J 5 HOH 20 820 46  HOH HOH B . 
J 5 HOH 21 821 14  HOH HOH B . 
J 5 HOH 22 822 43  HOH HOH B . 
J 5 HOH 23 823 16  HOH HOH B . 
J 5 HOH 24 824 152 HOH HOH B . 
J 5 HOH 25 825 93  HOH HOH B . 
J 5 HOH 26 826 130 HOH HOH B . 
J 5 HOH 27 827 157 HOH HOH B . 
J 5 HOH 28 828 38  HOH HOH B . 
J 5 HOH 29 829 18  HOH HOH B . 
J 5 HOH 30 830 47  HOH HOH B . 
J 5 HOH 31 831 124 HOH HOH B . 
J 5 HOH 32 832 86  HOH HOH B . 
J 5 HOH 33 833 74  HOH HOH B . 
J 5 HOH 34 834 96  HOH HOH B . 
J 5 HOH 35 835 26  HOH HOH B . 
J 5 HOH 36 836 37  HOH HOH B . 
J 5 HOH 37 837 11  HOH HOH B . 
J 5 HOH 38 838 5   HOH HOH B . 
J 5 HOH 39 839 104 HOH HOH B . 
J 5 HOH 40 840 31  HOH HOH B . 
J 5 HOH 41 841 129 HOH HOH B . 
J 5 HOH 42 842 7   HOH HOH B . 
J 5 HOH 43 843 117 HOH HOH B . 
J 5 HOH 44 844 63  HOH HOH B . 
J 5 HOH 45 845 45  HOH HOH B . 
J 5 HOH 46 846 146 HOH HOH B . 
J 5 HOH 47 847 15  HOH HOH B . 
J 5 HOH 48 848 83  HOH HOH B . 
J 5 HOH 49 849 67  HOH HOH B . 
J 5 HOH 50 850 134 HOH HOH B . 
J 5 HOH 51 851 85  HOH HOH B . 
J 5 HOH 52 852 92  HOH HOH B . 
J 5 HOH 53 853 98  HOH HOH B . 
J 5 HOH 54 854 164 HOH HOH B . 
J 5 HOH 55 855 109 HOH HOH B . 
J 5 HOH 56 856 166 HOH HOH B . 
J 5 HOH 57 857 50  HOH HOH B . 
J 5 HOH 58 858 42  HOH HOH B . 
J 5 HOH 59 859 132 HOH HOH B . 
J 5 HOH 60 860 25  HOH HOH B . 
J 5 HOH 61 861 73  HOH HOH B . 
J 5 HOH 62 862 23  HOH HOH B . 
J 5 HOH 63 863 87  HOH HOH B . 
J 5 HOH 64 864 151 HOH HOH B . 
J 5 HOH 65 865 17  HOH HOH B . 
J 5 HOH 66 866 70  HOH HOH B . 
J 5 HOH 67 867 41  HOH HOH B . 
J 5 HOH 68 868 160 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        2 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8PNS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     155.918 
_cell.length_a_esd                 ? 
_cell.length_b                     155.918 
_cell.length_b_esd                 ? 
_cell.length_c                     99.511 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8PNS 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8PNS 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.66 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.77 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M MES pH6, 0.1M Calcium chloride dihydrate, 20% w/v PEG6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-09-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9179 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9179 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          26.610 
_reflns.entry_id                                       8PNS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.08 
_reflns.d_resolution_low                               135.03 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     82487 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                15.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.246 
_reflns.pdbx_Rpim_I_all                                0.061 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.238 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
3.56 3.92 ? ?    ? ? ? ? 4117 ? ? ? ? ? ? ? ? ? ? ? 16.9  ? ? ? 0.142 0.034 ? 1 1 0.996 ? ? 100   ? 0.138 ? ? ? ? ? ? ? ? ? 
3.0  3.56 ? 12.2 ? ? ? ? 4145 ? ? ? ? ? ? ? ? ? ? ? ?     ? ? ? 0.198 0.047 ? 2 1 0.993 ? ? 100   ? 0.192 ? ? ? ? ? ? ? ? ? 
2.82 2.95 ? 4.7  ? ? ? ? 4125 ? ? ? ? ? ? ? ? ? ? ? 18.05 ? ? ? 0.439 0.103 ? 3 1 0.969 ? ? 100   ? 0.427 ? ? ? ? ? ? ? ? ? 
2.08 2.12 ? 0.4  ? ? ? ? 4038 ? ? ? ? ? ? ? ? ? ? ? 11.12 ? ? ? 3.041 0.905 ? 4 1 0.37  ? ? 99.17 ? 2.9   ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.68 
_refine.aniso_B[1][2]                            0.34 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.68 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -2.20 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.223 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.934 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8PNS 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.08 
_refine.ls_d_res_low                             135.03 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     78359 
_refine.ls_number_reflns_R_free                  4059 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20617 
_refine.ls_R_factor_R_free                       0.24872 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20392 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.210 
_refine.pdbx_overall_ESU_R_Free                  0.184 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             9.293 
_refine.overall_SU_ML                            0.211 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.08 
_refine_hist.d_res_low                        135.03 
_refine_hist.number_atoms_solvent             146 
_refine_hist.number_atoms_total               9521 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        9141 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         234 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.013  9610  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  8936  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.699  1.644  13013 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.336  1.575  20588 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.755  5.000  1201  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.175 22.700 474   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.062 15.000 1558  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.236 15.000 50    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.081  0.200  1223  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  10997 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  2175  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.242  4.098  4804  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.242  4.098  4803  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.558  6.141  6005  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.557  6.141  6006  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.142  4.487  4806  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.142  4.487  4807  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.093  6.599  7009  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.610  48.592 10787 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.608  48.594 10777 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.080 
_refine_ls_shell.d_res_low                        2.134 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             285 
_refine_ls_shell.number_reflns_R_work             5723 
_refine_ls_shell.percent_reflns_obs               99.11 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.367 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.376 
# 
_struct.entry_id                     8PNS 
_struct.title                        'Crystal structure of the acyl-CoA dehydrogenase PA0506 (FadE1) from Pseudomonas aeruginosa' 
_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        8PNS 
_struct_keywords.text            'acyl-CoA dehydrogenase, beta-oxidation, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 2 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A072ZR57_PSEAI 
_struct_ref.pdbx_db_accession          A0A072ZR57 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPDYKAPLRDIRFVRDELLGYEAHYQSLPGAEDATPDMVNAILEEGAKFCEQVIAPLNRVGDLEGCTWSADGVKTPTGFK
EAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGEWT
GTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEHDMADNIVHIVLARLPDAPQGTKGISLFIVPKFLPNAE
GNAGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARE
RLQMRSLTGPKAPEKPADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIVQRSQDEEQKKAADSMLAFLTPIAKAF
MTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALDLLGRKVLMTQGEALKGFTKIVHKFCQANEA
NEAVKEFVAPLAQLNKEWGDLTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTGEEAFYKAK
LQTARFYFQRILPRTRAHVAAMLSGANNLMEMAEEDFALGY
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8PNS A 3 ? 603 ? A0A072ZR57 1 ? 601 ? 1 601 
2 1 8PNS B 3 ? 603 ? A0A072ZR57 1 ? 601 ? 1 601 
# 
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 8PNS GLY A 1 ? UNP A0A072ZR57 ? ? 'expression tag' -1 1 
1 8PNS HIS A 2 ? UNP A0A072ZR57 ? ? 'expression tag' 0  2 
2 8PNS GLY B 1 ? UNP A0A072ZR57 ? ? 'expression tag' -1 3 
2 8PNS HIS B 2 ? UNP A0A072ZR57 ? ? 'expression tag' 0  4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 16150 ? 
1 MORE         -51   ? 
1 'SSA (A^2)'  39630 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                'Analytic ultracentrifuge indicated that it is dimer' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 9   ? GLU A 19  ? PRO A 7   GLU A 17  1 ? 11 
HELX_P HELX_P2  AA2 GLY A 22  ? SER A 29  ? GLY A 20  SER A 27  1 ? 8  
HELX_P HELX_P3  AA3 THR A 37  ? VAL A 55  ? THR A 35  VAL A 53  1 ? 19 
HELX_P HELX_P4  AA4 ILE A 56  ? PRO A 58  ? ILE A 54  PRO A 56  5 ? 3  
HELX_P HELX_P5  AA5 LEU A 59  ? GLY A 67  ? LEU A 57  GLY A 65  1 ? 9  
HELX_P HELX_P6  AA6 GLY A 80  ? GLY A 91  ? GLY A 78  GLY A 89  1 ? 12 
HELX_P HELX_P7  AA7 GLY A 92  ? LEU A 96  ? GLY A 90  LEU A 94  5 ? 5  
HELX_P HELX_P8  AA8 ASP A 99  ? GLY A 103 ? ASP A 97  GLY A 101 5 ? 5  
HELX_P HELX_P9  AA9 PRO A 108 ? GLY A 144 ? PRO A 106 GLY A 142 1 ? 37 
HELX_P HELX_P10 AB1 THR A 145 ? GLY A 159 ? THR A 143 GLY A 157 1 ? 15 
HELX_P HELX_P11 AB2 ASP A 175 ? LEU A 179 ? ASP A 173 LEU A 177 5 ? 5  
HELX_P HELX_P12 AB3 GLN A 224 ? ILE A 229 ? GLN A 222 ILE A 227 5 ? 6  
HELX_P HELX_P13 AB4 LYS A 285 ? ARG A 323 ? LYS A 283 ARG A 321 1 ? 39 
HELX_P HELX_P14 AB5 PRO A 341 ? VAL A 344 ? PRO A 339 VAL A 342 5 ? 4  
HELX_P HELX_P15 AB6 HIS A 345 ? SER A 379 ? HIS A 343 SER A 377 1 ? 35 
HELX_P HELX_P16 AB7 ASP A 381 ? PHE A 418 ? ASP A 379 PHE A 416 1 ? 38 
HELX_P HELX_P17 AB8 GLY A 419 ? HIS A 427 ? GLY A 417 HIS A 425 5 ? 9  
HELX_P HELX_P18 AB9 GLY A 428 ? ILE A 438 ? GLY A 426 ILE A 436 1 ? 11 
HELX_P HELX_P19 AC1 SER A 439 ? LEU A 441 ? SER A 437 LEU A 439 5 ? 3  
HELX_P HELX_P20 AC2 THR A 445 ? LYS A 457 ? THR A 443 LYS A 455 1 ? 13 
HELX_P HELX_P21 AC3 VAL A 458 ? GLN A 462 ? VAL A 456 GLN A 460 5 ? 5  
HELX_P HELX_P22 AC4 GLY A 463 ? ASN A 480 ? GLY A 461 ASN A 478 1 ? 18 
HELX_P HELX_P23 AC5 ASN A 483 ? ALA A 485 ? ASN A 481 ALA A 483 5 ? 3  
HELX_P HELX_P24 AC6 VAL A 486 ? ASP A 514 ? VAL A 484 ASP A 512 1 ? 29 
HELX_P HELX_P25 AC7 ARG A 515 ? ALA A 551 ? ARG A 513 ALA A 549 1 ? 37 
HELX_P HELX_P26 AC8 GLU A 555 ? ILE A 573 ? GLU A 553 ILE A 571 1 ? 19 
HELX_P HELX_P27 AC9 ARG A 576 ? SER A 586 ? ARG A 574 SER A 584 1 ? 11 
HELX_P HELX_P28 AD1 ALA A 588 ? GLU A 593 ? ALA A 586 GLU A 591 1 ? 6  
HELX_P HELX_P29 AD2 ALA A 595 ? PHE A 599 ? ALA A 593 PHE A 597 5 ? 5  
HELX_P HELX_P30 AD3 PRO B 9   ? GLU B 19  ? PRO B 7   GLU B 17  1 ? 11 
HELX_P HELX_P31 AD4 GLY B 22  ? SER B 29  ? GLY B 20  SER B 27  1 ? 8  
HELX_P HELX_P32 AD5 THR B 37  ? VAL B 55  ? THR B 35  VAL B 53  1 ? 19 
HELX_P HELX_P33 AD6 ILE B 56  ? PRO B 58  ? ILE B 54  PRO B 56  5 ? 3  
HELX_P HELX_P34 AD7 LEU B 59  ? GLY B 67  ? LEU B 57  GLY B 65  1 ? 9  
HELX_P HELX_P35 AD8 GLY B 80  ? GLY B 91  ? GLY B 78  GLY B 89  1 ? 12 
HELX_P HELX_P36 AD9 GLY B 92  ? LEU B 96  ? GLY B 90  LEU B 94  5 ? 5  
HELX_P HELX_P37 AE1 ASP B 99  ? GLY B 103 ? ASP B 97  GLY B 101 5 ? 5  
HELX_P HELX_P38 AE2 PRO B 108 ? ASN B 123 ? PRO B 106 ASN B 121 1 ? 16 
HELX_P HELX_P39 AE3 ASN B 123 ? GLY B 144 ? ASN B 121 GLY B 142 1 ? 22 
HELX_P HELX_P40 AE4 THR B 145 ? TYR B 152 ? THR B 143 TYR B 150 1 ? 8  
HELX_P HELX_P41 AE5 TYR B 152 ? SER B 158 ? TYR B 150 SER B 156 1 ? 7  
HELX_P HELX_P42 AE6 ASP B 175 ? LEU B 179 ? ASP B 173 LEU B 177 5 ? 5  
HELX_P HELX_P43 AE7 GLN B 224 ? ILE B 229 ? GLN B 222 ILE B 227 5 ? 6  
HELX_P HELX_P44 AE8 LYS B 285 ? ARG B 323 ? LYS B 283 ARG B 321 1 ? 39 
HELX_P HELX_P45 AE9 PRO B 341 ? VAL B 344 ? PRO B 339 VAL B 342 5 ? 4  
HELX_P HELX_P46 AF1 HIS B 345 ? SER B 379 ? HIS B 343 SER B 377 1 ? 35 
HELX_P HELX_P47 AF2 ASP B 381 ? PHE B 418 ? ASP B 379 PHE B 416 1 ? 38 
HELX_P HELX_P48 AF3 GLY B 419 ? HIS B 427 ? GLY B 417 HIS B 425 5 ? 9  
HELX_P HELX_P49 AF4 GLY B 428 ? ILE B 438 ? GLY B 426 ILE B 436 1 ? 11 
HELX_P HELX_P50 AF5 SER B 439 ? LEU B 441 ? SER B 437 LEU B 439 5 ? 3  
HELX_P HELX_P51 AF6 THR B 445 ? ARG B 456 ? THR B 443 ARG B 454 1 ? 12 
HELX_P HELX_P52 AF7 VAL B 458 ? GLN B 462 ? VAL B 456 GLN B 460 5 ? 5  
HELX_P HELX_P53 AF8 GLY B 463 ? ASN B 480 ? GLY B 461 ASN B 478 1 ? 18 
HELX_P HELX_P54 AF9 ASN B 483 ? ALA B 485 ? ASN B 481 ALA B 483 5 ? 3  
HELX_P HELX_P55 AG1 VAL B 486 ? ASP B 514 ? VAL B 484 ASP B 512 1 ? 29 
HELX_P HELX_P56 AG2 ARG B 515 ? ALA B 551 ? ARG B 513 ALA B 549 1 ? 37 
HELX_P HELX_P57 AG3 GLU B 555 ? ILE B 573 ? GLU B 553 ILE B 571 1 ? 19 
HELX_P HELX_P58 AG4 ARG B 576 ? SER B 586 ? ARG B 574 SER B 584 1 ? 11 
HELX_P HELX_P59 AG5 ALA B 588 ? GLU B 593 ? ALA B 586 GLU B 591 1 ? 6  
HELX_P HELX_P60 AG6 ALA B 595 ? PHE B 599 ? ALA B 593 PHE B 597 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 5 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 6 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 69  ? SER A 71  ? THR A 67  SER A 69  
AA1 2 GLY A 74  ? LYS A 76  ? GLY A 72  LYS A 74  
AA2 1 TRP A 161 ? CYS A 166 ? TRP A 159 CYS A 164 
AA2 2 ASN A 210 ? ALA A 217 ? ASN A 208 ALA A 215 
AA2 3 SER A 230 ? PRO A 235 ? SER A 228 PRO A 233 
AA2 4 THR A 267 ? ILE A 280 ? THR A 265 ILE A 278 
AA2 5 TYR A 191 ? SER A 201 ? TYR A 189 SER A 199 
AA2 6 LYS A 182 ? PRO A 185 ? LYS A 180 PRO A 183 
AA3 1 TRP A 161 ? CYS A 166 ? TRP A 159 CYS A 164 
AA3 2 ASN A 210 ? ALA A 217 ? ASN A 208 ALA A 215 
AA3 3 SER A 230 ? PRO A 235 ? SER A 228 PRO A 233 
AA3 4 THR A 267 ? ILE A 280 ? THR A 265 ILE A 278 
AA3 5 VAL A 251 ? ILE A 256 ? VAL A 249 ILE A 254 
AA4 1 PHE A 237 ? PRO A 239 ? PHE A 235 PRO A 237 
AA4 2 ALA A 245 ? ARG A 248 ? ALA A 243 ARG A 246 
AA5 1 THR B 69  ? SER B 71  ? THR B 67  SER B 69  
AA5 2 GLY B 74  ? LYS B 76  ? GLY B 72  LYS B 74  
AA6 1 TRP B 161 ? CYS B 166 ? TRP B 159 CYS B 164 
AA6 2 ASN B 210 ? ALA B 217 ? ASN B 208 ALA B 215 
AA6 3 SER B 230 ? PRO B 235 ? SER B 228 PRO B 233 
AA6 4 THR B 267 ? ILE B 280 ? THR B 265 ILE B 278 
AA6 5 TYR B 191 ? SER B 201 ? TYR B 189 SER B 199 
AA6 6 LYS B 182 ? PRO B 185 ? LYS B 180 PRO B 183 
AA7 1 TRP B 161 ? CYS B 166 ? TRP B 159 CYS B 164 
AA7 2 ASN B 210 ? ALA B 217 ? ASN B 208 ALA B 215 
AA7 3 SER B 230 ? PRO B 235 ? SER B 228 PRO B 233 
AA7 4 THR B 267 ? ILE B 280 ? THR B 265 ILE B 278 
AA7 5 VAL B 251 ? ILE B 256 ? VAL B 249 ILE B 254 
AA8 1 PHE B 237 ? PRO B 239 ? PHE B 235 PRO B 237 
AA8 2 ALA B 245 ? ARG B 248 ? ALA B 243 ARG B 246 
# 
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 THR A 69  ? N THR A 67  O LYS A 76  ? O LYS A 74  
AA2 1 2 N THR A 162 ? N THR A 160 O VAL A 212 ? O VAL A 210 
AA2 2 3 N HIS A 213 ? N HIS A 211 O VAL A 234 ? O VAL A 232 
AA2 3 4 N LEU A 231 ? N LEU A 229 O ILE A 280 ? O ILE A 278 
AA2 4 5 O ALA A 275 ? O ALA A 273 N VAL A 193 ? N VAL A 191 
AA2 5 6 O THR A 194 ? O THR A 192 N LYS A 182 ? N LYS A 180 
AA3 1 2 N THR A 162 ? N THR A 160 O VAL A 212 ? O VAL A 210 
AA3 2 3 N HIS A 213 ? N HIS A 211 O VAL A 234 ? O VAL A 232 
AA3 3 4 N LEU A 231 ? N LEU A 229 O ILE A 280 ? O ILE A 278 
AA3 4 5 O ASN A 271 ? O ASN A 269 N SER A 252 ? N SER A 250 
AA4 1 2 N LEU A 238 ? N LEU A 236 O GLU A 247 ? O GLU A 245 
AA5 1 2 N THR B 69  ? N THR B 67  O LYS B 76  ? O LYS B 74  
AA6 1 2 N THR B 162 ? N THR B 160 O VAL B 212 ? O VAL B 210 
AA6 2 3 N ALA B 217 ? N ALA B 215 O SER B 230 ? O SER B 228 
AA6 3 4 N LEU B 231 ? N LEU B 229 O ILE B 280 ? O ILE B 278 
AA6 4 5 O GLY B 277 ? O GLY B 275 N TYR B 191 ? N TYR B 189 
AA6 5 6 O THR B 194 ? O THR B 192 N LYS B 182 ? N LYS B 180 
AA7 1 2 N THR B 162 ? N THR B 160 O VAL B 212 ? O VAL B 210 
AA7 2 3 N ALA B 217 ? N ALA B 215 O SER B 230 ? O SER B 228 
AA7 3 4 N LEU B 231 ? N LEU B 229 O ILE B 280 ? O ILE B 278 
AA7 4 5 O ASN B 271 ? O ASN B 269 N SER B 252 ? N SER B 250 
AA8 1 2 N LEU B 238 ? N LEU B 236 O GLU B 247 ? O GLU B 245 
# 
_pdbx_entry_details.entry_id                   8PNS 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 95  ? ? -106.28 51.16   
2  1 ASN A 121 ? ? -170.03 91.39   
3  1 HIS A 141 ? ? -140.13 -9.73   
4  1 LEU A 165 ? ? -104.10 -60.20  
5  1 ILE A 260 ? ? 35.27   51.27   
6  1 ASP A 271 ? ? -107.43 73.94   
7  1 MET A 324 ? ? 66.82   -167.71 
8  1 ALA B 34  ? ? -91.02  54.54   
9  1 ASN B 121 ? ? -165.52 93.33   
10 1 LEU B 165 ? ? -103.48 -62.43  
11 1 ALA B 248 ? ? -90.90  56.52   
12 1 ILE B 260 ? ? 39.29   48.68   
13 1 MET B 324 ? ? 67.65   -166.05 
14 1 ARG B 376 ? ? -140.62 -22.43  
# 
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 GLY -1 ? A GLY 1 
2 1 Y 1 A HIS 0  ? A HIS 2 
3 1 Y 1 A MET 1  ? A MET 3 
4 1 Y 1 B GLY -1 ? B GLY 1 
5 1 Y 1 B HIS 0  ? B HIS 2 
6 1 Y 1 B MET 1  ? B MET 3 
7 1 Y 1 B PRO 2  ? B PRO 4 
# 
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  
CO8 N1A    N Y N 74  
CO8 C2A    C Y N 75  
CO8 N3A    N Y N 76  
CO8 C4A    C Y N 77  
CO8 C5A    C Y N 78  
CO8 C6A    C Y N 79  
CO8 N6A    N N N 80  
CO8 N7A    N Y N 81  
CO8 C8A    C Y N 82  
CO8 N9A    N Y N 83  
CO8 C1B    C N R 84  
CO8 C2B    C N R 85  
CO8 O2B    O N N 86  
CO8 C3B    C N S 87  
CO8 O3B    O N N 88  
CO8 P3B    P N N 89  
CO8 O7A    O N N 90  
CO8 O8A    O N N 91  
CO8 O9A    O N N 92  
CO8 C4B    C N R 93  
CO8 O4B    O N N 94  
CO8 C5B    C N N 95  
CO8 O5B    O N N 96  
CO8 P1A    P N R 97  
CO8 O1A    O N N 98  
CO8 O2A    O N N 99  
CO8 O3A    O N N 100 
CO8 P2A    P N S 101 
CO8 O4A    O N N 102 
CO8 O5A    O N N 103 
CO8 O6A    O N N 104 
CO8 CBP    C N N 105 
CO8 CCP    C N N 106 
CO8 CDP    C N N 107 
CO8 CEP    C N N 108 
CO8 CAP    C N R 109 
CO8 OAP    O N N 110 
CO8 C9P    C N N 111 
CO8 O9P    O N N 112 
CO8 N8P    N N N 113 
CO8 C7P    C N N 114 
CO8 C6P    C N N 115 
CO8 C5P    C N N 116 
CO8 O5P    O N N 117 
CO8 N4P    N N N 118 
CO8 C3P    C N N 119 
CO8 C2P    C N N 120 
CO8 S1P    S N N 121 
CO8 "C1'"  C N N 122 
CO8 "O1'"  O N N 123 
CO8 "C2'"  C N N 124 
CO8 "C3'"  C N N 125 
CO8 "C4'"  C N N 126 
CO8 "C5'"  C N N 127 
CO8 "C6'"  C N N 128 
CO8 "C7'"  C N N 129 
CO8 "C8'"  C N N 130 
CO8 H2A    H N N 131 
CO8 H61A   H N N 132 
CO8 H62A   H N N 133 
CO8 H8A    H N N 134 
CO8 H1B    H N N 135 
CO8 H2B    H N N 136 
CO8 HO2A   H N N 137 
CO8 H3B    H N N 138 
CO8 HOA8   H N N 139 
CO8 HOA9   H N N 140 
CO8 H4B    H N N 141 
CO8 H51A   H N N 142 
CO8 H52A   H N N 143 
CO8 HOA2   H N N 144 
CO8 HOA5   H N N 145 
CO8 H121   H N N 146 
CO8 H122   H N N 147 
CO8 H131   H N N 148 
CO8 H132   H N N 149 
CO8 H133   H N N 150 
CO8 H141   H N N 151 
CO8 H142   H N N 152 
CO8 H143   H N N 153 
CO8 H10    H N N 154 
CO8 HO1    H N N 155 
CO8 HN8    H N N 156 
CO8 H71    H N N 157 
CO8 H72    H N N 158 
CO8 H61    H N N 159 
CO8 H62    H N N 160 
CO8 HN4    H N N 161 
CO8 H31    H N N 162 
CO8 H32    H N N 163 
CO8 H21    H N N 164 
CO8 H22    H N N 165 
CO8 "H2'1" H N N 166 
CO8 "H2'2" H N N 167 
CO8 "H3'1" H N N 168 
CO8 "H3'2" H N N 169 
CO8 "H4'1" H N N 170 
CO8 "H4'2" H N N 171 
CO8 "H5'1" H N N 172 
CO8 "H5'2" H N N 173 
CO8 "H6'1" H N N 174 
CO8 "H6'2" H N N 175 
CO8 "H7'1" H N N 176 
CO8 "H7'2" H N N 177 
CO8 "H8'1" H N N 178 
CO8 "H8'2" H N N 179 
CO8 "H8'3" H N N 180 
CYS N      N N N 181 
CYS CA     C N R 182 
CYS C      C N N 183 
CYS O      O N N 184 
CYS CB     C N N 185 
CYS SG     S N N 186 
CYS OXT    O N N 187 
CYS H      H N N 188 
CYS H2     H N N 189 
CYS HA     H N N 190 
CYS HB2    H N N 191 
CYS HB3    H N N 192 
CYS HG     H N N 193 
CYS HXT    H N N 194 
FAD PA     P N R 195 
FAD O1A    O N N 196 
FAD O2A    O N N 197 
FAD O5B    O N N 198 
FAD C5B    C N N 199 
FAD C4B    C N R 200 
FAD O4B    O N N 201 
FAD C3B    C N S 202 
FAD O3B    O N N 203 
FAD C2B    C N R 204 
FAD O2B    O N N 205 
FAD C1B    C N R 206 
FAD N9A    N Y N 207 
FAD C8A    C Y N 208 
FAD N7A    N Y N 209 
FAD C5A    C Y N 210 
FAD C6A    C Y N 211 
FAD N6A    N N N 212 
FAD N1A    N Y N 213 
FAD C2A    C Y N 214 
FAD N3A    N Y N 215 
FAD C4A    C Y N 216 
FAD N1     N N N 217 
FAD C2     C N N 218 
FAD O2     O N N 219 
FAD N3     N N N 220 
FAD C4     C N N 221 
FAD O4     O N N 222 
FAD C4X    C N N 223 
FAD N5     N N N 224 
FAD C5X    C Y N 225 
FAD C6     C Y N 226 
FAD C7     C Y N 227 
FAD C7M    C N N 228 
FAD C8     C Y N 229 
FAD C8M    C N N 230 
FAD C9     C Y N 231 
FAD C9A    C Y N 232 
FAD N10    N N N 233 
FAD C10    C N N 234 
FAD "C1'"  C N N 235 
FAD "C2'"  C N S 236 
FAD "O2'"  O N N 237 
FAD "C3'"  C N S 238 
FAD "O3'"  O N N 239 
FAD "C4'"  C N R 240 
FAD "O4'"  O N N 241 
FAD "C5'"  C N N 242 
FAD "O5'"  O N N 243 
FAD P      P N R 244 
FAD O1P    O N N 245 
FAD O2P    O N N 246 
FAD O3P    O N N 247 
FAD HOA2   H N N 248 
FAD H51A   H N N 249 
FAD H52A   H N N 250 
FAD H4B    H N N 251 
FAD H3B    H N N 252 
FAD HO3A   H N N 253 
FAD H2B    H N N 254 
FAD HO2A   H N N 255 
FAD H1B    H N N 256 
FAD H8A    H N N 257 
FAD H61A   H N N 258 
FAD H62A   H N N 259 
FAD H2A    H N N 260 
FAD HN3    H N N 261 
FAD H6     H N N 262 
FAD HM71   H N N 263 
FAD HM72   H N N 264 
FAD HM73   H N N 265 
FAD HM81   H N N 266 
FAD HM82   H N N 267 
FAD HM83   H N N 268 
FAD H9     H N N 269 
FAD "H1'1" H N N 270 
FAD "H1'2" H N N 271 
FAD "H2'"  H N N 272 
FAD "HO2'" H N N 273 
FAD "H3'"  H N N 274 
FAD "HO3'" H N N 275 
FAD "H4'"  H N N 276 
FAD "HO4'" H N N 277 
FAD "H5'1" H N N 278 
FAD "H5'2" H N N 279 
FAD HOP2   H N N 280 
GLN N      N N N 281 
GLN CA     C N S 282 
GLN C      C N N 283 
GLN O      O N N 284 
GLN CB     C N N 285 
GLN CG     C N N 286 
GLN CD     C N N 287 
GLN OE1    O N N 288 
GLN NE2    N N N 289 
GLN OXT    O N N 290 
GLN H      H N N 291 
GLN H2     H N N 292 
GLN HA     H N N 293 
GLN HB2    H N N 294 
GLN HB3    H N N 295 
GLN HG2    H N N 296 
GLN HG3    H N N 297 
GLN HE21   H N N 298 
GLN HE22   H N N 299 
GLN HXT    H N N 300 
GLU N      N N N 301 
GLU CA     C N S 302 
GLU C      C N N 303 
GLU O      O N N 304 
GLU CB     C N N 305 
GLU CG     C N N 306 
GLU CD     C N N 307 
GLU OE1    O N N 308 
GLU OE2    O N N 309 
GLU OXT    O N N 310 
GLU H      H N N 311 
GLU H2     H N N 312 
GLU HA     H N N 313 
GLU HB2    H N N 314 
GLU HB3    H N N 315 
GLU HG2    H N N 316 
GLU HG3    H N N 317 
GLU HE2    H N N 318 
GLU HXT    H N N 319 
GLY N      N N N 320 
GLY CA     C N N 321 
GLY C      C N N 322 
GLY O      O N N 323 
GLY OXT    O N N 324 
GLY H      H N N 325 
GLY H2     H N N 326 
GLY HA2    H N N 327 
GLY HA3    H N N 328 
GLY HXT    H N N 329 
HIS N      N N N 330 
HIS CA     C N S 331 
HIS C      C N N 332 
HIS O      O N N 333 
HIS CB     C N N 334 
HIS CG     C Y N 335 
HIS ND1    N Y N 336 
HIS CD2    C Y N 337 
HIS CE1    C Y N 338 
HIS NE2    N Y N 339 
HIS OXT    O N N 340 
HIS H      H N N 341 
HIS H2     H N N 342 
HIS HA     H N N 343 
HIS HB2    H N N 344 
HIS HB3    H N N 345 
HIS HD1    H N N 346 
HIS HD2    H N N 347 
HIS HE1    H N N 348 
HIS HE2    H N N 349 
HIS HXT    H N N 350 
HOH O      O N N 351 
HOH H1     H N N 352 
HOH H2     H N N 353 
ILE N      N N N 354 
ILE CA     C N S 355 
ILE C      C N N 356 
ILE O      O N N 357 
ILE CB     C N S 358 
ILE CG1    C N N 359 
ILE CG2    C N N 360 
ILE CD1    C N N 361 
ILE OXT    O N N 362 
ILE H      H N N 363 
ILE H2     H N N 364 
ILE HA     H N N 365 
ILE HB     H N N 366 
ILE HG12   H N N 367 
ILE HG13   H N N 368 
ILE HG21   H N N 369 
ILE HG22   H N N 370 
ILE HG23   H N N 371 
ILE HD11   H N N 372 
ILE HD12   H N N 373 
ILE HD13   H N N 374 
ILE HXT    H N N 375 
LEU N      N N N 376 
LEU CA     C N S 377 
LEU C      C N N 378 
LEU O      O N N 379 
LEU CB     C N N 380 
LEU CG     C N N 381 
LEU CD1    C N N 382 
LEU CD2    C N N 383 
LEU OXT    O N N 384 
LEU H      H N N 385 
LEU H2     H N N 386 
LEU HA     H N N 387 
LEU HB2    H N N 388 
LEU HB3    H N N 389 
LEU HG     H N N 390 
LEU HD11   H N N 391 
LEU HD12   H N N 392 
LEU HD13   H N N 393 
LEU HD21   H N N 394 
LEU HD22   H N N 395 
LEU HD23   H N N 396 
LEU HXT    H N N 397 
LYS N      N N N 398 
LYS CA     C N S 399 
LYS C      C N N 400 
LYS O      O N N 401 
LYS CB     C N N 402 
LYS CG     C N N 403 
LYS CD     C N N 404 
LYS CE     C N N 405 
LYS NZ     N N N 406 
LYS OXT    O N N 407 
LYS H      H N N 408 
LYS H2     H N N 409 
LYS HA     H N N 410 
LYS HB2    H N N 411 
LYS HB3    H N N 412 
LYS HG2    H N N 413 
LYS HG3    H N N 414 
LYS HD2    H N N 415 
LYS HD3    H N N 416 
LYS HE2    H N N 417 
LYS HE3    H N N 418 
LYS HZ1    H N N 419 
LYS HZ2    H N N 420 
LYS HZ3    H N N 421 
LYS HXT    H N N 422 
MET N      N N N 423 
MET CA     C N S 424 
MET C      C N N 425 
MET O      O N N 426 
MET CB     C N N 427 
MET CG     C N N 428 
MET SD     S N N 429 
MET CE     C N N 430 
MET OXT    O N N 431 
MET H      H N N 432 
MET H2     H N N 433 
MET HA     H N N 434 
MET HB2    H N N 435 
MET HB3    H N N 436 
MET HG2    H N N 437 
MET HG3    H N N 438 
MET HE1    H N N 439 
MET HE2    H N N 440 
MET HE3    H N N 441 
MET HXT    H N N 442 
PEG C1     C N N 443 
PEG O1     O N N 444 
PEG C2     C N N 445 
PEG O2     O N N 446 
PEG C3     C N N 447 
PEG C4     C N N 448 
PEG O4     O N N 449 
PEG H11    H N N 450 
PEG H12    H N N 451 
PEG HO1    H N N 452 
PEG H21    H N N 453 
PEG H22    H N N 454 
PEG H31    H N N 455 
PEG H32    H N N 456 
PEG H41    H N N 457 
PEG H42    H N N 458 
PEG HO4    H N N 459 
PHE N      N N N 460 
PHE CA     C N S 461 
PHE C      C N N 462 
PHE O      O N N 463 
PHE CB     C N N 464 
PHE CG     C Y N 465 
PHE CD1    C Y N 466 
PHE CD2    C Y N 467 
PHE CE1    C Y N 468 
PHE CE2    C Y N 469 
PHE CZ     C Y N 470 
PHE OXT    O N N 471 
PHE H      H N N 472 
PHE H2     H N N 473 
PHE HA     H N N 474 
PHE HB2    H N N 475 
PHE HB3    H N N 476 
PHE HD1    H N N 477 
PHE HD2    H N N 478 
PHE HE1    H N N 479 
PHE HE2    H N N 480 
PHE HZ     H N N 481 
PHE HXT    H N N 482 
PRO N      N N N 483 
PRO CA     C N S 484 
PRO C      C N N 485 
PRO O      O N N 486 
PRO CB     C N N 487 
PRO CG     C N N 488 
PRO CD     C N N 489 
PRO OXT    O N N 490 
PRO H      H N N 491 
PRO HA     H N N 492 
PRO HB2    H N N 493 
PRO HB3    H N N 494 
PRO HG2    H N N 495 
PRO HG3    H N N 496 
PRO HD2    H N N 497 
PRO HD3    H N N 498 
PRO HXT    H N N 499 
SER N      N N N 500 
SER CA     C N S 501 
SER C      C N N 502 
SER O      O N N 503 
SER CB     C N N 504 
SER OG     O N N 505 
SER OXT    O N N 506 
SER H      H N N 507 
SER H2     H N N 508 
SER HA     H N N 509 
SER HB2    H N N 510 
SER HB3    H N N 511 
SER HG     H N N 512 
SER HXT    H N N 513 
THR N      N N N 514 
THR CA     C N S 515 
THR C      C N N 516 
THR O      O N N 517 
THR CB     C N R 518 
THR OG1    O N N 519 
THR CG2    C N N 520 
THR OXT    O N N 521 
THR H      H N N 522 
THR H2     H N N 523 
THR HA     H N N 524 
THR HB     H N N 525 
THR HG1    H N N 526 
THR HG21   H N N 527 
THR HG22   H N N 528 
THR HG23   H N N 529 
THR HXT    H N N 530 
TRP N      N N N 531 
TRP CA     C N S 532 
TRP C      C N N 533 
TRP O      O N N 534 
TRP CB     C N N 535 
TRP CG     C Y N 536 
TRP CD1    C Y N 537 
TRP CD2    C Y N 538 
TRP NE1    N Y N 539 
TRP CE2    C Y N 540 
TRP CE3    C Y N 541 
TRP CZ2    C Y N 542 
TRP CZ3    C Y N 543 
TRP CH2    C Y N 544 
TRP OXT    O N N 545 
TRP H      H N N 546 
TRP H2     H N N 547 
TRP HA     H N N 548 
TRP HB2    H N N 549 
TRP HB3    H N N 550 
TRP HD1    H N N 551 
TRP HE1    H N N 552 
TRP HE3    H N N 553 
TRP HZ2    H N N 554 
TRP HZ3    H N N 555 
TRP HH2    H N N 556 
TRP HXT    H N N 557 
TYR N      N N N 558 
TYR CA     C N S 559 
TYR C      C N N 560 
TYR O      O N N 561 
TYR CB     C N N 562 
TYR CG     C Y N 563 
TYR CD1    C Y N 564 
TYR CD2    C Y N 565 
TYR CE1    C Y N 566 
TYR CE2    C Y N 567 
TYR CZ     C Y N 568 
TYR OH     O N N 569 
TYR OXT    O N N 570 
TYR H      H N N 571 
TYR H2     H N N 572 
TYR HA     H N N 573 
TYR HB2    H N N 574 
TYR HB3    H N N 575 
TYR HD1    H N N 576 
TYR HD2    H N N 577 
TYR HE1    H N N 578 
TYR HE2    H N N 579 
TYR HH     H N N 580 
TYR HXT    H N N 581 
VAL N      N N N 582 
VAL CA     C N S 583 
VAL C      C N N 584 
VAL O      O N N 585 
VAL CB     C N N 586 
VAL CG1    C N N 587 
VAL CG2    C N N 588 
VAL OXT    O N N 589 
VAL H      H N N 590 
VAL H2     H N N 591 
VAL HA     H N N 592 
VAL HB     H N N 593 
VAL HG11   H N N 594 
VAL HG12   H N N 595 
VAL HG13   H N N 596 
VAL HG21   H N N 597 
VAL HG22   H N N 598 
VAL HG23   H N N 599 
VAL HXT    H N N 600 
# 
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  
CO8 N1A   C2A    sing Y N 70  
CO8 N1A   C6A    doub Y N 71  
CO8 C2A   N3A    doub Y N 72  
CO8 C2A   H2A    sing N N 73  
CO8 N3A   C4A    sing Y N 74  
CO8 C4A   C5A    doub Y N 75  
CO8 C4A   N9A    sing Y N 76  
CO8 C5A   C6A    sing Y N 77  
CO8 C5A   N7A    sing Y N 78  
CO8 C6A   N6A    sing N N 79  
CO8 N6A   H61A   sing N N 80  
CO8 N6A   H62A   sing N N 81  
CO8 N7A   C8A    doub Y N 82  
CO8 C8A   N9A    sing Y N 83  
CO8 C8A   H8A    sing N N 84  
CO8 N9A   C1B    sing N N 85  
CO8 C1B   C2B    sing N N 86  
CO8 C1B   O4B    sing N N 87  
CO8 C1B   H1B    sing N N 88  
CO8 C2B   O2B    sing N N 89  
CO8 C2B   C3B    sing N N 90  
CO8 C2B   H2B    sing N N 91  
CO8 O2B   HO2A   sing N N 92  
CO8 C3B   O3B    sing N N 93  
CO8 C3B   C4B    sing N N 94  
CO8 C3B   H3B    sing N N 95  
CO8 O3B   P3B    sing N N 96  
CO8 P3B   O7A    doub N N 97  
CO8 P3B   O8A    sing N N 98  
CO8 P3B   O9A    sing N N 99  
CO8 O8A   HOA8   sing N N 100 
CO8 O9A   HOA9   sing N N 101 
CO8 C4B   O4B    sing N N 102 
CO8 C4B   C5B    sing N N 103 
CO8 C4B   H4B    sing N N 104 
CO8 C5B   O5B    sing N N 105 
CO8 C5B   H51A   sing N N 106 
CO8 C5B   H52A   sing N N 107 
CO8 O5B   P1A    sing N N 108 
CO8 P1A   O1A    doub N N 109 
CO8 P1A   O2A    sing N N 110 
CO8 P1A   O3A    sing N N 111 
CO8 O2A   HOA2   sing N N 112 
CO8 O3A   P2A    sing N N 113 
CO8 P2A   O4A    doub N N 114 
CO8 P2A   O5A    sing N N 115 
CO8 P2A   O6A    sing N N 116 
CO8 O5A   HOA5   sing N N 117 
CO8 O6A   CCP    sing N N 118 
CO8 CBP   CCP    sing N N 119 
CO8 CBP   CDP    sing N N 120 
CO8 CBP   CEP    sing N N 121 
CO8 CBP   CAP    sing N N 122 
CO8 CCP   H121   sing N N 123 
CO8 CCP   H122   sing N N 124 
CO8 CDP   H131   sing N N 125 
CO8 CDP   H132   sing N N 126 
CO8 CDP   H133   sing N N 127 
CO8 CEP   H141   sing N N 128 
CO8 CEP   H142   sing N N 129 
CO8 CEP   H143   sing N N 130 
CO8 CAP   OAP    sing N N 131 
CO8 CAP   C9P    sing N N 132 
CO8 CAP   H10    sing N N 133 
CO8 OAP   HO1    sing N N 134 
CO8 C9P   O9P    doub N N 135 
CO8 C9P   N8P    sing N N 136 
CO8 N8P   C7P    sing N N 137 
CO8 N8P   HN8    sing N N 138 
CO8 C7P   C6P    sing N N 139 
CO8 C7P   H71    sing N N 140 
CO8 C7P   H72    sing N N 141 
CO8 C6P   C5P    sing N N 142 
CO8 C6P   H61    sing N N 143 
CO8 C6P   H62    sing N N 144 
CO8 C5P   O5P    doub N N 145 
CO8 C5P   N4P    sing N N 146 
CO8 N4P   C3P    sing N N 147 
CO8 N4P   HN4    sing N N 148 
CO8 C3P   C2P    sing N N 149 
CO8 C3P   H31    sing N N 150 
CO8 C3P   H32    sing N N 151 
CO8 C2P   S1P    sing N N 152 
CO8 C2P   H21    sing N N 153 
CO8 C2P   H22    sing N N 154 
CO8 S1P   "C1'"  sing N N 155 
CO8 "C1'" "O1'"  doub N N 156 
CO8 "C1'" "C2'"  sing N N 157 
CO8 "C2'" "C3'"  sing N N 158 
CO8 "C2'" "H2'1" sing N N 159 
CO8 "C2'" "H2'2" sing N N 160 
CO8 "C3'" "C4'"  sing N N 161 
CO8 "C3'" "H3'1" sing N N 162 
CO8 "C3'" "H3'2" sing N N 163 
CO8 "C4'" "C5'"  sing N N 164 
CO8 "C4'" "H4'1" sing N N 165 
CO8 "C4'" "H4'2" sing N N 166 
CO8 "C5'" "C6'"  sing N N 167 
CO8 "C5'" "H5'1" sing N N 168 
CO8 "C5'" "H5'2" sing N N 169 
CO8 "C6'" "C7'"  sing N N 170 
CO8 "C6'" "H6'1" sing N N 171 
CO8 "C6'" "H6'2" sing N N 172 
CO8 "C7'" "C8'"  sing N N 173 
CO8 "C7'" "H7'1" sing N N 174 
CO8 "C7'" "H7'2" sing N N 175 
CO8 "C8'" "H8'1" sing N N 176 
CO8 "C8'" "H8'2" sing N N 177 
CO8 "C8'" "H8'3" sing N N 178 
CYS N     CA     sing N N 179 
CYS N     H      sing N N 180 
CYS N     H2     sing N N 181 
CYS CA    C      sing N N 182 
CYS CA    CB     sing N N 183 
CYS CA    HA     sing N N 184 
CYS C     O      doub N N 185 
CYS C     OXT    sing N N 186 
CYS CB    SG     sing N N 187 
CYS CB    HB2    sing N N 188 
CYS CB    HB3    sing N N 189 
CYS SG    HG     sing N N 190 
CYS OXT   HXT    sing N N 191 
FAD PA    O1A    doub N N 192 
FAD PA    O2A    sing N N 193 
FAD PA    O5B    sing N N 194 
FAD PA    O3P    sing N N 195 
FAD O2A   HOA2   sing N N 196 
FAD O5B   C5B    sing N N 197 
FAD C5B   C4B    sing N N 198 
FAD C5B   H51A   sing N N 199 
FAD C5B   H52A   sing N N 200 
FAD C4B   O4B    sing N N 201 
FAD C4B   C3B    sing N N 202 
FAD C4B   H4B    sing N N 203 
FAD O4B   C1B    sing N N 204 
FAD C3B   O3B    sing N N 205 
FAD C3B   C2B    sing N N 206 
FAD C3B   H3B    sing N N 207 
FAD O3B   HO3A   sing N N 208 
FAD C2B   O2B    sing N N 209 
FAD C2B   C1B    sing N N 210 
FAD C2B   H2B    sing N N 211 
FAD O2B   HO2A   sing N N 212 
FAD C1B   N9A    sing N N 213 
FAD C1B   H1B    sing N N 214 
FAD N9A   C8A    sing Y N 215 
FAD N9A   C4A    sing Y N 216 
FAD C8A   N7A    doub Y N 217 
FAD C8A   H8A    sing N N 218 
FAD N7A   C5A    sing Y N 219 
FAD C5A   C6A    sing Y N 220 
FAD C5A   C4A    doub Y N 221 
FAD C6A   N6A    sing N N 222 
FAD C6A   N1A    doub Y N 223 
FAD N6A   H61A   sing N N 224 
FAD N6A   H62A   sing N N 225 
FAD N1A   C2A    sing Y N 226 
FAD C2A   N3A    doub Y N 227 
FAD C2A   H2A    sing N N 228 
FAD N3A   C4A    sing Y N 229 
FAD N1    C2     sing N N 230 
FAD N1    C10    doub N N 231 
FAD C2    O2     doub N N 232 
FAD C2    N3     sing N N 233 
FAD N3    C4     sing N N 234 
FAD N3    HN3    sing N N 235 
FAD C4    O4     doub N N 236 
FAD C4    C4X    sing N N 237 
FAD C4X   N5     doub N N 238 
FAD C4X   C10    sing N N 239 
FAD N5    C5X    sing N N 240 
FAD C5X   C6     doub Y N 241 
FAD C5X   C9A    sing Y N 242 
FAD C6    C7     sing Y N 243 
FAD C6    H6     sing N N 244 
FAD C7    C7M    sing N N 245 
FAD C7    C8     doub Y N 246 
FAD C7M   HM71   sing N N 247 
FAD C7M   HM72   sing N N 248 
FAD C7M   HM73   sing N N 249 
FAD C8    C8M    sing N N 250 
FAD C8    C9     sing Y N 251 
FAD C8M   HM81   sing N N 252 
FAD C8M   HM82   sing N N 253 
FAD C8M   HM83   sing N N 254 
FAD C9    C9A    doub Y N 255 
FAD C9    H9     sing N N 256 
FAD C9A   N10    sing N N 257 
FAD N10   C10    sing N N 258 
FAD N10   "C1'"  sing N N 259 
FAD "C1'" "C2'"  sing N N 260 
FAD "C1'" "H1'1" sing N N 261 
FAD "C1'" "H1'2" sing N N 262 
FAD "C2'" "O2'"  sing N N 263 
FAD "C2'" "C3'"  sing N N 264 
FAD "C2'" "H2'"  sing N N 265 
FAD "O2'" "HO2'" sing N N 266 
FAD "C3'" "O3'"  sing N N 267 
FAD "C3'" "C4'"  sing N N 268 
FAD "C3'" "H3'"  sing N N 269 
FAD "O3'" "HO3'" sing N N 270 
FAD "C4'" "O4'"  sing N N 271 
FAD "C4'" "C5'"  sing N N 272 
FAD "C4'" "H4'"  sing N N 273 
FAD "O4'" "HO4'" sing N N 274 
FAD "C5'" "O5'"  sing N N 275 
FAD "C5'" "H5'1" sing N N 276 
FAD "C5'" "H5'2" sing N N 277 
FAD "O5'" P      sing N N 278 
FAD P     O1P    doub N N 279 
FAD P     O2P    sing N N 280 
FAD P     O3P    sing N N 281 
FAD O2P   HOP2   sing N N 282 
GLN N     CA     sing N N 283 
GLN N     H      sing N N 284 
GLN N     H2     sing N N 285 
GLN CA    C      sing N N 286 
GLN CA    CB     sing N N 287 
GLN CA    HA     sing N N 288 
GLN C     O      doub N N 289 
GLN C     OXT    sing N N 290 
GLN CB    CG     sing N N 291 
GLN CB    HB2    sing N N 292 
GLN CB    HB3    sing N N 293 
GLN CG    CD     sing N N 294 
GLN CG    HG2    sing N N 295 
GLN CG    HG3    sing N N 296 
GLN CD    OE1    doub N N 297 
GLN CD    NE2    sing N N 298 
GLN NE2   HE21   sing N N 299 
GLN NE2   HE22   sing N N 300 
GLN OXT   HXT    sing N N 301 
GLU N     CA     sing N N 302 
GLU N     H      sing N N 303 
GLU N     H2     sing N N 304 
GLU CA    C      sing N N 305 
GLU CA    CB     sing N N 306 
GLU CA    HA     sing N N 307 
GLU C     O      doub N N 308 
GLU C     OXT    sing N N 309 
GLU CB    CG     sing N N 310 
GLU CB    HB2    sing N N 311 
GLU CB    HB3    sing N N 312 
GLU CG    CD     sing N N 313 
GLU CG    HG2    sing N N 314 
GLU CG    HG3    sing N N 315 
GLU CD    OE1    doub N N 316 
GLU CD    OE2    sing N N 317 
GLU OE2   HE2    sing N N 318 
GLU OXT   HXT    sing N N 319 
GLY N     CA     sing N N 320 
GLY N     H      sing N N 321 
GLY N     H2     sing N N 322 
GLY CA    C      sing N N 323 
GLY CA    HA2    sing N N 324 
GLY CA    HA3    sing N N 325 
GLY C     O      doub N N 326 
GLY C     OXT    sing N N 327 
GLY OXT   HXT    sing N N 328 
HIS N     CA     sing N N 329 
HIS N     H      sing N N 330 
HIS N     H2     sing N N 331 
HIS CA    C      sing N N 332 
HIS CA    CB     sing N N 333 
HIS CA    HA     sing N N 334 
HIS C     O      doub N N 335 
HIS C     OXT    sing N N 336 
HIS CB    CG     sing N N 337 
HIS CB    HB2    sing N N 338 
HIS CB    HB3    sing N N 339 
HIS CG    ND1    sing Y N 340 
HIS CG    CD2    doub Y N 341 
HIS ND1   CE1    doub Y N 342 
HIS ND1   HD1    sing N N 343 
HIS CD2   NE2    sing Y N 344 
HIS CD2   HD2    sing N N 345 
HIS CE1   NE2    sing Y N 346 
HIS CE1   HE1    sing N N 347 
HIS NE2   HE2    sing N N 348 
HIS OXT   HXT    sing N N 349 
HOH O     H1     sing N N 350 
HOH O     H2     sing N N 351 
ILE N     CA     sing N N 352 
ILE N     H      sing N N 353 
ILE N     H2     sing N N 354 
ILE CA    C      sing N N 355 
ILE CA    CB     sing N N 356 
ILE CA    HA     sing N N 357 
ILE C     O      doub N N 358 
ILE C     OXT    sing N N 359 
ILE CB    CG1    sing N N 360 
ILE CB    CG2    sing N N 361 
ILE CB    HB     sing N N 362 
ILE CG1   CD1    sing N N 363 
ILE CG1   HG12   sing N N 364 
ILE CG1   HG13   sing N N 365 
ILE CG2   HG21   sing N N 366 
ILE CG2   HG22   sing N N 367 
ILE CG2   HG23   sing N N 368 
ILE CD1   HD11   sing N N 369 
ILE CD1   HD12   sing N N 370 
ILE CD1   HD13   sing N N 371 
ILE OXT   HXT    sing N N 372 
LEU N     CA     sing N N 373 
LEU N     H      sing N N 374 
LEU N     H2     sing N N 375 
LEU CA    C      sing N N 376 
LEU CA    CB     sing N N 377 
LEU CA    HA     sing N N 378 
LEU C     O      doub N N 379 
LEU C     OXT    sing N N 380 
LEU CB    CG     sing N N 381 
LEU CB    HB2    sing N N 382 
LEU CB    HB3    sing N N 383 
LEU CG    CD1    sing N N 384 
LEU CG    CD2    sing N N 385 
LEU CG    HG     sing N N 386 
LEU CD1   HD11   sing N N 387 
LEU CD1   HD12   sing N N 388 
LEU CD1   HD13   sing N N 389 
LEU CD2   HD21   sing N N 390 
LEU CD2   HD22   sing N N 391 
LEU CD2   HD23   sing N N 392 
LEU OXT   HXT    sing N N 393 
LYS N     CA     sing N N 394 
LYS N     H      sing N N 395 
LYS N     H2     sing N N 396 
LYS CA    C      sing N N 397 
LYS CA    CB     sing N N 398 
LYS CA    HA     sing N N 399 
LYS C     O      doub N N 400 
LYS C     OXT    sing N N 401 
LYS CB    CG     sing N N 402 
LYS CB    HB2    sing N N 403 
LYS CB    HB3    sing N N 404 
LYS CG    CD     sing N N 405 
LYS CG    HG2    sing N N 406 
LYS CG    HG3    sing N N 407 
LYS CD    CE     sing N N 408 
LYS CD    HD2    sing N N 409 
LYS CD    HD3    sing N N 410 
LYS CE    NZ     sing N N 411 
LYS CE    HE2    sing N N 412 
LYS CE    HE3    sing N N 413 
LYS NZ    HZ1    sing N N 414 
LYS NZ    HZ2    sing N N 415 
LYS NZ    HZ3    sing N N 416 
LYS OXT   HXT    sing N N 417 
MET N     CA     sing N N 418 
MET N     H      sing N N 419 
MET N     H2     sing N N 420 
MET CA    C      sing N N 421 
MET CA    CB     sing N N 422 
MET CA    HA     sing N N 423 
MET C     O      doub N N 424 
MET C     OXT    sing N N 425 
MET CB    CG     sing N N 426 
MET CB    HB2    sing N N 427 
MET CB    HB3    sing N N 428 
MET CG    SD     sing N N 429 
MET CG    HG2    sing N N 430 
MET CG    HG3    sing N N 431 
MET SD    CE     sing N N 432 
MET CE    HE1    sing N N 433 
MET CE    HE2    sing N N 434 
MET CE    HE3    sing N N 435 
MET OXT   HXT    sing N N 436 
PEG C1    O1     sing N N 437 
PEG C1    C2     sing N N 438 
PEG C1    H11    sing N N 439 
PEG C1    H12    sing N N 440 
PEG O1    HO1    sing N N 441 
PEG C2    O2     sing N N 442 
PEG C2    H21    sing N N 443 
PEG C2    H22    sing N N 444 
PEG O2    C3     sing N N 445 
PEG C3    C4     sing N N 446 
PEG C3    H31    sing N N 447 
PEG C3    H32    sing N N 448 
PEG C4    O4     sing N N 449 
PEG C4    H41    sing N N 450 
PEG C4    H42    sing N N 451 
PEG O4    HO4    sing N N 452 
PHE N     CA     sing N N 453 
PHE N     H      sing N N 454 
PHE N     H2     sing N N 455 
PHE CA    C      sing N N 456 
PHE CA    CB     sing N N 457 
PHE CA    HA     sing N N 458 
PHE C     O      doub N N 459 
PHE C     OXT    sing N N 460 
PHE CB    CG     sing N N 461 
PHE CB    HB2    sing N N 462 
PHE CB    HB3    sing N N 463 
PHE CG    CD1    doub Y N 464 
PHE CG    CD2    sing Y N 465 
PHE CD1   CE1    sing Y N 466 
PHE CD1   HD1    sing N N 467 
PHE CD2   CE2    doub Y N 468 
PHE CD2   HD2    sing N N 469 
PHE CE1   CZ     doub Y N 470 
PHE CE1   HE1    sing N N 471 
PHE CE2   CZ     sing Y N 472 
PHE CE2   HE2    sing N N 473 
PHE CZ    HZ     sing N N 474 
PHE OXT   HXT    sing N N 475 
PRO N     CA     sing N N 476 
PRO N     CD     sing N N 477 
PRO N     H      sing N N 478 
PRO CA    C      sing N N 479 
PRO CA    CB     sing N N 480 
PRO CA    HA     sing N N 481 
PRO C     O      doub N N 482 
PRO C     OXT    sing N N 483 
PRO CB    CG     sing N N 484 
PRO CB    HB2    sing N N 485 
PRO CB    HB3    sing N N 486 
PRO CG    CD     sing N N 487 
PRO CG    HG2    sing N N 488 
PRO CG    HG3    sing N N 489 
PRO CD    HD2    sing N N 490 
PRO CD    HD3    sing N N 491 
PRO OXT   HXT    sing N N 492 
SER N     CA     sing N N 493 
SER N     H      sing N N 494 
SER N     H2     sing N N 495 
SER CA    C      sing N N 496 
SER CA    CB     sing N N 497 
SER CA    HA     sing N N 498 
SER C     O      doub N N 499 
SER C     OXT    sing N N 500 
SER CB    OG     sing N N 501 
SER CB    HB2    sing N N 502 
SER CB    HB3    sing N N 503 
SER OG    HG     sing N N 504 
SER OXT   HXT    sing N N 505 
THR N     CA     sing N N 506 
THR N     H      sing N N 507 
THR N     H2     sing N N 508 
THR CA    C      sing N N 509 
THR CA    CB     sing N N 510 
THR CA    HA     sing N N 511 
THR C     O      doub N N 512 
THR C     OXT    sing N N 513 
THR CB    OG1    sing N N 514 
THR CB    CG2    sing N N 515 
THR CB    HB     sing N N 516 
THR OG1   HG1    sing N N 517 
THR CG2   HG21   sing N N 518 
THR CG2   HG22   sing N N 519 
THR CG2   HG23   sing N N 520 
THR OXT   HXT    sing N N 521 
TRP N     CA     sing N N 522 
TRP N     H      sing N N 523 
TRP N     H2     sing N N 524 
TRP CA    C      sing N N 525 
TRP CA    CB     sing N N 526 
TRP CA    HA     sing N N 527 
TRP C     O      doub N N 528 
TRP C     OXT    sing N N 529 
TRP CB    CG     sing N N 530 
TRP CB    HB2    sing N N 531 
TRP CB    HB3    sing N N 532 
TRP CG    CD1    doub Y N 533 
TRP CG    CD2    sing Y N 534 
TRP CD1   NE1    sing Y N 535 
TRP CD1   HD1    sing N N 536 
TRP CD2   CE2    doub Y N 537 
TRP CD2   CE3    sing Y N 538 
TRP NE1   CE2    sing Y N 539 
TRP NE1   HE1    sing N N 540 
TRP CE2   CZ2    sing Y N 541 
TRP CE3   CZ3    doub Y N 542 
TRP CE3   HE3    sing N N 543 
TRP CZ2   CH2    doub Y N 544 
TRP CZ2   HZ2    sing N N 545 
TRP CZ3   CH2    sing Y N 546 
TRP CZ3   HZ3    sing N N 547 
TRP CH2   HH2    sing N N 548 
TRP OXT   HXT    sing N N 549 
TYR N     CA     sing N N 550 
TYR N     H      sing N N 551 
TYR N     H2     sing N N 552 
TYR CA    C      sing N N 553 
TYR CA    CB     sing N N 554 
TYR CA    HA     sing N N 555 
TYR C     O      doub N N 556 
TYR C     OXT    sing N N 557 
TYR CB    CG     sing N N 558 
TYR CB    HB2    sing N N 559 
TYR CB    HB3    sing N N 560 
TYR CG    CD1    doub Y N 561 
TYR CG    CD2    sing Y N 562 
TYR CD1   CE1    sing Y N 563 
TYR CD1   HD1    sing N N 564 
TYR CD2   CE2    doub Y N 565 
TYR CD2   HD2    sing N N 566 
TYR CE1   CZ     doub Y N 567 
TYR CE1   HE1    sing N N 568 
TYR CE2   CZ     sing Y N 569 
TYR CE2   HE2    sing N N 570 
TYR CZ    OH     sing N N 571 
TYR OH    HH     sing N N 572 
TYR OXT   HXT    sing N N 573 
VAL N     CA     sing N N 574 
VAL N     H      sing N N 575 
VAL N     H2     sing N N 576 
VAL CA    C      sing N N 577 
VAL CA    CB     sing N N 578 
VAL CA    HA     sing N N 579 
VAL C     O      doub N N 580 
VAL C     OXT    sing N N 581 
VAL CB    CG1    sing N N 582 
VAL CB    CG2    sing N N 583 
VAL CB    HB     sing N N 584 
VAL CG1   HG11   sing N N 585 
VAL CG1   HG12   sing N N 586 
VAL CG1   HG13   sing N N 587 
VAL CG2   HG21   sing N N 588 
VAL CG2   HG22   sing N N 589 
VAL CG2   HG23   sing N N 590 
VAL OXT   HXT    sing N N 591 
# 
_pdbx_audit_support.funding_organization   'Cystic Fibrosis Trust' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           SRC01 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6KPT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8PNS 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.006414 
_atom_sites.fract_transf_matrix[1][2]   0.003703 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007406 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.010049 
_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 
P 
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     . PRO A 1 4   ? 24.172  -45.674 11.677  1.00 72.41  ? 2   PRO A N     1 
ATOM   2    C CA    . PRO A 1 4   ? 24.052  -46.190 10.304  1.00 73.69  ? 2   PRO A CA    1 
ATOM   3    C C     . PRO A 1 4   ? 22.776  -45.701 9.599   1.00 61.29  ? 2   PRO A C     1 
ATOM   4    O O     . PRO A 1 4   ? 21.711  -45.950 10.110  1.00 67.14  ? 2   PRO A O     1 
ATOM   5    C CB    . PRO A 1 4   ? 24.045  -47.709 10.509  1.00 68.97  ? 2   PRO A CB    1 
ATOM   6    C CG    . PRO A 1 4   ? 24.986  -47.899 11.662  1.00 72.56  ? 2   PRO A CG    1 
ATOM   7    C CD    . PRO A 1 4   ? 24.697  -46.717 12.564  1.00 73.83  ? 2   PRO A CD    1 
ATOM   8    N N     . ASP A 1 5   ? 22.922  -45.015 8.466   1.00 56.43  ? 3   ASP A N     1 
ATOM   9    C CA    . ASP A 1 5   ? 21.763  -44.495 7.676   1.00 50.10  ? 3   ASP A CA    1 
ATOM   10   C C     . ASP A 1 5   ? 21.313  -45.530 6.640   1.00 43.20  ? 3   ASP A C     1 
ATOM   11   O O     . ASP A 1 5   ? 22.084  -46.431 6.387   1.00 40.71  ? 3   ASP A O     1 
ATOM   12   C CB    . ASP A 1 5   ? 22.144  -43.217 6.934   1.00 53.54  ? 3   ASP A CB    1 
ATOM   13   C CG    . ASP A 1 5   ? 22.571  -42.096 7.867   1.00 58.06  ? 3   ASP A CG    1 
ATOM   14   O OD1   . ASP A 1 5   ? 21.746  -41.688 8.704   1.00 59.14  ? 3   ASP A OD1   1 
ATOM   15   O OD2   . ASP A 1 5   ? 23.731  -41.658 7.764   1.00 62.80  ? 3   ASP A OD2   1 
ATOM   16   N N     . TYR A 1 6   ? 20.143  -45.365 6.007   1.00 40.11  ? 4   TYR A N     1 
ATOM   17   C CA    . TYR A 1 6   ? 19.623  -46.289 4.961   1.00 36.40  ? 4   TYR A CA    1 
ATOM   18   C C     . TYR A 1 6   ? 20.724  -46.674 3.967   1.00 35.83  ? 4   TYR A C     1 
ATOM   19   O O     . TYR A 1 6   ? 21.358  -45.771 3.415   1.00 34.96  ? 4   TYR A O     1 
ATOM   20   C CB    . TYR A 1 6   ? 18.478  -45.697 4.142   1.00 33.27  ? 4   TYR A CB    1 
ATOM   21   C CG    . TYR A 1 6   ? 18.039  -46.619 3.033   1.00 31.12  ? 4   TYR A CG    1 
ATOM   22   C CD1   . TYR A 1 6   ? 17.527  -47.871 3.309   1.00 30.92  ? 4   TYR A CD1   1 
ATOM   23   C CD2   . TYR A 1 6   ? 18.195  -46.266 1.698   1.00 31.21  ? 4   TYR A CD2   1 
ATOM   24   C CE1   . TYR A 1 6   ? 17.169  -48.742 2.284   1.00 35.39  ? 4   TYR A CE1   1 
ATOM   25   C CE2   . TYR A 1 6   ? 17.812  -47.105 0.667   1.00 29.93  ? 4   TYR A CE2   1 
ATOM   26   C CZ    . TYR A 1 6   ? 17.300  -48.351 0.962   1.00 31.21  ? 4   TYR A CZ    1 
ATOM   27   O OH    . TYR A 1 6   ? 16.935  -49.190 -0.051  1.00 35.11  ? 4   TYR A OH    1 
ATOM   28   N N     . LYS A 1 7   ? 20.918  -47.978 3.755   1.00 34.20  ? 5   LYS A N     1 
ATOM   29   C CA    . LYS A 1 7   ? 21.822  -48.562 2.739   1.00 38.94  ? 5   LYS A CA    1 
ATOM   30   C C     . LYS A 1 7   ? 20.981  -49.456 1.818   1.00 37.11  ? 5   LYS A C     1 
ATOM   31   O O     . LYS A 1 7   ? 20.375  -50.406 2.334   1.00 32.56  ? 5   LYS A O     1 
ATOM   32   C CB    . LYS A 1 7   ? 22.936  -49.343 3.439   1.00 48.83  ? 5   LYS A CB    1 
ATOM   33   C CG    . LYS A 1 7   ? 24.149  -49.690 2.579   1.00 62.88  ? 5   LYS A CG    1 
ATOM   34   C CD    . LYS A 1 7   ? 24.893  -48.487 1.994   1.00 75.94  ? 5   LYS A CD    1 
ATOM   35   C CE    . LYS A 1 7   ? 25.063  -47.328 2.966   1.00 82.51  ? 5   LYS A CE    1 
ATOM   36   N NZ    . LYS A 1 7   ? 25.841  -46.210 2.374   1.00 84.07  ? 5   LYS A NZ    1 
ATOM   37   N N     . ALA A 1 8   ? 20.900  -49.152 0.517   1.00 32.24  ? 6   ALA A N     1 
ATOM   38   C CA    . ALA A 1 8   ? 20.195  -50.007 -0.459  1.00 32.28  ? 6   ALA A CA    1 
ATOM   39   C C     . ALA A 1 8   ? 20.745  -51.424 -0.403  1.00 30.35  ? 6   ALA A C     1 
ATOM   40   O O     . ALA A 1 8   ? 21.952  -51.613 -0.409  1.00 32.68  ? 6   ALA A O     1 
ATOM   41   C CB    . ALA A 1 8   ? 20.321  -49.452 -1.846  1.00 34.93  ? 6   ALA A CB    1 
ATOM   42   N N     . PRO A 1 9   ? 19.890  -52.471 -0.355  1.00 29.91  ? 7   PRO A N     1 
ATOM   43   C CA    . PRO A 1 9   ? 20.379  -53.848 -0.387  1.00 30.77  ? 7   PRO A CA    1 
ATOM   44   C C     . PRO A 1 9   ? 20.633  -54.318 -1.818  1.00 33.62  ? 7   PRO A C     1 
ATOM   45   O O     . PRO A 1 9   ? 20.183  -55.391 -2.134  1.00 34.74  ? 7   PRO A O     1 
ATOM   46   C CB    . PRO A 1 9   ? 19.251  -54.678 0.233   1.00 28.91  ? 7   PRO A CB    1 
ATOM   47   C CG    . PRO A 1 9   ? 17.999  -53.848 0.014   1.00 29.47  ? 7   PRO A CG    1 
ATOM   48   C CD    . PRO A 1 9   ? 18.425  -52.401 -0.207  1.00 29.63  ? 7   PRO A CD    1 
ATOM   49   N N     . LEU A 1 10  ? 21.410  -53.573 -2.600  1.00 33.55  ? 8   LEU A N     1 
ATOM   50   C CA    . LEU A 1 10  ? 21.702  -53.920 -4.016  1.00 33.90  ? 8   LEU A CA    1 
ATOM   51   C C     . LEU A 1 10  ? 22.266  -55.342 -4.171  1.00 36.07  ? 8   LEU A C     1 
ATOM   52   O O     . LEU A 1 10  ? 21.856  -56.006 -5.116  1.00 38.09  ? 8   LEU A O     1 
ATOM   53   C CB    . LEU A 1 10  ? 22.646  -52.859 -4.585  1.00 32.89  ? 8   LEU A CB    1 
ATOM   54   C CG    . LEU A 1 10  ? 21.974  -51.558 -5.013  1.00 30.66  ? 8   LEU A CG    1 
ATOM   55   C CD1   . LEU A 1 10  ? 23.002  -50.551 -5.498  1.00 33.21  ? 8   LEU A CD1   1 
ATOM   56   C CD2   . LEU A 1 10  ? 20.932  -51.817 -6.087  1.00 33.17  ? 8   LEU A CD2   1 
ATOM   57   N N     . ARG A 1 11  ? 23.160  -55.792 -3.287  1.00 38.96  ? 9   ARG A N     1 
ATOM   58   C CA    . ARG A 1 11  ? 23.780  -57.140 -3.491  1.00 40.79  ? 9   ARG A CA    1 
ATOM   59   C C     . ARG A 1 11  ? 22.688  -58.216 -3.441  1.00 39.65  ? 9   ARG A C     1 
ATOM   60   O O     . ARG A 1 11  ? 22.797  -59.239 -4.198  1.00 33.01  ? 9   ARG A O     1 
ATOM   61   C CB    . ARG A 1 11  ? 24.877  -57.461 -2.465  1.00 39.06  ? 9   ARG A CB    1 
ATOM   62   C CG    . ARG A 1 11  ? 25.559  -58.805 -2.681  1.00 41.88  ? 9   ARG A CG    1 
ATOM   63   C CD    . ARG A 1 11  ? 26.215  -58.982 -4.056  1.00 42.12  ? 9   ARG A CD    1 
ATOM   64   N NE    . ARG A 1 11  ? 26.666  -60.365 -4.241  1.00 45.38  ? 9   ARG A NE    1 
ATOM   65   C CZ    . ARG A 1 11  ? 25.947  -61.358 -4.780  1.00 42.76  ? 9   ARG A CZ    1 
ATOM   66   N NH1   . ARG A 1 11  ? 24.720  -61.136 -5.224  1.00 38.50  ? 9   ARG A NH1   1 
ATOM   67   N NH2   . ARG A 1 11  ? 26.460  -62.580 -4.850  1.00 44.26  ? 9   ARG A NH2   1 
ATOM   68   N N     . ASP A 1 12  ? 21.682  -58.005 -2.584  1.00 37.14  ? 10  ASP A N     1 
ATOM   69   C CA    . ASP A 1 12  ? 20.605  -59.006 -2.408  1.00 36.95  ? 10  ASP A CA    1 
ATOM   70   C C     . ASP A 1 12  ? 19.617  -58.859 -3.565  1.00 36.02  ? 10  ASP A C     1 
ATOM   71   O O     . ASP A 1 12  ? 19.111  -59.894 -4.027  1.00 33.44  ? 10  ASP A O     1 
ATOM   72   C CB    . ASP A 1 12  ? 19.916  -58.916 -1.052  1.00 35.93  ? 10  ASP A CB    1 
ATOM   73   C CG    . ASP A 1 12  ? 19.266  -60.248 -0.709  1.00 38.44  ? 10  ASP A CG    1 
ATOM   74   O OD1   . ASP A 1 12  ? 20.010  -61.224 -0.426  1.00 44.62  ? 10  ASP A OD1   1 
ATOM   75   O OD2   . ASP A 1 12  ? 18.034  -60.320 -0.773  1.00 38.48  ? 10  ASP A OD2   1 
ATOM   76   N N     . ILE A 1 13  ? 19.381  -57.632 -4.030  1.00 32.18  ? 11  ILE A N     1 
ATOM   77   C CA    . ILE A 1 13  ? 18.475  -57.387 -5.184  1.00 33.09  ? 11  ILE A CA    1 
ATOM   78   C C     . ILE A 1 13  ? 19.078  -58.073 -6.412  1.00 36.33  ? 11  ILE A C     1 
ATOM   79   O O     . ILE A 1 13  ? 18.318  -58.730 -7.118  1.00 38.19  ? 11  ILE A O     1 
ATOM   80   C CB    . ILE A 1 13  ? 18.249  -55.892 -5.402  1.00 32.78  ? 11  ILE A CB    1 
ATOM   81   C CG1   . ILE A 1 13  ? 17.316  -55.309 -4.340  1.00 32.48  ? 11  ILE A CG1   1 
ATOM   82   C CG2   . ILE A 1 13  ? 17.738  -55.630 -6.804  1.00 33.32  ? 11  ILE A CG2   1 
ATOM   83   C CD1   . ILE A 1 13  ? 17.305  -53.793 -4.322  1.00 33.67  ? 11  ILE A CD1   1 
ATOM   84   N N     . ARG A 1 14  ? 20.393  -58.006 -6.587  1.00 36.48  ? 12  ARG A N     1 
ATOM   85   C CA    . ARG A 1 14  ? 21.077  -58.668 -7.727  1.00 42.02  ? 12  ARG A CA    1 
ATOM   86   C C     . ARG A 1 14  ? 21.004  -60.187 -7.559  1.00 39.63  ? 12  ARG A C     1 
ATOM   87   O O     . ARG A 1 14  ? 20.704  -60.865 -8.537  1.00 44.42  ? 12  ARG A O     1 
ATOM   88   C CB    . ARG A 1 14  ? 22.517  -58.159 -7.833  1.00 44.74  ? 12  ARG A CB    1 
ATOM   89   C CG    . ARG A 1 14  ? 22.625  -56.775 -8.453  1.00 47.06  ? 12  ARG A CG    1 
ATOM   90   C CD    . ARG A 1 14  ? 24.014  -56.442 -8.955  1.00 49.92  ? 12  ARG A CD    1 
ATOM   91   N NE    . ARG A 1 14  ? 24.315  -55.049 -8.669  1.00 60.76  ? 12  ARG A NE    1 
ATOM   92   C CZ    . ARG A 1 14  ? 24.887  -54.623 -7.551  1.00 61.42  ? 12  ARG A CZ    1 
ATOM   93   N NH1   . ARG A 1 14  ? 25.237  -55.487 -6.614  1.00 52.70  ? 12  ARG A NH1   1 
ATOM   94   N NH2   . ARG A 1 14  ? 25.111  -53.335 -7.376  1.00 69.30  ? 12  ARG A NH2   1 
ATOM   95   N N     . PHE A 1 15  ? 21.271  -60.683 -6.357  1.00 41.94  ? 13  PHE A N     1 
ATOM   96   C CA    . PHE A 1 15  ? 21.167  -62.135 -6.083  1.00 36.57  ? 13  PHE A CA    1 
ATOM   97   C C     . PHE A 1 15  ? 19.794  -62.590 -6.547  1.00 36.57  ? 13  PHE A C     1 
ATOM   98   O O     . PHE A 1 15  ? 19.734  -63.569 -7.275  1.00 36.84  ? 13  PHE A O     1 
ATOM   99   C CB    . PHE A 1 15  ? 21.324  -62.448 -4.604  1.00 37.16  ? 13  PHE A CB    1 
ATOM   100  C CG    . PHE A 1 15  ? 20.936  -63.854 -4.244  1.00 41.26  ? 13  PHE A CG    1 
ATOM   101  C CD1   . PHE A 1 15  ? 21.769  -64.915 -4.567  1.00 43.62  ? 13  PHE A CD1   1 
ATOM   102  C CD2   . PHE A 1 15  ? 19.744  -64.113 -3.599  1.00 40.94  ? 13  PHE A CD2   1 
ATOM   103  C CE1   . PHE A 1 15  ? 21.429  -66.208 -4.223  1.00 43.91  ? 13  PHE A CE1   1 
ATOM   104  C CE2   . PHE A 1 15  ? 19.399  -65.410 -3.271  1.00 42.21  ? 13  PHE A CE2   1 
ATOM   105  C CZ    . PHE A 1 15  ? 20.243  -66.450 -3.571  1.00 44.50  ? 13  PHE A CZ    1 
ATOM   106  N N     . VAL A 1 16  ? 18.738  -61.859 -6.174  1.00 37.04  ? 14  VAL A N     1 
ATOM   107  C CA    . VAL A 1 16  ? 17.342  -62.339 -6.382  1.00 37.47  ? 14  VAL A CA    1 
ATOM   108  C C     . VAL A 1 16  ? 17.024  -62.358 -7.881  1.00 35.17  ? 14  VAL A C     1 
ATOM   109  O O     . VAL A 1 16  ? 16.568  -63.382 -8.319  1.00 34.49  ? 14  VAL A O     1 
ATOM   110  C CB    . VAL A 1 16  ? 16.291  -61.534 -5.605  1.00 35.17  ? 14  VAL A CB    1 
ATOM   111  C CG1   . VAL A 1 16  ? 14.897  -61.776 -6.172  1.00 36.97  ? 14  VAL A CG1   1 
ATOM   112  C CG2   . VAL A 1 16  ? 16.330  -61.868 -4.130  1.00 34.46  ? 14  VAL A CG2   1 
ATOM   113  N N     . ARG A 1 17  ? 17.285  -61.266 -8.602  1.00 36.04  ? 15  ARG A N     1 
ATOM   114  C CA    . ARG A 1 17  ? 16.918  -61.047 -10.026 1.00 36.96  ? 15  ARG A CA    1 
ATOM   115  C C     . ARG A 1 17  ? 17.869  -61.794 -10.966 1.00 39.64  ? 15  ARG A C     1 
ATOM   116  O O     . ARG A 1 17  ? 17.406  -62.497 -11.880 1.00 47.66  ? 15  ARG A O     1 
ATOM   117  C CB    . ARG A 1 17  ? 16.986  -59.551 -10.340 1.00 36.93  ? 15  ARG A CB    1 
ATOM   118  C CG    . ARG A 1 17  ? 16.015  -58.707 -9.534  1.00 40.60  ? 15  ARG A CG    1 
ATOM   119  C CD    . ARG A 1 17  ? 16.308  -57.229 -9.649  1.00 39.55  ? 15  ARG A CD    1 
ATOM   120  N NE    . ARG A 1 17  ? 16.322  -56.750 -11.019 1.00 35.98  ? 15  ARG A NE    1 
ATOM   121  C CZ    . ARG A 1 17  ? 15.297  -56.175 -11.624 1.00 39.16  ? 15  ARG A CZ    1 
ATOM   122  N NH1   . ARG A 1 17  ? 14.147  -56.054 -10.984 1.00 36.15  ? 15  ARG A NH1   1 
ATOM   123  N NH2   . ARG A 1 17  ? 15.416  -55.732 -12.873 1.00 41.60  ? 15  ARG A NH2   1 
ATOM   124  N N     . ASP A 1 18  ? 19.169  -61.622 -10.762 1.00 41.69  ? 16  ASP A N     1 
ATOM   125  C CA    . ASP A 1 18  ? 20.204  -62.086 -11.715 1.00 38.18  ? 16  ASP A CA    1 
ATOM   126  C C     . ASP A 1 18  ? 20.401  -63.585 -11.473 1.00 39.83  ? 16  ASP A C     1 
ATOM   127  O O     . ASP A 1 18  ? 20.311  -64.350 -12.438 1.00 42.96  ? 16  ASP A O     1 
ATOM   128  C CB    . ASP A 1 18  ? 21.445  -61.209 -11.577 1.00 37.61  ? 16  ASP A CB    1 
ATOM   129  C CG    . ASP A 1 18  ? 21.163  -59.721 -11.780 1.00 39.26  ? 16  ASP A CG    1 
ATOM   130  O OD1   . ASP A 1 18  ? 20.147  -59.385 -12.422 1.00 42.54  ? 16  ASP A OD1   1 
ATOM   131  O OD2   . ASP A 1 18  ? 21.966  -58.895 -11.304 1.00 40.22  ? 16  ASP A OD2   1 
ATOM   132  N N     . GLU A 1 19  ? 20.612  -63.994 -10.226 1.00 34.93  ? 17  GLU A N     1 
ATOM   133  C CA    . GLU A 1 19  ? 21.029  -65.376 -9.894  1.00 37.94  ? 17  GLU A CA    1 
ATOM   134  C C     . GLU A 1 19  ? 19.798  -66.282 -9.689  1.00 39.49  ? 17  GLU A C     1 
ATOM   135  O O     . GLU A 1 19  ? 19.791  -67.351 -10.290 1.00 40.45  ? 17  GLU A O     1 
ATOM   136  C CB    . GLU A 1 19  ? 21.965  -65.390 -8.674  1.00 37.99  ? 17  GLU A CB    1 
ATOM   137  C CG    . GLU A 1 19  ? 23.248  -64.599 -8.861  1.00 35.82  ? 17  GLU A CG    1 
ATOM   138  C CD    . GLU A 1 19  ? 24.160  -64.589 -7.638  1.00 38.63  ? 17  GLU A CD    1 
ATOM   139  O OE1   . GLU A 1 19  ? 24.505  -63.478 -7.200  1.00 42.08  ? 17  GLU A OE1   1 
ATOM   140  O OE2   . GLU A 1 19  ? 24.506  -65.689 -7.097  1.00 37.01  ? 17  GLU A OE2   1 
ATOM   141  N N     . LEU A 1 20  ? 18.840  -65.929 -8.821  1.00 39.97  ? 18  LEU A N     1 
ATOM   142  C CA    . LEU A 1 20  ? 17.675  -66.805 -8.515  1.00 38.59  ? 18  LEU A CA    1 
ATOM   143  C C     . LEU A 1 20  ? 16.686  -66.763 -9.681  1.00 38.01  ? 18  LEU A C     1 
ATOM   144  O O     . LEU A 1 20  ? 16.219  -67.837 -10.037 1.00 40.86  ? 18  LEU A O     1 
ATOM   145  C CB    . LEU A 1 20  ? 16.995  -66.407 -7.202  1.00 38.90  ? 18  LEU A CB    1 
ATOM   146  C CG    . LEU A 1 20  ? 15.898  -67.354 -6.700  1.00 38.05  ? 18  LEU A CG    1 
ATOM   147  C CD1   . LEU A 1 20  ? 16.470  -68.675 -6.236  1.00 36.49  ? 18  LEU A CD1   1 
ATOM   148  C CD2   . LEU A 1 20  ? 15.122  -66.712 -5.548  1.00 38.39  ? 18  LEU A CD2   1 
ATOM   149  N N     . LEU A 1 21  ? 16.388  -65.602 -10.264 1.00 35.17  ? 19  LEU A N     1 
ATOM   150  C CA    . LEU A 1 21  ? 15.192  -65.464 -11.131 1.00 37.25  ? 19  LEU A CA    1 
ATOM   151  C C     . LEU A 1 21  ? 15.538  -65.246 -12.614 1.00 39.38  ? 19  LEU A C     1 
ATOM   152  O O     . LEU A 1 21  ? 14.583  -65.084 -13.398 1.00 39.39  ? 19  LEU A O     1 
ATOM   153  C CB    . LEU A 1 21  ? 14.305  -64.349 -10.569 1.00 34.53  ? 19  LEU A CB    1 
ATOM   154  C CG    . LEU A 1 21  ? 13.645  -64.688 -9.223  1.00 34.53  ? 19  LEU A CG    1 
ATOM   155  C CD1   . LEU A 1 21  ? 12.767  -63.533 -8.761  1.00 32.97  ? 19  LEU A CD1   1 
ATOM   156  C CD2   . LEU A 1 21  ? 12.848  -65.997 -9.261  1.00 31.31  ? 19  LEU A CD2   1 
ATOM   157  N N     . GLY A 1 22  ? 16.820  -65.270 -13.011 1.00 40.01  ? 20  GLY A N     1 
ATOM   158  C CA    . GLY A 1 22  ? 17.213  -65.364 -14.430 1.00 32.19  ? 20  GLY A CA    1 
ATOM   159  C C     . GLY A 1 22  ? 16.823  -64.117 -15.190 1.00 35.75  ? 20  GLY A C     1 
ATOM   160  O O     . GLY A 1 22  ? 16.578  -64.212 -16.392 1.00 38.02  ? 20  GLY A O     1 
ATOM   161  N N     . TYR A 1 23  ? 16.869  -62.952 -14.544 1.00 35.09  ? 21  TYR A N     1 
ATOM   162  C CA    . TYR A 1 23  ? 16.393  -61.683 -15.142 1.00 35.67  ? 21  TYR A CA    1 
ATOM   163  C C     . TYR A 1 23  ? 17.110  -61.322 -16.458 1.00 37.92  ? 21  TYR A C     1 
ATOM   164  O O     . TYR A 1 23  ? 16.489  -60.589 -17.276 1.00 39.85  ? 21  TYR A O     1 
ATOM   165  C CB    . TYR A 1 23  ? 16.462  -60.533 -14.138 1.00 34.22  ? 21  TYR A CB    1 
ATOM   166  C CG    . TYR A 1 23  ? 15.149  -60.244 -13.470 1.00 33.85  ? 21  TYR A CG    1 
ATOM   167  C CD1   . TYR A 1 23  ? 14.573  -61.139 -12.576 1.00 33.05  ? 21  TYR A CD1   1 
ATOM   168  C CD2   . TYR A 1 23  ? 14.495  -59.053 -13.704 1.00 34.88  ? 21  TYR A CD2   1 
ATOM   169  C CE1   . TYR A 1 23  ? 13.364  -60.865 -11.957 1.00 31.16  ? 21  TYR A CE1   1 
ATOM   170  C CE2   . TYR A 1 23  ? 13.274  -58.776 -13.108 1.00 34.65  ? 21  TYR A CE2   1 
ATOM   171  C CZ    . TYR A 1 23  ? 12.716  -59.677 -12.218 1.00 30.35  ? 21  TYR A CZ    1 
ATOM   172  O OH    . TYR A 1 23  ? 11.529  -59.378 -11.622 1.00 31.01  ? 21  TYR A OH    1 
ATOM   173  N N     . GLU A 1 24  ? 18.358  -61.742 -16.690 1.00 40.60  ? 22  GLU A N     1 
ATOM   174  C CA    . GLU A 1 24  ? 19.037  -61.399 -17.968 1.00 41.29  ? 22  GLU A CA    1 
ATOM   175  C C     . GLU A 1 24  ? 18.275  -62.062 -19.140 1.00 41.04  ? 22  GLU A C     1 
ATOM   176  O O     . GLU A 1 24  ? 17.851  -61.318 -20.059 1.00 38.70  ? 22  GLU A O     1 
ATOM   177  C CB    . GLU A 1 24  ? 20.515  -61.794 -17.972 1.00 46.03  ? 22  GLU A CB    1 
ATOM   178  C CG    . GLU A 1 24  ? 21.183  -61.452 -19.313 1.00 51.55  ? 22  GLU A CG    1 
ATOM   179  C CD    . GLU A 1 24  ? 22.676  -61.724 -19.482 1.00 51.10  ? 22  GLU A CD    1 
ATOM   180  O OE1   . GLU A 1 24  ? 23.193  -61.411 -20.555 1.00 54.99  ? 22  GLU A OE1   1 
ATOM   181  O OE2   . GLU A 1 24  ? 23.320  -62.238 -18.558 1.00 57.34  ? 22  GLU A OE2   1 
ATOM   182  N N     . ALA A 1 25  ? 18.094  -63.392 -19.070 1.00 38.78  ? 23  ALA A N     1 
ATOM   183  C CA    . ALA A 1 25  ? 17.371  -64.262 -20.039 1.00 40.81  ? 23  ALA A CA    1 
ATOM   184  C C     . ALA A 1 25  ? 15.919  -63.812 -20.184 1.00 42.76  ? 23  ALA A C     1 
ATOM   185  O O     . ALA A 1 25  ? 15.473  -63.681 -21.337 1.00 46.11  ? 23  ALA A O     1 
ATOM   186  C CB    . ALA A 1 25  ? 17.443  -65.703 -19.609 1.00 37.17  ? 23  ALA A CB    1 
ATOM   187  N N     . HIS A 1 26  ? 15.264  -63.452 -19.079 1.00 44.50  ? 24  HIS A N     1 
ATOM   188  C CA    . HIS A 1 26  ? 13.859  -62.968 -19.090 1.00 42.55  ? 24  HIS A CA    1 
ATOM   189  C C     . HIS A 1 26  ? 13.739  -61.683 -19.897 1.00 43.53  ? 24  HIS A C     1 
ATOM   190  O O     . HIS A 1 26  ? 12.764  -61.538 -20.632 1.00 54.41  ? 24  HIS A O     1 
ATOM   191  C CB    . HIS A 1 26  ? 13.403  -62.729 -17.644 1.00 43.77  ? 24  HIS A CB    1 
ATOM   192  C CG    . HIS A 1 26  ? 12.164  -61.916 -17.484 1.00 43.36  ? 24  HIS A CG    1 
ATOM   193  N ND1   . HIS A 1 26  ? 12.195  -60.606 -17.065 1.00 42.43  ? 24  HIS A ND1   1 
ATOM   194  C CD2   . HIS A 1 26  ? 10.862  -62.227 -17.644 1.00 46.93  ? 24  HIS A CD2   1 
ATOM   195  C CE1   . HIS A 1 26  ? 10.968  -60.138 -16.994 1.00 39.77  ? 24  HIS A CE1   1 
ATOM   196  N NE2   . HIS A 1 26  ? 10.134  -61.111 -17.341 1.00 51.02  ? 24  HIS A NE2   1 
ATOM   197  N N     . TYR A 1 27  ? 14.709  -60.798 -19.769 1.00 45.28  ? 25  TYR A N     1 
ATOM   198  C CA    . TYR A 1 27  ? 14.618  -59.465 -20.421 1.00 49.81  ? 25  TYR A CA    1 
ATOM   199  C C     . TYR A 1 27  ? 14.843  -59.619 -21.928 1.00 49.50  ? 25  TYR A C     1 
ATOM   200  O O     . TYR A 1 27  ? 14.150  -58.951 -22.736 1.00 48.06  ? 25  TYR A O     1 
ATOM   201  C CB    . TYR A 1 27  ? 15.581  -58.464 -19.766 1.00 51.74  ? 25  TYR A CB    1 
ATOM   202  C CG    . TYR A 1 27  ? 15.039  -57.723 -18.563 1.00 50.12  ? 25  TYR A CG    1 
ATOM   203  C CD1   . TYR A 1 27  ? 13.678  -57.674 -18.273 1.00 50.76  ? 25  TYR A CD1   1 
ATOM   204  C CD2   . TYR A 1 27  ? 15.893  -57.006 -17.739 1.00 47.88  ? 25  TYR A CD2   1 
ATOM   205  C CE1   . TYR A 1 27  ? 13.192  -56.973 -17.177 1.00 51.22  ? 25  TYR A CE1   1 
ATOM   206  C CE2   . TYR A 1 27  ? 15.425  -56.292 -16.643 1.00 49.60  ? 25  TYR A CE2   1 
ATOM   207  C CZ    . TYR A 1 27  ? 14.070  -56.280 -16.354 1.00 49.00  ? 25  TYR A CZ    1 
ATOM   208  O OH    . TYR A 1 27  ? 13.606  -55.586 -15.275 1.00 44.95  ? 25  TYR A OH    1 
ATOM   209  N N     . GLN A 1 28  ? 15.767  -60.495 -22.303 1.00 50.39  ? 26  GLN A N     1 
ATOM   210  C CA    . GLN A 1 28  ? 16.041  -60.796 -23.728 1.00 57.82  ? 26  GLN A CA    1 
ATOM   211  C C     . GLN A 1 28  ? 14.884  -61.540 -24.395 1.00 52.20  ? 26  GLN A C     1 
ATOM   212  O O     . GLN A 1 28  ? 14.819  -61.431 -25.616 1.00 40.67  ? 26  GLN A O     1 
ATOM   213  C CB    . GLN A 1 28  ? 17.259  -61.688 -23.865 1.00 65.61  ? 26  GLN A CB    1 
ATOM   214  C CG    . GLN A 1 28  ? 18.540  -60.949 -23.574 1.00 72.20  ? 26  GLN A CG    1 
ATOM   215  C CD    . GLN A 1 28  ? 19.629  -61.806 -24.140 1.00 78.03  ? 26  GLN A CD    1 
ATOM   216  O OE1   . GLN A 1 28  ? 19.458  -62.384 -25.213 1.00 81.97  ? 26  GLN A OE1   1 
ATOM   217  N NE2   . GLN A 1 28  ? 20.721  -61.919 -23.398 1.00 80.42  ? 26  GLN A NE2   1 
ATOM   218  N N     . SER A 1 29  ? 14.015  -62.202 -23.628 1.00 49.50  ? 27  SER A N     1 
ATOM   219  C CA    . SER A 1 29  ? 12.862  -62.970 -24.164 1.00 47.80  ? 27  SER A CA    1 
ATOM   220  C C     . SER A 1 29  ? 11.646  -62.068 -24.325 1.00 49.34  ? 27  SER A C     1 
ATOM   221  O O     . SER A 1 29  ? 10.601  -62.579 -24.736 1.00 55.88  ? 27  SER A O     1 
ATOM   222  C CB    . SER A 1 29  ? 12.519  -64.071 -23.222 1.00 43.71  ? 27  SER A CB    1 
ATOM   223  O OG    . SER A 1 29  ? 11.799  -63.573 -22.107 1.00 46.79  ? 27  SER A OG    1 
ATOM   224  N N     . LEU A 1 30  ? 11.794  -60.774 -24.096 1.00 46.55  ? 28  LEU A N     1 
ATOM   225  C CA    . LEU A 1 30  ? 10.615  -59.873 -24.034 1.00 53.57  ? 28  LEU A CA    1 
ATOM   226  C C     . LEU A 1 30  ? 10.748  -58.726 -25.025 1.00 54.95  ? 28  LEU A C     1 
ATOM   227  O O     . LEU A 1 30  ? 11.756  -58.035 -25.062 1.00 52.94  ? 28  LEU A O     1 
ATOM   228  C CB    . LEU A 1 30  ? 10.436  -59.342 -22.608 1.00 59.52  ? 28  LEU A CB    1 
ATOM   229  C CG    . LEU A 1 30  ? 9.781   -60.315 -21.627 1.00 64.46  ? 28  LEU A CG    1 
ATOM   230  C CD1   . LEU A 1 30  ? 9.213   -59.562 -20.432 1.00 64.01  ? 28  LEU A CD1   1 
ATOM   231  C CD2   . LEU A 1 30  ? 8.702   -61.156 -22.300 1.00 63.63  ? 28  LEU A CD2   1 
ATOM   232  N N     . PRO A 1 31  ? 9.691   -58.464 -25.821 1.00 60.00  ? 29  PRO A N     1 
ATOM   233  C CA    . PRO A 1 31  ? 9.717   -57.376 -26.790 1.00 65.10  ? 29  PRO A CA    1 
ATOM   234  C C     . PRO A 1 31  ? 9.945   -56.084 -26.020 1.00 66.48  ? 29  PRO A C     1 
ATOM   235  O O     . PRO A 1 31  ? 9.388   -55.996 -24.951 1.00 69.30  ? 29  PRO A O     1 
ATOM   236  C CB    . PRO A 1 31  ? 8.321   -57.390 -27.422 1.00 62.80  ? 29  PRO A CB    1 
ATOM   237  C CG    . PRO A 1 31  ? 7.847   -58.816 -27.197 1.00 66.08  ? 29  PRO A CG    1 
ATOM   238  C CD    . PRO A 1 31  ? 8.414   -59.197 -25.844 1.00 63.77  ? 29  PRO A CD    1 
ATOM   239  N N     . GLY A 1 32  ? 10.770  -55.186 -26.561 1.00 73.13  ? 30  GLY A N     1 
ATOM   240  C CA    . GLY A 1 32  ? 10.976  -53.815 -26.049 1.00 72.59  ? 30  GLY A CA    1 
ATOM   241  C C     . GLY A 1 32  ? 11.983  -53.764 -24.912 1.00 72.84  ? 30  GLY A C     1 
ATOM   242  O O     . GLY A 1 32  ? 12.245  -52.644 -24.407 1.00 72.57  ? 30  GLY A O     1 
ATOM   243  N N     . ALA A 1 33  ? 12.539  -54.921 -24.532 1.00 72.41  ? 31  ALA A N     1 
ATOM   244  C CA    . ALA A 1 33  ? 13.452  -55.080 -23.376 1.00 73.13  ? 31  ALA A CA    1 
ATOM   245  C C     . ALA A 1 33  ? 14.928  -55.111 -23.831 1.00 69.99  ? 31  ALA A C     1 
ATOM   246  O O     . ALA A 1 33  ? 15.807  -55.350 -22.985 1.00 80.32  ? 31  ALA A O     1 
ATOM   247  C CB    . ALA A 1 33  ? 13.041  -56.308 -22.603 1.00 65.08  ? 31  ALA A CB    1 
ATOM   248  N N     . GLU A 1 34  ? 15.198  -54.735 -25.073 1.00 61.99  ? 32  GLU A N     1 
ATOM   249  C CA    . GLU A 1 34  ? 16.582  -54.746 -25.609 1.00 65.98  ? 32  GLU A CA    1 
ATOM   250  C C     . GLU A 1 34  ? 17.442  -53.663 -24.952 1.00 63.78  ? 32  GLU A C     1 
ATOM   251  O O     . GLU A 1 34  ? 18.668  -53.816 -24.966 1.00 65.67  ? 32  GLU A O     1 
ATOM   252  C CB    . GLU A 1 34  ? 16.524  -54.513 -27.118 1.00 71.02  ? 32  GLU A CB    1 
ATOM   253  C CG    . GLU A 1 34  ? 15.389  -55.254 -27.798 1.00 74.30  ? 32  GLU A CG    1 
ATOM   254  C CD    . GLU A 1 34  ? 14.102  -54.460 -27.924 1.00 79.97  ? 32  GLU A CD    1 
ATOM   255  O OE1   . GLU A 1 34  ? 13.153  -54.974 -28.545 1.00 80.09  ? 32  GLU A OE1   1 
ATOM   256  O OE2   . GLU A 1 34  ? 14.054  -53.332 -27.401 1.00 85.98  ? 32  GLU A OE2   1 
ATOM   257  N N     . ASP A 1 35  ? 16.826  -52.605 -24.427 1.00 64.35  ? 33  ASP A N     1 
ATOM   258  C CA    . ASP A 1 35  ? 17.573  -51.483 -23.801 1.00 63.20  ? 33  ASP A CA    1 
ATOM   259  C C     . ASP A 1 35  ? 17.831  -51.796 -22.325 1.00 58.29  ? 33  ASP A C     1 
ATOM   260  O O     . ASP A 1 35  ? 18.575  -51.042 -21.692 1.00 65.69  ? 33  ASP A O     1 
ATOM   261  C CB    . ASP A 1 35  ? 16.831  -50.158 -23.984 1.00 60.17  ? 33  ASP A CB    1 
ATOM   262  C CG    . ASP A 1 35  ? 16.962  -49.584 -25.379 1.00 61.14  ? 33  ASP A CG    1 
ATOM   263  O OD1   . ASP A 1 35  ? 17.704  -50.175 -26.182 1.00 69.73  ? 33  ASP A OD1   1 
ATOM   264  O OD2   . ASP A 1 35  ? 16.323  -48.552 -25.645 1.00 57.98  ? 33  ASP A OD2   1 
ATOM   265  N N     . ALA A 1 36  ? 17.238  -52.865 -21.805 1.00 52.39  ? 34  ALA A N     1 
ATOM   266  C CA    . ALA A 1 36  ? 17.519  -53.281 -20.414 1.00 48.12  ? 34  ALA A CA    1 
ATOM   267  C C     . ALA A 1 36  ? 18.729  -54.215 -20.414 1.00 44.42  ? 34  ALA A C     1 
ATOM   268  O O     . ALA A 1 36  ? 18.618  -55.330 -19.889 1.00 40.98  ? 34  ALA A O     1 
ATOM   269  C CB    . ALA A 1 36  ? 16.300  -53.906 -19.795 1.00 46.36  ? 34  ALA A CB    1 
ATOM   270  N N     . THR A 1 37  ? 19.836  -53.762 -21.000 1.00 42.69  ? 35  THR A N     1 
ATOM   271  C CA    . THR A 1 37  ? 21.101  -54.528 -20.988 1.00 44.23  ? 35  THR A CA    1 
ATOM   272  C C     . THR A 1 37  ? 21.549  -54.709 -19.543 1.00 44.62  ? 35  THR A C     1 
ATOM   273  O O     . THR A 1 37  ? 21.274  -53.820 -18.730 1.00 46.13  ? 35  THR A O     1 
ATOM   274  C CB    . THR A 1 37  ? 22.170  -53.756 -21.765 1.00 51.02  ? 35  THR A CB    1 
ATOM   275  O OG1   . THR A 1 37  ? 21.645  -53.504 -23.069 1.00 50.16  ? 35  THR A OG1   1 
ATOM   276  C CG2   . THR A 1 37  ? 23.488  -54.483 -21.887 1.00 49.13  ? 35  THR A CG2   1 
ATOM   277  N N     . PRO A 1 38  ? 22.233  -55.813 -19.192 1.00 44.35  ? 36  PRO A N     1 
ATOM   278  C CA    . PRO A 1 38  ? 22.736  -55.985 -17.836 1.00 43.72  ? 36  PRO A CA    1 
ATOM   279  C C     . PRO A 1 38  ? 23.512  -54.770 -17.299 1.00 48.61  ? 36  PRO A C     1 
ATOM   280  O O     . PRO A 1 38  ? 23.328  -54.444 -16.151 1.00 50.37  ? 36  PRO A O     1 
ATOM   281  C CB    . PRO A 1 38  ? 23.653  -57.200 -17.993 1.00 40.31  ? 36  PRO A CB    1 
ATOM   282  C CG    . PRO A 1 38  ? 23.012  -58.007 -19.087 1.00 40.51  ? 36  PRO A CG    1 
ATOM   283  C CD    . PRO A 1 38  ? 22.493  -56.966 -20.051 1.00 40.65  ? 36  PRO A CD    1 
ATOM   284  N N     . ASP A 1 39  ? 24.323  -54.122 -18.136 1.00 45.61  ? 37  ASP A N     1 
ATOM   285  C CA    . ASP A 1 39  ? 25.181  -53.005 -17.664 1.00 39.22  ? 37  ASP A CA    1 
ATOM   286  C C     . ASP A 1 39  ? 24.335  -51.758 -17.442 1.00 36.11  ? 37  ASP A C     1 
ATOM   287  O O     . ASP A 1 39  ? 24.658  -51.001 -16.529 1.00 41.40  ? 37  ASP A O     1 
ATOM   288  C CB    . ASP A 1 39  ? 26.347  -52.761 -18.621 1.00 39.70  ? 37  ASP A CB    1 
ATOM   289  C CG    . ASP A 1 39  ? 27.463  -53.782 -18.504 1.00 45.75  ? 37  ASP A CG    1 
ATOM   290  O OD1   . ASP A 1 39  ? 27.422  -54.591 -17.564 1.00 45.06  ? 37  ASP A OD1   1 
ATOM   291  O OD2   . ASP A 1 39  ? 28.363  -53.760 -19.360 1.00 57.82  ? 37  ASP A OD2   1 
ATOM   292  N N     . MET A 1 40  ? 23.287  -51.576 -18.238 1.00 39.54  ? 38  MET A N     1 
ATOM   293  C CA    . MET A 1 40  ? 22.381  -50.410 -18.071 1.00 42.39  ? 38  MET A CA    1 
ATOM   294  C C     . MET A 1 40  ? 21.568  -50.571 -16.790 1.00 36.44  ? 38  MET A C     1 
ATOM   295  O O     . MET A 1 40  ? 21.429  -49.595 -16.063 1.00 33.17  ? 38  MET A O     1 
ATOM   296  C CB    . MET A 1 40  ? 21.422  -50.282 -19.252 1.00 48.39  ? 38  MET A CB    1 
ATOM   297  C CG    . MET A 1 40  ? 20.411  -49.166 -19.091 1.00 60.94  ? 38  MET A CG    1 
ATOM   298  S SD    . MET A 1 40  ? 21.194  -47.564 -18.783 1.00 82.09  ? 38  MET A SD    1 
ATOM   299  C CE    . MET A 1 40  ? 19.867  -46.450 -19.237 1.00 67.62  ? 38  MET A CE    1 
ATOM   300  N N     . VAL A 1 41  ? 21.039  -51.770 -16.568 1.00 40.25  ? 39  VAL A N     1 
ATOM   301  C CA    . VAL A 1 41  ? 20.242  -52.048 -15.341 1.00 42.04  ? 39  VAL A CA    1 
ATOM   302  C C     . VAL A 1 41  ? 21.141  -51.752 -14.143 1.00 38.81  ? 39  VAL A C     1 
ATOM   303  O O     . VAL A 1 41  ? 20.710  -51.023 -13.256 1.00 38.21  ? 39  VAL A O     1 
ATOM   304  C CB    . VAL A 1 41  ? 19.711  -53.496 -15.314 1.00 41.18  ? 39  VAL A CB    1 
ATOM   305  C CG1   . VAL A 1 41  ? 19.111  -53.858 -13.967 1.00 41.27  ? 39  VAL A CG1   1 
ATOM   306  C CG2   . VAL A 1 41  ? 18.730  -53.771 -16.441 1.00 42.14  ? 39  VAL A CG2   1 
ATOM   307  N N     . ASN A 1 42  ? 22.369  -52.247 -14.167 1.00 36.63  ? 40  ASN A N     1 
ATOM   308  C CA    . ASN A 1 42  ? 23.275  -52.053 -13.013 1.00 36.58  ? 40  ASN A CA    1 
ATOM   309  C C     . ASN A 1 42  ? 23.581  -50.559 -12.847 1.00 39.46  ? 40  ASN A C     1 
ATOM   310  O O     . ASN A 1 42  ? 23.724  -50.121 -11.704 1.00 41.93  ? 40  ASN A O     1 
ATOM   311  C CB    . ASN A 1 42  ? 24.509  -52.942 -13.135 1.00 39.61  ? 40  ASN A CB    1 
ATOM   312  C CG    . ASN A 1 42  ? 24.286  -54.336 -12.590 1.00 35.70  ? 40  ASN A CG    1 
ATOM   313  O OD1   . ASN A 1 42  ? 23.409  -54.548 -11.759 1.00 39.09  ? 40  ASN A OD1   1 
ATOM   314  N ND2   . ASN A 1 42  ? 25.074  -55.290 -13.049 1.00 33.45  ? 40  ASN A ND2   1 
ATOM   315  N N     . ALA A 1 43  ? 23.643  -49.808 -13.948 1.00 34.59  ? 41  ALA A N     1 
ATOM   316  C CA    . ALA A 1 43  ? 23.909  -48.351 -13.865 1.00 36.57  ? 41  ALA A CA    1 
ATOM   317  C C     . ALA A 1 43  ? 22.711  -47.630 -13.222 1.00 39.68  ? 41  ALA A C     1 
ATOM   318  O O     . ALA A 1 43  ? 22.905  -46.772 -12.330 1.00 39.92  ? 41  ALA A O     1 
ATOM   319  C CB    . ALA A 1 43  ? 24.237  -47.787 -15.232 1.00 35.12  ? 41  ALA A CB    1 
ATOM   320  N N     . ILE A 1 44  ? 21.506  -47.988 -13.671 1.00 42.97  ? 42  ILE A N     1 
ATOM   321  C CA    . ILE A 1 44  ? 20.244  -47.385 -13.156 1.00 40.05  ? 42  ILE A CA    1 
ATOM   322  C C     . ILE A 1 44  ? 20.055  -47.784 -11.694 1.00 35.34  ? 42  ILE A C     1 
ATOM   323  O O     . ILE A 1 44  ? 19.606  -46.946 -10.912 1.00 34.11  ? 42  ILE A O     1 
ATOM   324  C CB    . ILE A 1 44  ? 19.062  -47.856 -14.024 1.00 43.04  ? 42  ILE A CB    1 
ATOM   325  C CG1   . ILE A 1 44  ? 19.116  -47.257 -15.430 1.00 40.26  ? 42  ILE A CG1   1 
ATOM   326  C CG2   . ILE A 1 44  ? 17.732  -47.581 -13.343 1.00 45.39  ? 42  ILE A CG2   1 
ATOM   327  C CD1   . ILE A 1 44  ? 18.216  -47.953 -16.412 1.00 43.55  ? 42  ILE A CD1   1 
ATOM   328  N N     . LEU A 1 45  ? 20.387  -49.027 -11.364 1.00 32.17  ? 43  LEU A N     1 
ATOM   329  C CA    . LEU A 1 45  ? 20.288  -49.471 -9.953  1.00 36.13  ? 43  LEU A CA    1 
ATOM   330  C C     . LEU A 1 45  ? 21.208  -48.623 -9.063  1.00 37.55  ? 43  LEU A C     1 
ATOM   331  O O     . LEU A 1 45  ? 20.765  -48.232 -7.984  1.00 43.40  ? 43  LEU A O     1 
ATOM   332  C CB    . LEU A 1 45  ? 20.653  -50.955 -9.897  1.00 36.59  ? 43  LEU A CB    1 
ATOM   333  C CG    . LEU A 1 45  ? 19.567  -51.924 -10.362 1.00 38.06  ? 43  LEU A CG    1 
ATOM   334  C CD1   . LEU A 1 45  ? 20.011  -53.365 -10.179 1.00 38.67  ? 43  LEU A CD1   1 
ATOM   335  C CD2   . LEU A 1 45  ? 18.262  -51.672 -9.629  1.00 36.56  ? 43  LEU A CD2   1 
ATOM   336  N N     . GLU A 1 46  ? 22.434  -48.353 -9.509  1.00 40.30  ? 44  GLU A N     1 
ATOM   337  C CA    . GLU A 1 46  ? 23.403  -47.524 -8.744  1.00 38.91  ? 44  GLU A CA    1 
ATOM   338  C C     . GLU A 1 46  ? 22.872  -46.099 -8.603  1.00 37.17  ? 44  GLU A C     1 
ATOM   339  O O     . GLU A 1 46  ? 22.909  -45.574 -7.494  1.00 39.60  ? 44  GLU A O     1 
ATOM   340  C CB    . GLU A 1 46  ? 24.772  -47.519 -9.419  1.00 40.24  ? 44  GLU A CB    1 
ATOM   341  C CG    . GLU A 1 46  ? 25.587  -48.765 -9.139  1.00 51.09  ? 44  GLU A CG    1 
ATOM   342  C CD    . GLU A 1 46  ? 25.963  -48.968 -7.681  1.00 53.15  ? 44  GLU A CD    1 
ATOM   343  O OE1   . GLU A 1 46  ? 26.108  -50.134 -7.269  1.00 39.47  ? 44  GLU A OE1   1 
ATOM   344  O OE2   . GLU A 1 46  ? 26.117  -47.958 -6.966  1.00 45.78  ? 44  GLU A OE2   1 
ATOM   345  N N     . GLU A 1 47  ? 22.406  -45.511 -9.700  1.00 35.10  ? 45  GLU A N     1 
ATOM   346  C CA    . GLU A 1 47  ? 21.924  -44.102 -9.629  1.00 39.59  ? 45  GLU A CA    1 
ATOM   347  C C     . GLU A 1 47  ? 20.680  -44.036 -8.755  1.00 33.93  ? 45  GLU A C     1 
ATOM   348  O O     . GLU A 1 47  ? 20.487  -43.002 -8.108  1.00 33.81  ? 45  GLU A O     1 
ATOM   349  C CB    . GLU A 1 47  ? 21.606  -43.528 -11.010 1.00 42.98  ? 45  GLU A CB    1 
ATOM   350  C CG    . GLU A 1 47  ? 22.854  -43.209 -11.809 1.00 49.42  ? 45  GLU A CG    1 
ATOM   351  C CD    . GLU A 1 47  ? 23.662  -42.001 -11.356 1.00 47.43  ? 45  GLU A CD    1 
ATOM   352  O OE1   . GLU A 1 47  ? 24.872  -41.969 -11.634 1.00 47.07  ? 45  GLU A OE1   1 
ATOM   353  O OE2   . GLU A 1 47  ? 23.077  -41.074 -10.804 1.00 48.89  ? 45  GLU A OE2   1 
ATOM   354  N N     . GLY A 1 48  ? 19.864  -45.089 -8.805  1.00 33.31  ? 46  GLY A N     1 
ATOM   355  C CA    . GLY A 1 48  ? 18.664  -45.253 -7.962  1.00 34.38  ? 46  GLY A CA    1 
ATOM   356  C C     . GLY A 1 48  ? 18.997  -45.226 -6.472  1.00 32.12  ? 46  GLY A C     1 
ATOM   357  O O     . GLY A 1 48  ? 18.398  -44.398 -5.742  1.00 29.58  ? 46  GLY A O     1 
ATOM   358  N N     . ALA A 1 49  ? 19.919  -46.088 -6.047  1.00 32.54  ? 47  ALA A N     1 
ATOM   359  C CA    . ALA A 1 49  ? 20.459  -46.153 -4.666  1.00 37.26  ? 47  ALA A CA    1 
ATOM   360  C C     . ALA A 1 49  ? 21.064  -44.809 -4.249  1.00 37.42  ? 47  ALA A C     1 
ATOM   361  O O     . ALA A 1 49  ? 20.768  -44.412 -3.133  1.00 38.21  ? 47  ALA A O     1 
ATOM   362  C CB    . ALA A 1 49  ? 21.485  -47.249 -4.550  1.00 36.10  ? 47  ALA A CB    1 
ATOM   363  N N     . LYS A 1 50  ? 21.868  -44.150 -5.101  1.00 38.42  ? 48  LYS A N     1 
ATOM   364  C CA    . LYS A 1 50  ? 22.465  -42.818 -4.797  1.00 41.22  ? 48  LYS A CA    1 
ATOM   365  C C     . LYS A 1 50  ? 21.319  -41.872 -4.459  1.00 37.73  ? 48  LYS A C     1 
ATOM   366  O O     . LYS A 1 50  ? 21.325  -41.291 -3.387  1.00 36.01  ? 48  LYS A O     1 
ATOM   367  C CB    . LYS A 1 50  ? 23.280  -42.203 -5.941  1.00 50.03  ? 48  LYS A CB    1 
ATOM   368  C CG    . LYS A 1 50  ? 24.795  -42.255 -5.784  1.00 59.18  ? 48  LYS A CG    1 
ATOM   369  C CD    . LYS A 1 50  ? 25.571  -42.370 -7.109  1.00 67.59  ? 48  LYS A CD    1 
ATOM   370  C CE    . LYS A 1 50  ? 26.857  -43.183 -6.985  1.00 73.29  ? 48  LYS A CE    1 
ATOM   371  N NZ    . LYS A 1 50  ? 27.263  -43.875 -8.239  1.00 64.66  ? 48  LYS A NZ    1 
ATOM   372  N N     . PHE A 1 51  ? 20.318  -41.780 -5.319  1.00 35.78  ? 49  PHE A N     1 
ATOM   373  C CA    . PHE A 1 51  ? 19.192  -40.856 -5.070  1.00 34.54  ? 49  PHE A CA    1 
ATOM   374  C C     . PHE A 1 51  ? 18.479  -41.220 -3.748  1.00 36.05  ? 49  PHE A C     1 
ATOM   375  O O     . PHE A 1 51  ? 18.040  -40.297 -2.999  1.00 33.01  ? 49  PHE A O     1 
ATOM   376  C CB    . PHE A 1 51  ? 18.231  -40.843 -6.251  1.00 36.10  ? 49  PHE A CB    1 
ATOM   377  C CG    . PHE A 1 51  ? 17.077  -39.923 -5.994  1.00 35.95  ? 49  PHE A CG    1 
ATOM   378  C CD1   . PHE A 1 51  ? 17.170  -38.581 -6.333  1.00 37.36  ? 49  PHE A CD1   1 
ATOM   379  C CD2   . PHE A 1 51  ? 15.953  -40.384 -5.316  1.00 34.29  ? 49  PHE A CD2   1 
ATOM   380  C CE1   . PHE A 1 51  ? 16.117  -37.720 -6.065  1.00 41.43  ? 49  PHE A CE1   1 
ATOM   381  C CE2   . PHE A 1 51  ? 14.906  -39.525 -5.034  1.00 38.67  ? 49  PHE A CE2   1 
ATOM   382  C CZ    . PHE A 1 51  ? 14.993  -38.192 -5.405  1.00 47.14  ? 49  PHE A CZ    1 
ATOM   383  N N     . CYS A 1 52  ? 18.311  -42.511 -3.469  1.00 31.91  ? 50  CYS A N     1 
ATOM   384  C CA    . CYS A 1 52  ? 17.508  -42.964 -2.307  1.00 34.95  ? 50  CYS A CA    1 
ATOM   385  C C     . CYS A 1 52  ? 18.292  -42.648 -1.027  1.00 34.81  ? 50  CYS A C     1 
ATOM   386  O O     . CYS A 1 52  ? 17.718  -41.950 -0.144  1.00 32.87  ? 50  CYS A O     1 
ATOM   387  C CB    . CYS A 1 52  ? 17.136  -44.440 -2.430  1.00 35.70  ? 50  CYS A CB    1 
ATOM   388  S SG    . CYS A 1 52  ? 15.825  -44.722 -3.661  1.00 34.39  ? 50  CYS A SG    1 
ATOM   389  N N     . GLU A 1 53  ? 19.569  -43.049 -0.991  1.00 31.73  ? 51  GLU A N     1 
ATOM   390  C CA    . GLU A 1 53  ? 20.497  -42.889 0.168   1.00 36.48  ? 51  GLU A CA    1 
ATOM   391  C C     . GLU A 1 53  ? 20.885  -41.422 0.402   1.00 38.53  ? 51  GLU A C     1 
ATOM   392  O O     . GLU A 1 53  ? 21.165  -41.097 1.546   1.00 40.58  ? 51  GLU A O     1 
ATOM   393  C CB    . GLU A 1 53  ? 21.795  -43.672 -0.023  1.00 35.46  ? 51  GLU A CB    1 
ATOM   394  C CG    . GLU A 1 53  ? 21.625  -45.187 0.002   1.00 34.25  ? 51  GLU A CG    1 
ATOM   395  C CD    . GLU A 1 53  ? 22.823  -45.964 -0.513  1.00 35.67  ? 51  GLU A CD    1 
ATOM   396  O OE1   . GLU A 1 53  ? 22.807  -47.193 -0.447  1.00 39.50  ? 51  GLU A OE1   1 
ATOM   397  O OE2   . GLU A 1 53  ? 23.787  -45.341 -0.960  1.00 40.91  ? 51  GLU A OE2   1 
ATOM   398  N N     . GLN A 1 54  ? 20.925  -40.561 -0.615  1.00 40.91  ? 52  GLN A N     1 
ATOM   399  C CA    . GLN A 1 54  ? 21.539  -39.216 -0.446  1.00 42.18  ? 52  GLN A CA    1 
ATOM   400  C C     . GLN A 1 54  ? 20.476  -38.123 -0.471  1.00 40.35  ? 52  GLN A C     1 
ATOM   401  O O     . GLN A 1 54  ? 20.669  -37.165 0.235   1.00 39.39  ? 52  GLN A O     1 
ATOM   402  C CB    . GLN A 1 54  ? 22.656  -38.997 -1.459  1.00 45.50  ? 52  GLN A CB    1 
ATOM   403  C CG    . GLN A 1 54  ? 23.884  -39.853 -1.160  1.00 51.21  ? 52  GLN A CG    1 
ATOM   404  C CD    . GLN A 1 54  ? 24.889  -39.806 -2.285  1.00 58.99  ? 52  GLN A CD    1 
ATOM   405  O OE1   . GLN A 1 54  ? 24.927  -38.885 -3.095  1.00 59.67  ? 52  GLN A OE1   1 
ATOM   406  N NE2   . GLN A 1 54  ? 25.743  -40.808 -2.336  1.00 72.53  ? 52  GLN A NE2   1 
ATOM   407  N N     . VAL A 1 55  ? 19.368  -38.291 -1.185  1.00 38.99  ? 53  VAL A N     1 
ATOM   408  C CA    . VAL A 1 55  ? 18.364  -37.199 -1.354  1.00 35.32  ? 53  VAL A CA    1 
ATOM   409  C C     . VAL A 1 55  ? 17.148  -37.479 -0.466  1.00 35.02  ? 53  VAL A C     1 
ATOM   410  O O     . VAL A 1 55  ? 16.785  -36.563 0.273   1.00 37.77  ? 53  VAL A O     1 
ATOM   411  C CB    . VAL A 1 55  ? 17.968  -36.971 -2.831  1.00 36.73  ? 53  VAL A CB    1 
ATOM   412  C CG1   . VAL A 1 55  ? 17.021  -35.797 -2.987  1.00 35.33  ? 53  VAL A CG1   1 
ATOM   413  C CG2   . VAL A 1 55  ? 19.182  -36.774 -3.725  1.00 35.88  ? 53  VAL A CG2   1 
ATOM   414  N N     . ILE A 1 56  ? 16.527  -38.656 -0.521  1.00 32.72  ? 54  ILE A N     1 
ATOM   415  C CA    . ILE A 1 56  ? 15.242  -38.860 0.224   1.00 33.42  ? 54  ILE A CA    1 
ATOM   416  C C     . ILE A 1 56  ? 15.413  -39.497 1.620   1.00 33.13  ? 54  ILE A C     1 
ATOM   417  O O     . ILE A 1 56  ? 14.642  -39.128 2.507   1.00 32.28  ? 54  ILE A O     1 
ATOM   418  C CB    . ILE A 1 56  ? 14.213  -39.600 -0.653  1.00 33.02  ? 54  ILE A CB    1 
ATOM   419  C CG1   . ILE A 1 56  ? 14.771  -40.890 -1.255  1.00 34.90  ? 54  ILE A CG1   1 
ATOM   420  C CG2   . ILE A 1 56  ? 13.668  -38.668 -1.724  1.00 35.62  ? 54  ILE A CG2   1 
ATOM   421  C CD1   . ILE A 1 56  ? 13.723  -41.749 -1.916  1.00 31.79  ? 54  ILE A CD1   1 
ATOM   422  N N     . ALA A 1 57  ? 16.363  -40.411 1.809   1.00 33.14  ? 55  ALA A N     1 
ATOM   423  C CA    . ALA A 1 57  ? 16.501  -41.090 3.118   1.00 31.05  ? 55  ALA A CA    1 
ATOM   424  C C     . ALA A 1 57  ? 16.748  -40.047 4.188   1.00 33.12  ? 55  ALA A C     1 
ATOM   425  O O     . ALA A 1 57  ? 16.259  -40.219 5.284   1.00 33.71  ? 55  ALA A O     1 
ATOM   426  C CB    . ALA A 1 57  ? 17.577  -42.147 3.145   1.00 30.55  ? 55  ALA A CB    1 
ATOM   427  N N     . PRO A 1 58  ? 17.563  -38.989 3.976   1.00 34.92  ? 56  PRO A N     1 
ATOM   428  C CA    . PRO A 1 58  ? 17.744  -37.974 5.026   1.00 33.28  ? 56  PRO A CA    1 
ATOM   429  C C     . PRO A 1 58  ? 16.464  -37.199 5.358   1.00 35.46  ? 56  PRO A C     1 
ATOM   430  O O     . PRO A 1 58  ? 16.396  -36.651 6.400   1.00 42.54  ? 56  PRO A O     1 
ATOM   431  C CB    . PRO A 1 58  ? 18.830  -37.054 4.457   1.00 33.11  ? 56  PRO A CB    1 
ATOM   432  C CG    . PRO A 1 58  ? 19.605  -37.984 3.519   1.00 36.01  ? 56  PRO A CG    1 
ATOM   433  C CD    . PRO A 1 58  ? 18.516  -38.828 2.864   1.00 37.03  ? 56  PRO A CD    1 
ATOM   434  N N     . LEU A 1 59  ? 15.456  -37.225 4.490   1.00 36.33  ? 57  LEU A N     1 
ATOM   435  C CA    . LEU A 1 59  ? 14.221  -36.423 4.703   1.00 34.18  ? 57  LEU A CA    1 
ATOM   436  C C     . LEU A 1 59  ? 13.142  -37.219 5.447   1.00 31.15  ? 57  LEU A C     1 
ATOM   437  O O     . LEU A 1 59  ? 12.114  -36.625 5.766   1.00 30.45  ? 57  LEU A O     1 
ATOM   438  C CB    . LEU A 1 59  ? 13.701  -35.989 3.332   1.00 35.98  ? 57  LEU A CB    1 
ATOM   439  C CG    . LEU A 1 59  ? 14.647  -35.130 2.499   1.00 43.95  ? 57  LEU A CG    1 
ATOM   440  C CD1   . LEU A 1 59  ? 14.043  -34.838 1.136   1.00 41.89  ? 57  LEU A CD1   1 
ATOM   441  C CD2   . LEU A 1 59  ? 14.975  -33.835 3.221   1.00 38.70  ? 57  LEU A CD2   1 
ATOM   442  N N     . ASN A 1 60  ? 13.377  -38.500 5.718   1.00 27.74  ? 58  ASN A N     1 
ATOM   443  C CA    . ASN A 1 60  ? 12.332  -39.362 6.331   1.00 31.64  ? 58  ASN A CA    1 
ATOM   444  C C     . ASN A 1 60  ? 11.979  -38.904 7.759   1.00 31.73  ? 58  ASN A C     1 
ATOM   445  O O     . ASN A 1 60  ? 10.793  -38.887 8.079   1.00 26.07  ? 58  ASN A O     1 
ATOM   446  C CB    . ASN A 1 60  ? 12.711  -40.844 6.250   1.00 30.48  ? 58  ASN A CB    1 
ATOM   447  C CG    . ASN A 1 60  ? 11.523  -41.768 6.400   1.00 30.49  ? 58  ASN A CG    1 
ATOM   448  O OD1   . ASN A 1 60  ? 10.412  -41.422 6.021   1.00 29.33  ? 58  ASN A OD1   1 
ATOM   449  N ND2   . ASN A 1 60  ? 11.750  -42.943 6.956   1.00 31.76  ? 58  ASN A ND2   1 
ATOM   450  N N     . ARG A 1 61  ? 12.979  -38.539 8.570   1.00 31.87  ? 59  ARG A N     1 
ATOM   451  C CA    . ARG A 1 61  ? 12.702  -38.052 9.954   1.00 37.28  ? 59  ARG A CA    1 
ATOM   452  C C     . ARG A 1 61  ? 11.974  -36.697 9.884   1.00 36.47  ? 59  ARG A C     1 
ATOM   453  O O     . ARG A 1 61  ? 10.950  -36.485 10.669  1.00 30.08  ? 59  ARG A O     1 
ATOM   454  C CB    . ARG A 1 61  ? 13.986  -38.038 10.798  1.00 37.73  ? 59  ARG A CB    1 
ATOM   455  C CG    . ARG A 1 61  ? 14.494  -39.428 11.179  1.00 46.67  ? 59  ARG A CG    1 
ATOM   456  C CD    . ARG A 1 61  ? 13.635  -40.245 12.171  1.00 50.76  ? 59  ARG A CD    1 
ATOM   457  N NE    . ARG A 1 61  ? 13.136  -39.422 13.279  1.00 50.23  ? 59  ARG A NE    1 
ATOM   458  C CZ    . ARG A 1 61  ? 11.866  -39.297 13.680  1.00 51.08  ? 59  ARG A CZ    1 
ATOM   459  N NH1   . ARG A 1 61  ? 10.895  -39.994 13.117  1.00 47.17  ? 59  ARG A NH1   1 
ATOM   460  N NH2   . ARG A 1 61  ? 11.577  -38.487 14.688  1.00 53.05  ? 59  ARG A NH2   1 
ATOM   461  N N     . VAL A 1 62  ? 12.419  -35.820 8.975   1.00 36.46  ? 60  VAL A N     1 
ATOM   462  C CA    . VAL A 1 62  ? 11.832  -34.448 8.833   1.00 34.64  ? 60  VAL A CA    1 
ATOM   463  C C     . VAL A 1 62  ? 10.357  -34.588 8.443   1.00 32.56  ? 60  VAL A C     1 
ATOM   464  O O     . VAL A 1 62  ? 9.507   -33.902 9.040   1.00 35.98  ? 60  VAL A O     1 
ATOM   465  C CB    . VAL A 1 62  ? 12.603  -33.574 7.829   1.00 41.28  ? 60  VAL A CB    1 
ATOM   466  C CG1   . VAL A 1 62  ? 12.012  -32.168 7.795   1.00 43.20  ? 60  VAL A CG1   1 
ATOM   467  C CG2   . VAL A 1 62  ? 14.098  -33.518 8.137   1.00 45.62  ? 60  VAL A CG2   1 
ATOM   468  N N     . GLY A 1 63  ? 10.056  -35.465 7.476   1.00 36.58  ? 61  GLY A N     1 
ATOM   469  C CA    . GLY A 1 63  ? 8.679   -35.762 7.047   1.00 34.06  ? 61  GLY A CA    1 
ATOM   470  C C     . GLY A 1 63  ? 7.812   -36.099 8.237   1.00 31.82  ? 61  GLY A C     1 
ATOM   471  O O     . GLY A 1 63  ? 6.723   -35.557 8.352   1.00 32.27  ? 61  GLY A O     1 
ATOM   472  N N     . ASP A 1 64  ? 8.297   -36.979 9.107   1.00 33.25  ? 62  ASP A N     1 
ATOM   473  C CA    . ASP A 1 64  ? 7.535   -37.494 10.270  1.00 32.80  ? 62  ASP A CA    1 
ATOM   474  C C     . ASP A 1 64  ? 7.366   -36.398 11.329  1.00 31.50  ? 62  ASP A C     1 
ATOM   475  O O     . ASP A 1 64  ? 6.255   -36.347 11.901  1.00 29.61  ? 62  ASP A O     1 
ATOM   476  C CB    . ASP A 1 64  ? 8.166   -38.777 10.813  1.00 33.06  ? 62  ASP A CB    1 
ATOM   477  C CG    . ASP A 1 64  ? 7.547   -39.221 12.121  1.00 33.28  ? 62  ASP A CG    1 
ATOM   478  O OD1   . ASP A 1 64  ? 6.449   -39.788 12.107  1.00 36.19  ? 62  ASP A OD1   1 
ATOM   479  O OD2   . ASP A 1 64  ? 8.169   -38.974 13.131  1.00 35.21  ? 62  ASP A OD2   1 
ATOM   480  N N     . LEU A 1 65  ? 8.383   -35.557 11.573  1.00 32.48  ? 63  LEU A N     1 
ATOM   481  C CA    . LEU A 1 65  ? 8.335   -34.468 12.607  1.00 32.70  ? 63  LEU A CA    1 
ATOM   482  C C     . LEU A 1 65  ? 7.440   -33.311 12.146  1.00 34.65  ? 63  LEU A C     1 
ATOM   483  O O     . LEU A 1 65  ? 6.604   -32.864 12.915  1.00 30.90  ? 63  LEU A O     1 
ATOM   484  C CB    . LEU A 1 65  ? 9.752   -33.948 12.895  1.00 34.83  ? 63  LEU A CB    1 
ATOM   485  C CG    . LEU A 1 65  ? 10.625  -34.846 13.794  1.00 38.62  ? 63  LEU A CG    1 
ATOM   486  C CD1   . LEU A 1 65  ? 12.116  -34.565 13.610  1.00 39.68  ? 63  LEU A CD1   1 
ATOM   487  C CD2   . LEU A 1 65  ? 10.229  -34.715 15.266  1.00 33.64  ? 63  LEU A CD2   1 
ATOM   488  N N     . GLU A 1 66  ? 7.617   -32.806 10.927  1.00 38.57  ? 64  GLU A N     1 
ATOM   489  C CA    . GLU A 1 66  ? 6.814   -31.646 10.445  1.00 36.30  ? 64  GLU A CA    1 
ATOM   490  C C     . GLU A 1 66  ? 5.442   -32.127 9.996   1.00 34.14  ? 64  GLU A C     1 
ATOM   491  O O     . GLU A 1 66  ? 4.505   -31.403 10.145  1.00 31.07  ? 64  GLU A O     1 
ATOM   492  C CB    . GLU A 1 66  ? 7.468   -30.955 9.258   1.00 37.98  ? 64  GLU A CB    1 
ATOM   493  C CG    . GLU A 1 66  ? 8.885   -30.556 9.549   1.00 42.08  ? 64  GLU A CG    1 
ATOM   494  C CD    . GLU A 1 66  ? 9.458   -29.614 8.517   1.00 44.08  ? 64  GLU A CD    1 
ATOM   495  O OE1   . GLU A 1 66  ? 10.552  -29.070 8.765   1.00 43.98  ? 64  GLU A OE1   1 
ATOM   496  O OE2   . GLU A 1 66  ? 8.810   -29.451 7.464   1.00 49.17  ? 64  GLU A OE2   1 
ATOM   497  N N     . GLY A 1 67  ? 5.357   -33.297 9.378   1.00 39.11  ? 65  GLY A N     1 
ATOM   498  C CA    . GLY A 1 67  ? 4.231   -33.597 8.478   1.00 39.94  ? 65  GLY A CA    1 
ATOM   499  C C     . GLY A 1 67  ? 3.904   -32.409 7.580   1.00 38.68  ? 65  GLY A C     1 
ATOM   500  O O     . GLY A 1 67  ? 4.815   -31.570 7.279   1.00 43.84  ? 65  GLY A O     1 
ATOM   501  N N     . CYS A 1 68  ? 2.640   -32.329 7.187   1.00 34.36  ? 66  CYS A N     1 
ATOM   502  C CA    . CYS A 1 68  ? 2.111   -31.418 6.149   1.00 36.11  ? 66  CYS A CA    1 
ATOM   503  C C     . CYS A 1 68  ? 1.289   -30.326 6.828   1.00 37.34  ? 66  CYS A C     1 
ATOM   504  O O     . CYS A 1 68  ? 0.699   -30.610 7.890   1.00 41.01  ? 66  CYS A O     1 
ATOM   505  C CB    . CYS A 1 68  ? 1.252   -32.185 5.148   1.00 33.31  ? 66  CYS A CB    1 
ATOM   506  S SG    . CYS A 1 68  ? 2.225   -33.289 4.092   1.00 35.53  ? 66  CYS A SG    1 
ATOM   507  N N     . THR A 1 69  ? 1.230   -29.128 6.240   1.00 40.27  ? 67  THR A N     1 
ATOM   508  C CA    . THR A 1 69  ? 0.493   -27.983 6.834   1.00 40.69  ? 67  THR A CA    1 
ATOM   509  C C     . THR A 1 69  ? -0.610  -27.537 5.882   1.00 38.45  ? 67  THR A C     1 
ATOM   510  O O     . THR A 1 69  ? -0.311  -27.110 4.775   1.00 43.12  ? 67  THR A O     1 
ATOM   511  C CB    . THR A 1 69  ? 1.446   -26.861 7.252   1.00 41.38  ? 67  THR A CB    1 
ATOM   512  O OG1   . THR A 1 69  ? 2.450   -27.501 8.035   1.00 42.25  ? 67  THR A OG1   1 
ATOM   513  C CG2   . THR A 1 69  ? 0.757   -25.778 8.061   1.00 39.08  ? 67  THR A CG2   1 
ATOM   514  N N     . TRP A 1 70  ? -1.848  -27.663 6.326   1.00 37.26  ? 68  TRP A N     1 
ATOM   515  C CA    . TRP A 1 70  ? -3.042  -27.216 5.576   1.00 43.55  ? 68  TRP A CA    1 
ATOM   516  C C     . TRP A 1 70  ? -3.232  -25.711 5.738   1.00 45.43  ? 68  TRP A C     1 
ATOM   517  O O     . TRP A 1 70  ? -3.080  -25.220 6.844   1.00 43.06  ? 68  TRP A O     1 
ATOM   518  C CB    . TRP A 1 70  ? -4.296  -27.964 6.049   1.00 44.31  ? 68  TRP A CB    1 
ATOM   519  C CG    . TRP A 1 70  ? -5.551  -27.558 5.344   1.00 43.92  ? 68  TRP A CG    1 
ATOM   520  C CD1   . TRP A 1 70  ? -6.054  -28.069 4.183   1.00 40.16  ? 68  TRP A CD1   1 
ATOM   521  C CD2   . TRP A 1 70  ? -6.454  -26.526 5.765   1.00 46.49  ? 68  TRP A CD2   1 
ATOM   522  N NE1   . TRP A 1 70  ? -7.216  -27.431 3.857   1.00 41.20  ? 68  TRP A NE1   1 
ATOM   523  C CE2   . TRP A 1 70  ? -7.486  -26.475 4.806   1.00 47.65  ? 68  TRP A CE2   1 
ATOM   524  C CE3   . TRP A 1 70  ? -6.489  -25.648 6.854   1.00 48.31  ? 68  TRP A CE3   1 
ATOM   525  C CZ2   . TRP A 1 70  ? -8.546  -25.574 4.916   1.00 46.00  ? 68  TRP A CZ2   1 
ATOM   526  C CZ3   . TRP A 1 70  ? -7.551  -24.778 6.972   1.00 45.62  ? 68  TRP A CZ3   1 
ATOM   527  C CH2   . TRP A 1 70  ? -8.557  -24.734 6.005   1.00 43.81  ? 68  TRP A CH2   1 
ATOM   528  N N     . SER A 1 71  ? -3.644  -25.039 4.667   1.00 47.78  ? 69  SER A N     1 
ATOM   529  C CA    . SER A 1 71  ? -4.366  -23.745 4.730   1.00 48.32  ? 69  SER A CA    1 
ATOM   530  C C     . SER A 1 71  ? -5.456  -23.752 3.662   1.00 48.09  ? 69  SER A C     1 
ATOM   531  O O     . SER A 1 71  ? -5.452  -24.650 2.814   1.00 51.35  ? 69  SER A O     1 
ATOM   532  C CB    . SER A 1 71  ? -3.428  -22.612 4.558   1.00 43.72  ? 69  SER A CB    1 
ATOM   533  O OG    . SER A 1 71  ? -2.594  -22.870 3.468   1.00 43.51  ? 69  SER A OG    1 
ATOM   534  N N     . ALA A 1 72  ? -6.377  -22.801 3.730   1.00 49.84  ? 70  ALA A N     1 
ATOM   535  C CA    . ALA A 1 72  ? -7.486  -22.662 2.760   1.00 48.90  ? 70  ALA A CA    1 
ATOM   536  C C     . ALA A 1 72  ? -6.936  -22.774 1.334   1.00 43.95  ? 70  ALA A C     1 
ATOM   537  O O     . ALA A 1 72  ? -7.567  -23.446 0.540   1.00 44.06  ? 70  ALA A O     1 
ATOM   538  C CB    . ALA A 1 72  ? -8.197  -21.356 2.997   1.00 49.28  ? 70  ALA A CB    1 
ATOM   539  N N     . ASP A 1 73  ? -5.760  -22.196 1.076   1.00 48.91  ? 71  ASP A N     1 
ATOM   540  C CA    . ASP A 1 73  ? -5.137  -22.002 -0.261  1.00 54.41  ? 71  ASP A CA    1 
ATOM   541  C C     . ASP A 1 73  ? -4.340  -23.219 -0.738  1.00 53.95  ? 71  ASP A C     1 
ATOM   542  O O     . ASP A 1 73  ? -3.839  -23.146 -1.864  1.00 56.39  ? 71  ASP A O     1 
ATOM   543  C CB    . ASP A 1 73  ? -4.096  -20.876 -0.237  1.00 60.68  ? 71  ASP A CB    1 
ATOM   544  C CG    . ASP A 1 73  ? -4.685  -19.498 -0.007  1.00 72.17  ? 71  ASP A CG    1 
ATOM   545  O OD1   . ASP A 1 73  ? -5.936  -19.368 -0.123  1.00 66.01  ? 71  ASP A OD1   1 
ATOM   546  O OD2   . ASP A 1 73  ? -3.887  -18.566 0.276   1.00 77.06  ? 71  ASP A OD2   1 
ATOM   547  N N     . GLY A 1 74  ? -4.078  -24.223 0.099   1.00 44.51  ? 72  GLY A N     1 
ATOM   548  C CA    . GLY A 1 74  ? -3.041  -25.209 -0.251  1.00 44.19  ? 72  GLY A CA    1 
ATOM   549  C C     . GLY A 1 74  ? -2.573  -26.056 0.917   1.00 43.42  ? 72  GLY A C     1 
ATOM   550  O O     . GLY A 1 74  ? -3.086  -25.919 2.049   1.00 41.90  ? 72  GLY A O     1 
ATOM   551  N N     . VAL A 1 75  ? -1.606  -26.915 0.632   1.00 40.27  ? 73  VAL A N     1 
ATOM   552  C CA    . VAL A 1 75  ? -1.070  -27.906 1.594   1.00 43.22  ? 73  VAL A CA    1 
ATOM   553  C C     . VAL A 1 75  ? 0.430   -27.878 1.389   1.00 39.57  ? 73  VAL A C     1 
ATOM   554  O O     . VAL A 1 75  ? 0.855   -28.166 0.231   1.00 40.79  ? 73  VAL A O     1 
ATOM   555  C CB    . VAL A 1 75  ? -1.641  -29.321 1.384   1.00 43.86  ? 73  VAL A CB    1 
ATOM   556  C CG1   . VAL A 1 75  ? -0.901  -30.342 2.239   1.00 48.62  ? 73  VAL A CG1   1 
ATOM   557  C CG2   . VAL A 1 75  ? -3.132  -29.378 1.650   1.00 41.48  ? 73  VAL A CG2   1 
ATOM   558  N N     . LYS A 1 76  ? 1.142   -27.475 2.449   1.00 34.56  ? 74  LYS A N     1 
ATOM   559  C CA    . LYS A 1 76  ? 2.617   -27.403 2.511   1.00 36.62  ? 74  LYS A CA    1 
ATOM   560  C C     . LYS A 1 76  ? 3.141   -28.810 2.842   1.00 36.80  ? 74  LYS A C     1 
ATOM   561  O O     . LYS A 1 76  ? 2.551   -29.465 3.685   1.00 34.00  ? 74  LYS A O     1 
ATOM   562  C CB    . LYS A 1 76  ? 3.037   -26.381 3.569   1.00 39.96  ? 74  LYS A CB    1 
ATOM   563  C CG    . LYS A 1 76  ? 4.511   -26.000 3.521   1.00 48.86  ? 74  LYS A CG    1 
ATOM   564  C CD    . LYS A 1 76  ? 5.033   -25.167 4.716   1.00 53.89  ? 74  LYS A CD    1 
ATOM   565  C CE    . LYS A 1 76  ? 6.501   -24.778 4.584   1.00 51.95  ? 74  LYS A CE    1 
ATOM   566  N NZ    . LYS A 1 76  ? 7.359   -25.926 4.168   1.00 55.58  ? 74  LYS A NZ    1 
ATOM   567  N N     . THR A 1 77  ? 4.217   -29.204 2.168   1.00 35.33  ? 75  THR A N     1 
ATOM   568  C CA    . THR A 1 77  ? 4.861   -30.515 2.384   1.00 36.29  ? 75  THR A CA    1 
ATOM   569  C C     . THR A 1 77  ? 6.065   -30.300 3.293   1.00 38.47  ? 75  THR A C     1 
ATOM   570  O O     . THR A 1 77  ? 6.505   -29.156 3.415   1.00 41.47  ? 75  THR A O     1 
ATOM   571  C CB    . THR A 1 77  ? 5.311   -31.132 1.052   1.00 36.87  ? 75  THR A CB    1 
ATOM   572  O OG1   . THR A 1 77  ? 6.076   -30.181 0.311   1.00 30.96  ? 75  THR A OG1   1 
ATOM   573  C CG2   . THR A 1 77  ? 4.150   -31.636 0.222   1.00 38.07  ? 75  THR A CG2   1 
ATOM   574  N N     . PRO A 1 78  ? 6.606   -31.360 3.919   1.00 37.31  ? 76  PRO A N     1 
ATOM   575  C CA    . PRO A 1 78  ? 7.761   -31.224 4.790   1.00 37.54  ? 76  PRO A CA    1 
ATOM   576  C C     . PRO A 1 78  ? 8.978   -30.582 4.105   1.00 40.12  ? 76  PRO A C     1 
ATOM   577  O O     . PRO A 1 78  ? 9.109   -30.704 2.907   1.00 39.06  ? 76  PRO A O     1 
ATOM   578  C CB    . PRO A 1 78  ? 8.047   -32.680 5.189   1.00 39.55  ? 76  PRO A CB    1 
ATOM   579  C CG    . PRO A 1 78  ? 6.708   -33.354 5.095   1.00 35.76  ? 76  PRO A CG    1 
ATOM   580  C CD    . PRO A 1 78  ? 6.095   -32.729 3.864   1.00 37.07  ? 76  PRO A CD    1 
ATOM   581  N N     . THR A 1 79  ? 9.843   -29.938 4.890   1.00 38.39  ? 77  THR A N     1 
ATOM   582  C CA    . THR A 1 79  ? 11.041  -29.246 4.344   1.00 39.86  ? 77  THR A CA    1 
ATOM   583  C C     . THR A 1 79  ? 11.905  -30.223 3.545   1.00 39.37  ? 77  THR A C     1 
ATOM   584  O O     . THR A 1 79  ? 12.248  -31.272 4.096   1.00 38.52  ? 77  THR A O     1 
ATOM   585  C CB    . THR A 1 79  ? 11.836  -28.549 5.459   1.00 40.63  ? 77  THR A CB    1 
ATOM   586  O OG1   . THR A 1 79  ? 10.956  -27.678 6.168   1.00 43.35  ? 77  THR A OG1   1 
ATOM   587  C CG2   . THR A 1 79  ? 13.024  -27.769 4.943   1.00 35.54  ? 77  THR A CG2   1 
ATOM   588  N N     . GLY A 1 80  ? 12.228  -29.878 2.295   1.00 37.69  ? 78  GLY A N     1 
ATOM   589  C CA    . GLY A 1 80  ? 13.097  -30.710 1.438   1.00 37.26  ? 78  GLY A CA    1 
ATOM   590  C C     . GLY A 1 80  ? 12.348  -31.589 0.453   1.00 34.96  ? 78  GLY A C     1 
ATOM   591  O O     . GLY A 1 80  ? 12.957  -31.943 -0.556  1.00 41.09  ? 78  GLY A O     1 
ATOM   592  N N     . PHE A 1 81  ? 11.083  -31.910 0.713   1.00 29.74  ? 79  PHE A N     1 
ATOM   593  C CA    . PHE A 1 81  ? 10.325  -32.879 -0.121  1.00 31.60  ? 79  PHE A CA    1 
ATOM   594  C C     . PHE A 1 81  ? 10.190  -32.410 -1.573  1.00 33.90  ? 79  PHE A C     1 
ATOM   595  O O     . PHE A 1 81  ? 10.484  -33.199 -2.466  1.00 27.90  ? 79  PHE A O     1 
ATOM   596  C CB    . PHE A 1 81  ? 8.955   -33.136 0.511   1.00 30.68  ? 79  PHE A CB    1 
ATOM   597  C CG    . PHE A 1 81  ? 8.887   -34.257 1.518   1.00 33.72  ? 79  PHE A CG    1 
ATOM   598  C CD1   . PHE A 1 81  ? 9.904   -34.457 2.437   1.00 30.60  ? 79  PHE A CD1   1 
ATOM   599  C CD2   . PHE A 1 81  ? 7.794   -35.107 1.555   1.00 31.94  ? 79  PHE A CD2   1 
ATOM   600  C CE1   . PHE A 1 81  ? 9.835   -35.488 3.359   1.00 28.78  ? 79  PHE A CE1   1 
ATOM   601  C CE2   . PHE A 1 81  ? 7.724   -36.136 2.479   1.00 33.90  ? 79  PHE A CE2   1 
ATOM   602  C CZ    . PHE A 1 81  ? 8.746   -36.325 3.378   1.00 33.30  ? 79  PHE A CZ    1 
ATOM   603  N N     . LYS A 1 82  ? 9.766   -31.161 -1.787  1.00 35.09  ? 80  LYS A N     1 
ATOM   604  C CA    . LYS A 1 82  ? 9.500   -30.680 -3.166  1.00 35.72  ? 80  LYS A CA    1 
ATOM   605  C C     . LYS A 1 82  ? 10.817  -30.502 -3.918  1.00 35.20  ? 80  LYS A C     1 
ATOM   606  O O     . LYS A 1 82  ? 10.865  -30.842 -5.097  1.00 42.00  ? 80  LYS A O     1 
ATOM   607  C CB    . LYS A 1 82  ? 8.628   -29.422 -3.135  1.00 40.54  ? 80  LYS A CB    1 
ATOM   608  C CG    . LYS A 1 82  ? 9.274   -28.133 -2.656  1.00 41.76  ? 80  LYS A CG    1 
ATOM   609  C CD    . LYS A 1 82  ? 8.271   -27.000 -2.609  1.00 44.09  ? 80  LYS A CD    1 
ATOM   610  C CE    . LYS A 1 82  ? 8.900   -25.646 -2.362  1.00 51.87  ? 80  LYS A CE    1 
ATOM   611  N NZ    . LYS A 1 82  ? 9.461   -25.540 -0.995  1.00 55.03  ? 80  LYS A NZ    1 
ATOM   612  N N     . GLU A 1 83  ? 11.845  -30.018 -3.241  1.00 39.13  ? 81  GLU A N     1 
ATOM   613  C CA    . GLU A 1 83  ? 13.171  -29.887 -3.880  1.00 36.94  ? 81  GLU A CA    1 
ATOM   614  C C     . GLU A 1 83  ? 13.616  -31.283 -4.285  1.00 34.44  ? 81  GLU A C     1 
ATOM   615  O O     . GLU A 1 83  ? 14.066  -31.454 -5.419  1.00 35.12  ? 81  GLU A O     1 
ATOM   616  C CB    . GLU A 1 83  ? 14.132  -29.207 -2.909  1.00 42.79  ? 81  GLU A CB    1 
ATOM   617  C CG    . GLU A 1 83  ? 13.716  -27.794 -2.539  1.00 48.77  ? 81  GLU A CG    1 
ATOM   618  C CD    . GLU A 1 83  ? 12.615  -27.659 -1.499  1.00 53.60  ? 81  GLU A CD    1 
ATOM   619  O OE1   . GLU A 1 83  ? 11.971  -26.598 -1.463  1.00 48.49  ? 81  GLU A OE1   1 
ATOM   620  O OE2   . GLU A 1 83  ? 12.404  -28.612 -0.730  1.00 51.12  ? 81  GLU A OE2   1 
ATOM   621  N N     . ALA A 1 84  ? 13.502  -32.232 -3.368  1.00 37.81  ? 82  ALA A N     1 
ATOM   622  C CA    . ALA A 1 84  ? 13.803  -33.641 -3.703  1.00 35.49  ? 82  ALA A CA    1 
ATOM   623  C C     . ALA A 1 84  ? 12.952  -34.103 -4.908  1.00 31.27  ? 82  ALA A C     1 
ATOM   624  O O     . ALA A 1 84  ? 13.511  -34.765 -5.776  1.00 30.08  ? 82  ALA A O     1 
ATOM   625  C CB    . ALA A 1 84  ? 13.594  -34.488 -2.482  1.00 36.17  ? 82  ALA A CB    1 
ATOM   626  N N     . TYR A 1 85  ? 11.657  -33.783 -4.960  1.00 32.19  ? 83  TYR A N     1 
ATOM   627  C CA    . TYR A 1 85  ? 10.765  -34.168 -6.090  1.00 36.44  ? 83  TYR A CA    1 
ATOM   628  C C     . TYR A 1 85  ? 11.302  -33.514 -7.386  1.00 42.68  ? 83  TYR A C     1 
ATOM   629  O O     . TYR A 1 85  ? 11.346  -34.229 -8.433  1.00 37.84  ? 83  TYR A O     1 
ATOM   630  C CB    . TYR A 1 85  ? 9.271   -33.912 -5.802  1.00 37.67  ? 83  TYR A CB    1 
ATOM   631  C CG    . TYR A 1 85  ? 8.398   -34.505 -6.882  1.00 39.45  ? 83  TYR A CG    1 
ATOM   632  C CD1   . TYR A 1 85  ? 8.362   -35.876 -7.106  1.00 36.56  ? 83  TYR A CD1   1 
ATOM   633  C CD2   . TYR A 1 85  ? 7.720   -33.694 -7.770  1.00 42.66  ? 83  TYR A CD2   1 
ATOM   634  C CE1   . TYR A 1 85  ? 7.653   -36.433 -8.158  1.00 36.60  ? 83  TYR A CE1   1 
ATOM   635  C CE2   . TYR A 1 85  ? 6.988   -34.234 -8.814  1.00 43.96  ? 83  TYR A CE2   1 
ATOM   636  C CZ    . TYR A 1 85  ? 6.965   -35.605 -9.018  1.00 39.72  ? 83  TYR A CZ    1 
ATOM   637  O OH    . TYR A 1 85  ? 6.260   -36.094 -10.073 1.00 32.16  ? 83  TYR A OH    1 
ATOM   638  N N     . GLN A 1 86  ? 11.795  -32.260 -7.331  1.00 44.10  ? 84  GLN A N     1 
ATOM   639  C CA    . GLN A 1 86  ? 12.475  -31.607 -8.499  1.00 47.53  ? 84  GLN A CA    1 
ATOM   640  C C     . GLN A 1 86  ? 13.668  -32.451 -8.964  1.00 43.78  ? 84  GLN A C     1 
ATOM   641  O O     . GLN A 1 86  ? 13.730  -32.720 -10.167 1.00 38.22  ? 84  GLN A O     1 
ATOM   642  C CB    . GLN A 1 86  ? 12.959  -30.183 -8.225  1.00 52.94  ? 84  GLN A CB    1 
ATOM   643  C CG    . GLN A 1 86  ? 11.962  -29.115 -8.647  1.00 64.20  ? 84  GLN A CG    1 
ATOM   644  C CD    . GLN A 1 86  ? 12.069  -27.872 -7.793  1.00 79.20  ? 84  GLN A CD    1 
ATOM   645  O OE1   . GLN A 1 86  ? 13.145  -27.285 -7.648  1.00 88.59  ? 84  GLN A OE1   1 
ATOM   646  N NE2   . GLN A 1 86  ? 10.949  -27.458 -7.209  1.00 78.93  ? 84  GLN A NE2   1 
ATOM   647  N N     . GLN A 1 87  ? 14.575  -32.863 -8.068  1.00 38.50  ? 85  GLN A N     1 
ATOM   648  C CA    . GLN A 1 87  ? 15.801  -33.597 -8.483  1.00 40.07  ? 85  GLN A CA    1 
ATOM   649  C C     . GLN A 1 87  ? 15.395  -34.923 -9.129  1.00 41.13  ? 85  GLN A C     1 
ATOM   650  O O     . GLN A 1 87  ? 16.127  -35.413 -9.998  1.00 40.97  ? 85  GLN A O     1 
ATOM   651  C CB    . GLN A 1 87  ? 16.759  -33.841 -7.322  1.00 42.03  ? 85  GLN A CB    1 
ATOM   652  C CG    . GLN A 1 87  ? 17.265  -32.573 -6.630  1.00 47.61  ? 85  GLN A CG    1 
ATOM   653  C CD    . GLN A 1 87  ? 18.225  -32.917 -5.505  1.00 55.83  ? 85  GLN A CD    1 
ATOM   654  O OE1   . GLN A 1 87  ? 19.213  -33.642 -5.696  1.00 52.95  ? 85  GLN A OE1   1 
ATOM   655  N NE2   . GLN A 1 87  ? 17.924  -32.436 -4.301  1.00 55.98  ? 85  GLN A NE2   1 
ATOM   656  N N     . PHE A 1 88  ? 14.264  -35.476 -8.689  1.00 44.61  ? 86  PHE A N     1 
ATOM   657  C CA    . PHE A 1 88  ? 13.734  -36.792 -9.127  1.00 44.43  ? 86  PHE A CA    1 
ATOM   658  C C     . PHE A 1 88  ? 13.167  -36.630 -10.543 1.00 40.62  ? 86  PHE A C     1 
ATOM   659  O O     . PHE A 1 88  ? 13.440  -37.498 -11.341 1.00 34.77  ? 86  PHE A O     1 
ATOM   660  C CB    . PHE A 1 88  ? 12.663  -37.280 -8.144  1.00 40.94  ? 86  PHE A CB    1 
ATOM   661  C CG    . PHE A 1 88  ? 12.152  -38.692 -8.327  1.00 34.99  ? 86  PHE A CG    1 
ATOM   662  C CD1   . PHE A 1 88  ? 12.915  -39.778 -7.912  1.00 33.26  ? 86  PHE A CD1   1 
ATOM   663  C CD2   . PHE A 1 88  ? 10.882  -38.926 -8.833  1.00 34.20  ? 86  PHE A CD2   1 
ATOM   664  C CE1   . PHE A 1 88  ? 12.428  -41.068 -8.022  1.00 30.98  ? 86  PHE A CE1   1 
ATOM   665  C CE2   . PHE A 1 88  ? 10.392  -40.219 -8.931  1.00 34.21  ? 86  PHE A CE2   1 
ATOM   666  C CZ    . PHE A 1 88  ? 11.161  -41.283 -8.497  1.00 32.72  ? 86  PHE A CZ    1 
ATOM   667  N N     . VAL A 1 89  ? 12.370  -35.576 -10.778 1.00 38.38  ? 87  VAL A N     1 
ATOM   668  C CA    . VAL A 1 89  ? 11.918  -35.143 -12.130 1.00 40.07  ? 87  VAL A CA    1 
ATOM   669  C C     . VAL A 1 89  ? 13.145  -34.877 -13.005 1.00 40.26  ? 87  VAL A C     1 
ATOM   670  O O     . VAL A 1 89  ? 13.215  -35.494 -14.048 1.00 43.25  ? 87  VAL A O     1 
ATOM   671  C CB    . VAL A 1 89  ? 10.972  -33.935 -12.078 1.00 40.99  ? 87  VAL A CB    1 
ATOM   672  C CG1   . VAL A 1 89  ? 10.636  -33.459 -13.489 1.00 45.10  ? 87  VAL A CG1   1 
ATOM   673  C CG2   . VAL A 1 89  ? 9.691   -34.262 -11.320 1.00 36.70  ? 87  VAL A CG2   1 
ATOM   674  N N     . GLU A 1 90  ? 14.140  -34.115 -12.535 1.00 48.92  ? 88  GLU A N     1 
ATOM   675  C CA    . GLU A 1 90  ? 15.404  -33.828 -13.283 1.00 45.99  ? 88  GLU A CA    1 
ATOM   676  C C     . GLU A 1 90  ? 16.163  -35.142 -13.546 1.00 45.14  ? 88  GLU A C     1 
ATOM   677  O O     . GLU A 1 90  ? 16.864  -35.247 -14.591 1.00 47.08  ? 88  GLU A O     1 
ATOM   678  C CB    . GLU A 1 90  ? 16.246  -32.772 -12.550 1.00 53.10  ? 88  GLU A CB    1 
ATOM   679  C CG    . GLU A 1 90  ? 15.651  -31.350 -12.603 1.00 57.73  ? 88  GLU A CG    1 
ATOM   680  C CD    . GLU A 1 90  ? 15.880  -30.413 -11.411 1.00 62.05  ? 88  GLU A CD    1 
ATOM   681  O OE1   . GLU A 1 90  ? 15.295  -29.317 -11.415 1.00 59.46  ? 88  GLU A OE1   1 
ATOM   682  O OE2   . GLU A 1 90  ? 16.626  -30.770 -10.467 1.00 65.63  ? 88  GLU A OE2   1 
ATOM   683  N N     . GLY A 1 91  ? 15.996  -36.154 -12.701 1.00 37.98  ? 89  GLY A N     1 
ATOM   684  C CA    . GLY A 1 91  ? 16.668  -37.452 -12.916 1.00 37.14  ? 89  GLY A CA    1 
ATOM   685  C C     . GLY A 1 91  ? 15.993  -38.329 -13.956 1.00 38.35  ? 89  GLY A C     1 
ATOM   686  O O     . GLY A 1 91  ? 16.595  -39.324 -14.358 1.00 40.74  ? 89  GLY A O     1 
ATOM   687  N N     . GLY A 1 92  ? 14.775  -37.987 -14.351 1.00 43.28  ? 90  GLY A N     1 
ATOM   688  C CA    . GLY A 1 92  ? 14.002  -38.756 -15.340 1.00 43.33  ? 90  GLY A CA    1 
ATOM   689  C C     . GLY A 1 92  ? 13.363  -40.020 -14.774 1.00 45.07  ? 90  GLY A C     1 
ATOM   690  O O     . GLY A 1 92  ? 12.807  -40.830 -15.583 1.00 43.92  ? 90  GLY A O     1 
ATOM   691  N N     . TRP A 1 93  ? 13.359  -40.166 -13.454 1.00 39.67  ? 91  TRP A N     1 
ATOM   692  C CA    . TRP A 1 93  ? 12.835  -41.396 -12.805 1.00 38.23  ? 91  TRP A CA    1 
ATOM   693  C C     . TRP A 1 93  ? 11.345  -41.650 -13.105 1.00 34.45  ? 91  TRP A C     1 
ATOM   694  O O     . TRP A 1 93  ? 11.005  -42.811 -13.305 1.00 35.64  ? 91  TRP A O     1 
ATOM   695  C CB    . TRP A 1 93  ? 13.153  -41.342 -11.308 1.00 36.81  ? 91  TRP A CB    1 
ATOM   696  C CG    . TRP A 1 93  ? 14.624  -41.355 -11.040 1.00 34.48  ? 91  TRP A CG    1 
ATOM   697  C CD1   . TRP A 1 93  ? 15.400  -40.309 -10.641 1.00 37.27  ? 91  TRP A CD1   1 
ATOM   698  C CD2   . TRP A 1 93  ? 15.506  -42.479 -11.187 1.00 34.36  ? 91  TRP A CD2   1 
ATOM   699  N NE1   . TRP A 1 93  ? 16.702  -40.708 -10.515 1.00 36.15  ? 91  TRP A NE1   1 
ATOM   700  C CE2   . TRP A 1 93  ? 16.798  -42.034 -10.843 1.00 34.49  ? 91  TRP A CE2   1 
ATOM   701  C CE3   . TRP A 1 93  ? 15.331  -43.813 -11.564 1.00 31.83  ? 91  TRP A CE3   1 
ATOM   702  C CZ2   . TRP A 1 93  ? 17.904  -42.879 -10.867 1.00 31.53  ? 91  TRP A CZ2   1 
ATOM   703  C CZ3   . TRP A 1 93  ? 16.425  -44.646 -11.589 1.00 36.59  ? 91  TRP A CZ3   1 
ATOM   704  C CH2   . TRP A 1 93  ? 17.694  -44.183 -11.246 1.00 33.39  ? 91  TRP A CH2   1 
ATOM   705  N N     . PRO A 1 94  ? 10.433  -40.660 -13.127 1.00 31.53  ? 92  PRO A N     1 
ATOM   706  C CA    . PRO A 1 94  ? 9.025   -40.967 -13.394 1.00 33.50  ? 92  PRO A CA    1 
ATOM   707  C C     . PRO A 1 94  ? 8.756   -41.598 -14.779 1.00 39.54  ? 92  PRO A C     1 
ATOM   708  O O     . PRO A 1 94  ? 7.791   -42.320 -14.938 1.00 42.16  ? 92  PRO A O     1 
ATOM   709  C CB    . PRO A 1 94  ? 8.352   -39.588 -13.339 1.00 33.37  ? 92  PRO A CB    1 
ATOM   710  C CG    . PRO A 1 94  ? 9.309   -38.717 -12.520 1.00 34.56  ? 92  PRO A CG    1 
ATOM   711  C CD    . PRO A 1 94  ? 10.687  -39.236 -12.874 1.00 32.81  ? 92  PRO A CD    1 
ATOM   712  N N     . SER A 1 95  ? 9.613   -41.285 -15.754 1.00 37.87  ? 93  SER A N     1 
ATOM   713  C CA    . SER A 1 95  ? 9.481   -41.670 -17.179 1.00 40.15  ? 93  SER A CA    1 
ATOM   714  C C     . SER A 1 95  ? 10.051  -43.082 -17.381 1.00 38.79  ? 93  SER A C     1 
ATOM   715  O O     . SER A 1 95  ? 9.906   -43.647 -18.484 1.00 41.17  ? 93  SER A O     1 
ATOM   716  C CB    . SER A 1 95  ? 10.170  -40.623 -18.064 1.00 34.01  ? 93  SER A CB    1 
ATOM   717  O OG    . SER A 1 95  ? 11.575  -40.840 -18.108 1.00 34.34  ? 93  SER A OG    1 
ATOM   718  N N     . LEU A 1 96  ? 10.766  -43.614 -16.401 1.00 38.99  ? 94  LEU A N     1 
ATOM   719  C CA    . LEU A 1 96  ? 11.512  -44.889 -16.599 1.00 43.00  ? 94  LEU A CA    1 
ATOM   720  C C     . LEU A 1 96  ? 10.698  -46.022 -17.223 1.00 43.73  ? 94  LEU A C     1 
ATOM   721  O O     . LEU A 1 96  ? 11.096  -46.486 -18.296 1.00 50.96  ? 94  LEU A O     1 
ATOM   722  C CB    . LEU A 1 96  ? 12.089  -45.347 -15.256 1.00 41.24  ? 94  LEU A CB    1 
ATOM   723  C CG    . LEU A 1 96  ? 13.199  -46.391 -15.351 1.00 47.77  ? 94  LEU A CG    1 
ATOM   724  C CD1   . LEU A 1 96  ? 14.391  -45.994 -14.499 1.00 53.35  ? 94  LEU A CD1   1 
ATOM   725  C CD2   . LEU A 1 96  ? 12.690  -47.764 -14.948 1.00 55.53  ? 94  LEU A CD2   1 
ATOM   726  N N     . ALA A 1 97  ? 9.634   -46.467 -16.573 1.00 39.70  ? 95  ALA A N     1 
ATOM   727  C CA    . ALA A 1 97  ? 8.936   -47.681 -17.042 1.00 43.41  ? 95  ALA A CA    1 
ATOM   728  C C     . ALA A 1 97  ? 7.612   -47.299 -17.705 1.00 44.07  ? 95  ALA A C     1 
ATOM   729  O O     . ALA A 1 97  ? 6.607   -47.931 -17.387 1.00 51.20  ? 95  ALA A O     1 
ATOM   730  C CB    . ALA A 1 97  ? 8.763   -48.668 -15.918 1.00 44.19  ? 95  ALA A CB    1 
ATOM   731  N N     . HIS A 1 98  ? 7.640   -46.360 -18.653 1.00 41.33  ? 96  HIS A N     1 
ATOM   732  C CA    . HIS A 1 98  ? 6.453   -45.929 -19.438 1.00 45.70  ? 96  HIS A CA    1 
ATOM   733  C C     . HIS A 1 98  ? 6.780   -45.877 -20.929 1.00 46.43  ? 96  HIS A C     1 
ATOM   734  O O     . HIS A 1 98  ? 7.972   -45.784 -21.290 1.00 44.47  ? 96  HIS A O     1 
ATOM   735  C CB    . HIS A 1 98  ? 5.925   -44.619 -18.877 1.00 48.04  ? 96  HIS A CB    1 
ATOM   736  C CG    . HIS A 1 98  ? 5.444   -44.776 -17.473 1.00 52.20  ? 96  HIS A CG    1 
ATOM   737  N ND1   . HIS A 1 98  ? 4.182   -45.242 -17.174 1.00 51.68  ? 96  HIS A ND1   1 
ATOM   738  C CD2   . HIS A 1 98  ? 6.056   -44.556 -16.291 1.00 50.72  ? 96  HIS A CD2   1 
ATOM   739  C CE1   . HIS A 1 98  ? 4.036   -45.294 -15.874 1.00 49.56  ? 96  HIS A CE1   1 
ATOM   740  N NE2   . HIS A 1 98  ? 5.170   -44.877 -15.315 1.00 48.41  ? 96  HIS A NE2   1 
ATOM   741  N N     . ASP A 1 99  ? 5.741   -45.970 -21.756 1.00 54.90  ? 97  ASP A N     1 
ATOM   742  C CA    . ASP A 1 99  ? 5.856   -46.185 -23.226 1.00 54.60  ? 97  ASP A CA    1 
ATOM   743  C C     . ASP A 1 99  ? 6.616   -45.009 -23.862 1.00 54.24  ? 97  ASP A C     1 
ATOM   744  O O     . ASP A 1 99  ? 6.487   -43.845 -23.410 1.00 51.44  ? 97  ASP A O     1 
ATOM   745  C CB    . ASP A 1 99  ? 4.485   -46.477 -23.856 1.00 61.03  ? 97  ASP A CB    1 
ATOM   746  C CG    . ASP A 1 99  ? 3.471   -45.346 -23.776 1.00 70.18  ? 97  ASP A CG    1 
ATOM   747  O OD1   . ASP A 1 99  ? 3.536   -44.447 -24.626 1.00 72.31  ? 97  ASP A OD1   1 
ATOM   748  O OD2   . ASP A 1 99  ? 2.605   -45.383 -22.875 1.00 90.78  ? 97  ASP A OD2   1 
ATOM   749  N N     . VAL A 1 100 ? 7.407   -45.306 -24.885 1.00 57.74  ? 98  VAL A N     1 
ATOM   750  C CA    . VAL A 1 100 ? 8.292   -44.311 -25.554 1.00 58.26  ? 98  VAL A CA    1 
ATOM   751  C C     . VAL A 1 100 ? 7.437   -43.200 -26.184 1.00 56.74  ? 98  VAL A C     1 
ATOM   752  O O     . VAL A 1 100 ? 7.877   -42.036 -26.152 1.00 56.20  ? 98  VAL A O     1 
ATOM   753  C CB    . VAL A 1 100 ? 9.239   -44.996 -26.560 1.00 56.82  ? 98  VAL A CB    1 
ATOM   754  C CG1   . VAL A 1 100 ? 9.878   -43.996 -27.501 1.00 61.36  ? 98  VAL A CG1   1 
ATOM   755  C CG2   . VAL A 1 100 ? 10.308  -45.815 -25.839 1.00 54.61  ? 98  VAL A CG2   1 
ATOM   756  N N     . GLU A 1 101 ? 6.243   -43.488 -26.705 1.00 56.32  ? 99  GLU A N     1 
ATOM   757  C CA    . GLU A 1 101 ? 5.535   -42.460 -27.526 1.00 58.44  ? 99  GLU A CA    1 
ATOM   758  C C     . GLU A 1 101 ? 4.961   -41.359 -26.616 1.00 54.50  ? 99  GLU A C     1 
ATOM   759  O O     . GLU A 1 101 ? 4.741   -40.262 -27.119 1.00 54.52  ? 99  GLU A O     1 
ATOM   760  C CB    . GLU A 1 101 ? 4.519   -43.065 -28.506 1.00 61.19  ? 99  GLU A CB    1 
ATOM   761  C CG    . GLU A 1 101 ? 3.565   -44.080 -27.910 1.00 71.45  ? 99  GLU A CG    1 
ATOM   762  C CD    . GLU A 1 101 ? 4.062   -45.517 -27.840 1.00 79.16  ? 99  GLU A CD    1 
ATOM   763  O OE1   . GLU A 1 101 ? 5.263   -45.761 -28.118 1.00 69.95  ? 99  GLU A OE1   1 
ATOM   764  O OE2   . GLU A 1 101 ? 3.241   -46.399 -27.484 1.00 89.16  ? 99  GLU A OE2   1 
ATOM   765  N N     . HIS A 1 102 ? 4.810   -41.587 -25.308 1.00 57.73  ? 100 HIS A N     1 
ATOM   766  C CA    . HIS A 1 102 ? 4.167   -40.609 -24.386 1.00 55.25  ? 100 HIS A CA    1 
ATOM   767  C C     . HIS A 1 102 ? 5.182   -39.919 -23.463 1.00 53.98  ? 100 HIS A C     1 
ATOM   768  O O     . HIS A 1 102 ? 4.735   -39.237 -22.499 1.00 50.85  ? 100 HIS A O     1 
ATOM   769  C CB    . HIS A 1 102 ? 3.010   -41.286 -23.655 1.00 56.63  ? 100 HIS A CB    1 
ATOM   770  C CG    . HIS A 1 102 ? 1.849   -41.485 -24.567 1.00 55.26  ? 100 HIS A CG    1 
ATOM   771  N ND1   . HIS A 1 102 ? 1.112   -40.408 -25.040 1.00 57.13  ? 100 HIS A ND1   1 
ATOM   772  C CD2   . HIS A 1 102 ? 1.306   -42.597 -25.105 1.00 50.83  ? 100 HIS A CD2   1 
ATOM   773  C CE1   . HIS A 1 102 ? 0.161   -40.846 -25.830 1.00 53.81  ? 100 HIS A CE1   1 
ATOM   774  N NE2   . HIS A 1 102 ? 0.261   -42.185 -25.884 1.00 58.46  ? 100 HIS A NE2   1 
ATOM   775  N N     . GLY A 1 103 ? 6.476   -40.008 -23.793 1.00 46.98  ? 101 GLY A N     1 
ATOM   776  C CA    . GLY A 1 103 ? 7.555   -39.317 -23.060 1.00 46.06  ? 101 GLY A CA    1 
ATOM   777  C C     . GLY A 1 103 ? 8.466   -40.295 -22.348 1.00 46.95  ? 101 GLY A C     1 
ATOM   778  O O     . GLY A 1 103 ? 9.467   -39.836 -21.789 1.00 44.03  ? 101 GLY A O     1 
ATOM   779  N N     . GLY A 1 104 ? 8.161   -41.601 -22.417 1.00 47.39  ? 102 GLY A N     1 
ATOM   780  C CA    . GLY A 1 104 ? 8.749   -42.631 -21.541 1.00 42.63  ? 102 GLY A CA    1 
ATOM   781  C C     . GLY A 1 104 ? 10.082  -43.118 -22.069 1.00 42.65  ? 102 GLY A C     1 
ATOM   782  O O     . GLY A 1 104 ? 10.394  -42.792 -23.215 1.00 46.20  ? 102 GLY A O     1 
ATOM   783  N N     . GLN A 1 105 ? 10.811  -43.894 -21.261 1.00 36.58  ? 103 GLN A N     1 
ATOM   784  C CA    . GLN A 1 105 ? 12.111  -44.492 -21.652 1.00 35.59  ? 103 GLN A CA    1 
ATOM   785  C C     . GLN A 1 105 ? 11.825  -45.919 -22.104 1.00 36.23  ? 103 GLN A C     1 
ATOM   786  O O     . GLN A 1 105 ? 12.730  -46.540 -22.674 1.00 33.22  ? 103 GLN A O     1 
ATOM   787  C CB    . GLN A 1 105 ? 13.065  -44.454 -20.461 1.00 37.62  ? 103 GLN A CB    1 
ATOM   788  C CG    . GLN A 1 105 ? 13.315  -43.058 -19.911 1.00 38.19  ? 103 GLN A CG    1 
ATOM   789  C CD    . GLN A 1 105 ? 14.180  -43.080 -18.675 1.00 43.43  ? 103 GLN A CD    1 
ATOM   790  O OE1   . GLN A 1 105 ? 15.111  -43.871 -18.555 1.00 44.67  ? 103 GLN A OE1   1 
ATOM   791  N NE2   . GLN A 1 105 ? 13.877  -42.201 -17.737 1.00 46.98  ? 103 GLN A NE2   1 
ATOM   792  N N     . GLY A 1 106 ? 10.633  -46.423 -21.794 1.00 39.02  ? 104 GLY A N     1 
ATOM   793  C CA    . GLY A 1 106 ? 10.145  -47.744 -22.254 1.00 35.68  ? 104 GLY A CA    1 
ATOM   794  C C     . GLY A 1 106 ? 10.824  -48.932 -21.583 1.00 37.71  ? 104 GLY A C     1 
ATOM   795  O O     . GLY A 1 106 ? 10.649  -50.043 -22.074 1.00 41.33  ? 104 GLY A O     1 
ATOM   796  N N     . LEU A 1 107 ? 11.535  -48.761 -20.469 1.00 40.98  ? 105 LEU A N     1 
ATOM   797  C CA    . LEU A 1 107 ? 12.140  -49.889 -19.689 1.00 39.66  ? 105 LEU A CA    1 
ATOM   798  C C     . LEU A 1 107 ? 11.056  -50.715 -18.981 1.00 35.42  ? 105 LEU A C     1 
ATOM   799  O O     . LEU A 1 107 ? 9.972   -50.218 -18.677 1.00 33.15  ? 105 LEU A O     1 
ATOM   800  C CB    . LEU A 1 107 ? 13.130  -49.288 -18.691 1.00 46.74  ? 105 LEU A CB    1 
ATOM   801  C CG    . LEU A 1 107 ? 14.380  -48.700 -19.347 1.00 50.96  ? 105 LEU A CG    1 
ATOM   802  C CD1   . LEU A 1 107 ? 15.213  -47.920 -18.345 1.00 51.34  ? 105 LEU A CD1   1 
ATOM   803  C CD2   . LEU A 1 107 ? 15.210  -49.808 -19.979 1.00 51.92  ? 105 LEU A CD2   1 
ATOM   804  N N     . PRO A 1 108 ? 11.309  -52.007 -18.680 1.00 30.36  ? 106 PRO A N     1 
ATOM   805  C CA    . PRO A 1 108 ? 10.320  -52.870 -18.032 1.00 32.08  ? 106 PRO A CA    1 
ATOM   806  C C     . PRO A 1 108 ? 9.814   -52.422 -16.645 1.00 37.04  ? 106 PRO A C     1 
ATOM   807  O O     . PRO A 1 108 ? 10.571  -51.811 -15.876 1.00 37.71  ? 106 PRO A O     1 
ATOM   808  C CB    . PRO A 1 108 ? 11.080  -54.190 -17.795 1.00 34.26  ? 106 PRO A CB    1 
ATOM   809  C CG    . PRO A 1 108 ? 12.282  -54.143 -18.706 1.00 33.67  ? 106 PRO A CG    1 
ATOM   810  C CD    . PRO A 1 108 ? 12.600  -52.673 -18.858 1.00 33.16  ? 106 PRO A CD    1 
ATOM   811  N N     . GLU A 1 109 ? 8.582   -52.792 -16.312 1.00 33.45  ? 107 GLU A N     1 
ATOM   812  C CA    . GLU A 1 109 ? 7.947   -52.429 -15.030 1.00 37.14  ? 107 GLU A CA    1 
ATOM   813  C C     . GLU A 1 109 ? 8.734   -53.011 -13.857 1.00 32.08  ? 107 GLU A C     1 
ATOM   814  O O     . GLU A 1 109 ? 8.814   -52.364 -12.800 1.00 33.22  ? 107 GLU A O     1 
ATOM   815  C CB    . GLU A 1 109 ? 6.516   -52.942 -15.017 1.00 45.71  ? 107 GLU A CB    1 
ATOM   816  C CG    . GLU A 1 109 ? 5.579   -52.034 -15.774 1.00 53.10  ? 107 GLU A CG    1 
ATOM   817  C CD    . GLU A 1 109 ? 4.824   -51.119 -14.842 1.00 66.51  ? 107 GLU A CD    1 
ATOM   818  O OE1   . GLU A 1 109 ? 4.551   -49.954 -15.234 1.00 76.61  ? 107 GLU A OE1   1 
ATOM   819  O OE2   . GLU A 1 109 ? 4.551   -51.574 -13.705 1.00 64.97  ? 107 GLU A OE2   1 
ATOM   820  N N     . SER A 1 110 ? 9.264   -54.208 -14.027 1.00 31.37  ? 108 SER A N     1 
ATOM   821  C CA    . SER A 1 110 ? 10.072  -54.921 -13.016 1.00 31.43  ? 108 SER A CA    1 
ATOM   822  C C     . SER A 1 110 ? 11.414  -54.208 -12.754 1.00 36.08  ? 108 SER A C     1 
ATOM   823  O O     . SER A 1 110 ? 12.032  -54.522 -11.720 1.00 37.35  ? 108 SER A O     1 
ATOM   824  C CB    . SER A 1 110 ? 10.300  -56.305 -13.467 1.00 29.98  ? 108 SER A CB    1 
ATOM   825  O OG    . SER A 1 110 ? 11.211  -56.280 -14.550 1.00 29.87  ? 108 SER A OG    1 
ATOM   826  N N     . LEU A 1 111 ? 11.929  -53.384 -13.678 1.00 38.31  ? 109 LEU A N     1 
ATOM   827  C CA    . LEU A 1 111 ? 13.097  -52.503 -13.392 1.00 40.05  ? 109 LEU A CA    1 
ATOM   828  C C     . LEU A 1 111 ? 12.641  -51.307 -12.547 1.00 37.43  ? 109 LEU A C     1 
ATOM   829  O O     . LEU A 1 111 ? 13.317  -50.980 -11.566 1.00 39.69  ? 109 LEU A O     1 
ATOM   830  C CB    . LEU A 1 111 ? 13.760  -52.021 -14.678 1.00 39.69  ? 109 LEU A CB    1 
ATOM   831  C CG    . LEU A 1 111 ? 15.006  -51.156 -14.491 1.00 40.63  ? 109 LEU A CG    1 
ATOM   832  C CD1   . LEU A 1 111 ? 15.953  -51.694 -13.411 1.00 37.97  ? 109 LEU A CD1   1 
ATOM   833  C CD2   . LEU A 1 111 ? 15.737  -51.023 -15.817 1.00 42.78  ? 109 LEU A CD2   1 
ATOM   834  N N     . GLY A 1 112 ? 11.551  -50.673 -12.937 1.00 34.86  ? 110 GLY A N     1 
ATOM   835  C CA    . GLY A 1 112 ? 10.899  -49.589 -12.183 1.00 37.49  ? 110 GLY A CA    1 
ATOM   836  C C     . GLY A 1 112 ? 10.519  -50.003 -10.768 1.00 34.49  ? 110 GLY A C     1 
ATOM   837  O O     . GLY A 1 112 ? 10.530  -49.163 -9.903  1.00 32.35  ? 110 GLY A O     1 
ATOM   838  N N     . LEU A 1 113 ? 10.192  -51.264 -10.548 1.00 38.17  ? 111 LEU A N     1 
ATOM   839  C CA    . LEU A 1 113 ? 9.879   -51.818 -9.218  1.00 39.24  ? 111 LEU A CA    1 
ATOM   840  C C     . LEU A 1 113 ? 11.137  -51.870 -8.337  1.00 39.81  ? 111 LEU A C     1 
ATOM   841  O O     . LEU A 1 113 ? 11.018  -51.581 -7.111  1.00 36.62  ? 111 LEU A O     1 
ATOM   842  C CB    . LEU A 1 113 ? 9.252   -53.200 -9.403  1.00 43.94  ? 111 LEU A CB    1 
ATOM   843  C CG    . LEU A 1 113 ? 8.014   -53.450 -8.548  1.00 50.77  ? 111 LEU A CG    1 
ATOM   844  C CD1   . LEU A 1 113 ? 6.932   -52.399 -8.809  1.00 47.27  ? 111 LEU A CD1   1 
ATOM   845  C CD2   . LEU A 1 113 ? 7.494   -54.857 -8.797  1.00 57.48  ? 111 LEU A CD2   1 
ATOM   846  N N     . ALA A 1 114 ? 12.307  -52.234 -8.872  1.00 36.51  ? 112 ALA A N     1 
ATOM   847  C CA    . ALA A 1 114 ? 13.563  -52.192 -8.077  1.00 35.44  ? 112 ALA A CA    1 
ATOM   848  C C     . ALA A 1 114 ? 13.780  -50.765 -7.520  1.00 33.95  ? 112 ALA A C     1 
ATOM   849  O O     . ALA A 1 114 ? 14.101  -50.599 -6.338  1.00 30.65  ? 112 ALA A O     1 
ATOM   850  C CB    . ALA A 1 114 ? 14.737  -52.661 -8.900  1.00 34.98  ? 112 ALA A CB    1 
ATOM   851  N N     . ILE A 1 115 ? 13.576  -49.735 -8.329  1.00 31.48  ? 113 ILE A N     1 
ATOM   852  C CA    . ILE A 1 115 ? 13.683  -48.329 -7.843  1.00 35.21  ? 113 ILE A CA    1 
ATOM   853  C C     . ILE A 1 115 ? 12.661  -48.110 -6.707  1.00 36.90  ? 113 ILE A C     1 
ATOM   854  O O     . ILE A 1 115 ? 13.048  -47.589 -5.649  1.00 32.84  ? 113 ILE A O     1 
ATOM   855  C CB    . ILE A 1 115 ? 13.533  -47.320 -8.999  1.00 33.74  ? 113 ILE A CB    1 
ATOM   856  C CG1   . ILE A 1 115 ? 14.571  -47.556 -10.110 1.00 34.40  ? 113 ILE A CG1   1 
ATOM   857  C CG2   . ILE A 1 115 ? 13.556  -45.899 -8.459  1.00 32.12  ? 113 ILE A CG2   1 
ATOM   858  C CD1   . ILE A 1 115 ? 15.995  -47.775 -9.618  1.00 37.34  ? 113 ILE A CD1   1 
ATOM   859  N N     . SER A 1 116 ? 11.401  -48.479 -6.915  1.00 34.63  ? 114 SER A N     1 
ATOM   860  C CA    . SER A 1 116 ? 10.328  -48.356 -5.899  1.00 36.11  ? 114 SER A CA    1 
ATOM   861  C C     . SER A 1 116 ? 10.723  -49.086 -4.607  1.00 33.60  ? 114 SER A C     1 
ATOM   862  O O     . SER A 1 116 ? 10.465  -48.564 -3.540  1.00 36.48  ? 114 SER A O     1 
ATOM   863  C CB    . SER A 1 116 ? 9.024   -48.867 -6.454  1.00 36.22  ? 114 SER A CB    1 
ATOM   864  O OG    . SER A 1 116 ? 8.608   -48.053 -7.525  1.00 38.34  ? 114 SER A OG    1 
ATOM   865  N N     . GLU A 1 117 ? 11.343  -50.261 -4.695  1.00 33.97  ? 115 GLU A N     1 
ATOM   866  C CA    . GLU A 1 117 ? 11.784  -50.993 -3.490  1.00 30.46  ? 115 GLU A CA    1 
ATOM   867  C C     . GLU A 1 117 ? 12.668  -50.028 -2.690  1.00 31.07  ? 115 GLU A C     1 
ATOM   868  O O     . GLU A 1 117 ? 12.450  -49.899 -1.479  1.00 33.48  ? 115 GLU A O     1 
ATOM   869  C CB    . GLU A 1 117 ? 12.471  -52.327 -3.813  1.00 27.32  ? 115 GLU A CB    1 
ATOM   870  C CG    . GLU A 1 117 ? 13.365  -52.761 -2.681  1.00 31.48  ? 115 GLU A CG    1 
ATOM   871  C CD    . GLU A 1 117 ? 13.919  -54.164 -2.664  1.00 32.75  ? 115 GLU A CD    1 
ATOM   872  O OE1   . GLU A 1 117 ? 14.302  -54.615 -1.549  1.00 26.00  ? 115 GLU A OE1   1 
ATOM   873  O OE2   . GLU A 1 117 ? 13.959  -54.805 -3.752  1.00 32.15  ? 115 GLU A OE2   1 
ATOM   874  N N     . MET A 1 118 ? 13.643  -49.380 -3.335  1.00 33.53  ? 116 MET A N     1 
ATOM   875  C CA    . MET A 1 118 ? 14.666  -48.540 -2.649  1.00 35.26  ? 116 MET A CA    1 
ATOM   876  C C     . MET A 1 118 ? 14.027  -47.207 -2.194  1.00 35.30  ? 116 MET A C     1 
ATOM   877  O O     . MET A 1 118 ? 14.330  -46.747 -1.078  1.00 39.63  ? 116 MET A O     1 
ATOM   878  C CB    . MET A 1 118 ? 15.865  -48.314 -3.578  1.00 36.52  ? 116 MET A CB    1 
ATOM   879  C CG    . MET A 1 118 ? 16.669  -49.590 -3.802  1.00 35.43  ? 116 MET A CG    1 
ATOM   880  S SD    . MET A 1 118 ? 18.149  -49.302 -4.768  1.00 38.34  ? 116 MET A SD    1 
ATOM   881  C CE    . MET A 1 118 ? 17.455  -48.993 -6.387  1.00 37.91  ? 116 MET A CE    1 
ATOM   882  N N     . VAL A 1 119 ? 13.065  -46.672 -2.935  1.00 29.07  ? 117 VAL A N     1 
ATOM   883  C CA    . VAL A 1 119 ? 12.383  -45.409 -2.528  1.00 29.85  ? 117 VAL A CA    1 
ATOM   884  C C     . VAL A 1 119 ? 11.585  -45.627 -1.233  1.00 32.57  ? 117 VAL A C     1 
ATOM   885  O O     . VAL A 1 119 ? 11.767  -44.832 -0.312  1.00 29.68  ? 117 VAL A O     1 
ATOM   886  C CB    . VAL A 1 119 ? 11.507  -44.836 -3.662  1.00 29.23  ? 117 VAL A CB    1 
ATOM   887  C CG1   . VAL A 1 119 ? 10.619  -43.705 -3.179  1.00 30.43  ? 117 VAL A CG1   1 
ATOM   888  C CG2   . VAL A 1 119 ? 12.340  -44.390 -4.851  1.00 31.14  ? 117 VAL A CG2   1 
ATOM   889  N N     . GLY A 1 120 ? 10.740  -46.658 -1.177  1.00 28.23  ? 118 GLY A N     1 
ATOM   890  C CA    . GLY A 1 120 ? 9.877   -46.907 -0.007  1.00 28.09  ? 118 GLY A CA    1 
ATOM   891  C C     . GLY A 1 120 ? 10.665  -47.202 1.247   1.00 27.01  ? 118 GLY A C     1 
ATOM   892  O O     . GLY A 1 120 ? 10.210  -46.833 2.317   1.00 27.50  ? 118 GLY A O     1 
ATOM   893  N N     . GLN A 1 121 ? 11.810  -47.848 1.097   1.00 29.31  ? 119 GLN A N     1 
ATOM   894  C CA    . GLN A 1 121 ? 12.705  -48.111 2.245   1.00 32.06  ? 119 GLN A CA    1 
ATOM   895  C C     . GLN A 1 121 ? 13.314  -46.781 2.719   1.00 32.11  ? 119 GLN A C     1 
ATOM   896  O O     . GLN A 1 121 ? 13.415  -46.596 3.930   1.00 30.19  ? 119 GLN A O     1 
ATOM   897  C CB    . GLN A 1 121 ? 13.744  -49.150 1.818   1.00 29.35  ? 119 GLN A CB    1 
ATOM   898  C CG    . GLN A 1 121 ? 13.170  -50.544 1.633   1.00 28.26  ? 119 GLN A CG    1 
ATOM   899  C CD    . GLN A 1 121 ? 14.061  -51.474 0.847   1.00 30.73  ? 119 GLN A CD    1 
ATOM   900  O OE1   . GLN A 1 121 ? 15.197  -51.155 0.515   1.00 30.31  ? 119 GLN A OE1   1 
ATOM   901  N NE2   . GLN A 1 121 ? 13.545  -52.652 0.549   1.00 33.11  ? 119 GLN A NE2   1 
ATOM   902  N N     . ALA A 1 122 ? 13.676  -45.890 1.796   1.00 32.39  ? 120 ALA A N     1 
ATOM   903  C CA    . ALA A 1 122 ? 14.322  -44.595 2.128   1.00 28.66  ? 120 ALA A CA    1 
ATOM   904  C C     . ALA A 1 122 ? 13.346  -43.610 2.772   1.00 26.74  ? 120 ALA A C     1 
ATOM   905  O O     . ALA A 1 122 ? 13.743  -42.948 3.726   1.00 27.79  ? 120 ALA A O     1 
ATOM   906  C CB    . ALA A 1 122 ? 14.913  -44.007 0.873   1.00 30.18  ? 120 ALA A CB    1 
ATOM   907  N N     . ASN A 1 123 ? 12.127  -43.517 2.248   1.00 28.23  ? 121 ASN A N     1 
ATOM   908  C CA    . ASN A 1 123 ? 11.117  -42.555 2.752   1.00 27.63  ? 121 ASN A CA    1 
ATOM   909  C C     . ASN A 1 123 ? 9.786   -42.912 2.085   1.00 29.72  ? 121 ASN A C     1 
ATOM   910  O O     . ASN A 1 123 ? 9.520   -42.407 0.992   1.00 32.08  ? 121 ASN A O     1 
ATOM   911  C CB    . ASN A 1 123 ? 11.567  -41.106 2.539   1.00 29.21  ? 121 ASN A CB    1 
ATOM   912  C CG    . ASN A 1 123 ? 10.639  -40.052 3.101   1.00 31.40  ? 121 ASN A CG    1 
ATOM   913  O OD1   . ASN A 1 123 ? 9.465   -40.303 3.350   1.00 30.54  ? 121 ASN A OD1   1 
ATOM   914  N ND2   . ASN A 1 123 ? 11.162  -38.853 3.285   1.00 34.17  ? 121 ASN A ND2   1 
ATOM   915  N N     . TRP A 1 124 ? 8.993   -43.766 2.730   1.00 30.11  ? 122 TRP A N     1 
ATOM   916  C CA    . TRP A 1 124 ? 7.709   -44.219 2.136   1.00 28.98  ? 122 TRP A CA    1 
ATOM   917  C C     . TRP A 1 124 ? 6.777   -43.035 1.868   1.00 30.38  ? 122 TRP A C     1 
ATOM   918  O O     . TRP A 1 124 ? 6.210   -42.994 0.787   1.00 31.86  ? 122 TRP A O     1 
ATOM   919  C CB    . TRP A 1 124 ? 7.026   -45.263 3.020   1.00 28.56  ? 122 TRP A CB    1 
ATOM   920  C CG    . TRP A 1 124 ? 5.760   -45.746 2.389   1.00 27.26  ? 122 TRP A CG    1 
ATOM   921  C CD1   . TRP A 1 124 ? 4.492   -45.327 2.658   1.00 29.09  ? 122 TRP A CD1   1 
ATOM   922  C CD2   . TRP A 1 124 ? 5.652   -46.694 1.316   1.00 27.46  ? 122 TRP A CD2   1 
ATOM   923  N NE1   . TRP A 1 124 ? 3.601   -45.968 1.844   1.00 33.09  ? 122 TRP A NE1   1 
ATOM   924  C CE2   . TRP A 1 124 ? 4.282   -46.810 1.008   1.00 30.18  ? 122 TRP A CE2   1 
ATOM   925  C CE3   . TRP A 1 124 ? 6.572   -47.462 0.598   1.00 27.61  ? 122 TRP A CE3   1 
ATOM   926  C CZ2   . TRP A 1 124 ? 3.815   -47.665 0.014   1.00 27.59  ? 122 TRP A CZ2   1 
ATOM   927  C CZ3   . TRP A 1 124 ? 6.111   -48.307 -0.384  1.00 26.49  ? 122 TRP A CZ3   1 
ATOM   928  C CH2   . TRP A 1 124 ? 4.751   -48.403 -0.671  1.00 29.14  ? 122 TRP A CH2   1 
ATOM   929  N N     . SER A 1 125 ? 6.635   -42.122 2.825   1.00 30.32  ? 123 SER A N     1 
ATOM   930  C CA    . SER A 1 125 ? 5.702   -40.974 2.700   1.00 31.75  ? 123 SER A CA    1 
ATOM   931  C C     . SER A 1 125 ? 5.994   -40.161 1.433   1.00 30.11  ? 123 SER A C     1 
ATOM   932  O O     . SER A 1 125 ? 5.042   -39.821 0.740   1.00 30.08  ? 123 SER A O     1 
ATOM   933  C CB    . SER A 1 125 ? 5.755   -40.130 3.946   1.00 32.50  ? 123 SER A CB    1 
ATOM   934  O OG    . SER A 1 125 ? 5.517   -40.912 5.099   1.00 40.11  ? 123 SER A OG    1 
ATOM   935  N N     . TRP A 1 126 ? 7.265   -39.891 1.154   1.00 31.95  ? 124 TRP A N     1 
ATOM   936  C CA    . TRP A 1 126 ? 7.680   -39.144 -0.056  1.00 31.13  ? 124 TRP A CA    1 
ATOM   937  C C     . TRP A 1 126 ? 7.387   -39.982 -1.298  1.00 31.98  ? 124 TRP A C     1 
ATOM   938  O O     . TRP A 1 126 ? 6.860   -39.428 -2.250  1.00 29.12  ? 124 TRP A O     1 
ATOM   939  C CB    . TRP A 1 126 ? 9.171   -38.813 0.050   1.00 32.97  ? 124 TRP A CB    1 
ATOM   940  C CG    . TRP A 1 126 ? 9.694   -37.976 -1.077  1.00 36.09  ? 124 TRP A CG    1 
ATOM   941  C CD1   . TRP A 1 126 ? 9.806   -36.617 -1.109  1.00 33.71  ? 124 TRP A CD1   1 
ATOM   942  C CD2   . TRP A 1 126 ? 10.180  -38.445 -2.347  1.00 35.40  ? 124 TRP A CD2   1 
ATOM   943  N NE1   . TRP A 1 126 ? 10.326  -36.209 -2.306  1.00 32.56  ? 124 TRP A NE1   1 
ATOM   944  C CE2   . TRP A 1 126 ? 10.566  -37.307 -3.086  1.00 35.80  ? 124 TRP A CE2   1 
ATOM   945  C CE3   . TRP A 1 126 ? 10.329  -39.707 -2.931  1.00 36.47  ? 124 TRP A CE3   1 
ATOM   946  C CZ2   . TRP A 1 126 ? 11.089  -37.399 -4.373  1.00 33.29  ? 124 TRP A CZ2   1 
ATOM   947  C CZ3   . TRP A 1 126 ? 10.845  -39.796 -4.203  1.00 31.90  ? 124 TRP A CZ3   1 
ATOM   948  C CH2   . TRP A 1 126 ? 11.220  -38.657 -4.912  1.00 33.55  ? 124 TRP A CH2   1 
ATOM   949  N N     . GLY A 1 127 ? 7.703   -41.274 -1.247  1.00 32.43  ? 125 GLY A N     1 
ATOM   950  C CA    . GLY A 1 127 ? 7.502   -42.178 -2.388  1.00 30.53  ? 125 GLY A CA    1 
ATOM   951  C C     . GLY A 1 127 ? 6.050   -42.377 -2.776  1.00 28.86  ? 125 GLY A C     1 
ATOM   952  O O     . GLY A 1 127 ? 5.802   -42.735 -3.920  1.00 27.64  ? 125 GLY A O     1 
ATOM   953  N N     . MET A 1 128 ? 5.129   -42.117 -1.856  1.00 29.20  ? 126 MET A N     1 
ATOM   954  C CA    . MET A 1 128 ? 3.696   -42.242 -2.214  1.00 32.53  ? 126 MET A CA    1 
ATOM   955  C C     . MET A 1 128 ? 3.323   -41.207 -3.282  1.00 35.27  ? 126 MET A C     1 
ATOM   956  O O     . MET A 1 128 ? 2.352   -41.468 -4.043  1.00 32.67  ? 126 MET A O     1 
ATOM   957  C CB    . MET A 1 128 ? 2.796   -42.046 -1.000  1.00 29.37  ? 126 MET A CB    1 
ATOM   958  C CG    . MET A 1 128 ? 2.872   -43.226 -0.043  1.00 32.25  ? 126 MET A CG    1 
ATOM   959  S SD    . MET A 1 128 ? 2.104   -42.879 1.568   1.00 30.73  ? 126 MET A SD    1 
ATOM   960  C CE    . MET A 1 128 ? 0.364   -42.830 1.141   1.00 32.79  ? 126 MET A CE    1 
ATOM   961  N N     . TYR A 1 129 ? 4.036   -40.072 -3.317  1.00 36.05  ? 127 TYR A N     1 
ATOM   962  C CA    . TYR A 1 129 ? 3.712   -38.950 -4.227  1.00 33.46  ? 127 TYR A CA    1 
ATOM   963  C C     . TYR A 1 129 ? 3.898   -39.459 -5.650  1.00 34.43  ? 127 TYR A C     1 
ATOM   964  O O     . TYR A 1 129 ? 2.915   -39.499 -6.388  1.00 36.60  ? 127 TYR A O     1 
ATOM   965  C CB    . TYR A 1 129 ? 4.489   -37.686 -3.859  1.00 33.12  ? 127 TYR A CB    1 
ATOM   966  C CG    . TYR A 1 129 ? 3.973   -36.957 -2.636  1.00 30.18  ? 127 TYR A CG    1 
ATOM   967  C CD1   . TYR A 1 129 ? 2.885   -36.086 -2.686  1.00 30.56  ? 127 TYR A CD1   1 
ATOM   968  C CD2   . TYR A 1 129 ? 4.597   -37.125 -1.416  1.00 28.73  ? 127 TYR A CD2   1 
ATOM   969  C CE1   . TYR A 1 129 ? 2.439   -35.418 -1.547  1.00 31.05  ? 127 TYR A CE1   1 
ATOM   970  C CE2   . TYR A 1 129 ? 4.160   -36.476 -0.269  1.00 29.59  ? 127 TYR A CE2   1 
ATOM   971  C CZ    . TYR A 1 129 ? 3.083   -35.609 -0.327  1.00 30.32  ? 127 TYR A CZ    1 
ATOM   972  O OH    . TYR A 1 129 ? 2.701   -35.002 0.843   1.00 30.10  ? 127 TYR A OH    1 
ATOM   973  N N     . PRO A 1 130 ? 5.116   -39.898 -6.051  1.00 31.78  ? 128 PRO A N     1 
ATOM   974  C CA    . PRO A 1 130 ? 5.336   -40.455 -7.384  1.00 31.92  ? 128 PRO A CA    1 
ATOM   975  C C     . PRO A 1 130 ? 4.648   -41.818 -7.515  1.00 38.62  ? 128 PRO A C     1 
ATOM   976  O O     . PRO A 1 130 ? 4.098   -42.083 -8.556  1.00 42.71  ? 128 PRO A O     1 
ATOM   977  C CB    . PRO A 1 130 ? 6.866   -40.604 -7.523  1.00 30.00  ? 128 PRO A CB    1 
ATOM   978  C CG    . PRO A 1 130 ? 7.377   -40.625 -6.077  1.00 30.52  ? 128 PRO A CG    1 
ATOM   979  C CD    . PRO A 1 130 ? 6.369   -39.816 -5.283  1.00 31.01  ? 128 PRO A CD    1 
ATOM   980  N N     . GLY A 1 131 ? 4.679   -42.643 -6.463  1.00 39.88  ? 129 GLY A N     1 
ATOM   981  C CA    . GLY A 1 131 ? 4.114   -44.010 -6.499  1.00 38.73  ? 129 GLY A CA    1 
ATOM   982  C C     . GLY A 1 131 ? 2.627   -44.013 -6.856  1.00 39.28  ? 129 GLY A C     1 
ATOM   983  O O     . GLY A 1 131 ? 2.220   -44.883 -7.628  1.00 42.09  ? 129 GLY A O     1 
ATOM   984  N N     . LEU A 1 132 ? 1.838   -43.073 -6.342  1.00 36.97  ? 130 LEU A N     1 
ATOM   985  C CA    . LEU A 1 132 ? 0.412   -42.918 -6.739  1.00 46.23  ? 130 LEU A CA    1 
ATOM   986  C C     . LEU A 1 132 ? 0.286   -42.435 -8.194  1.00 45.49  ? 130 LEU A C     1 
ATOM   987  O O     . LEU A 1 132 ? -0.587  -42.953 -8.920  1.00 43.95  ? 130 LEU A O     1 
ATOM   988  C CB    . LEU A 1 132 ? -0.259  -41.954 -5.769  1.00 46.98  ? 130 LEU A CB    1 
ATOM   989  C CG    . LEU A 1 132 ? -0.538  -42.542 -4.394  1.00 45.87  ? 130 LEU A CG    1 
ATOM   990  C CD1   . LEU A 1 132 ? -0.922  -41.451 -3.422  1.00 51.05  ? 130 LEU A CD1   1 
ATOM   991  C CD2   . LEU A 1 132 ? -1.625  -43.586 -4.482  1.00 48.26  ? 130 LEU A CD2   1 
ATOM   992  N N     . SER A 1 133 ? 1.142   -41.508 -8.631  1.00 53.53  ? 131 SER A N     1 
ATOM   993  C CA    . SER A 1 133 ? 1.242   -41.072 -10.059 1.00 54.91  ? 131 SER A CA    1 
ATOM   994  C C     . SER A 1 133 ? 1.388   -42.330 -10.940 1.00 61.38  ? 131 SER A C     1 
ATOM   995  O O     . SER A 1 133 ? 0.548   -42.508 -11.855 1.00 60.92  ? 131 SER A O     1 
ATOM   996  C CB    . SER A 1 133 ? 2.373   -40.068 -10.299 1.00 44.73  ? 131 SER A CB    1 
ATOM   997  O OG    . SER A 1 133 ? 2.264   -38.920 -9.452  1.00 44.99  ? 131 SER A OG    1 
ATOM   998  N N     . HIS A 1 134 ? 2.370   -43.196 -10.615 1.00 63.94  ? 132 HIS A N     1 
ATOM   999  C CA    . HIS A 1 134 ? 2.715   -44.462 -11.324 1.00 61.68  ? 132 HIS A CA    1 
ATOM   1000 C C     . HIS A 1 134 ? 1.436   -45.270 -11.612 1.00 62.31  ? 132 HIS A C     1 
ATOM   1001 O O     . HIS A 1 134 ? 1.310   -45.812 -12.748 1.00 71.32  ? 132 HIS A O     1 
ATOM   1002 C CB    . HIS A 1 134 ? 3.780   -45.285 -10.569 1.00 55.52  ? 132 HIS A CB    1 
ATOM   1003 C CG    . HIS A 1 134 ? 4.159   -46.510 -11.325 1.00 59.82  ? 132 HIS A CG    1 
ATOM   1004 N ND1   . HIS A 1 134 ? 5.046   -46.476 -12.390 1.00 67.72  ? 132 HIS A ND1   1 
ATOM   1005 C CD2   . HIS A 1 134 ? 3.680   -47.774 -11.275 1.00 62.03  ? 132 HIS A CD2   1 
ATOM   1006 C CE1   . HIS A 1 134 ? 5.142   -47.681 -12.926 1.00 63.86  ? 132 HIS A CE1   1 
ATOM   1007 N NE2   . HIS A 1 134 ? 4.300   -48.494 -12.266 1.00 60.04  ? 132 HIS A NE2   1 
ATOM   1008 N N     . GLY A 1 135 ? 0.514   -45.317 -10.650 1.00 49.99  ? 133 GLY A N     1 
ATOM   1009 C CA    . GLY A 1 135 ? -0.811  -45.946 -10.795 1.00 49.38  ? 133 GLY A CA    1 
ATOM   1010 C C     . GLY A 1 135 ? -1.678  -45.323 -11.881 1.00 47.76  ? 133 GLY A C     1 
ATOM   1011 O O     . GLY A 1 135 ? -2.088  -46.081 -12.767 1.00 53.58  ? 133 GLY A O     1 
ATOM   1012 N N     . ALA A 1 136 ? -1.992  -44.017 -11.789 1.00 50.99  ? 134 ALA A N     1 
ATOM   1013 C CA    . ALA A 1 136 ? -2.944  -43.266 -12.657 1.00 47.47  ? 134 ALA A CA    1 
ATOM   1014 C C     . ALA A 1 136 ? -2.452  -43.243 -14.120 1.00 48.94  ? 134 ALA A C     1 
ATOM   1015 O O     . ALA A 1 136 ? -3.320  -43.097 -15.046 1.00 37.88  ? 134 ALA A O     1 
ATOM   1016 C CB    . ALA A 1 136 ? -3.119  -41.850 -12.150 1.00 49.14  ? 134 ALA A CB    1 
ATOM   1017 N N     . MET A 1 137 ? -1.122  -43.282 -14.307 1.00 41.13  ? 135 MET A N     1 
ATOM   1018 C CA    . MET A 1 137 ? -0.440  -43.428 -15.623 1.00 44.32  ? 135 MET A CA    1 
ATOM   1019 C C     . MET A 1 137 ? -0.882  -44.767 -16.251 1.00 49.97  ? 135 MET A C     1 
ATOM   1020 O O     . MET A 1 137 ? -1.405  -44.743 -17.415 1.00 42.53  ? 135 MET A O     1 
ATOM   1021 C CB    . MET A 1 137 ? 1.090   -43.398 -15.476 1.00 42.11  ? 135 MET A CB    1 
ATOM   1022 C CG    . MET A 1 137 ? 1.676   -42.057 -15.041 1.00 40.95  ? 135 MET A CG    1 
ATOM   1023 S SD    . MET A 1 137 ? 3.469   -41.960 -15.396 1.00 50.76  ? 135 MET A SD    1 
ATOM   1024 C CE    . MET A 1 137 ? 4.204   -42.200 -13.782 1.00 57.91  ? 135 MET A CE    1 
ATOM   1025 N N     . ASN A 1 138 ? -0.698  -45.882 -15.515 1.00 47.31  ? 136 ASN A N     1 
ATOM   1026 C CA    . ASN A 1 138 ? -1.088  -47.263 -15.926 1.00 52.03  ? 136 ASN A CA    1 
ATOM   1027 C C     . ASN A 1 138 ? -2.568  -47.289 -16.369 1.00 57.23  ? 136 ASN A C     1 
ATOM   1028 O O     . ASN A 1 138 ? -2.862  -47.974 -17.391 1.00 56.47  ? 136 ASN A O     1 
ATOM   1029 C CB    . ASN A 1 138 ? -0.767  -48.294 -14.837 1.00 49.85  ? 136 ASN A CB    1 
ATOM   1030 C CG    . ASN A 1 138 ? 0.715   -48.615 -14.714 1.00 56.26  ? 136 ASN A CG    1 
ATOM   1031 O OD1   . ASN A 1 138 ? 1.529   -48.225 -15.547 1.00 64.57  ? 136 ASN A OD1   1 
ATOM   1032 N ND2   . ASN A 1 138 ? 1.106   -49.306 -13.654 1.00 58.97  ? 136 ASN A ND2   1 
ATOM   1033 N N     . THR A 1 139 ? -3.451  -46.538 -15.691 1.00 49.22  ? 137 THR A N     1 
ATOM   1034 C CA    . THR A 1 139 ? -4.912  -46.447 -15.990 1.00 47.54  ? 137 THR A CA    1 
ATOM   1035 C C     . THR A 1 139 ? -5.176  -45.648 -17.279 1.00 50.10  ? 137 THR A C     1 
ATOM   1036 O O     . THR A 1 139 ? -6.075  -46.026 -18.063 1.00 48.19  ? 137 THR A O     1 
ATOM   1037 C CB    . THR A 1 139 ? -5.646  -45.789 -14.817 1.00 51.20  ? 137 THR A CB    1 
ATOM   1038 O OG1   . THR A 1 139 ? -4.999  -46.258 -13.630 1.00 52.96  ? 137 THR A OG1   1 
ATOM   1039 C CG2   . THR A 1 139 ? -7.136  -46.064 -14.808 1.00 53.90  ? 137 THR A CG2   1 
ATOM   1040 N N     . LEU A 1 140 ? -4.461  -44.540 -17.484 1.00 49.29  ? 138 LEU A N     1 
ATOM   1041 C CA    . LEU A 1 140 ? -4.546  -43.738 -18.731 1.00 45.31  ? 138 LEU A CA    1 
ATOM   1042 C C     . LEU A 1 140 ? -4.003  -44.581 -19.882 1.00 39.47  ? 138 LEU A C     1 
ATOM   1043 O O     . LEU A 1 140 ? -4.596  -44.575 -20.947 1.00 40.88  ? 138 LEU A O     1 
ATOM   1044 C CB    . LEU A 1 140 ? -3.760  -42.435 -18.565 1.00 49.20  ? 138 LEU A CB    1 
ATOM   1045 C CG    . LEU A 1 140 ? -4.530  -41.329 -17.852 1.00 51.88  ? 138 LEU A CG    1 
ATOM   1046 C CD1   . LEU A 1 140 ? -3.587  -40.410 -17.104 1.00 55.58  ? 138 LEU A CD1   1 
ATOM   1047 C CD2   . LEU A 1 140 ? -5.381  -40.547 -18.835 1.00 51.83  ? 138 LEU A CD2   1 
ATOM   1048 N N     . HIS A 1 141 ? -2.938  -45.328 -19.651 1.00 39.14  ? 139 HIS A N     1 
ATOM   1049 C CA    . HIS A 1 141 ? -2.344  -46.169 -20.708 1.00 41.20  ? 139 HIS A CA    1 
ATOM   1050 C C     . HIS A 1 141 ? -3.401  -47.176 -21.156 1.00 46.82  ? 139 HIS A C     1 
ATOM   1051 O O     . HIS A 1 141 ? -3.580  -47.305 -22.372 1.00 43.69  ? 139 HIS A O     1 
ATOM   1052 C CB    . HIS A 1 141 ? -1.055  -46.842 -20.254 1.00 40.42  ? 139 HIS A CB    1 
ATOM   1053 C CG    . HIS A 1 141 ? -0.347  -47.545 -21.363 1.00 44.91  ? 139 HIS A CG    1 
ATOM   1054 N ND1   . HIS A 1 141 ? -0.146  -48.927 -21.366 1.00 46.81  ? 139 HIS A ND1   1 
ATOM   1055 C CD2   . HIS A 1 141 ? 0.184   -47.063 -22.517 1.00 47.23  ? 139 HIS A CD2   1 
ATOM   1056 C CE1   . HIS A 1 141 ? 0.537   -49.256 -22.450 1.00 52.44  ? 139 HIS A CE1   1 
ATOM   1057 N NE2   . HIS A 1 141 ? 0.743   -48.113 -23.186 1.00 48.42  ? 139 HIS A NE2   1 
ATOM   1058 N N     . ALA A 1 142 ? -4.089  -47.826 -20.206 1.00 44.35  ? 140 ALA A N     1 
ATOM   1059 C CA    . ALA A 1 142 ? -4.916  -49.031 -20.457 1.00 41.33  ? 140 ALA A CA    1 
ATOM   1060 C C     . ALA A 1 142 ? -6.275  -48.675 -21.062 1.00 42.28  ? 140 ALA A C     1 
ATOM   1061 O O     . ALA A 1 142 ? -6.814  -49.544 -21.771 1.00 45.00  ? 140 ALA A O     1 
ATOM   1062 C CB    . ALA A 1 142 ? -5.111  -49.813 -19.178 1.00 42.46  ? 140 ALA A CB    1 
ATOM   1063 N N     . HIS A 1 143 ? -6.830  -47.497 -20.744 1.00 42.22  ? 141 HIS A N     1 
ATOM   1064 C CA    . HIS A 1 143 ? -8.281  -47.189 -20.897 1.00 39.33  ? 141 HIS A CA    1 
ATOM   1065 C C     . HIS A 1 143 ? -8.507  -45.771 -21.412 1.00 37.69  ? 141 HIS A C     1 
ATOM   1066 O O     . HIS A 1 143 ? -9.677  -45.438 -21.672 1.00 39.27  ? 141 HIS A O     1 
ATOM   1067 C CB    . HIS A 1 143 ? -9.022  -47.330 -19.554 1.00 41.19  ? 141 HIS A CB    1 
ATOM   1068 C CG    . HIS A 1 143 ? -8.795  -48.637 -18.868 1.00 45.26  ? 141 HIS A CG    1 
ATOM   1069 N ND1   . HIS A 1 143 ? -9.351  -49.818 -19.334 1.00 47.16  ? 141 HIS A ND1   1 
ATOM   1070 C CD2   . HIS A 1 143 ? -8.074  -48.958 -17.770 1.00 45.33  ? 141 HIS A CD2   1 
ATOM   1071 C CE1   . HIS A 1 143 ? -8.955  -50.811 -18.566 1.00 50.51  ? 141 HIS A CE1   1 
ATOM   1072 N NE2   . HIS A 1 143 ? -8.179  -50.307 -17.586 1.00 51.82  ? 141 HIS A NE2   1 
ATOM   1073 N N     . GLY A 1 144 ? -7.466  -44.937 -21.470 1.00 36.37  ? 142 GLY A N     1 
ATOM   1074 C CA    . GLY A 1 144 ? -7.601  -43.539 -21.930 1.00 43.31  ? 142 GLY A CA    1 
ATOM   1075 C C     . GLY A 1 144 ? -7.678  -43.464 -23.460 1.00 45.00  ? 142 GLY A C     1 
ATOM   1076 O O     . GLY A 1 144 ? -7.044  -44.303 -24.114 1.00 42.51  ? 142 GLY A O     1 
ATOM   1077 N N     . THR A 1 145 ? -8.428  -42.507 -24.014 1.00 42.39  ? 143 THR A N     1 
ATOM   1078 C CA    . THR A 1 145 ? -8.432  -42.190 -25.468 1.00 45.48  ? 143 THR A CA    1 
ATOM   1079 C C     . THR A 1 145 ? -7.064  -41.592 -25.813 1.00 50.27  ? 143 THR A C     1 
ATOM   1080 O O     . THR A 1 145 ? -6.467  -40.961 -24.916 1.00 48.14  ? 143 THR A O     1 
ATOM   1081 C CB    . THR A 1 145 ? -9.540  -41.193 -25.825 1.00 44.07  ? 143 THR A CB    1 
ATOM   1082 O OG1   . THR A 1 145 ? -9.240  -39.980 -25.136 1.00 46.41  ? 143 THR A OG1   1 
ATOM   1083 C CG2   . THR A 1 145 ? -10.935 -41.660 -25.474 1.00 39.91  ? 143 THR A CG2   1 
ATOM   1084 N N     . ALA A 1 146 ? -6.586  -41.748 -27.050 1.00 47.67  ? 144 ALA A N     1 
ATOM   1085 C CA    . ALA A 1 146 ? -5.279  -41.211 -27.509 1.00 46.09  ? 144 ALA A CA    1 
ATOM   1086 C C     . ALA A 1 146 ? -5.158  -39.708 -27.177 1.00 46.08  ? 144 ALA A C     1 
ATOM   1087 O O     . ALA A 1 146 ? -4.022  -39.239 -26.858 1.00 48.22  ? 144 ALA A O     1 
ATOM   1088 C CB    . ALA A 1 146 ? -5.099  -41.484 -28.983 1.00 48.35  ? 144 ALA A CB    1 
ATOM   1089 N N     . GLU A 1 147 ? -6.267  -38.970 -27.179 1.00 43.42  ? 145 GLU A N     1 
ATOM   1090 C CA    . GLU A 1 147 ? -6.275  -37.525 -26.840 1.00 48.58  ? 145 GLU A CA    1 
ATOM   1091 C C     . GLU A 1 147 ? -5.955  -37.358 -25.352 1.00 53.02  ? 145 GLU A C     1 
ATOM   1092 O O     . GLU A 1 147 ? -5.149  -36.477 -24.994 1.00 52.40  ? 145 GLU A O     1 
ATOM   1093 C CB    . GLU A 1 147 ? -7.656  -36.930 -27.132 1.00 60.03  ? 145 GLU A CB    1 
ATOM   1094 C CG    . GLU A 1 147 ? -7.762  -35.438 -26.826 1.00 68.34  ? 145 GLU A CG    1 
ATOM   1095 C CD    . GLU A 1 147 ? -9.188  -34.947 -26.601 1.00 82.85  ? 145 GLU A CD    1 
ATOM   1096 O OE1   . GLU A 1 147 ? -9.927  -35.595 -25.799 1.00 85.96  ? 145 GLU A OE1   1 
ATOM   1097 O OE2   . GLU A 1 147 ? -9.561  -33.911 -27.216 1.00 86.34  ? 145 GLU A OE2   1 
ATOM   1098 N N     . GLN A 1 148 ? -6.679  -38.114 -24.524 1.00 48.62  ? 146 GLN A N     1 
ATOM   1099 C CA    . GLN A 1 148 ? -6.555  -38.128 -23.048 1.00 47.83  ? 146 GLN A CA    1 
ATOM   1100 C C     . GLN A 1 148 ? -5.107  -38.462 -22.685 1.00 43.72  ? 146 GLN A C     1 
ATOM   1101 O O     . GLN A 1 148 ? -4.596  -37.798 -21.798 1.00 41.05  ? 146 GLN A O     1 
ATOM   1102 C CB    . GLN A 1 148 ? -7.532  -39.136 -22.427 1.00 44.85  ? 146 GLN A CB    1 
ATOM   1103 C CG    . GLN A 1 148 ? -8.977  -38.658 -22.396 1.00 42.42  ? 146 GLN A CG    1 
ATOM   1104 C CD    . GLN A 1 148 ? -9.901  -39.744 -21.911 1.00 41.18  ? 146 GLN A CD    1 
ATOM   1105 O OE1   . GLN A 1 148 ? -9.591  -40.936 -21.965 1.00 45.15  ? 146 GLN A OE1   1 
ATOM   1106 N NE2   . GLN A 1 148 ? -11.047 -39.324 -21.411 1.00 36.82  ? 146 GLN A NE2   1 
ATOM   1107 N N     . GLN A 1 149 ? -4.476  -39.427 -23.364 1.00 42.85  ? 147 GLN A N     1 
ATOM   1108 C CA    . GLN A 1 149 ? -3.044  -39.763 -23.131 1.00 48.49  ? 147 GLN A CA    1 
ATOM   1109 C C     . GLN A 1 149 ? -2.129  -38.587 -23.537 1.00 53.52  ? 147 GLN A C     1 
ATOM   1110 O O     . GLN A 1 149 ? -1.133  -38.309 -22.805 1.00 52.70  ? 147 GLN A O     1 
ATOM   1111 C CB    . GLN A 1 149 ? -2.642  -41.038 -23.865 1.00 47.84  ? 147 GLN A CB    1 
ATOM   1112 C CG    . GLN A 1 149 ? -3.547  -42.220 -23.576 1.00 53.71  ? 147 GLN A CG    1 
ATOM   1113 C CD    . GLN A 1 149 ? -2.948  -43.528 -24.028 1.00 57.21  ? 147 GLN A CD    1 
ATOM   1114 O OE1   . GLN A 1 149 ? -1.730  -43.724 -24.023 1.00 66.92  ? 147 GLN A OE1   1 
ATOM   1115 N NE2   . GLN A 1 149 ? -3.816  -44.465 -24.363 1.00 60.05  ? 147 GLN A NE2   1 
ATOM   1116 N N     . ALA A 1 150 ? -2.420  -37.915 -24.656 1.00 53.13  ? 148 ALA A N     1 
ATOM   1117 C CA    . ALA A 1 150 ? -1.645  -36.745 -25.124 1.00 49.51  ? 148 ALA A CA    1 
ATOM   1118 C C     . ALA A 1 150 ? -1.631  -35.686 -24.015 1.00 45.29  ? 148 ALA A C     1 
ATOM   1119 O O     . ALA A 1 150 ? -0.549  -35.251 -23.630 1.00 50.81  ? 148 ALA A O     1 
ATOM   1120 C CB    . ALA A 1 150 ? -2.215  -36.201 -26.416 1.00 48.45  ? 148 ALA A CB    1 
ATOM   1121 N N     . THR A 1 151 ? -2.793  -35.284 -23.512 1.00 45.79  ? 149 THR A N     1 
ATOM   1122 C CA    . THR A 1 151 ? -2.923  -34.214 -22.487 1.00 51.65  ? 149 THR A CA    1 
ATOM   1123 C C     . THR A 1 151 ? -2.339  -34.681 -21.132 1.00 49.31  ? 149 THR A C     1 
ATOM   1124 O O     . THR A 1 151 ? -1.360  -34.066 -20.676 1.00 51.83  ? 149 THR A O     1 
ATOM   1125 C CB    . THR A 1 151 ? -4.387  -33.770 -22.398 1.00 57.85  ? 149 THR A CB    1 
ATOM   1126 O OG1   . THR A 1 151 ? -4.840  -33.610 -23.743 1.00 55.66  ? 149 THR A OG1   1 
ATOM   1127 C CG2   . THR A 1 151 ? -4.591  -32.502 -21.592 1.00 58.33  ? 149 THR A CG2   1 
ATOM   1128 N N     . TYR A 1 152 ? -2.879  -35.749 -20.525 1.00 46.37  ? 150 TYR A N     1 
ATOM   1129 C CA    . TYR A 1 152 ? -2.623  -36.151 -19.111 1.00 42.92  ? 150 TYR A CA    1 
ATOM   1130 C C     . TYR A 1 152 ? -1.439  -37.110 -19.004 1.00 40.77  ? 150 TYR A C     1 
ATOM   1131 O O     . TYR A 1 152 ? -0.620  -36.839 -18.159 1.00 40.87  ? 150 TYR A O     1 
ATOM   1132 C CB    . TYR A 1 152 ? -3.894  -36.714 -18.489 1.00 40.55  ? 150 TYR A CB    1 
ATOM   1133 C CG    . TYR A 1 152 ? -4.989  -35.690 -18.497 1.00 38.76  ? 150 TYR A CG    1 
ATOM   1134 C CD1   . TYR A 1 152 ? -4.946  -34.585 -17.669 1.00 40.28  ? 150 TYR A CD1   1 
ATOM   1135 C CD2   . TYR A 1 152 ? -6.043  -35.804 -19.377 1.00 43.42  ? 150 TYR A CD2   1 
ATOM   1136 C CE1   . TYR A 1 152 ? -5.945  -33.627 -17.694 1.00 42.04  ? 150 TYR A CE1   1 
ATOM   1137 C CE2   . TYR A 1 152 ? -7.044  -34.853 -19.432 1.00 42.90  ? 150 TYR A CE2   1 
ATOM   1138 C CZ    . TYR A 1 152 ? -6.995  -33.758 -18.593 1.00 44.82  ? 150 TYR A CZ    1 
ATOM   1139 O OH    . TYR A 1 152 ? -8.000  -32.838 -18.682 1.00 49.12  ? 150 TYR A OH    1 
ATOM   1140 N N     . LEU A 1 153 ? -1.315  -38.137 -19.847 1.00 39.23  ? 151 LEU A N     1 
ATOM   1141 C CA    . LEU A 1 153 ? -0.312  -39.209 -19.621 1.00 41.25  ? 151 LEU A CA    1 
ATOM   1142 C C     . LEU A 1 153 ? 1.100   -38.658 -19.864 1.00 43.14  ? 151 LEU A C     1 
ATOM   1143 O O     . LEU A 1 153 ? 2.058   -39.177 -19.236 1.00 42.58  ? 151 LEU A O     1 
ATOM   1144 C CB    . LEU A 1 153 ? -0.609  -40.447 -20.483 1.00 37.50  ? 151 LEU A CB    1 
ATOM   1145 C CG    . LEU A 1 153 ? 0.386   -41.594 -20.285 1.00 42.63  ? 151 LEU A CG    1 
ATOM   1146 C CD1   . LEU A 1 153 ? 0.393   -42.028 -18.830 1.00 42.24  ? 151 LEU A CD1   1 
ATOM   1147 C CD2   . LEU A 1 153 ? 0.123   -42.788 -21.207 1.00 44.47  ? 151 LEU A CD2   1 
ATOM   1148 N N     . THR A 1 154 ? 1.241   -37.666 -20.746 1.00 44.21  ? 152 THR A N     1 
ATOM   1149 C CA    . THR A 1 154 ? 2.559   -37.119 -21.149 1.00 42.72  ? 152 THR A CA    1 
ATOM   1150 C C     . THR A 1 154 ? 3.101   -36.336 -19.958 1.00 40.96  ? 152 THR A C     1 
ATOM   1151 O O     . THR A 1 154 ? 4.268   -36.541 -19.617 1.00 38.50  ? 152 THR A O     1 
ATOM   1152 C CB    . THR A 1 154 ? 2.481   -36.269 -22.433 1.00 46.12  ? 152 THR A CB    1 
ATOM   1153 O OG1   . THR A 1 154 ? 1.751   -37.012 -23.403 1.00 51.57  ? 152 THR A OG1   1 
ATOM   1154 C CG2   . THR A 1 154 ? 3.838   -35.951 -23.033 1.00 47.42  ? 152 THR A CG2   1 
ATOM   1155 N N     . LYS A 1 155 ? 2.262   -35.485 -19.361 1.00 39.62  ? 153 LYS A N     1 
ATOM   1156 C CA    . LYS A 1 155 ? 2.611   -34.673 -18.173 1.00 41.85  ? 153 LYS A CA    1 
ATOM   1157 C C     . LYS A 1 155 ? 2.934   -35.577 -16.968 1.00 42.46  ? 153 LYS A C     1 
ATOM   1158 O O     . LYS A 1 155 ? 3.840   -35.234 -16.191 1.00 42.97  ? 153 LYS A O     1 
ATOM   1159 C CB    . LYS A 1 155 ? 1.471   -33.708 -17.876 1.00 42.21  ? 153 LYS A CB    1 
ATOM   1160 C CG    . LYS A 1 155 ? 1.336   -32.589 -18.882 1.00 48.54  ? 153 LYS A CG    1 
ATOM   1161 C CD    . LYS A 1 155 ? 2.501   -31.626 -18.887 1.00 52.86  ? 153 LYS A CD    1 
ATOM   1162 C CE    . LYS A 1 155 ? 2.472   -30.709 -20.094 1.00 57.77  ? 153 LYS A CE    1 
ATOM   1163 N NZ    . LYS A 1 155 ? 2.683   -29.308 -19.665 1.00 66.12  ? 153 LYS A NZ    1 
ATOM   1164 N N     . LEU A 1 156 ? 2.247   -36.706 -16.828 1.00 40.56  ? 154 LEU A N     1 
ATOM   1165 C CA    . LEU A 1 156 ? 2.454   -37.638 -15.697 1.00 41.47  ? 154 LEU A CA    1 
ATOM   1166 C C     . LEU A 1 156 ? 3.757   -38.389 -15.946 1.00 43.19  ? 154 LEU A C     1 
ATOM   1167 O O     . LEU A 1 156 ? 4.513   -38.564 -14.987 1.00 46.93  ? 154 LEU A O     1 
ATOM   1168 C CB    . LEU A 1 156 ? 1.257   -38.581 -15.549 1.00 39.12  ? 154 LEU A CB    1 
ATOM   1169 C CG    . LEU A 1 156 ? 0.004   -37.962 -14.933 1.00 39.94  ? 154 LEU A CG    1 
ATOM   1170 C CD1   . LEU A 1 156 ? -1.214  -38.809 -15.230 1.00 45.61  ? 154 LEU A CD1   1 
ATOM   1171 C CD2   . LEU A 1 156 ? 0.135   -37.817 -13.425 1.00 41.39  ? 154 LEU A CD2   1 
ATOM   1172 N N     . VAL A 1 157 ? 4.069   -38.704 -17.199 1.00 42.96  ? 155 VAL A N     1 
ATOM   1173 C CA    . VAL A 1 157 ? 5.271   -39.526 -17.522 1.00 42.60  ? 155 VAL A CA    1 
ATOM   1174 C C     . VAL A 1 157 ? 6.539   -38.692 -17.290 1.00 42.35  ? 155 VAL A C     1 
ATOM   1175 O O     . VAL A 1 157 ? 7.526   -39.274 -16.817 1.00 47.99  ? 155 VAL A O     1 
ATOM   1176 C CB    . VAL A 1 157 ? 5.161   -40.138 -18.937 1.00 44.90  ? 155 VAL A CB    1 
ATOM   1177 C CG1   . VAL A 1 157 ? 6.496   -40.349 -19.621 1.00 39.81  ? 155 VAL A CG1   1 
ATOM   1178 C CG2   . VAL A 1 157 ? 4.393   -41.457 -18.901 1.00 44.16  ? 155 VAL A CG2   1 
ATOM   1179 N N     . SER A 1 158 ? 6.502   -37.391 -17.589 1.00 46.03  ? 156 SER A N     1 
ATOM   1180 C CA    . SER A 1 158 ? 7.574   -36.384 -17.334 1.00 43.04  ? 156 SER A CA    1 
ATOM   1181 C C     . SER A 1 158 ? 7.754   -36.175 -15.827 1.00 47.74  ? 156 SER A C     1 
ATOM   1182 O O     . SER A 1 158 ? 8.895   -35.890 -15.406 1.00 59.06  ? 156 SER A O     1 
ATOM   1183 C CB    . SER A 1 158 ? 7.249   -35.071 -18.000 1.00 45.80  ? 156 SER A CB    1 
ATOM   1184 O OG    . SER A 1 158 ? 6.432   -34.245 -17.180 1.00 47.53  ? 156 SER A OG    1 
ATOM   1185 N N     . GLY A 1 159 ? 6.664   -36.308 -15.059 1.00 43.27  ? 157 GLY A N     1 
ATOM   1186 C CA    . GLY A 1 159 ? 6.619   -36.087 -13.604 1.00 37.77  ? 157 GLY A CA    1 
ATOM   1187 C C     . GLY A 1 159 ? 6.205   -34.675 -13.264 1.00 39.20  ? 157 GLY A C     1 
ATOM   1188 O O     . GLY A 1 159 ? 6.133   -34.367 -12.079 1.00 41.03  ? 157 GLY A O     1 
ATOM   1189 N N     . GLU A 1 160 ? 5.931   -33.829 -14.258 1.00 46.60  ? 158 GLU A N     1 
ATOM   1190 C CA    . GLU A 1 160 ? 5.538   -32.403 -14.039 1.00 46.46  ? 158 GLU A CA    1 
ATOM   1191 C C     . GLU A 1 160 ? 4.195   -32.384 -13.320 1.00 41.08  ? 158 GLU A C     1 
ATOM   1192 O O     . GLU A 1 160 ? 3.988   -31.508 -12.472 1.00 39.56  ? 158 GLU A O     1 
ATOM   1193 C CB    . GLU A 1 160 ? 5.488   -31.604 -15.346 1.00 51.09  ? 158 GLU A CB    1 
ATOM   1194 C CG    . GLU A 1 160 ? 6.816   -30.974 -15.746 1.00 57.38  ? 158 GLU A CG    1 
ATOM   1195 C CD    . GLU A 1 160 ? 7.042   -30.904 -17.249 1.00 69.82  ? 158 GLU A CD    1 
ATOM   1196 O OE1   . GLU A 1 160 ? 6.044   -30.877 -18.020 1.00 68.03  ? 158 GLU A OE1   1 
ATOM   1197 O OE2   . GLU A 1 160 ? 8.222   -30.892 -17.656 1.00 81.76  ? 158 GLU A OE2   1 
ATOM   1198 N N     . TRP A 1 161 ? 3.306   -33.318 -13.666 1.00 46.63  ? 159 TRP A N     1 
ATOM   1199 C CA    . TRP A 1 161 ? 1.994   -33.497 -12.993 1.00 42.74  ? 159 TRP A CA    1 
ATOM   1200 C C     . TRP A 1 161 ? 2.030   -34.801 -12.197 1.00 40.05  ? 159 TRP A C     1 
ATOM   1201 O O     . TRP A 1 161 ? 2.708   -35.758 -12.628 1.00 33.25  ? 159 TRP A O     1 
ATOM   1202 C CB    . TRP A 1 161 ? 0.848   -33.475 -14.007 1.00 44.79  ? 159 TRP A CB    1 
ATOM   1203 C CG    . TRP A 1 161 ? 0.712   -32.173 -14.730 1.00 49.08  ? 159 TRP A CG    1 
ATOM   1204 C CD1   . TRP A 1 161 ? 1.486   -31.062 -14.588 1.00 49.27  ? 159 TRP A CD1   1 
ATOM   1205 C CD2   . TRP A 1 161 ? -0.240  -31.865 -15.755 1.00 46.09  ? 159 TRP A CD2   1 
ATOM   1206 N NE1   . TRP A 1 161 ? 1.046   -30.068 -15.407 1.00 53.34  ? 159 TRP A NE1   1 
ATOM   1207 C CE2   . TRP A 1 161 ? -0.001  -30.534 -16.149 1.00 50.45  ? 159 TRP A CE2   1 
ATOM   1208 C CE3   . TRP A 1 161 ? -1.282  -32.574 -16.354 1.00 47.05  ? 159 TRP A CE3   1 
ATOM   1209 C CZ2   . TRP A 1 161 ? -0.754  -29.902 -17.137 1.00 50.98  ? 159 TRP A CZ2   1 
ATOM   1210 C CZ3   . TRP A 1 161 ? -2.036  -31.949 -17.325 1.00 51.70  ? 159 TRP A CZ3   1 
ATOM   1211 C CH2   . TRP A 1 161 ? -1.769  -30.635 -17.714 1.00 51.72  ? 159 TRP A CH2   1 
ATOM   1212 N N     . THR A 1 162 ? 1.329   -34.819 -11.065 1.00 38.44  ? 160 THR A N     1 
ATOM   1213 C CA    . THR A 1 162 ? 1.181   -36.015 -10.199 1.00 37.84  ? 160 THR A CA    1 
ATOM   1214 C C     . THR A 1 162 ? -0.275  -36.480 -10.319 1.00 37.24  ? 160 THR A C     1 
ATOM   1215 O O     . THR A 1 162 ? -1.111  -35.688 -10.837 1.00 34.50  ? 160 THR A O     1 
ATOM   1216 C CB    . THR A 1 162 ? 1.617   -35.688 -8.766  1.00 35.28  ? 160 THR A CB    1 
ATOM   1217 O OG1   . THR A 1 162 ? 0.758   -34.635 -8.316  1.00 37.36  ? 160 THR A OG1   1 
ATOM   1218 C CG2   . THR A 1 162 ? 3.070   -35.287 -8.661  1.00 34.83  ? 160 THR A CG2   1 
ATOM   1219 N N     . GLY A 1 163 ? -0.555  -37.710 -9.879  1.00 37.93  ? 161 GLY A N     1 
ATOM   1220 C CA    . GLY A 1 163 ? -1.878  -38.353 -10.006 1.00 39.06  ? 161 GLY A CA    1 
ATOM   1221 C C     . GLY A 1 163 ? -2.350  -38.982 -8.702  1.00 37.89  ? 161 GLY A C     1 
ATOM   1222 O O     . GLY A 1 163 ? -1.508  -39.486 -7.937  1.00 38.28  ? 161 GLY A O     1 
ATOM   1223 N N     . THR A 1 164 ? -3.662  -38.936 -8.475  1.00 36.30  ? 162 THR A N     1 
ATOM   1224 C CA    . THR A 1 164 ? -4.376  -39.516 -7.319  1.00 37.18  ? 162 THR A CA    1 
ATOM   1225 C C     . THR A 1 164 ? -5.381  -40.586 -7.770  1.00 40.87  ? 162 THR A C     1 
ATOM   1226 O O     . THR A 1 164 ? -5.765  -40.626 -8.986  1.00 41.33  ? 162 THR A O     1 
ATOM   1227 C CB    . THR A 1 164 ? -5.101  -38.420 -6.529  1.00 37.81  ? 162 THR A CB    1 
ATOM   1228 O OG1   . THR A 1 164 ? -6.224  -38.014 -7.298  1.00 33.24  ? 162 THR A OG1   1 
ATOM   1229 C CG2   . THR A 1 164 ? -4.212  -37.239 -6.191  1.00 38.09  ? 162 THR A CG2   1 
ATOM   1230 N N     . MET A 1 165 ? -5.763  -41.451 -6.824  1.00 37.31  ? 163 MET A N     1 
ATOM   1231 C CA    . MET A 1 165 ? -6.930  -42.358 -6.943  1.00 39.37  ? 163 MET A CA    1 
ATOM   1232 C C     . MET A 1 165 ? -7.963  -41.849 -5.926  1.00 38.28  ? 163 MET A C     1 
ATOM   1233 O O     . MET A 1 165 ? -7.583  -41.619 -4.768  1.00 35.40  ? 163 MET A O     1 
ATOM   1234 C CB    . MET A 1 165 ? -6.568  -43.846 -6.774  1.00 42.89  ? 163 MET A CB    1 
ATOM   1235 C CG    . MET A 1 165 ? -5.514  -44.175 -5.712  1.00 50.66  ? 163 MET A CG    1 
ATOM   1236 S SD    . MET A 1 165 ? -5.209  -45.972 -5.582  1.00 61.57  ? 163 MET A SD    1 
ATOM   1237 C CE    . MET A 1 165 ? -3.483  -46.038 -5.119  1.00 65.60  ? 163 MET A CE    1 
ATOM   1238 N N     . CYS A 1 166 ? -9.178  -41.514 -6.376  1.00 33.94  ? 164 CYS A N     1 
ATOM   1239 C CA    . CYS A 1 166 ? -10.218 -40.906 -5.517  1.00 33.45  ? 164 CYS A CA    1 
ATOM   1240 C C     . CYS A 1 166 ? -11.412 -41.848 -5.452  1.00 34.69  ? 164 CYS A C     1 
ATOM   1241 O O     . CYS A 1 166 ? -12.356 -41.633 -6.203  1.00 33.07  ? 164 CYS A O     1 
ATOM   1242 C CB    . CYS A 1 166 ? -10.626 -39.521 -6.002  1.00 34.79  ? 164 CYS A CB    1 
ATOM   1243 S SG    . CYS A 1 166 ? -9.303  -38.291 -5.840  1.00 38.63  ? 164 CYS A SG    1 
ATOM   1244 N N     . LEU A 1 167 ? -11.373 -42.828 -4.541  1.00 35.61  ? 165 LEU A N     1 
ATOM   1245 C CA    . LEU A 1 167 ? -12.477 -43.811 -4.347  1.00 34.96  ? 165 LEU A CA    1 
ATOM   1246 C C     . LEU A 1 167 ? -13.272 -43.466 -3.089  1.00 32.73  ? 165 LEU A C     1 
ATOM   1247 O O     . LEU A 1 167 ? -14.496 -43.321 -3.166  1.00 28.83  ? 165 LEU A O     1 
ATOM   1248 C CB    . LEU A 1 167 ? -11.888 -45.218 -4.217  1.00 34.28  ? 165 LEU A CB    1 
ATOM   1249 C CG    . LEU A 1 167 ? -11.063 -45.702 -5.398  1.00 34.08  ? 165 LEU A CG    1 
ATOM   1250 C CD1   . LEU A 1 167 ? -9.675  -45.096 -5.373  1.00 34.27  ? 165 LEU A CD1   1 
ATOM   1251 C CD2   . LEU A 1 167 ? -10.982 -47.216 -5.411  1.00 34.52  ? 165 LEU A CD2   1 
ATOM   1252 N N     . THR A 1 168 ? -12.561 -43.475 -1.964  1.00 32.93  ? 166 THR A N     1 
ATOM   1253 C CA    . THR A 1 168 ? -13.184 -43.447 -0.622  1.00 29.06  ? 166 THR A CA    1 
ATOM   1254 C C     . THR A 1 168 ? -14.025 -42.239 -0.225  1.00 29.22  ? 166 THR A C     1 
ATOM   1255 O O     . THR A 1 168 ? -13.611 -41.112 -0.476  1.00 28.00  ? 166 THR A O     1 
ATOM   1256 C CB    . THR A 1 168 ? -12.096 -43.730 0.431   1.00 29.27  ? 166 THR A CB    1 
ATOM   1257 O OG1   . THR A 1 168 ? -11.351 -44.875 0.022   1.00 31.11  ? 166 THR A OG1   1 
ATOM   1258 C CG2   . THR A 1 168 ? -12.656 -43.956 1.817   1.00 32.03  ? 166 THR A CG2   1 
ATOM   1259 N N     . GLU A 1 169 ? -15.185 -42.530 0.356   1.00 32.88  ? 167 GLU A N     1 
ATOM   1260 C CA    . GLU A 1 169 ? -16.041 -41.489 0.990   1.00 33.71  ? 167 GLU A CA    1 
ATOM   1261 C C     . GLU A 1 169 ? -16.282 -41.854 2.466   1.00 33.76  ? 167 GLU A C     1 
ATOM   1262 O O     . GLU A 1 169 ? -15.962 -42.961 2.897   1.00 30.91  ? 167 GLU A O     1 
ATOM   1263 C CB    . GLU A 1 169 ? -17.339 -41.390 0.193   1.00 36.16  ? 167 GLU A CB    1 
ATOM   1264 C CG    . GLU A 1 169 ? -17.100 -41.134 -1.287  1.00 38.32  ? 167 GLU A CG    1 
ATOM   1265 C CD    . GLU A 1 169 ? -18.329 -41.168 -2.174  1.00 37.59  ? 167 GLU A CD    1 
ATOM   1266 O OE1   . GLU A 1 169 ? -18.157 -40.936 -3.359  1.00 45.22  ? 167 GLU A OE1   1 
ATOM   1267 O OE2   . GLU A 1 169 ? -19.428 -41.463 -1.692  1.00 37.51  ? 167 GLU A OE2   1 
ATOM   1268 N N     . PRO A 1 170 ? -16.846 -40.939 3.291   1.00 33.40  ? 168 PRO A N     1 
ATOM   1269 C CA    . PRO A 1 170 ? -17.001 -41.170 4.739   1.00 30.88  ? 168 PRO A CA    1 
ATOM   1270 C C     . PRO A 1 170 ? -17.687 -42.487 5.093   1.00 29.74  ? 168 PRO A C     1 
ATOM   1271 O O     . PRO A 1 170 ? -17.221 -43.170 6.010   1.00 28.32  ? 168 PRO A O     1 
ATOM   1272 C CB    . PRO A 1 170 ? -17.827 -39.958 5.213   1.00 27.96  ? 168 PRO A CB    1 
ATOM   1273 C CG    . PRO A 1 170 ? -17.416 -38.853 4.245   1.00 30.70  ? 168 PRO A CG    1 
ATOM   1274 C CD    . PRO A 1 170 ? -17.255 -39.566 2.908   1.00 31.07  ? 168 PRO A CD    1 
ATOM   1275 N N     . HIS A 1 171 ? -18.714 -42.864 4.330   1.00 31.31  ? 169 HIS A N     1 
ATOM   1276 C CA    . HIS A 1 171 ? -19.531 -44.090 4.591   1.00 31.02  ? 169 HIS A CA    1 
ATOM   1277 C C     . HIS A 1 171 ? -18.954 -45.336 3.872   1.00 29.11  ? 169 HIS A C     1 
ATOM   1278 O O     . HIS A 1 171 ? -19.481 -46.457 4.072   1.00 25.66  ? 169 HIS A O     1 
ATOM   1279 C CB    . HIS A 1 171 ? -21.002 -43.822 4.246   1.00 30.59  ? 169 HIS A CB    1 
ATOM   1280 C CG    . HIS A 1 171 ? -21.202 -43.702 2.770   1.00 35.08  ? 169 HIS A CG    1 
ATOM   1281 N ND1   . HIS A 1 171 ? -20.709 -42.622 2.039   1.00 32.18  ? 169 HIS A ND1   1 
ATOM   1282 C CD2   . HIS A 1 171 ? -21.755 -44.552 1.881   1.00 35.58  ? 169 HIS A CD2   1 
ATOM   1283 C CE1   . HIS A 1 171 ? -21.014 -42.778 0.770   1.00 39.51  ? 169 HIS A CE1   1 
ATOM   1284 N NE2   . HIS A 1 171 ? -21.631 -43.975 0.642   1.00 45.58  ? 169 HIS A NE2   1 
ATOM   1285 N N     . CYS A 1 172 ? -17.977 -45.148 2.993   1.00 29.58  ? 170 CYS A N     1 
ATOM   1286 C CA    . CYS A 1 172 ? -17.564 -46.305 2.157   1.00 29.22  ? 170 CYS A CA    1 
ATOM   1287 C C     . CYS A 1 172 ? -16.071 -46.358 1.810   1.00 28.16  ? 170 CYS A C     1 
ATOM   1288 O O     . CYS A 1 172 ? -15.551 -45.390 1.251   1.00 30.40  ? 170 CYS A O     1 
ATOM   1289 C CB    . CYS A 1 172 ? -18.393 -46.312 0.873   1.00 30.84  ? 170 CYS A CB    1 
ATOM   1290 S SG    . CYS A 1 172 ? -18.122 -44.918 -0.242  1.00 36.80  ? 170 CYS A SG    1 
ATOM   1291 N N     . GLY A 1 173 ? -15.428 -47.479 2.120   1.00 31.91  ? 171 GLY A N     1 
ATOM   1292 C CA    . GLY A 1 173 ? -14.032 -47.709 1.712   1.00 34.77  ? 171 GLY A CA    1 
ATOM   1293 C C     . GLY A 1 173 ? -13.952 -49.042 0.990   1.00 35.46  ? 171 GLY A C     1 
ATOM   1294 O O     . GLY A 1 173 ? -13.599 -49.051 -0.195  1.00 39.83  ? 171 GLY A O     1 
ATOM   1295 N N     . THR A 1 174 ? -14.311 -50.125 1.670   1.00 30.07  ? 172 THR A N     1 
ATOM   1296 C CA    . THR A 1 174 ? -14.366 -51.455 1.020   1.00 32.71  ? 172 THR A CA    1 
ATOM   1297 C C     . THR A 1 174 ? -15.611 -51.524 0.130   1.00 33.90  ? 172 THR A C     1 
ATOM   1298 O O     . THR A 1 174 ? -15.488 -52.028 -0.987  1.00 36.42  ? 172 THR A O     1 
ATOM   1299 C CB    . THR A 1 174 ? -14.366 -52.580 2.066   1.00 32.30  ? 172 THR A CB    1 
ATOM   1300 O OG1   . THR A 1 174 ? -13.165 -52.527 2.837   1.00 31.74  ? 172 THR A OG1   1 
ATOM   1301 C CG2   . THR A 1 174 ? -14.530 -53.952 1.451   1.00 31.28  ? 172 THR A CG2   1 
ATOM   1302 N N     . ASP A 1 175 ? -16.746 -51.002 0.594   1.00 29.65  ? 173 ASP A N     1 
ATOM   1303 C CA    . ASP A 1 175 ? -18.027 -51.124 -0.151  1.00 30.61  ? 173 ASP A CA    1 
ATOM   1304 C C     . ASP A 1 175 ? -18.186 -49.961 -1.140  1.00 31.40  ? 173 ASP A C     1 
ATOM   1305 O O     . ASP A 1 175 ? -19.035 -49.103 -0.908  1.00 31.46  ? 173 ASP A O     1 
ATOM   1306 C CB    . ASP A 1 175 ? -19.179 -51.306 0.842   1.00 32.56  ? 173 ASP A CB    1 
ATOM   1307 C CG    . ASP A 1 175 ? -20.501 -51.710 0.224   1.00 34.25  ? 173 ASP A CG    1 
ATOM   1308 O OD1   . ASP A 1 175 ? -20.616 -51.648 -1.010  1.00 33.13  ? 173 ASP A OD1   1 
ATOM   1309 O OD2   . ASP A 1 175 ? -21.404 -52.074 0.993   1.00 34.42  ? 173 ASP A OD2   1 
ATOM   1310 N N     . LEU A 1 176 ? -17.412 -49.975 -2.221  1.00 33.25  ? 174 LEU A N     1 
ATOM   1311 C CA    . LEU A 1 176 ? -17.439 -48.874 -3.216  1.00 35.19  ? 174 LEU A CA    1 
ATOM   1312 C C     . LEU A 1 176 ? -18.809 -48.819 -3.889  1.00 39.46  ? 174 LEU A C     1 
ATOM   1313 O O     . LEU A 1 176 ? -19.164 -47.749 -4.390  1.00 39.86  ? 174 LEU A O     1 
ATOM   1314 C CB    . LEU A 1 176 ? -16.305 -49.103 -4.214  1.00 41.02  ? 174 LEU A CB    1 
ATOM   1315 C CG    . LEU A 1 176 ? -14.896 -48.947 -3.648  1.00 41.66  ? 174 LEU A CG    1 
ATOM   1316 C CD1   . LEU A 1 176 ? -13.860 -49.474 -4.627  1.00 41.03  ? 174 LEU A CD1   1 
ATOM   1317 C CD2   . LEU A 1 176 ? -14.613 -47.496 -3.301  1.00 39.73  ? 174 LEU A CD2   1 
ATOM   1318 N N     . GLY A 1 177 ? -19.569 -49.907 -3.881  1.00 36.15  ? 175 GLY A N     1 
ATOM   1319 C CA    . GLY A 1 177 ? -20.929 -49.878 -4.450  1.00 36.70  ? 175 GLY A CA    1 
ATOM   1320 C C     . GLY A 1 177 ? -21.817 -48.803 -3.846  1.00 34.04  ? 175 GLY A C     1 
ATOM   1321 O O     . GLY A 1 177 ? -22.755 -48.386 -4.523  1.00 33.09  ? 175 GLY A O     1 
ATOM   1322 N N     . MET A 1 178 ? -21.532 -48.372 -2.620  1.00 32.72  ? 176 MET A N     1 
ATOM   1323 C CA    . MET A 1 178 ? -22.410 -47.388 -1.928  1.00 35.84  ? 176 MET A CA    1 
ATOM   1324 C C     . MET A 1 178 ? -21.993 -45.949 -2.267  1.00 35.41  ? 176 MET A C     1 
ATOM   1325 O O     . MET A 1 178 ? -22.679 -45.042 -1.770  1.00 38.61  ? 176 MET A O     1 
ATOM   1326 C CB    . MET A 1 178 ? -22.322 -47.542 -0.405  1.00 34.92  ? 176 MET A CB    1 
ATOM   1327 C CG    . MET A 1 178 ? -22.943 -48.794 0.139   1.00 34.25  ? 176 MET A CG    1 
ATOM   1328 S SD    . MET A 1 178 ? -23.296 -48.602 1.925   1.00 37.61  ? 176 MET A SD    1 
ATOM   1329 C CE    . MET A 1 178 ? -21.656 -48.606 2.649   1.00 31.73  ? 176 MET A CE    1 
ATOM   1330 N N     . LEU A 1 179 ? -20.903 -45.741 -3.004  1.00 32.77  ? 177 LEU A N     1 
ATOM   1331 C CA    . LEU A 1 179 ? -20.401 -44.364 -3.282  1.00 37.39  ? 177 LEU A CA    1 
ATOM   1332 C C     . LEU A 1 179 ? -21.497 -43.502 -3.926  1.00 40.42  ? 177 LEU A C     1 
ATOM   1333 O O     . LEU A 1 179 ? -22.316 -44.051 -4.671  1.00 38.24  ? 177 LEU A O     1 
ATOM   1334 C CB    . LEU A 1 179 ? -19.117 -44.424 -4.117  1.00 39.24  ? 177 LEU A CB    1 
ATOM   1335 C CG    . LEU A 1 179 ? -19.254 -44.446 -5.637  1.00 36.79  ? 177 LEU A CG    1 
ATOM   1336 C CD1   . LEU A 1 179 ? -19.358 -43.037 -6.199  1.00 36.43  ? 177 LEU A CD1   1 
ATOM   1337 C CD2   . LEU A 1 179 ? -18.056 -45.152 -6.247  1.00 37.34  ? 177 LEU A CD2   1 
ATOM   1338 N N     . ARG A 1 180 ? -21.488 -42.197 -3.654  1.00 39.61  ? 178 ARG A N     1 
ATOM   1339 C CA    . ARG A 1 180 ? -22.576 -41.302 -4.113  1.00 37.26  ? 178 ARG A CA    1 
ATOM   1340 C C     . ARG A 1 180 ? -22.023 -40.034 -4.765  1.00 39.31  ? 178 ARG A C     1 
ATOM   1341 O O     . ARG A 1 180 ? -22.812 -39.114 -4.996  1.00 36.25  ? 178 ARG A O     1 
ATOM   1342 C CB    . ARG A 1 180 ? -23.426 -40.938 -2.901  1.00 38.17  ? 178 ARG A CB    1 
ATOM   1343 C CG    . ARG A 1 180 ? -24.077 -42.131 -2.221  1.00 44.17  ? 178 ARG A CG    1 
ATOM   1344 C CD    . ARG A 1 180 ? -24.369 -41.885 -0.756  1.00 44.54  ? 178 ARG A CD    1 
ATOM   1345 N NE    . ARG A 1 180 ? -24.829 -43.111 -0.128  1.00 46.44  ? 178 ARG A NE    1 
ATOM   1346 C CZ    . ARG A 1 180 ? -24.833 -43.334 1.177   1.00 46.59  ? 178 ARG A CZ    1 
ATOM   1347 N NH1   . ARG A 1 180 ? -24.401 -42.403 2.008   1.00 46.45  ? 178 ARG A NH1   1 
ATOM   1348 N NH2   . ARG A 1 180 ? -25.268 -44.489 1.647   1.00 49.37  ? 178 ARG A NH2   1 
ATOM   1349 N N     . THR A 1 181 ? -20.718 -39.976 -5.023  1.00 39.02  ? 179 THR A N     1 
ATOM   1350 C CA    . THR A 1 181 ? -20.167 -38.813 -5.763  1.00 39.13  ? 179 THR A CA    1 
ATOM   1351 C C     . THR A 1 181 ? -20.828 -38.814 -7.150  1.00 43.76  ? 179 THR A C     1 
ATOM   1352 O O     . THR A 1 181 ? -20.869 -39.876 -7.774  1.00 39.89  ? 179 THR A O     1 
ATOM   1353 C CB    . THR A 1 181 ? -18.635 -38.796 -5.726  1.00 40.10  ? 179 THR A CB    1 
ATOM   1354 O OG1   . THR A 1 181 ? -18.234 -38.317 -4.444  1.00 40.56  ? 179 THR A OG1   1 
ATOM   1355 C CG2   . THR A 1 181 ? -18.030 -37.934 -6.809  1.00 42.35  ? 179 THR A CG2   1 
ATOM   1356 N N     . LYS A 1 182 ? -21.334 -37.666 -7.596  1.00 50.11  ? 180 LYS A N     1 
ATOM   1357 C CA    . LYS A 1 182 ? -22.123 -37.600 -8.853  1.00 50.80  ? 180 LYS A CA    1 
ATOM   1358 C C     . LYS A 1 182 ? -21.356 -37.004 -10.032 1.00 48.00  ? 180 LYS A C     1 
ATOM   1359 O O     . LYS A 1 182 ? -20.428 -36.219 -9.806  1.00 44.09  ? 180 LYS A O     1 
ATOM   1360 C CB    . LYS A 1 182 ? -23.364 -36.738 -8.609  1.00 52.05  ? 180 LYS A CB    1 
ATOM   1361 C CG    . LYS A 1 182 ? -24.106 -37.011 -7.310  1.00 55.44  ? 180 LYS A CG    1 
ATOM   1362 C CD    . LYS A 1 182 ? -25.355 -37.842 -7.495  1.00 64.82  ? 180 LYS A CD    1 
ATOM   1363 C CE    . LYS A 1 182 ? -25.082 -39.330 -7.553  1.00 78.78  ? 180 LYS A CE    1 
ATOM   1364 N NZ    . LYS A 1 182 ? -25.895 -39.995 -8.599  1.00 84.89  ? 180 LYS A NZ    1 
ATOM   1365 N N     . ALA A 1 183 ? -21.751 -37.382 -11.246 1.00 48.61  ? 181 ALA A N     1 
ATOM   1366 C CA    . ALA A 1 183 ? -21.167 -36.792 -12.471 1.00 45.12  ? 181 ALA A CA    1 
ATOM   1367 C C     . ALA A 1 183 ? -22.317 -36.407 -13.402 1.00 44.80  ? 181 ALA A C     1 
ATOM   1368 O O     . ALA A 1 183 ? -22.973 -37.319 -13.905 1.00 44.75  ? 181 ALA A O     1 
ATOM   1369 C CB    . ALA A 1 183 ? -20.234 -37.762 -13.121 1.00 45.55  ? 181 ALA A CB    1 
ATOM   1370 N N     . GLU A 1 184 ? -22.574 -35.112 -13.571 1.00 48.09  ? 182 GLU A N     1 
ATOM   1371 C CA    . GLU A 1 184 ? -23.661 -34.591 -14.459 1.00 53.52  ? 182 GLU A CA    1 
ATOM   1372 C C     . GLU A 1 184 ? -23.097 -34.374 -15.873 1.00 53.56  ? 182 GLU A C     1 
ATOM   1373 O O     . GLU A 1 184 ? -22.142 -33.607 -16.033 1.00 47.95  ? 182 GLU A O     1 
ATOM   1374 C CB    . GLU A 1 184 ? -24.234 -33.278 -13.903 1.00 57.63  ? 182 GLU A CB    1 
ATOM   1375 C CG    . GLU A 1 184 ? -25.539 -33.408 -13.118 1.00 63.26  ? 182 GLU A CG    1 
ATOM   1376 C CD    . GLU A 1 184 ? -26.749 -33.845 -13.940 1.00 73.35  ? 182 GLU A CD    1 
ATOM   1377 O OE1   . GLU A 1 184 ? -27.480 -34.768 -13.505 1.00 74.23  ? 182 GLU A OE1   1 
ATOM   1378 O OE2   . GLU A 1 184 ? -26.958 -33.272 -15.024 1.00 76.44  ? 182 GLU A OE2   1 
ATOM   1379 N N     . PRO A 1 185 ? -23.634 -35.030 -16.940 1.00 54.21  ? 183 PRO A N     1 
ATOM   1380 C CA    . PRO A 1 185 ? -23.288 -34.686 -18.335 1.00 53.93  ? 183 PRO A CA    1 
ATOM   1381 C C     . PRO A 1 185 ? -23.480 -33.203 -18.705 1.00 53.45  ? 183 PRO A C     1 
ATOM   1382 O O     . PRO A 1 185 ? -24.460 -32.630 -18.266 1.00 48.53  ? 183 PRO A O     1 
ATOM   1383 C CB    . PRO A 1 185 ? -24.272 -35.521 -19.164 1.00 51.90  ? 183 PRO A CB    1 
ATOM   1384 C CG    . PRO A 1 185 ? -24.532 -36.737 -18.283 1.00 54.55  ? 183 PRO A CG    1 
ATOM   1385 C CD    . PRO A 1 185 ? -24.562 -36.173 -16.871 1.00 51.15  ? 183 PRO A CD    1 
ATOM   1386 N N     . GLN A 1 186 ? -22.516 -32.599 -19.420 1.00 56.21  ? 184 GLN A N     1 
ATOM   1387 C CA    . GLN A 1 186 ? -22.599 -31.205 -19.958 1.00 60.33  ? 184 GLN A CA    1 
ATOM   1388 C C     . GLN A 1 186 ? -22.739 -31.257 -21.492 1.00 57.68  ? 184 GLN A C     1 
ATOM   1389 O O     . GLN A 1 186 ? -22.236 -32.208 -22.105 1.00 57.33  ? 184 GLN A O     1 
ATOM   1390 C CB    . GLN A 1 186 ? -21.374 -30.348 -19.602 1.00 55.35  ? 184 GLN A CB    1 
ATOM   1391 C CG    . GLN A 1 186 ? -20.942 -30.395 -18.147 1.00 55.63  ? 184 GLN A CG    1 
ATOM   1392 C CD    . GLN A 1 186 ? -21.989 -29.829 -17.228 1.00 54.11  ? 184 GLN A CD    1 
ATOM   1393 O OE1   . GLN A 1 186 ? -22.319 -28.652 -17.295 1.00 51.53  ? 184 GLN A OE1   1 
ATOM   1394 N NE2   . GLN A 1 186 ? -22.536 -30.675 -16.371 1.00 52.25  ? 184 GLN A NE2   1 
ATOM   1395 N N     . ALA A 1 187 ? -23.333 -30.226 -22.092 1.00 58.62  ? 185 ALA A N     1 
ATOM   1396 C CA    . ALA A 1 187 ? -23.607 -30.125 -23.547 1.00 57.59  ? 185 ALA A CA    1 
ATOM   1397 C C     . ALA A 1 187 ? -22.343 -30.398 -24.374 1.00 50.31  ? 185 ALA A C     1 
ATOM   1398 O O     . ALA A 1 187 ? -22.486 -30.999 -25.433 1.00 51.67  ? 185 ALA A O     1 
ATOM   1399 C CB    . ALA A 1 187 ? -24.177 -28.761 -23.849 1.00 64.10  ? 185 ALA A CB    1 
ATOM   1400 N N     . ASP A 1 188 ? -21.158 -29.983 -23.906 1.00 45.02  ? 186 ASP A N     1 
ATOM   1401 C CA    . ASP A 1 188 ? -19.873 -30.124 -24.642 1.00 39.66  ? 186 ASP A CA    1 
ATOM   1402 C C     . ASP A 1 188 ? -19.202 -31.482 -24.431 1.00 41.35  ? 186 ASP A C     1 
ATOM   1403 O O     . ASP A 1 188 ? -18.026 -31.596 -24.793 1.00 47.11  ? 186 ASP A O     1 
ATOM   1404 C CB    . ASP A 1 188 ? -18.859 -29.070 -24.202 1.00 46.32  ? 186 ASP A CB    1 
ATOM   1405 C CG    . ASP A 1 188 ? -18.585 -29.055 -22.701 1.00 52.25  ? 186 ASP A CG    1 
ATOM   1406 O OD1   . ASP A 1 188 ? -18.662 -30.122 -22.060 1.00 47.82  ? 186 ASP A OD1   1 
ATOM   1407 O OD2   . ASP A 1 188 ? -18.326 -27.961 -22.188 1.00 59.23  ? 186 ASP A OD2   1 
ATOM   1408 N N     . GLY A 1 189 ? -19.877 -32.474 -23.849 1.00 46.72  ? 187 GLY A N     1 
ATOM   1409 C CA    . GLY A 1 189 ? -19.343 -33.841 -23.697 1.00 47.78  ? 187 GLY A CA    1 
ATOM   1410 C C     . GLY A 1 189 ? -18.396 -34.006 -22.504 1.00 50.11  ? 187 GLY A C     1 
ATOM   1411 O O     . GLY A 1 189 ? -17.930 -35.131 -22.283 1.00 52.45  ? 187 GLY A O     1 
ATOM   1412 N N     . SER A 1 190 ? -18.085 -32.939 -21.775 1.00 47.26  ? 188 SER A N     1 
ATOM   1413 C CA    . SER A 1 190 ? -17.404 -33.014 -20.457 1.00 46.60  ? 188 SER A CA    1 
ATOM   1414 C C     . SER A 1 190 ? -18.455 -33.320 -19.388 1.00 47.96  ? 188 SER A C     1 
ATOM   1415 O O     . SER A 1 190 ? -19.670 -33.285 -19.695 1.00 44.10  ? 188 SER A O     1 
ATOM   1416 C CB    . SER A 1 190 ? -16.689 -31.727 -20.141 1.00 42.28  ? 188 SER A CB    1 
ATOM   1417 O OG    . SER A 1 190 ? -17.594 -30.832 -19.503 1.00 38.94  ? 188 SER A OG    1 
ATOM   1418 N N     . TYR A 1 191 ? -17.997 -33.561 -18.158 1.00 49.75  ? 189 TYR A N     1 
ATOM   1419 C CA    . TYR A 1 191 ? -18.861 -33.795 -16.975 1.00 50.03  ? 189 TYR A CA    1 
ATOM   1420 C C     . TYR A 1 191 ? -18.503 -32.814 -15.853 1.00 49.06  ? 189 TYR A C     1 
ATOM   1421 O O     . TYR A 1 191 ? -17.448 -32.156 -15.895 1.00 46.78  ? 189 TYR A O     1 
ATOM   1422 C CB    . TYR A 1 191 ? -18.746 -35.246 -16.512 1.00 50.63  ? 189 TYR A CB    1 
ATOM   1423 C CG    . TYR A 1 191 ? -19.221 -36.266 -17.511 1.00 47.28  ? 189 TYR A CG    1 
ATOM   1424 C CD1   . TYR A 1 191 ? -18.424 -36.683 -18.561 1.00 46.92  ? 189 TYR A CD1   1 
ATOM   1425 C CD2   . TYR A 1 191 ? -20.477 -36.829 -17.386 1.00 53.56  ? 189 TYR A CD2   1 
ATOM   1426 C CE1   . TYR A 1 191 ? -18.860 -37.640 -19.460 1.00 45.09  ? 189 TYR A CE1   1 
ATOM   1427 C CE2   . TYR A 1 191 ? -20.935 -37.770 -18.285 1.00 48.62  ? 189 TYR A CE2   1 
ATOM   1428 C CZ    . TYR A 1 191 ? -20.123 -38.180 -19.318 1.00 46.09  ? 189 TYR A CZ    1 
ATOM   1429 O OH    . TYR A 1 191 ? -20.596 -39.123 -20.183 1.00 51.77  ? 189 TYR A OH    1 
ATOM   1430 N N     . LYS A 1 192 ? -19.401 -32.724 -14.877 1.00 47.96  ? 190 LYS A N     1 
ATOM   1431 C CA    . LYS A 1 192 ? -19.260 -31.896 -13.656 1.00 49.49  ? 190 LYS A CA    1 
ATOM   1432 C C     . LYS A 1 192 ? -19.425 -32.795 -12.426 1.00 49.38  ? 190 LYS A C     1 
ATOM   1433 O O     . LYS A 1 192 ? -20.539 -33.282 -12.172 1.00 49.29  ? 190 LYS A O     1 
ATOM   1434 C CB    . LYS A 1 192 ? -20.248 -30.727 -13.662 1.00 51.17  ? 190 LYS A CB    1 
ATOM   1435 C CG    . LYS A 1 192 ? -19.610 -29.397 -14.020 1.00 55.91  ? 190 LYS A CG    1 
ATOM   1436 C CD    . LYS A 1 192 ? -20.579 -28.262 -14.209 1.00 58.12  ? 190 LYS A CD    1 
ATOM   1437 C CE    . LYS A 1 192 ? -19.849 -26.946 -14.343 1.00 61.51  ? 190 LYS A CE    1 
ATOM   1438 N NZ    . LYS A 1 192 ? -20.354 -26.191 -15.507 1.00 68.38  ? 190 LYS A NZ    1 
ATOM   1439 N N     . VAL A 1 193 ? -18.334 -32.998 -11.700 1.00 48.79  ? 191 VAL A N     1 
ATOM   1440 C CA    . VAL A 1 193 ? -18.273 -33.949 -10.558 1.00 49.80  ? 191 VAL A CA    1 
ATOM   1441 C C     . VAL A 1 193 ? -18.574 -33.172 -9.281  1.00 44.31  ? 191 VAL A C     1 
ATOM   1442 O O     . VAL A 1 193 ? -17.917 -32.158 -9.020  1.00 39.19  ? 191 VAL A O     1 
ATOM   1443 C CB    . VAL A 1 193 ? -16.905 -34.649 -10.500 1.00 50.29  ? 191 VAL A CB    1 
ATOM   1444 C CG1   . VAL A 1 193 ? -16.903 -35.760 -9.454  1.00 49.19  ? 191 VAL A CG1   1 
ATOM   1445 C CG2   . VAL A 1 193 ? -16.508 -35.157 -11.884 1.00 45.79  ? 191 VAL A CG2   1 
ATOM   1446 N N     . THR A 1 194 ? -19.574 -33.617 -8.539  1.00 44.35  ? 192 THR A N     1 
ATOM   1447 C CA    . THR A 1 194 ? -19.947 -33.032 -7.228  1.00 46.69  ? 192 THR A CA    1 
ATOM   1448 C C     . THR A 1 194 ? -19.898 -34.162 -6.181  1.00 48.26  ? 192 THR A C     1 
ATOM   1449 O O     . THR A 1 194 ? -20.553 -35.215 -6.386  1.00 47.43  ? 192 THR A O     1 
ATOM   1450 C CB    . THR A 1 194 ? -21.272 -32.253 -7.338  1.00 44.40  ? 192 THR A CB    1 
ATOM   1451 O OG1   . THR A 1 194 ? -21.087 -31.183 -8.266  1.00 46.43  ? 192 THR A OG1   1 
ATOM   1452 C CG2   . THR A 1 194 ? -21.723 -31.653 -6.023  1.00 41.21  ? 192 THR A CG2   1 
ATOM   1453 N N     . GLY A 1 195 ? -19.100 -33.969 -5.127  1.00 45.51  ? 193 GLY A N     1 
ATOM   1454 C CA    . GLY A 1 195 ? -19.030 -34.885 -3.979  1.00 40.45  ? 193 GLY A CA    1 
ATOM   1455 C C     . GLY A 1 195 ? -17.777 -34.662 -3.147  1.00 43.88  ? 193 GLY A C     1 
ATOM   1456 O O     . GLY A 1 195 ? -16.822 -33.946 -3.606  1.00 41.14  ? 193 GLY A O     1 
ATOM   1457 N N     . THR A 1 196 ? -17.773 -35.255 -1.952  1.00 39.63  ? 194 THR A N     1 
ATOM   1458 C CA    . THR A 1 196 ? -16.623 -35.225 -1.028  1.00 39.86  ? 194 THR A CA    1 
ATOM   1459 C C     . THR A 1 196 ? -15.985 -36.621 -1.009  1.00 36.87  ? 194 THR A C     1 
ATOM   1460 O O     . THR A 1 196 ? -16.722 -37.646 -0.816  1.00 36.71  ? 194 THR A O     1 
ATOM   1461 C CB    . THR A 1 196 ? -17.069 -34.707 0.345   1.00 43.89  ? 194 THR A CB    1 
ATOM   1462 O OG1   . THR A 1 196 ? -17.670 -33.422 0.156   1.00 40.92  ? 194 THR A OG1   1 
ATOM   1463 C CG2   . THR A 1 196 ? -15.916 -34.633 1.326   1.00 46.52  ? 194 THR A CG2   1 
ATOM   1464 N N     . LYS A 1 197 ? -14.685 -36.647 -1.283  1.00 33.16  ? 195 LYS A N     1 
ATOM   1465 C CA    . LYS A 1 197 ? -13.823 -37.836 -1.128  1.00 35.63  ? 195 LYS A CA    1 
ATOM   1466 C C     . LYS A 1 197 ? -12.914 -37.606 0.069   1.00 33.94  ? 195 LYS A C     1 
ATOM   1467 O O     . LYS A 1 197 ? -12.440 -36.461 0.220   1.00 32.78  ? 195 LYS A O     1 
ATOM   1468 C CB    . LYS A 1 197 ? -12.993 -38.086 -2.384  1.00 35.52  ? 195 LYS A CB    1 
ATOM   1469 C CG    . LYS A 1 197 ? -13.804 -38.460 -3.614  1.00 37.47  ? 195 LYS A CG    1 
ATOM   1470 C CD    . LYS A 1 197 ? -14.315 -39.878 -3.626  1.00 39.51  ? 195 LYS A CD    1 
ATOM   1471 C CE    . LYS A 1 197 ? -15.043 -40.215 -4.911  1.00 38.00  ? 195 LYS A CE    1 
ATOM   1472 N NZ    . LYS A 1 197 ? -15.794 -41.482 -4.785  1.00 36.89  ? 195 LYS A NZ    1 
ATOM   1473 N N     . ILE A 1 198 ? -12.697 -38.660 0.868   1.00 34.69  ? 196 ILE A N     1 
ATOM   1474 C CA    . ILE A 1 198 ? -11.833 -38.625 2.094   1.00 34.75  ? 196 ILE A CA    1 
ATOM   1475 C C     . ILE A 1 198 ? -10.613 -39.528 1.881   1.00 36.61  ? 196 ILE A C     1 
ATOM   1476 O O     . ILE A 1 198 ? -10.649 -40.453 1.026   1.00 35.38  ? 196 ILE A O     1 
ATOM   1477 C CB    . ILE A 1 198 ? -12.596 -38.994 3.390   1.00 32.32  ? 196 ILE A CB    1 
ATOM   1478 C CG1   . ILE A 1 198 ? -13.041 -40.458 3.428   1.00 35.04  ? 196 ILE A CG1   1 
ATOM   1479 C CG2   . ILE A 1 198 ? -13.770 -38.064 3.647   1.00 28.41  ? 196 ILE A CG2   1 
ATOM   1480 C CD1   . ILE A 1 198 ? -13.534 -40.913 4.803   1.00 36.58  ? 196 ILE A CD1   1 
ATOM   1481 N N     . PHE A 1 199 ? -9.565  -39.263 2.659   1.00 32.49  ? 197 PHE A N     1 
ATOM   1482 C CA    . PHE A 1 199 ? -8.345  -40.092 2.731   1.00 29.32  ? 197 PHE A CA    1 
ATOM   1483 C C     . PHE A 1 199 ? -7.647  -40.113 1.369   1.00 33.08  ? 197 PHE A C     1 
ATOM   1484 O O     . PHE A 1 199 ? -7.001  -41.123 1.126   1.00 33.04  ? 197 PHE A O     1 
ATOM   1485 C CB    . PHE A 1 199 ? -8.661  -41.524 3.192   1.00 31.34  ? 197 PHE A CB    1 
ATOM   1486 C CG    . PHE A 1 199 ? -9.203  -41.714 4.590   1.00 28.39  ? 197 PHE A CG    1 
ATOM   1487 C CD1   . PHE A 1 199 ? -9.119  -40.723 5.554   1.00 30.48  ? 197 PHE A CD1   1 
ATOM   1488 C CD2   . PHE A 1 199 ? -9.806  -42.905 4.945   1.00 29.36  ? 197 PHE A CD2   1 
ATOM   1489 C CE1   . PHE A 1 199 ? -9.646  -40.911 6.832   1.00 28.91  ? 197 PHE A CE1   1 
ATOM   1490 C CE2   . PHE A 1 199 ? -10.297 -43.117 6.232   1.00 29.75  ? 197 PHE A CE2   1 
ATOM   1491 C CZ    . PHE A 1 199 ? -10.208 -42.115 7.184   1.00 28.95  ? 197 PHE A CZ    1 
ATOM   1492 N N     . ILE A 1 200 ? -7.708  -39.044 0.559   1.00 28.18  ? 198 ILE A N     1 
ATOM   1493 C CA    . ILE A 1 200 ? -6.959  -38.966 -0.725  1.00 30.10  ? 198 ILE A CA    1 
ATOM   1494 C C     . ILE A 1 200 ? -5.483  -38.633 -0.477  1.00 31.60  ? 198 ILE A C     1 
ATOM   1495 O O     . ILE A 1 200 ? -5.144  -37.468 -0.251  1.00 31.06  ? 198 ILE A O     1 
ATOM   1496 C CB    . ILE A 1 200 ? -7.584  -37.952 -1.705  1.00 29.56  ? 198 ILE A CB    1 
ATOM   1497 C CG1   . ILE A 1 200 ? -9.085  -38.185 -1.912  1.00 29.89  ? 198 ILE A CG1   1 
ATOM   1498 C CG2   . ILE A 1 200 ? -6.798  -37.971 -3.002  1.00 29.25  ? 198 ILE A CG2   1 
ATOM   1499 C CD1   . ILE A 1 200 ? -9.509  -39.645 -2.035  1.00 29.78  ? 198 ILE A CD1   1 
ATOM   1500 N N     . SER A 1 201 ? -4.619  -39.619 -0.652  1.00 32.41  ? 199 SER A N     1 
ATOM   1501 C CA    . SER A 1 201 ? -3.147  -39.486 -0.585  1.00 29.49  ? 199 SER A CA    1 
ATOM   1502 C C     . SER A 1 201 ? -2.676  -38.524 -1.682  1.00 31.30  ? 199 SER A C     1 
ATOM   1503 O O     . SER A 1 201 ? -3.005  -38.753 -2.861  1.00 31.30  ? 199 SER A O     1 
ATOM   1504 C CB    . SER A 1 201 ? -2.489  -40.850 -0.708  1.00 29.67  ? 199 SER A CB    1 
ATOM   1505 O OG    . SER A 1 201 ? -2.938  -41.753 0.312   1.00 31.75  ? 199 SER A OG    1 
ATOM   1506 N N     . ALA A 1 202 ? -1.911  -37.493 -1.320  1.00 30.54  ? 200 ALA A N     1 
ATOM   1507 C CA    . ALA A 1 202 ? -1.325  -36.557 -2.291  1.00 31.33  ? 200 ALA A CA    1 
ATOM   1508 C C     . ALA A 1 202 ? -2.446  -35.753 -2.972  1.00 31.42  ? 200 ALA A C     1 
ATOM   1509 O O     . ALA A 1 202 ? -2.254  -35.323 -4.114  1.00 34.02  ? 200 ALA A O     1 
ATOM   1510 C CB    . ALA A 1 202 ? -0.512  -37.349 -3.286  1.00 30.28  ? 200 ALA A CB    1 
ATOM   1511 N N     . GLY A 1 203 ? -3.581  -35.593 -2.297  1.00 32.27  ? 201 GLY A N     1 
ATOM   1512 C CA    . GLY A 1 203 ? -4.798  -34.965 -2.843  1.00 36.52  ? 201 GLY A CA    1 
ATOM   1513 C C     . GLY A 1 203 ? -4.542  -33.497 -3.160  1.00 39.45  ? 201 GLY A C     1 
ATOM   1514 O O     . GLY A 1 203 ? -5.122  -32.991 -4.142  1.00 39.01  ? 201 GLY A O     1 
ATOM   1515 N N     . GLU A 1 204 ? -3.696  -32.858 -2.346  1.00 35.24  ? 202 GLU A N     1 
ATOM   1516 C CA    . GLU A 1 204 ? -3.209  -31.472 -2.500  1.00 35.71  ? 202 GLU A CA    1 
ATOM   1517 C C     . GLU A 1 204 ? -1.830  -31.394 -1.871  1.00 36.36  ? 202 GLU A C     1 
ATOM   1518 O O     . GLU A 1 204 ? -1.666  -31.945 -0.787  1.00 36.13  ? 202 GLU A O     1 
ATOM   1519 C CB    . GLU A 1 204 ? -4.112  -30.475 -1.792  1.00 36.10  ? 202 GLU A CB    1 
ATOM   1520 C CG    . GLU A 1 204 ? -3.624  -29.044 -1.919  1.00 38.59  ? 202 GLU A CG    1 
ATOM   1521 C CD    . GLU A 1 204 ? -4.052  -28.430 -3.233  1.00 40.26  ? 202 GLU A CD    1 
ATOM   1522 O OE1   . GLU A 1 204 ? -3.323  -28.598 -4.217  1.00 35.39  ? 202 GLU A OE1   1 
ATOM   1523 O OE2   . GLU A 1 204 ? -5.151  -27.852 -3.264  1.00 43.86  ? 202 GLU A OE2   1 
ATOM   1524 N N     . HIS A 1 205 ? -0.896  -30.740 -2.552  1.00 37.51  ? 203 HIS A N     1 
ATOM   1525 C CA    . HIS A 1 205 ? 0.502   -30.543 -2.097  1.00 37.92  ? 203 HIS A CA    1 
ATOM   1526 C C     . HIS A 1 205 ? 1.112   -29.418 -2.928  1.00 37.98  ? 203 HIS A C     1 
ATOM   1527 O O     . HIS A 1 205 ? 0.402   -28.897 -3.777  1.00 40.71  ? 203 HIS A O     1 
ATOM   1528 C CB    . HIS A 1 205 ? 1.279   -31.865 -2.218  1.00 41.96  ? 203 HIS A CB    1 
ATOM   1529 C CG    . HIS A 1 205 ? 1.266   -32.447 -3.591  1.00 43.56  ? 203 HIS A CG    1 
ATOM   1530 N ND1   . HIS A 1 205 ? 2.200   -32.092 -4.544  1.00 38.56  ? 203 HIS A ND1   1 
ATOM   1531 C CD2   . HIS A 1 205 ? 0.434   -33.348 -4.164  1.00 43.07  ? 203 HIS A CD2   1 
ATOM   1532 C CE1   . HIS A 1 205 ? 1.934   -32.736 -5.656  1.00 42.17  ? 203 HIS A CE1   1 
ATOM   1533 N NE2   . HIS A 1 205 ? 0.852   -33.523 -5.449  1.00 44.11  ? 203 HIS A NE2   1 
ATOM   1534 N N     . ASP A 1 206 ? 2.391   -29.122 -2.719  1.00 42.39  ? 204 ASP A N     1 
ATOM   1535 C CA    . ASP A 1 206 ? 3.085   -28.004 -3.399  1.00 38.79  ? 204 ASP A CA    1 
ATOM   1536 C C     . ASP A 1 206 ? 4.285   -28.536 -4.170  1.00 40.18  ? 204 ASP A C     1 
ATOM   1537 O O     . ASP A 1 206 ? 5.235   -27.780 -4.367  1.00 41.78  ? 204 ASP A O     1 
ATOM   1538 C CB    . ASP A 1 206 ? 3.593   -27.037 -2.339  1.00 41.70  ? 204 ASP A CB    1 
ATOM   1539 C CG    . ASP A 1 206 ? 4.419   -27.702 -1.251  1.00 42.62  ? 204 ASP A CG    1 
ATOM   1540 O OD1   . ASP A 1 206 ? 4.537   -28.933 -1.279  1.00 43.54  ? 204 ASP A OD1   1 
ATOM   1541 O OD2   . ASP A 1 206 ? 4.938   -26.980 -0.389  1.00 44.56  ? 204 ASP A OD2   1 
ATOM   1542 N N     . MET A 1 207 ? 4.224   -29.779 -4.624  1.00 41.90  ? 205 MET A N     1 
ATOM   1543 C CA    . MET A 1 207 ? 5.420   -30.404 -5.241  1.00 42.23  ? 205 MET A CA    1 
ATOM   1544 C C     . MET A 1 207 ? 5.390   -30.333 -6.780  1.00 39.47  ? 205 MET A C     1 
ATOM   1545 O O     . MET A 1 207 ? 6.456   -30.530 -7.392  1.00 36.03  ? 205 MET A O     1 
ATOM   1546 C CB    . MET A 1 207 ? 5.535   -31.862 -4.813  1.00 43.90  ? 205 MET A CB    1 
ATOM   1547 C CG    . MET A 1 207 ? 5.601   -32.038 -3.319  1.00 50.44  ? 205 MET A CG    1 
ATOM   1548 S SD    . MET A 1 207 ? 6.757   -33.348 -2.903  1.00 50.35  ? 205 MET A SD    1 
ATOM   1549 C CE    . MET A 1 207 ? 5.728   -34.297 -1.798  1.00 62.35  ? 205 MET A CE    1 
ATOM   1550 N N     . ALA A 1 208 ? 4.237   -30.131 -7.409  1.00 38.71  ? 206 ALA A N     1 
ATOM   1551 C CA    . ALA A 1 208 ? 4.113   -30.224 -8.888  1.00 39.16  ? 206 ALA A CA    1 
ATOM   1552 C C     . ALA A 1 208 ? 3.292   -29.049 -9.461  1.00 39.45  ? 206 ALA A C     1 
ATOM   1553 O O     . ALA A 1 208 ? 2.877   -28.183 -8.683  1.00 43.05  ? 206 ALA A O     1 
ATOM   1554 C CB    . ALA A 1 208 ? 3.534   -31.579 -9.243  1.00 38.49  ? 206 ALA A CB    1 
ATOM   1555 N N     . ASP A 1 209 ? 3.105   -28.992 -10.793 1.00 46.57  ? 207 ASP A N     1 
ATOM   1556 C CA    . ASP A 1 209 ? 2.453   -27.848 -11.502 1.00 45.90  ? 207 ASP A CA    1 
ATOM   1557 C C     . ASP A 1 209 ? 0.961   -28.140 -11.629 1.00 44.02  ? 207 ASP A C     1 
ATOM   1558 O O     . ASP A 1 209 ? 0.195   -27.239 -11.990 1.00 49.26  ? 207 ASP A O     1 
ATOM   1559 C CB    . ASP A 1 209 ? 3.059   -27.593 -12.889 1.00 46.57  ? 207 ASP A CB    1 
ATOM   1560 C CG    . ASP A 1 209 ? 4.571   -27.416 -12.930 1.00 51.78  ? 207 ASP A CG    1 
ATOM   1561 O OD1   . ASP A 1 209 ? 5.130   -26.850 -11.963 1.00 56.98  ? 207 ASP A OD1   1 
ATOM   1562 O OD2   . ASP A 1 209 ? 5.186   -27.850 -13.931 1.00 57.83  ? 207 ASP A OD2   1 
ATOM   1563 N N     . ASN A 1 210 ? 0.580   -29.394 -11.422 1.00 44.99  ? 208 ASN A N     1 
ATOM   1564 C CA    . ASN A 1 210 ? -0.823  -29.847 -11.563 1.00 43.44  ? 208 ASN A CA    1 
ATOM   1565 C C     . ASN A 1 210 ? -0.954  -31.203 -10.870 1.00 40.34  ? 208 ASN A C     1 
ATOM   1566 O O     . ASN A 1 210 ? 0.054   -31.919 -10.724 1.00 38.95  ? 208 ASN A O     1 
ATOM   1567 C CB    . ASN A 1 210 ? -1.254  -29.929 -13.036 1.00 43.70  ? 208 ASN A CB    1 
ATOM   1568 C CG    . ASN A 1 210 ? -2.756  -29.812 -13.269 1.00 44.29  ? 208 ASN A CG    1 
ATOM   1569 O OD1   . ASN A 1 210 ? -3.547  -29.541 -12.358 1.00 35.76  ? 208 ASN A OD1   1 
ATOM   1570 N ND2   . ASN A 1 210 ? -3.170  -30.020 -14.513 1.00 44.17  ? 208 ASN A ND2   1 
ATOM   1571 N N     . ILE A 1 211 ? -2.188  -31.538 -10.527 1.00 38.64  ? 209 ILE A N     1 
ATOM   1572 C CA    . ILE A 1 211 ? -2.588  -32.835 -9.941  1.00 36.55  ? 209 ILE A CA    1 
ATOM   1573 C C     . ILE A 1 211 ? -3.760  -33.376 -10.766 1.00 33.88  ? 209 ILE A C     1 
ATOM   1574 O O     . ILE A 1 211 ? -4.770  -32.666 -10.877 1.00 31.34  ? 209 ILE A O     1 
ATOM   1575 C CB    . ILE A 1 211 ? -2.948  -32.632 -8.461  1.00 36.45  ? 209 ILE A CB    1 
ATOM   1576 C CG1   . ILE A 1 211 ? -1.791  -31.989 -7.683  1.00 36.48  ? 209 ILE A CG1   1 
ATOM   1577 C CG2   . ILE A 1 211 ? -3.416  -33.951 -7.841  1.00 38.26  ? 209 ILE A CG2   1 
ATOM   1578 C CD1   . ILE A 1 211 ? -2.190  -31.571 -6.289  1.00 36.68  ? 209 ILE A CD1   1 
ATOM   1579 N N     . VAL A 1 212 ? -3.626  -34.605 -11.262 1.00 30.72  ? 210 VAL A N     1 
ATOM   1580 C CA    . VAL A 1 212 ? -4.647  -35.332 -12.064 1.00 37.00  ? 210 VAL A CA    1 
ATOM   1581 C C     . VAL A 1 212 ? -5.397  -36.363 -11.192 1.00 36.04  ? 210 VAL A C     1 
ATOM   1582 O O     . VAL A 1 212 ? -4.876  -37.488 -10.981 1.00 37.76  ? 210 VAL A O     1 
ATOM   1583 C CB    . VAL A 1 212 ? -3.974  -36.020 -13.273 1.00 38.02  ? 210 VAL A CB    1 
ATOM   1584 C CG1   . VAL A 1 212 ? -5.038  -36.689 -14.146 1.00 35.67  ? 210 VAL A CG1   1 
ATOM   1585 C CG2   . VAL A 1 212 ? -3.104  -35.047 -14.075 1.00 35.19  ? 210 VAL A CG2   1 
ATOM   1586 N N     . HIS A 1 213 ? -6.617  -36.042 -10.781 1.00 36.75  ? 211 HIS A N     1 
ATOM   1587 C CA    . HIS A 1 213 ? -7.501  -36.939 -10.002 1.00 37.59  ? 211 HIS A CA    1 
ATOM   1588 C C     . HIS A 1 213 ? -8.218  -37.920 -10.934 1.00 42.53  ? 211 HIS A C     1 
ATOM   1589 O O     . HIS A 1 213 ? -8.817  -37.479 -11.917 1.00 41.81  ? 211 HIS A O     1 
ATOM   1590 C CB    . HIS A 1 213 ? -8.489  -36.131 -9.175  1.00 38.52  ? 211 HIS A CB    1 
ATOM   1591 C CG    . HIS A 1 213 ? -7.845  -35.093 -8.315  1.00 38.31  ? 211 HIS A CG    1 
ATOM   1592 N ND1   . HIS A 1 213 ? -7.022  -35.424 -7.264  1.00 36.65  ? 211 HIS A ND1   1 
ATOM   1593 C CD2   . HIS A 1 213 ? -7.933  -33.749 -8.332  1.00 35.50  ? 211 HIS A CD2   1 
ATOM   1594 C CE1   . HIS A 1 213 ? -6.633  -34.315 -6.669  1.00 42.31  ? 211 HIS A CE1   1 
ATOM   1595 N NE2   . HIS A 1 213 ? -7.166  -33.277 -7.317  1.00 38.92  ? 211 HIS A NE2   1 
ATOM   1596 N N     . ILE A 1 214 ? -8.108  -39.214 -10.634 1.00 41.64  ? 212 ILE A N     1 
ATOM   1597 C CA    . ILE A 1 214 ? -8.907  -40.310 -11.241 1.00 37.43  ? 212 ILE A CA    1 
ATOM   1598 C C     . ILE A 1 214 ? -9.964  -40.633 -10.188 1.00 35.62  ? 212 ILE A C     1 
ATOM   1599 O O     . ILE A 1 214 ? -9.571  -41.126 -9.111  1.00 38.65  ? 212 ILE A O     1 
ATOM   1600 C CB    . ILE A 1 214 ? -7.977  -41.481 -11.609 1.00 37.56  ? 212 ILE A CB    1 
ATOM   1601 C CG1   . ILE A 1 214 ? -6.784  -41.032 -12.461 1.00 44.68  ? 212 ILE A CG1   1 
ATOM   1602 C CG2   . ILE A 1 214 ? -8.728  -42.614 -12.268 1.00 36.06  ? 212 ILE A CG2   1 
ATOM   1603 C CD1   . ILE A 1 214 ? -7.156  -40.391 -13.811 1.00 50.82  ? 212 ILE A CD1   1 
ATOM   1604 N N     . VAL A 1 215 ? -11.204 -40.222 -10.448 1.00 31.70  ? 213 VAL A N     1 
ATOM   1605 C CA    . VAL A 1 215 ? -12.336 -40.144 -9.488  1.00 32.38  ? 213 VAL A CA    1 
ATOM   1606 C C     . VAL A 1 215 ? -13.400 -41.194 -9.839  1.00 39.64  ? 213 VAL A C     1 
ATOM   1607 O O     . VAL A 1 215 ? -13.823 -41.263 -11.013 1.00 38.14  ? 213 VAL A O     1 
ATOM   1608 C CB    . VAL A 1 215 ? -12.967 -38.744 -9.544  1.00 34.74  ? 213 VAL A CB    1 
ATOM   1609 C CG1   . VAL A 1 215 ? -14.087 -38.566 -8.528  1.00 35.68  ? 213 VAL A CG1   1 
ATOM   1610 C CG2   . VAL A 1 215 ? -11.936 -37.643 -9.401  1.00 34.98  ? 213 VAL A CG2   1 
ATOM   1611 N N     . LEU A 1 216 ? -13.887 -41.949 -8.850  1.00 37.61  ? 214 LEU A N     1 
ATOM   1612 C CA    . LEU A 1 216 ? -15.050 -42.852 -9.026  1.00 35.41  ? 214 LEU A CA    1 
ATOM   1613 C C     . LEU A 1 216 ? -16.314 -42.048 -8.740  1.00 34.94  ? 214 LEU A C     1 
ATOM   1614 O O     . LEU A 1 216 ? -16.407 -41.479 -7.655  1.00 35.53  ? 214 LEU A O     1 
ATOM   1615 C CB    . LEU A 1 216 ? -14.922 -44.055 -8.083  1.00 37.16  ? 214 LEU A CB    1 
ATOM   1616 C CG    . LEU A 1 216 ? -13.882 -45.106 -8.460  1.00 36.62  ? 214 LEU A CG    1 
ATOM   1617 C CD1   . LEU A 1 216 ? -13.871 -46.243 -7.454  1.00 37.09  ? 214 LEU A CD1   1 
ATOM   1618 C CD2   . LEU A 1 216 ? -14.142 -45.677 -9.847  1.00 38.98  ? 214 LEU A CD2   1 
ATOM   1619 N N     . ALA A 1 217 ? -17.228 -41.983 -9.703  1.00 36.82  ? 215 ALA A N     1 
ATOM   1620 C CA    . ALA A 1 217 ? -18.469 -41.198 -9.539  1.00 37.04  ? 215 ALA A CA    1 
ATOM   1621 C C     . ALA A 1 217 ? -19.627 -41.861 -10.289 1.00 39.29  ? 215 ALA A C     1 
ATOM   1622 O O     . ALA A 1 217 ? -19.365 -42.681 -11.171 1.00 43.52  ? 215 ALA A O     1 
ATOM   1623 C CB    . ALA A 1 217 ? -18.253 -39.781 -9.992  1.00 33.78  ? 215 ALA A CB    1 
ATOM   1624 N N     . ARG A 1 218 ? -20.857 -41.473 -9.964  1.00 41.44  ? 216 ARG A N     1 
ATOM   1625 C CA    . ARG A 1 218 ? -22.048 -42.128 -10.553 1.00 43.45  ? 216 ARG A CA    1 
ATOM   1626 C C     . ARG A 1 218 ? -22.729 -41.231 -11.582 1.00 43.50  ? 216 ARG A C     1 
ATOM   1627 O O     . ARG A 1 218 ? -22.970 -40.058 -11.269 1.00 39.86  ? 216 ARG A O     1 
ATOM   1628 C CB    . ARG A 1 218 ? -23.055 -42.459 -9.451  1.00 41.58  ? 216 ARG A CB    1 
ATOM   1629 C CG    . ARG A 1 218 ? -22.513 -43.309 -8.315  1.00 42.42  ? 216 ARG A CG    1 
ATOM   1630 C CD    . ARG A 1 218 ? -23.676 -43.794 -7.474  1.00 41.07  ? 216 ARG A CD    1 
ATOM   1631 N NE    . ARG A 1 218 ? -24.240 -45.032 -7.982  1.00 51.26  ? 216 ARG A NE    1 
ATOM   1632 C CZ    . ARG A 1 218 ? -23.814 -46.244 -7.654  1.00 56.41  ? 216 ARG A CZ    1 
ATOM   1633 N NH1   . ARG A 1 218 ? -22.814 -46.391 -6.802  1.00 60.00  ? 216 ARG A NH1   1 
ATOM   1634 N NH2   . ARG A 1 218 ? -24.391 -47.307 -8.179  1.00 59.47  ? 216 ARG A NH2   1 
ATOM   1635 N N     . LEU A 1 219 ? -23.023 -41.779 -12.758 1.00 41.91  ? 217 LEU A N     1 
ATOM   1636 C CA    . LEU A 1 219 ? -23.807 -41.025 -13.768 1.00 49.97  ? 217 LEU A CA    1 
ATOM   1637 C C     . LEU A 1 219 ? -25.265 -40.987 -13.298 1.00 50.45  ? 217 LEU A C     1 
ATOM   1638 O O     . LEU A 1 219 ? -25.658 -41.877 -12.539 1.00 47.14  ? 217 LEU A O     1 
ATOM   1639 C CB    . LEU A 1 219 ? -23.634 -41.694 -15.132 1.00 49.90  ? 217 LEU A CB    1 
ATOM   1640 C CG    . LEU A 1 219 ? -22.215 -41.639 -15.689 1.00 50.81  ? 217 LEU A CG    1 
ATOM   1641 C CD1   . LEU A 1 219 ? -22.060 -42.593 -16.857 1.00 54.24  ? 217 LEU A CD1   1 
ATOM   1642 C CD2   . LEU A 1 219 ? -21.852 -40.223 -16.101 1.00 50.34  ? 217 LEU A CD2   1 
ATOM   1643 N N     . PRO A 1 220 ? -26.081 -40.002 -13.719 1.00 57.01  ? 218 PRO A N     1 
ATOM   1644 C CA    . PRO A 1 220 ? -27.452 -39.816 -13.164 1.00 59.93  ? 218 PRO A CA    1 
ATOM   1645 C C     . PRO A 1 220 ? -28.536 -40.923 -13.125 1.00 54.64  ? 218 PRO A C     1 
ATOM   1646 O O     . PRO A 1 220 ? -29.397 -40.813 -12.284 1.00 62.07  ? 218 PRO A O     1 
ATOM   1647 C CB    . PRO A 1 220 ? -27.957 -38.644 -14.024 1.00 59.44  ? 218 PRO A CB    1 
ATOM   1648 C CG    . PRO A 1 220 ? -26.709 -37.885 -14.377 1.00 61.55  ? 218 PRO A CG    1 
ATOM   1649 C CD    . PRO A 1 220 ? -25.723 -38.983 -14.700 1.00 57.64  ? 218 PRO A CD    1 
ATOM   1650 N N     . ASP A 1 221 ? -28.492 -41.943 -13.971 1.00 49.02  ? 219 ASP A N     1 
ATOM   1651 C CA    . ASP A 1 221 ? -29.509 -43.028 -13.887 1.00 54.82  ? 219 ASP A CA    1 
ATOM   1652 C C     . ASP A 1 221 ? -28.796 -44.375 -13.899 1.00 57.37  ? 219 ASP A C     1 
ATOM   1653 O O     . ASP A 1 221 ? -29.379 -45.359 -14.402 1.00 60.42  ? 219 ASP A O     1 
ATOM   1654 C CB    . ASP A 1 221 ? -30.551 -42.951 -15.009 1.00 63.86  ? 219 ASP A CB    1 
ATOM   1655 C CG    . ASP A 1 221 ? -31.388 -41.684 -15.003 1.00 63.73  ? 219 ASP A CG    1 
ATOM   1656 O OD1   . ASP A 1 221 ? -31.917 -41.325 -13.932 1.00 66.97  ? 219 ASP A OD1   1 
ATOM   1657 O OD2   . ASP A 1 221 ? -31.496 -41.067 -16.071 1.00 74.44  ? 219 ASP A OD2   1 
ATOM   1658 N N     . ALA A 1 222 ? -27.579 -44.418 -13.362 1.00 50.53  ? 220 ALA A N     1 
ATOM   1659 C CA    . ALA A 1 222 ? -26.745 -45.627 -13.387 1.00 41.44  ? 220 ALA A CA    1 
ATOM   1660 C C     . ALA A 1 222 ? -27.414 -46.648 -12.476 1.00 42.26  ? 220 ALA A C     1 
ATOM   1661 O O     . ALA A 1 222 ? -28.143 -46.268 -11.559 1.00 40.78  ? 220 ALA A O     1 
ATOM   1662 C CB    . ALA A 1 222 ? -25.351 -45.237 -12.974 1.00 46.24  ? 220 ALA A CB    1 
ATOM   1663 N N     . PRO A 1 223 ? -27.151 -47.952 -12.718 1.00 42.42  ? 221 PRO A N     1 
ATOM   1664 C CA    . PRO A 1 223 ? -27.677 -48.989 -11.867 1.00 44.79  ? 221 PRO A CA    1 
ATOM   1665 C C     . PRO A 1 223 ? -27.072 -48.883 -10.468 1.00 53.12  ? 221 PRO A C     1 
ATOM   1666 O O     . PRO A 1 223 ? -26.097 -48.189 -10.293 1.00 52.16  ? 221 PRO A O     1 
ATOM   1667 C CB    . PRO A 1 223 ? -27.173 -50.277 -12.516 1.00 49.26  ? 221 PRO A CB    1 
ATOM   1668 C CG    . PRO A 1 223 ? -25.971 -49.873 -13.304 1.00 47.97  ? 221 PRO A CG    1 
ATOM   1669 C CD    . PRO A 1 223 ? -26.349 -48.509 -13.820 1.00 49.27  ? 221 PRO A CD    1 
ATOM   1670 N N     . GLN A 1 224 ? -27.673 -49.585 -9.515  1.00 57.37  ? 222 GLN A N     1 
ATOM   1671 C CA    . GLN A 1 224 ? -27.198 -49.531 -8.117  1.00 55.65  ? 222 GLN A CA    1 
ATOM   1672 C C     . GLN A 1 224 ? -25.964 -50.408 -7.954  1.00 46.80  ? 222 GLN A C     1 
ATOM   1673 O O     . GLN A 1 224 ? -25.812 -51.367 -8.715  1.00 45.58  ? 222 GLN A O     1 
ATOM   1674 C CB    . GLN A 1 224 ? -28.306 -49.995 -7.178  1.00 64.28  ? 222 GLN A CB    1 
ATOM   1675 C CG    . GLN A 1 224 ? -29.353 -48.930 -6.895  1.00 73.92  ? 222 GLN A CG    1 
ATOM   1676 C CD    . GLN A 1 224 ? -29.759 -48.899 -5.441  1.00 84.42  ? 222 GLN A CD    1 
ATOM   1677 O OE1   . GLN A 1 224 ? -30.148 -49.911 -4.861  1.00 77.89  ? 222 GLN A OE1   1 
ATOM   1678 N NE2   . GLN A 1 224 ? -29.668 -47.725 -4.838  1.00 91.57  ? 222 GLN A NE2   1 
ATOM   1679 N N     . GLY A 1 225 ? -25.115 -50.057 -6.998  1.00 44.39  ? 223 GLY A N     1 
ATOM   1680 C CA    . GLY A 1 225 ? -23.938 -50.886 -6.701  1.00 37.82  ? 223 GLY A CA    1 
ATOM   1681 C C     . GLY A 1 225 ? -22.741 -50.597 -7.571  1.00 35.09  ? 223 GLY A C     1 
ATOM   1682 O O     . GLY A 1 225 ? -22.678 -49.511 -8.151  1.00 31.97  ? 223 GLY A O     1 
ATOM   1683 N N     . THR A 1 226 ? -21.839 -51.566 -7.655  1.00 35.39  ? 224 THR A N     1 
ATOM   1684 C CA    . THR A 1 226 ? -20.585 -51.402 -8.421  1.00 38.44  ? 224 THR A CA    1 
ATOM   1685 C C     . THR A 1 226 ? -20.919 -51.310 -9.919  1.00 38.26  ? 224 THR A C     1 
ATOM   1686 O O     . THR A 1 226 ? -20.176 -50.625 -10.631 1.00 40.74  ? 224 THR A O     1 
ATOM   1687 C CB    . THR A 1 226 ? -19.613 -52.499 -7.990  1.00 36.55  ? 224 THR A CB    1 
ATOM   1688 O OG1   . THR A 1 226 ? -20.337 -53.689 -8.257  1.00 39.93  ? 224 THR A OG1   1 
ATOM   1689 C CG2   . THR A 1 226 ? -19.235 -52.439 -6.522  1.00 34.23  ? 224 THR A CG2   1 
ATOM   1690 N N     . LYS A 1 227 ? -22.044 -51.875 -10.361 1.00 41.71  ? 225 LYS A N     1 
ATOM   1691 C CA    . LYS A 1 227 ? -22.519 -51.799 -11.782 1.00 46.20  ? 225 LYS A CA    1 
ATOM   1692 C C     . LYS A 1 227 ? -22.810 -50.352 -12.191 1.00 44.43  ? 225 LYS A C     1 
ATOM   1693 O O     . LYS A 1 227 ? -23.016 -50.148 -13.393 1.00 46.62  ? 225 LYS A O     1 
ATOM   1694 C CB    . LYS A 1 227 ? -23.778 -52.648 -11.999 1.00 47.19  ? 225 LYS A CB    1 
ATOM   1695 C CG    . LYS A 1 227 ? -23.497 -54.106 -12.332 1.00 51.58  ? 225 LYS A CG    1 
ATOM   1696 C CD    . LYS A 1 227 ? -24.266 -55.105 -11.480 1.00 61.72  ? 225 LYS A CD    1 
ATOM   1697 C CE    . LYS A 1 227 ? -23.495 -56.398 -11.272 1.00 68.98  ? 225 LYS A CE    1 
ATOM   1698 N NZ    . LYS A 1 227 ? -22.915 -56.894 -12.546 1.00 72.86  ? 225 LYS A NZ    1 
ATOM   1699 N N     . GLY A 1 228 ? -22.828 -49.404 -11.255 1.00 41.41  ? 226 GLY A N     1 
ATOM   1700 C CA    . GLY A 1 228 ? -23.194 -48.013 -11.585 1.00 42.63  ? 226 GLY A CA    1 
ATOM   1701 C C     . GLY A 1 228 ? -22.068 -47.023 -11.374 1.00 40.03  ? 226 GLY A C     1 
ATOM   1702 O O     . GLY A 1 228 ? -22.355 -45.828 -11.254 1.00 40.99  ? 226 GLY A O     1 
ATOM   1703 N N     . ILE A 1 229 ? -20.830 -47.502 -11.349 1.00 38.83  ? 227 ILE A N     1 
ATOM   1704 C CA    . ILE A 1 229 ? -19.676 -46.608 -11.058 1.00 39.80  ? 227 ILE A CA    1 
ATOM   1705 C C     . ILE A 1 229 ? -18.896 -46.330 -12.340 1.00 38.32  ? 227 ILE A C     1 
ATOM   1706 O O     . ILE A 1 229 ? -18.565 -47.280 -13.045 1.00 38.75  ? 227 ILE A O     1 
ATOM   1707 C CB    . ILE A 1 229 ? -18.775 -47.207 -9.964  1.00 43.79  ? 227 ILE A CB    1 
ATOM   1708 C CG1   . ILE A 1 229 ? -19.509 -47.336 -8.628  1.00 48.32  ? 227 ILE A CG1   1 
ATOM   1709 C CG2   . ILE A 1 229 ? -17.489 -46.412 -9.829  1.00 49.52  ? 227 ILE A CG2   1 
ATOM   1710 C CD1   . ILE A 1 229 ? -18.919 -48.380 -7.715  1.00 52.81  ? 227 ILE A CD1   1 
ATOM   1711 N N     . SER A 1 230 ? -18.628 -45.061 -12.606 1.00 39.35  ? 228 SER A N     1 
ATOM   1712 C CA    . SER A 1 230 ? -17.838 -44.647 -13.781 1.00 43.30  ? 228 SER A CA    1 
ATOM   1713 C C     . SER A 1 230 ? -16.594 -43.904 -13.275 1.00 43.97  ? 228 SER A C     1 
ATOM   1714 O O     . SER A 1 230 ? -16.576 -43.454 -12.108 1.00 38.15  ? 228 SER A O     1 
ATOM   1715 C CB    . SER A 1 230 ? -18.693 -43.806 -14.712 1.00 46.95  ? 228 SER A CB    1 
ATOM   1716 O OG    . SER A 1 230 ? -19.957 -44.425 -14.977 1.00 45.71  ? 228 SER A OG    1 
ATOM   1717 N N     . LEU A 1 231 ? -15.605 -43.765 -14.150 1.00 41.90  ? 229 LEU A N     1 
ATOM   1718 C CA    . LEU A 1 231 ? -14.257 -43.271 -13.824 1.00 37.69  ? 229 LEU A CA    1 
ATOM   1719 C C     . LEU A 1 231 ? -14.008 -41.990 -14.626 1.00 40.77  ? 229 LEU A C     1 
ATOM   1720 O O     . LEU A 1 231 ? -14.318 -41.989 -15.849 1.00 44.55  ? 229 LEU A O     1 
ATOM   1721 C CB    . LEU A 1 231 ? -13.310 -44.414 -14.176 1.00 37.85  ? 229 LEU A CB    1 
ATOM   1722 C CG    . LEU A 1 231 ? -11.901 -44.307 -13.614 1.00 41.15  ? 229 LEU A CG    1 
ATOM   1723 C CD1   . LEU A 1 231 ? -11.916 -44.472 -12.098 1.00 39.73  ? 229 LEU A CD1   1 
ATOM   1724 C CD2   . LEU A 1 231 ? -10.987 -45.343 -14.269 1.00 40.65  ? 229 LEU A CD2   1 
ATOM   1725 N N     . PHE A 1 232 ? -13.520 -40.940 -13.956 1.00 34.62  ? 230 PHE A N     1 
ATOM   1726 C CA    . PHE A 1 232 ? -13.405 -39.548 -14.460 1.00 36.26  ? 230 PHE A CA    1 
ATOM   1727 C C     . PHE A 1 232 ? -12.014 -38.986 -14.150 1.00 39.52  ? 230 PHE A C     1 
ATOM   1728 O O     . PHE A 1 232 ? -11.526 -39.102 -13.010 1.00 41.64  ? 230 PHE A O     1 
ATOM   1729 C CB    . PHE A 1 232 ? -14.462 -38.642 -13.837 1.00 37.09  ? 230 PHE A CB    1 
ATOM   1730 C CG    . PHE A 1 232 ? -15.850 -39.115 -14.131 1.00 42.21  ? 230 PHE A CG    1 
ATOM   1731 C CD1   . PHE A 1 232 ? -16.495 -38.721 -15.294 1.00 45.29  ? 230 PHE A CD1   1 
ATOM   1732 C CD2   . PHE A 1 232 ? -16.457 -40.052 -13.317 1.00 45.58  ? 230 PHE A CD2   1 
ATOM   1733 C CE1   . PHE A 1 232 ? -17.758 -39.208 -15.596 1.00 45.98  ? 230 PHE A CE1   1 
ATOM   1734 C CE2   . PHE A 1 232 ? -17.714 -40.550 -13.628 1.00 50.07  ? 230 PHE A CE2   1 
ATOM   1735 C CZ    . PHE A 1 232 ? -18.369 -40.120 -14.764 1.00 49.95  ? 230 PHE A CZ    1 
ATOM   1736 N N     . ILE A 1 233 ? -11.409 -38.356 -15.151 1.00 38.12  ? 231 ILE A N     1 
ATOM   1737 C CA    . ILE A 1 233 ? -10.211 -37.498 -15.013 1.00 35.56  ? 231 ILE A CA    1 
ATOM   1738 C C     . ILE A 1 233 ? -10.701 -36.136 -14.539 1.00 38.15  ? 231 ILE A C     1 
ATOM   1739 O O     . ILE A 1 233 ? -11.520 -35.566 -15.227 1.00 37.70  ? 231 ILE A O     1 
ATOM   1740 C CB    . ILE A 1 233 ? -9.447  -37.405 -16.332 1.00 37.94  ? 231 ILE A CB    1 
ATOM   1741 C CG1   . ILE A 1 233 ? -9.219  -38.784 -16.951 1.00 39.99  ? 231 ILE A CG1   1 
ATOM   1742 C CG2   . ILE A 1 233 ? -8.138  -36.657 -16.108 1.00 41.94  ? 231 ILE A CG2   1 
ATOM   1743 C CD1   . ILE A 1 233 ? -8.755  -38.751 -18.396 1.00 42.16  ? 231 ILE A CD1   1 
ATOM   1744 N N     . VAL A 1 234 ? -10.262 -35.669 -13.370 1.00 39.65  ? 232 VAL A N     1 
ATOM   1745 C CA    . VAL A 1 234 ? -10.615 -34.315 -12.843 1.00 39.00  ? 232 VAL A CA    1 
ATOM   1746 C C     . VAL A 1 234 ? -9.322  -33.628 -12.437 1.00 40.12  ? 232 VAL A C     1 
ATOM   1747 O O     . VAL A 1 234 ? -8.761  -33.932 -11.397 1.00 44.02  ? 232 VAL A O     1 
ATOM   1748 C CB    . VAL A 1 234 ? -11.627 -34.414 -11.694 1.00 35.37  ? 232 VAL A CB    1 
ATOM   1749 C CG1   . VAL A 1 234 ? -12.103 -33.049 -11.222 1.00 37.89  ? 232 VAL A CG1   1 
ATOM   1750 C CG2   . VAL A 1 234 ? -12.800 -35.281 -12.086 1.00 36.33  ? 232 VAL A CG2   1 
ATOM   1751 N N     . PRO A 1 235 ? -8.720  -32.799 -13.309 1.00 43.53  ? 233 PRO A N     1 
ATOM   1752 C CA    . PRO A 1 235 ? -7.478  -32.115 -12.961 1.00 40.87  ? 233 PRO A CA    1 
ATOM   1753 C C     . PRO A 1 235 ? -7.755  -30.890 -12.097 1.00 34.35  ? 233 PRO A C     1 
ATOM   1754 O O     . PRO A 1 235 ? -8.819  -30.360 -12.126 1.00 33.09  ? 233 PRO A O     1 
ATOM   1755 C CB    . PRO A 1 235 ? -6.864  -31.734 -14.306 1.00 42.88  ? 233 PRO A CB    1 
ATOM   1756 C CG    . PRO A 1 235 ? -8.062  -31.630 -15.232 1.00 44.22  ? 233 PRO A CG    1 
ATOM   1757 C CD    . PRO A 1 235 ? -9.121  -32.571 -14.704 1.00 43.53  ? 233 PRO A CD    1 
ATOM   1758 N N     . LYS A 1 236 ? -6.756  -30.510 -11.324 1.00 36.80  ? 234 LYS A N     1 
ATOM   1759 C CA    . LYS A 1 236 ? -6.830  -29.363 -10.392 1.00 40.18  ? 234 LYS A CA    1 
ATOM   1760 C C     . LYS A 1 236 ? -6.899  -28.109 -11.268 1.00 39.10  ? 234 LYS A C     1 
ATOM   1761 O O     . LYS A 1 236 ? -7.815  -27.305 -11.023 1.00 48.27  ? 234 LYS A O     1 
ATOM   1762 C CB    . LYS A 1 236 ? -5.637  -29.429 -9.425  1.00 41.02  ? 234 LYS A CB    1 
ATOM   1763 C CG    . LYS A 1 236 ? -5.529  -28.314 -8.399  1.00 40.64  ? 234 LYS A CG    1 
ATOM   1764 C CD    . LYS A 1 236 ? -4.167  -28.278 -7.735  1.00 43.45  ? 234 LYS A CD    1 
ATOM   1765 C CE    . LYS A 1 236 ? -3.915  -27.053 -6.877  1.00 46.97  ? 234 LYS A CE    1 
ATOM   1766 N NZ    . LYS A 1 236 ? -2.475  -26.962 -6.517  1.00 48.38  ? 234 LYS A NZ    1 
ATOM   1767 N N     . PHE A 1 237 ? -5.959  -27.986 -12.217 1.00 37.62  ? 235 PHE A N     1 
ATOM   1768 C CA    . PHE A 1 237 ? -5.872  -26.973 -13.305 1.00 40.99  ? 235 PHE A CA    1 
ATOM   1769 C C     . PHE A 1 237 ? -6.249  -27.663 -14.623 1.00 40.49  ? 235 PHE A C     1 
ATOM   1770 O O     . PHE A 1 237 ? -5.513  -28.552 -15.094 1.00 37.46  ? 235 PHE A O     1 
ATOM   1771 C CB    . PHE A 1 237 ? -4.463  -26.353 -13.384 1.00 42.87  ? 235 PHE A CB    1 
ATOM   1772 C CG    . PHE A 1 237 ? -4.021  -25.676 -12.113 1.00 47.35  ? 235 PHE A CG    1 
ATOM   1773 C CD1   . PHE A 1 237 ? -4.626  -24.500 -11.689 1.00 49.31  ? 235 PHE A CD1   1 
ATOM   1774 C CD2   . PHE A 1 237 ? -3.061  -26.251 -11.295 1.00 50.19  ? 235 PHE A CD2   1 
ATOM   1775 C CE1   . PHE A 1 237 ? -4.274  -23.914 -10.481 1.00 47.26  ? 235 PHE A CE1   1 
ATOM   1776 C CE2   . PHE A 1 237 ? -2.689  -25.653 -10.102 1.00 47.92  ? 235 PHE A CE2   1 
ATOM   1777 C CZ    . PHE A 1 237 ? -3.303  -24.490 -9.694  1.00 47.16  ? 235 PHE A CZ    1 
ATOM   1778 N N     . LEU A 1 238 ? -7.391  -27.284 -15.196 1.00 45.56  ? 236 LEU A N     1 
ATOM   1779 C CA    . LEU A 1 238 ? -7.807  -27.631 -16.583 1.00 42.69  ? 236 LEU A CA    1 
ATOM   1780 C C     . LEU A 1 238 ? -6.704  -27.276 -17.566 1.00 43.10  ? 236 LEU A C     1 
ATOM   1781 O O     . LEU A 1 238 ? -6.172  -26.184 -17.495 1.00 45.04  ? 236 LEU A O     1 
ATOM   1782 C CB    . LEU A 1 238 ? -9.058  -26.822 -16.909 1.00 43.74  ? 236 LEU A CB    1 
ATOM   1783 C CG    . LEU A 1 238 ? -10.318 -27.287 -16.192 1.00 47.48  ? 236 LEU A CG    1 
ATOM   1784 C CD1   . LEU A 1 238 ? -11.480 -26.347 -16.489 1.00 48.01  ? 236 LEU A CD1   1 
ATOM   1785 C CD2   . LEU A 1 238 ? -10.647 -28.726 -16.585 1.00 49.25  ? 236 LEU A CD2   1 
ATOM   1786 N N     . PRO A 1 239 ? -6.331  -28.166 -18.507 1.00 47.60  ? 237 PRO A N     1 
ATOM   1787 C CA    . PRO A 1 239 ? -5.330  -27.844 -19.516 1.00 49.52  ? 237 PRO A CA    1 
ATOM   1788 C C     . PRO A 1 239 ? -5.711  -26.574 -20.289 1.00 52.62  ? 237 PRO A C     1 
ATOM   1789 O O     . PRO A 1 239 ? -6.884  -26.385 -20.466 1.00 56.04  ? 237 PRO A O     1 
ATOM   1790 C CB    . PRO A 1 239 ? -5.363  -29.048 -20.479 1.00 51.37  ? 237 PRO A CB    1 
ATOM   1791 C CG    . PRO A 1 239 ? -5.952  -30.186 -19.694 1.00 50.28  ? 237 PRO A CG    1 
ATOM   1792 C CD    . PRO A 1 239 ? -6.838  -29.543 -18.641 1.00 54.18  ? 237 PRO A CD    1 
ATOM   1793 N N     . ASN A 1 240 ? -4.730  -25.764 -20.716 1.00 59.95  ? 238 ASN A N     1 
ATOM   1794 C CA    . ASN A 1 240 ? -4.910  -24.651 -21.699 1.00 55.42  ? 238 ASN A CA    1 
ATOM   1795 C C     . ASN A 1 240 ? -4.556  -25.178 -23.095 1.00 59.19  ? 238 ASN A C     1 
ATOM   1796 O O     . ASN A 1 240 ? -4.242  -26.381 -23.227 1.00 60.25  ? 238 ASN A O     1 
ATOM   1797 C CB    . ASN A 1 240 ? -4.156  -23.368 -21.306 1.00 50.88  ? 238 ASN A CB    1 
ATOM   1798 C CG    . ASN A 1 240 ? -2.640  -23.471 -21.264 1.00 47.47  ? 238 ASN A CG    1 
ATOM   1799 O OD1   . ASN A 1 240 ? -2.021  -24.232 -22.003 1.00 47.90  ? 238 ASN A OD1   1 
ATOM   1800 N ND2   . ASN A 1 240 ? -2.016  -22.681 -20.403 1.00 47.28  ? 238 ASN A ND2   1 
ATOM   1801 N N     . ALA A 1 241 ? -4.611  -24.305 -24.103 1.00 71.51  ? 239 ALA A N     1 
ATOM   1802 C CA    . ALA A 1 241 ? -4.407  -24.633 -25.536 1.00 63.37  ? 239 ALA A CA    1 
ATOM   1803 C C     . ALA A 1 241 ? -3.043  -25.314 -25.750 1.00 59.22  ? 239 ALA A C     1 
ATOM   1804 O O     . ALA A 1 241 ? -2.977  -26.273 -26.543 1.00 62.96  ? 239 ALA A O     1 
ATOM   1805 C CB    . ALA A 1 241 ? -4.550  -23.370 -26.348 1.00 60.58  ? 239 ALA A CB    1 
ATOM   1806 N N     . GLU A 1 242 ? -1.992  -24.864 -25.059 1.00 58.60  ? 240 GLU A N     1 
ATOM   1807 C CA    . GLU A 1 242 ? -0.624  -25.458 -25.151 1.00 64.21  ? 240 GLU A CA    1 
ATOM   1808 C C     . GLU A 1 242 ? -0.567  -26.865 -24.512 1.00 66.99  ? 240 GLU A C     1 
ATOM   1809 O O     . GLU A 1 242 ? 0.362   -27.614 -24.875 1.00 61.64  ? 240 GLU A O     1 
ATOM   1810 C CB    . GLU A 1 242 ? 0.421   -24.564 -24.475 1.00 66.37  ? 240 GLU A CB    1 
ATOM   1811 C CG    . GLU A 1 242 ? 0.852   -23.368 -25.301 1.00 67.55  ? 240 GLU A CG    1 
ATOM   1812 C CD    . GLU A 1 242 ? -0.136  -22.208 -25.303 1.00 78.20  ? 240 GLU A CD    1 
ATOM   1813 O OE1   . GLU A 1 242 ? 0.078   -21.261 -26.089 1.00 83.05  ? 240 GLU A OE1   1 
ATOM   1814 O OE2   . GLU A 1 242 ? -1.123  -22.246 -24.522 1.00 80.03  ? 240 GLU A OE2   1 
ATOM   1815 N N     . GLY A 1 243 ? -1.478  -27.209 -23.586 1.00 61.32  ? 241 GLY A N     1 
ATOM   1816 C CA    . GLY A 1 243 ? -1.472  -28.490 -22.849 1.00 60.83  ? 241 GLY A CA    1 
ATOM   1817 C C     . GLY A 1 243 ? -0.879  -28.359 -21.454 1.00 59.70  ? 241 GLY A C     1 
ATOM   1818 O O     . GLY A 1 243 ? -0.483  -29.384 -20.887 1.00 58.10  ? 241 GLY A O     1 
ATOM   1819 N N     . ASN A 1 244 ? -0.848  -27.138 -20.922 1.00 56.96  ? 242 ASN A N     1 
ATOM   1820 C CA    . ASN A 1 244 ? -0.200  -26.760 -19.643 1.00 55.49  ? 242 ASN A CA    1 
ATOM   1821 C C     . ASN A 1 244 ? -1.274  -26.345 -18.638 1.00 55.23  ? 242 ASN A C     1 
ATOM   1822 O O     . ASN A 1 244 ? -2.431  -26.173 -19.038 1.00 51.59  ? 242 ASN A O     1 
ATOM   1823 C CB    . ASN A 1 244 ? 0.791   -25.615 -19.841 1.00 53.65  ? 242 ASN A CB    1 
ATOM   1824 C CG    . ASN A 1 244 ? 1.975   -25.994 -20.711 1.00 56.10  ? 242 ASN A CG    1 
ATOM   1825 O OD1   . ASN A 1 244 ? 2.308   -27.163 -20.865 1.00 52.62  ? 242 ASN A OD1   1 
ATOM   1826 N ND2   . ASN A 1 244 ? 2.619   -25.006 -21.304 1.00 55.36  ? 242 ASN A ND2   1 
ATOM   1827 N N     . ALA A 1 245 ? -0.883  -26.183 -17.377 1.00 52.39  ? 243 ALA A N     1 
ATOM   1828 C CA    . ALA A 1 245 ? -1.781  -25.793 -16.277 1.00 51.71  ? 243 ALA A CA    1 
ATOM   1829 C C     . ALA A 1 245 ? -2.427  -24.448 -16.606 1.00 53.25  ? 243 ALA A C     1 
ATOM   1830 O O     . ALA A 1 245 ? -1.686  -23.440 -16.639 1.00 48.92  ? 243 ALA A O     1 
ATOM   1831 C CB    . ALA A 1 245 ? -1.003  -25.737 -14.996 1.00 58.20  ? 243 ALA A CB    1 
ATOM   1832 N N     . GLY A 1 246 ? -3.749  -24.462 -16.835 1.00 52.89  ? 244 GLY A N     1 
ATOM   1833 C CA    . GLY A 1 246 ? -4.594  -23.292 -17.144 1.00 47.69  ? 244 GLY A CA    1 
ATOM   1834 C C     . GLY A 1 246 ? -5.544  -22.952 -16.011 1.00 44.00  ? 244 GLY A C     1 
ATOM   1835 O O     . GLY A 1 246 ? -5.073  -22.747 -14.893 1.00 49.29  ? 244 GLY A O     1 
ATOM   1836 N N     . GLU A 1 247 ? -6.833  -22.840 -16.324 1.00 46.98  ? 245 GLU A N     1 
ATOM   1837 C CA    . GLU A 1 247 ? -7.941  -22.472 -15.412 1.00 52.52  ? 245 GLU A CA    1 
ATOM   1838 C C     . GLU A 1 247 ? -7.926  -23.364 -14.177 1.00 54.86  ? 245 GLU A C     1 
ATOM   1839 O O     . GLU A 1 247 ? -7.873  -24.588 -14.338 1.00 65.62  ? 245 GLU A O     1 
ATOM   1840 C CB    . GLU A 1 247 ? -9.296  -22.685 -16.096 1.00 65.79  ? 245 GLU A CB    1 
ATOM   1841 C CG    . GLU A 1 247 ? -9.714  -21.552 -17.006 1.00 77.67  ? 245 GLU A CG    1 
ATOM   1842 C CD    . GLU A 1 247 ? -9.678  -20.204 -16.306 1.00 90.89  ? 245 GLU A CD    1 
ATOM   1843 O OE1   . GLU A 1 247 ? -8.688  -19.446 -16.516 1.00 88.06  ? 245 GLU A OE1   1 
ATOM   1844 O OE2   . GLU A 1 247 ? -10.619 -19.929 -15.523 1.00 93.10  ? 245 GLU A OE2   1 
ATOM   1845 N N     . ARG A 1 248 ? -8.038  -22.774 -12.994 1.00 52.81  ? 246 ARG A N     1 
ATOM   1846 C CA    . ARG A 1 248 ? -8.237  -23.523 -11.733 1.00 45.60  ? 246 ARG A CA    1 
ATOM   1847 C C     . ARG A 1 248 ? -9.607  -24.220 -11.809 1.00 43.37  ? 246 ARG A C     1 
ATOM   1848 O O     . ARG A 1 248 ? -10.607 -23.513 -11.781 1.00 43.97  ? 246 ARG A O     1 
ATOM   1849 C CB    . ARG A 1 248 ? -8.102  -22.565 -10.538 1.00 42.61  ? 246 ARG A CB    1 
ATOM   1850 C CG    . ARG A 1 248 ? -8.488  -23.155 -9.184  1.00 41.51  ? 246 ARG A CG    1 
ATOM   1851 C CD    . ARG A 1 248 ? -7.704  -24.436 -8.946  1.00 46.84  ? 246 ARG A CD    1 
ATOM   1852 N NE    . ARG A 1 248 ? -7.941  -25.067 -7.661  1.00 48.99  ? 246 ARG A NE    1 
ATOM   1853 C CZ    . ARG A 1 248 ? -7.314  -24.757 -6.529  1.00 50.63  ? 246 ARG A CZ    1 
ATOM   1854 N NH1   . ARG A 1 248 ? -6.395  -23.802 -6.501  1.00 47.85  ? 246 ARG A NH1   1 
ATOM   1855 N NH2   . ARG A 1 248 ? -7.624  -25.409 -5.423  1.00 48.72  ? 246 ARG A NH2   1 
ATOM   1856 N N     . ASN A 1 249 ? -9.644  -25.558 -11.871 1.00 41.44  ? 247 ASN A N     1 
ATOM   1857 C CA    . ASN A 1 249 ? -10.870 -26.413 -11.734 1.00 43.11  ? 247 ASN A CA    1 
ATOM   1858 C C     . ASN A 1 249 ? -11.488 -26.176 -10.335 1.00 40.25  ? 247 ASN A C     1 
ATOM   1859 O O     . ASN A 1 249 ? -10.795 -25.634 -9.491  1.00 39.42  ? 247 ASN A O     1 
ATOM   1860 C CB    . ASN A 1 249 ? -10.508 -27.886 -12.017 1.00 42.28  ? 247 ASN A CB    1 
ATOM   1861 C CG    . ASN A 1 249 ? -11.649 -28.712 -12.572 1.00 43.73  ? 247 ASN A CG    1 
ATOM   1862 O OD1   . ASN A 1 249 ? -12.750 -28.211 -12.741 1.00 42.74  ? 247 ASN A OD1   1 
ATOM   1863 N ND2   . ASN A 1 249 ? -11.407 -29.978 -12.863 1.00 46.07  ? 247 ASN A ND2   1 
ATOM   1864 N N     . ALA A 1 250 ? -12.731 -26.586 -10.060 1.00 43.68  ? 248 ALA A N     1 
ATOM   1865 C CA    . ALA A 1 250 ? -13.387 -26.439 -8.727  1.00 40.44  ? 248 ALA A CA    1 
ATOM   1866 C C     . ALA A 1 250 ? -13.078 -27.658 -7.818  1.00 40.83  ? 248 ALA A C     1 
ATOM   1867 O O     . ALA A 1 250 ? -14.035 -28.326 -7.287  1.00 37.03  ? 248 ALA A O     1 
ATOM   1868 C CB    . ALA A 1 250 ? -14.865 -26.237 -8.923  1.00 38.33  ? 248 ALA A CB    1 
ATOM   1869 N N     . VAL A 1 251 ? -11.777 -27.937 -7.655  1.00 42.22  ? 249 VAL A N     1 
ATOM   1870 C CA    . VAL A 1 251 ? -11.161 -29.031 -6.842  1.00 45.79  ? 249 VAL A CA    1 
ATOM   1871 C C     . VAL A 1 251 ? -10.422 -28.373 -5.670  1.00 41.57  ? 249 VAL A C     1 
ATOM   1872 O O     . VAL A 1 251 ? -9.439  -27.672 -5.937  1.00 46.01  ? 249 VAL A O     1 
ATOM   1873 C CB    . VAL A 1 251 ? -10.185 -29.872 -7.691  1.00 49.00  ? 249 VAL A CB    1 
ATOM   1874 C CG1   . VAL A 1 251 ? -9.543  -31.002 -6.899  1.00 50.95  ? 249 VAL A CG1   1 
ATOM   1875 C CG2   . VAL A 1 251 ? -10.847 -30.448 -8.926  1.00 52.13  ? 249 VAL A CG2   1 
ATOM   1876 N N     . SER A 1 252 ? -10.871 -28.572 -4.430  1.00 37.76  ? 250 SER A N     1 
ATOM   1877 C CA    . SER A 1 252 ? -10.166 -28.032 -3.232  1.00 38.91  ? 250 SER A CA    1 
ATOM   1878 C C     . SER A 1 252 ? -10.122 -29.042 -2.075  1.00 36.51  ? 250 SER A C     1 
ATOM   1879 O O     . SER A 1 252 ? -11.037 -29.904 -1.921  1.00 36.80  ? 250 SER A O     1 
ATOM   1880 C CB    . SER A 1 252 ? -10.748 -26.727 -2.783  1.00 35.79  ? 250 SER A CB    1 
ATOM   1881 O OG    . SER A 1 252 ? -12.001 -26.947 -2.165  1.00 35.84  ? 250 SER A OG    1 
ATOM   1882 N N     . CYS A 1 253 ? -9.058  -28.909 -1.292  1.00 38.21  ? 251 CYS A N     1 
ATOM   1883 C CA    . CYS A 1 253 ? -8.756  -29.692 -0.075  1.00 38.10  ? 251 CYS A CA    1 
ATOM   1884 C C     . CYS A 1 253 ? -9.319  -28.951 1.147   1.00 37.70  ? 251 CYS A C     1 
ATOM   1885 O O     . CYS A 1 253 ? -8.714  -27.959 1.537   1.00 38.48  ? 251 CYS A O     1 
ATOM   1886 C CB    . CYS A 1 253 ? -7.253  -29.941 0.054   1.00 36.98  ? 251 CYS A CB    1 
ATOM   1887 S SG    . CYS A 1 253 ? -6.846  -30.923 1.528   1.00 39.13  ? 251 CYS A SG    1 
ATOM   1888 N N     . GLY A 1 254 ? -10.419 -29.439 1.733   1.00 37.44  ? 252 GLY A N     1 
ATOM   1889 C CA    . GLY A 1 254 ? -11.046 -28.880 2.941   1.00 34.78  ? 252 GLY A CA    1 
ATOM   1890 C C     . GLY A 1 254 ? -10.275 -29.200 4.221   1.00 38.85  ? 252 GLY A C     1 
ATOM   1891 O O     . GLY A 1 254 ? -10.449 -28.462 5.187   1.00 36.63  ? 252 GLY A O     1 
ATOM   1892 N N     . SER A 1 255 ? -9.464  -30.264 4.261   1.00 38.13  ? 253 SER A N     1 
ATOM   1893 C CA    . SER A 1 255 ? -8.582  -30.580 5.420   1.00 36.00  ? 253 SER A CA    1 
ATOM   1894 C C     . SER A 1 255 ? -7.641  -31.732 5.106   1.00 40.82  ? 253 SER A C     1 
ATOM   1895 O O     . SER A 1 255 ? -7.862  -32.445 4.117   1.00 43.87  ? 253 SER A O     1 
ATOM   1896 C CB    . SER A 1 255 ? -9.350  -30.919 6.642   1.00 34.71  ? 253 SER A CB    1 
ATOM   1897 O OG    . SER A 1 255 ? -10.162 -32.054 6.432   1.00 36.68  ? 253 SER A OG    1 
ATOM   1898 N N     . ILE A 1 256 ? -6.634  -31.892 5.960   1.00 42.80  ? 254 ILE A N     1 
ATOM   1899 C CA    . ILE A 1 256 ? -5.792  -33.115 6.052   1.00 37.69  ? 254 ILE A CA    1 
ATOM   1900 C C     . ILE A 1 256 ? -5.979  -33.773 7.427   1.00 40.31  ? 254 ILE A C     1 
ATOM   1901 O O     . ILE A 1 256 ? -6.268  -33.072 8.411   1.00 37.32  ? 254 ILE A O     1 
ATOM   1902 C CB    . ILE A 1 256 ? -4.327  -32.776 5.747   1.00 38.22  ? 254 ILE A CB    1 
ATOM   1903 C CG1   . ILE A 1 256 ? -3.717  -31.846 6.795   1.00 33.89  ? 254 ILE A CG1   1 
ATOM   1904 C CG2   . ILE A 1 256 ? -4.222  -32.221 4.331   1.00 41.89  ? 254 ILE A CG2   1 
ATOM   1905 C CD1   . ILE A 1 256 ? -2.273  -31.660 6.595   1.00 34.57  ? 254 ILE A CD1   1 
ATOM   1906 N N     . GLU A 1 257 ? -5.801  -35.095 7.487   1.00 39.36  ? 255 GLU A N     1 
ATOM   1907 C CA    . GLU A 1 257 ? -5.992  -35.886 8.718   1.00 36.48  ? 255 GLU A CA    1 
ATOM   1908 C C     . GLU A 1 257 ? -4.734  -35.731 9.575   1.00 33.17  ? 255 GLU A C     1 
ATOM   1909 O O     . GLU A 1 257 ? -3.613  -35.563 9.008   1.00 33.95  ? 255 GLU A O     1 
ATOM   1910 C CB    . GLU A 1 257 ? -6.229  -37.375 8.423   1.00 38.49  ? 255 GLU A CB    1 
ATOM   1911 C CG    . GLU A 1 257 ? -7.324  -37.668 7.428   1.00 39.47  ? 255 GLU A CG    1 
ATOM   1912 C CD    . GLU A 1 257 ? -8.712  -37.300 7.881   1.00 42.07  ? 255 GLU A CD    1 
ATOM   1913 O OE1   . GLU A 1 257 ? -9.500  -36.848 7.014   1.00 42.53  ? 255 GLU A OE1   1 
ATOM   1914 O OE2   . GLU A 1 257 ? -9.003  -37.456 9.093   1.00 43.34  ? 255 GLU A OE2   1 
ATOM   1915 N N     . HIS A 1 258 ? -4.922  -35.852 10.891  1.00 36.17  ? 256 HIS A N     1 
ATOM   1916 C CA    . HIS A 1 258 ? -3.867  -36.135 11.904  1.00 36.00  ? 256 HIS A CA    1 
ATOM   1917 C C     . HIS A 1 258 ? -3.794  -37.659 12.040  1.00 33.37  ? 256 HIS A C     1 
ATOM   1918 O O     . HIS A 1 258 ? -4.826  -38.297 12.356  1.00 30.05  ? 256 HIS A O     1 
ATOM   1919 C CB    . HIS A 1 258 ? -4.203  -35.410 13.217  1.00 41.43  ? 256 HIS A CB    1 
ATOM   1920 C CG    . HIS A 1 258 ? -4.689  -34.001 13.021  1.00 50.08  ? 256 HIS A CG    1 
ATOM   1921 N ND1   . HIS A 1 258 ? -3.825  -32.916 12.906  1.00 54.00  ? 256 HIS A ND1   1 
ATOM   1922 C CD2   . HIS A 1 258 ? -5.944  -33.496 12.905  1.00 50.41  ? 256 HIS A CD2   1 
ATOM   1923 C CE1   . HIS A 1 258 ? -4.527  -31.816 12.713  1.00 60.09  ? 256 HIS A CE1   1 
ATOM   1924 N NE2   . HIS A 1 258 ? -5.831  -32.146 12.715  1.00 55.07  ? 256 HIS A NE2   1 
ATOM   1925 N N     . LYS A 1 259 ? -2.650  -38.252 11.740  1.00 31.51  ? 257 LYS A N     1 
ATOM   1926 C CA    . LYS A 1 259 ? -2.553  -39.729 11.622  1.00 32.63  ? 257 LYS A CA    1 
ATOM   1927 C C     . LYS A 1 259 ? -1.474  -40.289 12.555  1.00 31.66  ? 257 LYS A C     1 
ATOM   1928 O O     . LYS A 1 259 ? -0.545  -39.577 12.898  1.00 31.01  ? 257 LYS A O     1 
ATOM   1929 C CB    . LYS A 1 259 ? -2.242  -40.068 10.157  1.00 36.65  ? 257 LYS A CB    1 
ATOM   1930 C CG    . LYS A 1 259 ? -3.002  -39.232 9.122   1.00 35.53  ? 257 LYS A CG    1 
ATOM   1931 C CD    . LYS A 1 259 ? -2.935  -39.783 7.712   1.00 30.54  ? 257 LYS A CD    1 
ATOM   1932 C CE    . LYS A 1 259 ? -1.532  -39.872 7.165   1.00 31.17  ? 257 LYS A CE    1 
ATOM   1933 N NZ    . LYS A 1 259 ? -0.891  -38.535 7.039   1.00 30.92  ? 257 LYS A NZ    1 
ATOM   1934 N N     . MET A 1 260 ? -1.533  -41.587 12.832  1.00 32.62  ? 258 MET A N     1 
ATOM   1935 C CA    . MET A 1 260 ? -0.467  -42.354 13.534  1.00 30.23  ? 258 MET A CA    1 
ATOM   1936 C C     . MET A 1 260 ? 0.894   -42.199 12.850  1.00 28.92  ? 258 MET A C     1 
ATOM   1937 O O     . MET A 1 260 ? 1.940   -42.231 13.555  1.00 27.67  ? 258 MET A O     1 
ATOM   1938 C CB    . MET A 1 260 ? -0.844  -43.830 13.528  1.00 29.53  ? 258 MET A CB    1 
ATOM   1939 C CG    . MET A 1 260 ? 0.174   -44.750 14.139  1.00 31.20  ? 258 MET A CG    1 
ATOM   1940 S SD    . MET A 1 260 ? -0.530  -46.422 14.210  1.00 33.96  ? 258 MET A SD    1 
ATOM   1941 C CE    . MET A 1 260 ? 0.550   -47.204 15.400  1.00 35.07  ? 258 MET A CE    1 
ATOM   1942 N N     . GLY A 1 261 ? 0.904   -42.094 11.524  1.00 27.66  ? 259 GLY A N     1 
ATOM   1943 C CA    . GLY A 1 261 ? 2.148   -42.180 10.739  1.00 27.66  ? 259 GLY A CA    1 
ATOM   1944 C C     . GLY A 1 261 ? 1.995   -41.688 9.312   1.00 29.72  ? 259 GLY A C     1 
ATOM   1945 O O     . GLY A 1 261 ? 0.964   -41.051 8.995   1.00 30.20  ? 259 GLY A O     1 
ATOM   1946 N N     . ILE A 1 262 ? 2.998   -41.972 8.482   1.00 27.97  ? 260 ILE A N     1 
ATOM   1947 C CA    . ILE A 1 262 ? 3.156   -41.389 7.123   1.00 30.53  ? 260 ILE A CA    1 
ATOM   1948 C C     . ILE A 1 262 ? 2.657   -39.944 7.163   1.00 32.69  ? 260 ILE A C     1 
ATOM   1949 O O     . ILE A 1 262 ? 1.800   -39.566 6.322   1.00 33.52  ? 260 ILE A O     1 
ATOM   1950 C CB    . ILE A 1 262 ? 2.461   -42.259 6.058   1.00 28.92  ? 260 ILE A CB    1 
ATOM   1951 C CG1   . ILE A 1 262 ? 0.952   -42.433 6.243   1.00 28.27  ? 260 ILE A CG1   1 
ATOM   1952 C CG2   . ILE A 1 262 ? 3.148   -43.599 5.989   1.00 28.42  ? 260 ILE A CG2   1 
ATOM   1953 C CD1   . ILE A 1 262 ? 0.245   -42.817 4.941   1.00 30.88  ? 260 ILE A CD1   1 
ATOM   1954 N N     . HIS A 1 263 ? 3.167   -39.180 8.136   1.00 33.23  ? 261 HIS A N     1 
ATOM   1955 C CA    . HIS A 1 263 ? 2.845   -37.740 8.359   1.00 31.04  ? 261 HIS A CA    1 
ATOM   1956 C C     . HIS A 1 263 ? 3.213   -36.929 7.111   1.00 30.64  ? 261 HIS A C     1 
ATOM   1957 O O     . HIS A 1 263 ? 2.525   -35.936 6.833   1.00 33.49  ? 261 HIS A O     1 
ATOM   1958 C CB    . HIS A 1 263 ? 3.601   -37.172 9.571   1.00 32.98  ? 261 HIS A CB    1 
ATOM   1959 C CG    . HIS A 1 263 ? 3.280   -37.762 10.906  1.00 29.21  ? 261 HIS A CG    1 
ATOM   1960 N ND1   . HIS A 1 263 ? 4.131   -37.613 11.963  1.00 28.30  ? 261 HIS A ND1   1 
ATOM   1961 C CD2   . HIS A 1 263 ? 2.226   -38.484 11.356  1.00 32.25  ? 261 HIS A CD2   1 
ATOM   1962 C CE1   . HIS A 1 263 ? 3.614   -38.195 13.032  1.00 32.84  ? 261 HIS A CE1   1 
ATOM   1963 N NE2   . HIS A 1 263 ? 2.437   -38.744 12.694  1.00 31.60  ? 261 HIS A NE2   1 
ATOM   1964 N N     . GLY A 1 264 ? 4.269   -37.321 6.394   1.00 29.51  ? 262 GLY A N     1 
ATOM   1965 C CA    . GLY A 1 264 ? 4.806   -36.546 5.264   1.00 31.34  ? 262 GLY A CA    1 
ATOM   1966 C C     . GLY A 1 264 ? 3.941   -36.661 4.016   1.00 33.96  ? 262 GLY A C     1 
ATOM   1967 O O     . GLY A 1 264 ? 4.094   -35.829 3.104   1.00 33.35  ? 262 GLY A O     1 
ATOM   1968 N N     . ASN A 1 265 ? 3.001   -37.605 3.990   1.00 33.17  ? 263 ASN A N     1 
ATOM   1969 C CA    . ASN A 1 265 ? 2.084   -37.774 2.842   1.00 31.21  ? 263 ASN A CA    1 
ATOM   1970 C C     . ASN A 1 265 ? 0.723   -37.200 3.211   1.00 32.00  ? 263 ASN A C     1 
ATOM   1971 O O     . ASN A 1 265 ? 0.009   -37.817 4.063   1.00 35.23  ? 263 ASN A O     1 
ATOM   1972 C CB    . ASN A 1 265 ? 1.942   -39.225 2.397   1.00 30.29  ? 263 ASN A CB    1 
ATOM   1973 C CG    . ASN A 1 265 ? 1.297   -39.278 1.034   1.00 31.30  ? 263 ASN A CG    1 
ATOM   1974 O OD1   . ASN A 1 265 ? 0.100   -39.551 0.929   1.00 25.24  ? 263 ASN A OD1   1 
ATOM   1975 N ND2   . ASN A 1 265 ? 2.070   -38.916 0.014   1.00 30.98  ? 263 ASN A ND2   1 
ATOM   1976 N N     . ALA A 1 266 ? 0.332   -36.122 2.534   1.00 27.63  ? 264 ALA A N     1 
ATOM   1977 C CA    . ALA A 1 266 ? -0.895  -35.356 2.836   1.00 32.52  ? 264 ALA A CA    1 
ATOM   1978 C C     . ALA A 1 266 ? -2.129  -36.219 2.534   1.00 31.30  ? 264 ALA A C     1 
ATOM   1979 O O     . ALA A 1 266 ? -2.241  -36.755 1.451   1.00 27.28  ? 264 ALA A O     1 
ATOM   1980 C CB    . ALA A 1 266 ? -0.884  -34.050 2.078   1.00 35.90  ? 264 ALA A CB    1 
ATOM   1981 N N     . THR A 1 267 ? -2.962  -36.429 3.544   1.00 35.93  ? 265 THR A N     1 
ATOM   1982 C CA    . THR A 1 267 ? -4.163  -37.295 3.486   1.00 36.09  ? 265 THR A CA    1 
ATOM   1983 C C     . THR A 1 267 ? -5.391  -36.385 3.537   1.00 36.48  ? 265 THR A C     1 
ATOM   1984 O O     . THR A 1 267 ? -5.730  -35.913 4.658   1.00 33.72  ? 265 THR A O     1 
ATOM   1985 C CB    . THR A 1 267 ? -4.082  -38.339 4.606   1.00 36.00  ? 265 THR A CB    1 
ATOM   1986 O OG1   . THR A 1 267 ? -2.830  -39.006 4.436   1.00 33.93  ? 265 THR A OG1   1 
ATOM   1987 C CG2   . THR A 1 267 ? -5.211  -39.345 4.577   1.00 37.52  ? 265 THR A CG2   1 
ATOM   1988 N N     . CYS A 1 268 ? -6.026  -36.158 2.377   1.00 31.66  ? 266 CYS A N     1 
ATOM   1989 C CA    . CYS A 1 268 ? -6.840  -34.951 2.099   1.00 31.26  ? 266 CYS A CA    1 
ATOM   1990 C C     . CYS A 1 268 ? -8.328  -35.271 1.984   1.00 31.40  ? 266 CYS A C     1 
ATOM   1991 O O     . CYS A 1 268 ? -8.706  -36.289 1.386   1.00 33.42  ? 266 CYS A O     1 
ATOM   1992 C CB    . CYS A 1 268 ? -6.367  -34.266 0.829   1.00 32.87  ? 266 CYS A CB    1 
ATOM   1993 S SG    . CYS A 1 268 ? -4.595  -33.904 0.836   1.00 40.23  ? 266 CYS A SG    1 
ATOM   1994 N N     . VAL A 1 269 ? -9.147  -34.406 2.568   1.00 31.07  ? 267 VAL A N     1 
ATOM   1995 C CA    . VAL A 1 269 ? -10.604 -34.335 2.285   1.00 33.53  ? 267 VAL A CA    1 
ATOM   1996 C C     . VAL A 1 269 ? -10.706 -33.465 1.035   1.00 35.08  ? 267 VAL A C     1 
ATOM   1997 O O     . VAL A 1 269 ? -10.363 -32.302 1.136   1.00 35.78  ? 267 VAL A O     1 
ATOM   1998 C CB    . VAL A 1 269 ? -11.394 -33.776 3.479   1.00 30.69  ? 267 VAL A CB    1 
ATOM   1999 C CG1   . VAL A 1 269 ? -12.889 -33.694 3.204   1.00 27.72  ? 267 VAL A CG1   1 
ATOM   2000 C CG2   . VAL A 1 269 ? -11.121 -34.608 4.729   1.00 30.02  ? 267 VAL A CG2   1 
ATOM   2001 N N     . MET A 1 270 ? -11.047 -34.075 -0.103  1.00 37.52  ? 268 MET A N     1 
ATOM   2002 C CA    . MET A 1 270 ? -11.139 -33.414 -1.429  1.00 36.53  ? 268 MET A CA    1 
ATOM   2003 C C     . MET A 1 270 ? -12.614 -33.107 -1.732  1.00 37.39  ? 268 MET A C     1 
ATOM   2004 O O     . MET A 1 270 ? -13.448 -34.054 -1.780  1.00 37.59  ? 268 MET A O     1 
ATOM   2005 C CB    . MET A 1 270 ? -10.533 -34.315 -2.498  1.00 33.82  ? 268 MET A CB    1 
ATOM   2006 C CG    . MET A 1 270 ? -9.059  -34.562 -2.257  1.00 38.62  ? 268 MET A CG    1 
ATOM   2007 S SD    . MET A 1 270 ? -7.993  -33.061 -2.086  1.00 38.87  ? 268 MET A SD    1 
ATOM   2008 C CE    . MET A 1 270 ? -8.230  -32.232 -3.660  1.00 42.21  ? 268 MET A CE    1 
ATOM   2009 N N     . ASN A 1 271 ? -12.931 -31.813 -1.834  1.00 39.91  ? 269 ASN A N     1 
ATOM   2010 C CA    . ASN A 1 271 ? -14.274 -31.287 -2.211  1.00 41.49  ? 269 ASN A CA    1 
ATOM   2011 C C     . ASN A 1 271 ? -14.274 -30.984 -3.724  1.00 42.48  ? 269 ASN A C     1 
ATOM   2012 O O     . ASN A 1 271 ? -13.488 -30.114 -4.158  1.00 39.39  ? 269 ASN A O     1 
ATOM   2013 C CB    . ASN A 1 271 ? -14.647 -30.105 -1.306  1.00 41.26  ? 269 ASN A CB    1 
ATOM   2014 C CG    . ASN A 1 271 ? -14.572 -30.469 0.165   1.00 39.66  ? 269 ASN A CG    1 
ATOM   2015 O OD1   . ASN A 1 271 ? -15.320 -31.316 0.642   1.00 39.04  ? 269 ASN A OD1   1 
ATOM   2016 N ND2   . ASN A 1 271 ? -13.632 -29.882 0.882   1.00 40.86  ? 269 ASN A ND2   1 
ATOM   2017 N N     . PHE A 1 272 ? -15.039 -31.763 -4.505  1.00 44.41  ? 270 PHE A N     1 
ATOM   2018 C CA    . PHE A 1 272 ? -15.308 -31.521 -5.950  1.00 41.46  ? 270 PHE A CA    1 
ATOM   2019 C C     . PHE A 1 272 ? -16.644 -30.783 -6.061  1.00 42.57  ? 270 PHE A C     1 
ATOM   2020 O O     . PHE A 1 272 ? -17.677 -31.374 -5.715  1.00 38.38  ? 270 PHE A O     1 
ATOM   2021 C CB    . PHE A 1 272 ? -15.318 -32.834 -6.724  1.00 42.43  ? 270 PHE A CB    1 
ATOM   2022 C CG    . PHE A 1 272 ? -14.042 -33.616 -6.612  1.00 41.87  ? 270 PHE A CG    1 
ATOM   2023 C CD1   . PHE A 1 272 ? -12.997 -33.389 -7.491  1.00 39.30  ? 270 PHE A CD1   1 
ATOM   2024 C CD2   . PHE A 1 272 ? -13.887 -34.561 -5.606  1.00 41.41  ? 270 PHE A CD2   1 
ATOM   2025 C CE1   . PHE A 1 272 ? -11.814 -34.098 -7.366  1.00 41.05  ? 270 PHE A CE1   1 
ATOM   2026 C CE2   . PHE A 1 272 ? -12.706 -35.285 -5.499  1.00 38.70  ? 270 PHE A CE2   1 
ATOM   2027 C CZ    . PHE A 1 272 ? -11.672 -35.048 -6.378  1.00 39.42  ? 270 PHE A CZ    1 
ATOM   2028 N N     . ASP A 1 273 ? -16.605 -29.508 -6.461  1.00 43.95  ? 271 ASP A N     1 
ATOM   2029 C CA    . ASP A 1 273 ? -17.773 -28.587 -6.429  1.00 46.17  ? 271 ASP A CA    1 
ATOM   2030 C C     . ASP A 1 273 ? -18.256 -28.358 -7.879  1.00 49.22  ? 271 ASP A C     1 
ATOM   2031 O O     . ASP A 1 273 ? -17.985 -27.284 -8.439  1.00 42.24  ? 271 ASP A O     1 
ATOM   2032 C CB    . ASP A 1 273 ? -17.374 -27.316 -5.674  1.00 46.93  ? 271 ASP A CB    1 
ATOM   2033 C CG    . ASP A 1 273 ? -18.523 -26.361 -5.391  1.00 53.84  ? 271 ASP A CG    1 
ATOM   2034 O OD1   . ASP A 1 273 ? -19.682 -26.722 -5.684  1.00 63.20  ? 271 ASP A OD1   1 
ATOM   2035 O OD2   . ASP A 1 273 ? -18.250 -25.246 -4.903  1.00 61.82  ? 271 ASP A OD2   1 
ATOM   2036 N N     . ALA A 1 274 ? -18.915 -29.352 -8.486  1.00 46.16  ? 272 ALA A N     1 
ATOM   2037 C CA    . ALA A 1 274 ? -19.102 -29.439 -9.953  1.00 48.66  ? 272 ALA A CA    1 
ATOM   2038 C C     . ALA A 1 274 ? -17.798 -29.077 -10.674 1.00 44.52  ? 272 ALA A C     1 
ATOM   2039 O O     . ALA A 1 274 ? -17.812 -28.175 -11.483 1.00 46.23  ? 272 ALA A O     1 
ATOM   2040 C CB    . ALA A 1 274 ? -20.223 -28.528 -10.370 1.00 51.57  ? 272 ALA A CB    1 
ATOM   2041 N N     . ALA A 1 275 ? -16.699 -29.747 -10.357 1.00 44.73  ? 273 ALA A N     1 
ATOM   2042 C CA    . ALA A 1 275 ? -15.434 -29.679 -11.118 1.00 45.54  ? 273 ALA A CA    1 
ATOM   2043 C C     . ALA A 1 275 ? -15.654 -30.352 -12.466 1.00 47.19  ? 273 ALA A C     1 
ATOM   2044 O O     . ALA A 1 275 ? -16.406 -31.353 -12.500 1.00 46.61  ? 273 ALA A O     1 
ATOM   2045 C CB    . ALA A 1 275 ? -14.312 -30.393 -10.393 1.00 48.34  ? 273 ALA A CB    1 
ATOM   2046 N N     . THR A 1 276 ? -14.940 -29.883 -13.490 1.00 42.06  ? 274 THR A N     1 
ATOM   2047 C CA    . THR A 1 276 ? -14.979 -30.412 -14.875 1.00 40.54  ? 274 THR A CA    1 
ATOM   2048 C C     . THR A 1 276 ? -14.164 -31.706 -14.860 1.00 42.41  ? 274 THR A C     1 
ATOM   2049 O O     . THR A 1 276 ? -12.997 -31.667 -14.376 1.00 41.74  ? 274 THR A O     1 
ATOM   2050 C CB    . THR A 1 276 ? -14.460 -29.345 -15.855 1.00 40.83  ? 274 THR A CB    1 
ATOM   2051 O OG1   . THR A 1 276 ? -15.406 -28.279 -15.818 1.00 42.89  ? 274 THR A OG1   1 
ATOM   2052 C CG2   . THR A 1 276 ? -14.256 -29.829 -17.273 1.00 39.56  ? 274 THR A CG2   1 
ATOM   2053 N N     . GLY A 1 277 ? -14.769 -32.800 -15.323 1.00 41.85  ? 275 GLY A N     1 
ATOM   2054 C CA    . GLY A 1 277 ? -14.098 -34.100 -15.520 1.00 43.74  ? 275 GLY A CA    1 
ATOM   2055 C C     . GLY A 1 277 ? -14.406 -34.717 -16.874 1.00 43.36  ? 275 GLY A C     1 
ATOM   2056 O O     . GLY A 1 277 ? -15.383 -34.309 -17.540 1.00 45.73  ? 275 GLY A O     1 
ATOM   2057 N N     . PHE A 1 278 ? -13.590 -35.673 -17.287 1.00 40.62  ? 276 PHE A N     1 
ATOM   2058 C CA    . PHE A 1 278 ? -13.738 -36.361 -18.587 1.00 41.88  ? 276 PHE A CA    1 
ATOM   2059 C C     . PHE A 1 278 ? -13.856 -37.859 -18.338 1.00 41.75  ? 276 PHE A C     1 
ATOM   2060 O O     . PHE A 1 278 ? -12.977 -38.394 -17.677 1.00 43.81  ? 276 PHE A O     1 
ATOM   2061 C CB    . PHE A 1 278 ? -12.559 -36.000 -19.481 1.00 41.66  ? 276 PHE A CB    1 
ATOM   2062 C CG    . PHE A 1 278 ? -12.324 -34.520 -19.515 1.00 39.71  ? 276 PHE A CG    1 
ATOM   2063 C CD1   . PHE A 1 278 ? -13.102 -33.708 -20.316 1.00 40.85  ? 276 PHE A CD1   1 
ATOM   2064 C CD2   . PHE A 1 278 ? -11.359 -33.942 -18.705 1.00 44.58  ? 276 PHE A CD2   1 
ATOM   2065 C CE1   . PHE A 1 278 ? -12.905 -32.336 -20.327 1.00 42.65  ? 276 PHE A CE1   1 
ATOM   2066 C CE2   . PHE A 1 278 ? -11.164 -32.571 -18.705 1.00 49.65  ? 276 PHE A CE2   1 
ATOM   2067 C CZ    . PHE A 1 278 ? -11.927 -31.773 -19.538 1.00 49.48  ? 276 PHE A CZ    1 
ATOM   2068 N N     . LEU A 1 279 ? -14.937 -38.476 -18.818 1.00 40.81  ? 277 LEU A N     1 
ATOM   2069 C CA    . LEU A 1 279 ? -15.160 -39.930 -18.710 1.00 40.07  ? 277 LEU A CA    1 
ATOM   2070 C C     . LEU A 1 279 ? -13.976 -40.622 -19.363 1.00 36.96  ? 277 LEU A C     1 
ATOM   2071 O O     . LEU A 1 279 ? -13.645 -40.278 -20.489 1.00 36.42  ? 277 LEU A O     1 
ATOM   2072 C CB    . LEU A 1 279 ? -16.467 -40.360 -19.374 1.00 44.69  ? 277 LEU A CB    1 
ATOM   2073 C CG    . LEU A 1 279 ? -16.739 -41.866 -19.283 1.00 47.41  ? 277 LEU A CG    1 
ATOM   2074 C CD1   . LEU A 1 279 ? -17.375 -42.229 -17.945 1.00 47.71  ? 277 LEU A CD1   1 
ATOM   2075 C CD2   . LEU A 1 279 ? -17.627 -42.307 -20.430 1.00 48.43  ? 277 LEU A CD2   1 
ATOM   2076 N N     . ILE A 1 280 ? -13.355 -41.528 -18.621 1.00 34.02  ? 278 ILE A N     1 
ATOM   2077 C CA    . ILE A 1 280 ? -12.304 -42.450 -19.105 1.00 33.88  ? 278 ILE A CA    1 
ATOM   2078 C C     . ILE A 1 280 ? -12.875 -43.839 -18.883 1.00 37.19  ? 278 ILE A C     1 
ATOM   2079 O O     . ILE A 1 280 ? -13.371 -44.091 -17.745 1.00 40.64  ? 278 ILE A O     1 
ATOM   2080 C CB    . ILE A 1 280 ? -10.950 -42.258 -18.389 1.00 36.01  ? 278 ILE A CB    1 
ATOM   2081 C CG1   . ILE A 1 280 ? -9.974  -43.358 -18.785 1.00 35.18  ? 278 ILE A CG1   1 
ATOM   2082 C CG2   . ILE A 1 280 ? -11.066 -42.208 -16.868 1.00 36.42  ? 278 ILE A CG2   1 
ATOM   2083 C CD1   . ILE A 1 280 ? -8.540  -42.961 -18.576 1.00 39.33  ? 278 ILE A CD1   1 
ATOM   2084 N N     . GLY A 1 281 ? -12.842 -44.660 -19.935 1.00 37.75  ? 279 GLY A N     1 
ATOM   2085 C CA    . GLY A 1 281 ? -13.421 -46.013 -19.982 1.00 37.11  ? 279 GLY A CA    1 
ATOM   2086 C C     . GLY A 1 281 ? -14.937 -45.964 -20.163 1.00 39.02  ? 279 GLY A C     1 
ATOM   2087 O O     . GLY A 1 281 ? -15.579 -44.905 -20.113 1.00 37.31  ? 279 GLY A O     1 
ATOM   2088 N N     . PRO A 1 282 ? -15.577 -47.128 -20.363 1.00 41.59  ? 280 PRO A N     1 
ATOM   2089 C CA    . PRO A 1 282 ? -17.008 -47.126 -20.656 1.00 45.36  ? 280 PRO A CA    1 
ATOM   2090 C C     . PRO A 1 282 ? -17.811 -46.597 -19.463 1.00 47.64  ? 280 PRO A C     1 
ATOM   2091 O O     . PRO A 1 282 ? -17.370 -46.647 -18.313 1.00 47.46  ? 280 PRO A O     1 
ATOM   2092 C CB    . PRO A 1 282 ? -17.320 -48.586 -21.033 1.00 45.57  ? 280 PRO A CB    1 
ATOM   2093 C CG    . PRO A 1 282 ? -15.968 -49.328 -21.085 1.00 43.56  ? 280 PRO A CG    1 
ATOM   2094 C CD    . PRO A 1 282 ? -14.951 -48.462 -20.365 1.00 43.43  ? 280 PRO A CD    1 
ATOM   2095 N N     . PRO A 1 283 ? -19.032 -46.072 -19.680 1.00 50.94  ? 281 PRO A N     1 
ATOM   2096 C CA    . PRO A 1 283 ? -19.845 -45.594 -18.572 1.00 49.46  ? 281 PRO A CA    1 
ATOM   2097 C C     . PRO A 1 283 ? -20.203 -46.875 -17.804 1.00 44.64  ? 281 PRO A C     1 
ATOM   2098 O O     . PRO A 1 283 ? -20.282 -47.886 -18.453 1.00 37.11  ? 281 PRO A O     1 
ATOM   2099 C CB    . PRO A 1 283 ? -21.038 -44.862 -19.229 1.00 51.36  ? 281 PRO A CB    1 
ATOM   2100 C CG    . PRO A 1 283 ? -20.812 -44.958 -20.739 1.00 51.78  ? 281 PRO A CG    1 
ATOM   2101 C CD    . PRO A 1 283 ? -19.777 -46.051 -20.947 1.00 52.64  ? 281 PRO A CD    1 
ATOM   2102 N N     . ASN A 1 284 ? -20.279 -46.814 -16.463 1.00 43.94  ? 282 ASN A N     1 
ATOM   2103 C CA    . ASN A 1 284 ? -20.718 -47.913 -15.557 1.00 43.55  ? 282 ASN A CA    1 
ATOM   2104 C C     . ASN A 1 284 ? -19.703 -49.051 -15.505 1.00 41.77  ? 282 ASN A C     1 
ATOM   2105 O O     . ASN A 1 284 ? -19.979 -50.023 -14.802 1.00 45.07  ? 282 ASN A O     1 
ATOM   2106 C CB    . ASN A 1 284 ? -22.096 -48.453 -15.927 1.00 45.31  ? 282 ASN A CB    1 
ATOM   2107 C CG    . ASN A 1 284 ? -23.155 -47.385 -15.775 1.00 48.69  ? 282 ASN A CG    1 
ATOM   2108 O OD1   . ASN A 1 284 ? -22.933 -46.322 -15.193 1.00 50.64  ? 282 ASN A OD1   1 
ATOM   2109 N ND2   . ASN A 1 284 ? -24.315 -47.645 -16.334 1.00 54.04  ? 282 ASN A ND2   1 
ATOM   2110 N N     . LYS A 1 285 ? -18.542 -48.903 -16.133 1.00 43.85  ? 283 LYS A N     1 
ATOM   2111 C CA    . LYS A 1 285 ? -17.438 -49.898 -16.044 1.00 48.11  ? 283 LYS A CA    1 
ATOM   2112 C C     . LYS A 1 285 ? -16.253 -49.271 -15.296 1.00 44.59  ? 283 LYS A C     1 
ATOM   2113 O O     . LYS A 1 285 ? -15.105 -49.735 -15.503 1.00 43.63  ? 283 LYS A O     1 
ATOM   2114 C CB    . LYS A 1 285 ? -16.999 -50.380 -17.436 1.00 50.90  ? 283 LYS A CB    1 
ATOM   2115 C CG    . LYS A 1 285 ? -18.090 -51.018 -18.280 1.00 54.89  ? 283 LYS A CG    1 
ATOM   2116 C CD    . LYS A 1 285 ? -19.029 -51.916 -17.514 1.00 54.74  ? 283 LYS A CD    1 
ATOM   2117 C CE    . LYS A 1 285 ? -19.849 -52.822 -18.404 1.00 56.96  ? 283 LYS A CE    1 
ATOM   2118 N NZ    . LYS A 1 285 ? -19.572 -54.229 -18.046 1.00 61.04  ? 283 LYS A NZ    1 
ATOM   2119 N N     . GLY A 1 286 ? -16.513 -48.263 -14.457 1.00 39.69  ? 284 GLY A N     1 
ATOM   2120 C CA    . GLY A 1 286 ? -15.469 -47.602 -13.655 1.00 42.21  ? 284 GLY A CA    1 
ATOM   2121 C C     . GLY A 1 286 ? -14.648 -48.608 -12.860 1.00 39.68  ? 284 GLY A C     1 
ATOM   2122 O O     . GLY A 1 286 ? -13.425 -48.517 -12.874 1.00 41.65  ? 284 GLY A O     1 
ATOM   2123 N N     . LEU A 1 287 ? -15.292 -49.530 -12.154 1.00 41.57  ? 285 LEU A N     1 
ATOM   2124 C CA    . LEU A 1 287 ? -14.573 -50.401 -11.206 1.00 42.18  ? 285 LEU A CA    1 
ATOM   2125 C C     . LEU A 1 287 ? -13.605 -51.285 -12.006 1.00 44.56  ? 285 LEU A C     1 
ATOM   2126 O O     . LEU A 1 287 ? -12.437 -51.400 -11.591 1.00 53.38  ? 285 LEU A O     1 
ATOM   2127 C CB    . LEU A 1 287 ? -15.580 -51.177 -10.358 1.00 46.34  ? 285 LEU A CB    1 
ATOM   2128 C CG    . LEU A 1 287 ? -14.982 -52.038 -9.234  1.00 54.95  ? 285 LEU A CG    1 
ATOM   2129 C CD1   . LEU A 1 287 ? -14.112 -51.213 -8.293  1.00 60.02  ? 285 LEU A CD1   1 
ATOM   2130 C CD2   . LEU A 1 287 ? -16.065 -52.756 -8.437  1.00 55.01  ? 285 LEU A CD2   1 
ATOM   2131 N N     . ASN A 1 288 ? -14.019 -51.792 -13.161 1.00 45.32  ? 286 ASN A N     1 
ATOM   2132 C CA    . ASN A 1 288 ? -13.159 -52.596 -14.084 1.00 53.13  ? 286 ASN A CA    1 
ATOM   2133 C C     . ASN A 1 288 ? -11.894 -51.779 -14.424 1.00 55.83  ? 286 ASN A C     1 
ATOM   2134 O O     . ASN A 1 288 ? -10.747 -52.194 -14.075 1.00 55.49  ? 286 ASN A O     1 
ATOM   2135 C CB    . ASN A 1 288 ? -13.952 -53.049 -15.314 1.00 54.89  ? 286 ASN A CB    1 
ATOM   2136 C CG    . ASN A 1 288 ? -15.353 -53.538 -14.965 1.00 67.17  ? 286 ASN A CG    1 
ATOM   2137 O OD1   . ASN A 1 288 ? -15.667 -54.708 -15.153 1.00 68.17  ? 286 ASN A OD1   1 
ATOM   2138 N ND2   . ASN A 1 288 ? -16.214 -52.676 -14.424 1.00 68.48  ? 286 ASN A ND2   1 
ATOM   2139 N N     . CYS A 1 289 ? -12.076 -50.591 -14.988 1.00 52.70  ? 287 CYS A N     1 
ATOM   2140 C CA    . CYS A 1 289 ? -10.961 -49.677 -15.344 1.00 54.72  ? 287 CYS A CA    1 
ATOM   2141 C C     . CYS A 1 289 ? -10.095 -49.320 -14.123 1.00 57.29  ? 287 CYS A C     1 
ATOM   2142 O O     . CYS A 1 289 ? -8.873  -49.320 -14.262 1.00 59.05  ? 287 CYS A O     1 
ATOM   2143 C CB    . CYS A 1 289 ? -11.530 -48.424 -15.988 1.00 51.89  ? 287 CYS A CB    1 
ATOM   2144 S SG    . CYS A 1 289 ? -12.400 -48.807 -17.527 1.00 52.75  ? 287 CYS A SG    1 
ATOM   2145 N N     . MET A 1 290 ? -10.691 -49.000 -12.968 1.00 57.90  ? 288 MET A N     1 
ATOM   2146 C CA    . MET A 1 290 ? -9.949  -48.555 -11.755 1.00 56.28  ? 288 MET A CA    1 
ATOM   2147 C C     . MET A 1 290 ? -9.091  -49.709 -11.199 1.00 59.33  ? 288 MET A C     1 
ATOM   2148 O O     . MET A 1 290 ? -8.239  -49.390 -10.361 1.00 72.23  ? 288 MET A O     1 
ATOM   2149 C CB    . MET A 1 290 ? -10.908 -47.989 -10.685 1.00 54.46  ? 288 MET A CB    1 
ATOM   2150 C CG    . MET A 1 290 ? -10.275 -47.468 -9.373  1.00 44.62  ? 288 MET A CG    1 
ATOM   2151 S SD    . MET A 1 290 ? -8.867  -46.223 -9.438  1.00 51.19  ? 288 MET A SD    1 
ATOM   2152 C CE    . MET A 1 290 ? -9.737  -44.688 -9.084  1.00 45.82  ? 288 MET A CE    1 
ATOM   2153 N N     . PHE A 1 291 ? -9.187  -50.950 -11.710 1.00 57.71  ? 289 PHE A N     1 
ATOM   2154 C CA    . PHE A 1 291 ? -8.440  -52.128 -11.180 1.00 61.22  ? 289 PHE A CA    1 
ATOM   2155 C C     . PHE A 1 291 ? -7.049  -52.337 -11.825 1.00 62.82  ? 289 PHE A C     1 
ATOM   2156 O O     . PHE A 1 291 ? -6.200  -53.105 -11.262 1.00 68.73  ? 289 PHE A O     1 
ATOM   2157 C CB    . PHE A 1 291 ? -9.317  -53.383 -11.211 1.00 62.44  ? 289 PHE A CB    1 
ATOM   2158 C CG    . PHE A 1 291 ? -9.850  -53.770 -9.845  1.00 61.58  ? 289 PHE A CG    1 
ATOM   2159 C CD1   . PHE A 1 291 ? -9.008  -54.310 -8.868  1.00 61.92  ? 289 PHE A CD1   1 
ATOM   2160 C CD2   . PHE A 1 291 ? -11.192 -53.593 -9.527  1.00 59.51  ? 289 PHE A CD2   1 
ATOM   2161 C CE1   . PHE A 1 291 ? -9.491  -54.665 -7.610  1.00 62.10  ? 289 PHE A CE1   1 
ATOM   2162 C CE2   . PHE A 1 291 ? -11.673 -53.949 -8.271  1.00 64.04  ? 289 PHE A CE2   1 
ATOM   2163 C CZ    . PHE A 1 291 ? -10.825 -54.483 -7.315  1.00 59.97  ? 289 PHE A CZ    1 
ATOM   2164 N N     . THR A 1 292 ? -6.739  -51.672 -12.932 1.00 65.40  ? 290 THR A N     1 
ATOM   2165 C CA    . THR A 1 292 ? -5.335  -51.539 -13.412 1.00 63.33  ? 290 THR A CA    1 
ATOM   2166 C C     . THR A 1 292 ? -4.542  -50.719 -12.377 1.00 57.24  ? 290 THR A C     1 
ATOM   2167 O O     . THR A 1 292 ? -3.479  -51.167 -11.966 1.00 56.16  ? 290 THR A O     1 
ATOM   2168 C CB    . THR A 1 292 ? -5.299  -50.858 -14.780 1.00 65.47  ? 290 THR A CB    1 
ATOM   2169 O OG1   . THR A 1 292 ? -6.225  -51.557 -15.624 1.00 60.53  ? 290 THR A OG1   1 
ATOM   2170 C CG2   . THR A 1 292 ? -3.890  -50.811 -15.337 1.00 69.35  ? 290 THR A CG2   1 
ATOM   2171 N N     . PHE A 1 293 ? -5.093  -49.576 -11.964 1.00 50.28  ? 291 PHE A N     1 
ATOM   2172 C CA    . PHE A 1 293 ? -4.610  -48.675 -10.882 1.00 61.34  ? 291 PHE A CA    1 
ATOM   2173 C C     . PHE A 1 293 ? -4.506  -49.400 -9.517  1.00 65.00  ? 291 PHE A C     1 
ATOM   2174 O O     . PHE A 1 293 ? -3.475  -49.183 -8.801  1.00 63.39  ? 291 PHE A O     1 
ATOM   2175 C CB    . PHE A 1 293 ? -5.575  -47.491 -10.749 1.00 66.09  ? 291 PHE A CB    1 
ATOM   2176 C CG    . PHE A 1 293 ? -5.035  -46.184 -10.209 1.00 74.19  ? 291 PHE A CG    1 
ATOM   2177 C CD1   . PHE A 1 293 ? -3.834  -46.095 -9.512  1.00 78.88  ? 291 PHE A CD1   1 
ATOM   2178 C CD2   . PHE A 1 293 ? -5.792  -45.024 -10.348 1.00 81.68  ? 291 PHE A CD2   1 
ATOM   2179 C CE1   . PHE A 1 293 ? -3.386  -44.875 -9.016  1.00 79.54  ? 291 PHE A CE1   1 
ATOM   2180 C CE2   . PHE A 1 293 ? -5.343  -43.808 -9.857  1.00 83.13  ? 291 PHE A CE2   1 
ATOM   2181 C CZ    . PHE A 1 293 ? -4.135  -43.732 -9.200  1.00 85.27  ? 291 PHE A CZ    1 
ATOM   2182 N N     . MET A 1 294 ? -5.535  -50.180 -9.118  1.00 57.51  ? 292 MET A N     1 
ATOM   2183 C CA    . MET A 1 294 ? -5.608  -50.862 -7.791  1.00 57.37  ? 292 MET A CA    1 
ATOM   2184 C C     . MET A 1 294 ? -4.594  -52.032 -7.709  1.00 59.37  ? 292 MET A C     1 
ATOM   2185 O O     . MET A 1 294 ? -3.925  -52.102 -6.669  1.00 45.98  ? 292 MET A O     1 
ATOM   2186 C CB    . MET A 1 294 ? -7.027  -51.342 -7.450  1.00 58.68  ? 292 MET A CB    1 
ATOM   2187 C CG    . MET A 1 294 ? -8.013  -50.202 -7.141  1.00 61.23  ? 292 MET A CG    1 
ATOM   2188 S SD    . MET A 1 294 ? -9.792  -50.639 -7.319  1.00 60.70  ? 292 MET A SD    1 
ATOM   2189 C CE    . MET A 1 294 ? -10.086 -51.376 -5.706  1.00 62.26  ? 292 MET A CE    1 
ATOM   2190 N N     . ASN A 1 295 ? -4.402  -52.884 -8.737  1.00 59.41  ? 293 ASN A N     1 
ATOM   2191 C CA    . ASN A 1 295 ? -3.458  -54.039 -8.627  1.00 59.05  ? 293 ASN A CA    1 
ATOM   2192 C C     . ASN A 1 295 ? -1.982  -53.583 -8.668  1.00 59.91  ? 293 ASN A C     1 
ATOM   2193 O O     . ASN A 1 295 ? -1.163  -54.148 -7.917  1.00 61.43  ? 293 ASN A O     1 
ATOM   2194 C CB    . ASN A 1 295 ? -3.797  -55.110 -9.646  1.00 54.06  ? 293 ASN A CB    1 
ATOM   2195 C CG    . ASN A 1 295 ? -5.183  -55.624 -9.394  1.00 58.00  ? 293 ASN A CG    1 
ATOM   2196 O OD1   . ASN A 1 295 ? -5.448  -56.184 -8.337  1.00 75.39  ? 293 ASN A OD1   1 
ATOM   2197 N ND2   . ASN A 1 295 ? -6.068  -55.418 -10.342 1.00 60.25  ? 293 ASN A ND2   1 
ATOM   2198 N N     . THR A 1 296 ? -1.627  -52.620 -9.513  1.00 58.19  ? 294 THR A N     1 
ATOM   2199 C CA    . THR A 1 296 ? -0.314  -51.923 -9.445  1.00 63.74  ? 294 THR A CA    1 
ATOM   2200 C C     . THR A 1 296 ? -0.065  -51.598 -7.976  1.00 60.01  ? 294 THR A C     1 
ATOM   2201 O O     . THR A 1 296 ? 0.943   -52.094 -7.426  1.00 57.39  ? 294 THR A O     1 
ATOM   2202 C CB    . THR A 1 296 ? -0.284  -50.596 -10.232 1.00 63.98  ? 294 THR A CB    1 
ATOM   2203 O OG1   . THR A 1 296 ? -0.301  -50.913 -11.626 1.00 60.09  ? 294 THR A OG1   1 
ATOM   2204 C CG2   . THR A 1 296 ? 0.909   -49.721 -9.884  1.00 58.25  ? 294 THR A CG2   1 
ATOM   2205 N N     . ALA A 1 297 ? -1.000  -50.830 -7.389  1.00 54.85  ? 295 ALA A N     1 
ATOM   2206 C CA    . ALA A 1 297 ? -0.935  -50.271 -6.014  1.00 58.78  ? 295 ALA A CA    1 
ATOM   2207 C C     . ALA A 1 297 ? -1.039  -51.381 -4.951  1.00 52.86  ? 295 ALA A C     1 
ATOM   2208 O O     . ALA A 1 297 ? -0.651  -51.052 -3.799  1.00 57.26  ? 295 ALA A O     1 
ATOM   2209 C CB    . ALA A 1 297 ? -1.994  -49.206 -5.808  1.00 59.98  ? 295 ALA A CB    1 
ATOM   2210 N N     . ARG A 1 298 ? -1.433  -52.604 -5.324  1.00 44.69  ? 296 ARG A N     1 
ATOM   2211 C CA    . ARG A 1 298 ? -1.454  -53.756 -4.379  1.00 46.54  ? 296 ARG A CA    1 
ATOM   2212 C C     . ARG A 1 298 ? -0.058  -54.396 -4.365  1.00 44.35  ? 296 ARG A C     1 
ATOM   2213 O O     . ARG A 1 298 ? 0.448   -54.636 -3.270  1.00 31.82  ? 296 ARG A O     1 
ATOM   2214 C CB    . ARG A 1 298 ? -2.582  -54.728 -4.735  1.00 48.68  ? 296 ARG A CB    1 
ATOM   2215 C CG    . ARG A 1 298 ? -3.803  -54.594 -3.836  1.00 51.52  ? 296 ARG A CG    1 
ATOM   2216 C CD    . ARG A 1 298 ? -5.123  -54.941 -4.495  1.00 46.51  ? 296 ARG A CD    1 
ATOM   2217 N NE    . ARG A 1 298 ? -6.248  -54.215 -3.924  1.00 43.32  ? 296 ARG A NE    1 
ATOM   2218 C CZ    . ARG A 1 298 ? -7.453  -54.730 -3.712  1.00 39.85  ? 296 ARG A CZ    1 
ATOM   2219 N NH1   . ARG A 1 298 ? -8.410  -53.982 -3.192  1.00 40.12  ? 296 ARG A NH1   1 
ATOM   2220 N NH2   . ARG A 1 298 ? -7.698  -55.991 -4.013  1.00 41.34  ? 296 ARG A NH2   1 
ATOM   2221 N N     . LEU A 1 299 ? 0.518   -54.683 -5.536  1.00 42.83  ? 297 LEU A N     1 
ATOM   2222 C CA    . LEU A 1 299 ? 1.935   -55.141 -5.583  1.00 42.23  ? 297 LEU A CA    1 
ATOM   2223 C C     . LEU A 1 299 ? 2.839   -54.003 -5.047  1.00 41.86  ? 297 LEU A C     1 
ATOM   2224 O O     . LEU A 1 299 ? 3.820   -54.302 -4.349  1.00 37.61  ? 297 LEU A O     1 
ATOM   2225 C CB    . LEU A 1 299 ? 2.256   -55.555 -7.020  1.00 44.18  ? 297 LEU A CB    1 
ATOM   2226 C CG    . LEU A 1 299 ? 3.360   -56.601 -7.184  1.00 51.99  ? 297 LEU A CG    1 
ATOM   2227 C CD1   . LEU A 1 299 ? 3.207   -57.745 -6.193  1.00 51.94  ? 297 LEU A CD1   1 
ATOM   2228 C CD2   . LEU A 1 299 ? 3.384   -57.153 -8.608  1.00 55.34  ? 297 LEU A CD2   1 
ATOM   2229 N N     . GLY A 1 300 ? 2.448   -52.742 -5.273  1.00 36.41  ? 298 GLY A N     1 
ATOM   2230 C CA    . GLY A 1 300 ? 3.088   -51.536 -4.716  1.00 37.63  ? 298 GLY A CA    1 
ATOM   2231 C C     . GLY A 1 300 ? 3.019   -51.505 -3.196  1.00 36.88  ? 298 GLY A C     1 
ATOM   2232 O O     . GLY A 1 300 ? 4.013   -51.112 -2.599  1.00 35.62  ? 298 GLY A O     1 
ATOM   2233 N N     . THR A 1 301 ? 1.914   -51.947 -2.588  1.00 32.49  ? 299 THR A N     1 
ATOM   2234 C CA    . THR A 1 301 ? 1.734   -51.944 -1.117  1.00 33.37  ? 299 THR A CA    1 
ATOM   2235 C C     . THR A 1 301 ? 2.412   -53.170 -0.507  1.00 32.66  ? 299 THR A C     1 
ATOM   2236 O O     . THR A 1 301 ? 2.826   -53.078 0.671   1.00 34.76  ? 299 THR A O     1 
ATOM   2237 C CB    . THR A 1 301 ? 0.263   -51.815 -0.704  1.00 36.55  ? 299 THR A CB    1 
ATOM   2238 O OG1   . THR A 1 301 ? -0.260  -50.622 -1.282  1.00 43.01  ? 299 THR A OG1   1 
ATOM   2239 C CG2   . THR A 1 301 ? 0.090   -51.685 0.792   1.00 36.36  ? 299 THR A CG2   1 
ATOM   2240 N N     . ALA A 1 302 ? 2.520   -54.277 -1.242  1.00 30.23  ? 300 ALA A N     1 
ATOM   2241 C CA    . ALA A 1 302 ? 3.287   -55.460 -0.798  1.00 34.48  ? 300 ALA A CA    1 
ATOM   2242 C C     . ALA A 1 302 ? 4.737   -55.018 -0.558  1.00 34.63  ? 300 ALA A C     1 
ATOM   2243 O O     . ALA A 1 302 ? 5.374   -55.460 0.403   1.00 37.91  ? 300 ALA A O     1 
ATOM   2244 C CB    . ALA A 1 302 ? 3.215   -56.570 -1.828  1.00 36.56  ? 300 ALA A CB    1 
ATOM   2245 N N     . LEU A 1 303 ? 5.226   -54.201 -1.472  1.00 33.75  ? 301 LEU A N     1 
ATOM   2246 C CA    . LEU A 1 303 ? 6.570   -53.591 -1.458  1.00 37.78  ? 301 LEU A CA    1 
ATOM   2247 C C     . LEU A 1 303 ? 6.750   -52.740 -0.192  1.00 31.63  ? 301 LEU A C     1 
ATOM   2248 O O     . LEU A 1 303 ? 7.860   -52.684 0.301   1.00 31.00  ? 301 LEU A O     1 
ATOM   2249 C CB    . LEU A 1 303 ? 6.683   -52.772 -2.747  1.00 37.35  ? 301 LEU A CB    1 
ATOM   2250 C CG    . LEU A 1 303 ? 8.067   -52.260 -3.090  1.00 41.12  ? 301 LEU A CG    1 
ATOM   2251 C CD1   . LEU A 1 303 ? 8.273   -52.265 -4.596  1.00 43.88  ? 301 LEU A CD1   1 
ATOM   2252 C CD2   . LEU A 1 303 ? 8.218   -50.853 -2.545  1.00 44.42  ? 301 LEU A CD2   1 
ATOM   2253 N N     . GLN A 1 304 ? 5.698   -52.090 0.299   1.00 30.47  ? 302 GLN A N     1 
ATOM   2254 C CA    . GLN A 1 304 ? 5.741   -51.324 1.568   1.00 30.04  ? 302 GLN A CA    1 
ATOM   2255 C C     . GLN A 1 304 ? 6.030   -52.268 2.733   1.00 27.43  ? 302 GLN A C     1 
ATOM   2256 O O     . GLN A 1 304 ? 6.848   -51.911 3.574   1.00 28.41  ? 302 GLN A O     1 
ATOM   2257 C CB    . GLN A 1 304 ? 4.442   -50.587 1.837   1.00 27.97  ? 302 GLN A CB    1 
ATOM   2258 C CG    . GLN A 1 304 ? 4.565   -49.746 3.075   1.00 29.67  ? 302 GLN A CG    1 
ATOM   2259 C CD    . GLN A 1 304 ? 3.335   -48.959 3.432   1.00 31.45  ? 302 GLN A CD    1 
ATOM   2260 O OE1   . GLN A 1 304 ? 2.347   -48.891 2.687   1.00 29.92  ? 302 GLN A OE1   1 
ATOM   2261 N NE2   . GLN A 1 304 ? 3.421   -48.352 4.603   1.00 32.69  ? 302 GLN A NE2   1 
ATOM   2262 N N     . GLY A 1 305 ? 5.357   -53.416 2.769   1.00 27.29  ? 303 GLY A N     1 
ATOM   2263 C CA    . GLY A 1 305 ? 5.631   -54.510 3.710   1.00 26.77  ? 303 GLY A CA    1 
ATOM   2264 C C     . GLY A 1 305 ? 7.084   -54.959 3.642   1.00 29.00  ? 303 GLY A C     1 
ATOM   2265 O O     . GLY A 1 305 ? 7.680   -55.224 4.702   1.00 27.49  ? 303 GLY A O     1 
ATOM   2266 N N     . LEU A 1 306 ? 7.632   -55.154 2.440   1.00 29.06  ? 304 LEU A N     1 
ATOM   2267 C CA    . LEU A 1 306 ? 9.059   -55.530 2.299   1.00 28.57  ? 304 LEU A CA    1 
ATOM   2268 C C     . LEU A 1 306 ? 9.894   -54.409 2.926   1.00 27.47  ? 304 LEU A C     1 
ATOM   2269 O O     . LEU A 1 306 ? 10.816  -54.716 3.643   1.00 29.43  ? 304 LEU A O     1 
ATOM   2270 C CB    . LEU A 1 306 ? 9.374   -55.716 0.812   1.00 29.74  ? 304 LEU A CB    1 
ATOM   2271 C CG    . LEU A 1 306 ? 10.849  -55.840 0.458   1.00 30.66  ? 304 LEU A CG    1 
ATOM   2272 C CD1   . LEU A 1 306 ? 11.493  -57.003 1.163   1.00 30.50  ? 304 LEU A CD1   1 
ATOM   2273 C CD2   . LEU A 1 306 ? 11.032  -55.967 -1.060  1.00 35.77  ? 304 LEU A CD2   1 
ATOM   2274 N N     . ALA A 1 307 ? 9.567   -53.149 2.624   1.00 25.50  ? 305 ALA A N     1 
ATOM   2275 C CA    . ALA A 1 307 ? 10.310  -51.946 3.056   1.00 28.08  ? 305 ALA A CA    1 
ATOM   2276 C C     . ALA A 1 307 ? 10.447  -51.919 4.594   1.00 27.23  ? 305 ALA A C     1 
ATOM   2277 O O     . ALA A 1 307 ? 11.571  -51.731 5.131   1.00 25.78  ? 305 ALA A O     1 
ATOM   2278 C CB    . ALA A 1 307 ? 9.603   -50.701 2.543   1.00 29.03  ? 305 ALA A CB    1 
ATOM   2279 N N     . HIS A 1 308 ? 9.348   -52.142 5.296   1.00 27.91  ? 306 HIS A N     1 
ATOM   2280 C CA    . HIS A 1 308 ? 9.302   -52.109 6.782   1.00 27.45  ? 306 HIS A CA    1 
ATOM   2281 C C     . HIS A 1 308 ? 10.186  -53.209 7.371   1.00 28.78  ? 306 HIS A C     1 
ATOM   2282 O O     . HIS A 1 308 ? 10.871  -52.906 8.357   1.00 30.19  ? 306 HIS A O     1 
ATOM   2283 C CB    . HIS A 1 308 ? 7.853   -52.122 7.252   1.00 25.80  ? 306 HIS A CB    1 
ATOM   2284 C CG    . HIS A 1 308 ? 7.183   -50.854 6.855   1.00 26.85  ? 306 HIS A CG    1 
ATOM   2285 N ND1   . HIS A 1 308 ? 7.753   -49.629 7.100   1.00 25.17  ? 306 HIS A ND1   1 
ATOM   2286 C CD2   . HIS A 1 308 ? 6.031   -50.612 6.197   1.00 27.86  ? 306 HIS A CD2   1 
ATOM   2287 C CE1   . HIS A 1 308 ? 6.958   -48.681 6.632   1.00 28.00  ? 306 HIS A CE1   1 
ATOM   2288 N NE2   . HIS A 1 308 ? 5.898   -49.254 6.078   1.00 27.07  ? 306 HIS A NE2   1 
ATOM   2289 N N     . ALA A 1 309 ? 10.147  -54.429 6.828   1.00 26.74  ? 307 ALA A N     1 
ATOM   2290 C CA    . ALA A 1 309 ? 11.015  -55.554 7.255   1.00 28.01  ? 307 ALA A CA    1 
ATOM   2291 C C     . ALA A 1 309 ? 12.491  -55.215 7.009   1.00 28.06  ? 307 ALA A C     1 
ATOM   2292 O O     . ALA A 1 309 ? 13.323  -55.485 7.895   1.00 28.65  ? 307 ALA A O     1 
ATOM   2293 C CB    . ALA A 1 309 ? 10.638  -56.810 6.509   1.00 31.12  ? 307 ALA A CB    1 
ATOM   2294 N N     . GLU A 1 310 ? 12.801  -54.680 5.825   1.00 28.28  ? 308 GLU A N     1 
ATOM   2295 C CA    . GLU A 1 310 ? 14.162  -54.215 5.452   1.00 29.83  ? 308 GLU A CA    1 
ATOM   2296 C C     . GLU A 1 310 ? 14.697  -53.169 6.450   1.00 30.50  ? 308 GLU A C     1 
ATOM   2297 O O     . GLU A 1 310 ? 15.879  -53.309 6.865   1.00 29.15  ? 308 GLU A O     1 
ATOM   2298 C CB    . GLU A 1 310 ? 14.163  -53.614 4.039   1.00 31.35  ? 308 GLU A CB    1 
ATOM   2299 C CG    . GLU A 1 310 ? 15.556  -53.226 3.560   1.00 30.41  ? 308 GLU A CG    1 
ATOM   2300 C CD    . GLU A 1 310 ? 16.549  -54.385 3.592   1.00 32.05  ? 308 GLU A CD    1 
ATOM   2301 O OE1   . GLU A 1 310 ? 17.758  -54.163 3.825   1.00 33.43  ? 308 GLU A OE1   1 
ATOM   2302 O OE2   . GLU A 1 310 ? 16.107  -55.526 3.401   1.00 34.70  ? 308 GLU A OE2   1 
ATOM   2303 N N     . VAL A 1 311 ? 13.911  -52.137 6.772   1.00 29.92  ? 309 VAL A N     1 
ATOM   2304 C CA    . VAL A 1 311 ? 14.369  -51.024 7.661   1.00 31.33  ? 309 VAL A CA    1 
ATOM   2305 C C     . VAL A 1 311 ? 14.564  -51.539 9.094   1.00 33.32  ? 309 VAL A C     1 
ATOM   2306 O O     . VAL A 1 311 ? 15.513  -51.093 9.743   1.00 37.33  ? 309 VAL A O     1 
ATOM   2307 C CB    . VAL A 1 311 ? 13.416  -49.812 7.594   1.00 31.06  ? 309 VAL A CB    1 
ATOM   2308 C CG1   . VAL A 1 311 ? 13.695  -48.792 8.685   1.00 29.89  ? 309 VAL A CG1   1 
ATOM   2309 C CG2   . VAL A 1 311 ? 13.435  -49.157 6.224   1.00 33.49  ? 309 VAL A CG2   1 
ATOM   2310 N N     . GLY A 1 312 ? 13.709  -52.453 9.548   1.00 34.08  ? 310 GLY A N     1 
ATOM   2311 C CA    . GLY A 1 312 ? 13.866  -53.044 10.886  1.00 33.00  ? 310 GLY A CA    1 
ATOM   2312 C C     . GLY A 1 312 ? 15.116  -53.885 10.950  1.00 31.75  ? 310 GLY A C     1 
ATOM   2313 O O     . GLY A 1 312 ? 15.807  -53.822 11.965  1.00 30.53  ? 310 GLY A O     1 
ATOM   2314 N N     . PHE A 1 313 ? 15.383  -54.632 9.884   1.00 32.62  ? 311 PHE A N     1 
ATOM   2315 C CA    . PHE A 1 313 ? 16.604  -55.471 9.797   1.00 32.45  ? 311 PHE A CA    1 
ATOM   2316 C C     . PHE A 1 313 ? 17.865  -54.581 9.844   1.00 33.74  ? 311 PHE A C     1 
ATOM   2317 O O     . PHE A 1 313 ? 18.780  -54.890 10.673  1.00 32.50  ? 311 PHE A O     1 
ATOM   2318 C CB    . PHE A 1 313 ? 16.608  -56.375 8.559   1.00 30.62  ? 311 PHE A CB    1 
ATOM   2319 C CG    . PHE A 1 313 ? 17.860  -57.214 8.512   1.00 30.54  ? 311 PHE A CG    1 
ATOM   2320 C CD1   . PHE A 1 313 ? 18.007  -58.300 9.356   1.00 35.05  ? 311 PHE A CD1   1 
ATOM   2321 C CD2   . PHE A 1 313 ? 18.955  -56.828 7.766   1.00 29.68  ? 311 PHE A CD2   1 
ATOM   2322 C CE1   . PHE A 1 313 ? 19.181  -59.036 9.378   1.00 34.51  ? 311 PHE A CE1   1 
ATOM   2323 C CE2   . PHE A 1 313 ? 20.131  -57.562 7.797   1.00 28.45  ? 311 PHE A CE2   1 
ATOM   2324 C CZ    . PHE A 1 313 ? 20.235  -58.668 8.589   1.00 30.41  ? 311 PHE A CZ    1 
ATOM   2325 N N     . GLN A 1 314 ? 17.930  -53.522 9.021   1.00 31.72  ? 312 GLN A N     1 
ATOM   2326 C CA    . GLN A 1 314 ? 19.133  -52.629 8.925   1.00 34.54  ? 312 GLN A CA    1 
ATOM   2327 C C     . GLN A 1 314 ? 19.368  -51.936 10.266  1.00 32.72  ? 312 GLN A C     1 
ATOM   2328 O O     . GLN A 1 314 ? 20.515  -51.788 10.663  1.00 36.22  ? 312 GLN A O     1 
ATOM   2329 C CB    . GLN A 1 314 ? 19.010  -51.535 7.856   1.00 32.78  ? 312 GLN A CB    1 
ATOM   2330 C CG    . GLN A 1 314 ? 19.128  -52.051 6.429   1.00 33.93  ? 312 GLN A CG    1 
ATOM   2331 C CD    . GLN A 1 314 ? 19.079  -50.905 5.446   1.00 33.36  ? 312 GLN A CD    1 
ATOM   2332 O OE1   . GLN A 1 314 ? 19.551  -49.816 5.724   1.00 33.84  ? 312 GLN A OE1   1 
ATOM   2333 N NE2   . GLN A 1 314 ? 18.504  -51.127 4.279   1.00 35.89  ? 312 GLN A NE2   1 
ATOM   2334 N N     . GLY A 1 315 ? 18.316  -51.517 10.949  1.00 29.28  ? 313 GLY A N     1 
ATOM   2335 C CA    . GLY A 1 315 ? 18.532  -50.914 12.264  1.00 30.29  ? 313 GLY A CA    1 
ATOM   2336 C C     . GLY A 1 315 ? 18.977  -51.939 13.275  1.00 31.33  ? 313 GLY A C     1 
ATOM   2337 O O     . GLY A 1 315 ? 19.967  -51.681 13.954  1.00 33.32  ? 313 GLY A O     1 
ATOM   2338 N N     . GLY A 1 316 ? 18.272  -53.063 13.346  1.00 34.41  ? 314 GLY A N     1 
ATOM   2339 C CA    . GLY A 1 316 ? 18.551  -54.100 14.349  1.00 34.05  ? 314 GLY A CA    1 
ATOM   2340 C C     . GLY A 1 316 ? 19.934  -54.687 14.225  1.00 31.34  ? 314 GLY A C     1 
ATOM   2341 O O     . GLY A 1 316 ? 20.574  -54.851 15.258  1.00 34.96  ? 314 GLY A O     1 
ATOM   2342 N N     . ILE A 1 317 ? 20.404  -55.027 13.028  1.00 29.91  ? 315 ILE A N     1 
ATOM   2343 C CA    . ILE A 1 317 ? 21.737  -55.705 12.914  1.00 33.25  ? 315 ILE A CA    1 
ATOM   2344 C C     . ILE A 1 317 ? 22.841  -54.753 13.389  1.00 32.96  ? 315 ILE A C     1 
ATOM   2345 O O     . ILE A 1 317 ? 23.726  -55.201 14.119  1.00 35.01  ? 315 ILE A O     1 
ATOM   2346 C CB    . ILE A 1 317 ? 22.021  -56.238 11.493  1.00 33.12  ? 315 ILE A CB    1 
ATOM   2347 C CG1   . ILE A 1 317 ? 23.300  -57.076 11.456  1.00 37.84  ? 315 ILE A CG1   1 
ATOM   2348 C CG2   . ILE A 1 317 ? 22.048  -55.118 10.465  1.00 35.57  ? 315 ILE A CG2   1 
ATOM   2349 C CD1   . ILE A 1 317 ? 23.360  -58.147 12.518  1.00 40.92  ? 315 ILE A CD1   1 
ATOM   2350 N N     . ALA A 1 318 ? 22.764  -53.488 12.996  1.00 29.63  ? 316 ALA A N     1 
ATOM   2351 C CA    . ALA A 1 318 ? 23.756  -52.483 13.418  1.00 28.89  ? 316 ALA A CA    1 
ATOM   2352 C C     . ALA A 1 318 ? 23.759  -52.343 14.946  1.00 31.05  ? 316 ALA A C     1 
ATOM   2353 O O     . ALA A 1 318 ? 24.842  -52.383 15.526  1.00 30.55  ? 316 ALA A O     1 
ATOM   2354 C CB    . ALA A 1 318 ? 23.445  -51.189 12.733  1.00 27.14  ? 316 ALA A CB    1 
ATOM   2355 N N     . TYR A 1 319 ? 22.585  -52.207 15.559  1.00 30.07  ? 317 TYR A N     1 
ATOM   2356 C CA    . TYR A 1 319 ? 22.480  -52.059 17.035  1.00 32.37  ? 317 TYR A CA    1 
ATOM   2357 C C     . TYR A 1 319 ? 22.897  -53.348 17.754  1.00 30.90  ? 317 TYR A C     1 
ATOM   2358 O O     . TYR A 1 319 ? 23.558  -53.231 18.786  1.00 30.93  ? 317 TYR A O     1 
ATOM   2359 C CB    . TYR A 1 319 ? 21.069  -51.623 17.435  1.00 32.88  ? 317 TYR A CB    1 
ATOM   2360 C CG    . TYR A 1 319 ? 20.949  -51.029 18.813  1.00 31.78  ? 317 TYR A CG    1 
ATOM   2361 C CD1   . TYR A 1 319 ? 21.452  -49.771 19.090  1.00 35.08  ? 317 TYR A CD1   1 
ATOM   2362 C CD2   . TYR A 1 319 ? 20.329  -51.718 19.839  1.00 30.90  ? 317 TYR A CD2   1 
ATOM   2363 C CE1   . TYR A 1 319 ? 21.346  -49.211 20.351  1.00 32.78  ? 317 TYR A CE1   1 
ATOM   2364 C CE2   . TYR A 1 319 ? 20.216  -51.174 21.107  1.00 31.24  ? 317 TYR A CE2   1 
ATOM   2365 C CZ    . TYR A 1 319 ? 20.726  -49.915 21.364  1.00 32.88  ? 317 TYR A CZ    1 
ATOM   2366 O OH    . TYR A 1 319 ? 20.623  -49.364 22.606  1.00 34.49  ? 317 TYR A OH    1 
ATOM   2367 N N     . ALA A 1 320 ? 22.532  -54.512 17.220  1.00 28.28  ? 318 ALA A N     1 
ATOM   2368 C CA    . ALA A 1 320 ? 22.860  -55.812 17.847  1.00 29.60  ? 318 ALA A CA    1 
ATOM   2369 C C     . ALA A 1 320 ? 24.376  -55.999 17.903  1.00 31.59  ? 318 ALA A C     1 
ATOM   2370 O O     . ALA A 1 320 ? 24.854  -56.642 18.836  1.00 35.20  ? 318 ALA A O     1 
ATOM   2371 C CB    . ALA A 1 320 ? 22.190  -56.928 17.096  1.00 27.27  ? 318 ALA A CB    1 
ATOM   2372 N N     . ARG A 1 321 ? 25.086  -55.453 16.930  1.00 32.99  ? 319 ARG A N     1 
ATOM   2373 C CA    A ARG A 1 321 ? 26.571  -55.539 16.905  0.50 34.67  ? 319 ARG A CA    1 
ATOM   2374 C CA    B ARG A 1 321 ? 26.571  -55.544 16.913  0.50 34.67  ? 319 ARG A CA    1 
ATOM   2375 C C     . ARG A 1 321 ? 27.336  -54.465 17.724  1.00 33.23  ? 319 ARG A C     1 
ATOM   2376 O O     . ARG A 1 321 ? 28.562  -54.509 18.188  1.00 35.37  ? 319 ARG A O     1 
ATOM   2377 C CB    A ARG A 1 321 ? 27.033  -55.468 15.445  0.50 34.21  ? 319 ARG A CB    1 
ATOM   2378 C CB    B ARG A 1 321 ? 27.034  -55.522 15.453  0.50 34.21  ? 319 ARG A CB    1 
ATOM   2379 C CG    A ARG A 1 321 ? 26.643  -56.659 14.581  0.50 33.49  ? 319 ARG A CG    1 
ATOM   2380 C CG    B ARG A 1 321 ? 26.509  -56.678 14.614  0.50 33.49  ? 319 ARG A CG    1 
ATOM   2381 C CD    A ARG A 1 321 ? 26.953  -56.360 13.125  0.50 30.64  ? 319 ARG A CD    1 
ATOM   2382 C CD    B ARG A 1 321 ? 27.331  -56.896 13.359  0.50 30.64  ? 319 ARG A CD    1 
ATOM   2383 N NE    A ARG A 1 321 ? 26.806  -57.483 12.208  0.50 30.60  ? 319 ARG A NE    1 
ATOM   2384 N NE    B ARG A 1 321 ? 28.612  -57.521 13.660  0.50 30.60  ? 319 ARG A NE    1 
ATOM   2385 C CZ    A ARG A 1 321 ? 26.702  -57.368 10.886  0.50 25.75  ? 319 ARG A CZ    1 
ATOM   2386 C CZ    B ARG A 1 321 ? 29.634  -57.597 12.816  0.50 25.75  ? 319 ARG A CZ    1 
ATOM   2387 N NH1   A ARG A 1 321 ? 26.571  -58.447 10.133  0.50 21.16  ? 319 ARG A NH1   1 
ATOM   2388 N NH1   B ARG A 1 321 ? 29.533  -57.084 11.603  0.50 21.16  ? 319 ARG A NH1   1 
ATOM   2389 N NH2   A ARG A 1 321 ? 26.722  -56.174 10.322  0.50 21.49  ? 319 ARG A NH2   1 
ATOM   2390 N NH2   B ARG A 1 321 ? 30.755  -58.187 13.189  0.50 21.49  ? 319 ARG A NH2   1 
ATOM   2391 N N     . GLU A 1 322 ? 26.607  -53.397 18.035  1.00 34.39  ? 320 GLU A N     1 
ATOM   2392 C CA    . GLU A 1 322 ? 27.247  -52.277 18.772  1.00 37.11  ? 320 GLU A CA    1 
ATOM   2393 C C     . GLU A 1 322 ? 26.845  -52.283 20.252  1.00 37.21  ? 320 GLU A C     1 
ATOM   2394 O O     . GLU A 1 322 ? 27.715  -52.026 21.083  1.00 39.62  ? 320 GLU A O     1 
ATOM   2395 C CB    . GLU A 1 322 ? 26.879  -50.964 18.088  1.00 41.59  ? 320 GLU A CB    1 
ATOM   2396 C CG    . GLU A 1 322 ? 27.262  -49.740 18.894  1.00 54.28  ? 320 GLU A CG    1 
ATOM   2397 C CD    . GLU A 1 322 ? 26.633  -48.441 18.426  1.00 64.26  ? 320 GLU A CD    1 
ATOM   2398 O OE1   . GLU A 1 322 ? 27.317  -47.682 17.715  1.00 78.91  ? 320 GLU A OE1   1 
ATOM   2399 O OE2   . GLU A 1 322 ? 25.465  -48.189 18.776  1.00 61.17  ? 320 GLU A OE2   1 
ATOM   2400 N N     . ARG A 1 323 ? 25.584  -52.574 20.559  1.00 36.56  ? 321 ARG A N     1 
ATOM   2401 C CA    . ARG A 1 323 ? 25.098  -52.532 21.963  1.00 34.56  ? 321 ARG A CA    1 
ATOM   2402 C C     . ARG A 1 323 ? 25.683  -53.668 22.798  1.00 35.30  ? 321 ARG A C     1 
ATOM   2403 O O     . ARG A 1 323 ? 25.478  -54.831 22.447  1.00 33.07  ? 321 ARG A O     1 
ATOM   2404 C CB    . ARG A 1 323 ? 23.569  -52.546 22.066  1.00 33.78  ? 321 ARG A CB    1 
ATOM   2405 C CG    . ARG A 1 323 ? 23.035  -52.530 23.489  1.00 31.95  ? 321 ARG A CG    1 
ATOM   2406 C CD    . ARG A 1 323 ? 23.184  -51.187 24.174  1.00 31.14  ? 321 ARG A CD    1 
ATOM   2407 N NE    . ARG A 1 323 ? 22.406  -51.139 25.402  1.00 33.90  ? 321 ARG A NE    1 
ATOM   2408 C CZ    . ARG A 1 323 ? 22.281  -50.079 26.187  1.00 30.44  ? 321 ARG A CZ    1 
ATOM   2409 N NH1   . ARG A 1 323 ? 22.894  -48.950 25.884  1.00 29.85  ? 321 ARG A NH1   1 
ATOM   2410 N NH2   . ARG A 1 323 ? 21.546  -50.152 27.279  1.00 36.77  ? 321 ARG A NH2   1 
ATOM   2411 N N     . LEU A 1 324 ? 26.367  -53.308 23.875  1.00 32.62  ? 322 LEU A N     1 
ATOM   2412 C CA    . LEU A 1 324 ? 26.897  -54.297 24.836  1.00 35.72  ? 322 LEU A CA    1 
ATOM   2413 C C     . LEU A 1 324 ? 25.944  -54.367 26.032  1.00 34.83  ? 322 LEU A C     1 
ATOM   2414 O O     . LEU A 1 324 ? 25.713  -53.310 26.674  1.00 36.59  ? 322 LEU A O     1 
ATOM   2415 C CB    . LEU A 1 324 ? 28.294  -53.844 25.260  1.00 41.38  ? 322 LEU A CB    1 
ATOM   2416 C CG    . LEU A 1 324 ? 29.258  -53.465 24.136  1.00 43.60  ? 322 LEU A CG    1 
ATOM   2417 C CD1   . LEU A 1 324 ? 30.583  -52.969 24.721  1.00 42.08  ? 322 LEU A CD1   1 
ATOM   2418 C CD2   . LEU A 1 324 ? 29.487  -54.654 23.210  1.00 41.66  ? 322 LEU A CD2   1 
ATOM   2419 N N     . GLN A 1 325 ? 25.359  -55.537 26.264  1.00 32.74  ? 323 GLN A N     1 
ATOM   2420 C CA    . GLN A 1 325 ? 24.477  -55.745 27.436  1.00 35.22  ? 323 GLN A CA    1 
ATOM   2421 C C     . GLN A 1 325 ? 24.553  -57.217 27.828  1.00 34.17  ? 323 GLN A C     1 
ATOM   2422 O O     . GLN A 1 325 ? 24.300  -58.064 26.969  1.00 29.75  ? 323 GLN A O     1 
ATOM   2423 C CB    . GLN A 1 325 ? 23.022  -55.346 27.187  1.00 40.29  ? 323 GLN A CB    1 
ATOM   2424 C CG    . GLN A 1 325 ? 22.763  -53.851 27.215  1.00 44.49  ? 323 GLN A CG    1 
ATOM   2425 C CD    . GLN A 1 325 ? 22.830  -53.251 28.596  1.00 38.58  ? 323 GLN A CD    1 
ATOM   2426 O OE1   . GLN A 1 325 ? 22.015  -53.535 29.466  1.00 39.55  ? 323 GLN A OE1   1 
ATOM   2427 N NE2   . GLN A 1 325 ? 23.809  -52.390 28.796  1.00 40.91  ? 323 GLN A NE2   1 
ATOM   2428 N N     . MET A 1 326 ? 24.930  -57.477 29.076  1.00 34.11  ? 324 MET A N     1 
ATOM   2429 C CA    . MET A 1 326 ? 25.012  -58.862 29.601  1.00 35.62  ? 324 MET A CA    1 
ATOM   2430 C C     . MET A 1 326 ? 26.124  -59.653 28.906  1.00 35.18  ? 324 MET A C     1 
ATOM   2431 O O     . MET A 1 326 ? 26.952  -59.043 28.218  1.00 35.17  ? 324 MET A O     1 
ATOM   2432 C CB    . MET A 1 326 ? 23.665  -59.581 29.466  1.00 35.29  ? 324 MET A CB    1 
ATOM   2433 C CG    . MET A 1 326 ? 22.516  -58.852 30.140  1.00 37.16  ? 324 MET A CG    1 
ATOM   2434 S SD    . MET A 1 326 ? 22.796  -58.507 31.894  1.00 42.03  ? 324 MET A SD    1 
ATOM   2435 C CE    . MET A 1 326 ? 21.921  -59.877 32.645  1.00 36.83  ? 324 MET A CE    1 
ATOM   2436 N N     . ARG A 1 327 ? 26.129  -60.967 29.108  1.00 41.37  ? 325 ARG A N     1 
ATOM   2437 C CA    . ARG A 1 327 ? 27.197  -61.831 28.550  1.00 41.17  ? 325 ARG A CA    1 
ATOM   2438 C C     . ARG A 1 327 ? 26.580  -63.088 27.944  1.00 38.36  ? 325 ARG A C     1 
ATOM   2439 O O     . ARG A 1 327 ? 25.489  -63.463 28.371  1.00 34.68  ? 325 ARG A O     1 
ATOM   2440 C CB    . ARG A 1 327 ? 28.207  -62.187 29.644  1.00 41.24  ? 325 ARG A CB    1 
ATOM   2441 C CG    . ARG A 1 327 ? 28.932  -60.995 30.246  1.00 39.69  ? 325 ARG A CG    1 
ATOM   2442 C CD    . ARG A 1 327 ? 29.967  -60.472 29.279  1.00 41.96  ? 325 ARG A CD    1 
ATOM   2443 N NE    . ARG A 1 327 ? 30.954  -59.663 29.967  1.00 40.00  ? 325 ARG A NE    1 
ATOM   2444 C CZ    . ARG A 1 327 ? 31.959  -59.047 29.370  1.00 43.63  ? 325 ARG A CZ    1 
ATOM   2445 N NH1   . ARG A 1 327 ? 32.115  -59.149 28.062  1.00 44.19  ? 325 ARG A NH1   1 
ATOM   2446 N NH2   . ARG A 1 327 ? 32.806  -58.332 30.083  1.00 46.77  ? 325 ARG A NH2   1 
ATOM   2447 N N     . SER A 1 328 ? 27.271  -63.701 26.984  1.00 41.47  ? 326 SER A N     1 
ATOM   2448 C CA    . SER A 1 328 ? 26.775  -64.917 26.297  1.00 39.26  ? 326 SER A CA    1 
ATOM   2449 C C     . SER A 1 328 ? 26.438  -65.936 27.372  1.00 39.52  ? 326 SER A C     1 
ATOM   2450 O O     . SER A 1 328 ? 27.092  -65.890 28.401  1.00 43.24  ? 326 SER A O     1 
ATOM   2451 C CB    . SER A 1 328 ? 27.801  -65.447 25.346  1.00 39.30  ? 326 SER A CB    1 
ATOM   2452 O OG    . SER A 1 328 ? 27.702  -66.852 25.254  1.00 40.01  ? 326 SER A OG    1 
ATOM   2453 N N     . LEU A 1 329 ? 25.486  -66.836 27.140  1.00 42.67  ? 327 LEU A N     1 
ATOM   2454 C CA    . LEU A 1 329 ? 25.199  -67.923 28.111  1.00 41.02  ? 327 LEU A CA    1 
ATOM   2455 C C     . LEU A 1 329 ? 26.370  -68.916 28.218  1.00 41.95  ? 327 LEU A C     1 
ATOM   2456 O O     . LEU A 1 329 ? 26.352  -69.652 29.189  1.00 43.03  ? 327 LEU A O     1 
ATOM   2457 C CB    . LEU A 1 329 ? 23.930  -68.658 27.693  1.00 41.32  ? 327 LEU A CB    1 
ATOM   2458 C CG    . LEU A 1 329 ? 22.668  -67.831 27.850  1.00 42.83  ? 327 LEU A CG    1 
ATOM   2459 C CD1   . LEU A 1 329 ? 21.558  -68.371 26.961  1.00 40.95  ? 327 LEU A CD1   1 
ATOM   2460 C CD2   . LEU A 1 329 ? 22.230  -67.805 29.313  1.00 41.84  ? 327 LEU A CD2   1 
ATOM   2461 N N     . THR A 1 330 ? 27.297  -68.990 27.248  1.00 41.66  ? 328 THR A N     1 
ATOM   2462 C CA    . THR A 1 330 ? 28.421  -69.969 27.201  1.00 39.42  ? 328 THR A CA    1 
ATOM   2463 C C     . THR A 1 330 ? 29.748  -69.283 27.549  1.00 42.08  ? 328 THR A C     1 
ATOM   2464 O O     . THR A 1 330 ? 30.758  -69.709 27.025  1.00 42.74  ? 328 THR A O     1 
ATOM   2465 C CB    . THR A 1 330 ? 28.557  -70.652 25.829  1.00 41.38  ? 328 THR A CB    1 
ATOM   2466 O OG1   . THR A 1 330 ? 28.602  -69.684 24.784  1.00 38.54  ? 328 THR A OG1   1 
ATOM   2467 C CG2   . THR A 1 330 ? 27.438  -71.615 25.508  1.00 42.63  ? 328 THR A CG2   1 
ATOM   2468 N N     . GLY A 1 331 ? 29.750  -68.273 28.416  1.00 43.90  ? 329 GLY A N     1 
ATOM   2469 C CA    . GLY A 1 331 ? 30.970  -67.575 28.863  1.00 47.84  ? 329 GLY A CA    1 
ATOM   2470 C C     . GLY A 1 331 ? 31.229  -66.319 28.031  1.00 49.97  ? 329 GLY A C     1 
ATOM   2471 O O     . GLY A 1 331 ? 30.928  -66.294 26.842  1.00 48.92  ? 329 GLY A O     1 
ATOM   2472 N N     . PRO A 1 332 ? 31.798  -65.244 28.624  1.00 47.99  ? 330 PRO A N     1 
ATOM   2473 C CA    . PRO A 1 332 ? 31.966  -63.974 27.922  1.00 46.56  ? 330 PRO A CA    1 
ATOM   2474 C C     . PRO A 1 332 ? 32.693  -64.133 26.582  1.00 48.40  ? 330 PRO A C     1 
ATOM   2475 O O     . PRO A 1 332 ? 33.763  -64.659 26.597  1.00 49.12  ? 330 PRO A O     1 
ATOM   2476 C CB    . PRO A 1 332 ? 32.780  -63.131 28.918  1.00 45.73  ? 330 PRO A CB    1 
ATOM   2477 C CG    . PRO A 1 332 ? 32.366  -63.671 30.265  1.00 48.31  ? 330 PRO A CG    1 
ATOM   2478 C CD    . PRO A 1 332 ? 32.264  -65.168 30.024  1.00 52.26  ? 330 PRO A CD    1 
ATOM   2479 N N     . LYS A 1 333 ? 32.075  -63.666 25.492  1.00 45.87  ? 331 LYS A N     1 
ATOM   2480 C CA    . LYS A 1 333 ? 32.622  -63.721 24.108  1.00 46.88  ? 331 LYS A CA    1 
ATOM   2481 C C     . LYS A 1 333 ? 33.486  -62.482 23.827  1.00 45.91  ? 331 LYS A C     1 
ATOM   2482 O O     . LYS A 1 333 ? 34.213  -62.500 22.858  1.00 47.30  ? 331 LYS A O     1 
ATOM   2483 C CB    . LYS A 1 333 ? 31.502  -63.804 23.058  1.00 43.15  ? 331 LYS A CB    1 
ATOM   2484 C CG    . LYS A 1 333 ? 30.611  -65.032 23.145  1.00 42.49  ? 331 LYS A CG    1 
ATOM   2485 C CD    . LYS A 1 333 ? 31.308  -66.304 22.694  1.00 42.44  ? 331 LYS A CD    1 
ATOM   2486 C CE    . LYS A 1 333 ? 30.557  -67.565 23.060  1.00 41.15  ? 331 LYS A CE    1 
ATOM   2487 N NZ    . LYS A 1 333 ? 30.552  -67.789 24.526  1.00 42.29  ? 331 LYS A NZ    1 
ATOM   2488 N N     . ALA A 1 334 ? 33.383  -61.420 24.615  1.00 46.47  ? 332 ALA A N     1 
ATOM   2489 C CA    . ALA A 1 334 ? 34.189  -60.194 24.436  1.00 44.71  ? 332 ALA A CA    1 
ATOM   2490 C C     . ALA A 1 334 ? 34.673  -59.769 25.810  1.00 46.99  ? 332 ALA A C     1 
ATOM   2491 O O     . ALA A 1 334 ? 34.279  -58.694 26.273  1.00 50.45  ? 332 ALA A O     1 
ATOM   2492 C CB    . ALA A 1 334 ? 33.374  -59.115 23.765  1.00 44.95  ? 332 ALA A CB    1 
ATOM   2493 N N     . PRO A 1 335 ? 35.526  -60.609 26.466  1.00 48.09  ? 333 PRO A N     1 
ATOM   2494 C CA    . PRO A 1 335 ? 35.935  -60.413 27.862  1.00 49.17  ? 333 PRO A CA    1 
ATOM   2495 C C     . PRO A 1 335 ? 36.760  -59.133 28.082  1.00 49.93  ? 333 PRO A C     1 
ATOM   2496 O O     . PRO A 1 335 ? 36.776  -58.608 29.206  1.00 47.45  ? 333 PRO A O     1 
ATOM   2497 C CB    . PRO A 1 335 ? 36.774  -61.656 28.199  1.00 48.49  ? 333 PRO A CB    1 
ATOM   2498 C CG    . PRO A 1 335 ? 37.264  -62.157 26.851  1.00 48.00  ? 333 PRO A CG    1 
ATOM   2499 C CD    . PRO A 1 335 ? 36.186  -61.780 25.858  1.00 48.45  ? 333 PRO A CD    1 
ATOM   2500 N N     . GLU A 1 336 ? 37.393  -58.646 27.008  1.00 49.23  ? 334 GLU A N     1 
ATOM   2501 C CA    . GLU A 1 336 ? 38.195  -57.391 26.986  1.00 52.20  ? 334 GLU A CA    1 
ATOM   2502 C C     . GLU A 1 336 ? 37.253  -56.179 27.077  1.00 54.26  ? 334 GLU A C     1 
ATOM   2503 O O     . GLU A 1 336 ? 37.770  -55.054 27.264  1.00 52.99  ? 334 GLU A O     1 
ATOM   2504 C CB    . GLU A 1 336 ? 39.088  -57.348 25.741  1.00 52.57  ? 334 GLU A CB    1 
ATOM   2505 C CG    . GLU A 1 336 ? 38.357  -56.991 24.446  1.00 63.92  ? 334 GLU A CG    1 
ATOM   2506 C CD    . GLU A 1 336 ? 37.638  -58.089 23.651  1.00 67.06  ? 334 GLU A CD    1 
ATOM   2507 O OE1   . GLU A 1 336 ? 37.347  -59.189 24.191  1.00 61.50  ? 334 GLU A OE1   1 
ATOM   2508 O OE2   . GLU A 1 336 ? 37.369  -57.834 22.466  1.00 68.24  ? 334 GLU A OE2   1 
ATOM   2509 N N     . LYS A 1 337 ? 35.939  -56.389 26.917  1.00 48.83  ? 335 LYS A N     1 
ATOM   2510 C CA    . LYS A 1 337 ? 34.910  -55.319 26.970  1.00 44.78  ? 335 LYS A CA    1 
ATOM   2511 C C     . LYS A 1 337 ? 34.066  -55.507 28.221  1.00 42.88  ? 335 LYS A C     1 
ATOM   2512 O O     . LYS A 1 337 ? 34.004  -56.609 28.773  1.00 43.16  ? 335 LYS A O     1 
ATOM   2513 C CB    . LYS A 1 337 ? 34.035  -55.362 25.719  1.00 47.08  ? 335 LYS A CB    1 
ATOM   2514 C CG    . LYS A 1 337 ? 34.732  -54.978 24.424  1.00 46.38  ? 335 LYS A CG    1 
ATOM   2515 C CD    . LYS A 1 337 ? 33.853  -55.244 23.240  1.00 44.94  ? 335 LYS A CD    1 
ATOM   2516 C CE    . LYS A 1 337 ? 34.594  -55.113 21.939  1.00 46.61  ? 335 LYS A CE    1 
ATOM   2517 N NZ    . LYS A 1 337 ? 33.709  -54.578 20.891  1.00 48.68  ? 335 LYS A NZ    1 
ATOM   2518 N N     . PRO A 1 338 ? 33.345  -54.458 28.671  1.00 39.19  ? 336 PRO A N     1 
ATOM   2519 C CA    . PRO A 1 338 ? 32.556  -54.550 29.901  1.00 38.81  ? 336 PRO A CA    1 
ATOM   2520 C C     . PRO A 1 338 ? 31.284  -55.423 29.764  1.00 41.16  ? 336 PRO A C     1 
ATOM   2521 O O     . PRO A 1 338 ? 30.804  -55.898 30.768  1.00 38.74  ? 336 PRO A O     1 
ATOM   2522 C CB    . PRO A 1 338 ? 32.189  -53.085 30.222  1.00 38.57  ? 336 PRO A CB    1 
ATOM   2523 C CG    . PRO A 1 338 ? 32.795  -52.221 29.104  1.00 38.19  ? 336 PRO A CG    1 
ATOM   2524 C CD    . PRO A 1 338 ? 33.197  -53.161 27.992  1.00 37.77  ? 336 PRO A CD    1 
ATOM   2525 N N     . ALA A 1 339 ? 30.818  -55.617 28.527  1.00 39.28  ? 337 ALA A N     1 
ATOM   2526 C CA    . ALA A 1 339 ? 29.680  -56.524 28.244  1.00 38.45  ? 337 ALA A CA    1 
ATOM   2527 C C     . ALA A 1 339 ? 29.844  -57.079 26.827  1.00 37.26  ? 337 ALA A C     1 
ATOM   2528 O O     . ALA A 1 339 ? 30.724  -56.599 26.107  1.00 35.67  ? 337 ALA A O     1 
ATOM   2529 C CB    . ALA A 1 339 ? 28.351  -55.839 28.423  1.00 33.73  ? 337 ALA A CB    1 
ATOM   2530 N N     . ASP A 1 340 ? 29.032  -58.066 26.466  1.00 33.11  ? 338 ASP A N     1 
ATOM   2531 C CA    . ASP A 1 340 ? 29.114  -58.698 25.128  1.00 32.01  ? 338 ASP A CA    1 
ATOM   2532 C C     . ASP A 1 340 ? 28.115  -58.025 24.181  1.00 31.83  ? 338 ASP A C     1 
ATOM   2533 O O     . ASP A 1 340 ? 27.067  -57.588 24.660  1.00 34.83  ? 338 ASP A O     1 
ATOM   2534 C CB    . ASP A 1 340 ? 28.865  -60.201 25.238  1.00 35.32  ? 338 ASP A CB    1 
ATOM   2535 C CG    . ASP A 1 340 ? 30.015  -61.009 25.802  1.00 35.49  ? 338 ASP A CG    1 
ATOM   2536 O OD1   . ASP A 1 340 ? 31.091  -60.432 26.008  1.00 42.13  ? 338 ASP A OD1   1 
ATOM   2537 O OD2   . ASP A 1 340 ? 29.816  -62.209 26.024  1.00 34.08  ? 338 ASP A OD2   1 
ATOM   2538 N N     . PRO A 1 341 ? 28.371  -57.964 22.854  1.00 32.25  ? 339 PRO A N     1 
ATOM   2539 C CA    . PRO A 1 341 ? 27.376  -57.439 21.915  1.00 33.40  ? 339 PRO A CA    1 
ATOM   2540 C C     . PRO A 1 341 ? 26.082  -58.246 22.090  1.00 32.99  ? 339 PRO A C     1 
ATOM   2541 O O     . PRO A 1 341 ? 26.181  -59.422 22.287  1.00 33.83  ? 339 PRO A O     1 
ATOM   2542 C CB    . PRO A 1 341 ? 28.027  -57.593 20.536  1.00 31.08  ? 339 PRO A CB    1 
ATOM   2543 C CG    . PRO A 1 341 ? 29.128  -58.598 20.747  1.00 33.92  ? 339 PRO A CG    1 
ATOM   2544 C CD    . PRO A 1 341 ? 29.603  -58.355 22.161  1.00 33.35  ? 339 PRO A CD    1 
ATOM   2545 N N     . ILE A 1 342 ? 24.917  -57.603 21.979  1.00 34.36  ? 340 ILE A N     1 
ATOM   2546 C CA    . ILE A 1 342 ? 23.631  -58.308 22.294  1.00 31.29  ? 340 ILE A CA    1 
ATOM   2547 C C     . ILE A 1 342 ? 23.368  -59.394 21.242  1.00 30.43  ? 340 ILE A C     1 
ATOM   2548 O O     . ILE A 1 342 ? 22.641  -60.351 21.549  1.00 30.00  ? 340 ILE A O     1 
ATOM   2549 C CB    . ILE A 1 342 ? 22.440  -57.343 22.491  1.00 31.63  ? 340 ILE A CB    1 
ATOM   2550 C CG1   . ILE A 1 342 ? 22.158  -56.487 21.257  1.00 32.72  ? 340 ILE A CG1   1 
ATOM   2551 C CG2   . ILE A 1 342 ? 22.621  -56.482 23.747  1.00 33.57  ? 340 ILE A CG2   1 
ATOM   2552 C CD1   . ILE A 1 342 ? 20.874  -55.691 21.329  1.00 32.31  ? 340 ILE A CD1   1 
ATOM   2553 N N     . ILE A 1 343 ? 24.072  -59.379 20.116  1.00 31.23  ? 341 ILE A N     1 
ATOM   2554 C CA    . ILE A 1 343 ? 23.965  -60.454 19.080  1.00 35.05  ? 341 ILE A CA    1 
ATOM   2555 C C     . ILE A 1 343 ? 24.417  -61.826 19.621  1.00 35.87  ? 341 ILE A C     1 
ATOM   2556 O O     . ILE A 1 343 ? 24.132  -62.822 18.961  1.00 39.19  ? 341 ILE A O     1 
ATOM   2557 C CB    . ILE A 1 343 ? 24.770  -60.065 17.822  1.00 32.92  ? 341 ILE A CB    1 
ATOM   2558 C CG1   . ILE A 1 343 ? 24.336  -60.879 16.600  1.00 36.43  ? 341 ILE A CG1   1 
ATOM   2559 C CG2   . ILE A 1 343 ? 26.265  -60.171 18.076  1.00 31.62  ? 341 ILE A CG2   1 
ATOM   2560 C CD1   . ILE A 1 343 ? 24.935  -60.411 15.295  1.00 33.44  ? 341 ILE A CD1   1 
ATOM   2561 N N     . VAL A 1 344 ? 25.104  -61.870 20.762  1.00 31.49  ? 342 VAL A N     1 
ATOM   2562 C CA    . VAL A 1 344 ? 25.546  -63.160 21.369  1.00 30.80  ? 342 VAL A CA    1 
ATOM   2563 C C     . VAL A 1 344 ? 24.332  -63.874 21.961  1.00 32.42  ? 342 VAL A C     1 
ATOM   2564 O O     . VAL A 1 344 ? 24.407  -65.089 22.157  1.00 32.85  ? 342 VAL A O     1 
ATOM   2565 C CB    . VAL A 1 344 ? 26.635  -62.934 22.432  1.00 33.55  ? 342 VAL A CB    1 
ATOM   2566 C CG1   . VAL A 1 344 ? 27.812  -62.146 21.883  1.00 33.09  ? 342 VAL A CG1   1 
ATOM   2567 C CG2   . VAL A 1 344 ? 26.082  -62.285 23.690  1.00 33.18  ? 342 VAL A CG2   1 
ATOM   2568 N N     . HIS A 1 345 ? 23.255  -63.139 22.210  1.00 30.33  ? 343 HIS A N     1 
ATOM   2569 C CA    . HIS A 1 345 ? 22.058  -63.715 22.874  1.00 32.84  ? 343 HIS A CA    1 
ATOM   2570 C C     . HIS A 1 345 ? 21.153  -64.403 21.853  1.00 31.09  ? 343 HIS A C     1 
ATOM   2571 O O     . HIS A 1 345 ? 20.828  -63.785 20.844  1.00 30.95  ? 343 HIS A O     1 
ATOM   2572 C CB    . HIS A 1 345 ? 21.298  -62.645 23.673  1.00 32.88  ? 343 HIS A CB    1 
ATOM   2573 C CG    . HIS A 1 345 ? 22.120  -61.853 24.629  1.00 34.71  ? 343 HIS A CG    1 
ATOM   2574 N ND1   . HIS A 1 345 ? 22.912  -62.442 25.588  1.00 39.50  ? 343 HIS A ND1   1 
ATOM   2575 C CD2   . HIS A 1 345 ? 22.252  -60.521 24.795  1.00 36.20  ? 343 HIS A CD2   1 
ATOM   2576 C CE1   . HIS A 1 345 ? 23.510  -61.506 26.294  1.00 35.50  ? 343 HIS A CE1   1 
ATOM   2577 N NE2   . HIS A 1 345 ? 23.122  -60.323 25.827  1.00 34.67  ? 343 HIS A NE2   1 
ATOM   2578 N N     . PRO A 1 346 ? 20.740  -65.663 22.089  1.00 34.41  ? 344 PRO A N     1 
ATOM   2579 C CA    . PRO A 1 346 ? 19.916  -66.371 21.112  1.00 32.25  ? 344 PRO A CA    1 
ATOM   2580 C C     . PRO A 1 346 ? 18.644  -65.585 20.750  1.00 32.82  ? 344 PRO A C     1 
ATOM   2581 O O     . PRO A 1 346 ? 18.242  -65.622 19.619  1.00 32.43  ? 344 PRO A O     1 
ATOM   2582 C CB    . PRO A 1 346 ? 19.548  -67.692 21.818  1.00 32.94  ? 344 PRO A CB    1 
ATOM   2583 C CG    . PRO A 1 346 ? 20.633  -67.887 22.843  1.00 32.36  ? 344 PRO A CG    1 
ATOM   2584 C CD    . PRO A 1 346 ? 21.015  -66.488 23.280  1.00 33.94  ? 344 PRO A CD    1 
ATOM   2585 N N     . ASP A 1 347 ? 17.978  -64.959 21.724  1.00 33.61  ? 345 ASP A N     1 
ATOM   2586 C CA    . ASP A 1 347 ? 16.668  -64.299 21.465  1.00 34.95  ? 345 ASP A CA    1 
ATOM   2587 C C     . ASP A 1 347 ? 16.853  -63.121 20.473  1.00 37.24  ? 345 ASP A C     1 
ATOM   2588 O O     . ASP A 1 347 ? 16.002  -62.958 19.589  1.00 31.31  ? 345 ASP A O     1 
ATOM   2589 C CB    . ASP A 1 347 ? 15.994  -63.889 22.775  1.00 36.19  ? 345 ASP A CB    1 
ATOM   2590 C CG    . ASP A 1 347 ? 14.617  -63.291 22.546  1.00 35.99  ? 345 ASP A CG    1 
ATOM   2591 O OD1   . ASP A 1 347 ? 13.755  -64.002 22.000  1.00 39.99  ? 345 ASP A OD1   1 
ATOM   2592 O OD2   . ASP A 1 347 ? 14.461  -62.096 22.810  1.00 36.88  ? 345 ASP A OD2   1 
ATOM   2593 N N     . VAL A 1 348 ? 17.924  -62.325 20.617  1.00 34.72  ? 346 VAL A N     1 
ATOM   2594 C CA    . VAL A 1 348 ? 18.278  -61.229 19.673  1.00 32.72  ? 346 VAL A CA    1 
ATOM   2595 C C     . VAL A 1 348 ? 18.579  -61.825 18.292  1.00 32.15  ? 346 VAL A C     1 
ATOM   2596 O O     . VAL A 1 348 ? 18.133  -61.241 17.328  1.00 35.99  ? 346 VAL A O     1 
ATOM   2597 C CB    . VAL A 1 348 ? 19.437  -60.380 20.206  1.00 30.94  ? 346 VAL A CB    1 
ATOM   2598 C CG1   . VAL A 1 348 ? 19.928  -59.427 19.142  1.00 29.72  ? 346 VAL A CG1   1 
ATOM   2599 C CG2   . VAL A 1 348 ? 19.029  -59.630 21.458  1.00 30.37  ? 346 VAL A CG2   1 
ATOM   2600 N N     . ARG A 1 349 ? 19.244  -62.970 18.225  1.00 32.73  ? 347 ARG A N     1 
ATOM   2601 C CA    . ARG A 1 349 ? 19.465  -63.635 16.918  1.00 33.35  ? 347 ARG A CA    1 
ATOM   2602 C C     . ARG A 1 349 ? 18.110  -64.077 16.349  1.00 30.35  ? 347 ARG A C     1 
ATOM   2603 O O     . ARG A 1 349 ? 17.925  -63.971 15.144  1.00 31.68  ? 347 ARG A O     1 
ATOM   2604 C CB    . ARG A 1 349 ? 20.470  -64.785 17.059  1.00 32.63  ? 347 ARG A CB    1 
ATOM   2605 C CG    . ARG A 1 349 ? 21.920  -64.330 17.096  1.00 33.13  ? 347 ARG A CG    1 
ATOM   2606 C CD    . ARG A 1 349 ? 22.875  -65.369 17.640  1.00 34.87  ? 347 ARG A CD    1 
ATOM   2607 N NE    . ARG A 1 349 ? 24.236  -65.016 17.273  1.00 33.22  ? 347 ARG A NE    1 
ATOM   2608 C CZ    . ARG A 1 349 ? 24.851  -65.438 16.178  1.00 35.46  ? 347 ARG A CZ    1 
ATOM   2609 N NH1   . ARG A 1 349 ? 24.231  -66.248 15.339  1.00 35.26  ? 347 ARG A NH1   1 
ATOM   2610 N NH2   . ARG A 1 349 ? 26.087  -65.051 15.926  1.00 34.15  ? 347 ARG A NH2   1 
ATOM   2611 N N     . ARG A 1 350 ? 17.210  -64.538 17.212  1.00 27.35  ? 348 ARG A N     1 
ATOM   2612 C CA    . ARG A 1 350 ? 15.875  -64.975 16.744  1.00 32.78  ? 348 ARG A CA    1 
ATOM   2613 C C     . ARG A 1 350 ? 15.147  -63.775 16.102  1.00 29.16  ? 348 ARG A C     1 
ATOM   2614 O O     . ARG A 1 350 ? 14.558  -63.936 15.049  1.00 24.12  ? 348 ARG A O     1 
ATOM   2615 C CB    . ARG A 1 350 ? 15.073  -65.591 17.888  1.00 30.15  ? 348 ARG A CB    1 
ATOM   2616 C CG    . ARG A 1 350 ? 13.668  -65.973 17.456  1.00 32.04  ? 348 ARG A CG    1 
ATOM   2617 C CD    . ARG A 1 350 ? 12.746  -66.257 18.621  1.00 30.90  ? 348 ARG A CD    1 
ATOM   2618 N NE    . ARG A 1 350 ? 12.600  -65.161 19.567  1.00 32.39  ? 348 ARG A NE    1 
ATOM   2619 C CZ    . ARG A 1 350 ? 11.731  -64.142 19.455  1.00 32.91  ? 348 ARG A CZ    1 
ATOM   2620 N NH1   . ARG A 1 350 ? 10.927  -64.015 18.418  1.00 30.10  ? 348 ARG A NH1   1 
ATOM   2621 N NH2   . ARG A 1 350 ? 11.648  -63.241 20.406  1.00 33.92  ? 348 ARG A NH2   1 
ATOM   2622 N N     . MET A 1 351 ? 15.220  -62.593 16.696  1.00 30.22  ? 349 MET A N     1 
ATOM   2623 C CA    . MET A 1 351 ? 14.496  -61.404 16.160  1.00 31.66  ? 349 MET A CA    1 
ATOM   2624 C C     . MET A 1 351 ? 15.182  -60.972 14.866  1.00 31.23  ? 349 MET A C     1 
ATOM   2625 O O     . MET A 1 351 ? 14.465  -60.695 13.901  1.00 28.88  ? 349 MET A O     1 
ATOM   2626 C CB    . MET A 1 351 ? 14.463  -60.270 17.185  1.00 32.55  ? 349 MET A CB    1 
ATOM   2627 C CG    . MET A 1 351 ? 13.745  -60.687 18.464  1.00 33.99  ? 349 MET A CG    1 
ATOM   2628 S SD    . MET A 1 351 ? 13.364  -59.338 19.593  1.00 32.06  ? 349 MET A SD    1 
ATOM   2629 C CE    . MET A 1 351 ? 14.889  -59.204 20.527  1.00 32.14  ? 349 MET A CE    1 
ATOM   2630 N N     . LEU A 1 352 ? 16.519  -61.003 14.835  1.00 30.57  ? 350 LEU A N     1 
ATOM   2631 C CA    . LEU A 1 352 ? 17.321  -60.636 13.632  1.00 32.60  ? 350 LEU A CA    1 
ATOM   2632 C C     . LEU A 1 352 ? 16.928  -61.524 12.444  1.00 32.47  ? 350 LEU A C     1 
ATOM   2633 O O     . LEU A 1 352 ? 16.643  -60.987 11.349  1.00 31.96  ? 350 LEU A O     1 
ATOM   2634 C CB    . LEU A 1 352 ? 18.825  -60.791 13.926  1.00 31.76  ? 350 LEU A CB    1 
ATOM   2635 C CG    . LEU A 1 352 ? 19.480  -59.672 14.731  1.00 32.21  ? 350 LEU A CG    1 
ATOM   2636 C CD1   . LEU A 1 352 ? 20.925  -60.014 15.079  1.00 30.37  ? 350 LEU A CD1   1 
ATOM   2637 C CD2   . LEU A 1 352 ? 19.376  -58.349 13.973  1.00 34.73  ? 350 LEU A CD2   1 
ATOM   2638 N N     . LEU A 1 353 ? 17.020  -62.839 12.645  1.00 31.64  ? 351 LEU A N     1 
ATOM   2639 C CA    . LEU A 1 353 ? 16.761  -63.876 11.624  1.00 31.63  ? 351 LEU A CA    1 
ATOM   2640 C C     . LEU A 1 353 ? 15.285  -63.889 11.172  1.00 31.96  ? 351 LEU A C     1 
ATOM   2641 O O     . LEU A 1 353 ? 15.061  -64.238 9.967   1.00 27.60  ? 351 LEU A O     1 
ATOM   2642 C CB    . LEU A 1 353 ? 17.190  -65.221 12.221  1.00 33.55  ? 351 LEU A CB    1 
ATOM   2643 C CG    . LEU A 1 353 ? 18.700  -65.411 12.318  1.00 33.27  ? 351 LEU A CG    1 
ATOM   2644 C CD1   . LEU A 1 353 ? 19.029  -66.669 13.107  1.00 33.74  ? 351 LEU A CD1   1 
ATOM   2645 C CD2   . LEU A 1 353 ? 19.330  -65.454 10.926  1.00 32.36  ? 351 LEU A CD2   1 
ATOM   2646 N N     . THR A 1 354 ? 14.314  -63.583 12.065  1.00 29.83  ? 352 THR A N     1 
ATOM   2647 C CA    . THR A 1 354 ? 12.889  -63.347 11.676  1.00 31.30  ? 352 THR A CA    1 
ATOM   2648 C C     . THR A 1 354 ? 12.826  -62.214 10.631  1.00 32.54  ? 352 THR A C     1 
ATOM   2649 O O     . THR A 1 354 ? 12.238  -62.404 9.518   1.00 29.74  ? 352 THR A O     1 
ATOM   2650 C CB    . THR A 1 354 ? 12.014  -63.102 12.911  1.00 30.72  ? 352 THR A CB    1 
ATOM   2651 O OG1   . THR A 1 354 ? 12.317  -64.221 13.730  1.00 32.90  ? 352 THR A OG1   1 
ATOM   2652 C CG2   . THR A 1 354 ? 10.525  -63.074 12.650  1.00 26.46  ? 352 THR A CG2   1 
ATOM   2653 N N     . MET A 1 355 ? 13.438  -61.071 10.929  1.00 31.03  ? 353 MET A N     1 
ATOM   2654 C CA    . MET A 1 355 ? 13.383  -59.923 10.001  1.00 31.04  ? 353 MET A CA    1 
ATOM   2655 C C     . MET A 1 355 ? 14.089  -60.320 8.706   1.00 30.53  ? 353 MET A C     1 
ATOM   2656 O O     . MET A 1 355 ? 13.618  -59.934 7.653   1.00 30.91  ? 353 MET A O     1 
ATOM   2657 C CB    . MET A 1 355 ? 14.033  -58.684 10.615  1.00 31.48  ? 353 MET A CB    1 
ATOM   2658 C CG    . MET A 1 355 ? 13.259  -58.184 11.800  1.00 30.03  ? 353 MET A CG    1 
ATOM   2659 S SD    . MET A 1 355 ? 13.876  -56.637 12.414  1.00 29.92  ? 353 MET A SD    1 
ATOM   2660 C CE    . MET A 1 355 ? 15.539  -57.092 12.921  1.00 27.69  ? 353 MET A CE    1 
ATOM   2661 N N     . LYS A 1 356 ? 15.149  -61.110 8.811   1.00 32.10  ? 354 LYS A N     1 
ATOM   2662 C CA    . LYS A 1 356 ? 16.001  -61.492 7.662   1.00 32.21  ? 354 LYS A CA    1 
ATOM   2663 C C     . LYS A 1 356 ? 15.217  -62.471 6.800   1.00 27.27  ? 354 LYS A C     1 
ATOM   2664 O O     . LYS A 1 356 ? 15.167  -62.275 5.614   1.00 30.77  ? 354 LYS A O     1 
ATOM   2665 C CB    . LYS A 1 356 ? 17.337  -62.061 8.152   1.00 33.86  ? 354 LYS A CB    1 
ATOM   2666 C CG    . LYS A 1 356 ? 18.448  -62.101 7.113   1.00 38.22  ? 354 LYS A CG    1 
ATOM   2667 C CD    . LYS A 1 356 ? 19.746  -62.674 7.696   1.00 41.46  ? 354 LYS A CD    1 
ATOM   2668 C CE    . LYS A 1 356 ? 20.661  -63.259 6.641   1.00 44.45  ? 354 LYS A CE    1 
ATOM   2669 N NZ    . LYS A 1 356 ? 21.282  -62.219 5.775   1.00 45.73  ? 354 LYS A NZ    1 
ATOM   2670 N N     . ALA A 1 357 ? 14.638  -63.510 7.381   1.00 27.45  ? 355 ALA A N     1 
ATOM   2671 C CA    . ALA A 1 357 ? 13.843  -64.506 6.631   1.00 26.11  ? 355 ALA A CA    1 
ATOM   2672 C C     . ALA A 1 357 ? 12.747  -63.785 5.849   1.00 27.67  ? 355 ALA A C     1 
ATOM   2673 O O     . ALA A 1 357 ? 12.562  -64.116 4.674   1.00 30.78  ? 355 ALA A O     1 
ATOM   2674 C CB    . ALA A 1 357 ? 13.275  -65.531 7.559   1.00 27.03  ? 355 ALA A CB    1 
ATOM   2675 N N     . PHE A 1 358 ? 12.093  -62.791 6.459   1.00 28.80  ? 356 PHE A N     1 
ATOM   2676 C CA    . PHE A 1 358 ? 10.924  -62.097 5.865   1.00 28.48  ? 356 PHE A CA    1 
ATOM   2677 C C     . PHE A 1 358 ? 11.389  -61.138 4.768   1.00 30.80  ? 356 PHE A C     1 
ATOM   2678 O O     . PHE A 1 358 ? 10.804  -61.182 3.685   1.00 29.95  ? 356 PHE A O     1 
ATOM   2679 C CB    . PHE A 1 358 ? 10.074  -61.407 6.931   1.00 27.89  ? 356 PHE A CB    1 
ATOM   2680 C CG    . PHE A 1 358 ? 9.202   -62.348 7.729   1.00 26.66  ? 356 PHE A CG    1 
ATOM   2681 C CD1   . PHE A 1 358 ? 8.553   -63.419 7.125   1.00 26.72  ? 356 PHE A CD1   1 
ATOM   2682 C CD2   . PHE A 1 358 ? 9.002   -62.145 9.081   1.00 25.23  ? 356 PHE A CD2   1 
ATOM   2683 C CE1   . PHE A 1 358 ? 7.742   -64.269 7.863   1.00 25.90  ? 356 PHE A CE1   1 
ATOM   2684 C CE2   . PHE A 1 358 ? 8.177   -62.986 9.820   1.00 26.68  ? 356 PHE A CE2   1 
ATOM   2685 C CZ    . PHE A 1 358 ? 7.545   -64.046 9.212   1.00 26.42  ? 356 PHE A CZ    1 
ATOM   2686 N N     . ALA A 1 359 ? 12.396  -60.310 5.023   1.00 29.60  ? 357 ALA A N     1 
ATOM   2687 C CA    . ALA A 1 359 ? 12.917  -59.360 4.010   1.00 32.48  ? 357 ALA A CA    1 
ATOM   2688 C C     . ALA A 1 359 ? 13.405  -60.096 2.753   1.00 30.19  ? 357 ALA A C     1 
ATOM   2689 O O     . ALA A 1 359 ? 13.051  -59.695 1.652   1.00 25.33  ? 357 ALA A O     1 
ATOM   2690 C CB    . ALA A 1 359 ? 14.032  -58.514 4.592   1.00 33.59  ? 357 ALA A CB    1 
ATOM   2691 N N     . GLU A 1 360 ? 14.265  -61.093 2.916   1.00 35.14  ? 358 GLU A N     1 
ATOM   2692 C CA    . GLU A 1 360 ? 14.956  -61.751 1.780   1.00 35.95  ? 358 GLU A CA    1 
ATOM   2693 C C     . GLU A 1 360 ? 13.957  -62.691 1.088   1.00 34.56  ? 358 GLU A C     1 
ATOM   2694 O O     . GLU A 1 360 ? 13.963  -62.735 -0.161  1.00 37.49  ? 358 GLU A O     1 
ATOM   2695 C CB    . GLU A 1 360 ? 16.256  -62.400 2.278   1.00 38.60  ? 358 GLU A CB    1 
ATOM   2696 C CG    . GLU A 1 360 ? 17.385  -61.410 2.627   1.00 39.07  ? 358 GLU A CG    1 
ATOM   2697 C CD    . GLU A 1 360 ? 18.680  -62.012 3.211   1.00 44.03  ? 358 GLU A CD    1 
ATOM   2698 O OE1   . GLU A 1 360 ? 19.510  -61.231 3.776   1.00 40.10  ? 358 GLU A OE1   1 
ATOM   2699 O OE2   . GLU A 1 360 ? 18.905  -63.263 3.065   1.00 35.20  ? 358 GLU A OE2   1 
ATOM   2700 N N     . GLY A 1 361 ? 13.125  -63.409 1.853   1.00 34.03  ? 359 GLY A N     1 
ATOM   2701 C CA    . GLY A 1 361 ? 12.058  -64.275 1.309   1.00 30.90  ? 359 GLY A CA    1 
ATOM   2702 C C     . GLY A 1 361 ? 11.045  -63.466 0.496   1.00 31.60  ? 359 GLY A C     1 
ATOM   2703 O O     . GLY A 1 361 ? 10.734  -63.874 -0.659  1.00 30.67  ? 359 GLY A O     1 
ATOM   2704 N N     . ASN A 1 362 ? 10.544  -62.345 1.050   1.00 31.10  ? 360 ASN A N     1 
ATOM   2705 C CA    . ASN A 1 362 ? 9.570   -61.439 0.378   1.00 30.06  ? 360 ASN A CA    1 
ATOM   2706 C C     . ASN A 1 362 ? 10.242  -60.780 -0.842  1.00 30.01  ? 360 ASN A C     1 
ATOM   2707 O O     . ASN A 1 362 ? 9.570   -60.601 -1.836  1.00 28.52  ? 360 ASN A O     1 
ATOM   2708 C CB    . ASN A 1 362 ? 8.901   -60.452 1.346   1.00 29.36  ? 360 ASN A CB    1 
ATOM   2709 C CG    . ASN A 1 362 ? 7.952   -61.135 2.316   1.00 34.65  ? 360 ASN A CG    1 
ATOM   2710 O OD1   . ASN A 1 362 ? 7.390   -62.185 1.997   1.00 35.44  ? 360 ASN A OD1   1 
ATOM   2711 N ND2   . ASN A 1 362 ? 7.743   -60.557 3.496   1.00 35.01  ? 360 ASN A ND2   1 
ATOM   2712 N N     . ARG A 1 363 ? 11.521  -60.423 -0.798  1.00 30.93  ? 361 ARG A N     1 
ATOM   2713 C CA    . ARG A 1 363 ? 12.177  -59.819 -1.984  1.00 31.74  ? 361 ARG A CA    1 
ATOM   2714 C C     . ARG A 1 363 ? 12.085  -60.828 -3.149  1.00 31.20  ? 361 ARG A C     1 
ATOM   2715 O O     . ARG A 1 363 ? 11.767  -60.430 -4.281  1.00 28.03  ? 361 ARG A O     1 
ATOM   2716 C CB    . ARG A 1 363 ? 13.618  -59.418 -1.663  1.00 30.80  ? 361 ARG A CB    1 
ATOM   2717 C CG    . ARG A 1 363 ? 14.336  -58.703 -2.809  1.00 32.02  ? 361 ARG A CG    1 
ATOM   2718 C CD    . ARG A 1 363 ? 15.657  -58.114 -2.327  1.00 33.26  ? 361 ARG A CD    1 
ATOM   2719 N NE    . ARG A 1 363 ? 15.445  -57.026 -1.365  1.00 31.58  ? 361 ARG A NE    1 
ATOM   2720 C CZ    . ARG A 1 363 ? 15.723  -57.068 -0.067  1.00 31.95  ? 361 ARG A CZ    1 
ATOM   2721 N NH1   . ARG A 1 363 ? 16.281  -58.135 0.474   1.00 30.90  ? 361 ARG A NH1   1 
ATOM   2722 N NH2   . ARG A 1 363 ? 15.468  -56.014 0.688   1.00 32.76  ? 361 ARG A NH2   1 
ATOM   2723 N N     . ALA A 1 364 ? 12.353  -62.096 -2.856  1.00 31.43  ? 362 ALA A N     1 
ATOM   2724 C CA    . ALA A 1 364 ? 12.340  -63.197 -3.832  1.00 33.06  ? 362 ALA A CA    1 
ATOM   2725 C C     . ALA A 1 364 ? 10.919  -63.317 -4.390  1.00 33.98  ? 362 ALA A C     1 
ATOM   2726 O O     . ALA A 1 364 ? 10.752  -63.259 -5.628  1.00 30.95  ? 362 ALA A O     1 
ATOM   2727 C CB    . ALA A 1 364 ? 12.803  -64.457 -3.170  1.00 32.20  ? 362 ALA A CB    1 
ATOM   2728 N N     . MET A 1 365 ? 9.918   -63.390 -3.512  1.00 34.84  ? 363 MET A N     1 
ATOM   2729 C CA    . MET A 1 365 ? 8.498   -63.432 -3.945  1.00 35.98  ? 363 MET A CA    1 
ATOM   2730 C C     . MET A 1 365 ? 8.199   -62.213 -4.826  1.00 35.01  ? 363 MET A C     1 
ATOM   2731 O O     . MET A 1 365 ? 7.582   -62.388 -5.878  1.00 34.11  ? 363 MET A O     1 
ATOM   2732 C CB    . MET A 1 365 ? 7.510   -63.488 -2.775  1.00 37.67  ? 363 MET A CB    1 
ATOM   2733 C CG    . MET A 1 365 ? 6.031   -63.479 -3.243  1.00 39.32  ? 363 MET A CG    1 
ATOM   2734 S SD    . MET A 1 365 ? 4.872   -64.318 -2.148  1.00 39.07  ? 363 MET A SD    1 
ATOM   2735 C CE    . MET A 1 365 ? 5.310   -63.633 -0.556  1.00 50.42  ? 363 MET A CE    1 
ATOM   2736 N N     . LEU A 1 366 ? 8.639   -61.024 -4.442  1.00 33.51  ? 364 LEU A N     1 
ATOM   2737 C CA    . LEU A 1 366 ? 8.254   -59.780 -5.157  1.00 38.15  ? 364 LEU A CA    1 
ATOM   2738 C C     . LEU A 1 366 ? 8.726   -59.791 -6.623  1.00 38.82  ? 364 LEU A C     1 
ATOM   2739 O O     . LEU A 1 366 ? 7.962   -59.341 -7.482  1.00 31.72  ? 364 LEU A O     1 
ATOM   2740 C CB    . LEU A 1 366 ? 8.841   -58.566 -4.431  1.00 45.42  ? 364 LEU A CB    1 
ATOM   2741 C CG    . LEU A 1 366 ? 8.306   -57.221 -4.920  1.00 51.02  ? 364 LEU A CG    1 
ATOM   2742 C CD1   . LEU A 1 366 ? 7.150   -56.775 -4.042  1.00 59.96  ? 364 LEU A CD1   1 
ATOM   2743 C CD2   . LEU A 1 366 ? 9.407   -56.167 -4.964  1.00 55.13  ? 364 LEU A CD2   1 
ATOM   2744 N N     . TYR A 1 367 ? 9.969   -60.209 -6.893  1.00 38.58  ? 365 TYR A N     1 
ATOM   2745 C CA    . TYR A 1 367 ? 10.592  -60.108 -8.236  1.00 36.71  ? 365 TYR A CA    1 
ATOM   2746 C C     . TYR A 1 367 ? 10.158  -61.310 -9.071  1.00 36.33  ? 365 TYR A C     1 
ATOM   2747 O O     . TYR A 1 367 ? 10.239  -61.231 -10.327 1.00 31.48  ? 365 TYR A O     1 
ATOM   2748 C CB    . TYR A 1 367 ? 12.113  -59.931 -8.115  1.00 39.71  ? 365 TYR A CB    1 
ATOM   2749 C CG    . TYR A 1 367 ? 12.505  -58.552 -7.640  1.00 40.13  ? 365 TYR A CG    1 
ATOM   2750 C CD1   . TYR A 1 367 ? 12.126  -57.427 -8.363  1.00 40.62  ? 365 TYR A CD1   1 
ATOM   2751 C CD2   . TYR A 1 367 ? 13.181  -58.360 -6.439  1.00 38.57  ? 365 TYR A CD2   1 
ATOM   2752 C CE1   . TYR A 1 367 ? 12.427  -56.150 -7.923  1.00 40.70  ? 365 TYR A CE1   1 
ATOM   2753 C CE2   . TYR A 1 367 ? 13.516  -57.089 -6.002  1.00 37.49  ? 365 TYR A CE2   1 
ATOM   2754 C CZ    . TYR A 1 367 ? 13.110  -55.986 -6.729  1.00 39.54  ? 365 TYR A CZ    1 
ATOM   2755 O OH    . TYR A 1 367 ? 13.399  -54.730 -6.302  1.00 37.61  ? 365 TYR A OH    1 
ATOM   2756 N N     . PHE A 1 368 ? 9.774   -62.406 -8.399  1.00 38.14  ? 366 PHE A N     1 
ATOM   2757 C CA    . PHE A 1 368 ? 9.021   -63.513 -9.032  1.00 33.91  ? 366 PHE A CA    1 
ATOM   2758 C C     . PHE A 1 368 ? 7.716   -62.922 -9.598  1.00 35.64  ? 366 PHE A C     1 
ATOM   2759 O O     . PHE A 1 368 ? 7.463   -63.087 -10.802 1.00 32.56  ? 366 PHE A O     1 
ATOM   2760 C CB    . PHE A 1 368 ? 8.805   -64.674 -8.071  1.00 35.58  ? 366 PHE A CB    1 
ATOM   2761 C CG    . PHE A 1 368 ? 8.059   -65.797 -8.739  1.00 45.59  ? 366 PHE A CG    1 
ATOM   2762 C CD1   . PHE A 1 368 ? 8.724   -66.668 -9.599  1.00 45.48  ? 366 PHE A CD1   1 
ATOM   2763 C CD2   . PHE A 1 368 ? 6.683   -65.913 -8.607  1.00 44.99  ? 366 PHE A CD2   1 
ATOM   2764 C CE1   . PHE A 1 368 ? 8.038   -67.665 -10.266 1.00 44.75  ? 366 PHE A CE1   1 
ATOM   2765 C CE2   . PHE A 1 368 ? 6.006   -66.934 -9.261  1.00 47.90  ? 366 PHE A CE2   1 
ATOM   2766 C CZ    . PHE A 1 368 ? 6.679   -67.793 -10.098 1.00 45.69  ? 366 PHE A CZ    1 
ATOM   2767 N N     . ALA A 1 369 ? 6.930   -62.203 -8.787  1.00 32.67  ? 367 ALA A N     1 
ATOM   2768 C CA    . ALA A 1 369 ? 5.658   -61.586 -9.232  1.00 35.13  ? 367 ALA A CA    1 
ATOM   2769 C C     . ALA A 1 369 ? 5.942   -60.578 -10.352 1.00 36.68  ? 367 ALA A C     1 
ATOM   2770 O O     . ALA A 1 369 ? 5.185   -60.544 -11.349 1.00 37.14  ? 367 ALA A O     1 
ATOM   2771 C CB    . ALA A 1 369 ? 4.930   -60.930 -8.073  1.00 34.43  ? 367 ALA A CB    1 
ATOM   2772 N N     . ALA A 1 370 ? 6.982   -59.759 -10.213 1.00 34.92  ? 368 ALA A N     1 
ATOM   2773 C CA    . ALA A 1 370 ? 7.249   -58.666 -11.169 1.00 33.47  ? 368 ALA A CA    1 
ATOM   2774 C C     . ALA A 1 370 ? 7.598   -59.234 -12.559 1.00 33.38  ? 368 ALA A C     1 
ATOM   2775 O O     . ALA A 1 370 ? 7.315   -58.588 -13.577 1.00 29.16  ? 368 ALA A O     1 
ATOM   2776 C CB    . ALA A 1 370 ? 8.350   -57.815 -10.622 1.00 36.57  ? 368 ALA A CB    1 
ATOM   2777 N N     . LYS A 1 371 ? 8.178   -60.423 -12.617 1.00 31.81  ? 369 LYS A N     1 
ATOM   2778 C CA    . LYS A 1 371 ? 8.437   -61.060 -13.931 1.00 35.79  ? 369 LYS A CA    1 
ATOM   2779 C C     . LYS A 1 371 ? 7.095   -61.356 -14.624 1.00 36.60  ? 369 LYS A C     1 
ATOM   2780 O O     . LYS A 1 371 ? 7.060   -61.302 -15.852 1.00 35.74  ? 369 LYS A O     1 
ATOM   2781 C CB    . LYS A 1 371 ? 9.299   -62.309 -13.738 1.00 38.62  ? 369 LYS A CB    1 
ATOM   2782 C CG    . LYS A 1 371 ? 10.794  -62.113 -13.934 1.00 41.77  ? 369 LYS A CG    1 
ATOM   2783 C CD    . LYS A 1 371 ? 11.612  -63.276 -13.430 1.00 43.92  ? 369 LYS A CD    1 
ATOM   2784 C CE    . LYS A 1 371 ? 11.253  -64.585 -14.095 1.00 44.77  ? 369 LYS A CE    1 
ATOM   2785 N NZ    . LYS A 1 371 ? 11.992  -65.723 -13.501 1.00 47.85  ? 369 LYS A NZ    1 
ATOM   2786 N N     . GLN A 1 372 ? 6.037   -61.618 -13.852 1.00 34.44  ? 370 GLN A N     1 
ATOM   2787 C CA    . GLN A 1 372 ? 4.700   -61.900 -14.411 1.00 36.42  ? 370 GLN A CA    1 
ATOM   2788 C C     . GLN A 1 372 ? 4.125   -60.609 -14.963 1.00 37.09  ? 370 GLN A C     1 
ATOM   2789 O O     . GLN A 1 372 ? 3.673   -60.625 -16.124 1.00 42.42  ? 370 GLN A O     1 
ATOM   2790 C CB    . GLN A 1 372 ? 3.720   -62.484 -13.406 1.00 34.67  ? 370 GLN A CB    1 
ATOM   2791 C CG    . GLN A 1 372 ? 4.298   -63.618 -12.611 1.00 36.41  ? 370 GLN A CG    1 
ATOM   2792 C CD    . GLN A 1 372 ? 4.831   -64.724 -13.475 1.00 40.09  ? 370 GLN A CD    1 
ATOM   2793 O OE1   . GLN A 1 372 ? 4.239   -65.124 -14.476 1.00 44.79  ? 370 GLN A OE1   1 
ATOM   2794 N NE2   . GLN A 1 372 ? 5.932   -65.288 -13.027 1.00 45.60  ? 370 GLN A NE2   1 
ATOM   2795 N N     . VAL A 1 373 ? 4.133   -59.543 -14.171 1.00 34.61  ? 371 VAL A N     1 
ATOM   2796 C CA    . VAL A 1 373 ? 3.726   -58.195 -14.666 1.00 33.12  ? 371 VAL A CA    1 
ATOM   2797 C C     . VAL A 1 373 ? 4.345   -58.012 -16.062 1.00 33.93  ? 371 VAL A C     1 
ATOM   2798 O O     . VAL A 1 373 ? 3.625   -57.575 -16.950 1.00 38.83  ? 371 VAL A O     1 
ATOM   2799 C CB    . VAL A 1 373 ? 4.158   -57.069 -13.702 1.00 35.52  ? 371 VAL A CB    1 
ATOM   2800 C CG1   . VAL A 1 373 ? 3.845   -55.680 -14.259 1.00 33.94  ? 371 VAL A CG1   1 
ATOM   2801 C CG2   . VAL A 1 373 ? 3.555   -57.232 -12.306 1.00 34.15  ? 371 VAL A CG2   1 
ATOM   2802 N N     . ASP A 1 374 ? 5.633   -58.327 -16.244 1.00 36.27  ? 372 ASP A N     1 
ATOM   2803 C CA    . ASP A 1 374 ? 6.390   -58.024 -17.491 1.00 40.70  ? 372 ASP A CA    1 
ATOM   2804 C C     . ASP A 1 374 ? 5.802   -58.846 -18.646 1.00 42.52  ? 372 ASP A C     1 
ATOM   2805 O O     . ASP A 1 374 ? 5.574   -58.270 -19.718 1.00 38.13  ? 372 ASP A O     1 
ATOM   2806 C CB    . ASP A 1 374 ? 7.891   -58.310 -17.360 1.00 38.31  ? 372 ASP A CB    1 
ATOM   2807 C CG    . ASP A 1 374 ? 8.653   -57.247 -16.600 1.00 36.94  ? 372 ASP A CG    1 
ATOM   2808 O OD1   . ASP A 1 374 ? 8.147   -56.137 -16.511 1.00 38.86  ? 372 ASP A OD1   1 
ATOM   2809 O OD2   . ASP A 1 374 ? 9.740   -57.545 -16.103 1.00 37.44  ? 372 ASP A OD2   1 
ATOM   2810 N N     . ILE A 1 375 ? 5.519   -60.126 -18.400 1.00 40.66  ? 373 ILE A N     1 
ATOM   2811 C CA    . ILE A 1 375 ? 4.925   -61.021 -19.435 1.00 39.07  ? 373 ILE A CA    1 
ATOM   2812 C C     . ILE A 1 375 ? 3.511   -60.545 -19.778 1.00 41.30  ? 373 ILE A C     1 
ATOM   2813 O O     . ILE A 1 375 ? 3.220   -60.406 -20.966 1.00 41.38  ? 373 ILE A O     1 
ATOM   2814 C CB    . ILE A 1 375 ? 4.942   -62.480 -18.951 1.00 39.40  ? 373 ILE A CB    1 
ATOM   2815 C CG1   . ILE A 1 375 ? 6.372   -62.991 -18.762 1.00 35.92  ? 373 ILE A CG1   1 
ATOM   2816 C CG2   . ILE A 1 375 ? 4.139   -63.370 -19.886 1.00 41.74  ? 373 ILE A CG2   1 
ATOM   2817 C CD1   . ILE A 1 375 ? 6.506   -64.057 -17.705 1.00 36.02  ? 373 ILE A CD1   1 
ATOM   2818 N N     . VAL A 1 376 ? 2.678   -60.279 -18.771 1.00 43.75  ? 374 VAL A N     1 
ATOM   2819 C CA    . VAL A 1 376 ? 1.327   -59.725 -19.084 1.00 43.67  ? 374 VAL A CA    1 
ATOM   2820 C C     . VAL A 1 376 ? 1.466   -58.498 -20.004 1.00 45.15  ? 374 VAL A C     1 
ATOM   2821 O O     . VAL A 1 376 ? 0.680   -58.374 -20.932 1.00 43.03  ? 374 VAL A O     1 
ATOM   2822 C CB    . VAL A 1 376 ? 0.511   -59.429 -17.812 1.00 41.49  ? 374 VAL A CB    1 
ATOM   2823 C CG1   . VAL A 1 376 ? -0.741  -58.602 -18.113 1.00 38.94  ? 374 VAL A CG1   1 
ATOM   2824 C CG2   . VAL A 1 376 ? 0.127   -60.732 -17.119 1.00 41.06  ? 374 VAL A CG2   1 
ATOM   2825 N N     . GLN A 1 377 ? 2.425   -57.611 -19.781 1.00 49.38  ? 375 GLN A N     1 
ATOM   2826 C CA    . GLN A 1 377 ? 2.415   -56.295 -20.475 1.00 57.21  ? 375 GLN A CA    1 
ATOM   2827 C C     . GLN A 1 377 ? 3.016   -56.377 -21.888 1.00 47.59  ? 375 GLN A C     1 
ATOM   2828 O O     . GLN A 1 377 ? 2.621   -55.549 -22.691 1.00 39.94  ? 375 GLN A O     1 
ATOM   2829 C CB    . GLN A 1 377 ? 3.164   -55.241 -19.660 1.00 61.62  ? 375 GLN A CB    1 
ATOM   2830 C CG    . GLN A 1 377 ? 2.265   -54.555 -18.652 1.00 74.78  ? 375 GLN A CG    1 
ATOM   2831 C CD    . GLN A 1 377 ? 3.073   -53.695 -17.713 1.00 79.34  ? 375 GLN A CD    1 
ATOM   2832 O OE1   . GLN A 1 377 ? 4.148   -53.216 -18.070 1.00 67.96  ? 375 GLN A OE1   1 
ATOM   2833 N NE2   . GLN A 1 377 ? 2.554   -53.496 -16.509 1.00 78.15  ? 375 GLN A NE2   1 
ATOM   2834 N N     . ARG A 1 378 ? 3.955   -57.291 -22.147 1.00 49.53  ? 376 ARG A N     1 
ATOM   2835 C CA    . ARG A 1 378 ? 4.858   -57.287 -23.333 1.00 51.61  ? 376 ARG A CA    1 
ATOM   2836 C C     . ARG A 1 378 ? 4.793   -58.589 -24.158 1.00 59.94  ? 376 ARG A C     1 
ATOM   2837 O O     . ARG A 1 378 ? 5.156   -58.531 -25.361 1.00 50.63  ? 376 ARG A O     1 
ATOM   2838 C CB    . ARG A 1 378 ? 6.305   -57.144 -22.866 1.00 54.28  ? 376 ARG A CB    1 
ATOM   2839 C CG    . ARG A 1 378 ? 6.712   -55.735 -22.478 1.00 57.79  ? 376 ARG A CG    1 
ATOM   2840 C CD    . ARG A 1 378 ? 8.100   -55.744 -21.861 1.00 55.52  ? 376 ARG A CD    1 
ATOM   2841 N NE    . ARG A 1 378 ? 8.304   -54.433 -21.266 1.00 56.85  ? 376 ARG A NE    1 
ATOM   2842 C CZ    . ARG A 1 378 ? 8.907   -53.412 -21.844 1.00 52.08  ? 376 ARG A CZ    1 
ATOM   2843 N NH1   . ARG A 1 378 ? 9.428   -53.538 -23.049 1.00 60.67  ? 376 ARG A NH1   1 
ATOM   2844 N NH2   . ARG A 1 378 ? 9.026   -52.271 -21.196 1.00 47.73  ? 376 ARG A NH2   1 
ATOM   2845 N N     . SER A 1 379 ? 4.476   -59.746 -23.561 1.00 53.41  ? 377 SER A N     1 
ATOM   2846 C CA    . SER A 1 379 ? 4.553   -61.029 -24.302 1.00 55.07  ? 377 SER A CA    1 
ATOM   2847 C C     . SER A 1 379 ? 3.453   -61.034 -25.355 1.00 56.78  ? 377 SER A C     1 
ATOM   2848 O O     . SER A 1 379 ? 2.403   -60.396 -25.146 1.00 55.72  ? 377 SER A O     1 
ATOM   2849 C CB    . SER A 1 379 ? 4.460   -62.232 -23.442 1.00 52.97  ? 377 SER A CB    1 
ATOM   2850 O OG    . SER A 1 379 ? 4.841   -63.374 -24.179 1.00 50.21  ? 377 SER A OG    1 
ATOM   2851 N N     . GLN A 1 380 ? 3.746   -61.672 -26.477 1.00 61.78  ? 378 GLN A N     1 
ATOM   2852 C CA    . GLN A 1 380 ? 2.826   -61.779 -27.631 1.00 63.90  ? 378 GLN A CA    1 
ATOM   2853 C C     . GLN A 1 380 ? 2.352   -63.226 -27.767 1.00 58.55  ? 378 GLN A C     1 
ATOM   2854 O O     . GLN A 1 380 ? 1.477   -63.450 -28.586 1.00 65.90  ? 378 GLN A O     1 
ATOM   2855 C CB    . GLN A 1 380 ? 3.534   -61.303 -28.891 1.00 64.35  ? 378 GLN A CB    1 
ATOM   2856 C CG    . GLN A 1 380 ? 3.484   -59.796 -29.085 1.00 67.23  ? 378 GLN A CG    1 
ATOM   2857 C CD    . GLN A 1 380 ? 4.779   -59.344 -29.714 1.00 73.82  ? 378 GLN A CD    1 
ATOM   2858 O OE1   . GLN A 1 380 ? 5.550   -60.145 -30.240 1.00 73.34  ? 378 GLN A OE1   1 
ATOM   2859 N NE2   . GLN A 1 380 ? 5.054   -58.056 -29.632 1.00 75.63  ? 378 GLN A NE2   1 
ATOM   2860 N N     . ASP A 1 381 ? 2.934   -64.156 -27.007 1.00 56.31  ? 379 ASP A N     1 
ATOM   2861 C CA    . ASP A 1 381 ? 2.418   -65.536 -26.826 1.00 58.86  ? 379 ASP A CA    1 
ATOM   2862 C C     . ASP A 1 381 ? 1.229   -65.485 -25.859 1.00 66.22  ? 379 ASP A C     1 
ATOM   2863 O O     . ASP A 1 381 ? 1.373   -64.917 -24.751 1.00 75.78  ? 379 ASP A O     1 
ATOM   2864 C CB    . ASP A 1 381 ? 3.510   -66.464 -26.302 1.00 58.22  ? 379 ASP A CB    1 
ATOM   2865 C CG    . ASP A 1 381 ? 3.037   -67.883 -26.108 1.00 61.42  ? 379 ASP A CG    1 
ATOM   2866 O OD1   . ASP A 1 381 ? 1.826   -68.111 -26.228 1.00 76.52  ? 379 ASP A OD1   1 
ATOM   2867 O OD2   . ASP A 1 381 ? 3.885   -68.745 -25.850 1.00 74.60  ? 379 ASP A OD2   1 
ATOM   2868 N N     . GLU A 1 382 ? 0.105   -66.080 -26.248 1.00 70.75  ? 380 GLU A N     1 
ATOM   2869 C CA    . GLU A 1 382 ? -1.170  -65.966 -25.503 1.00 72.76  ? 380 GLU A CA    1 
ATOM   2870 C C     . GLU A 1 382 ? -1.136  -66.933 -24.326 1.00 67.39  ? 380 GLU A C     1 
ATOM   2871 O O     . GLU A 1 382 ? -1.598  -66.541 -23.252 1.00 64.56  ? 380 GLU A O     1 
ATOM   2872 C CB    . GLU A 1 382 ? -2.359  -66.190 -26.436 1.00 76.05  ? 380 GLU A CB    1 
ATOM   2873 C CG    . GLU A 1 382 ? -2.507  -65.073 -27.464 1.00 84.20  ? 380 GLU A CG    1 
ATOM   2874 C CD    . GLU A 1 382 ? -2.295  -63.657 -26.943 1.00 86.61  ? 380 GLU A CD    1 
ATOM   2875 O OE1   . GLU A 1 382 ? -3.186  -63.132 -26.236 1.00 84.56  ? 380 GLU A OE1   1 
ATOM   2876 O OE2   . GLU A 1 382 ? -1.227  -63.083 -27.230 1.00 93.19  ? 380 GLU A OE2   1 
ATOM   2877 N N     . GLU A 1 383 ? -0.603  -68.136 -24.523 1.00 65.67  ? 381 GLU A N     1 
ATOM   2878 C CA    . GLU A 1 383 ? -0.577  -69.176 -23.462 1.00 68.42  ? 381 GLU A CA    1 
ATOM   2879 C C     . GLU A 1 383 ? 0.232   -68.664 -22.263 1.00 62.46  ? 381 GLU A C     1 
ATOM   2880 O O     . GLU A 1 383 ? -0.130  -69.010 -21.121 1.00 59.91  ? 381 GLU A O     1 
ATOM   2881 C CB    . GLU A 1 383 ? -0.052  -70.504 -24.020 1.00 73.13  ? 381 GLU A CB    1 
ATOM   2882 C CG    . GLU A 1 383 ? -1.130  -71.297 -24.754 1.00 83.13  ? 381 GLU A CG    1 
ATOM   2883 C CD    . GLU A 1 383 ? -2.511  -71.288 -24.093 1.00 84.26  ? 381 GLU A CD    1 
ATOM   2884 O OE1   . GLU A 1 383 ? -3.463  -70.766 -24.702 1.00 79.33  ? 381 GLU A OE1   1 
ATOM   2885 O OE2   . GLU A 1 383 ? -2.636  -71.778 -22.956 1.00 82.41  ? 381 GLU A OE2   1 
ATOM   2886 N N     . GLN A 1 384 ? 1.261   -67.857 -22.529 1.00 57.96  ? 382 GLN A N     1 
ATOM   2887 C CA    . GLN A 1 384 ? 2.239   -67.349 -21.533 1.00 56.35  ? 382 GLN A CA    1 
ATOM   2888 C C     . GLN A 1 384 ? 1.610   -66.154 -20.799 1.00 48.66  ? 382 GLN A C     1 
ATOM   2889 O O     . GLN A 1 384 ? 1.653   -66.149 -19.567 1.00 46.72  ? 382 GLN A O     1 
ATOM   2890 C CB    . GLN A 1 384 ? 3.530   -67.009 -22.275 1.00 59.68  ? 382 GLN A CB    1 
ATOM   2891 C CG    . GLN A 1 384 ? 4.782   -67.102 -21.427 1.00 64.66  ? 382 GLN A CG    1 
ATOM   2892 C CD    . GLN A 1 384 ? 5.825   -66.109 -21.883 1.00 72.98  ? 382 GLN A CD    1 
ATOM   2893 O OE1   . GLN A 1 384 ? 5.743   -65.538 -22.971 1.00 77.93  ? 382 GLN A OE1   1 
ATOM   2894 N NE2   . GLN A 1 384 ? 6.811   -65.869 -21.037 1.00 72.67  ? 382 GLN A NE2   1 
ATOM   2895 N N     . LYS A 1 385 ? 0.982   -65.237 -21.548 1.00 47.33  ? 383 LYS A N     1 
ATOM   2896 C CA    . LYS A 1 385 ? 0.202   -64.060 -21.072 1.00 46.67  ? 383 LYS A CA    1 
ATOM   2897 C C     . LYS A 1 385 ? -0.907  -64.522 -20.119 1.00 51.03  ? 383 LYS A C     1 
ATOM   2898 O O     . LYS A 1 385 ? -1.108  -63.867 -19.075 1.00 43.11  ? 383 LYS A O     1 
ATOM   2899 C CB    . LYS A 1 385 ? -0.441  -63.327 -22.250 1.00 51.20  ? 383 LYS A CB    1 
ATOM   2900 C CG    . LYS A 1 385 ? -0.188  -61.826 -22.368 1.00 57.51  ? 383 LYS A CG    1 
ATOM   2901 C CD    . LYS A 1 385 ? -1.068  -61.166 -23.446 1.00 61.16  ? 383 LYS A CD    1 
ATOM   2902 C CE    . LYS A 1 385 ? -1.061  -59.647 -23.479 1.00 63.39  ? 383 LYS A CE    1 
ATOM   2903 N NZ    . LYS A 1 385 ? 0.248   -59.082 -23.910 1.00 64.35  ? 383 LYS A NZ    1 
ATOM   2904 N N     . LYS A 1 386 ? -1.611  -65.595 -20.492 1.00 47.55  ? 384 LYS A N     1 
ATOM   2905 C CA    . LYS A 1 386 ? -2.725  -66.197 -19.728 1.00 45.67  ? 384 LYS A CA    1 
ATOM   2906 C C     . LYS A 1 386 ? -2.186  -66.764 -18.410 1.00 45.66  ? 384 LYS A C     1 
ATOM   2907 O O     . LYS A 1 386 ? -2.827  -66.545 -17.369 1.00 46.81  ? 384 LYS A O     1 
ATOM   2908 C CB    . LYS A 1 386 ? -3.406  -67.268 -20.583 1.00 55.40  ? 384 LYS A CB    1 
ATOM   2909 C CG    . LYS A 1 386 ? -4.226  -68.312 -19.836 1.00 61.85  ? 384 LYS A CG    1 
ATOM   2910 C CD    . LYS A 1 386 ? -4.141  -69.694 -20.460 1.00 70.91  ? 384 LYS A CD    1 
ATOM   2911 C CE    . LYS A 1 386 ? -5.140  -70.674 -19.873 1.00 77.35  ? 384 LYS A CE    1 
ATOM   2912 N NZ    . LYS A 1 386 ? -6.541  -70.260 -20.131 1.00 78.31  ? 384 LYS A NZ    1 
ATOM   2913 N N     . ALA A 1 387 ? -1.073  -67.492 -18.437 1.00 40.94  ? 385 ALA A N     1 
ATOM   2914 C CA    . ALA A 1 387 ? -0.534  -68.177 -17.240 1.00 43.62  ? 385 ALA A CA    1 
ATOM   2915 C C     . ALA A 1 387 ? 0.071   -67.144 -16.278 1.00 42.38  ? 385 ALA A C     1 
ATOM   2916 O O     . ALA A 1 387 ? -0.042  -67.336 -15.057 1.00 41.46  ? 385 ALA A O     1 
ATOM   2917 C CB    . ALA A 1 387 ? 0.477   -69.234 -17.626 1.00 43.11  ? 385 ALA A CB    1 
ATOM   2918 N N     . ALA A 1 388 ? 0.724   -66.111 -16.808 1.00 41.85  ? 386 ALA A N     1 
ATOM   2919 C CA    . ALA A 1 388 ? 1.368   -65.055 -16.000 1.00 44.74  ? 386 ALA A CA    1 
ATOM   2920 C C     . ALA A 1 388 ? 0.245   -64.226 -15.367 1.00 43.63  ? 386 ALA A C     1 
ATOM   2921 O O     . ALA A 1 388 ? 0.251   -64.031 -14.138 1.00 41.51  ? 386 ALA A O     1 
ATOM   2922 C CB    . ALA A 1 388 ? 2.322   -64.237 -16.842 1.00 47.04  ? 386 ALA A CB    1 
ATOM   2923 N N     . ASP A 1 389 ? -0.763  -63.880 -16.155 1.00 41.79  ? 387 ASP A N     1 
ATOM   2924 C CA    . ASP A 1 389 ? -1.973  -63.162 -15.680 1.00 45.89  ? 387 ASP A CA    1 
ATOM   2925 C C     . ASP A 1 389 ? -2.628  -63.933 -14.522 1.00 45.07  ? 387 ASP A C     1 
ATOM   2926 O O     . ASP A 1 389 ? -2.988  -63.315 -13.473 1.00 38.25  ? 387 ASP A O     1 
ATOM   2927 C CB    . ASP A 1 389 ? -2.923  -62.944 -16.847 1.00 50.20  ? 387 ASP A CB    1 
ATOM   2928 C CG    . ASP A 1 389 ? -4.142  -62.170 -16.445 1.00 49.83  ? 387 ASP A CG    1 
ATOM   2929 O OD1   . ASP A 1 389 ? -5.066  -62.802 -15.914 1.00 63.39  ? 387 ASP A OD1   1 
ATOM   2930 O OD2   . ASP A 1 389 ? -4.142  -60.968 -16.658 1.00 58.25  ? 387 ASP A OD2   1 
ATOM   2931 N N     . SER A 1 390 ? -2.744  -65.247 -14.671 1.00 41.58  ? 388 SER A N     1 
ATOM   2932 C CA    . SER A 1 390 ? -3.376  -66.128 -13.671 1.00 39.78  ? 388 SER A CA    1 
ATOM   2933 C C     . SER A 1 390 ? -2.479  -66.248 -12.421 1.00 40.38  ? 388 SER A C     1 
ATOM   2934 O O     . SER A 1 390 ? -2.986  -66.226 -11.296 1.00 38.62  ? 388 SER A O     1 
ATOM   2935 C CB    . SER A 1 390 ? -3.669  -67.420 -14.313 1.00 39.85  ? 388 SER A CB    1 
ATOM   2936 O OG    . SER A 1 390 ? -4.420  -68.209 -13.435 1.00 51.37  ? 388 SER A OG    1 
ATOM   2937 N N     . MET A 1 391 ? -1.171  -66.346 -12.596 1.00 38.40  ? 389 MET A N     1 
ATOM   2938 C CA    . MET A 1 391 ? -0.198  -66.377 -11.478 1.00 40.69  ? 389 MET A CA    1 
ATOM   2939 C C     . MET A 1 391 ? -0.257  -65.048 -10.690 1.00 38.35  ? 389 MET A C     1 
ATOM   2940 O O     . MET A 1 391 ? -0.222  -65.103 -9.478  1.00 37.12  ? 389 MET A O     1 
ATOM   2941 C CB    . MET A 1 391 ? 1.213   -66.605 -12.039 1.00 42.79  ? 389 MET A CB    1 
ATOM   2942 C CG    . MET A 1 391 ? 2.289   -66.686 -10.991 1.00 42.76  ? 389 MET A CG    1 
ATOM   2943 S SD    . MET A 1 391 ? 2.059   -68.068 -9.843  1.00 43.94  ? 389 MET A SD    1 
ATOM   2944 C CE    . MET A 1 391 ? 2.466   -69.468 -10.889 1.00 48.34  ? 389 MET A CE    1 
ATOM   2945 N N     . LEU A 1 392 ? -0.324  -63.891 -11.352 1.00 35.89  ? 390 LEU A N     1 
ATOM   2946 C CA    . LEU A 1 392 ? -0.447  -62.563 -10.697 1.00 38.81  ? 390 LEU A CA    1 
ATOM   2947 C C     . LEU A 1 392 ? -1.714  -62.509 -9.865  1.00 38.42  ? 390 LEU A C     1 
ATOM   2948 O O     . LEU A 1 392 ? -1.624  -61.996 -8.767  1.00 40.93  ? 390 LEU A O     1 
ATOM   2949 C CB    . LEU A 1 392 ? -0.514  -61.444 -11.730 1.00 45.33  ? 390 LEU A CB    1 
ATOM   2950 C CG    . LEU A 1 392 ? 0.823   -60.803 -12.072 1.00 55.74  ? 390 LEU A CG    1 
ATOM   2951 C CD1   . LEU A 1 392 ? 0.655   -59.772 -13.195 1.00 62.33  ? 390 LEU A CD1   1 
ATOM   2952 C CD2   . LEU A 1 392 ? 1.443   -60.179 -10.826 1.00 58.79  ? 390 LEU A CD2   1 
ATOM   2953 N N     . ALA A 1 393 ? -2.833  -63.001 -10.411 1.00 39.86  ? 391 ALA A N     1 
ATOM   2954 C CA    . ALA A 1 393 ? -4.169  -63.001 -9.775  1.00 36.68  ? 391 ALA A CA    1 
ATOM   2955 C C     . ALA A 1 393 ? -4.081  -63.712 -8.425  1.00 35.63  ? 391 ALA A C     1 
ATOM   2956 O O     . ALA A 1 393 ? -4.684  -63.218 -7.475  1.00 35.88  ? 391 ALA A O     1 
ATOM   2957 C CB    . ALA A 1 393 ? -5.191  -63.648 -10.668 1.00 37.19  ? 391 ALA A CB    1 
ATOM   2958 N N     . PHE A 1 394 ? -3.329  -64.809 -8.352  1.00 33.22  ? 392 PHE A N     1 
ATOM   2959 C CA    . PHE A 1 394 ? -3.123  -65.635 -7.128  1.00 35.34  ? 392 PHE A CA    1 
ATOM   2960 C C     . PHE A 1 394 ? -2.186  -64.891 -6.156  1.00 35.24  ? 392 PHE A C     1 
ATOM   2961 O O     . PHE A 1 394 ? -2.526  -64.751 -4.986  1.00 40.73  ? 392 PHE A O     1 
ATOM   2962 C CB    . PHE A 1 394 ? -2.603  -67.025 -7.540  1.00 34.15  ? 392 PHE A CB    1 
ATOM   2963 C CG    . PHE A 1 394 ? -2.200  -67.925 -6.407  1.00 31.70  ? 392 PHE A CG    1 
ATOM   2964 C CD1   . PHE A 1 394 ? -3.145  -68.536 -5.617  1.00 33.72  ? 392 PHE A CD1   1 
ATOM   2965 C CD2   . PHE A 1 394 ? -0.870  -68.125 -6.093  1.00 36.42  ? 392 PHE A CD2   1 
ATOM   2966 C CE1   . PHE A 1 394 ? -2.774  -69.327 -4.536  1.00 30.17  ? 392 PHE A CE1   1 
ATOM   2967 C CE2   . PHE A 1 394 ? -0.501  -68.924 -5.020  1.00 32.67  ? 392 PHE A CE2   1 
ATOM   2968 C CZ    . PHE A 1 394 ? -1.457  -69.521 -4.249  1.00 30.35  ? 392 PHE A CZ    1 
ATOM   2969 N N     . LEU A 1 395 ? -1.068  -64.351 -6.637  1.00 34.85  ? 393 LEU A N     1 
ATOM   2970 C CA    . LEU A 1 395 ? 0.057   -63.875 -5.780  1.00 38.90  ? 393 LEU A CA    1 
ATOM   2971 C C     . LEU A 1 395 ? -0.187  -62.464 -5.253  1.00 38.00  ? 393 LEU A C     1 
ATOM   2972 O O     . LEU A 1 395 ? 0.319   -62.161 -4.179  1.00 39.76  ? 393 LEU A O     1 
ATOM   2973 C CB    . LEU A 1 395 ? 1.350   -63.868 -6.597  1.00 42.16  ? 393 LEU A CB    1 
ATOM   2974 C CG    . LEU A 1 395 ? 1.993   -65.224 -6.838  1.00 42.72  ? 393 LEU A CG    1 
ATOM   2975 C CD1   . LEU A 1 395 ? 3.315   -65.009 -7.539  1.00 49.79  ? 393 LEU A CD1   1 
ATOM   2976 C CD2   . LEU A 1 395 ? 2.159   -65.999 -5.534  1.00 46.75  ? 393 LEU A CD2   1 
ATOM   2977 N N     . THR A 1 396 ? -0.870  -61.628 -6.031  1.00 39.08  ? 394 THR A N     1 
ATOM   2978 C CA    . THR A 1 396 ? -1.087  -60.178 -5.767  1.00 37.69  ? 394 THR A CA    1 
ATOM   2979 C C     . THR A 1 396 ? -1.681  -59.963 -4.375  1.00 33.99  ? 394 THR A C     1 
ATOM   2980 O O     . THR A 1 396 ? -1.139  -59.166 -3.629  1.00 36.45  ? 394 THR A O     1 
ATOM   2981 C CB    . THR A 1 396 ? -1.892  -59.571 -6.921  1.00 35.05  ? 394 THR A CB    1 
ATOM   2982 O OG1   . THR A 1 396 ? -0.946  -59.599 -7.987  1.00 38.91  ? 394 THR A OG1   1 
ATOM   2983 C CG2   . THR A 1 396 ? -2.380  -58.169 -6.659  1.00 43.52  ? 394 THR A CG2   1 
ATOM   2984 N N     . PRO A 1 397 ? -2.814  -60.603 -3.987  1.00 35.32  ? 395 PRO A N     1 
ATOM   2985 C CA    . PRO A 1 397 ? -3.359  -60.448 -2.632  1.00 35.03  ? 395 PRO A CA    1 
ATOM   2986 C C     . PRO A 1 397 ? -2.548  -61.145 -1.520  1.00 34.32  ? 395 PRO A C     1 
ATOM   2987 O O     . PRO A 1 397 ? -2.546  -60.669 -0.402  1.00 29.36  ? 395 PRO A O     1 
ATOM   2988 C CB    . PRO A 1 397 ? -4.739  -61.096 -2.694  1.00 32.39  ? 395 PRO A CB    1 
ATOM   2989 C CG    . PRO A 1 397 ? -4.667  -62.028 -3.862  1.00 36.36  ? 395 PRO A CG    1 
ATOM   2990 C CD    . PRO A 1 397 ? -3.673  -61.437 -4.837  1.00 33.93  ? 395 PRO A CD    1 
ATOM   2991 N N     . ILE A 1 398 ? -1.896  -62.261 -1.834  1.00 29.41  ? 396 ILE A N     1 
ATOM   2992 C CA    . ILE A 1 398 ? -0.970  -62.928 -0.883  1.00 29.98  ? 396 ILE A CA    1 
ATOM   2993 C C     . ILE A 1 398 ? 0.180   -61.966 -0.615  1.00 30.20  ? 396 ILE A C     1 
ATOM   2994 O O     . ILE A 1 398 ? 0.445   -61.657 0.569   1.00 30.15  ? 396 ILE A O     1 
ATOM   2995 C CB    . ILE A 1 398 ? -0.443  -64.277 -1.406  1.00 30.52  ? 396 ILE A CB    1 
ATOM   2996 C CG1   . ILE A 1 398 ? -1.595  -65.247 -1.719  1.00 30.13  ? 396 ILE A CG1   1 
ATOM   2997 C CG2   . ILE A 1 398 ? 0.535   -64.835 -0.382  1.00 30.49  ? 396 ILE A CG2   1 
ATOM   2998 C CD1   . ILE A 1 398 ? -1.186  -66.602 -2.231  1.00 29.64  ? 396 ILE A CD1   1 
ATOM   2999 N N     . ALA A 1 399 ? 0.797   -61.447 -1.672  1.00 29.85  ? 397 ALA A N     1 
ATOM   3000 C CA    . ALA A 1 399 ? 1.912   -60.480 -1.539  1.00 31.88  ? 397 ALA A CA    1 
ATOM   3001 C C     . ALA A 1 399 ? 1.437   -59.255 -0.731  1.00 33.85  ? 397 ALA A C     1 
ATOM   3002 O O     . ALA A 1 399 ? 2.133   -58.901 0.228   1.00 34.64  ? 397 ALA A O     1 
ATOM   3003 C CB    . ALA A 1 399 ? 2.468   -60.092 -2.876  1.00 29.87  ? 397 ALA A CB    1 
ATOM   3004 N N     . LYS A 1 400 ? 0.292   -58.654 -1.039  1.00 29.36  ? 398 LYS A N     1 
ATOM   3005 C CA    . LYS A 1 400 ? -0.111  -57.415 -0.320  1.00 29.49  ? 398 LYS A CA    1 
ATOM   3006 C C     . LYS A 1 400 ? -0.377  -57.688 1.171   1.00 28.89  ? 398 LYS A C     1 
ATOM   3007 O O     . LYS A 1 400 ? 0.216   -57.005 1.988   1.00 31.58  ? 398 LYS A O     1 
ATOM   3008 C CB    . LYS A 1 400 ? -1.325  -56.779 -1.004  1.00 26.84  ? 398 LYS A CB    1 
ATOM   3009 C CG    . LYS A 1 400 ? -1.679  -55.372 -0.546  1.00 27.82  ? 398 LYS A CG    1 
ATOM   3010 C CD    . LYS A 1 400 ? -2.551  -55.333 0.688   1.00 26.83  ? 398 LYS A CD    1 
ATOM   3011 C CE    . LYS A 1 400 ? -2.482  -54.002 1.398   1.00 25.50  ? 398 LYS A CE    1 
ATOM   3012 N NZ    . LYS A 1 400 ? -3.427  -53.932 2.532   1.00 31.96  ? 398 LYS A NZ    1 
ATOM   3013 N N     . ALA A 1 401 ? -1.219  -58.659 1.501   1.00 28.78  ? 399 ALA A N     1 
ATOM   3014 C CA    . ALA A 1 401 ? -1.630  -58.956 2.883   1.00 29.89  ? 399 ALA A CA    1 
ATOM   3015 C C     . ALA A 1 401 ? -0.457  -59.550 3.676   1.00 29.50  ? 399 ALA A C     1 
ATOM   3016 O O     . ALA A 1 401 ? -0.128  -59.035 4.794   1.00 29.90  ? 399 ALA A O     1 
ATOM   3017 C CB    . ALA A 1 401 ? -2.836  -59.878 2.866   1.00 30.35  ? 399 ALA A CB    1 
ATOM   3018 N N     . PHE A 1 402 ? 0.108   -60.641 3.185   1.00 26.29  ? 400 PHE A N     1 
ATOM   3019 C CA    . PHE A 1 402 ? 1.179   -61.358 3.917   1.00 26.44  ? 400 PHE A CA    1 
ATOM   3020 C C     . PHE A 1 402 ? 2.341   -60.400 4.164   1.00 25.97  ? 400 PHE A C     1 
ATOM   3021 O O     . PHE A 1 402 ? 2.787   -60.284 5.325   1.00 24.68  ? 400 PHE A O     1 
ATOM   3022 C CB    . PHE A 1 402 ? 1.664   -62.601 3.159   1.00 25.40  ? 400 PHE A CB    1 
ATOM   3023 C CG    . PHE A 1 402 ? 2.699   -63.429 3.877   1.00 24.58  ? 400 PHE A CG    1 
ATOM   3024 C CD1   . PHE A 1 402 ? 2.365   -64.225 4.947   1.00 26.26  ? 400 PHE A CD1   1 
ATOM   3025 C CD2   . PHE A 1 402 ? 4.020   -63.414 3.475   1.00 28.89  ? 400 PHE A CD2   1 
ATOM   3026 C CE1   . PHE A 1 402 ? 3.324   -64.994 5.595   1.00 27.36  ? 400 PHE A CE1   1 
ATOM   3027 C CE2   . PHE A 1 402 ? 4.976   -64.205 4.100   1.00 27.35  ? 400 PHE A CE2   1 
ATOM   3028 C CZ    . PHE A 1 402 ? 4.626   -64.989 5.165   1.00 26.10  ? 400 PHE A CZ    1 
ATOM   3029 N N     . MET A 1 403 ? 2.865   -59.781 3.105   1.00 26.98  ? 401 MET A N     1 
ATOM   3030 C CA    . MET A 1 403 ? 4.110   -58.979 3.238   1.00 30.45  ? 401 MET A CA    1 
ATOM   3031 C C     . MET A 1 403 ? 3.871   -57.765 4.165   1.00 29.67  ? 401 MET A C     1 
ATOM   3032 O O     . MET A 1 403 ? 4.824   -57.420 4.857   1.00 25.59  ? 401 MET A O     1 
ATOM   3033 C CB    . MET A 1 403 ? 4.672   -58.518 1.892   1.00 30.97  ? 401 MET A CB    1 
ATOM   3034 C CG    . MET A 1 403 ? 5.058   -59.620 0.942   1.00 29.93  ? 401 MET A CG    1 
ATOM   3035 S SD    . MET A 1 403 ? 5.911   -58.876 -0.462  1.00 32.94  ? 401 MET A SD    1 
ATOM   3036 C CE    . MET A 1 403 ? 6.242   -60.347 -1.429  1.00 32.20  ? 401 MET A CE    1 
ATOM   3037 N N     . THR A 1 404 ? 2.665   -57.165 4.206   1.00 28.87  ? 402 THR A N     1 
ATOM   3038 C CA    . THR A 1 404 ? 2.346   -56.038 5.133   1.00 28.21  ? 402 THR A CA    1 
ATOM   3039 C C     . THR A 1 404 ? 2.313   -56.571 6.560   1.00 27.34  ? 402 THR A C     1 
ATOM   3040 O O     . THR A 1 404 ? 3.106   -56.115 7.357   1.00 32.59  ? 402 THR A O     1 
ATOM   3041 C CB    . THR A 1 404 ? 1.133   -55.202 4.694   1.00 27.48  ? 402 THR A CB    1 
ATOM   3042 O OG1   . THR A 1 404 ? -0.107  -55.891 4.466   1.00 24.95  ? 402 THR A OG1   1 
ATOM   3043 C CG2   . THR A 1 404 ? 1.502   -54.473 3.421   1.00 26.79  ? 402 THR A CG2   1 
ATOM   3044 N N     . GLU A 1 405 ? 1.541   -57.617 6.805   1.00 27.22  ? 403 GLU A N     1 
ATOM   3045 C CA    . GLU A 1 405 ? 1.456   -58.239 8.145   1.00 24.85  ? 403 GLU A CA    1 
ATOM   3046 C C     . GLU A 1 405 ? 2.846   -58.636 8.670   1.00 26.11  ? 403 GLU A C     1 
ATOM   3047 O O     . GLU A 1 405 ? 3.133   -58.298 9.818   1.00 25.08  ? 403 GLU A O     1 
ATOM   3048 C CB    . GLU A 1 405 ? 0.495   -59.425 8.092   1.00 26.92  ? 403 GLU A CB    1 
ATOM   3049 C CG    . GLU A 1 405 ? -0.950  -59.031 7.851   1.00 28.81  ? 403 GLU A CG    1 
ATOM   3050 C CD    . GLU A 1 405 ? -1.683  -58.527 9.081   1.00 29.06  ? 403 GLU A CD    1 
ATOM   3051 O OE1   . GLU A 1 405 ? -2.705  -57.849 8.916   1.00 29.50  ? 403 GLU A OE1   1 
ATOM   3052 O OE2   . GLU A 1 405 ? -1.225  -58.814 10.197  1.00 27.80  ? 403 GLU A OE2   1 
ATOM   3053 N N     . VAL A 1 406 ? 3.666   -59.334 7.878   1.00 25.86  ? 404 VAL A N     1 
ATOM   3054 C CA    . VAL A 1 406 ? 4.965   -59.820 8.447   1.00 25.93  ? 404 VAL A CA    1 
ATOM   3055 C C     . VAL A 1 406 ? 5.976   -58.650 8.453   1.00 27.81  ? 404 VAL A C     1 
ATOM   3056 O O     . VAL A 1 406 ? 6.981   -58.676 9.248   1.00 25.61  ? 404 VAL A O     1 
ATOM   3057 C CB    . VAL A 1 406 ? 5.475   -61.080 7.725   1.00 26.90  ? 404 VAL A CB    1 
ATOM   3058 C CG1   . VAL A 1 406 ? 4.476   -62.234 7.833   1.00 26.00  ? 404 VAL A CG1   1 
ATOM   3059 C CG2   . VAL A 1 406 ? 5.875   -60.817 6.280   1.00 26.91  ? 404 VAL A CG2   1 
ATOM   3060 N N     . GLY A 1 407 ? 5.701   -57.640 7.619   1.00 26.44  ? 405 GLY A N     1 
ATOM   3061 C CA    . GLY A 1 407 ? 6.406   -56.350 7.630   1.00 27.72  ? 405 GLY A CA    1 
ATOM   3062 C C     . GLY A 1 407 ? 6.230   -55.603 8.942   1.00 27.48  ? 405 GLY A C     1 
ATOM   3063 O O     . GLY A 1 407 ? 7.235   -55.099 9.476   1.00 31.04  ? 405 GLY A O     1 
ATOM   3064 N N     . PHE A 1 408 ? 4.997   -55.515 9.440   1.00 29.15  ? 406 PHE A N     1 
ATOM   3065 C CA    . PHE A 1 408 ? 4.667   -54.910 10.751  1.00 28.84  ? 406 PHE A CA    1 
ATOM   3066 C C     . PHE A 1 408 ? 5.351   -55.711 11.867  1.00 29.19  ? 406 PHE A C     1 
ATOM   3067 O O     . PHE A 1 408 ? 6.011   -55.116 12.741  1.00 31.15  ? 406 PHE A O     1 
ATOM   3068 C CB    . PHE A 1 408 ? 3.152   -54.871 10.941  1.00 28.84  ? 406 PHE A CB    1 
ATOM   3069 C CG    . PHE A 1 408 ? 2.714   -54.136 12.182  1.00 29.63  ? 406 PHE A CG    1 
ATOM   3070 C CD1   . PHE A 1 408 ? 2.864   -52.749 12.276  1.00 29.41  ? 406 PHE A CD1   1 
ATOM   3071 C CD2   . PHE A 1 408 ? 2.138   -54.816 13.248  1.00 26.49  ? 406 PHE A CD2   1 
ATOM   3072 C CE1   . PHE A 1 408 ? 2.435   -52.061 13.404  1.00 25.89  ? 406 PHE A CE1   1 
ATOM   3073 C CE2   . PHE A 1 408 ? 1.687   -54.113 14.360  1.00 25.94  ? 406 PHE A CE2   1 
ATOM   3074 C CZ    . PHE A 1 408 ? 1.853   -52.743 14.434  1.00 25.00  ? 406 PHE A CZ    1 
ATOM   3075 N N     . GLU A 1 409 ? 5.227   -57.044 11.849  1.00 26.92  ? 407 GLU A N     1 
ATOM   3076 C CA    . GLU A 1 409 ? 5.940   -57.868 12.844  1.00 27.73  ? 407 GLU A CA    1 
ATOM   3077 C C     . GLU A 1 409 ? 7.428   -57.474 12.819  1.00 27.67  ? 407 GLU A C     1 
ATOM   3078 O O     . GLU A 1 409 ? 7.999   -57.182 13.896  1.00 28.97  ? 407 GLU A O     1 
ATOM   3079 C CB    . GLU A 1 409 ? 5.747   -59.359 12.590  1.00 27.64  ? 407 GLU A CB    1 
ATOM   3080 C CG    . GLU A 1 409 ? 6.277   -60.219 13.731  1.00 28.62  ? 407 GLU A CG    1 
ATOM   3081 C CD    . GLU A 1 409 ? 6.435   -61.670 13.297  1.00 33.22  ? 407 GLU A CD    1 
ATOM   3082 O OE1   . GLU A 1 409 ? 7.322   -62.365 13.810  1.00 31.43  ? 407 GLU A OE1   1 
ATOM   3083 O OE2   . GLU A 1 409 ? 5.676   -62.092 12.413  1.00 33.05  ? 407 GLU A OE2   1 
ATOM   3084 N N     . SER A 1 410 ? 8.052   -57.503 11.643  1.00 26.86  ? 408 SER A N     1 
ATOM   3085 C CA    . SER A 1 410 ? 9.510   -57.280 11.472  1.00 27.78  ? 408 SER A CA    1 
ATOM   3086 C C     . SER A 1 410 ? 9.932   -55.894 11.989  1.00 28.25  ? 408 SER A C     1 
ATOM   3087 O O     . SER A 1 410 ? 11.007  -55.806 12.636  1.00 27.55  ? 408 SER A O     1 
ATOM   3088 C CB    . SER A 1 410 ? 9.891   -57.492 10.048  1.00 25.78  ? 408 SER A CB    1 
ATOM   3089 O OG    . SER A 1 410 ? 9.720   -58.846 9.776   1.00 24.02  ? 408 SER A OG    1 
ATOM   3090 N N     . ALA A 1 411 ? 9.113   -54.866 11.758  1.00 25.53  ? 409 ALA A N     1 
ATOM   3091 C CA    . ALA A 1 411 ? 9.374   -53.494 12.249  1.00 24.10  ? 409 ALA A CA    1 
ATOM   3092 C C     . ALA A 1 411 ? 9.368   -53.530 13.780  1.00 23.69  ? 409 ALA A C     1 
ATOM   3093 O O     . ALA A 1 411 ? 10.251  -52.889 14.405  1.00 23.01  ? 409 ALA A O     1 
ATOM   3094 C CB    . ALA A 1 411 ? 8.357   -52.505 11.675  1.00 23.73  ? 409 ALA A CB    1 
ATOM   3095 N N     . ASN A 1 412 ? 8.414   -54.254 14.356  1.00 23.42  ? 410 ASN A N     1 
ATOM   3096 C CA    . ASN A 1 412 ? 8.311   -54.418 15.832  1.00 25.93  ? 410 ASN A CA    1 
ATOM   3097 C C     . ASN A 1 412 ? 9.501   -55.205 16.374  1.00 28.08  ? 410 ASN A C     1 
ATOM   3098 O O     . ASN A 1 412 ? 10.029  -54.771 17.384  1.00 26.78  ? 410 ASN A O     1 
ATOM   3099 C CB    . ASN A 1 412 ? 6.960   -54.958 16.249  1.00 24.52  ? 410 ASN A CB    1 
ATOM   3100 C CG    . ASN A 1 412 ? 5.948   -53.834 16.212  1.00 27.75  ? 410 ASN A CG    1 
ATOM   3101 O OD1   . ASN A 1 412 ? 5.982   -52.920 17.041  1.00 26.66  ? 410 ASN A OD1   1 
ATOM   3102 N ND2   . ASN A 1 412 ? 5.100   -53.848 15.195  1.00 30.13  ? 410 ASN A ND2   1 
ATOM   3103 N N     . HIS A 1 413 ? 9.989   -56.238 15.688  1.00 30.71  ? 411 HIS A N     1 
ATOM   3104 C CA    . HIS A 1 413 ? 11.248  -56.895 16.123  1.00 33.46  ? 411 HIS A CA    1 
ATOM   3105 C C     . HIS A 1 413 ? 12.347  -55.831 16.167  1.00 34.09  ? 411 HIS A C     1 
ATOM   3106 O O     . HIS A 1 413 ? 13.065  -55.746 17.193  1.00 33.89  ? 411 HIS A O     1 
ATOM   3107 C CB    . HIS A 1 413 ? 11.641  -58.092 15.247  1.00 31.98  ? 411 HIS A CB    1 
ATOM   3108 C CG    . HIS A 1 413 ? 10.721  -59.251 15.397  1.00 29.50  ? 411 HIS A CG    1 
ATOM   3109 N ND1   . HIS A 1 413 ? 10.332  -59.713 16.629  1.00 29.18  ? 411 HIS A ND1   1 
ATOM   3110 C CD2   . HIS A 1 413 ? 10.139  -60.057 14.480  1.00 31.08  ? 411 HIS A CD2   1 
ATOM   3111 C CE1   . HIS A 1 413 ? 9.549   -60.755 16.486  1.00 29.10  ? 411 HIS A CE1   1 
ATOM   3112 N NE2   . HIS A 1 413 ? 9.421   -60.998 15.171  1.00 28.86  ? 411 HIS A NE2   1 
ATOM   3113 N N     . GLY A 1 414 ? 12.480  -55.021 15.123  1.00 30.39  ? 412 GLY A N     1 
ATOM   3114 C CA    . GLY A 1 414 ? 13.476  -53.936 15.113  1.00 29.43  ? 412 GLY A CA    1 
ATOM   3115 C C     . GLY A 1 414 ? 13.481  -53.123 16.398  1.00 29.48  ? 412 GLY A C     1 
ATOM   3116 O O     . GLY A 1 414 ? 14.544  -53.013 17.011  1.00 29.97  ? 412 GLY A O     1 
ATOM   3117 N N     . VAL A 1 415 ? 12.339  -52.555 16.773  1.00 28.36  ? 413 VAL A N     1 
ATOM   3118 C CA    . VAL A 1 415 ? 12.221  -51.806 18.058  1.00 28.72  ? 413 VAL A CA    1 
ATOM   3119 C C     . VAL A 1 415 ? 12.636  -52.712 19.226  1.00 28.13  ? 413 VAL A C     1 
ATOM   3120 O O     . VAL A 1 415 ? 13.402  -52.240 20.064  1.00 28.20  ? 413 VAL A O     1 
ATOM   3121 C CB    . VAL A 1 415 ? 10.805  -51.230 18.264  1.00 25.66  ? 413 VAL A CB    1 
ATOM   3122 C CG1   . VAL A 1 415 ? 10.615  -50.676 19.665  1.00 25.04  ? 413 VAL A CG1   1 
ATOM   3123 C CG2   . VAL A 1 415 ? 10.458  -50.183 17.219  1.00 26.61  ? 413 VAL A CG2   1 
ATOM   3124 N N     . GLN A 1 416 ? 12.164  -53.959 19.255  1.00 27.70  ? 414 GLN A N     1 
ATOM   3125 C CA    . GLN A 1 416 ? 12.450  -54.842 20.420  1.00 31.12  ? 414 GLN A CA    1 
ATOM   3126 C C     . GLN A 1 416 ? 13.974  -54.967 20.671  1.00 30.90  ? 414 GLN A C     1 
ATOM   3127 O O     . GLN A 1 416 ? 14.408  -54.972 21.858  1.00 27.05  ? 414 GLN A O     1 
ATOM   3128 C CB    . GLN A 1 416 ? 11.785  -56.195 20.206  1.00 31.57  ? 414 GLN A CB    1 
ATOM   3129 C CG    . GLN A 1 416 ? 11.589  -56.994 21.478  1.00 30.63  ? 414 GLN A CG    1 
ATOM   3130 C CD    . GLN A 1 416 ? 10.596  -56.317 22.384  1.00 30.65  ? 414 GLN A CD    1 
ATOM   3131 O OE1   . GLN A 1 416 ? 9.699   -55.606 21.917  1.00 29.71  ? 414 GLN A OE1   1 
ATOM   3132 N NE2   . GLN A 1 416 ? 10.769  -56.524 23.687  1.00 27.18  ? 414 GLN A NE2   1 
ATOM   3133 N N     . ILE A 1 417 ? 14.770  -55.026 19.610  1.00 28.35  ? 415 ILE A N     1 
ATOM   3134 C CA    . ILE A 1 417 ? 16.255  -55.179 19.657  1.00 30.68  ? 415 ILE A CA    1 
ATOM   3135 C C     . ILE A 1 417 ? 16.888  -53.948 20.330  1.00 31.39  ? 415 ILE A C     1 
ATOM   3136 O O     . ILE A 1 417 ? 17.950  -54.084 21.001  1.00 30.63  ? 415 ILE A O     1 
ATOM   3137 C CB    . ILE A 1 417 ? 16.798  -55.439 18.236  1.00 29.02  ? 415 ILE A CB    1 
ATOM   3138 C CG1   . ILE A 1 417 ? 16.331  -56.817 17.753  1.00 30.97  ? 415 ILE A CG1   1 
ATOM   3139 C CG2   . ILE A 1 417 ? 18.311  -55.296 18.186  1.00 28.21  ? 415 ILE A CG2   1 
ATOM   3140 C CD1   . ILE A 1 417 ? 16.581  -57.125 16.271  1.00 31.38  ? 415 ILE A CD1   1 
ATOM   3141 N N     . PHE A 1 418 ? 16.285  -52.778 20.161  1.00 29.55  ? 416 PHE A N     1 
ATOM   3142 C CA    . PHE A 1 418 ? 16.826  -51.525 20.743  1.00 30.01  ? 416 PHE A CA    1 
ATOM   3143 C C     . PHE A 1 418 ? 16.360  -51.369 22.191  1.00 30.13  ? 416 PHE A C     1 
ATOM   3144 O O     . PHE A 1 418 ? 16.799  -50.418 22.836  1.00 30.34  ? 416 PHE A O     1 
ATOM   3145 C CB    . PHE A 1 418 ? 16.353  -50.329 19.917  1.00 30.24  ? 416 PHE A CB    1 
ATOM   3146 C CG    . PHE A 1 418 ? 17.076  -50.071 18.621  1.00 31.95  ? 416 PHE A CG    1 
ATOM   3147 C CD1   . PHE A 1 418 ? 17.002  -50.969 17.571  1.00 32.25  ? 416 PHE A CD1   1 
ATOM   3148 C CD2   . PHE A 1 418 ? 17.800  -48.905 18.438  1.00 33.52  ? 416 PHE A CD2   1 
ATOM   3149 C CE1   . PHE A 1 418 ? 17.653  -50.719 16.376  1.00 32.07  ? 416 PHE A CE1   1 
ATOM   3150 C CE2   . PHE A 1 418 ? 18.450  -48.655 17.241  1.00 32.91  ? 416 PHE A CE2   1 
ATOM   3151 C CZ    . PHE A 1 418 ? 18.374  -49.562 16.212  1.00 30.82  ? 416 PHE A CZ    1 
ATOM   3152 N N     . GLY A 1 419 ? 15.543  -52.292 22.687  1.00 28.74  ? 417 GLY A N     1 
ATOM   3153 C CA    . GLY A 1 419 ? 14.930  -52.185 24.029  1.00 29.35  ? 417 GLY A CA    1 
ATOM   3154 C C     . GLY A 1 419 ? 14.211  -50.858 24.188  1.00 29.06  ? 417 GLY A C     1 
ATOM   3155 O O     . GLY A 1 419 ? 13.626  -50.412 23.227  1.00 33.22  ? 417 GLY A O     1 
ATOM   3156 N N     . GLY A 1 420 ? 14.268  -50.247 25.366  1.00 32.34  ? 418 GLY A N     1 
ATOM   3157 C CA    . GLY A 1 420 ? 13.669  -48.931 25.644  1.00 31.32  ? 418 GLY A CA    1 
ATOM   3158 C C     . GLY A 1 420 ? 14.044  -47.917 24.586  1.00 28.80  ? 418 GLY A C     1 
ATOM   3159 O O     . GLY A 1 420 ? 13.187  -47.143 24.195  1.00 30.56  ? 418 GLY A O     1 
ATOM   3160 N N     . HIS A 1 421 ? 15.282  -47.920 24.131  1.00 28.81  ? 419 HIS A N     1 
ATOM   3161 C CA    . HIS A 1 421 ? 15.800  -46.918 23.160  1.00 32.95  ? 419 HIS A CA    1 
ATOM   3162 C C     . HIS A 1 421 ? 14.972  -46.959 21.863  1.00 31.59  ? 419 HIS A C     1 
ATOM   3163 O O     . HIS A 1 421 ? 14.822  -45.907 21.243  1.00 31.92  ? 419 HIS A O     1 
ATOM   3164 C CB    . HIS A 1 421 ? 17.297  -47.126 22.907  1.00 32.52  ? 419 HIS A CB    1 
ATOM   3165 C CG    . HIS A 1 421 ? 18.121  -46.667 24.052  1.00 35.21  ? 419 HIS A CG    1 
ATOM   3166 N ND1   . HIS A 1 421 ? 18.501  -47.521 25.079  1.00 38.07  ? 419 HIS A ND1   1 
ATOM   3167 C CD2   . HIS A 1 421 ? 18.636  -45.454 24.341  1.00 34.03  ? 419 HIS A CD2   1 
ATOM   3168 C CE1   . HIS A 1 421 ? 19.230  -46.847 25.944  1.00 34.47  ? 419 HIS A CE1   1 
ATOM   3169 N NE2   . HIS A 1 421 ? 19.319  -45.585 25.515  1.00 36.63  ? 419 HIS A NE2   1 
ATOM   3170 N N     . GLY A 1 422 ? 14.358  -48.095 21.544  1.00 29.36  ? 420 GLY A N     1 
ATOM   3171 C CA    . GLY A 1 422 ? 13.519  -48.243 20.337  1.00 33.29  ? 420 GLY A CA    1 
ATOM   3172 C C     . GLY A 1 422 ? 12.203  -47.486 20.398  1.00 32.89  ? 420 GLY A C     1 
ATOM   3173 O O     . GLY A 1 422 ? 11.650  -47.216 19.333  1.00 28.53  ? 420 GLY A O     1 
ATOM   3174 N N     . PHE A 1 423 ? 11.729  -47.151 21.597  1.00 29.70  ? 421 PHE A N     1 
ATOM   3175 C CA    . PHE A 1 423 ? 10.485  -46.344 21.759  1.00 28.34  ? 421 PHE A CA    1 
ATOM   3176 C C     . PHE A 1 423 ? 10.760  -44.854 21.562  1.00 27.42  ? 421 PHE A C     1 
ATOM   3177 O O     . PHE A 1 423 ? 9.805   -44.088 21.509  1.00 29.95  ? 421 PHE A O     1 
ATOM   3178 C CB    . PHE A 1 423 ? 9.942   -46.534 23.176  1.00 28.47  ? 421 PHE A CB    1 
ATOM   3179 C CG    . PHE A 1 423 ? 8.509   -46.143 23.427  1.00 27.05  ? 421 PHE A CG    1 
ATOM   3180 C CD1   . PHE A 1 423 ? 7.466   -46.848 22.854  1.00 30.29  ? 421 PHE A CD1   1 
ATOM   3181 C CD2   . PHE A 1 423 ? 8.206   -45.094 24.278  1.00 28.32  ? 421 PHE A CD2   1 
ATOM   3182 C CE1   . PHE A 1 423 ? 6.151   -46.495 23.106  1.00 29.25  ? 421 PHE A CE1   1 
ATOM   3183 C CE2   . PHE A 1 423 ? 6.891   -44.740 24.527  1.00 25.99  ? 421 PHE A CE2   1 
ATOM   3184 C CZ    . PHE A 1 423 ? 5.867   -45.443 23.943  1.00 28.03  ? 421 PHE A CZ    1 
ATOM   3185 N N     . ILE A 1 424 ? 12.024  -44.472 21.424  1.00 28.98  ? 422 ILE A N     1 
ATOM   3186 C CA    . ILE A 1 424 ? 12.440  -43.032 21.348  1.00 31.57  ? 422 ILE A CA    1 
ATOM   3187 C C     . ILE A 1 424 ? 12.524  -42.598 19.883  1.00 29.37  ? 422 ILE A C     1 
ATOM   3188 O O     . ILE A 1 424 ? 13.021  -43.374 19.106  1.00 29.56  ? 422 ILE A O     1 
ATOM   3189 C CB    . ILE A 1 424 ? 13.774  -42.854 22.105  1.00 32.13  ? 422 ILE A CB    1 
ATOM   3190 C CG1   . ILE A 1 424 ? 13.629  -43.334 23.542  1.00 35.76  ? 422 ILE A CG1   1 
ATOM   3191 C CG2   . ILE A 1 424 ? 14.264  -41.432 22.055  1.00 34.88  ? 422 ILE A CG2   1 
ATOM   3192 C CD1   . ILE A 1 424 ? 12.513  -42.618 24.276  1.00 34.82  ? 422 ILE A CD1   1 
ATOM   3193 N N     . ALA A 1 425 ? 12.049  -41.400 19.551  1.00 30.84  ? 423 ALA A N     1 
ATOM   3194 C CA    . ALA A 1 425 ? 11.867  -40.899 18.169  1.00 37.53  ? 423 ALA A CA    1 
ATOM   3195 C C     . ALA A 1 425 ? 13.205  -40.893 17.418  1.00 44.85  ? 423 ALA A C     1 
ATOM   3196 O O     . ALA A 1 425 ? 13.236  -41.254 16.197  1.00 50.05  ? 423 ALA A O     1 
ATOM   3197 C CB    . ALA A 1 425 ? 11.227  -39.524 18.190  1.00 38.05  ? 423 ALA A CB    1 
ATOM   3198 N N     . GLU A 1 426 ? 14.278  -40.537 18.122  1.00 46.01  ? 424 GLU A N     1 
ATOM   3199 C CA    . GLU A 1 426 ? 15.616  -40.245 17.536  1.00 50.04  ? 424 GLU A CA    1 
ATOM   3200 C C     . GLU A 1 426 ? 16.095  -41.430 16.678  1.00 45.41  ? 424 GLU A C     1 
ATOM   3201 O O     . GLU A 1 426 ? 16.651  -41.165 15.629  1.00 41.83  ? 424 GLU A O     1 
ATOM   3202 C CB    . GLU A 1 426 ? 16.609  -39.833 18.634  1.00 56.66  ? 424 GLU A CB    1 
ATOM   3203 C CG    . GLU A 1 426 ? 16.486  -38.354 19.035  1.00 64.97  ? 424 GLU A CG    1 
ATOM   3204 C CD    . GLU A 1 426 ? 15.180  -37.898 19.699  1.00 65.39  ? 424 GLU A CD    1 
ATOM   3205 O OE1   . GLU A 1 426 ? 14.819  -36.691 19.605  1.00 66.81  ? 424 GLU A OE1   1 
ATOM   3206 O OE2   . GLU A 1 426 ? 14.521  -38.738 20.327  1.00 58.99  ? 424 GLU A OE2   1 
ATOM   3207 N N     . HIS A 1 427 ? 15.834  -42.678 17.067  1.00 45.42  ? 425 HIS A N     1 
ATOM   3208 C CA    . HIS A 1 427 ? 16.410  -43.858 16.356  1.00 41.54  ? 425 HIS A CA    1 
ATOM   3209 C C     . HIS A 1 427 ? 15.662  -44.242 15.071  1.00 40.20  ? 425 HIS A C     1 
ATOM   3210 O O     . HIS A 1 427 ? 16.242  -44.974 14.272  1.00 41.02  ? 425 HIS A O     1 
ATOM   3211 C CB    . HIS A 1 427 ? 16.547  -45.021 17.337  1.00 44.64  ? 425 HIS A CB    1 
ATOM   3212 C CG    . HIS A 1 427 ? 17.250  -44.646 18.594  1.00 48.71  ? 425 HIS A CG    1 
ATOM   3213 N ND1   . HIS A 1 427 ? 18.599  -44.854 18.769  1.00 48.56  ? 425 HIS A ND1   1 
ATOM   3214 C CD2   . HIS A 1 427 ? 16.803  -44.067 19.727  1.00 45.83  ? 425 HIS A CD2   1 
ATOM   3215 C CE1   . HIS A 1 427 ? 18.953  -44.428 19.962  1.00 55.46  ? 425 HIS A CE1   1 
ATOM   3216 N NE2   . HIS A 1 427 ? 17.870  -43.939 20.568  1.00 50.26  ? 425 HIS A NE2   1 
ATOM   3217 N N     . GLY A 1 428 ? 14.426  -43.794 14.890  1.00 41.06  ? 426 GLY A N     1 
ATOM   3218 C CA    . GLY A 1 428 ? 13.708  -44.042 13.626  1.00 36.63  ? 426 GLY A CA    1 
ATOM   3219 C C     . GLY A 1 428 ? 12.975  -45.367 13.575  1.00 33.07  ? 426 GLY A C     1 
ATOM   3220 O O     . GLY A 1 428 ? 12.202  -45.562 12.641  1.00 35.77  ? 426 GLY A O     1 
ATOM   3221 N N     . MET A 1 429 ? 13.240  -46.249 14.528  1.00 31.52  ? 427 MET A N     1 
ATOM   3222 C CA    A MET A 1 429 ? 12.593  -47.591 14.549  0.50 30.94  ? 427 MET A CA    1 
ATOM   3223 C CA    B MET A 1 429 ? 12.593  -47.591 14.547  0.50 30.94  ? 427 MET A CA    1 
ATOM   3224 C C     . MET A 1 429 ? 11.079  -47.558 14.876  1.00 32.32  ? 427 MET A C     1 
ATOM   3225 O O     . MET A 1 429 ? 10.115  -48.285 14.350  1.00 29.29  ? 427 MET A O     1 
ATOM   3226 C CB    A MET A 1 429 ? 13.310  -48.496 15.555  0.50 33.32  ? 427 MET A CB    1 
ATOM   3227 C CB    B MET A 1 429 ? 13.310  -48.500 15.550  0.50 33.32  ? 427 MET A CB    1 
ATOM   3228 C CG    A MET A 1 429 ? 14.787  -48.670 15.261  0.50 36.09  ? 427 MET A CG    1 
ATOM   3229 C CG    B MET A 1 429 ? 14.797  -48.638 15.282  0.50 36.09  ? 427 MET A CG    1 
ATOM   3230 S SD    A MET A 1 429 ? 15.091  -49.574 13.722  0.50 42.02  ? 427 MET A SD    1 
ATOM   3231 S SD    B MET A 1 429 ? 15.161  -49.217 13.605  0.50 42.02  ? 427 MET A SD    1 
ATOM   3232 C CE    A MET A 1 429 ? 15.789  -48.273 12.708  0.50 42.74  ? 427 MET A CE    1 
ATOM   3233 C CE    B MET A 1 429 ? 15.004  -50.987 13.824  0.50 42.74  ? 427 MET A CE    1 
ATOM   3234 N N     . GLU A 1 430 ? 10.736  -46.596 15.729  1.00 31.97  ? 428 GLU A N     1 
ATOM   3235 C CA    . GLU A 1 430 ? 9.311   -46.458 16.121  1.00 31.21  ? 428 GLU A CA    1 
ATOM   3236 C C     . GLU A 1 430 ? 8.522   -45.820 14.969  1.00 30.35  ? 428 GLU A C     1 
ATOM   3237 O O     . GLU A 1 430 ? 7.338   -46.120 14.848  1.00 28.84  ? 428 GLU A O     1 
ATOM   3238 C CB    . GLU A 1 430 ? 9.217   -45.681 17.434  1.00 28.65  ? 428 GLU A CB    1 
ATOM   3239 C CG    . GLU A 1 430 ? 9.754   -44.266 17.369  1.00 29.53  ? 428 GLU A CG    1 
ATOM   3240 C CD    . GLU A 1 430 ? 8.708   -43.221 17.028  1.00 30.74  ? 428 GLU A CD    1 
ATOM   3241 O OE1   . GLU A 1 430 ? 9.090   -42.135 16.579  1.00 34.24  ? 428 GLU A OE1   1 
ATOM   3242 O OE2   . GLU A 1 430 ? 7.519   -43.508 17.195  1.00 31.23  ? 428 GLU A OE2   1 
ATOM   3243 N N     . GLN A 1 431 ? 9.165   -44.968 14.169  1.00 31.61  ? 429 GLN A N     1 
ATOM   3244 C CA    . GLN A 1 431 ? 8.486   -44.387 12.981  1.00 30.35  ? 429 GLN A CA    1 
ATOM   3245 C C     . GLN A 1 431 ? 8.225   -45.517 11.987  1.00 31.52  ? 429 GLN A C     1 
ATOM   3246 O O     . GLN A 1 431 ? 7.151   -45.534 11.397  1.00 31.43  ? 429 GLN A O     1 
ATOM   3247 C CB    . GLN A 1 431 ? 9.316   -43.285 12.328  1.00 28.92  ? 429 GLN A CB    1 
ATOM   3248 C CG    . GLN A 1 431 ? 8.638   -42.629 11.132  1.00 29.69  ? 429 GLN A CG    1 
ATOM   3249 C CD    . GLN A 1 431 ? 9.556   -41.755 10.310  1.00 32.60  ? 429 GLN A CD    1 
ATOM   3250 O OE1   . GLN A 1 431 ? 10.555  -41.235 10.794  1.00 31.86  ? 429 GLN A OE1   1 
ATOM   3251 N NE2   . GLN A 1 431 ? 9.213   -41.574 9.047   1.00 33.65  ? 429 GLN A NE2   1 
ATOM   3252 N N     . ASN A 1 432 ? 9.195   -46.412 11.823  1.00 29.76  ? 430 ASN A N     1 
ATOM   3253 C CA    . ASN A 1 432 ? 9.034   -47.571 10.911  1.00 30.74  ? 430 ASN A CA    1 
ATOM   3254 C C     . ASN A 1 432 ? 7.751   -48.316 11.288  1.00 31.16  ? 430 ASN A C     1 
ATOM   3255 O O     . ASN A 1 432 ? 6.995   -48.655 10.385  1.00 34.42  ? 430 ASN A O     1 
ATOM   3256 C CB    . ASN A 1 432 ? 10.281  -48.461 10.918  1.00 29.94  ? 430 ASN A CB    1 
ATOM   3257 C CG    . ASN A 1 432 ? 10.301  -49.500 9.820   1.00 29.29  ? 430 ASN A CG    1 
ATOM   3258 O OD1   . ASN A 1 432 ? 9.943   -49.215 8.685   1.00 28.50  ? 430 ASN A OD1   1 
ATOM   3259 N ND2   . ASN A 1 432 ? 10.742  -50.700 10.150  1.00 29.53  ? 430 ASN A ND2   1 
ATOM   3260 N N     . VAL A 1 433 ? 7.521   -48.513 12.586  1.00 28.86  ? 431 VAL A N     1 
ATOM   3261 C CA    . VAL A 1 433 ? 6.317   -49.246 13.066  1.00 28.57  ? 431 VAL A CA    1 
ATOM   3262 C C     . VAL A 1 433 ? 5.063   -48.416 12.768  1.00 26.24  ? 431 VAL A C     1 
ATOM   3263 O O     . VAL A 1 433 ? 4.087   -48.990 12.284  1.00 26.81  ? 431 VAL A O     1 
ATOM   3264 C CB    . VAL A 1 433 ? 6.440   -49.598 14.561  1.00 28.84  ? 431 VAL A CB    1 
ATOM   3265 C CG1   . VAL A 1 433 ? 5.158   -50.210 15.097  1.00 31.12  ? 431 VAL A CG1   1 
ATOM   3266 C CG2   . VAL A 1 433 ? 7.623   -50.510 14.835  1.00 29.22  ? 431 VAL A CG2   1 
ATOM   3267 N N     . ARG A 1 434 ? 5.112   -47.116 13.048  1.00 24.20  ? 432 ARG A N     1 
ATOM   3268 C CA    . ARG A 1 434 ? 3.916   -46.266 12.856  1.00 25.19  ? 432 ARG A CA    1 
ATOM   3269 C C     . ARG A 1 434 ? 3.582   -46.108 11.358  1.00 26.38  ? 432 ARG A C     1 
ATOM   3270 O O     . ARG A 1 434 ? 2.385   -46.115 11.030  1.00 25.44  ? 432 ARG A O     1 
ATOM   3271 C CB    . ARG A 1 434 ? 4.173   -44.918 13.514  1.00 26.29  ? 432 ARG A CB    1 
ATOM   3272 C CG    . ARG A 1 434 ? 4.117   -44.969 15.032  1.00 25.51  ? 432 ARG A CG    1 
ATOM   3273 C CD    . ARG A 1 434 ? 4.221   -43.567 15.541  1.00 25.99  ? 432 ARG A CD    1 
ATOM   3274 N NE    . ARG A 1 434 ? 5.543   -42.988 15.310  1.00 27.58  ? 432 ARG A NE    1 
ATOM   3275 C CZ    . ARG A 1 434 ? 5.820   -41.923 14.589  1.00 27.48  ? 432 ARG A CZ    1 
ATOM   3276 N NH1   . ARG A 1 434 ? 4.879   -41.326 13.876  1.00 29.01  ? 432 ARG A NH1   1 
ATOM   3277 N NH2   . ARG A 1 434 ? 7.079   -41.514 14.531  1.00 29.22  ? 432 ARG A NH2   1 
ATOM   3278 N N     . ASP A 1 435 ? 4.585   -45.936 10.495  1.00 26.25  ? 433 ASP A N     1 
ATOM   3279 C CA    . ASP A 1 435 ? 4.419   -45.882 9.011   1.00 27.50  ? 433 ASP A CA    1 
ATOM   3280 C C     . ASP A 1 435 ? 3.870   -47.243 8.544   1.00 27.20  ? 433 ASP A C     1 
ATOM   3281 O O     . ASP A 1 435 ? 3.001   -47.269 7.648   1.00 25.39  ? 433 ASP A O     1 
ATOM   3282 C CB    . ASP A 1 435 ? 5.732   -45.467 8.327   1.00 24.22  ? 433 ASP A CB    1 
ATOM   3283 C CG    . ASP A 1 435 ? 6.145   -44.013 8.563   1.00 24.26  ? 433 ASP A CG    1 
ATOM   3284 O OD1   . ASP A 1 435 ? 5.377   -43.260 9.136   1.00 25.74  ? 433 ASP A OD1   1 
ATOM   3285 O OD2   . ASP A 1 435 ? 7.242   -43.646 8.174   1.00 25.39  ? 433 ASP A OD2   1 
ATOM   3286 N N     . SER A 1 436 ? 4.345   -48.342 9.139   1.00 26.96  ? 434 SER A N     1 
ATOM   3287 C CA    . SER A 1 436 ? 3.975   -49.720 8.723   1.00 26.85  ? 434 SER A CA    1 
ATOM   3288 C C     . SER A 1 436 ? 2.480   -49.956 8.953   1.00 28.10  ? 434 SER A C     1 
ATOM   3289 O O     . SER A 1 436 ? 1.867   -50.683 8.130   1.00 25.31  ? 434 SER A O     1 
ATOM   3290 C CB    . SER A 1 436 ? 4.812   -50.764 9.413   1.00 27.61  ? 434 SER A CB    1 
ATOM   3291 O OG    . SER A 1 436 ? 4.368   -52.079 9.107   1.00 27.36  ? 434 SER A OG    1 
ATOM   3292 N N     . ARG A 1 437 ? 1.892   -49.396 10.014  1.00 27.18  ? 435 ARG A N     1 
ATOM   3293 C CA    . ARG A 1 437 ? 0.555   -49.858 10.453  1.00 26.64  ? 435 ARG A CA    1 
ATOM   3294 C C     . ARG A 1 437 ? -0.506  -49.601 9.368   1.00 28.26  ? 435 ARG A C     1 
ATOM   3295 O O     . ARG A 1 437 ? -1.463  -50.431 9.269   1.00 27.29  ? 435 ARG A O     1 
ATOM   3296 C CB    . ARG A 1 437 ? 0.151   -49.160 11.744  1.00 27.87  ? 435 ARG A CB    1 
ATOM   3297 C CG    . ARG A 1 437 ? -1.132  -49.723 12.343  1.00 29.85  ? 435 ARG A CG    1 
ATOM   3298 C CD    . ARG A 1 437 ? -1.024  -51.197 12.684  1.00 26.58  ? 435 ARG A CD    1 
ATOM   3299 N NE    . ARG A 1 437 ? -2.259  -51.841 13.091  1.00 25.26  ? 435 ARG A NE    1 
ATOM   3300 C CZ    . ARG A 1 437 ? -3.178  -52.275 12.250  1.00 24.58  ? 435 ARG A CZ    1 
ATOM   3301 N NH1   . ARG A 1 437 ? -3.015  -52.062 10.956  1.00 25.31  ? 435 ARG A NH1   1 
ATOM   3302 N NH2   . ARG A 1 437 ? -4.235  -52.937 12.690  1.00 23.26  ? 435 ARG A NH2   1 
ATOM   3303 N N     . ILE A 1 438 ? -0.418  -48.477 8.639   1.00 24.78  ? 436 ILE A N     1 
ATOM   3304 C CA    . ILE A 1 438 ? -1.391  -48.169 7.544   1.00 27.57  ? 436 ILE A CA    1 
ATOM   3305 C C     . ILE A 1 438 ? -1.383  -49.293 6.490   1.00 27.88  ? 436 ILE A C     1 
ATOM   3306 O O     . ILE A 1 438 ? -2.444  -49.555 5.905   1.00 24.65  ? 436 ILE A O     1 
ATOM   3307 C CB    . ILE A 1 438 ? -1.139  -46.779 6.907   1.00 27.61  ? 436 ILE A CB    1 
ATOM   3308 C CG1   . ILE A 1 438 ? -2.330  -46.272 6.094   1.00 30.14  ? 436 ILE A CG1   1 
ATOM   3309 C CG2   . ILE A 1 438 ? 0.117   -46.763 6.071   1.00 25.02  ? 436 ILE A CG2   1 
ATOM   3310 C CD1   . ILE A 1 438 ? -3.645  -46.239 6.827   1.00 30.87  ? 436 ILE A CD1   1 
ATOM   3311 N N     . SER A 1 439 ? -0.248  -49.960 6.263   1.00 27.56  ? 437 SER A N     1 
ATOM   3312 C CA    . SER A 1 439 ? -0.076  -50.890 5.118   1.00 27.41  ? 437 SER A CA    1 
ATOM   3313 C C     . SER A 1 439 ? -1.088  -52.049 5.192   1.00 28.40  ? 437 SER A C     1 
ATOM   3314 O O     . SER A 1 439 ? -1.500  -52.547 4.127   1.00 27.70  ? 437 SER A O     1 
ATOM   3315 C CB    . SER A 1 439 ? 1.364   -51.340 4.970   1.00 26.83  ? 437 SER A CB    1 
ATOM   3316 O OG    . SER A 1 439 ? 1.789   -52.175 6.039   1.00 27.59  ? 437 SER A OG    1 
ATOM   3317 N N     . MET A 1 440 ? -1.589  -52.405 6.368   1.00 26.68  ? 438 MET A N     1 
ATOM   3318 C CA    . MET A 1 440 ? -2.638  -53.463 6.490   1.00 28.30  ? 438 MET A CA    1 
ATOM   3319 C C     . MET A 1 440 ? -4.071  -52.884 6.386   1.00 25.77  ? 438 MET A C     1 
ATOM   3320 O O     . MET A 1 440 ? -5.042  -53.666 6.339   1.00 26.91  ? 438 MET A O     1 
ATOM   3321 C CB    . MET A 1 440 ? -2.467  -54.197 7.825   1.00 31.02  ? 438 MET A CB    1 
ATOM   3322 C CG    . MET A 1 440 ? -1.169  -54.993 7.972   1.00 32.78  ? 438 MET A CG    1 
ATOM   3323 S SD    . MET A 1 440 ? -0.267  -54.614 9.510   1.00 50.53  ? 438 MET A SD    1 
ATOM   3324 C CE    . MET A 1 440 ? 0.643   -53.227 8.870   1.00 40.68  ? 438 MET A CE    1 
ATOM   3325 N N     . LEU A 1 441 ? -4.203  -51.567 6.291   1.00 26.18  ? 439 LEU A N     1 
ATOM   3326 C CA    . LEU A 1 441 ? -5.544  -50.929 6.270   1.00 28.83  ? 439 LEU A CA    1 
ATOM   3327 C C     . LEU A 1 441 ? -5.899  -50.407 4.871   1.00 29.08  ? 439 LEU A C     1 
ATOM   3328 O O     . LEU A 1 441 ? -7.039  -50.609 4.452   1.00 34.73  ? 439 LEU A O     1 
ATOM   3329 C CB    . LEU A 1 441 ? -5.563  -49.809 7.313   1.00 30.43  ? 439 LEU A CB    1 
ATOM   3330 C CG    . LEU A 1 441 ? -5.185  -50.221 8.734   1.00 28.59  ? 439 LEU A CG    1 
ATOM   3331 C CD1   . LEU A 1 441 ? -4.944  -49.001 9.604   1.00 30.64  ? 439 LEU A CD1   1 
ATOM   3332 C CD2   . LEU A 1 441 ? -6.260  -51.105 9.344   1.00 29.74  ? 439 LEU A CD2   1 
ATOM   3333 N N     . TYR A 1 442 ? -4.965  -49.760 4.183   1.00 28.15  ? 440 TYR A N     1 
ATOM   3334 C CA    . TYR A 1 442 ? -5.290  -49.160 2.863   1.00 29.17  ? 440 TYR A CA    1 
ATOM   3335 C C     . TYR A 1 442 ? -4.954  -50.129 1.719   1.00 28.57  ? 440 TYR A C     1 
ATOM   3336 O O     . TYR A 1 442 ? -4.358  -51.170 1.988   1.00 28.80  ? 440 TYR A O     1 
ATOM   3337 C CB    . TYR A 1 442 ? -4.730  -47.734 2.734   1.00 27.99  ? 440 TYR A CB    1 
ATOM   3338 C CG    . TYR A 1 442 ? -3.241  -47.533 2.620   1.00 29.34  ? 440 TYR A CG    1 
ATOM   3339 C CD1   . TYR A 1 442 ? -2.347  -48.588 2.568   1.00 25.83  ? 440 TYR A CD1   1 
ATOM   3340 C CD2   . TYR A 1 442 ? -2.730  -46.249 2.561   1.00 26.33  ? 440 TYR A CD2   1 
ATOM   3341 C CE1   . TYR A 1 442 ? -0.985  -48.369 2.456   1.00 24.71  ? 440 TYR A CE1   1 
ATOM   3342 C CE2   . TYR A 1 442 ? -1.374  -46.012 2.455   1.00 26.11  ? 440 TYR A CE2   1 
ATOM   3343 C CZ    . TYR A 1 442 ? -0.497  -47.076 2.400   1.00 25.74  ? 440 TYR A CZ    1 
ATOM   3344 O OH    . TYR A 1 442 ? 0.837   -46.827 2.295   1.00 27.70  ? 440 TYR A OH    1 
ATOM   3345 N N     . GLU A 1 443 ? -5.367  -49.785 0.499   1.00 35.18  ? 441 GLU A N     1 
ATOM   3346 C CA    . GLU A 1 443 ? -5.160  -50.642 -0.697  1.00 34.86  ? 441 GLU A CA    1 
ATOM   3347 C C     . GLU A 1 443 ? -5.761  -52.025 -0.432  1.00 33.21  ? 441 GLU A C     1 
ATOM   3348 O O     . GLU A 1 443 ? -5.143  -53.020 -0.806  1.00 32.51  ? 441 GLU A O     1 
ATOM   3349 C CB    . GLU A 1 443 ? -3.684  -50.671 -1.094  1.00 46.04  ? 441 GLU A CB    1 
ATOM   3350 C CG    . GLU A 1 443 ? -3.415  -50.109 -2.477  1.00 62.59  ? 441 GLU A CG    1 
ATOM   3351 C CD    . GLU A 1 443 ? -4.530  -50.285 -3.493  1.00 71.70  ? 441 GLU A CD    1 
ATOM   3352 O OE1   . GLU A 1 443 ? -4.990  -49.266 -4.036  1.00 82.30  ? 441 GLU A OE1   1 
ATOM   3353 O OE2   . GLU A 1 443 ? -4.927  -51.438 -3.747  1.00 72.64  ? 441 GLU A OE2   1 
ATOM   3354 N N     . GLY A 1 444 ? -6.928  -52.056 0.200   1.00 30.53  ? 442 GLY A N     1 
ATOM   3355 C CA    . GLY A 1 444 ? -7.552  -53.337 0.558   1.00 31.54  ? 442 GLY A CA    1 
ATOM   3356 C C     . GLY A 1 444 ? -7.062  -53.866 1.887   1.00 31.27  ? 442 GLY A C     1 
ATOM   3357 O O     . GLY A 1 444 ? -5.880  -54.172 1.985   1.00 30.25  ? 442 GLY A O     1 
ATOM   3358 N N     . THR A 1 445 ? -7.959  -53.984 2.858   1.00 28.56  ? 443 THR A N     1 
ATOM   3359 C CA    . THR A 1 445 ? -7.612  -54.499 4.205   1.00 29.34  ? 443 THR A CA    1 
ATOM   3360 C C     . THR A 1 445 ? -7.145  -55.950 4.131   1.00 29.48  ? 443 THR A C     1 
ATOM   3361 O O     . THR A 1 445 ? -7.497  -56.628 3.174   1.00 32.14  ? 443 THR A O     1 
ATOM   3362 C CB    . THR A 1 445 ? -8.812  -54.405 5.159   1.00 29.41  ? 443 THR A CB    1 
ATOM   3363 O OG1   . THR A 1 445 ? -9.837  -55.287 4.710   1.00 25.73  ? 443 THR A OG1   1 
ATOM   3364 C CG2   . THR A 1 445 ? -9.348  -52.996 5.289   1.00 28.76  ? 443 THR A CG2   1 
ATOM   3365 N N     . THR A 1 446 ? -6.412  -56.398 5.141   1.00 29.80  ? 444 THR A N     1 
ATOM   3366 C CA    . THR A 1 446 ? -5.983  -57.816 5.211   1.00 32.28  ? 444 THR A CA    1 
ATOM   3367 C C     . THR A 1 446 ? -7.217  -58.713 5.028   1.00 30.34  ? 444 THR A C     1 
ATOM   3368 O O     . THR A 1 446 ? -7.158  -59.605 4.184   1.00 32.94  ? 444 THR A O     1 
ATOM   3369 C CB    . THR A 1 446 ? -5.188  -58.069 6.503   1.00 29.67  ? 444 THR A CB    1 
ATOM   3370 O OG1   . THR A 1 446 ? -4.011  -57.263 6.481   1.00 31.57  ? 444 THR A OG1   1 
ATOM   3371 C CG2   . THR A 1 446 ? -4.818  -59.523 6.692   1.00 27.85  ? 444 THR A CG2   1 
ATOM   3372 N N     . GLY A 1 447 ? -8.289  -58.458 5.779   1.00 28.31  ? 445 GLY A N     1 
ATOM   3373 C CA    . GLY A 1 447 ? -9.534  -59.248 5.688   1.00 29.12  ? 445 GLY A CA    1 
ATOM   3374 C C     . GLY A 1 447 ? -10.073 -59.267 4.267   1.00 30.97  ? 445 GLY A C     1 
ATOM   3375 O O     . GLY A 1 447 ? -10.548 -60.340 3.815   1.00 31.62  ? 445 GLY A O     1 
ATOM   3376 N N     . VAL A 1 448 ? -9.998  -58.142 3.553   1.00 32.35  ? 446 VAL A N     1 
ATOM   3377 C CA    . VAL A 1 448 ? -10.590 -58.042 2.185   1.00 29.80  ? 446 VAL A CA    1 
ATOM   3378 C C     . VAL A 1 448 ? -9.709  -58.779 1.165   1.00 31.61  ? 446 VAL A C     1 
ATOM   3379 O O     . VAL A 1 448 ? -10.263 -59.496 0.332   1.00 28.83  ? 446 VAL A O     1 
ATOM   3380 C CB    . VAL A 1 448 ? -10.852 -56.570 1.820   1.00 33.06  ? 446 VAL A CB    1 
ATOM   3381 C CG1   . VAL A 1 448 ? -11.056 -56.367 0.328   1.00 33.10  ? 446 VAL A CG1   1 
ATOM   3382 C CG2   . VAL A 1 448 ? -12.023 -56.007 2.607   1.00 32.87  ? 446 VAL A CG2   1 
ATOM   3383 N N     . GLN A 1 449 ? -8.391  -58.609 1.238   1.00 31.10  ? 447 GLN A N     1 
ATOM   3384 C CA    . GLN A 1 449 ? -7.458  -59.354 0.357   1.00 32.50  ? 447 GLN A CA    1 
ATOM   3385 C C     . GLN A 1 449 ? -7.653  -60.857 0.594   1.00 33.56  ? 447 GLN A C     1 
ATOM   3386 O O     . GLN A 1 449 ? -7.709  -61.591 -0.389  1.00 35.61  ? 447 GLN A O     1 
ATOM   3387 C CB    . GLN A 1 449 ? -6.022  -58.906 0.628   1.00 33.42  ? 447 GLN A CB    1 
ATOM   3388 C CG    . GLN A 1 449 ? -5.816  -57.403 0.561   1.00 33.33  ? 447 GLN A CG    1 
ATOM   3389 C CD    . GLN A 1 449 ? -5.631  -56.924 -0.855  1.00 34.58  ? 447 GLN A CD    1 
ATOM   3390 O OE1   . GLN A 1 449 ? -5.473  -57.712 -1.781  1.00 40.00  ? 447 GLN A OE1   1 
ATOM   3391 N NE2   . GLN A 1 449 ? -5.647  -55.616 -1.033  1.00 35.01  ? 447 GLN A NE2   1 
ATOM   3392 N N     . ALA A 1 450 ? -7.762  -61.277 1.854   1.00 34.20  ? 448 ALA A N     1 
ATOM   3393 C CA    . ALA A 1 450 ? -8.000  -62.695 2.222   1.00 31.13  ? 448 ALA A CA    1 
ATOM   3394 C C     . ALA A 1 450 ? -9.298  -63.203 1.569   1.00 30.89  ? 448 ALA A C     1 
ATOM   3395 O O     . ALA A 1 450 ? -9.296  -64.299 0.998   1.00 25.56  ? 448 ALA A O     1 
ATOM   3396 C CB    . ALA A 1 450 ? -8.053  -62.814 3.723   1.00 30.59  ? 448 ALA A CB    1 
ATOM   3397 N N     . LEU A 1 451 ? -10.370 -62.421 1.609   1.00 33.04  ? 449 LEU A N     1 
ATOM   3398 C CA    . LEU A 1 451 ? -11.629 -62.823 0.928   1.00 37.57  ? 449 LEU A CA    1 
ATOM   3399 C C     . LEU A 1 451 ? -11.424 -62.857 -0.592  1.00 35.34  ? 449 LEU A C     1 
ATOM   3400 O O     . LEU A 1 451 ? -11.925 -63.782 -1.217  1.00 37.98  ? 449 LEU A O     1 
ATOM   3401 C CB    . LEU A 1 451 ? -12.740 -61.853 1.335   1.00 42.74  ? 449 LEU A CB    1 
ATOM   3402 C CG    . LEU A 1 451 ? -14.115 -62.472 1.561   1.00 45.34  ? 449 LEU A CG    1 
ATOM   3403 C CD1   . LEU A 1 451 ? -14.071 -63.480 2.696   1.00 42.17  ? 449 LEU A CD1   1 
ATOM   3404 C CD2   . LEU A 1 451 ? -15.142 -61.389 1.848   1.00 44.48  ? 449 LEU A CD2   1 
ATOM   3405 N N     . ASP A 1 452 ? -10.693 -61.895 -1.153  1.00 37.55  ? 450 ASP A N     1 
ATOM   3406 C CA    . ASP A 1 452 ? -10.383 -61.898 -2.603  1.00 39.36  ? 450 ASP A CA    1 
ATOM   3407 C C     . ASP A 1 452 ? -9.676  -63.213 -2.974  1.00 40.71  ? 450 ASP A C     1 
ATOM   3408 O O     . ASP A 1 452 ? -10.193 -63.926 -3.836  1.00 48.20  ? 450 ASP A O     1 
ATOM   3409 C CB    . ASP A 1 452 ? -9.544  -60.671 -2.969  1.00 45.50  ? 450 ASP A CB    1 
ATOM   3410 C CG    . ASP A 1 452 ? -9.194  -60.518 -4.441  1.00 48.13  ? 450 ASP A CG    1 
ATOM   3411 O OD1   . ASP A 1 452 ? -10.128 -60.365 -5.234  1.00 44.56  ? 450 ASP A OD1   1 
ATOM   3412 O OD2   . ASP A 1 452 ? -7.977  -60.528 -4.763  1.00 51.79  ? 450 ASP A OD2   1 
ATOM   3413 N N     . LEU A 1 453 ? -8.518  -63.509 -2.380  1.00 40.43  ? 451 LEU A N     1 
ATOM   3414 C CA    . LEU A 1 453 ? -7.774  -64.781 -2.592  1.00 38.63  ? 451 LEU A CA    1 
ATOM   3415 C C     . LEU A 1 453 ? -8.720  -65.998 -2.527  1.00 36.51  ? 451 LEU A C     1 
ATOM   3416 O O     . LEU A 1 453 ? -8.854  -66.647 -3.552  1.00 41.10  ? 451 LEU A O     1 
ATOM   3417 C CB    . LEU A 1 453 ? -6.665  -64.907 -1.548  1.00 38.70  ? 451 LEU A CB    1 
ATOM   3418 C CG    . LEU A 1 453 ? -5.840  -66.188 -1.654  1.00 37.23  ? 451 LEU A CG    1 
ATOM   3419 C CD1   . LEU A 1 453 ? -5.102  -66.256 -2.999  1.00 36.36  ? 451 LEU A CD1   1 
ATOM   3420 C CD2   . LEU A 1 453 ? -4.881  -66.301 -0.481  1.00 35.76  ? 451 LEU A CD2   1 
ATOM   3421 N N     . LEU A 1 454 ? -9.359  -66.288 -1.383  1.00 36.36  ? 452 LEU A N     1 
ATOM   3422 C CA    . LEU A 1 454 ? -10.090 -67.565 -1.124  1.00 33.58  ? 452 LEU A CA    1 
ATOM   3423 C C     . LEU A 1 454 ? -11.416 -67.605 -1.879  1.00 34.66  ? 452 LEU A C     1 
ATOM   3424 O O     . LEU A 1 454 ? -11.677 -68.615 -2.514  1.00 35.63  ? 452 LEU A O     1 
ATOM   3425 C CB    . LEU A 1 454 ? -10.364 -67.745 0.361   1.00 31.07  ? 452 LEU A CB    1 
ATOM   3426 C CG    . LEU A 1 454 ? -10.894 -69.122 0.752   1.00 33.87  ? 452 LEU A CG    1 
ATOM   3427 C CD1   . LEU A 1 454 ? -9.992  -70.260 0.259   1.00 33.60  ? 452 LEU A CD1   1 
ATOM   3428 C CD2   . LEU A 1 454 ? -11.030 -69.217 2.256   1.00 35.40  ? 452 LEU A CD2   1 
ATOM   3429 N N     . GLY A 1 455 ? -12.220 -66.549 -1.765  1.00 34.78  ? 453 GLY A N     1 
ATOM   3430 C CA    . GLY A 1 455 ? -13.586 -66.480 -2.301  1.00 36.79  ? 453 GLY A CA    1 
ATOM   3431 C C     . GLY A 1 455 ? -13.600 -66.227 -3.797  1.00 36.39  ? 453 GLY A C     1 
ATOM   3432 O O     . GLY A 1 455 ? -14.236 -66.983 -4.492  1.00 41.16  ? 453 GLY A O     1 
ATOM   3433 N N     . ARG A 1 456 ? -12.897 -65.211 -4.281  1.00 37.11  ? 454 ARG A N     1 
ATOM   3434 C CA    . ARG A 1 456 ? -12.993 -64.750 -5.691  1.00 41.10  ? 454 ARG A CA    1 
ATOM   3435 C C     . ARG A 1 456 ? -12.089 -65.592 -6.604  1.00 36.46  ? 454 ARG A C     1 
ATOM   3436 O O     . ARG A 1 456 ? -12.514 -65.926 -7.687  1.00 39.73  ? 454 ARG A O     1 
ATOM   3437 C CB    . ARG A 1 456 ? -12.652 -63.260 -5.772  1.00 46.54  ? 454 ARG A CB    1 
ATOM   3438 C CG    . ARG A 1 456 ? -13.713 -62.430 -6.478  1.00 55.64  ? 454 ARG A CG    1 
ATOM   3439 C CD    . ARG A 1 456 ? -13.139 -61.125 -6.994  1.00 66.28  ? 454 ARG A CD    1 
ATOM   3440 N NE    . ARG A 1 456 ? -12.243 -61.341 -8.135  1.00 73.80  ? 454 ARG A NE    1 
ATOM   3441 C CZ    . ARG A 1 456 ? -12.537 -61.123 -9.426  1.00 76.64  ? 454 ARG A CZ    1 
ATOM   3442 N NH1   . ARG A 1 456 ? -11.615 -61.359 -10.348 1.00 79.26  ? 454 ARG A NH1   1 
ATOM   3443 N NH2   . ARG A 1 456 ? -13.723 -60.666 -9.803  1.00 73.44  ? 454 ARG A NH2   1 
ATOM   3444 N N     . LYS A 1 457 ? -10.878 -65.930 -6.188  1.00 34.07  ? 455 LYS A N     1 
ATOM   3445 C CA    . LYS A 1 457 ? -9.876  -66.542 -7.085  1.00 35.05  ? 455 LYS A CA    1 
ATOM   3446 C C     . LYS A 1 457 ? -9.841  -68.046 -6.821  1.00 35.92  ? 455 LYS A C     1 
ATOM   3447 O O     . LYS A 1 457 ? -10.126 -68.797 -7.779  1.00 39.85  ? 455 LYS A O     1 
ATOM   3448 C CB    . LYS A 1 457 ? -8.560  -65.791 -6.904  1.00 39.19  ? 455 LYS A CB    1 
ATOM   3449 C CG    . LYS A 1 457 ? -8.756  -64.278 -6.906  1.00 40.27  ? 455 LYS A CG    1 
ATOM   3450 C CD    . LYS A 1 457 ? -7.758  -63.538 -7.737  1.00 43.39  ? 455 LYS A CD    1 
ATOM   3451 C CE    . LYS A 1 457 ? -7.957  -62.035 -7.744  1.00 46.37  ? 455 LYS A CE    1 
ATOM   3452 N NZ    . LYS A 1 457 ? -6.658  -61.315 -7.659  1.00 45.43  ? 455 LYS A NZ    1 
ATOM   3453 N N     . VAL A 1 458 ? -9.594  -68.487 -5.583  1.00 29.97  ? 456 VAL A N     1 
ATOM   3454 C CA    . VAL A 1 458 ? -9.356  -69.932 -5.291  1.00 32.93  ? 456 VAL A CA    1 
ATOM   3455 C C     . VAL A 1 458 ? -10.672 -70.720 -5.400  1.00 36.57  ? 456 VAL A C     1 
ATOM   3456 O O     . VAL A 1 458 ? -10.710 -71.628 -6.245  1.00 41.03  ? 456 VAL A O     1 
ATOM   3457 C CB    . VAL A 1 458 ? -8.627  -70.173 -3.957  1.00 33.73  ? 456 VAL A CB    1 
ATOM   3458 C CG1   . VAL A 1 458 ? -8.571  -71.640 -3.593  1.00 36.53  ? 456 VAL A CG1   1 
ATOM   3459 C CG2   . VAL A 1 458 ? -7.219  -69.617 -3.999  1.00 35.86  ? 456 VAL A CG2   1 
ATOM   3460 N N     . LEU A 1 459 ? -11.701 -70.442 -4.595  1.00 36.86  ? 457 LEU A N     1 
ATOM   3461 C CA    . LEU A 1 459 ? -12.941 -71.275 -4.613  1.00 36.11  ? 457 LEU A CA    1 
ATOM   3462 C C     . LEU A 1 459 ? -13.751 -71.034 -5.892  1.00 34.27  ? 457 LEU A C     1 
ATOM   3463 O O     . LEU A 1 459 ? -14.428 -71.967 -6.338  1.00 38.07  ? 457 LEU A O     1 
ATOM   3464 C CB    . LEU A 1 459 ? -13.788 -71.026 -3.363  1.00 32.56  ? 457 LEU A CB    1 
ATOM   3465 C CG    . LEU A 1 459 ? -13.104 -71.395 -2.059  1.00 34.64  ? 457 LEU A CG    1 
ATOM   3466 C CD1   . LEU A 1 459 ? -13.970 -71.062 -0.867  1.00 34.00  ? 457 LEU A CD1   1 
ATOM   3467 C CD2   . LEU A 1 459 ? -12.691 -72.860 -2.051  1.00 37.28  ? 457 LEU A CD2   1 
ATOM   3468 N N     . MET A 1 460 ? -13.709 -69.849 -6.485  1.00 39.94  ? 458 MET A N     1 
ATOM   3469 C CA    . MET A 1 460 ? -14.460 -69.585 -7.746  1.00 46.87  ? 458 MET A CA    1 
ATOM   3470 C C     . MET A 1 460 ? -13.891 -70.416 -8.913  1.00 48.33  ? 458 MET A C     1 
ATOM   3471 O O     . MET A 1 460 ? -14.628 -70.602 -9.892  1.00 50.63  ? 458 MET A O     1 
ATOM   3472 C CB    . MET A 1 460 ? -14.417 -68.110 -8.159  1.00 53.82  ? 458 MET A CB    1 
ATOM   3473 C CG    . MET A 1 460 ? -15.601 -67.694 -9.008  1.00 54.32  ? 458 MET A CG    1 
ATOM   3474 S SD    . MET A 1 460 ? -16.817 -66.860 -7.974  1.00 73.83  ? 458 MET A SD    1 
ATOM   3475 C CE    . MET A 1 460 ? -17.166 -68.069 -6.690  1.00 67.09  ? 458 MET A CE    1 
ATOM   3476 N N     . THR A 1 461 ? -12.613 -70.819 -8.856  1.00 42.28  ? 459 THR A N     1 
ATOM   3477 C CA    . THR A 1 461 ? -11.920 -71.621 -9.899  1.00 38.25  ? 459 THR A CA    1 
ATOM   3478 C C     . THR A 1 461 ? -11.829 -73.073 -9.419  1.00 38.12  ? 459 THR A C     1 
ATOM   3479 O O     . THR A 1 461 ? -11.041 -73.814 -9.984  1.00 44.12  ? 459 THR A O     1 
ATOM   3480 C CB    . THR A 1 461 ? -10.546 -71.015 -10.226 1.00 38.28  ? 459 THR A CB    1 
ATOM   3481 O OG1   . THR A 1 461 ? -9.704  -71.121 -9.066  1.00 37.70  ? 459 THR A OG1   1 
ATOM   3482 C CG2   . THR A 1 461 ? -10.652 -69.578 -10.700 1.00 32.46  ? 459 THR A CG2   1 
ATOM   3483 N N     . GLN A 1 462 ? -12.586 -73.439 -8.382  1.00 42.62  ? 460 GLN A N     1 
ATOM   3484 C CA    . GLN A 1 462 ? -12.584 -74.780 -7.724  1.00 46.95  ? 460 GLN A CA    1 
ATOM   3485 C C     . GLN A 1 462 ? -11.167 -75.289 -7.463  1.00 43.59  ? 460 GLN A C     1 
ATOM   3486 O O     . GLN A 1 462 ? -10.997 -76.507 -7.513  1.00 46.46  ? 460 GLN A O     1 
ATOM   3487 C CB    . GLN A 1 462 ? -13.302 -75.804 -8.601  1.00 46.44  ? 460 GLN A CB    1 
ATOM   3488 C CG    . GLN A 1 462 ? -14.763 -75.462 -8.805  1.00 48.46  ? 460 GLN A CG    1 
ATOM   3489 C CD    . GLN A 1 462 ? -15.518 -76.681 -9.252  1.00 53.70  ? 460 GLN A CD    1 
ATOM   3490 O OE1   . GLN A 1 462 ? -15.256 -77.807 -8.818  1.00 60.23  ? 460 GLN A OE1   1 
ATOM   3491 N NE2   . GLN A 1 462 ? -16.459 -76.458 -10.146 1.00 55.66  ? 460 GLN A NE2   1 
ATOM   3492 N N     . GLY A 1 463 ? -10.217 -74.391 -7.180  1.00 42.07  ? 461 GLY A N     1 
ATOM   3493 C CA    . GLY A 1 463 ? -8.847  -74.723 -6.740  1.00 39.90  ? 461 GLY A CA    1 
ATOM   3494 C C     . GLY A 1 463 ? -7.816  -74.520 -7.841  1.00 40.37  ? 461 GLY A C     1 
ATOM   3495 O O     . GLY A 1 463 ? -6.596  -74.676 -7.548  1.00 36.52  ? 461 GLY A O     1 
ATOM   3496 N N     . GLU A 1 464 ? -8.267  -74.185 -9.058  1.00 40.21  ? 462 GLU A N     1 
ATOM   3497 C CA    . GLU A 1 464 ? -7.396  -74.022 -10.251 1.00 43.21  ? 462 GLU A CA    1 
ATOM   3498 C C     . GLU A 1 464 ? -6.404  -72.874 -10.028 1.00 39.62  ? 462 GLU A C     1 
ATOM   3499 O O     . GLU A 1 464 ? -5.288  -73.028 -10.454 1.00 43.53  ? 462 GLU A O     1 
ATOM   3500 C CB    . GLU A 1 464 ? -8.208  -73.809 -11.533 1.00 46.86  ? 462 GLU A CB    1 
ATOM   3501 C CG    . GLU A 1 464 ? -8.708  -75.112 -12.139 1.00 56.66  ? 462 GLU A CG    1 
ATOM   3502 C CD    . GLU A 1 464 ? -7.613  -75.981 -12.745 1.00 60.45  ? 462 GLU A CD    1 
ATOM   3503 O OE1   . GLU A 1 464 ? -7.627  -77.207 -12.471 1.00 61.10  ? 462 GLU A OE1   1 
ATOM   3504 O OE2   . GLU A 1 464 ? -6.742  -75.426 -13.483 1.00 59.12  ? 462 GLU A OE2   1 
ATOM   3505 N N     . ALA A 1 465 ? -6.775  -71.766 -9.395  1.00 35.08  ? 463 ALA A N     1 
ATOM   3506 C CA    . ALA A 1 465 ? -5.882  -70.589 -9.251  1.00 35.73  ? 463 ALA A CA    1 
ATOM   3507 C C     . ALA A 1 465 ? -4.598  -70.980 -8.488  1.00 34.78  ? 463 ALA A C     1 
ATOM   3508 O O     . ALA A 1 465 ? -3.550  -70.421 -8.776  1.00 41.16  ? 463 ALA A O     1 
ATOM   3509 C CB    . ALA A 1 465 ? -6.623  -69.471 -8.558  1.00 35.95  ? 463 ALA A CB    1 
ATOM   3510 N N     . LEU A 1 466 ? -4.681  -71.928 -7.562  1.00 34.54  ? 464 LEU A N     1 
ATOM   3511 C CA    . LEU A 1 466 ? -3.558  -72.459 -6.740  1.00 36.68  ? 464 LEU A CA    1 
ATOM   3512 C C     . LEU A 1 466 ? -2.576  -73.298 -7.572  1.00 41.86  ? 464 LEU A C     1 
ATOM   3513 O O     . LEU A 1 466 ? -1.369  -73.352 -7.198  1.00 45.40  ? 464 LEU A O     1 
ATOM   3514 C CB    . LEU A 1 466 ? -4.205  -73.298 -5.639  1.00 38.96  ? 464 LEU A CB    1 
ATOM   3515 C CG    . LEU A 1 466 ? -3.291  -73.931 -4.606  1.00 39.61  ? 464 LEU A CG    1 
ATOM   3516 C CD1   . LEU A 1 466 ? -2.439  -72.886 -3.906  1.00 47.89  ? 464 LEU A CD1   1 
ATOM   3517 C CD2   . LEU A 1 466 ? -4.122  -74.678 -3.595  1.00 39.89  ? 464 LEU A CD2   1 
ATOM   3518 N N     . LYS A 1 467 ? -3.047  -73.920 -8.663  1.00 44.81  ? 465 LYS A N     1 
ATOM   3519 C CA    . LYS A 1 467 ? -2.301  -74.965 -9.425  1.00 44.51  ? 465 LYS A CA    1 
ATOM   3520 C C     . LYS A 1 467 ? -1.042  -74.368 -10.063 1.00 42.12  ? 465 LYS A C     1 
ATOM   3521 O O     . LYS A 1 467 ? -0.001  -75.023 -10.000 1.00 38.54  ? 465 LYS A O     1 
ATOM   3522 C CB    . LYS A 1 467 ? -3.162  -75.596 -10.527 1.00 47.69  ? 465 LYS A CB    1 
ATOM   3523 C CG    . LYS A 1 467 ? -4.347  -76.427 -10.041 1.00 52.12  ? 465 LYS A CG    1 
ATOM   3524 C CD    . LYS A 1 467 ? -3.973  -77.696 -9.290  1.00 56.48  ? 465 LYS A CD    1 
ATOM   3525 C CE    . LYS A 1 467 ? -5.174  -78.443 -8.744  1.00 68.32  ? 465 LYS A CE    1 
ATOM   3526 N NZ    . LYS A 1 467 ? -6.281  -78.511 -9.736  1.00 71.87  ? 465 LYS A NZ    1 
ATOM   3527 N N     . GLY A 1 468 ? -1.139  -73.191 -10.685 1.00 41.07  ? 466 GLY A N     1 
ATOM   3528 C CA    . GLY A 1 468 ? 0.011   -72.531 -11.336 1.00 40.81  ? 466 GLY A CA    1 
ATOM   3529 C C     . GLY A 1 468 ? 1.238   -72.657 -10.450 1.00 40.84  ? 466 GLY A C     1 
ATOM   3530 O O     . GLY A 1 468 ? 2.300   -73.124 -10.947 1.00 45.75  ? 466 GLY A O     1 
ATOM   3531 N N     . PHE A 1 469 ? 1.060   -72.329 -9.165  1.00 38.21  ? 467 PHE A N     1 
ATOM   3532 C CA    . PHE A 1 469 ? 2.134   -72.223 -8.146  1.00 38.76  ? 467 PHE A CA    1 
ATOM   3533 C C     . PHE A 1 469 ? 2.481   -73.622 -7.600  1.00 36.54  ? 467 PHE A C     1 
ATOM   3534 O O     . PHE A 1 469 ? 3.675   -73.916 -7.502  1.00 34.02  ? 467 PHE A O     1 
ATOM   3535 C CB    . PHE A 1 469 ? 1.786   -71.199 -7.044  1.00 38.83  ? 467 PHE A CB    1 
ATOM   3536 C CG    . PHE A 1 469 ? 2.981   -70.791 -6.214  1.00 34.83  ? 467 PHE A CG    1 
ATOM   3537 C CD1   . PHE A 1 469 ? 3.837   -69.788 -6.646  1.00 37.99  ? 467 PHE A CD1   1 
ATOM   3538 C CD2   . PHE A 1 469 ? 3.312   -71.488 -5.063  1.00 31.24  ? 467 PHE A CD2   1 
ATOM   3539 C CE1   . PHE A 1 469 ? 4.966   -69.456 -5.911  1.00 36.07  ? 467 PHE A CE1   1 
ATOM   3540 C CE2   . PHE A 1 469 ? 4.433   -71.157 -4.332  1.00 32.11  ? 467 PHE A CE2   1 
ATOM   3541 C CZ    . PHE A 1 469 ? 5.250   -70.128 -4.746  1.00 33.25  ? 467 PHE A CZ    1 
ATOM   3542 N N     . THR A 1 470 ? 1.502   -74.454 -7.227  1.00 36.65  ? 468 THR A N     1 
ATOM   3543 C CA    . THR A 1 470 ? 1.781   -75.804 -6.657  1.00 39.45  ? 468 THR A CA    1 
ATOM   3544 C C     . THR A 1 470 ? 2.553   -76.660 -7.681  1.00 37.53  ? 468 THR A C     1 
ATOM   3545 O O     . THR A 1 470 ? 3.442   -77.438 -7.255  1.00 37.72  ? 468 THR A O     1 
ATOM   3546 C CB    . THR A 1 470 ? 0.495   -76.454 -6.141  1.00 38.18  ? 468 THR A CB    1 
ATOM   3547 O OG1   . THR A 1 470 ? -0.510  -76.424 -7.152  1.00 39.45  ? 468 THR A OG1   1 
ATOM   3548 C CG2   . THR A 1 470 ? -0.028  -75.745 -4.914  1.00 41.35  ? 468 THR A CG2   1 
ATOM   3549 N N     . LYS A 1 471 ? 2.218   -76.522 -8.961  1.00 35.53  ? 469 LYS A N     1 
ATOM   3550 C CA    . LYS A 1 471 ? 2.910   -77.161 -10.114 1.00 45.23  ? 469 LYS A CA    1 
ATOM   3551 C C     . LYS A 1 471 ? 4.406   -76.817 -10.004 1.00 44.11  ? 469 LYS A C     1 
ATOM   3552 O O     . LYS A 1 471 ? 5.242   -77.755 -9.838  1.00 40.40  ? 469 LYS A O     1 
ATOM   3553 C CB    . LYS A 1 471 ? 2.202   -76.731 -11.417 1.00 51.96  ? 469 LYS A CB    1 
ATOM   3554 C CG    . LYS A 1 471 ? 2.905   -76.980 -12.753 1.00 62.82  ? 469 LYS A CG    1 
ATOM   3555 C CD    . LYS A 1 471 ? 2.496   -78.269 -13.442 1.00 71.86  ? 469 LYS A CD    1 
ATOM   3556 C CE    . LYS A 1 471 ? 2.847   -79.500 -12.617 1.00 79.95  ? 469 LYS A CE    1 
ATOM   3557 N NZ    . LYS A 1 471 ? 2.153   -80.716 -13.099 1.00 80.37  ? 469 LYS A NZ    1 
ATOM   3558 N N     . ILE A 1 472 ? 4.730   -75.521 -10.030 1.00 43.96  ? 470 ILE A N     1 
ATOM   3559 C CA    . ILE A 1 472 ? 6.135   -75.031 -9.917  1.00 43.11  ? 470 ILE A CA    1 
ATOM   3560 C C     . ILE A 1 472 ? 6.782   -75.677 -8.687  1.00 40.32  ? 470 ILE A C     1 
ATOM   3561 O O     . ILE A 1 472 ? 7.952   -76.098 -8.791  1.00 40.55  ? 470 ILE A O     1 
ATOM   3562 C CB    . ILE A 1 472 ? 6.194   -73.487 -9.918  1.00 43.30  ? 470 ILE A CB    1 
ATOM   3563 C CG1   . ILE A 1 472 ? 5.794   -72.927 -11.284 1.00 43.21  ? 470 ILE A CG1   1 
ATOM   3564 C CG2   . ILE A 1 472 ? 7.574   -72.983 -9.510  1.00 41.67  ? 470 ILE A CG2   1 
ATOM   3565 C CD1   . ILE A 1 472 ? 5.562   -71.442 -11.269 1.00 43.99  ? 470 ILE A CD1   1 
ATOM   3566 N N     . VAL A 1 473 ? 6.065   -75.793 -7.572  1.00 35.46  ? 471 VAL A N     1 
ATOM   3567 C CA    . VAL A 1 473 ? 6.680   -76.269 -6.300  1.00 39.60  ? 471 VAL A CA    1 
ATOM   3568 C C     . VAL A 1 473 ? 6.957   -77.771 -6.413  1.00 42.75  ? 471 VAL A C     1 
ATOM   3569 O O     . VAL A 1 473 ? 8.007   -78.239 -5.873  1.00 42.39  ? 471 VAL A O     1 
ATOM   3570 C CB    . VAL A 1 473 ? 5.791   -75.952 -5.087  1.00 40.13  ? 471 VAL A CB    1 
ATOM   3571 C CG1   . VAL A 1 473 ? 6.284   -76.654 -3.835  1.00 38.35  ? 471 VAL A CG1   1 
ATOM   3572 C CG2   . VAL A 1 473 ? 5.687   -74.447 -4.868  1.00 40.83  ? 471 VAL A CG2   1 
ATOM   3573 N N     . HIS A 1 474 ? 6.042   -78.492 -7.063  1.00 42.15  ? 472 HIS A N     1 
ATOM   3574 C CA    . HIS A 1 474 ? 6.078   -79.972 -7.195  1.00 43.42  ? 472 HIS A CA    1 
ATOM   3575 C C     . HIS A 1 474 ? 7.256   -80.365 -8.102  1.00 42.58  ? 472 HIS A C     1 
ATOM   3576 O O     . HIS A 1 474 ? 8.063   -81.216 -7.677  1.00 37.97  ? 472 HIS A O     1 
ATOM   3577 C CB    . HIS A 1 474 ? 4.709   -80.475 -7.657  1.00 44.82  ? 472 HIS A CB    1 
ATOM   3578 C CG    . HIS A 1 474 ? 4.695   -81.911 -8.012  1.00 45.55  ? 472 HIS A CG    1 
ATOM   3579 N ND1   . HIS A 1 474 ? 4.840   -82.898 -7.062  1.00 45.30  ? 472 HIS A ND1   1 
ATOM   3580 C CD2   . HIS A 1 474 ? 4.600   -82.525 -9.213  1.00 48.75  ? 472 HIS A CD2   1 
ATOM   3581 C CE1   . HIS A 1 474 ? 4.818   -84.072 -7.655  1.00 43.26  ? 472 HIS A CE1   1 
ATOM   3582 N NE2   . HIS A 1 474 ? 4.689   -83.867 -8.976  1.00 44.83  ? 472 HIS A NE2   1 
ATOM   3583 N N     . LYS A 1 475 ? 7.400   -79.705 -9.256  1.00 43.19  ? 473 LYS A N     1 
ATOM   3584 C CA    . LYS A 1 475 ? 8.584   -79.844 -10.147 1.00 45.09  ? 473 LYS A CA    1 
ATOM   3585 C C     . LYS A 1 475 ? 9.892   -79.583 -9.376  1.00 46.40  ? 473 LYS A C     1 
ATOM   3586 O O     . LYS A 1 475 ? 10.883  -80.271 -9.639  1.00 49.64  ? 473 LYS A O     1 
ATOM   3587 C CB    . LYS A 1 475 ? 8.461   -78.932 -11.367 1.00 44.79  ? 473 LYS A CB    1 
ATOM   3588 C CG    . LYS A 1 475 ? 8.030   -79.681 -12.622 1.00 62.36  ? 473 LYS A CG    1 
ATOM   3589 C CD    . LYS A 1 475 ? 8.215   -78.921 -13.938 1.00 67.15  ? 473 LYS A CD    1 
ATOM   3590 C CE    . LYS A 1 475 ? 7.126   -79.246 -14.942 1.00 64.50  ? 473 LYS A CE    1 
ATOM   3591 N NZ    . LYS A 1 475 ? 5.782   -78.961 -14.381 1.00 63.48  ? 473 LYS A NZ    1 
ATOM   3592 N N     . PHE A 1 476 ? 9.911   -78.631 -8.448  1.00 42.36  ? 474 PHE A N     1 
ATOM   3593 C CA    . PHE A 1 476 ? 11.128  -78.294 -7.680  1.00 43.32  ? 474 PHE A CA    1 
ATOM   3594 C C     . PHE A 1 476 ? 11.446  -79.482 -6.766  1.00 45.41  ? 474 PHE A C     1 
ATOM   3595 O O     . PHE A 1 476 ? 12.611  -79.895 -6.697  1.00 50.41  ? 474 PHE A O     1 
ATOM   3596 C CB    . PHE A 1 476 ? 10.957  -76.955 -6.942  1.00 42.84  ? 474 PHE A CB    1 
ATOM   3597 C CG    . PHE A 1 476 ? 12.070  -76.646 -5.973  1.00 42.53  ? 474 PHE A CG    1 
ATOM   3598 C CD1   . PHE A 1 476 ? 12.045  -77.156 -4.679  1.00 42.63  ? 474 PHE A CD1   1 
ATOM   3599 C CD2   . PHE A 1 476 ? 13.161  -75.890 -6.371  1.00 37.95  ? 474 PHE A CD2   1 
ATOM   3600 C CE1   . PHE A 1 476 ? 13.077  -76.894 -3.797  1.00 40.56  ? 474 PHE A CE1   1 
ATOM   3601 C CE2   . PHE A 1 476 ? 14.197  -75.645 -5.488  1.00 36.76  ? 474 PHE A CE2   1 
ATOM   3602 C CZ    . PHE A 1 476 ? 14.152  -76.146 -4.209  1.00 38.34  ? 474 PHE A CZ    1 
ATOM   3603 N N     . CYS A 1 477 ? 10.435  -80.045 -6.109  1.00 45.43  ? 475 CYS A N     1 
ATOM   3604 C CA    . CYS A 1 477 ? 10.604  -81.170 -5.147  1.00 49.15  ? 475 CYS A CA    1 
ATOM   3605 C C     . CYS A 1 477 ? 11.056  -82.448 -5.864  1.00 47.82  ? 475 CYS A C     1 
ATOM   3606 O O     . CYS A 1 477 ? 11.839  -83.192 -5.256  1.00 53.99  ? 475 CYS A O     1 
ATOM   3607 C CB    . CYS A 1 477 ? 9.329   -81.406 -4.344  1.00 47.82  ? 475 CYS A CB    1 
ATOM   3608 S SG    . CYS A 1 477 ? 8.959   -80.013 -3.247  1.00 46.79  ? 475 CYS A SG    1 
ATOM   3609 N N     . GLN A 1 478 ? 10.590  -82.686 -7.096  1.00 48.26  ? 476 GLN A N     1 
ATOM   3610 C CA    . GLN A 1 478 ? 11.045  -83.813 -7.953  1.00 49.96  ? 476 GLN A CA    1 
ATOM   3611 C C     . GLN A 1 478 ? 12.471  -83.547 -8.425  1.00 44.45  ? 476 GLN A C     1 
ATOM   3612 O O     . GLN A 1 478 ? 13.324  -84.424 -8.216  1.00 49.14  ? 476 GLN A O     1 
ATOM   3613 C CB    . GLN A 1 478 ? 10.129  -84.009 -9.152  1.00 52.54  ? 476 GLN A CB    1 
ATOM   3614 C CG    . GLN A 1 478 ? 8.774   -84.537 -8.731  1.00 60.71  ? 476 GLN A CG    1 
ATOM   3615 C CD    . GLN A 1 478 ? 7.838   -84.680 -9.903  1.00 67.91  ? 476 GLN A CD    1 
ATOM   3616 O OE1   . GLN A 1 478 ? 8.067   -84.124 -10.979 1.00 80.88  ? 476 GLN A OE1   1 
ATOM   3617 N NE2   . GLN A 1 478 ? 6.774   -85.443 -9.700  1.00 68.76  ? 476 GLN A NE2   1 
ATOM   3618 N N     . ALA A 1 479 ? 12.729  -82.361 -8.968  1.00 41.97  ? 477 ALA A N     1 
ATOM   3619 C CA    . ALA A 1 479 ? 14.056  -81.955 -9.483  1.00 42.04  ? 477 ALA A CA    1 
ATOM   3620 C C     . ALA A 1 479 ? 15.131  -82.027 -8.376  1.00 42.63  ? 477 ALA A C     1 
ATOM   3621 O O     . ALA A 1 479 ? 16.302  -82.112 -8.747  1.00 53.20  ? 477 ALA A O     1 
ATOM   3622 C CB    . ALA A 1 479 ? 13.967  -80.590 -10.132 1.00 39.01  ? 477 ALA A CB    1 
ATOM   3623 N N     . ASN A 1 480 ? 14.779  -82.077 -7.082  1.00 40.48  ? 478 ASN A N     1 
ATOM   3624 C CA    . ASN A 1 480 ? 15.756  -81.988 -5.969  1.00 41.33  ? 478 ASN A CA    1 
ATOM   3625 C C     . ASN A 1 480 ? 15.509  -83.044 -4.877  1.00 48.95  ? 478 ASN A C     1 
ATOM   3626 O O     . ASN A 1 480 ? 16.176  -82.921 -3.820  1.00 44.64  ? 478 ASN A O     1 
ATOM   3627 C CB    . ASN A 1 480 ? 15.755  -80.589 -5.340  1.00 42.71  ? 478 ASN A CB    1 
ATOM   3628 C CG    . ASN A 1 480 ? 16.161  -79.476 -6.287  1.00 40.20  ? 478 ASN A CG    1 
ATOM   3629 O OD1   . ASN A 1 480 ? 17.343  -79.242 -6.512  1.00 42.82  ? 478 ASN A OD1   1 
ATOM   3630 N ND2   . ASN A 1 480 ? 15.190  -78.727 -6.788  1.00 42.82  ? 478 ASN A ND2   1 
ATOM   3631 N N     . GLU A 1 481 ? 14.647  -84.057 -5.095  1.00 56.41  ? 479 GLU A N     1 
ATOM   3632 C CA    . GLU A 1 481 ? 14.437  -85.186 -4.137  1.00 60.47  ? 479 GLU A CA    1 
ATOM   3633 C C     . GLU A 1 481 ? 15.793  -85.811 -3.777  1.00 59.79  ? 479 GLU A C     1 
ATOM   3634 O O     . GLU A 1 481 ? 15.987  -86.116 -2.596  1.00 65.03  ? 479 GLU A O     1 
ATOM   3635 C CB    . GLU A 1 481 ? 13.537  -86.280 -4.725  1.00 69.39  ? 479 GLU A CB    1 
ATOM   3636 C CG    . GLU A 1 481 ? 12.106  -86.305 -4.195  1.00 72.51  ? 479 GLU A CG    1 
ATOM   3637 C CD    . GLU A 1 481 ? 11.121  -87.089 -5.073  1.00 80.38  ? 479 GLU A CD    1 
ATOM   3638 O OE1   . GLU A 1 481 ? 11.369  -88.287 -5.373  1.00 69.57  ? 479 GLU A OE1   1 
ATOM   3639 O OE2   . GLU A 1 481 ? 10.105  -86.498 -5.488  1.00 79.56  ? 479 GLU A OE2   1 
ATOM   3640 N N     . ALA A 1 482 ? 16.692  -85.986 -4.759  1.00 65.35  ? 480 ALA A N     1 
ATOM   3641 C CA    . ALA A 1 482 ? 17.995  -86.692 -4.632  1.00 61.59  ? 480 ALA A CA    1 
ATOM   3642 C C     . ALA A 1 482 ? 19.126  -85.728 -4.257  1.00 58.14  ? 480 ALA A C     1 
ATOM   3643 O O     . ALA A 1 482 ? 20.221  -86.211 -3.973  1.00 55.55  ? 480 ALA A O     1 
ATOM   3644 C CB    . ALA A 1 482 ? 18.345  -87.390 -5.923  1.00 58.77  ? 480 ALA A CB    1 
ATOM   3645 N N     . ASN A 1 483 ? 18.876  -84.422 -4.276  1.00 54.50  ? 481 ASN A N     1 
ATOM   3646 C CA    . ASN A 1 483 ? 19.906  -83.374 -4.051  1.00 55.70  ? 481 ASN A CA    1 
ATOM   3647 C C     . ASN A 1 483 ? 20.246  -83.277 -2.551  1.00 59.17  ? 481 ASN A C     1 
ATOM   3648 O O     . ASN A 1 483 ? 19.414  -82.756 -1.766  1.00 58.97  ? 481 ASN A O     1 
ATOM   3649 C CB    . ASN A 1 483 ? 19.441  -82.057 -4.669  1.00 53.62  ? 481 ASN A CB    1 
ATOM   3650 C CG    . ASN A 1 483 ? 20.386  -80.908 -4.420  1.00 51.96  ? 481 ASN A CG    1 
ATOM   3651 O OD1   . ASN A 1 483 ? 21.315  -81.006 -3.617  1.00 53.22  ? 481 ASN A OD1   1 
ATOM   3652 N ND2   . ASN A 1 483 ? 20.112  -79.801 -5.083  1.00 49.85  ? 481 ASN A ND2   1 
ATOM   3653 N N     . GLU A 1 484 ? 21.439  -83.761 -2.178  1.00 62.34  ? 482 GLU A N     1 
ATOM   3654 C CA    . GLU A 1 484 ? 21.893  -83.938 -0.769  1.00 61.63  ? 482 GLU A CA    1 
ATOM   3655 C C     . GLU A 1 484 ? 21.863  -82.588 -0.045  1.00 54.83  ? 482 GLU A C     1 
ATOM   3656 O O     . GLU A 1 484 ? 21.306  -82.544 1.032   1.00 51.85  ? 482 GLU A O     1 
ATOM   3657 C CB    . GLU A 1 484 ? 23.289  -84.568 -0.688  1.00 64.13  ? 482 GLU A CB    1 
ATOM   3658 C CG    . GLU A 1 484 ? 23.304  -86.077 -0.902  1.00 71.36  ? 482 GLU A CG    1 
ATOM   3659 C CD    . GLU A 1 484 ? 22.424  -86.858 0.064   1.00 77.35  ? 482 GLU A CD    1 
ATOM   3660 O OE1   . GLU A 1 484 ? 21.670  -87.748 -0.388  1.00 70.52  ? 482 GLU A OE1   1 
ATOM   3661 O OE2   . GLU A 1 484 ? 22.485  -86.568 1.275   1.00 83.26  ? 482 GLU A OE2   1 
ATOM   3662 N N     . ALA A 1 485 ? 22.406  -81.518 -0.622  1.00 55.72  ? 483 ALA A N     1 
ATOM   3663 C CA    . ALA A 1 485 ? 22.562  -80.222 0.081   1.00 53.26  ? 483 ALA A CA    1 
ATOM   3664 C C     . ALA A 1 485 ? 21.189  -79.630 0.465   1.00 54.75  ? 483 ALA A C     1 
ATOM   3665 O O     . ALA A 1 485 ? 21.152  -78.871 1.433   1.00 52.86  ? 483 ALA A O     1 
ATOM   3666 C CB    . ALA A 1 485 ? 23.377  -79.273 -0.756  1.00 49.71  ? 483 ALA A CB    1 
ATOM   3667 N N     . VAL A 1 486 ? 20.081  -79.980 -0.202  1.00 53.36  ? 484 VAL A N     1 
ATOM   3668 C CA    . VAL A 1 486 ? 18.746  -79.391 0.138   1.00 55.72  ? 484 VAL A CA    1 
ATOM   3669 C C     . VAL A 1 486 ? 17.684  -80.457 0.441   1.00 57.22  ? 484 VAL A C     1 
ATOM   3670 O O     . VAL A 1 486 ? 16.516  -80.085 0.625   1.00 55.77  ? 484 VAL A O     1 
ATOM   3671 C CB    . VAL A 1 486 ? 18.269  -78.422 -0.956  1.00 56.75  ? 484 VAL A CB    1 
ATOM   3672 C CG1   . VAL A 1 486 ? 19.280  -77.303 -1.140  1.00 55.58  ? 484 VAL A CG1   1 
ATOM   3673 C CG2   . VAL A 1 486 ? 17.959  -79.131 -2.267  1.00 53.19  ? 484 VAL A CG2   1 
ATOM   3674 N N     . LYS A 1 487 ? 18.059  -81.719 0.583   1.00 61.18  ? 485 LYS A N     1 
ATOM   3675 C CA    . LYS A 1 487 ? 17.081  -82.789 0.882   1.00 61.83  ? 485 LYS A CA    1 
ATOM   3676 C C     . LYS A 1 487 ? 16.223  -82.365 2.085   1.00 49.99  ? 485 LYS A C     1 
ATOM   3677 O O     . LYS A 1 487 ? 15.040  -82.690 2.086   1.00 43.99  ? 485 LYS A O     1 
ATOM   3678 C CB    . LYS A 1 487 ? 17.822  -84.115 1.086   1.00 70.27  ? 485 LYS A CB    1 
ATOM   3679 C CG    . LYS A 1 487 ? 16.979  -85.231 1.681   1.00 82.95  ? 485 LYS A CG    1 
ATOM   3680 C CD    . LYS A 1 487 ? 17.631  -86.590 1.564   1.00 90.18  ? 485 LYS A CD    1 
ATOM   3681 C CE    . LYS A 1 487 ? 16.991  -87.629 2.458   1.00 86.05  ? 485 LYS A CE    1 
ATOM   3682 N NZ    . LYS A 1 487 ? 17.983  -88.661 2.829   1.00 88.07  ? 485 LYS A NZ    1 
ATOM   3683 N N     . GLU A 1 488 ? 16.804  -81.673 3.071   1.00 54.75  ? 486 GLU A N     1 
ATOM   3684 C CA    . GLU A 1 488 ? 16.162  -81.346 4.384   1.00 51.92  ? 486 GLU A CA    1 
ATOM   3685 C C     . GLU A 1 488 ? 15.042  -80.294 4.206   1.00 47.21  ? 486 GLU A C     1 
ATOM   3686 O O     . GLU A 1 488 ? 14.128  -80.245 5.043   1.00 41.83  ? 486 GLU A O     1 
ATOM   3687 C CB    . GLU A 1 488 ? 17.224  -80.904 5.407   1.00 53.21  ? 486 GLU A CB    1 
ATOM   3688 C CG    . GLU A 1 488 ? 17.967  -79.620 5.054   1.00 57.28  ? 486 GLU A CG    1 
ATOM   3689 C CD    . GLU A 1 488 ? 18.620  -78.876 6.216   1.00 60.70  ? 486 GLU A CD    1 
ATOM   3690 O OE1   . GLU A 1 488 ? 19.844  -78.645 6.156   1.00 57.13  ? 486 GLU A OE1   1 
ATOM   3691 O OE2   . GLU A 1 488 ? 17.903  -78.484 7.160   1.00 59.19  ? 486 GLU A OE2   1 
ATOM   3692 N N     . PHE A 1 489 ? 15.105  -79.476 3.155   1.00 47.95  ? 487 PHE A N     1 
ATOM   3693 C CA    . PHE A 1 489 ? 14.048  -78.500 2.783   1.00 44.31  ? 487 PHE A CA    1 
ATOM   3694 C C     . PHE A 1 489 ? 13.003  -79.189 1.910   1.00 47.21  ? 487 PHE A C     1 
ATOM   3695 O O     . PHE A 1 489 ? 11.808  -78.849 2.010   1.00 42.48  ? 487 PHE A O     1 
ATOM   3696 C CB    . PHE A 1 489 ? 14.631  -77.284 2.054   1.00 42.67  ? 487 PHE A CB    1 
ATOM   3697 C CG    . PHE A 1 489 ? 15.768  -76.618 2.781   1.00 40.56  ? 487 PHE A CG    1 
ATOM   3698 C CD1   . PHE A 1 489 ? 15.575  -76.065 4.036   1.00 47.32  ? 487 PHE A CD1   1 
ATOM   3699 C CD2   . PHE A 1 489 ? 17.036  -76.566 2.229   1.00 42.38  ? 487 PHE A CD2   1 
ATOM   3700 C CE1   . PHE A 1 489 ? 16.627  -75.465 4.724   1.00 47.80  ? 487 PHE A CE1   1 
ATOM   3701 C CE2   . PHE A 1 489 ? 18.086  -75.976 2.917   1.00 46.74  ? 487 PHE A CE2   1 
ATOM   3702 C CZ    . PHE A 1 489 ? 17.878  -75.416 4.162   1.00 46.78  ? 487 PHE A CZ    1 
ATOM   3703 N N     . VAL A 1 490 ? 13.441  -80.085 1.026   1.00 53.35  ? 488 VAL A N     1 
ATOM   3704 C CA    . VAL A 1 490 ? 12.553  -80.633 -0.034  1.00 51.77  ? 488 VAL A CA    1 
ATOM   3705 C C     . VAL A 1 490 ? 11.441  -81.430 0.645   1.00 51.08  ? 488 VAL A C     1 
ATOM   3706 O O     . VAL A 1 490 ? 10.281  -81.268 0.265   1.00 58.88  ? 488 VAL A O     1 
ATOM   3707 C CB    . VAL A 1 490 ? 13.339  -81.452 -1.069  1.00 52.71  ? 488 VAL A CB    1 
ATOM   3708 C CG1   . VAL A 1 490 ? 12.422  -82.331 -1.922  1.00 51.30  ? 488 VAL A CG1   1 
ATOM   3709 C CG2   . VAL A 1 490 ? 14.174  -80.527 -1.939  1.00 50.77  ? 488 VAL A CG2   1 
ATOM   3710 N N     . ALA A 1 491 ? 11.790  -82.222 1.650   1.00 48.71  ? 489 ALA A N     1 
ATOM   3711 C CA    . ALA A 1 491 ? 10.862  -83.160 2.313   1.00 47.47  ? 489 ALA A CA    1 
ATOM   3712 C C     . ALA A 1 491 ? 9.680   -82.389 2.900   1.00 45.84  ? 489 ALA A C     1 
ATOM   3713 O O     . ALA A 1 491 ? 8.544   -82.677 2.538   1.00 46.02  ? 489 ALA A O     1 
ATOM   3714 C CB    . ALA A 1 491 ? 11.605  -83.983 3.342   1.00 42.12  ? 489 ALA A CB    1 
ATOM   3715 N N     . PRO A 1 492 ? 9.887   -81.436 3.843   1.00 49.31  ? 490 PRO A N     1 
ATOM   3716 C CA    . PRO A 1 492 ? 8.787   -80.624 4.385   1.00 44.27  ? 490 PRO A CA    1 
ATOM   3717 C C     . PRO A 1 492 ? 8.064   -79.788 3.329   1.00 44.18  ? 490 PRO A C     1 
ATOM   3718 O O     . PRO A 1 492 ? 6.867   -79.609 3.453   1.00 45.08  ? 490 PRO A O     1 
ATOM   3719 C CB    . PRO A 1 492 ? 9.416   -79.674 5.416   1.00 45.27  ? 490 PRO A CB    1 
ATOM   3720 C CG    . PRO A 1 492 ? 10.931  -79.847 5.262   1.00 50.10  ? 490 PRO A CG    1 
ATOM   3721 C CD    . PRO A 1 492 ? 11.157  -81.171 4.545   1.00 49.32  ? 490 PRO A CD    1 
ATOM   3722 N N     . LEU A 1 493 ? 8.777   -79.313 2.304   1.00 43.97  ? 491 LEU A N     1 
ATOM   3723 C CA    . LEU A 1 493 ? 8.156   -78.496 1.231   1.00 38.66  ? 491 LEU A CA    1 
ATOM   3724 C C     . LEU A 1 493 ? 7.115   -79.346 0.502   1.00 38.43  ? 491 LEU A C     1 
ATOM   3725 O O     . LEU A 1 493 ? 6.013   -78.827 0.259   1.00 41.64  ? 491 LEU A O     1 
ATOM   3726 C CB    . LEU A 1 493 ? 9.207   -77.956 0.259   1.00 38.85  ? 491 LEU A CB    1 
ATOM   3727 C CG    . LEU A 1 493 ? 8.633   -77.045 -0.816  1.00 40.93  ? 491 LEU A CG    1 
ATOM   3728 C CD1   . LEU A 1 493 ? 7.854   -75.883 -0.169  1.00 44.19  ? 491 LEU A CD1   1 
ATOM   3729 C CD2   . LEU A 1 493 ? 9.713   -76.536 -1.752  1.00 37.87  ? 491 LEU A CD2   1 
ATOM   3730 N N     . ALA A 1 494 ? 7.454   -80.592 0.158   1.00 40.84  ? 492 ALA A N     1 
ATOM   3731 C CA    . ALA A 1 494 ? 6.581   -81.525 -0.604  1.00 40.52  ? 492 ALA A CA    1 
ATOM   3732 C C     . ALA A 1 494 ? 5.396   -81.918 0.290   1.00 35.96  ? 492 ALA A C     1 
ATOM   3733 O O     . ALA A 1 494 ? 4.261   -81.921 -0.219  1.00 36.79  ? 492 ALA A O     1 
ATOM   3734 C CB    . ALA A 1 494 ? 7.362   -82.729 -1.108  1.00 37.47  ? 492 ALA A CB    1 
ATOM   3735 N N     . GLN A 1 495 ? 5.629   -82.180 1.581   1.00 39.42  ? 493 GLN A N     1 
ATOM   3736 C CA    . GLN A 1 495 ? 4.532   -82.450 2.564   1.00 44.57  ? 493 GLN A CA    1 
ATOM   3737 C C     . GLN A 1 495 ? 3.580   -81.248 2.592   1.00 42.51  ? 493 GLN A C     1 
ATOM   3738 O O     . GLN A 1 495 ? 2.368   -81.454 2.554   1.00 43.84  ? 493 GLN A O     1 
ATOM   3739 C CB    . GLN A 1 495 ? 5.066   -82.746 3.968   1.00 49.62  ? 493 GLN A CB    1 
ATOM   3740 C CG    . GLN A 1 495 ? 3.991   -83.236 4.938   1.00 59.97  ? 493 GLN A CG    1 
ATOM   3741 C CD    . GLN A 1 495 ? 4.455   -83.356 6.378   1.00 61.87  ? 493 GLN A CD    1 
ATOM   3742 O OE1   . GLN A 1 495 ? 5.193   -82.530 6.900   1.00 64.99  ? 493 GLN A OE1   1 
ATOM   3743 N NE2   . GLN A 1 495 ? 3.997   -84.386 7.064   1.00 64.83  ? 493 GLN A NE2   1 
ATOM   3744 N N     . LEU A 1 496 ? 4.124   -80.030 2.621   1.00 43.38  ? 494 LEU A N     1 
ATOM   3745 C CA    . LEU A 1 496 ? 3.331   -78.783 2.766   1.00 40.78  ? 494 LEU A CA    1 
ATOM   3746 C C     . LEU A 1 496 ? 2.626   -78.510 1.448   1.00 38.35  ? 494 LEU A C     1 
ATOM   3747 O O     . LEU A 1 496 ? 1.486   -78.015 1.476   1.00 37.97  ? 494 LEU A O     1 
ATOM   3748 C CB    . LEU A 1 496 ? 4.253   -77.618 3.147   1.00 39.75  ? 494 LEU A CB    1 
ATOM   3749 C CG    . LEU A 1 496 ? 3.555   -76.291 3.438   1.00 37.95  ? 494 LEU A CG    1 
ATOM   3750 C CD1   . LEU A 1 496 ? 2.818   -76.366 4.767   1.00 36.30  ? 494 LEU A CD1   1 
ATOM   3751 C CD2   . LEU A 1 496 ? 4.543   -75.124 3.399   1.00 38.44  ? 494 LEU A CD2   1 
ATOM   3752 N N     . ASN A 1 497 ? 3.302   -78.757 0.326   1.00 39.99  ? 495 ASN A N     1 
ATOM   3753 C CA    . ASN A 1 497 ? 2.704   -78.436 -0.995  1.00 39.76  ? 495 ASN A CA    1 
ATOM   3754 C C     . ASN A 1 497 ? 1.443   -79.293 -1.170  1.00 40.50  ? 495 ASN A C     1 
ATOM   3755 O O     . ASN A 1 497 ? 0.427   -78.770 -1.574  1.00 40.02  ? 495 ASN A O     1 
ATOM   3756 C CB    . ASN A 1 497 ? 3.685   -78.659 -2.129  1.00 38.48  ? 495 ASN A CB    1 
ATOM   3757 C CG    . ASN A 1 497 ? 3.249   -77.963 -3.394  1.00 40.55  ? 495 ASN A CG    1 
ATOM   3758 O OD1   . ASN A 1 497 ? 2.906   -76.784 -3.368  1.00 41.99  ? 495 ASN A OD1   1 
ATOM   3759 N ND2   . ASN A 1 497 ? 3.328   -78.659 -4.516  1.00 38.83  ? 495 ASN A ND2   1 
ATOM   3760 N N     . LYS A 1 498 ? 1.511   -80.563 -0.783  1.00 40.28  ? 496 LYS A N     1 
ATOM   3761 C CA    . LYS A 1 498 ? 0.364   -81.498 -0.819  1.00 40.79  ? 496 LYS A CA    1 
ATOM   3762 C C     . LYS A 1 498 ? -0.751  -80.994 0.116   1.00 36.87  ? 496 LYS A C     1 
ATOM   3763 O O     . LYS A 1 498 ? -1.912  -80.887 -0.345  1.00 34.16  ? 496 LYS A O     1 
ATOM   3764 C CB    . LYS A 1 498 ? 0.889   -82.893 -0.482  1.00 46.04  ? 496 LYS A CB    1 
ATOM   3765 C CG    . LYS A 1 498 ? -0.003  -84.043 -0.926  1.00 58.47  ? 496 LYS A CG    1 
ATOM   3766 C CD    . LYS A 1 498 ? 0.101   -85.274 -0.039  1.00 63.41  ? 496 LYS A CD    1 
ATOM   3767 C CE    . LYS A 1 498 ? -0.287  -84.957 1.390   1.00 70.68  ? 496 LYS A CE    1 
ATOM   3768 N NZ    . LYS A 1 498 ? -1.206  -85.987 1.921   1.00 76.25  ? 496 LYS A NZ    1 
ATOM   3769 N N     . GLU A 1 499 ? -0.419  -80.674 1.369   1.00 35.33  ? 497 GLU A N     1 
ATOM   3770 C CA    . GLU A 1 499 ? -1.382  -80.180 2.396   1.00 37.48  ? 497 GLU A CA    1 
ATOM   3771 C C     . GLU A 1 499 ? -2.126  -78.936 1.892   1.00 37.03  ? 497 GLU A C     1 
ATOM   3772 O O     . GLU A 1 499 ? -3.320  -78.801 2.186   1.00 44.68  ? 497 GLU A O     1 
ATOM   3773 C CB    . GLU A 1 499 ? -0.654  -79.836 3.690   1.00 38.20  ? 497 GLU A CB    1 
ATOM   3774 C CG    . GLU A 1 499 ? -1.575  -79.537 4.854   1.00 37.22  ? 497 GLU A CG    1 
ATOM   3775 C CD    . GLU A 1 499 ? -0.833  -78.998 6.057   1.00 39.80  ? 497 GLU A CD    1 
ATOM   3776 O OE1   . GLU A 1 499 ? -1.248  -79.316 7.187   1.00 40.92  ? 497 GLU A OE1   1 
ATOM   3777 O OE2   . GLU A 1 499 ? 0.134   -78.218 5.862   1.00 43.92  ? 497 GLU A OE2   1 
ATOM   3778 N N     . TRP A 1 500 ? -1.426  -78.050 1.191   1.00 37.71  ? 498 TRP A N     1 
ATOM   3779 C CA    . TRP A 1 500 ? -1.970  -76.789 0.645   1.00 36.97  ? 498 TRP A CA    1 
ATOM   3780 C C     . TRP A 1 500 ? -3.153  -77.154 -0.255  1.00 39.58  ? 498 TRP A C     1 
ATOM   3781 O O     . TRP A 1 500 ? -4.225  -76.515 -0.138  1.00 41.60  ? 498 TRP A O     1 
ATOM   3782 C CB    . TRP A 1 500 ? -0.848  -76.056 -0.101  1.00 38.66  ? 498 TRP A CB    1 
ATOM   3783 C CG    . TRP A 1 500 ? -1.041  -74.597 -0.374  1.00 35.28  ? 498 TRP A CG    1 
ATOM   3784 C CD1   . TRP A 1 500 ? -2.142  -73.827 -0.146  1.00 35.36  ? 498 TRP A CD1   1 
ATOM   3785 C CD2   . TRP A 1 500 ? -0.071  -73.741 -0.996  1.00 37.21  ? 498 TRP A CD2   1 
ATOM   3786 N NE1   . TRP A 1 500 ? -1.918  -72.543 -0.559  1.00 34.64  ? 498 TRP A NE1   1 
ATOM   3787 C CE2   . TRP A 1 500 ? -0.652  -72.457 -1.084  1.00 37.14  ? 498 TRP A CE2   1 
ATOM   3788 C CE3   . TRP A 1 500 ? 1.234   -73.931 -1.478  1.00 36.62  ? 498 TRP A CE3   1 
ATOM   3789 C CZ2   . TRP A 1 500 ? 0.052   -71.365 -1.597  1.00 34.55  ? 498 TRP A CZ2   1 
ATOM   3790 C CZ3   . TRP A 1 500 ? 1.922   -72.854 -1.996  1.00 37.04  ? 498 TRP A CZ3   1 
ATOM   3791 C CH2   . TRP A 1 500 ? 1.326   -71.592 -2.066  1.00 35.91  ? 498 TRP A CH2   1 
ATOM   3792 N N     . GLY A 1 501 ? -2.969  -78.156 -1.124  1.00 39.41  ? 499 GLY A N     1 
ATOM   3793 C CA    . GLY A 1 501 ? -4.020  -78.612 -2.053  1.00 39.74  ? 499 GLY A CA    1 
ATOM   3794 C C     . GLY A 1 501 ? -5.173  -79.254 -1.295  1.00 40.80  ? 499 GLY A C     1 
ATOM   3795 O O     . GLY A 1 501 ? -6.349  -78.960 -1.624  1.00 40.37  ? 499 GLY A O     1 
ATOM   3796 N N     . ASP A 1 502 ? -4.863  -80.074 -0.284  1.00 40.86  ? 500 ASP A N     1 
ATOM   3797 C CA    . ASP A 1 502 ? -5.886  -80.756 0.558   1.00 43.09  ? 500 ASP A CA    1 
ATOM   3798 C C     . ASP A 1 502 ? -6.715  -79.699 1.285   1.00 42.34  ? 500 ASP A C     1 
ATOM   3799 O O     . ASP A 1 502 ? -7.945  -79.779 1.184   1.00 40.03  ? 500 ASP A O     1 
ATOM   3800 C CB    . ASP A 1 502 ? -5.264  -81.777 1.512   1.00 46.10  ? 500 ASP A CB    1 
ATOM   3801 C CG    . ASP A 1 502 ? -4.529  -82.904 0.787   1.00 54.34  ? 500 ASP A CG    1 
ATOM   3802 O OD1   . ASP A 1 502 ? -4.817  -83.118 -0.441  1.00 53.40  ? 500 ASP A OD1   1 
ATOM   3803 O OD2   . ASP A 1 502 ? -3.651  -83.542 1.432   1.00 51.22  ? 500 ASP A OD2   1 
ATOM   3804 N N     . LEU A 1 503 ? -6.061  -78.746 1.957   1.00 40.42  ? 501 LEU A N     1 
ATOM   3805 C CA    . LEU A 1 503 ? -6.735  -77.665 2.725   1.00 43.16  ? 501 LEU A CA    1 
ATOM   3806 C C     . LEU A 1 503 ? -7.699  -76.905 1.811   1.00 39.43  ? 501 LEU A C     1 
ATOM   3807 O O     . LEU A 1 503 ? -8.818  -76.603 2.239   1.00 36.17  ? 501 LEU A O     1 
ATOM   3808 C CB    . LEU A 1 503 ? -5.687  -76.697 3.267   1.00 43.87  ? 501 LEU A CB    1 
ATOM   3809 C CG    . LEU A 1 503 ? -5.085  -77.068 4.608   1.00 48.12  ? 501 LEU A CG    1 
ATOM   3810 C CD1   . LEU A 1 503 ? -4.021  -76.051 4.994   1.00 51.16  ? 501 LEU A CD1   1 
ATOM   3811 C CD2   . LEU A 1 503 ? -6.162  -77.145 5.683   1.00 53.91  ? 501 LEU A CD2   1 
ATOM   3812 N N     . THR A 1 504 ? -7.266  -76.554 0.607   1.00 39.37  ? 502 THR A N     1 
ATOM   3813 C CA    . THR A 1 504 ? -8.118  -75.822 -0.367  1.00 43.38  ? 502 THR A CA    1 
ATOM   3814 C C     . THR A 1 504 ? -9.453  -76.587 -0.505  1.00 46.42  ? 502 THR A C     1 
ATOM   3815 O O     . THR A 1 504 ? -10.528 -75.979 -0.298  1.00 44.27  ? 502 THR A O     1 
ATOM   3816 C CB    . THR A 1 504 ? -7.316  -75.601 -1.660  1.00 47.47  ? 502 THR A CB    1 
ATOM   3817 O OG1   . THR A 1 504 ? -6.115  -74.883 -1.340  1.00 42.50  ? 502 THR A OG1   1 
ATOM   3818 C CG2   . THR A 1 504 ? -8.099  -74.878 -2.735  1.00 49.71  ? 502 THR A CG2   1 
ATOM   3819 N N     . MET A 1 505 ? -9.392  -77.900 -0.761  1.00 47.88  ? 503 MET A N     1 
ATOM   3820 C CA    . MET A 1 505 ? -10.574 -78.769 -1.034  1.00 43.77  ? 503 MET A CA    1 
ATOM   3821 C C     . MET A 1 505 ? -11.479 -78.834 0.202   1.00 40.58  ? 503 MET A C     1 
ATOM   3822 O O     . MET A 1 505 ? -12.697 -78.667 0.055   1.00 44.51  ? 503 MET A O     1 
ATOM   3823 C CB    . MET A 1 505 ? -10.118 -80.181 -1.407  1.00 49.26  ? 503 MET A CB    1 
ATOM   3824 C CG    . MET A 1 505 ? -9.278  -80.248 -2.681  1.00 51.17  ? 503 MET A CG    1 
ATOM   3825 S SD    . MET A 1 505 ? -10.255 -79.794 -4.130  1.00 54.40  ? 503 MET A SD    1 
ATOM   3826 C CE    . MET A 1 505 ? -9.462  -78.262 -4.608  1.00 57.70  ? 503 MET A CE    1 
ATOM   3827 N N     . LYS A 1 506 ? -10.906 -79.109 1.374   1.00 40.20  ? 504 LYS A N     1 
ATOM   3828 C CA    . LYS A 1 506 ? -11.633 -79.132 2.671   1.00 41.32  ? 504 LYS A CA    1 
ATOM   3829 C C     . LYS A 1 506 ? -12.326 -77.787 2.926   1.00 41.66  ? 504 LYS A C     1 
ATOM   3830 O O     . LYS A 1 506 ? -13.487 -77.796 3.314   1.00 41.70  ? 504 LYS A O     1 
ATOM   3831 C CB    . LYS A 1 506 ? -10.693 -79.436 3.837   1.00 43.57  ? 504 LYS A CB    1 
ATOM   3832 C CG    . LYS A 1 506 ? -10.439 -80.904 4.080   1.00 42.15  ? 504 LYS A CG    1 
ATOM   3833 C CD    . LYS A 1 506 ? -9.121  -81.162 4.694   1.00 42.95  ? 504 LYS A CD    1 
ATOM   3834 C CE    . LYS A 1 506 ? -9.087  -82.501 5.380   1.00 51.46  ? 504 LYS A CE    1 
ATOM   3835 N NZ    . LYS A 1 506 ? -7.706  -82.820 5.798   1.00 56.91  ? 504 LYS A NZ    1 
ATOM   3836 N N     . VAL A 1 507 ? -11.647 -76.657 2.730   1.00 41.71  ? 505 VAL A N     1 
ATOM   3837 C CA    . VAL A 1 507 ? -12.308 -75.340 2.932   1.00 38.46  ? 505 VAL A CA    1 
ATOM   3838 C C     . VAL A 1 507 ? -13.478 -75.304 1.956   1.00 35.57  ? 505 VAL A C     1 
ATOM   3839 O O     . VAL A 1 507 ? -14.566 -74.927 2.387   1.00 35.01  ? 505 VAL A O     1 
ATOM   3840 C CB    . VAL A 1 507 ? -11.360 -74.139 2.746   1.00 37.94  ? 505 VAL A CB    1 
ATOM   3841 C CG1   . VAL A 1 507 ? -12.112 -72.821 2.850   1.00 39.26  ? 505 VAL A CG1   1 
ATOM   3842 C CG2   . VAL A 1 507 ? -10.227 -74.160 3.743   1.00 37.28  ? 505 VAL A CG2   1 
ATOM   3843 N N     . GLY A 1 508 ? -13.255 -75.714 0.706   1.00 34.31  ? 506 GLY A N     1 
ATOM   3844 C CA    . GLY A 1 508 ? -14.326 -75.776 -0.311  1.00 39.70  ? 506 GLY A CA    1 
ATOM   3845 C C     . GLY A 1 508 ? -15.540 -76.589 0.151   1.00 39.43  ? 506 GLY A C     1 
ATOM   3846 O O     . GLY A 1 508 ? -16.660 -76.089 0.017   1.00 40.38  ? 506 GLY A O     1 
ATOM   3847 N N     . MET A 1 509 ? -15.318 -77.788 0.700   1.00 40.65  ? 507 MET A N     1 
ATOM   3848 C CA    . MET A 1 509 ? -16.347 -78.737 1.222   1.00 43.39  ? 507 MET A CA    1 
ATOM   3849 C C     . MET A 1 509 ? -17.148 -78.067 2.361   1.00 40.84  ? 507 MET A C     1 
ATOM   3850 O O     . MET A 1 509 ? -18.425 -78.166 2.411   1.00 34.21  ? 507 MET A O     1 
ATOM   3851 C CB    . MET A 1 509 ? -15.615 -79.991 1.724   1.00 45.44  ? 507 MET A CB    1 
ATOM   3852 C CG    . MET A 1 509 ? -16.497 -81.018 2.397   1.00 52.81  ? 507 MET A CG    1 
ATOM   3853 S SD    . MET A 1 509 ? -17.124 -82.317 1.287   1.00 58.83  ? 507 MET A SD    1 
ATOM   3854 C CE    . MET A 1 509 ? -15.607 -83.170 0.879   1.00 52.78  ? 507 MET A CE    1 
ATOM   3855 N N     . ALA A 1 510 ? -16.415 -77.375 3.229   1.00 34.59  ? 508 ALA A N     1 
ATOM   3856 C CA    . ALA A 1 510 ? -16.935 -76.638 4.397   1.00 34.88  ? 508 ALA A CA    1 
ATOM   3857 C C     . ALA A 1 510 ? -17.825 -75.499 3.918   1.00 34.16  ? 508 ALA A C     1 
ATOM   3858 O O     . ALA A 1 510 ? -18.904 -75.334 4.519   1.00 37.89  ? 508 ALA A O     1 
ATOM   3859 C CB    . ALA A 1 510 ? -15.798 -76.130 5.247   1.00 35.73  ? 508 ALA A CB    1 
ATOM   3860 N N     . ALA A 1 511 ? -17.429 -74.788 2.854   1.00 36.42  ? 509 ALA A N     1 
ATOM   3861 C CA    . ALA A 1 511 ? -18.194 -73.643 2.296   1.00 37.35  ? 509 ALA A CA    1 
ATOM   3862 C C     . ALA A 1 511 ? -19.480 -74.158 1.629   1.00 35.93  ? 509 ALA A C     1 
ATOM   3863 O O     . ALA A 1 511 ? -20.461 -73.437 1.586   1.00 35.68  ? 509 ALA A O     1 
ATOM   3864 C CB    . ALA A 1 511 ? -17.334 -72.813 1.353   1.00 39.79  ? 509 ALA A CB    1 
ATOM   3865 N N     . MET A 1 512 ? -19.478 -75.385 1.118   1.00 42.95  ? 510 MET A N     1 
ATOM   3866 C CA    . MET A 1 512 ? -20.669 -76.022 0.484   1.00 43.33  ? 510 MET A CA    1 
ATOM   3867 C C     . MET A 1 512 ? -21.790 -76.084 1.523   1.00 41.36  ? 510 MET A C     1 
ATOM   3868 O O     . MET A 1 512 ? -22.934 -75.779 1.180   1.00 39.91  ? 510 MET A O     1 
ATOM   3869 C CB    . MET A 1 512 ? -20.301 -77.434 0.001   1.00 48.10  ? 510 MET A CB    1 
ATOM   3870 C CG    . MET A 1 512 ? -21.413 -78.195 -0.696  1.00 48.65  ? 510 MET A CG    1 
ATOM   3871 S SD    . MET A 1 512 ? -22.040 -79.491 0.363   1.00 52.30  ? 510 MET A SD    1 
ATOM   3872 C CE    . MET A 1 512 ? -20.584 -80.496 0.626   1.00 60.08  ? 510 MET A CE    1 
ATOM   3873 N N     . LYS A 1 513 ? -21.434 -76.431 2.761   1.00 42.11  ? 511 LYS A N     1 
ATOM   3874 C CA    . LYS A 1 513 ? -22.359 -76.655 3.897   1.00 42.57  ? 511 LYS A CA    1 
ATOM   3875 C C     . LYS A 1 513 ? -22.714 -75.318 4.548   1.00 40.84  ? 511 LYS A C     1 
ATOM   3876 O O     . LYS A 1 513 ? -23.859 -75.167 5.025   1.00 38.92  ? 511 LYS A O     1 
ATOM   3877 C CB    . LYS A 1 513 ? -21.676 -77.592 4.892   1.00 48.16  ? 511 LYS A CB    1 
ATOM   3878 C CG    . LYS A 1 513 ? -22.482 -77.858 6.141   1.00 54.76  ? 511 LYS A CG    1 
ATOM   3879 C CD    . LYS A 1 513 ? -22.159 -79.175 6.807   1.00 60.14  ? 511 LYS A CD    1 
ATOM   3880 C CE    . LYS A 1 513 ? -23.200 -79.500 7.854   1.00 59.40  ? 511 LYS A CE    1 
ATOM   3881 N NZ    . LYS A 1 513 ? -23.120 -80.905 8.283   1.00 63.13  ? 511 LYS A NZ    1 
ATOM   3882 N N     . ASP A 1 514 ? -21.758 -74.389 4.591   1.00 38.42  ? 512 ASP A N     1 
ATOM   3883 C CA    . ASP A 1 514 ? -21.896 -73.104 5.330   1.00 37.89  ? 512 ASP A CA    1 
ATOM   3884 C C     . ASP A 1 514 ? -21.010 -72.015 4.687   1.00 38.04  ? 512 ASP A C     1 
ATOM   3885 O O     . ASP A 1 514 ? -19.756 -72.077 4.828   1.00 33.65  ? 512 ASP A O     1 
ATOM   3886 C CB    . ASP A 1 514 ? -21.599 -73.324 6.817   1.00 32.66  ? 512 ASP A CB    1 
ATOM   3887 C CG    . ASP A 1 514 ? -21.740 -72.039 7.598   1.00 34.28  ? 512 ASP A CG    1 
ATOM   3888 O OD1   . ASP A 1 514 ? -22.227 -71.023 7.015   1.00 34.88  ? 512 ASP A OD1   1 
ATOM   3889 O OD2   . ASP A 1 514 ? -21.354 -72.048 8.769   1.00 43.13  ? 512 ASP A OD2   1 
ATOM   3890 N N     . ARG A 1 515 ? -21.628 -71.023 4.040   1.00 39.90  ? 513 ARG A N     1 
ATOM   3891 C CA    . ARG A 1 515 ? -20.896 -69.970 3.263   1.00 42.62  ? 513 ARG A CA    1 
ATOM   3892 C C     . ARG A 1 515 ? -20.102 -69.046 4.210   1.00 35.23  ? 513 ARG A C     1 
ATOM   3893 O O     . ARG A 1 515 ? -19.201 -68.367 3.711   1.00 33.49  ? 513 ARG A O     1 
ATOM   3894 C CB    . ARG A 1 515 ? -21.834 -69.134 2.378   1.00 41.46  ? 513 ARG A CB    1 
ATOM   3895 C CG    . ARG A 1 515 ? -22.358 -69.846 1.137   1.00 45.02  ? 513 ARG A CG    1 
ATOM   3896 C CD    . ARG A 1 515 ? -23.711 -69.267 0.713   1.00 52.46  ? 513 ARG A CD    1 
ATOM   3897 N NE    . ARG A 1 515 ? -24.762 -69.389 1.736   1.00 58.71  ? 513 ARG A NE    1 
ATOM   3898 C CZ    . ARG A 1 515 ? -25.929 -68.728 1.760   1.00 56.66  ? 513 ARG A CZ    1 
ATOM   3899 N NH1   . ARG A 1 515 ? -26.232 -67.856 0.812   1.00 61.28  ? 513 ARG A NH1   1 
ATOM   3900 N NH2   . ARG A 1 515 ? -26.781 -68.922 2.758   1.00 53.12  ? 513 ARG A NH2   1 
ATOM   3901 N N     . GLU A 1 516 ? -20.427 -69.003 5.506   1.00 31.82  ? 514 GLU A N     1 
ATOM   3902 C CA    . GLU A 1 516 ? -19.626 -68.252 6.506   1.00 32.66  ? 514 GLU A CA    1 
ATOM   3903 C C     . GLU A 1 516 ? -18.192 -68.823 6.481   1.00 31.80  ? 514 GLU A C     1 
ATOM   3904 O O     . GLU A 1 516 ? -17.267 -68.081 6.808   1.00 33.37  ? 514 GLU A O     1 
ATOM   3905 C CB    . GLU A 1 516 ? -20.234 -68.310 7.925   1.00 35.20  ? 514 GLU A CB    1 
ATOM   3906 C CG    . GLU A 1 516 ? -21.636 -67.735 8.103   1.00 32.68  ? 514 GLU A CG    1 
ATOM   3907 C CD    . GLU A 1 516 ? -21.785 -66.232 7.886   1.00 34.64  ? 514 GLU A CD    1 
ATOM   3908 O OE1   . GLU A 1 516 ? -20.812 -65.563 7.467   1.00 36.86  ? 514 GLU A OE1   1 
ATOM   3909 O OE2   . GLU A 1 516 ? -22.896 -65.732 8.089   1.00 34.09  ? 514 GLU A OE2   1 
ATOM   3910 N N     . GLU A 1 517 ? -18.000 -70.089 6.106   1.00 29.30  ? 515 GLU A N     1 
ATOM   3911 C CA    . GLU A 1 517 ? -16.670 -70.760 6.172   1.00 33.52  ? 515 GLU A CA    1 
ATOM   3912 C C     . GLU A 1 517 ? -15.658 -70.001 5.298   1.00 34.53  ? 515 GLU A C     1 
ATOM   3913 O O     . GLU A 1 517 ? -14.449 -70.061 5.562   1.00 31.74  ? 515 GLU A O     1 
ATOM   3914 C CB    . GLU A 1 517 ? -16.735 -72.230 5.721   1.00 36.33  ? 515 GLU A CB    1 
ATOM   3915 C CG    . GLU A 1 517 ? -17.449 -73.183 6.682   1.00 37.67  ? 515 GLU A CG    1 
ATOM   3916 C CD    . GLU A 1 517 ? -16.761 -73.507 7.996   1.00 37.16  ? 515 GLU A CD    1 
ATOM   3917 O OE1   . GLU A 1 517 ? -17.383 -74.189 8.827   1.00 46.59  ? 515 GLU A OE1   1 
ATOM   3918 O OE2   . GLU A 1 517 ? -15.611 -73.085 8.199   1.00 40.09  ? 515 GLU A OE2   1 
ATOM   3919 N N     . VAL A 1 518 ? -16.116 -69.330 4.252   1.00 34.94  ? 516 VAL A N     1 
ATOM   3920 C CA    . VAL A 1 518 ? -15.177 -68.601 3.361   1.00 35.75  ? 516 VAL A CA    1 
ATOM   3921 C C     . VAL A 1 518 ? -14.535 -67.458 4.160   1.00 35.63  ? 516 VAL A C     1 
ATOM   3922 O O     . VAL A 1 518 ? -13.313 -67.329 4.132   1.00 38.52  ? 516 VAL A O     1 
ATOM   3923 C CB    . VAL A 1 518 ? -15.912 -68.098 2.114   1.00 33.28  ? 516 VAL A CB    1 
ATOM   3924 C CG1   . VAL A 1 518 ? -14.980 -67.301 1.208   1.00 32.78  ? 516 VAL A CG1   1 
ATOM   3925 C CG2   . VAL A 1 518 ? -16.554 -69.259 1.369   1.00 31.38  ? 516 VAL A CG2   1 
ATOM   3926 N N     . GLY A 1 519 ? -15.319 -66.652 4.863   1.00 31.35  ? 517 GLY A N     1 
ATOM   3927 C CA    . GLY A 1 519 ? -14.745 -65.587 5.701   1.00 36.13  ? 517 GLY A CA    1 
ATOM   3928 C C     . GLY A 1 519 ? -14.008 -66.133 6.905   1.00 30.59  ? 517 GLY A C     1 
ATOM   3929 O O     . GLY A 1 519 ? -12.968 -65.577 7.241   1.00 30.56  ? 517 GLY A O     1 
ATOM   3930 N N     . ALA A 1 520 ? -14.534 -67.196 7.505   1.00 29.39  ? 518 ALA A N     1 
ATOM   3931 C CA    . ALA A 1 520 ? -13.921 -67.818 8.708   1.00 32.10  ? 518 ALA A CA    1 
ATOM   3932 C C     . ALA A 1 520 ? -12.492 -68.350 8.430   1.00 32.75  ? 518 ALA A C     1 
ATOM   3933 O O     . ALA A 1 520 ? -11.615 -68.234 9.318   1.00 36.59  ? 518 ALA A O     1 
ATOM   3934 C CB    . ALA A 1 520 ? -14.848 -68.896 9.216   1.00 30.57  ? 518 ALA A CB    1 
ATOM   3935 N N     . ALA A 1 521 ? -12.242 -68.917 7.249   1.00 33.91  ? 519 ALA A N     1 
ATOM   3936 C CA    . ALA A 1 521 ? -10.944 -69.531 6.887   1.00 34.66  ? 519 ALA A CA    1 
ATOM   3937 C C     . ALA A 1 521 ? -10.026 -68.520 6.172   1.00 33.77  ? 519 ALA A C     1 
ATOM   3938 O O     . ALA A 1 521 ? -8.804  -68.747 6.143   1.00 35.06  ? 519 ALA A O     1 
ATOM   3939 C CB    . ALA A 1 521 ? -11.197 -70.765 6.057   1.00 32.51  ? 519 ALA A CB    1 
ATOM   3940 N N     . SER A 1 522 ? -10.578 -67.423 5.654   1.00 32.43  ? 520 SER A N     1 
ATOM   3941 C CA    . SER A 1 522 ? -9.906  -66.512 4.690   1.00 30.21  ? 520 SER A CA    1 
ATOM   3942 C C     . SER A 1 522 ? -8.504  -66.079 5.178   1.00 29.66  ? 520 SER A C     1 
ATOM   3943 O O     . SER A 1 522 ? -7.528  -66.372 4.489   1.00 29.82  ? 520 SER A O     1 
ATOM   3944 C CB    . SER A 1 522 ? -10.802 -65.333 4.379   1.00 29.77  ? 520 SER A CB    1 
ATOM   3945 O OG    . SER A 1 522 ? -11.113 -64.570 5.532   1.00 28.31  ? 520 SER A OG    1 
ATOM   3946 N N     . VAL A 1 523 ? -8.371  -65.398 6.314   1.00 29.72  ? 521 VAL A N     1 
ATOM   3947 C CA    . VAL A 1 523 ? -7.084  -64.734 6.684   1.00 29.93  ? 521 VAL A CA    1 
ATOM   3948 C C     . VAL A 1 523 ? -6.055  -65.810 7.047   1.00 33.00  ? 521 VAL A C     1 
ATOM   3949 O O     . VAL A 1 523 ? -4.899  -65.689 6.601   1.00 36.10  ? 521 VAL A O     1 
ATOM   3950 C CB    . VAL A 1 523 ? -7.245  -63.709 7.813   1.00 29.45  ? 521 VAL A CB    1 
ATOM   3951 C CG1   . VAL A 1 523 ? -5.882  -63.215 8.273   1.00 31.59  ? 521 VAL A CG1   1 
ATOM   3952 C CG2   . VAL A 1 523 ? -8.124  -62.535 7.403   1.00 28.12  ? 521 VAL A CG2   1 
ATOM   3953 N N     . ASP A 1 524 ? -6.480  -66.841 7.781   1.00 31.48  ? 522 ASP A N     1 
ATOM   3954 C CA    . ASP A 1 524 ? -5.663  -68.041 8.086   1.00 30.52  ? 522 ASP A CA    1 
ATOM   3955 C C     . ASP A 1 524 ? -5.182  -68.688 6.781   1.00 30.94  ? 522 ASP A C     1 
ATOM   3956 O O     . ASP A 1 524 ? -4.007  -69.056 6.730   1.00 35.22  ? 522 ASP A O     1 
ATOM   3957 C CB    . ASP A 1 524 ? -6.445  -69.036 8.946   1.00 32.36  ? 522 ASP A CB    1 
ATOM   3958 C CG    . ASP A 1 524 ? -6.472  -68.656 10.402  1.00 29.24  ? 522 ASP A CG    1 
ATOM   3959 O OD1   . ASP A 1 524 ? -5.382  -68.537 10.952  1.00 30.51  ? 522 ASP A OD1   1 
ATOM   3960 O OD2   . ASP A 1 524 ? -7.573  -68.433 10.946  1.00 31.57  ? 522 ASP A OD2   1 
ATOM   3961 N N     . TYR A 1 525 ? -6.042  -68.838 5.777   1.00 29.86  ? 523 TYR A N     1 
ATOM   3962 C CA    . TYR A 1 525 ? -5.678  -69.450 4.473   1.00 32.21  ? 523 TYR A CA    1 
ATOM   3963 C C     . TYR A 1 525 ? -4.632  -68.584 3.726   1.00 29.53  ? 523 TYR A C     1 
ATOM   3964 O O     . TYR A 1 525 ? -3.743  -69.118 3.016   1.00 27.39  ? 523 TYR A O     1 
ATOM   3965 C CB    . TYR A 1 525 ? -6.940  -69.679 3.631   1.00 31.99  ? 523 TYR A CB    1 
ATOM   3966 C CG    . TYR A 1 525 ? -6.671  -70.349 2.304   1.00 32.00  ? 523 TYR A CG    1 
ATOM   3967 C CD1   . TYR A 1 525 ? -6.622  -71.732 2.193   1.00 31.65  ? 523 TYR A CD1   1 
ATOM   3968 C CD2   . TYR A 1 525 ? -6.411  -69.605 1.165   1.00 31.01  ? 523 TYR A CD2   1 
ATOM   3969 C CE1   . TYR A 1 525 ? -6.336  -72.347 0.983   1.00 29.68  ? 523 TYR A CE1   1 
ATOM   3970 C CE2   . TYR A 1 525 ? -6.124  -70.208 -0.055  1.00 30.52  ? 523 TYR A CE2   1 
ATOM   3971 C CZ    . TYR A 1 525 ? -6.107  -71.587 -0.147  1.00 29.93  ? 523 TYR A CZ    1 
ATOM   3972 O OH    . TYR A 1 525 ? -5.857  -72.195 -1.340  1.00 29.73  ? 523 TYR A OH    1 
ATOM   3973 N N     . LEU A 1 526 ? -4.777  -67.265 3.783   1.00 28.10  ? 524 LEU A N     1 
ATOM   3974 C CA    . LEU A 1 526 ? -3.841  -66.336 3.096   1.00 28.66  ? 524 LEU A CA    1 
ATOM   3975 C C     . LEU A 1 526 ? -2.504  -66.359 3.833   1.00 26.34  ? 524 LEU A C     1 
ATOM   3976 O O     . LEU A 1 526 ? -1.493  -66.424 3.178   1.00 29.63  ? 524 LEU A O     1 
ATOM   3977 C CB    . LEU A 1 526 ? -4.447  -64.938 3.043   1.00 29.16  ? 524 LEU A CB    1 
ATOM   3978 C CG    . LEU A 1 526 ? -3.616  -63.909 2.295   1.00 31.20  ? 524 LEU A CG    1 
ATOM   3979 C CD1   . LEU A 1 526 ? -4.516  -62.829 1.685   1.00 32.81  ? 524 LEU A CD1   1 
ATOM   3980 C CD2   . LEU A 1 526 ? -2.582  -63.295 3.227   1.00 36.12  ? 524 LEU A CD2   1 
ATOM   3981 N N     . MET A 1 527 ? -2.503  -66.346 5.166   1.00 28.74  ? 525 MET A N     1 
ATOM   3982 C CA    . MET A 1 527 ? -1.247  -66.400 5.951   1.00 29.20  ? 525 MET A CA    1 
ATOM   3983 C C     . MET A 1 527 ? -0.525  -67.742 5.707   1.00 27.65  ? 525 MET A C     1 
ATOM   3984 O O     . MET A 1 527 ? 0.684   -67.697 5.382   1.00 24.17  ? 525 MET A O     1 
ATOM   3985 C CB    . MET A 1 527 ? -1.512  -66.126 7.435   1.00 28.90  ? 525 MET A CB    1 
ATOM   3986 C CG    . MET A 1 527 ? -2.019  -64.715 7.656   1.00 28.01  ? 525 MET A CG    1 
ATOM   3987 S SD    . MET A 1 527 ? -0.839  -63.446 7.151   1.00 31.34  ? 525 MET A SD    1 
ATOM   3988 C CE    . MET A 1 527 ? 0.468   -63.678 8.350   1.00 33.64  ? 525 MET A CE    1 
ATOM   3989 N N     . TYR A 1 528 ? -1.226  -68.875 5.776   1.00 27.16  ? 526 TYR A N     1 
ATOM   3990 C CA    . TYR A 1 528 ? -0.686  -70.207 5.385   1.00 28.67  ? 526 TYR A CA    1 
ATOM   3991 C C     . TYR A 1 528 ? -0.049  -70.106 3.989   1.00 28.73  ? 526 TYR A C     1 
ATOM   3992 O O     . TYR A 1 528 ? 1.141   -70.502 3.823   1.00 27.68  ? 526 TYR A O     1 
ATOM   3993 C CB    . TYR A 1 528 ? -1.772  -71.282 5.439   1.00 28.78  ? 526 TYR A CB    1 
ATOM   3994 C CG    . TYR A 1 528 ? -1.342  -72.664 5.014   1.00 30.15  ? 526 TYR A CG    1 
ATOM   3995 C CD1   . TYR A 1 528 ? -1.214  -72.992 3.675   1.00 31.76  ? 526 TYR A CD1   1 
ATOM   3996 C CD2   . TYR A 1 528 ? -1.042  -73.636 5.947   1.00 31.42  ? 526 TYR A CD2   1 
ATOM   3997 C CE1   . TYR A 1 528 ? -0.837  -74.257 3.278   1.00 32.18  ? 526 TYR A CE1   1 
ATOM   3998 C CE2   . TYR A 1 528 ? -0.625  -74.898 5.569   1.00 32.82  ? 526 TYR A CE2   1 
ATOM   3999 C CZ    . TYR A 1 528 ? -0.557  -75.214 4.228   1.00 32.23  ? 526 TYR A CZ    1 
ATOM   4000 O OH    . TYR A 1 528 ? -0.217  -76.468 3.846   1.00 34.81  ? 526 TYR A OH    1 
ATOM   4001 N N     . SER A 1 529 ? -0.799  -69.568 3.030   1.00 29.24  ? 527 SER A N     1 
ATOM   4002 C CA    . SER A 1 529 ? -0.375  -69.457 1.617   1.00 31.57  ? 527 SER A CA    1 
ATOM   4003 C C     . SER A 1 529 ? 0.906   -68.622 1.566   1.00 34.76  ? 527 SER A C     1 
ATOM   4004 O O     . SER A 1 529 ? 1.840   -69.012 0.822   1.00 36.15  ? 527 SER A O     1 
ATOM   4005 C CB    . SER A 1 529 ? -1.467  -68.898 0.743   1.00 32.93  ? 527 SER A CB    1 
ATOM   4006 O OG    . SER A 1 529 ? -2.661  -69.659 0.866   1.00 33.49  ? 527 SER A OG    1 
ATOM   4007 N N     . GLY A 1 530 ? 0.976   -67.545 2.357   1.00 33.07  ? 528 GLY A N     1 
ATOM   4008 C CA    . GLY A 1 530 ? 2.178   -66.697 2.426   1.00 33.31  ? 528 GLY A CA    1 
ATOM   4009 C C     . GLY A 1 530 ? 3.385   -67.507 2.872   1.00 33.96  ? 528 GLY A C     1 
ATOM   4010 O O     . GLY A 1 530 ? 4.422   -67.492 2.166   1.00 30.78  ? 528 GLY A O     1 
ATOM   4011 N N     . TYR A 1 531 ? 3.265   -68.192 4.010   1.00 32.78  ? 529 TYR A N     1 
ATOM   4012 C CA    . TYR A 1 531 ? 4.340   -69.038 4.580   1.00 34.41  ? 529 TYR A CA    1 
ATOM   4013 C C     . TYR A 1 531 ? 4.787   -70.107 3.568   1.00 38.06  ? 529 TYR A C     1 
ATOM   4014 O O     . TYR A 1 531 ? 6.008   -70.372 3.520   1.00 37.88  ? 529 TYR A O     1 
ATOM   4015 C CB    . TYR A 1 531 ? 3.875   -69.649 5.898   1.00 34.03  ? 529 TYR A CB    1 
ATOM   4016 C CG    . TYR A 1 531 ? 3.777   -68.631 7.005   1.00 33.24  ? 529 TYR A CG    1 
ATOM   4017 C CD1   . TYR A 1 531 ? 4.898   -67.946 7.451   1.00 30.48  ? 529 TYR A CD1   1 
ATOM   4018 C CD2   . TYR A 1 531 ? 2.556   -68.306 7.562   1.00 31.50  ? 529 TYR A CD2   1 
ATOM   4019 C CE1   . TYR A 1 531 ? 4.815   -67.013 8.464   1.00 27.99  ? 529 TYR A CE1   1 
ATOM   4020 C CE2   . TYR A 1 531 ? 2.456   -67.360 8.565   1.00 31.76  ? 529 TYR A CE2   1 
ATOM   4021 C CZ    . TYR A 1 531 ? 3.593   -66.732 9.024   1.00 29.47  ? 529 TYR A CZ    1 
ATOM   4022 O OH    . TYR A 1 531 ? 3.479   -65.806 9.998   1.00 30.87  ? 529 TYR A OH    1 
ATOM   4023 N N     . ALA A 1 532 ? 3.854   -70.659 2.780   1.00 35.44  ? 530 ALA A N     1 
ATOM   4024 C CA    . ALA A 1 532 ? 4.091   -71.722 1.776   1.00 35.06  ? 530 ALA A CA    1 
ATOM   4025 C C     . ALA A 1 532 ? 4.899   -71.171 0.603   1.00 33.14  ? 530 ALA A C     1 
ATOM   4026 O O     . ALA A 1 532 ? 5.825   -71.879 0.107   1.00 32.80  ? 530 ALA A O     1 
ATOM   4027 C CB    . ALA A 1 532 ? 2.780   -72.288 1.279   1.00 37.10  ? 530 ALA A CB    1 
ATOM   4028 N N     . CYS A 1 533 ? 4.548   -69.974 0.145   1.00 32.79  ? 531 CYS A N     1 
ATOM   4029 C CA    . CYS A 1 533 ? 5.275   -69.269 -0.942  1.00 33.42  ? 531 CYS A CA    1 
ATOM   4030 C C     . CYS A 1 533 ? 6.733   -69.077 -0.508  1.00 34.67  ? 531 CYS A C     1 
ATOM   4031 O O     . CYS A 1 533 ? 7.651   -69.481 -1.232  1.00 36.10  ? 531 CYS A O     1 
ATOM   4032 C CB    . CYS A 1 533 ? 4.618   -67.938 -1.275  1.00 35.77  ? 531 CYS A CB    1 
ATOM   4033 S SG    . CYS A 1 533 ? 3.061   -68.101 -2.192  1.00 35.00  ? 531 CYS A SG    1 
ATOM   4034 N N     . LEU A 1 534 ? 6.940   -68.550 0.683   1.00 35.21  ? 532 LEU A N     1 
ATOM   4035 C CA    . LEU A 1 534 ? 8.303   -68.334 1.224   1.00 37.99  ? 532 LEU A CA    1 
ATOM   4036 C C     . LEU A 1 534 ? 9.018   -69.667 1.489   1.00 37.19  ? 532 LEU A C     1 
ATOM   4037 O O     . LEU A 1 534 ? 10.255  -69.677 1.385   1.00 36.46  ? 532 LEU A O     1 
ATOM   4038 C CB    . LEU A 1 534 ? 8.228   -67.458 2.479   1.00 36.09  ? 532 LEU A CB    1 
ATOM   4039 C CG    . LEU A 1 534 ? 8.557   -65.996 2.213   1.00 35.07  ? 532 LEU A CG    1 
ATOM   4040 C CD1   . LEU A 1 534 ? 7.739   -65.452 1.074   1.00 35.66  ? 532 LEU A CD1   1 
ATOM   4041 C CD2   . LEU A 1 534 ? 8.374   -65.162 3.453   1.00 36.37  ? 532 LEU A CD2   1 
ATOM   4042 N N     . ALA A 1 535 ? 8.318   -70.747 1.853   1.00 35.39  ? 533 ALA A N     1 
ATOM   4043 C CA    . ALA A 1 535 ? 8.985   -72.056 2.017   1.00 33.67  ? 533 ALA A CA    1 
ATOM   4044 C C     . ALA A 1 535 ? 9.603   -72.477 0.663   1.00 34.69  ? 533 ALA A C     1 
ATOM   4045 O O     . ALA A 1 535 ? 10.796  -72.878 0.648   1.00 35.93  ? 533 ALA A O     1 
ATOM   4046 C CB    . ALA A 1 535 ? 8.042   -73.062 2.594   1.00 35.51  ? 533 ALA A CB    1 
ATOM   4047 N N     . TYR A 1 536 ? 8.883   -72.308 -0.448  1.00 31.63  ? 534 TYR A N     1 
ATOM   4048 C CA    . TYR A 1 536 ? 9.427   -72.547 -1.814  1.00 34.61  ? 534 TYR A CA    1 
ATOM   4049 C C     . TYR A 1 536 ? 10.661  -71.657 -2.108  1.00 33.68  ? 534 TYR A C     1 
ATOM   4050 O O     . TYR A 1 536 ? 11.757  -72.195 -2.452  1.00 34.70  ? 534 TYR A O     1 
ATOM   4051 C CB    . TYR A 1 536 ? 8.355   -72.346 -2.879  1.00 30.82  ? 534 TYR A CB    1 
ATOM   4052 C CG    . TYR A 1 536 ? 8.931   -72.247 -4.266  1.00 31.59  ? 534 TYR A CG    1 
ATOM   4053 C CD1   . TYR A 1 536 ? 9.436   -73.362 -4.915  1.00 31.75  ? 534 TYR A CD1   1 
ATOM   4054 C CD2   . TYR A 1 536 ? 8.985   -71.029 -4.924  1.00 34.42  ? 534 TYR A CD2   1 
ATOM   4055 C CE1   . TYR A 1 536 ? 9.969   -73.268 -6.188  1.00 33.87  ? 534 TYR A CE1   1 
ATOM   4056 C CE2   . TYR A 1 536 ? 9.517   -70.912 -6.195  1.00 36.13  ? 534 TYR A CE2   1 
ATOM   4057 C CZ    . TYR A 1 536 ? 10.006  -72.040 -6.828  1.00 37.73  ? 534 TYR A CZ    1 
ATOM   4058 O OH    . TYR A 1 536 ? 10.563  -71.910 -8.059  1.00 36.86  ? 534 TYR A OH    1 
ATOM   4059 N N     . PHE A 1 537 ? 10.517  -70.340 -1.944  1.00 32.86  ? 535 PHE A N     1 
ATOM   4060 C CA    . PHE A 1 537 ? 11.577  -69.330 -2.224  1.00 33.88  ? 535 PHE A CA    1 
ATOM   4061 C C     . PHE A 1 537 ? 12.818  -69.591 -1.353  1.00 32.57  ? 535 PHE A C     1 
ATOM   4062 O O     . PHE A 1 537 ? 13.910  -69.580 -1.916  1.00 31.91  ? 535 PHE A O     1 
ATOM   4063 C CB    . PHE A 1 537 ? 11.000  -67.908 -2.149  1.00 32.83  ? 535 PHE A CB    1 
ATOM   4064 C CG    . PHE A 1 537 ? 10.066  -67.610 -3.297  1.00 33.56  ? 535 PHE A CG    1 
ATOM   4065 C CD1   . PHE A 1 537 ? 10.497  -67.710 -4.612  1.00 34.54  ? 535 PHE A CD1   1 
ATOM   4066 C CD2   . PHE A 1 537 ? 8.736   -67.282 -3.071  1.00 34.75  ? 535 PHE A CD2   1 
ATOM   4067 C CE1   . PHE A 1 537 ? 9.626   -67.472 -5.665  1.00 35.33  ? 535 PHE A CE1   1 
ATOM   4068 C CE2   . PHE A 1 537 ? 7.861   -67.055 -4.123  1.00 31.87  ? 535 PHE A CE2   1 
ATOM   4069 C CZ    . PHE A 1 537 ? 8.308   -67.145 -5.420  1.00 33.95  ? 535 PHE A CZ    1 
ATOM   4070 N N     . TRP A 1 538 ? 12.679  -69.865 -0.056  1.00 29.27  ? 536 TRP A N     1 
ATOM   4071 C CA    . TRP A 1 538 ? 13.834  -70.251 0.789   1.00 34.43  ? 536 TRP A CA    1 
ATOM   4072 C C     . TRP A 1 538 ? 14.441  -71.580 0.341   1.00 34.56  ? 536 TRP A C     1 
ATOM   4073 O O     . TRP A 1 538 ? 15.675  -71.652 0.279   1.00 34.82  ? 536 TRP A O     1 
ATOM   4074 C CB    . TRP A 1 538 ? 13.498  -70.222 2.282   1.00 33.84  ? 536 TRP A CB    1 
ATOM   4075 C CG    . TRP A 1 538 ? 13.608  -68.820 2.773   1.00 36.71  ? 536 TRP A CG    1 
ATOM   4076 C CD1   . TRP A 1 538 ? 12.591  -68.005 3.174   1.00 36.79  ? 536 TRP A CD1   1 
ATOM   4077 C CD2   . TRP A 1 538 ? 14.801  -68.018 2.790   1.00 36.78  ? 536 TRP A CD2   1 
ATOM   4078 N NE1   . TRP A 1 538 ? 13.077  -66.760 3.466   1.00 40.73  ? 536 TRP A NE1   1 
ATOM   4079 C CE2   . TRP A 1 538 ? 14.433  -66.743 3.272   1.00 36.27  ? 536 TRP A CE2   1 
ATOM   4080 C CE3   . TRP A 1 538 ? 16.143  -68.256 2.481   1.00 37.07  ? 536 TRP A CE3   1 
ATOM   4081 C CZ2   . TRP A 1 538 ? 15.349  -65.711 3.427   1.00 31.91  ? 536 TRP A CZ2   1 
ATOM   4082 C CZ3   . TRP A 1 538 ? 17.061  -67.244 2.680   1.00 36.44  ? 536 TRP A CZ3   1 
ATOM   4083 C CH2   . TRP A 1 538 ? 16.662  -65.983 3.122   1.00 35.89  ? 536 TRP A CH2   1 
ATOM   4084 N N     . ALA A 1 539 ? 13.639  -72.588 0.019   1.00 37.24  ? 537 ALA A N     1 
ATOM   4085 C CA    . ALA A 1 539 ? 14.166  -73.857 -0.546  1.00 38.26  ? 537 ALA A CA    1 
ATOM   4086 C C     . ALA A 1 539 ? 14.932  -73.542 -1.846  1.00 39.76  ? 537 ALA A C     1 
ATOM   4087 O O     . ALA A 1 539 ? 16.055  -74.039 -2.029  1.00 42.92  ? 537 ALA A O     1 
ATOM   4088 C CB    . ALA A 1 539 ? 13.059  -74.857 -0.765  1.00 36.25  ? 537 ALA A CB    1 
ATOM   4089 N N     . ASP A 1 540 ? 14.390  -72.688 -2.704  1.00 36.57  ? 538 ASP A N     1 
ATOM   4090 C CA    . ASP A 1 540 ? 15.016  -72.437 -4.024  1.00 36.50  ? 538 ASP A CA    1 
ATOM   4091 C C     . ASP A 1 540 ? 16.310  -71.647 -3.810  1.00 37.06  ? 538 ASP A C     1 
ATOM   4092 O O     . ASP A 1 540 ? 17.326  -72.017 -4.376  1.00 40.93  ? 538 ASP A O     1 
ATOM   4093 C CB    . ASP A 1 540 ? 14.035  -71.752 -4.970  1.00 33.54  ? 538 ASP A CB    1 
ATOM   4094 C CG    . ASP A 1 540 ? 14.511  -71.797 -6.406  1.00 35.37  ? 538 ASP A CG    1 
ATOM   4095 O OD1   . ASP A 1 540 ? 15.224  -72.779 -6.795  1.00 36.95  ? 538 ASP A OD1   1 
ATOM   4096 O OD2   . ASP A 1 540 ? 14.192  -70.855 -7.118  1.00 36.58  ? 538 ASP A OD2   1 
ATOM   4097 N N     . MET A 1 541 ? 16.297  -70.665 -2.915  1.00 38.96  ? 539 MET A N     1 
ATOM   4098 C CA    . MET A 1 541 ? 17.496  -69.858 -2.599  1.00 37.09  ? 539 MET A CA    1 
ATOM   4099 C C     . MET A 1 541 ? 18.555  -70.764 -1.932  1.00 39.72  ? 539 MET A C     1 
ATOM   4100 O O     . MET A 1 541 ? 19.759  -70.566 -2.219  1.00 37.57  ? 539 MET A O     1 
ATOM   4101 C CB    . MET A 1 541 ? 17.124  -68.654 -1.733  1.00 33.34  ? 539 MET A CB    1 
ATOM   4102 C CG    . MET A 1 541 ? 16.475  -67.567 -2.521  1.00 34.67  ? 539 MET A CG    1 
ATOM   4103 S SD    . MET A 1 541 ? 16.281  -66.019 -1.594  1.00 36.24  ? 539 MET A SD    1 
ATOM   4104 C CE    . MET A 1 541 ? 14.958  -66.451 -0.462  1.00 34.78  ? 539 MET A CE    1 
ATOM   4105 N N     . ALA A 1 542 ? 18.140  -71.762 -1.140  1.00 39.54  ? 540 ALA A N     1 
ATOM   4106 C CA    . ALA A 1 542 ? 19.064  -72.744 -0.511  1.00 43.70  ? 540 ALA A CA    1 
ATOM   4107 C C     . ALA A 1 542 ? 19.717  -73.614 -1.606  1.00 43.62  ? 540 ALA A C     1 
ATOM   4108 O O     . ALA A 1 542 ? 20.955  -73.843 -1.513  1.00 40.31  ? 540 ALA A O     1 
ATOM   4109 C CB    . ALA A 1 542 ? 18.378  -73.573 0.566   1.00 38.95  ? 540 ALA A CB    1 
ATOM   4110 N N     . ARG A 1 543 ? 18.943  -74.049 -2.611  1.00 45.64  ? 541 ARG A N     1 
ATOM   4111 C CA    . ARG A 1 543 ? 19.425  -74.853 -3.764  1.00 41.32  ? 541 ARG A CA    1 
ATOM   4112 C C     . ARG A 1 543 ? 20.484  -74.063 -4.528  1.00 43.20  ? 541 ARG A C     1 
ATOM   4113 O O     . ARG A 1 543 ? 21.588  -74.640 -4.855  1.00 42.81  ? 541 ARG A O     1 
ATOM   4114 C CB    . ARG A 1 543 ? 18.268  -75.167 -4.706  1.00 45.61  ? 541 ARG A CB    1 
ATOM   4115 C CG    . ARG A 1 543 ? 18.682  -75.924 -5.957  1.00 44.79  ? 541 ARG A CG    1 
ATOM   4116 C CD    . ARG A 1 543 ? 17.682  -75.753 -7.069  1.00 46.76  ? 541 ARG A CD    1 
ATOM   4117 N NE    . ARG A 1 543 ? 17.387  -74.362 -7.378  1.00 49.45  ? 541 ARG A NE    1 
ATOM   4118 C CZ    . ARG A 1 543 ? 18.160  -73.541 -8.088  1.00 49.08  ? 541 ARG A CZ    1 
ATOM   4119 N NH1   . ARG A 1 543 ? 19.322  -73.942 -8.566  1.00 52.13  ? 541 ARG A NH1   1 
ATOM   4120 N NH2   . ARG A 1 543 ? 17.771  -72.301 -8.310  1.00 43.97  ? 541 ARG A NH2   1 
ATOM   4121 N N     . LEU A 1 544 ? 20.162  -72.804 -4.831  1.00 40.37  ? 542 LEU A N     1 
ATOM   4122 C CA    . LEU A 1 544 ? 21.076  -71.914 -5.597  1.00 42.02  ? 542 LEU A CA    1 
ATOM   4123 C C     . LEU A 1 544 ? 22.401  -71.757 -4.815  1.00 42.78  ? 542 LEU A C     1 
ATOM   4124 O O     . LEU A 1 544 ? 23.491  -71.907 -5.409  1.00 46.87  ? 542 LEU A O     1 
ATOM   4125 C CB    . LEU A 1 544 ? 20.387  -70.572 -5.879  1.00 40.19  ? 542 LEU A CB    1 
ATOM   4126 C CG    . LEU A 1 544 ? 21.219  -69.605 -6.722  1.00 40.97  ? 542 LEU A CG    1 
ATOM   4127 C CD1   . LEU A 1 544 ? 21.576  -70.246 -8.072  1.00 42.10  ? 542 LEU A CD1   1 
ATOM   4128 C CD2   . LEU A 1 544 ? 20.522  -68.281 -6.916  1.00 38.06  ? 542 LEU A CD2   1 
ATOM   4129 N N     . ALA A 1 545 ? 22.318  -71.514 -3.512  1.00 41.77  ? 543 ALA A N     1 
ATOM   4130 C CA    . ALA A 1 545 ? 23.485  -71.288 -2.641  1.00 45.67  ? 543 ALA A CA    1 
ATOM   4131 C C     . ALA A 1 545 ? 24.365  -72.550 -2.556  1.00 46.59  ? 543 ALA A C     1 
ATOM   4132 O O     . ALA A 1 545 ? 25.595  -72.401 -2.482  1.00 45.44  ? 543 ALA A O     1 
ATOM   4133 C CB    . ALA A 1 545 ? 23.002  -70.845 -1.292  1.00 44.59  ? 543 ALA A CB    1 
ATOM   4134 N N     . ALA A 1 546 ? 23.770  -73.744 -2.493  1.00 48.61  ? 544 ALA A N     1 
ATOM   4135 C CA    . ALA A 1 546 ? 24.470  -75.053 -2.559  1.00 47.42  ? 544 ALA A CA    1 
ATOM   4136 C C     . ALA A 1 546 ? 25.247  -75.156 -3.880  1.00 45.59  ? 544 ALA A C     1 
ATOM   4137 O O     . ALA A 1 546 ? 26.399  -75.627 -3.890  1.00 43.02  ? 544 ALA A O     1 
ATOM   4138 C CB    . ALA A 1 546 ? 23.465  -76.176 -2.443  1.00 45.77  ? 544 ALA A CB    1 
ATOM   4139 N N     . GLU A 1 547 ? 24.608  -74.747 -4.968  1.00 48.80  ? 545 GLU A N     1 
ATOM   4140 C CA    . GLU A 1 547 ? 25.133  -74.895 -6.345  1.00 49.57  ? 545 GLU A CA    1 
ATOM   4141 C C     . GLU A 1 547 ? 26.281  -73.887 -6.541  1.00 56.95  ? 545 GLU A C     1 
ATOM   4142 O O     . GLU A 1 547 ? 27.247  -74.196 -7.284  1.00 60.15  ? 545 GLU A O     1 
ATOM   4143 C CB    . GLU A 1 547 ? 23.950  -74.744 -7.293  1.00 46.38  ? 545 GLU A CB    1 
ATOM   4144 C CG    . GLU A 1 547 ? 24.310  -74.666 -8.753  1.00 52.84  ? 545 GLU A CG    1 
ATOM   4145 C CD    . GLU A 1 547 ? 23.186  -74.054 -9.576  1.00 59.70  ? 545 GLU A CD    1 
ATOM   4146 O OE1   . GLU A 1 547 ? 22.059  -74.574 -9.516  1.00 68.48  ? 545 GLU A OE1   1 
ATOM   4147 O OE2   . GLU A 1 547 ? 23.424  -73.034 -10.235 1.00 64.24  ? 545 GLU A OE2   1 
ATOM   4148 N N     . LYS A 1 548 ? 26.205  -72.738 -5.877  1.00 51.80  ? 546 LYS A N     1 
ATOM   4149 C CA    . LYS A 1 548 ? 27.266  -71.712 -6.009  1.00 51.08  ? 546 LYS A CA    1 
ATOM   4150 C C     . LYS A 1 548 ? 28.444  -72.097 -5.118  1.00 51.21  ? 546 LYS A C     1 
ATOM   4151 O O     . LYS A 1 548 ? 29.572  -71.722 -5.452  1.00 60.82  ? 546 LYS A O     1 
ATOM   4152 C CB    . LYS A 1 548 ? 26.733  -70.326 -5.636  1.00 50.76  ? 546 LYS A CB    1 
ATOM   4153 C CG    . LYS A 1 548 ? 25.639  -69.781 -6.541  1.00 53.17  ? 546 LYS A CG    1 
ATOM   4154 C CD    . LYS A 1 548 ? 26.168  -68.961 -7.691  1.00 46.16  ? 546 LYS A CD    1 
ATOM   4155 C CE    . LYS A 1 548 ? 25.086  -68.564 -8.670  1.00 50.57  ? 546 LYS A CE    1 
ATOM   4156 N NZ    . LYS A 1 548 ? 25.606  -67.663 -9.724  1.00 56.45  ? 546 LYS A NZ    1 
ATOM   4157 N N     . LEU A 1 549 ? 28.184  -72.831 -4.044  1.00 47.97  ? 547 LEU A N     1 
ATOM   4158 C CA    . LEU A 1 549 ? 29.258  -73.192 -3.088  1.00 49.61  ? 547 LEU A CA    1 
ATOM   4159 C C     . LEU A 1 549 ? 29.975  -74.439 -3.600  1.00 50.35  ? 547 LEU A C     1 
ATOM   4160 O O     . LEU A 1 549 ? 31.199  -74.514 -3.438  1.00 52.34  ? 547 LEU A O     1 
ATOM   4161 C CB    . LEU A 1 549 ? 28.639  -73.430 -1.709  1.00 48.67  ? 547 LEU A CB    1 
ATOM   4162 C CG    . LEU A 1 549 ? 28.349  -72.176 -0.887  1.00 51.62  ? 547 LEU A CG    1 
ATOM   4163 C CD1   . LEU A 1 549 ? 27.373  -72.483 0.236   1.00 50.09  ? 547 LEU A CD1   1 
ATOM   4164 C CD2   . LEU A 1 549 ? 29.632  -71.585 -0.327  1.00 49.89  ? 547 LEU A CD2   1 
ATOM   4165 N N     . ALA A 1 550 ? 29.231  -75.369 -4.199  1.00 49.35  ? 548 ALA A N     1 
ATOM   4166 C CA    . ALA A 1 550 ? 29.832  -76.589 -4.772  1.00 47.12  ? 548 ALA A CA    1 
ATOM   4167 C C     . ALA A 1 550 ? 30.755  -76.208 -5.928  1.00 47.92  ? 548 ALA A C     1 
ATOM   4168 O O     . ALA A 1 550 ? 31.756  -76.899 -6.121  1.00 50.14  ? 548 ALA A O     1 
ATOM   4169 C CB    . ALA A 1 550 ? 28.737  -77.502 -5.234  1.00 43.38  ? 548 ALA A CB    1 
ATOM   4170 N N     . ALA A 1 551 ? 30.441  -75.125 -6.630  1.00 47.34  ? 549 ALA A N     1 
ATOM   4171 C CA    . ALA A 1 551 ? 31.220  -74.718 -7.815  1.00 46.49  ? 549 ALA A CA    1 
ATOM   4172 C C     . ALA A 1 551 ? 32.374  -73.810 -7.410  1.00 52.85  ? 549 ALA A C     1 
ATOM   4173 O O     . ALA A 1 551 ? 33.183  -73.468 -8.281  1.00 61.76  ? 549 ALA A O     1 
ATOM   4174 C CB    . ALA A 1 551 ? 30.307  -74.007 -8.771  1.00 42.58  ? 549 ALA A CB    1 
ATOM   4175 N N     . GLY A 1 552 ? 32.436  -73.425 -6.143  1.00 54.77  ? 550 GLY A N     1 
ATOM   4176 C CA    . GLY A 1 552 ? 33.465  -72.467 -5.717  1.00 51.77  ? 550 GLY A CA    1 
ATOM   4177 C C     . GLY A 1 552 ? 33.069  -71.041 -6.037  1.00 52.72  ? 550 GLY A C     1 
ATOM   4178 O O     . GLY A 1 552 ? 32.824  -70.748 -7.214  1.00 54.21  ? 550 GLY A O     1 
ATOM   4179 N N     . THR A 1 553 ? 33.034  -70.184 -5.021  1.00 53.91  ? 551 THR A N     1 
ATOM   4180 C CA    . THR A 1 553 ? 32.685  -68.758 -5.210  1.00 51.78  ? 551 THR A CA    1 
ATOM   4181 C C     . THR A 1 553 ? 33.579  -67.888 -4.329  1.00 57.86  ? 551 THR A C     1 
ATOM   4182 O O     . THR A 1 553 ? 33.991  -68.361 -3.263  1.00 57.67  ? 551 THR A O     1 
ATOM   4183 C CB    . THR A 1 553 ? 31.230  -68.480 -4.818  1.00 50.00  ? 551 THR A CB    1 
ATOM   4184 O OG1   . THR A 1 553 ? 31.034  -67.067 -4.819  1.00 45.68  ? 551 THR A OG1   1 
ATOM   4185 C CG2   . THR A 1 553 ? 30.873  -69.044 -3.461  1.00 48.72  ? 551 THR A CG2   1 
ATOM   4186 N N     . GLY A 1 554 ? 33.881  -66.674 -4.773  1.00 59.87  ? 552 GLY A N     1 
ATOM   4187 C CA    . GLY A 1 554 ? 34.624  -65.723 -3.926  1.00 61.54  ? 552 GLY A CA    1 
ATOM   4188 C C     . GLY A 1 554 ? 33.761  -65.116 -2.827  1.00 64.46  ? 552 GLY A C     1 
ATOM   4189 O O     . GLY A 1 554 ? 34.313  -64.287 -2.073  1.00 62.24  ? 552 GLY A O     1 
ATOM   4190 N N     . GLU A 1 555 ? 32.468  -65.480 -2.749  1.00 61.93  ? 553 GLU A N     1 
ATOM   4191 C CA    . GLU A 1 555 ? 31.477  -64.941 -1.771  1.00 53.56  ? 553 GLU A CA    1 
ATOM   4192 C C     . GLU A 1 555 ? 30.851  -66.125 -1.023  1.00 51.69  ? 553 GLU A C     1 
ATOM   4193 O O     . GLU A 1 555 ? 29.639  -66.289 -1.074  1.00 55.39  ? 553 GLU A O     1 
ATOM   4194 C CB    . GLU A 1 555 ? 30.401  -64.115 -2.491  1.00 56.06  ? 553 GLU A CB    1 
ATOM   4195 C CG    . GLU A 1 555 ? 30.919  -63.163 -3.567  1.00 56.25  ? 553 GLU A CG    1 
ATOM   4196 C CD    . GLU A 1 555 ? 29.911  -62.153 -4.113  1.00 57.57  ? 553 GLU A CD    1 
ATOM   4197 O OE1   . GLU A 1 555 ? 29.543  -61.257 -3.369  1.00 59.92  ? 553 GLU A OE1   1 
ATOM   4198 O OE2   . GLU A 1 555 ? 29.505  -62.241 -5.296  1.00 56.92  ? 553 GLU A OE2   1 
ATOM   4199 N N     . GLU A 1 556 ? 31.656  -66.953 -0.376  1.00 47.72  ? 554 GLU A N     1 
ATOM   4200 C CA    . GLU A 1 556 ? 31.165  -68.163 0.327   1.00 50.46  ? 554 GLU A CA    1 
ATOM   4201 C C     . GLU A 1 556 ? 30.191  -67.763 1.435   1.00 48.37  ? 554 GLU A C     1 
ATOM   4202 O O     . GLU A 1 556 ? 29.102  -68.330 1.486   1.00 50.71  ? 554 GLU A O     1 
ATOM   4203 C CB    . GLU A 1 556 ? 32.316  -68.920 0.986   1.00 52.69  ? 554 GLU A CB    1 
ATOM   4204 C CG    . GLU A 1 556 ? 33.012  -69.885 0.064   1.00 58.24  ? 554 GLU A CG    1 
ATOM   4205 C CD    . GLU A 1 556 ? 34.192  -70.525 0.760   1.00 64.91  ? 554 GLU A CD    1 
ATOM   4206 O OE1   . GLU A 1 556 ? 35.320  -70.342 0.278   1.00 62.21  ? 554 GLU A OE1   1 
ATOM   4207 O OE2   . GLU A 1 556 ? 33.975  -71.157 1.812   1.00 74.59  ? 554 GLU A OE2   1 
ATOM   4208 N N     . ALA A 1 557 ? 30.616  -66.855 2.314   1.00 40.58  ? 555 ALA A N     1 
ATOM   4209 C CA    . ALA A 1 557 ? 29.833  -66.361 3.468   1.00 41.42  ? 555 ALA A CA    1 
ATOM   4210 C C     . ALA A 1 557 ? 28.412  -65.949 3.028   1.00 38.88  ? 555 ALA A C     1 
ATOM   4211 O O     . ALA A 1 557 ? 27.439  -66.373 3.683   1.00 35.88  ? 555 ALA A O     1 
ATOM   4212 C CB    . ALA A 1 557 ? 30.573  -65.224 4.148   1.00 38.84  ? 555 ALA A CB    1 
ATOM   4213 N N     . PHE A 1 558 ? 28.297  -65.167 1.955   1.00 37.18  ? 556 PHE A N     1 
ATOM   4214 C CA    . PHE A 1 558 ? 27.002  -64.659 1.424   1.00 40.35  ? 556 PHE A CA    1 
ATOM   4215 C C     . PHE A 1 558 ? 26.055  -65.842 1.185   1.00 40.34  ? 556 PHE A C     1 
ATOM   4216 O O     . PHE A 1 558 ? 24.898  -65.749 1.611   1.00 41.39  ? 556 PHE A O     1 
ATOM   4217 C CB    . PHE A 1 558 ? 27.185  -63.830 0.146   1.00 39.40  ? 556 PHE A CB    1 
ATOM   4218 C CG    . PHE A 1 558 ? 25.870  -63.456 -0.474  1.00 39.10  ? 556 PHE A CG    1 
ATOM   4219 C CD1   . PHE A 1 558 ? 25.201  -64.346 -1.293  1.00 42.00  ? 556 PHE A CD1   1 
ATOM   4220 C CD2   . PHE A 1 558 ? 25.267  -62.250 -0.183  1.00 41.24  ? 556 PHE A CD2   1 
ATOM   4221 C CE1   . PHE A 1 558 ? 23.969  -64.022 -1.830  1.00 40.02  ? 556 PHE A CE1   1 
ATOM   4222 C CE2   . PHE A 1 558 ? 24.030  -61.925 -0.717  1.00 40.57  ? 556 PHE A CE2   1 
ATOM   4223 C CZ    . PHE A 1 558 ? 23.385  -62.813 -1.535  1.00 40.00  ? 556 PHE A CZ    1 
ATOM   4224 N N     . TYR A 1 559 ? 26.555  -66.915 0.567   1.00 37.68  ? 557 TYR A N     1 
ATOM   4225 C CA    . TYR A 1 559 ? 25.793  -68.128 0.187   1.00 36.38  ? 557 TYR A CA    1 
ATOM   4226 C C     . TYR A 1 559 ? 25.598  -69.016 1.407   1.00 35.66  ? 557 TYR A C     1 
ATOM   4227 O O     . TYR A 1 559 ? 24.499  -69.594 1.559   1.00 37.20  ? 557 TYR A O     1 
ATOM   4228 C CB    . TYR A 1 559 ? 26.480  -68.852 -0.974  1.00 37.65  ? 557 TYR A CB    1 
ATOM   4229 C CG    . TYR A 1 559 ? 26.430  -68.056 -2.252  1.00 39.68  ? 557 TYR A CG    1 
ATOM   4230 C CD1   . TYR A 1 559 ? 25.219  -67.743 -2.844  1.00 37.62  ? 557 TYR A CD1   1 
ATOM   4231 C CD2   . TYR A 1 559 ? 27.579  -67.566 -2.834  1.00 40.13  ? 557 TYR A CD2   1 
ATOM   4232 C CE1   . TYR A 1 559 ? 25.151  -66.980 -3.991  1.00 41.24  ? 557 TYR A CE1   1 
ATOM   4233 C CE2   . TYR A 1 559 ? 27.531  -66.795 -3.984  1.00 44.58  ? 557 TYR A CE2   1 
ATOM   4234 C CZ    . TYR A 1 559 ? 26.313  -66.505 -4.573  1.00 45.28  ? 557 TYR A CZ    1 
ATOM   4235 O OH    . TYR A 1 559 ? 26.259  -65.738 -5.705  1.00 42.05  ? 557 TYR A OH    1 
ATOM   4236 N N     . LYS A 1 560 ? 26.594  -69.138 2.280   1.00 42.51  ? 558 LYS A N     1 
ATOM   4237 C CA    . LYS A 1 560 ? 26.388  -69.889 3.549   1.00 44.38  ? 558 LYS A CA    1 
ATOM   4238 C C     . LYS A 1 560 ? 25.264  -69.223 4.354   1.00 39.71  ? 558 LYS A C     1 
ATOM   4239 O O     . LYS A 1 560 ? 24.527  -69.966 5.012   1.00 38.41  ? 558 LYS A O     1 
ATOM   4240 C CB    . LYS A 1 560 ? 27.656  -69.979 4.393   1.00 50.31  ? 558 LYS A CB    1 
ATOM   4241 C CG    . LYS A 1 560 ? 28.612  -71.087 3.986   1.00 60.18  ? 558 LYS A CG    1 
ATOM   4242 C CD    . LYS A 1 560 ? 29.759  -71.272 4.962   1.00 67.49  ? 558 LYS A CD    1 
ATOM   4243 C CE    . LYS A 1 560 ? 31.116  -71.338 4.287   1.00 73.10  ? 558 LYS A CE    1 
ATOM   4244 N NZ    . LYS A 1 560 ? 31.276  -72.579 3.495   1.00 73.81  ? 558 LYS A NZ    1 
ATOM   4245 N N     . ALA A 1 561 ? 25.111  -67.892 4.284   1.00 40.06  ? 559 ALA A N     1 
ATOM   4246 C CA    . ALA A 1 561 ? 24.132  -67.135 5.114   1.00 39.95  ? 559 ALA A CA    1 
ATOM   4247 C C     . ALA A 1 561 ? 22.715  -67.418 4.610   1.00 40.22  ? 559 ALA A C     1 
ATOM   4248 O O     . ALA A 1 561 ? 21.809  -67.555 5.477   1.00 38.50  ? 559 ALA A O     1 
ATOM   4249 C CB    . ALA A 1 561 ? 24.428  -65.655 5.165   1.00 38.93  ? 559 ALA A CB    1 
ATOM   4250 N N     . LYS A 1 562 ? 22.552  -67.583 3.292   1.00 35.90  ? 560 LYS A N     1 
ATOM   4251 C CA    . LYS A 1 562 ? 21.260  -67.978 2.662   1.00 39.04  ? 560 LYS A CA    1 
ATOM   4252 C C     . LYS A 1 562 ? 20.812  -69.348 3.185   1.00 37.22  ? 560 LYS A C     1 
ATOM   4253 O O     . LYS A 1 562 ? 19.635  -69.468 3.461   1.00 36.62  ? 560 LYS A O     1 
ATOM   4254 C CB    . LYS A 1 562 ? 21.352  -68.010 1.133   1.00 38.08  ? 560 LYS A CB    1 
ATOM   4255 C CG    . LYS A 1 562 ? 21.506  -66.641 0.496   1.00 37.39  ? 560 LYS A CG    1 
ATOM   4256 C CD    . LYS A 1 562 ? 20.266  -65.797 0.644   1.00 37.11  ? 560 LYS A CD    1 
ATOM   4257 C CE    . LYS A 1 562 ? 20.417  -64.393 0.091   1.00 36.43  ? 560 LYS A CE    1 
ATOM   4258 N NZ    . LYS A 1 562 ? 19.156  -63.611 0.158   1.00 37.38  ? 560 LYS A NZ    1 
ATOM   4259 N N     . LEU A 1 563 ? 21.721  -70.322 3.321   1.00 37.17  ? 561 LEU A N     1 
ATOM   4260 C CA    . LEU A 1 563 ? 21.417  -71.699 3.785   1.00 34.13  ? 561 LEU A CA    1 
ATOM   4261 C C     . LEU A 1 563 ? 20.983  -71.620 5.245   1.00 35.86  ? 561 LEU A C     1 
ATOM   4262 O O     . LEU A 1 563 ? 19.948  -72.225 5.608   1.00 36.56  ? 561 LEU A O     1 
ATOM   4263 C CB    . LEU A 1 563 ? 22.635  -72.618 3.612   1.00 33.52  ? 561 LEU A CB    1 
ATOM   4264 C CG    . LEU A 1 563 ? 22.846  -73.138 2.188   1.00 37.18  ? 561 LEU A CG    1 
ATOM   4265 C CD1   . LEU A 1 563 ? 24.301  -73.523 1.924   1.00 36.71  ? 561 LEU A CD1   1 
ATOM   4266 C CD2   . LEU A 1 563 ? 21.938  -74.318 1.900   1.00 36.30  ? 561 LEU A CD2   1 
ATOM   4267 N N     . GLN A 1 564 ? 21.744  -70.898 6.054   1.00 35.38  ? 562 GLN A N     1 
ATOM   4268 C CA    . GLN A 1 564 ? 21.424  -70.730 7.483   1.00 33.60  ? 562 GLN A CA    1 
ATOM   4269 C C     . GLN A 1 564 ? 20.073  -70.024 7.637   1.00 34.77  ? 562 GLN A C     1 
ATOM   4270 O O     . GLN A 1 564 ? 19.337  -70.422 8.556   1.00 36.05  ? 562 GLN A O     1 
ATOM   4271 C CB    . GLN A 1 564 ? 22.585  -70.027 8.166   1.00 37.49  ? 562 GLN A CB    1 
ATOM   4272 C CG    . GLN A 1 564 ? 23.683  -71.013 8.520   1.00 41.45  ? 562 GLN A CG    1 
ATOM   4273 C CD    . GLN A 1 564 ? 25.035  -70.361 8.673   1.00 49.80  ? 562 GLN A CD    1 
ATOM   4274 O OE1   . GLN A 1 564 ? 25.324  -69.298 8.119   1.00 47.08  ? 562 GLN A OE1   1 
ATOM   4275 N NE2   . GLN A 1 564 ? 25.882  -71.019 9.449   1.00 54.45  ? 562 GLN A NE2   1 
ATOM   4276 N N     . THR A 1 565 ? 19.737  -69.034 6.795   1.00 32.05  ? 563 THR A N     1 
ATOM   4277 C CA    . THR A 1 565 ? 18.456  -68.283 6.944   1.00 32.38  ? 563 THR A CA    1 
ATOM   4278 C C     . THR A 1 565 ? 17.296  -69.214 6.533   1.00 36.03  ? 563 THR A C     1 
ATOM   4279 O O     . THR A 1 565 ? 16.209  -69.207 7.217   1.00 33.88  ? 563 THR A O     1 
ATOM   4280 C CB    . THR A 1 565 ? 18.428  -66.954 6.177   1.00 32.60  ? 563 THR A CB    1 
ATOM   4281 O OG1   . THR A 1 565 ? 19.534  -66.099 6.475   1.00 30.74  ? 563 THR A OG1   1 
ATOM   4282 C CG2   . THR A 1 565 ? 17.157  -66.193 6.470   1.00 30.46  ? 563 THR A CG2   1 
ATOM   4283 N N     . ALA A 1 566 ? 17.508  -70.005 5.473   1.00 34.62  ? 564 ALA A N     1 
ATOM   4284 C CA    . ALA A 1 566 ? 16.496  -70.933 4.931   1.00 33.63  ? 564 ALA A CA    1 
ATOM   4285 C C     . ALA A 1 566 ? 16.193  -71.979 6.010   1.00 32.91  ? 564 ALA A C     1 
ATOM   4286 O O     . ALA A 1 566 ? 15.013  -72.308 6.186   1.00 29.98  ? 564 ALA A O     1 
ATOM   4287 C CB    . ALA A 1 566 ? 16.952  -71.538 3.611   1.00 33.93  ? 564 ALA A CB    1 
ATOM   4288 N N     . ARG A 1 567 ? 17.212  -72.442 6.736   1.00 33.75  ? 565 ARG A N     1 
ATOM   4289 C CA    . ARG A 1 567 ? 17.067  -73.485 7.797   1.00 38.13  ? 565 ARG A CA    1 
ATOM   4290 C C     . ARG A 1 567 ? 16.294  -72.896 8.984   1.00 36.74  ? 565 ARG A C     1 
ATOM   4291 O O     . ARG A 1 567 ? 15.485  -73.627 9.585   1.00 36.55  ? 565 ARG A O     1 
ATOM   4292 C CB    . ARG A 1 567 ? 18.435  -74.030 8.251   1.00 37.75  ? 565 ARG A CB    1 
ATOM   4293 C CG    . ARG A 1 567 ? 18.377  -74.984 9.443   1.00 42.81  ? 565 ARG A CG    1 
ATOM   4294 C CD    . ARG A 1 567 ? 19.629  -75.820 9.640   1.00 43.83  ? 565 ARG A CD    1 
ATOM   4295 N NE    . ARG A 1 567 ? 20.059  -76.291 8.322   1.00 48.57  ? 565 ARG A NE    1 
ATOM   4296 C CZ    . ARG A 1 567 ? 21.157  -75.888 7.663   1.00 54.14  ? 565 ARG A CZ    1 
ATOM   4297 N NH1   . ARG A 1 567 ? 22.010  -75.027 8.196   1.00 56.93  ? 565 ARG A NH1   1 
ATOM   4298 N NH2   . ARG A 1 567 ? 21.404  -76.356 6.454   1.00 55.01  ? 565 ARG A NH2   1 
ATOM   4299 N N     . PHE A 1 568 ? 16.616  -71.657 9.362   1.00 35.33  ? 566 PHE A N     1 
ATOM   4300 C CA    . PHE A 1 568 ? 15.889  -70.880 10.395  1.00 37.89  ? 566 PHE A CA    1 
ATOM   4301 C C     . PHE A 1 568 ? 14.413  -70.718 9.992   1.00 35.22  ? 566 PHE A C     1 
ATOM   4302 O O     . PHE A 1 568 ? 13.534  -70.886 10.868  1.00 31.18  ? 566 PHE A O     1 
ATOM   4303 C CB    . PHE A 1 568 ? 16.528  -69.503 10.614  1.00 36.39  ? 566 PHE A CB    1 
ATOM   4304 C CG    . PHE A 1 568 ? 15.671  -68.613 11.468  1.00 32.23  ? 566 PHE A CG    1 
ATOM   4305 C CD1   . PHE A 1 568 ? 15.733  -68.685 12.846  1.00 33.60  ? 566 PHE A CD1   1 
ATOM   4306 C CD2   . PHE A 1 568 ? 14.735  -67.773 10.885  1.00 33.29  ? 566 PHE A CD2   1 
ATOM   4307 C CE1   . PHE A 1 568 ? 14.897  -67.890 13.613  1.00 34.88  ? 566 PHE A CE1   1 
ATOM   4308 C CE2   . PHE A 1 568 ? 13.905  -66.980 11.658  1.00 30.51  ? 566 PHE A CE2   1 
ATOM   4309 C CZ    . PHE A 1 568 ? 13.998  -67.030 13.020  1.00 29.64  ? 566 PHE A CZ    1 
ATOM   4310 N N     . TYR A 1 569 ? 14.149  -70.372 8.730   1.00 30.36  ? 567 TYR A N     1 
ATOM   4311 C CA    . TYR A 1 569 ? 12.773  -70.085 8.272   1.00 32.76  ? 567 TYR A CA    1 
ATOM   4312 C C     . TYR A 1 569 ? 11.981  -71.376 8.437   1.00 34.67  ? 567 TYR A C     1 
ATOM   4313 O O     . TYR A 1 569 ? 10.983  -71.388 9.210   1.00 36.51  ? 567 TYR A O     1 
ATOM   4314 C CB    . TYR A 1 569 ? 12.698  -69.528 6.850   1.00 30.47  ? 567 TYR A CB    1 
ATOM   4315 C CG    . TYR A 1 569 ? 11.266  -69.388 6.406   1.00 31.13  ? 567 TYR A CG    1 
ATOM   4316 C CD1   . TYR A 1 569 ? 10.512  -68.276 6.754   1.00 30.02  ? 567 TYR A CD1   1 
ATOM   4317 C CD2   . TYR A 1 569 ? 10.630  -70.400 5.699   1.00 30.39  ? 567 TYR A CD2   1 
ATOM   4318 C CE1   . TYR A 1 569 ? 9.177   -68.175 6.408   1.00 29.03  ? 567 TYR A CE1   1 
ATOM   4319 C CE2   . TYR A 1 569 ? 9.302   -70.302 5.331   1.00 28.35  ? 567 TYR A CE2   1 
ATOM   4320 C CZ    . TYR A 1 569 ? 8.568   -69.191 5.697   1.00 27.67  ? 567 TYR A CZ    1 
ATOM   4321 O OH    . TYR A 1 569 ? 7.253   -69.097 5.352   1.00 26.63  ? 567 TYR A OH    1 
ATOM   4322 N N     . PHE A 1 570 ? 12.483  -72.450 7.831   1.00 33.90  ? 568 PHE A N     1 
ATOM   4323 C CA    . PHE A 1 570 ? 11.861  -73.804 7.913   1.00 36.48  ? 568 PHE A CA    1 
ATOM   4324 C C     . PHE A 1 570 ? 11.634  -74.265 9.355   1.00 35.63  ? 568 PHE A C     1 
ATOM   4325 O O     . PHE A 1 570 ? 10.596  -74.842 9.599   1.00 36.26  ? 568 PHE A O     1 
ATOM   4326 C CB    . PHE A 1 570 ? 12.662  -74.861 7.149   1.00 36.10  ? 568 PHE A CB    1 
ATOM   4327 C CG    . PHE A 1 570 ? 12.198  -74.982 5.718   1.00 36.42  ? 568 PHE A CG    1 
ATOM   4328 C CD1   . PHE A 1 570 ? 12.598  -74.050 4.765   1.00 31.49  ? 568 PHE A CD1   1 
ATOM   4329 C CD2   . PHE A 1 570 ? 11.336  -75.998 5.334   1.00 32.99  ? 568 PHE A CD2   1 
ATOM   4330 C CE1   . PHE A 1 570 ? 12.159  -74.141 3.462   1.00 31.49  ? 568 PHE A CE1   1 
ATOM   4331 C CE2   . PHE A 1 570 ? 10.914  -76.094 4.020   1.00 30.67  ? 568 PHE A CE2   1 
ATOM   4332 C CZ    . PHE A 1 570 ? 11.321  -75.169 3.091   1.00 31.82  ? 568 PHE A CZ    1 
ATOM   4333 N N     . GLN A 1 571 ? 12.542  -74.024 10.290  1.00 37.84  ? 569 GLN A N     1 
ATOM   4334 C CA    . GLN A 1 571 ? 12.449  -74.679 11.623  1.00 37.49  ? 569 GLN A CA    1 
ATOM   4335 C C     . GLN A 1 571 ? 11.700  -73.817 12.647  1.00 34.86  ? 569 GLN A C     1 
ATOM   4336 O O     . GLN A 1 571 ? 11.050  -74.434 13.548  1.00 34.86  ? 569 GLN A O     1 
ATOM   4337 C CB    . GLN A 1 571 ? 13.842  -75.091 12.101  1.00 35.43  ? 569 GLN A CB    1 
ATOM   4338 C CG    . GLN A 1 571 ? 14.416  -76.235 11.288  1.00 35.85  ? 569 GLN A CG    1 
ATOM   4339 C CD    . GLN A 1 571 ? 15.797  -76.611 11.752  1.00 38.25  ? 569 GLN A CD    1 
ATOM   4340 O OE1   . GLN A 1 571 ? 16.319  -76.126 12.754  1.00 42.61  ? 569 GLN A OE1   1 
ATOM   4341 N NE2   . GLN A 1 571 ? 16.410  -77.498 11.009  1.00 37.74  ? 569 GLN A NE2   1 
ATOM   4342 N N     . ARG A 1 572 ? 11.770  -72.482 12.550  1.00 34.40  ? 570 ARG A N     1 
ATOM   4343 C CA    . ARG A 1 572 ? 11.217  -71.580 13.617  1.00 38.02  ? 570 ARG A CA    1 
ATOM   4344 C C     . ARG A 1 572 ? 9.997   -70.760 13.145  1.00 36.12  ? 570 ARG A C     1 
ATOM   4345 O O     . ARG A 1 572 ? 9.277   -70.234 14.033  1.00 31.43  ? 570 ARG A O     1 
ATOM   4346 C CB    . ARG A 1 572 ? 12.311  -70.682 14.218  1.00 35.37  ? 570 ARG A CB    1 
ATOM   4347 C CG    . ARG A 1 572 ? 13.297  -71.469 15.064  1.00 37.52  ? 570 ARG A CG    1 
ATOM   4348 C CD    . ARG A 1 572 ? 14.269  -70.652 15.872  1.00 38.89  ? 570 ARG A CD    1 
ATOM   4349 N NE    . ARG A 1 572 ? 15.047  -71.456 16.811  1.00 39.15  ? 570 ARG A NE    1 
ATOM   4350 C CZ    . ARG A 1 572 ? 14.800  -71.586 18.121  1.00 37.40  ? 570 ARG A CZ    1 
ATOM   4351 N NH1   . ARG A 1 572 ? 13.773  -70.988 18.688  1.00 37.70  ? 570 ARG A NH1   1 
ATOM   4352 N NH2   . ARG A 1 572 ? 15.575  -72.337 18.870  1.00 37.72  ? 570 ARG A NH2   1 
ATOM   4353 N N     . ILE A 1 573 ? 9.743   -70.651 11.837  1.00 36.21  ? 571 ILE A N     1 
ATOM   4354 C CA    . ILE A 1 573 ? 8.692   -69.740 11.305  1.00 35.81  ? 571 ILE A CA    1 
ATOM   4355 C C     . ILE A 1 573 ? 7.612   -70.535 10.588  1.00 36.58  ? 571 ILE A C     1 
ATOM   4356 O O     . ILE A 1 573 ? 6.455   -70.324 10.912  1.00 36.72  ? 571 ILE A O     1 
ATOM   4357 C CB    . ILE A 1 573 ? 9.334   -68.667 10.413  1.00 43.10  ? 571 ILE A CB    1 
ATOM   4358 C CG1   . ILE A 1 573 ? 10.372  -67.903 11.240  1.00 44.04  ? 571 ILE A CG1   1 
ATOM   4359 C CG2   . ILE A 1 573 ? 8.251   -67.776 9.798   1.00 44.08  ? 571 ILE A CG2   1 
ATOM   4360 C CD1   . ILE A 1 573 ? 10.409  -66.456 10.988  1.00 53.06  ? 571 ILE A CD1   1 
ATOM   4361 N N     . LEU A 1 574 ? 7.995   -71.383 9.637   1.00 33.72  ? 572 LEU A N     1 
ATOM   4362 C CA    . LEU A 1 574 ? 7.054   -72.240 8.883   1.00 35.72  ? 572 LEU A CA    1 
ATOM   4363 C C     . LEU A 1 574 ? 6.090   -72.976 9.824   1.00 34.63  ? 572 LEU A C     1 
ATOM   4364 O O     . LEU A 1 574 ? 4.943   -73.143 9.441   1.00 35.99  ? 572 LEU A O     1 
ATOM   4365 C CB    . LEU A 1 574 ? 7.841   -73.216 8.001   1.00 33.12  ? 572 LEU A CB    1 
ATOM   4366 C CG    . LEU A 1 574 ? 7.031   -73.946 6.930   1.00 34.36  ? 572 LEU A CG    1 
ATOM   4367 C CD1   . LEU A 1 574 ? 6.209   -72.960 6.089   1.00 33.26  ? 572 LEU A CD1   1 
ATOM   4368 C CD2   . LEU A 1 574 ? 7.962   -74.791 6.044   1.00 34.56  ? 572 LEU A CD2   1 
ATOM   4369 N N     . PRO A 1 575 ? 6.474   -73.473 11.028  1.00 33.23  ? 573 PRO A N     1 
ATOM   4370 C CA    . PRO A 1 575 ? 5.517   -74.149 11.917  1.00 34.13  ? 573 PRO A CA    1 
ATOM   4371 C C     . PRO A 1 575 ? 4.274   -73.329 12.322  1.00 37.30  ? 573 PRO A C     1 
ATOM   4372 O O     . PRO A 1 575 ? 3.313   -73.909 12.782  1.00 38.99  ? 573 PRO A O     1 
ATOM   4373 C CB    . PRO A 1 575 ? 6.357   -74.533 13.154  1.00 36.07  ? 573 PRO A CB    1 
ATOM   4374 C CG    . PRO A 1 575 ? 7.779   -74.645 12.602  1.00 39.22  ? 573 PRO A CG    1 
ATOM   4375 C CD    . PRO A 1 575 ? 7.854   -73.560 11.539  1.00 38.99  ? 573 PRO A CD    1 
ATOM   4376 N N     . ARG A 1 576 ? 4.297   -72.001 12.158  1.00 36.62  ? 574 ARG A N     1 
ATOM   4377 C CA    . ARG A 1 576 ? 3.105   -71.124 12.312  1.00 30.98  ? 574 ARG A CA    1 
ATOM   4378 C C     . ARG A 1 576 ? 1.951   -71.664 11.465  1.00 31.45  ? 574 ARG A C     1 
ATOM   4379 O O     . ARG A 1 576 ? 0.798   -71.484 11.868  1.00 26.48  ? 574 ARG A O     1 
ATOM   4380 C CB    . ARG A 1 576 ? 3.430   -69.701 11.864  1.00 28.83  ? 574 ARG A CB    1 
ATOM   4381 C CG    . ARG A 1 576 ? 4.396   -68.986 12.789  1.00 29.47  ? 574 ARG A CG    1 
ATOM   4382 C CD    . ARG A 1 576 ? 4.821   -67.683 12.210  1.00 27.94  ? 574 ARG A CD    1 
ATOM   4383 N NE    . ARG A 1 576 ? 5.750   -67.012 13.086  1.00 28.37  ? 574 ARG A NE    1 
ATOM   4384 C CZ    . ARG A 1 576 ? 6.057   -65.717 12.987  1.00 29.21  ? 574 ARG A CZ    1 
ATOM   4385 N NH1   . ARG A 1 576 ? 5.507   -64.954 12.062  1.00 30.02  ? 574 ARG A NH1   1 
ATOM   4386 N NH2   . ARG A 1 576 ? 6.947   -65.184 13.788  1.00 26.25  ? 574 ARG A NH2   1 
ATOM   4387 N N     . THR A 1 577 ? 2.245   -72.301 10.325  1.00 30.91  ? 575 THR A N     1 
ATOM   4388 C CA    . THR A 1 577 ? 1.197   -72.950 9.483   1.00 33.43  ? 575 THR A CA    1 
ATOM   4389 C C     . THR A 1 577 ? 0.333   -73.898 10.344  1.00 36.86  ? 575 THR A C     1 
ATOM   4390 O O     . THR A 1 577 ? -0.867  -74.050 9.978   1.00 38.20  ? 575 THR A O     1 
ATOM   4391 C CB    . THR A 1 577 ? 1.780   -73.688 8.267   1.00 33.12  ? 575 THR A CB    1 
ATOM   4392 O OG1   . THR A 1 577 ? 2.715   -74.645 8.774   1.00 32.10  ? 575 THR A OG1   1 
ATOM   4393 C CG2   . THR A 1 577 ? 2.439   -72.772 7.262   1.00 30.91  ? 575 THR A CG2   1 
ATOM   4394 N N     . ARG A 1 578 ? 0.875   -74.485 11.434  1.00 35.23  ? 576 ARG A N     1 
ATOM   4395 C CA    . ARG A 1 578 ? 0.161   -75.477 12.290  1.00 34.99  ? 576 ARG A CA    1 
ATOM   4396 C C     . ARG A 1 578 ? -1.062  -74.770 12.872  1.00 36.91  ? 576 ARG A C     1 
ATOM   4397 O O     . ARG A 1 578 ? -2.173  -75.323 12.728  1.00 40.75  ? 576 ARG A O     1 
ATOM   4398 C CB    . ARG A 1 578 ? 1.021   -76.066 13.429  1.00 33.93  ? 576 ARG A CB    1 
ATOM   4399 C CG    . ARG A 1 578 ? 2.236   -76.903 13.017  1.00 32.04  ? 576 ARG A CG    1 
ATOM   4400 C CD    . ARG A 1 578 ? 1.902   -77.981 11.991  1.00 33.92  ? 576 ARG A CD    1 
ATOM   4401 N NE    . ARG A 1 578 ? 2.032   -77.508 10.609  1.00 32.41  ? 576 ARG A NE    1 
ATOM   4402 C CZ    . ARG A 1 578 ? 1.208   -77.771 9.595   1.00 32.17  ? 576 ARG A CZ    1 
ATOM   4403 N NH1   . ARG A 1 578 ? 0.136   -78.527 9.741   1.00 35.82  ? 576 ARG A NH1   1 
ATOM   4404 N NH2   . ARG A 1 578 ? 1.450   -77.264 8.400   1.00 34.04  ? 576 ARG A NH2   1 
ATOM   4405 N N     . ALA A 1 579 ? -0.845  -73.604 13.508  1.00 40.82  ? 577 ALA A N     1 
ATOM   4406 C CA    . ALA A 1 579 ? -1.873  -72.716 14.132  1.00 34.27  ? 577 ALA A CA    1 
ATOM   4407 C C     . ALA A 1 579 ? -2.947  -72.339 13.105  1.00 30.83  ? 577 ALA A C     1 
ATOM   4408 O O     . ALA A 1 579 ? -4.140  -72.452 13.411  1.00 32.19  ? 577 ALA A O     1 
ATOM   4409 C CB    . ALA A 1 579 ? -1.223  -71.468 14.696  1.00 33.47  ? 577 ALA A CB    1 
ATOM   4410 N N     . HIS A 1 580 ? -2.538  -71.922 11.910  1.00 30.56  ? 578 HIS A N     1 
ATOM   4411 C CA    . HIS A 1 580 ? -3.431  -71.461 10.823  1.00 31.98  ? 578 HIS A CA    1 
ATOM   4412 C C     . HIS A 1 580 ? -4.267  -72.641 10.289  1.00 35.35  ? 578 HIS A C     1 
ATOM   4413 O O     . HIS A 1 580 ? -5.439  -72.410 9.924   1.00 34.68  ? 578 HIS A O     1 
ATOM   4414 C CB    . HIS A 1 580 ? -2.602  -70.752 9.735   1.00 33.48  ? 578 HIS A CB    1 
ATOM   4415 C CG    . HIS A 1 580 ? -1.987  -69.459 10.155  1.00 31.73  ? 578 HIS A CG    1 
ATOM   4416 N ND1   . HIS A 1 580 ? -2.737  -68.386 10.586  1.00 33.83  ? 578 HIS A ND1   1 
ATOM   4417 C CD2   . HIS A 1 580 ? -0.702  -69.054 10.175  1.00 33.00  ? 578 HIS A CD2   1 
ATOM   4418 C CE1   . HIS A 1 580 ? -1.939  -67.380 10.865  1.00 34.88  ? 578 HIS A CE1   1 
ATOM   4419 N NE2   . HIS A 1 580 ? -0.682  -67.766 10.613  1.00 33.50  ? 578 HIS A NE2   1 
ATOM   4420 N N     . VAL A 1 581 ? -3.698  -73.851 10.192  1.00 36.01  ? 579 VAL A N     1 
ATOM   4421 C CA    . VAL A 1 581 ? -4.434  -75.073 9.745   1.00 37.19  ? 579 VAL A CA    1 
ATOM   4422 C C     . VAL A 1 581 ? -5.559  -75.381 10.752  1.00 35.75  ? 579 VAL A C     1 
ATOM   4423 O O     . VAL A 1 581 ? -6.734  -75.502 10.340  1.00 34.23  ? 579 VAL A O     1 
ATOM   4424 C CB    . VAL A 1 581 ? -3.487  -76.282 9.608   1.00 40.34  ? 579 VAL A CB    1 
ATOM   4425 C CG1   . VAL A 1 581 ? -4.242  -77.606 9.593   1.00 37.59  ? 579 VAL A CG1   1 
ATOM   4426 C CG2   . VAL A 1 581 ? -2.596  -76.174 8.381   1.00 41.11  ? 579 VAL A CG2   1 
ATOM   4427 N N     . ALA A 1 582 ? -5.203  -75.546 12.025  1.00 34.16  ? 580 ALA A N     1 
ATOM   4428 C CA    . ALA A 1 582 ? -6.159  -75.827 13.123  1.00 34.83  ? 580 ALA A CA    1 
ATOM   4429 C C     . ALA A 1 582 ? -7.271  -74.753 13.152  1.00 37.68  ? 580 ALA A C     1 
ATOM   4430 O O     . ALA A 1 582 ? -8.472  -75.103 13.132  1.00 40.88  ? 580 ALA A O     1 
ATOM   4431 C CB    . ALA A 1 582 ? -5.411  -75.939 14.419  1.00 30.58  ? 580 ALA A CB    1 
ATOM   4432 N N     . ALA A 1 583 ? -6.926  -73.471 13.099  1.00 38.99  ? 581 ALA A N     1 
ATOM   4433 C CA    . ALA A 1 583 ? -7.938  -72.388 13.115  1.00 36.70  ? 581 ALA A CA    1 
ATOM   4434 C C     . ALA A 1 583 ? -8.884  -72.562 11.923  1.00 35.13  ? 581 ALA A C     1 
ATOM   4435 O O     . ALA A 1 583 ? -10.101 -72.596 12.140  1.00 33.67  ? 581 ALA A O     1 
ATOM   4436 C CB    . ALA A 1 583 ? -7.292  -71.025 13.122  1.00 34.57  ? 581 ALA A CB    1 
ATOM   4437 N N     . MET A 1 584 ? -8.354  -72.700 10.712  1.00 33.93  ? 582 MET A N     1 
ATOM   4438 C CA    . MET A 1 584 ? -9.210  -72.681 9.503   1.00 38.33  ? 582 MET A CA    1 
ATOM   4439 C C     . MET A 1 584 ? -10.035 -73.975 9.431   1.00 38.73  ? 582 MET A C     1 
ATOM   4440 O O     . MET A 1 584 ? -11.124 -73.890 8.908   1.00 35.75  ? 582 MET A O     1 
ATOM   4441 C CB    . MET A 1 584 ? -8.431  -72.384 8.214   1.00 36.77  ? 582 MET A CB    1 
ATOM   4442 C CG    . MET A 1 584 ? -7.904  -73.548 7.445   1.00 40.87  ? 582 MET A CG    1 
ATOM   4443 S SD    . MET A 1 584 ? -6.984  -72.951 5.956   1.00 42.84  ? 582 MET A SD    1 
ATOM   4444 C CE    . MET A 1 584 ? -5.368  -72.593 6.646   1.00 40.11  ? 582 MET A CE    1 
ATOM   4445 N N     . LEU A 1 585 ? -9.617  -75.083 10.061  1.00 42.06  ? 583 LEU A N     1 
ATOM   4446 C CA    . LEU A 1 585 ? -10.418 -76.344 10.069  1.00 42.91  ? 583 LEU A CA    1 
ATOM   4447 C C     . LEU A 1 585 ? -11.347 -76.412 11.306  1.00 40.70  ? 583 LEU A C     1 
ATOM   4448 O O     . LEU A 1 585 ? -12.165 -77.355 11.368  1.00 43.76  ? 583 LEU A O     1 
ATOM   4449 C CB    . LEU A 1 585 ? -9.475  -77.554 9.969   1.00 46.46  ? 583 LEU A CB    1 
ATOM   4450 C CG    . LEU A 1 585 ? -8.748  -77.721 8.627   1.00 47.03  ? 583 LEU A CG    1 
ATOM   4451 C CD1   . LEU A 1 585 ? -7.810  -78.920 8.640   1.00 48.61  ? 583 LEU A CD1   1 
ATOM   4452 C CD2   . LEU A 1 585 ? -9.722  -77.852 7.478   1.00 47.22  ? 583 LEU A CD2   1 
ATOM   4453 N N     . SER A 1 586 ? -11.301 -75.394 12.176  1.00 35.21  ? 584 SER A N     1 
ATOM   4454 C CA    . SER A 1 586 ? -12.105 -75.330 13.431  1.00 34.30  ? 584 SER A CA    1 
ATOM   4455 C C     . SER A 1 586 ? -13.595 -75.101 13.167  1.00 34.40  ? 584 SER A C     1 
ATOM   4456 O O     . SER A 1 586 ? -14.389 -75.414 14.048  1.00 38.64  ? 584 SER A O     1 
ATOM   4457 C CB    . SER A 1 586 ? -11.578 -74.252 14.351  1.00 32.82  ? 584 SER A CB    1 
ATOM   4458 O OG    . SER A 1 586 ? -12.019 -72.971 13.944  1.00 35.17  ? 584 SER A OG    1 
ATOM   4459 N N     . GLY A 1 587 ? -13.940 -74.517 12.027  1.00 31.68  ? 585 GLY A N     1 
ATOM   4460 C CA    . GLY A 1 587 ? -15.347 -74.230 11.723  1.00 32.42  ? 585 GLY A CA    1 
ATOM   4461 C C     . GLY A 1 587 ? -15.749 -72.792 11.972  1.00 31.40  ? 585 GLY A C     1 
ATOM   4462 O O     . GLY A 1 587 ? -15.117 -72.145 12.811  1.00 40.87  ? 585 GLY A O     1 
ATOM   4463 N N     . ALA A 1 588 ? -16.799 -72.337 11.300  1.00 30.31  ? 586 ALA A N     1 
ATOM   4464 C CA    . ALA A 1 588 ? -17.295 -70.951 11.424  1.00 33.38  ? 586 ALA A CA    1 
ATOM   4465 C C     . ALA A 1 588 ? -18.137 -70.757 12.686  1.00 33.01  ? 586 ALA A C     1 
ATOM   4466 O O     . ALA A 1 588 ? -18.238 -69.619 13.145  1.00 32.19  ? 586 ALA A O     1 
ATOM   4467 C CB    . ALA A 1 588 ? -18.108 -70.637 10.197  1.00 34.12  ? 586 ALA A CB    1 
ATOM   4468 N N     . ASN A 1 589 ? -18.704 -71.830 13.224  1.00 33.35  ? 587 ASN A N     1 
ATOM   4469 C CA    . ASN A 1 589 ? -19.637 -71.708 14.376  1.00 39.81  ? 587 ASN A CA    1 
ATOM   4470 C C     . ASN A 1 589 ? -18.945 -71.084 15.597  1.00 35.30  ? 587 ASN A C     1 
ATOM   4471 O O     . ASN A 1 589 ? -19.598 -70.303 16.277  1.00 37.04  ? 587 ASN A O     1 
ATOM   4472 C CB    . ASN A 1 589 ? -20.339 -73.041 14.652  1.00 42.11  ? 587 ASN A CB    1 
ATOM   4473 C CG    . ASN A 1 589 ? -21.340 -73.408 13.578  1.00 47.47  ? 587 ASN A CG    1 
ATOM   4474 O OD1   . ASN A 1 589 ? -21.890 -72.538 12.909  1.00 55.85  ? 587 ASN A OD1   1 
ATOM   4475 N ND2   . ASN A 1 589 ? -21.584 -74.695 13.406  1.00 51.22  ? 587 ASN A ND2   1 
ATOM   4476 N N     . ASN A 1 590 ? -17.677 -71.399 15.832  1.00 31.43  ? 588 ASN A N     1 
ATOM   4477 C CA    . ASN A 1 590 ? -16.917 -70.789 16.955  1.00 31.84  ? 588 ASN A CA    1 
ATOM   4478 C C     . ASN A 1 590 ? -16.790 -69.271 16.747  1.00 29.47  ? 588 ASN A C     1 
ATOM   4479 O O     . ASN A 1 590 ? -16.387 -68.591 17.687  1.00 30.31  ? 588 ASN A O     1 
ATOM   4480 C CB    . ASN A 1 590 ? -15.578 -71.497 17.179  1.00 30.61  ? 588 ASN A CB    1 
ATOM   4481 C CG    . ASN A 1 590 ? -14.588 -71.358 16.046  1.00 36.27  ? 588 ASN A CG    1 
ATOM   4482 O OD1   . ASN A 1 590 ? -14.645 -70.412 15.269  1.00 33.83  ? 588 ASN A OD1   1 
ATOM   4483 N ND2   . ASN A 1 590 ? -13.662 -72.295 15.959  1.00 39.87  ? 588 ASN A ND2   1 
ATOM   4484 N N     . LEU A 1 591 ? -17.166 -68.752 15.585  1.00 28.47  ? 589 LEU A N     1 
ATOM   4485 C CA    . LEU A 1 591 ? -17.125 -67.284 15.350  1.00 29.85  ? 589 LEU A CA    1 
ATOM   4486 C C     . LEU A 1 591 ? -18.529 -66.687 15.221  1.00 29.33  ? 589 LEU A C     1 
ATOM   4487 O O     . LEU A 1 591 ? -18.687 -65.524 15.581  1.00 33.37  ? 589 LEU A O     1 
ATOM   4488 C CB    . LEU A 1 591 ? -16.342 -66.999 14.065  1.00 25.89  ? 589 LEU A CB    1 
ATOM   4489 C CG    . LEU A 1 591 ? -14.889 -67.459 14.016  1.00 28.71  ? 589 LEU A CG    1 
ATOM   4490 C CD1   . LEU A 1 591 ? -14.319 -67.231 12.626  1.00 32.48  ? 589 LEU A CD1   1 
ATOM   4491 C CD2   . LEU A 1 591 ? -14.057 -66.724 15.048  1.00 28.56  ? 589 LEU A CD2   1 
ATOM   4492 N N     . MET A 1 592 ? -19.505 -67.453 14.750  1.00 29.79  ? 590 MET A N     1 
ATOM   4493 C CA    . MET A 1 592 ? -20.831 -66.870 14.428  1.00 31.07  ? 590 MET A CA    1 
ATOM   4494 C C     . MET A 1 592 ? -21.895 -67.149 15.488  1.00 34.95  ? 590 MET A C     1 
ATOM   4495 O O     . MET A 1 592 ? -22.947 -66.504 15.421  1.00 39.20  ? 590 MET A O     1 
ATOM   4496 C CB    . MET A 1 592 ? -21.312 -67.436 13.091  1.00 31.82  ? 590 MET A CB    1 
ATOM   4497 C CG    . MET A 1 592 ? -20.264 -67.412 11.994  1.00 34.60  ? 590 MET A CG    1 
ATOM   4498 S SD    . MET A 1 592 ? -19.622 -65.762 11.637  1.00 34.80  ? 590 MET A SD    1 
ATOM   4499 C CE    . MET A 1 592 ? -21.140 -64.859 11.352  1.00 32.71  ? 590 MET A CE    1 
ATOM   4500 N N     . GLU A 1 593 ? -21.633 -68.040 16.436  1.00 37.61  ? 591 GLU A N     1 
ATOM   4501 C CA    . GLU A 1 593 ? -22.677 -68.450 17.409  1.00 42.54  ? 591 GLU A CA    1 
ATOM   4502 C C     . GLU A 1 593 ? -23.029 -67.314 18.376  1.00 39.81  ? 591 GLU A C     1 
ATOM   4503 O O     . GLU A 1 593 ? -24.200 -67.200 18.734  1.00 42.76  ? 591 GLU A O     1 
ATOM   4504 C CB    . GLU A 1 593 ? -22.206 -69.703 18.139  1.00 52.56  ? 591 GLU A CB    1 
ATOM   4505 C CG    . GLU A 1 593 ? -23.299 -70.418 18.902  1.00 62.68  ? 591 GLU A CG    1 
ATOM   4506 C CD    . GLU A 1 593 ? -22.765 -71.414 19.913  1.00 74.38  ? 591 GLU A CD    1 
ATOM   4507 O OE1   . GLU A 1 593 ? -23.344 -71.510 21.011  1.00 82.89  ? 591 GLU A OE1   1 
ATOM   4508 O OE2   . GLU A 1 593 ? -21.766 -72.085 19.600  1.00 79.56  ? 591 GLU A OE2   1 
ATOM   4509 N N     . MET A 1 594 ? -22.053 -66.515 18.781  1.00 39.34  ? 592 MET A N     1 
ATOM   4510 C CA    . MET A 1 594 ? -22.318 -65.454 19.779  1.00 38.46  ? 592 MET A CA    1 
ATOM   4511 C C     . MET A 1 594 ? -23.205 -64.374 19.159  1.00 38.82  ? 592 MET A C     1 
ATOM   4512 O O     . MET A 1 594 ? -22.808 -63.794 18.155  1.00 35.88  ? 592 MET A O     1 
ATOM   4513 C CB    . MET A 1 594 ? -21.023 -64.826 20.298  1.00 38.97  ? 592 MET A CB    1 
ATOM   4514 C CG    . MET A 1 594 ? -21.253 -63.824 21.404  1.00 39.75  ? 592 MET A CG    1 
ATOM   4515 S SD    . MET A 1 594 ? -19.707 -63.210 22.082  1.00 43.36  ? 592 MET A SD    1 
ATOM   4516 C CE    . MET A 1 594 ? -19.071 -64.700 22.845  1.00 42.67  ? 592 MET A CE    1 
ATOM   4517 N N     . ALA A 1 595 ? -24.359 -64.123 19.772  1.00 34.74  ? 593 ALA A N     1 
ATOM   4518 C CA    . ALA A 1 595 ? -25.268 -63.066 19.270  1.00 34.97  ? 593 ALA A CA    1 
ATOM   4519 C C     . ALA A 1 595 ? -24.566 -61.716 19.403  1.00 37.13  ? 593 ALA A C     1 
ATOM   4520 O O     . ALA A 1 595 ? -23.736 -61.530 20.327  1.00 39.44  ? 593 ALA A O     1 
ATOM   4521 C CB    . ALA A 1 595 ? -26.578 -63.060 20.021  1.00 36.31  ? 593 ALA A CB    1 
ATOM   4522 N N     . GLU A 1 596 ? -24.869 -60.768 18.529  1.00 38.49  ? 594 GLU A N     1 
ATOM   4523 C CA    . GLU A 1 596 ? -24.119 -59.484 18.528  1.00 40.46  ? 594 GLU A CA    1 
ATOM   4524 C C     . GLU A 1 596 ? -24.317 -58.733 19.850  1.00 39.48  ? 594 GLU A C     1 
ATOM   4525 O O     . GLU A 1 596 ? -23.391 -58.027 20.251  1.00 34.86  ? 594 GLU A O     1 
ATOM   4526 C CB    . GLU A 1 596 ? -24.502 -58.687 17.278  1.00 42.28  ? 594 GLU A CB    1 
ATOM   4527 C CG    . GLU A 1 596 ? -25.453 -57.535 17.515  1.00 53.48  ? 594 GLU A CG    1 
ATOM   4528 C CD    . GLU A 1 596 ? -25.568 -56.594 16.328  1.00 56.07  ? 594 GLU A CD    1 
ATOM   4529 O OE1   . GLU A 1 596 ? -25.305 -55.393 16.499  1.00 50.97  ? 594 GLU A OE1   1 
ATOM   4530 O OE2   . GLU A 1 596 ? -25.916 -57.068 15.233  1.00 55.15  ? 594 GLU A OE2   1 
ATOM   4531 N N     . GLU A 1 597 ? -25.451 -58.928 20.515  1.00 38.62  ? 595 GLU A N     1 
ATOM   4532 C CA    . GLU A 1 597 ? -25.770 -58.151 21.740  1.00 41.48  ? 595 GLU A CA    1 
ATOM   4533 C C     . GLU A 1 597 ? -25.159 -58.800 22.980  1.00 41.54  ? 595 GLU A C     1 
ATOM   4534 O O     . GLU A 1 597 ? -25.372 -58.269 24.066  1.00 43.02  ? 595 GLU A O     1 
ATOM   4535 C CB    . GLU A 1 597 ? -27.285 -58.047 21.890  1.00 40.66  ? 595 GLU A CB    1 
ATOM   4536 C CG    . GLU A 1 597 ? -27.965 -59.390 22.043  1.00 40.75  ? 595 GLU A CG    1 
ATOM   4537 C CD    . GLU A 1 597 ? -28.456 -59.999 20.744  1.00 48.10  ? 595 GLU A CD    1 
ATOM   4538 O OE1   . GLU A 1 597 ? -27.954 -59.604 19.677  1.00 43.34  ? 595 GLU A OE1   1 
ATOM   4539 O OE2   . GLU A 1 597 ? -29.339 -60.870 20.809  1.00 59.08  ? 595 GLU A OE2   1 
ATOM   4540 N N     . ASP A 1 598 ? -24.405 -59.883 22.813  1.00 37.97  ? 596 ASP A N     1 
ATOM   4541 C CA    . ASP A 1 598 ? -23.881 -60.623 23.986  1.00 35.55  ? 596 ASP A CA    1 
ATOM   4542 C C     . ASP A 1 598 ? -22.357 -60.517 24.053  1.00 34.39  ? 596 ASP A C     1 
ATOM   4543 O O     . ASP A 1 598 ? -21.778 -61.135 24.939  1.00 35.90  ? 596 ASP A O     1 
ATOM   4544 C CB    . ASP A 1 598 ? -24.369 -62.071 23.940  1.00 39.75  ? 596 ASP A CB    1 
ATOM   4545 C CG    . ASP A 1 598 ? -25.875 -62.222 24.032  1.00 38.13  ? 596 ASP A CG    1 
ATOM   4546 O OD1   . ASP A 1 598 ? -26.523 -61.305 24.554  1.00 42.84  ? 596 ASP A OD1   1 
ATOM   4547 O OD2   . ASP A 1 598 ? -26.381 -63.262 23.586  1.00 38.53  ? 596 ASP A OD2   1 
ATOM   4548 N N     . PHE A 1 599 ? -21.751 -59.744 23.161  1.00 32.65  ? 597 PHE A N     1 
ATOM   4549 C CA    . PHE A 1 599 ? -20.274 -59.626 23.096  1.00 33.31  ? 597 PHE A CA    1 
ATOM   4550 C C     . PHE A 1 599 ? -19.735 -58.780 24.251  1.00 33.37  ? 597 PHE A C     1 
ATOM   4551 O O     . PHE A 1 599 ? -18.596 -59.005 24.639  1.00 36.15  ? 597 PHE A O     1 
ATOM   4552 C CB    . PHE A 1 599 ? -19.867 -58.997 21.761  1.00 32.27  ? 597 PHE A CB    1 
ATOM   4553 C CG    . PHE A 1 599 ? -19.586 -59.940 20.621  1.00 31.99  ? 597 PHE A CG    1 
ATOM   4554 C CD1   . PHE A 1 599 ? -20.615 -60.436 19.840  1.00 34.26  ? 597 PHE A CD1   1 
ATOM   4555 C CD2   . PHE A 1 599 ? -18.288 -60.300 20.305  1.00 33.85  ? 597 PHE A CD2   1 
ATOM   4556 C CE1   . PHE A 1 599 ? -20.352 -61.293 18.785  1.00 36.94  ? 597 PHE A CE1   1 
ATOM   4557 C CE2   . PHE A 1 599 ? -18.026 -61.156 19.249  1.00 34.90  ? 597 PHE A CE2   1 
ATOM   4558 C CZ    . PHE A 1 599 ? -19.058 -61.652 18.492  1.00 36.99  ? 597 PHE A CZ    1 
ATOM   4559 N N     . ALA A 1 600 ? -20.527 -57.847 24.776  1.00 31.89  ? 598 ALA A N     1 
ATOM   4560 C CA    . ALA A 1 600 ? -20.023 -56.905 25.800  1.00 33.81  ? 598 ALA A CA    1 
ATOM   4561 C C     . ALA A 1 600 ? -20.947 -56.840 27.021  1.00 33.00  ? 598 ALA A C     1 
ATOM   4562 O O     . ALA A 1 600 ? -21.512 -55.779 27.268  1.00 31.84  ? 598 ALA A O     1 
ATOM   4563 C CB    . ALA A 1 600 ? -19.860 -55.552 25.168  1.00 33.33  ? 598 ALA A CB    1 
ATOM   4564 N N     . LEU A 1 601 ? -21.046 -57.931 27.771  1.00 34.22  ? 599 LEU A N     1 
ATOM   4565 C CA    . LEU A 1 601 ? -21.967 -57.997 28.933  1.00 35.24  ? 599 LEU A CA    1 
ATOM   4566 C C     . LEU A 1 601 ? -21.191 -57.834 30.252  1.00 39.61  ? 599 LEU A C     1 
ATOM   4567 O O     . LEU A 1 601 ? -21.819 -58.031 31.325  1.00 45.11  ? 599 LEU A O     1 
ATOM   4568 C CB    . LEU A 1 601 ? -22.710 -59.333 28.892  1.00 35.30  ? 599 LEU A CB    1 
ATOM   4569 C CG    . LEU A 1 601 ? -23.632 -59.526 27.692  1.00 36.99  ? 599 LEU A CG    1 
ATOM   4570 C CD1   . LEU A 1 601 ? -24.263 -60.917 27.687  1.00 36.15  ? 599 LEU A CD1   1 
ATOM   4571 C CD2   . LEU A 1 601 ? -24.715 -58.453 27.667  1.00 37.63  ? 599 LEU A CD2   1 
ATOM   4572 N N     . GLY A 1 602 ? -19.911 -57.447 30.210  1.00 36.60  ? 600 GLY A N     1 
ATOM   4573 C CA    . GLY A 1 602 ? -19.094 -57.234 31.418  1.00 32.80  ? 600 GLY A CA    1 
ATOM   4574 C C     . GLY A 1 602 ? -19.053 -55.786 31.905  1.00 41.96  ? 600 GLY A C     1 
ATOM   4575 O O     . GLY A 1 602 ? -18.082 -55.486 32.618  1.00 50.56  ? 600 GLY A O     1 
ATOM   4576 N N     . TYR A 1 603 ? -20.026 -54.956 31.572  1.00 41.27  ? 601 TYR A N     1 
ATOM   4577 C CA    . TYR A 1 603 ? -19.918 -53.535 31.971  1.00 43.49  ? 601 TYR A CA    1 
ATOM   4578 C C     . TYR A 1 603 ? -21.070 -53.199 32.923  1.00 39.18  ? 601 TYR A C     1 
ATOM   4579 O O     . TYR A 1 603 ? -20.983 -53.670 34.055  1.00 38.41  ? 601 TYR A O     1 
ATOM   4580 C CB    . TYR A 1 603 ? -19.805 -52.675 30.711  1.00 45.79  ? 601 TYR A CB    1 
ATOM   4581 C CG    . TYR A 1 603 ? -18.633 -53.073 29.855  1.00 52.89  ? 601 TYR A CG    1 
ATOM   4582 C CD1   . TYR A 1 603 ? -17.382 -52.515 30.050  1.00 55.07  ? 601 TYR A CD1   1 
ATOM   4583 C CD2   . TYR A 1 603 ? -18.761 -54.053 28.886  1.00 52.95  ? 601 TYR A CD2   1 
ATOM   4584 C CE1   . TYR A 1 603 ? -16.295 -52.898 29.284  1.00 51.46  ? 601 TYR A CE1   1 
ATOM   4585 C CE2   . TYR A 1 603 ? -17.684 -54.450 28.114  1.00 51.71  ? 601 TYR A CE2   1 
ATOM   4586 C CZ    . TYR A 1 603 ? -16.447 -53.869 28.312  1.00 49.99  ? 601 TYR A CZ    1 
ATOM   4587 O OH    . TYR A 1 603 ? -15.390 -54.260 27.548  1.00 47.21  ? 601 TYR A OH    1 
ATOM   4588 N N     . ASP B 1 5   ? -16.275 -43.775 24.710  1.00 49.62  ? 3   ASP B N     1 
ATOM   4589 C CA    . ASP B 1 5   ? -15.978 -43.274 26.096  1.00 53.19  ? 3   ASP B CA    1 
ATOM   4590 C C     . ASP B 1 5   ? -15.734 -44.456 27.037  1.00 44.86  ? 3   ASP B C     1 
ATOM   4591 O O     . ASP B 1 5   ? -16.645 -45.301 27.162  1.00 46.31  ? 3   ASP B O     1 
ATOM   4592 C CB    . ASP B 1 5   ? -17.125 -42.438 26.669  1.00 58.16  ? 3   ASP B CB    1 
ATOM   4593 C CG    . ASP B 1 5   ? -16.844 -40.945 26.653  1.00 65.07  ? 3   ASP B CG    1 
ATOM   4594 O OD1   . ASP B 1 5   ? -15.764 -40.559 26.162  1.00 80.77  ? 3   ASP B OD1   1 
ATOM   4595 O OD2   . ASP B 1 5   ? -17.700 -40.181 27.124  1.00 66.08  ? 3   ASP B OD2   1 
ATOM   4596 N N     . TYR B 1 6   ? -14.587 -44.479 27.714  1.00 37.04  ? 4   TYR B N     1 
ATOM   4597 C CA    . TYR B 1 6   ? -14.203 -45.547 28.675  1.00 38.48  ? 4   TYR B CA    1 
ATOM   4598 C C     . TYR B 1 6   ? -15.363 -45.878 29.621  1.00 39.07  ? 4   TYR B C     1 
ATOM   4599 O O     . TYR B 1 6   ? -15.873 -44.975 30.320  1.00 39.25  ? 4   TYR B O     1 
ATOM   4600 C CB    . TYR B 1 6   ? -12.961 -45.202 29.505  1.00 35.80  ? 4   TYR B CB    1 
ATOM   4601 C CG    . TYR B 1 6   ? -12.628 -46.289 30.499  1.00 33.92  ? 4   TYR B CG    1 
ATOM   4602 C CD1   . TYR B 1 6   ? -12.196 -47.531 30.076  1.00 31.43  ? 4   TYR B CD1   1 
ATOM   4603 C CD2   . TYR B 1 6   ? -12.843 -46.108 31.855  1.00 31.68  ? 4   TYR B CD2   1 
ATOM   4604 C CE1   . TYR B 1 6   ? -11.912 -48.542 30.980  1.00 35.04  ? 4   TYR B CE1   1 
ATOM   4605 C CE2   . TYR B 1 6   ? -12.586 -47.117 32.768  1.00 35.51  ? 4   TYR B CE2   1 
ATOM   4606 C CZ    . TYR B 1 6   ? -12.115 -48.344 32.340  1.00 37.64  ? 4   TYR B CZ    1 
ATOM   4607 O OH    . TYR B 1 6   ? -11.859 -49.335 33.263  1.00 37.28  ? 4   TYR B OH    1 
ATOM   4608 N N     . LYS B 1 7   ? -15.736 -47.159 29.630  1.00 36.33  ? 5   LYS B N     1 
ATOM   4609 C CA    . LYS B 1 7   ? -16.700 -47.768 30.568  1.00 39.88  ? 5   LYS B CA    1 
ATOM   4610 C C     . LYS B 1 7   ? -15.962 -48.899 31.309  1.00 37.35  ? 5   LYS B C     1 
ATOM   4611 O O     . LYS B 1 7   ? -15.396 -49.778 30.658  1.00 37.80  ? 5   LYS B O     1 
ATOM   4612 C CB    . LYS B 1 7   ? -17.952 -48.136 29.762  1.00 47.00  ? 5   LYS B CB    1 
ATOM   4613 C CG    . LYS B 1 7   ? -18.956 -49.069 30.435  1.00 62.65  ? 5   LYS B CG    1 
ATOM   4614 C CD    . LYS B 1 7   ? -20.250 -48.432 30.981  1.00 66.36  ? 5   LYS B CD    1 
ATOM   4615 C CE    . LYS B 1 7   ? -20.243 -48.164 32.478  1.00 67.14  ? 5   LYS B CE    1 
ATOM   4616 N NZ    . LYS B 1 7   ? -20.775 -46.812 32.769  1.00 67.28  ? 5   LYS B NZ    1 
ATOM   4617 N N     . ALA B 1 8   ? -15.913 -48.855 32.645  1.00 37.09  ? 6   ALA B N     1 
ATOM   4618 C CA    . ALA B 1 8   ? -15.222 -49.869 33.472  1.00 32.41  ? 6   ALA B CA    1 
ATOM   4619 C C     . ALA B 1 8   ? -15.916 -51.213 33.327  1.00 30.09  ? 6   ALA B C     1 
ATOM   4620 O O     . ALA B 1 8   ? -17.138 -51.265 33.293  1.00 34.55  ? 6   ALA B O     1 
ATOM   4621 C CB    . ALA B 1 8   ? -15.166 -49.435 34.904  1.00 34.31  ? 6   ALA B CB    1 
ATOM   4622 N N     . PRO B 1 9   ? -15.165 -52.331 33.209  1.00 28.71  ? 7   PRO B N     1 
ATOM   4623 C CA    . PRO B 1 9   ? -15.760 -53.666 33.151  1.00 32.81  ? 7   PRO B CA    1 
ATOM   4624 C C     . PRO B 1 9   ? -16.135 -54.256 34.519  1.00 35.63  ? 7   PRO B C     1 
ATOM   4625 O O     . PRO B 1 9   ? -15.680 -55.326 34.831  1.00 37.06  ? 7   PRO B O     1 
ATOM   4626 C CB    . PRO B 1 9   ? -14.644 -54.512 32.504  1.00 31.48  ? 7   PRO B CB    1 
ATOM   4627 C CG    . PRO B 1 9   ? -13.375 -53.849 32.962  1.00 29.74  ? 7   PRO B CG    1 
ATOM   4628 C CD    . PRO B 1 9   ? -13.703 -52.376 33.095  1.00 27.87  ? 7   PRO B CD    1 
ATOM   4629 N N     . LEU B 1 10  ? -16.989 -53.571 35.279  1.00 41.11  ? 8   LEU B N     1 
ATOM   4630 C CA    . LEU B 1 10  ? -17.313 -53.942 36.680  1.00 42.25  ? 8   LEU B CA    1 
ATOM   4631 C C     . LEU B 1 10  ? -18.002 -55.298 36.728  1.00 43.40  ? 8   LEU B C     1 
ATOM   4632 O O     . LEU B 1 10  ? -17.748 -56.044 37.692  1.00 45.04  ? 8   LEU B O     1 
ATOM   4633 C CB    . LEU B 1 10  ? -18.215 -52.877 37.305  1.00 47.45  ? 8   LEU B CB    1 
ATOM   4634 C CG    . LEU B 1 10  ? -17.466 -51.704 37.925  1.00 50.38  ? 8   LEU B CG    1 
ATOM   4635 C CD1   . LEU B 1 10  ? -18.437 -50.631 38.391  1.00 53.56  ? 8   LEU B CD1   1 
ATOM   4636 C CD2   . LEU B 1 10  ? -16.592 -52.179 39.069  1.00 49.94  ? 8   LEU B CD2   1 
ATOM   4637 N N     . ARG B 1 11  ? -18.872 -55.605 35.770  1.00 42.84  ? 9   ARG B N     1 
ATOM   4638 C CA    . ARG B 1 11  ? -19.609 -56.883 35.847  1.00 41.07  ? 9   ARG B CA    1 
ATOM   4639 C C     . ARG B 1 11  ? -18.564 -57.989 35.664  1.00 42.45  ? 9   ARG B C     1 
ATOM   4640 O O     . ARG B 1 11  ? -18.702 -59.049 36.319  1.00 43.04  ? 9   ARG B O     1 
ATOM   4641 C CB    . ARG B 1 11  ? -20.776 -56.920 34.854  1.00 44.06  ? 9   ARG B CB    1 
ATOM   4642 C CG    . ARG B 1 11  ? -21.573 -58.224 34.847  1.00 45.61  ? 9   ARG B CG    1 
ATOM   4643 C CD    . ARG B 1 11  ? -22.208 -58.594 36.186  1.00 50.66  ? 9   ARG B CD    1 
ATOM   4644 N NE    . ARG B 1 11  ? -22.734 -59.971 36.219  1.00 52.55  ? 9   ARG B NE    1 
ATOM   4645 C CZ    . ARG B 1 11  ? -22.142 -61.047 36.766  1.00 51.96  ? 9   ARG B CZ    1 
ATOM   4646 N NH1   . ARG B 1 11  ? -20.955 -60.968 37.350  1.00 54.90  ? 9   ARG B NH1   1 
ATOM   4647 N NH2   . ARG B 1 11  ? -22.741 -62.221 36.703  1.00 50.10  ? 9   ARG B NH2   1 
ATOM   4648 N N     . ASP B 1 12  ? -17.521 -57.749 34.861  1.00 37.86  ? 10  ASP B N     1 
ATOM   4649 C CA    . ASP B 1 12  ? -16.519 -58.813 34.552  1.00 40.39  ? 10  ASP B CA    1 
ATOM   4650 C C     . ASP B 1 12  ? -15.517 -58.910 35.706  1.00 35.29  ? 10  ASP B C     1 
ATOM   4651 O O     . ASP B 1 12  ? -15.138 -60.028 36.041  1.00 35.65  ? 10  ASP B O     1 
ATOM   4652 C CB    . ASP B 1 12  ? -15.839 -58.675 33.180  1.00 35.71  ? 10  ASP B CB    1 
ATOM   4653 C CG    . ASP B 1 12  ? -15.283 -60.018 32.738  1.00 38.02  ? 10  ASP B CG    1 
ATOM   4654 O OD1   . ASP B 1 12  ? -16.111 -60.898 32.451  1.00 36.39  ? 10  ASP B OD1   1 
ATOM   4655 O OD2   . ASP B 1 12  ? -14.031 -60.215 32.803  1.00 37.56  ? 10  ASP B OD2   1 
ATOM   4656 N N     . ILE B 1 13  ? -15.163 -57.789 36.315  1.00 36.02  ? 11  ILE B N     1 
ATOM   4657 C CA    . ILE B 1 13  ? -14.296 -57.747 37.529  1.00 41.26  ? 11  ILE B CA    1 
ATOM   4658 C C     . ILE B 1 13  ? -14.960 -58.551 38.663  1.00 39.56  ? 11  ILE B C     1 
ATOM   4659 O O     . ILE B 1 13  ? -14.268 -59.343 39.294  1.00 39.14  ? 11  ILE B O     1 
ATOM   4660 C CB    . ILE B 1 13  ? -13.999 -56.280 37.902  1.00 45.10  ? 11  ILE B CB    1 
ATOM   4661 C CG1   . ILE B 1 13  ? -13.047 -55.643 36.881  1.00 44.80  ? 11  ILE B CG1   1 
ATOM   4662 C CG2   . ILE B 1 13  ? -13.459 -56.182 39.317  1.00 46.73  ? 11  ILE B CG2   1 
ATOM   4663 C CD1   . ILE B 1 13  ? -12.998 -54.130 36.907  1.00 47.29  ? 11  ILE B CD1   1 
ATOM   4664 N N     . ARG B 1 14  ? -16.274 -58.419 38.843  1.00 41.54  ? 12  ARG B N     1 
ATOM   4665 C CA    . ARG B 1 14  ? -17.092 -59.169 39.847  1.00 44.45  ? 12  ARG B CA    1 
ATOM   4666 C C     . ARG B 1 14  ? -17.197 -60.663 39.501  1.00 42.48  ? 12  ARG B C     1 
ATOM   4667 O O     . ARG B 1 14  ? -17.069 -61.525 40.412  1.00 36.12  ? 12  ARG B O     1 
ATOM   4668 C CB    . ARG B 1 14  ? -18.513 -58.606 39.909  1.00 46.23  ? 12  ARG B CB    1 
ATOM   4669 C CG    . ARG B 1 14  ? -18.604 -57.239 40.558  1.00 50.06  ? 12  ARG B CG    1 
ATOM   4670 C CD    . ARG B 1 14  ? -20.038 -56.750 40.683  1.00 55.64  ? 12  ARG B CD    1 
ATOM   4671 N NE    . ARG B 1 14  ? -19.931 -55.466 41.358  1.00 58.30  ? 12  ARG B NE    1 
ATOM   4672 C CZ    . ARG B 1 14  ? -20.203 -54.290 40.816  1.00 65.44  ? 12  ARG B CZ    1 
ATOM   4673 N NH1   . ARG B 1 14  ? -20.670 -54.209 39.577  1.00 64.49  ? 12  ARG B NH1   1 
ATOM   4674 N NH2   . ARG B 1 14  ? -20.011 -53.197 41.535  1.00 66.43  ? 12  ARG B NH2   1 
ATOM   4675 N N     . PHE B 1 15  ? -17.451 -60.981 38.234  1.00 42.14  ? 13  PHE B N     1 
ATOM   4676 C CA    . PHE B 1 15  ? -17.435 -62.382 37.767  1.00 41.30  ? 13  PHE B CA    1 
ATOM   4677 C C     . PHE B 1 15  ? -16.143 -63.022 38.279  1.00 45.21  ? 13  PHE B C     1 
ATOM   4678 O O     . PHE B 1 15  ? -16.227 -64.044 38.996  1.00 44.98  ? 13  PHE B O     1 
ATOM   4679 C CB    . PHE B 1 15  ? -17.543 -62.489 36.245  1.00 41.59  ? 13  PHE B CB    1 
ATOM   4680 C CG    . PHE B 1 15  ? -17.389 -63.908 35.766  1.00 36.15  ? 13  PHE B CG    1 
ATOM   4681 C CD1   . PHE B 1 15  ? -18.342 -64.855 36.081  1.00 36.22  ? 13  PHE B CD1   1 
ATOM   4682 C CD2   . PHE B 1 15  ? -16.250 -64.310 35.087  1.00 35.88  ? 13  PHE B CD2   1 
ATOM   4683 C CE1   . PHE B 1 15  ? -18.194 -66.172 35.668  1.00 42.56  ? 13  PHE B CE1   1 
ATOM   4684 C CE2   . PHE B 1 15  ? -16.095 -65.625 34.687  1.00 37.60  ? 13  PHE B CE2   1 
ATOM   4685 C CZ    . PHE B 1 15  ? -17.070 -66.555 34.972  1.00 40.96  ? 13  PHE B CZ    1 
ATOM   4686 N N     . VAL B 1 16  ? -15.001 -62.398 37.966  1.00 41.00  ? 14  VAL B N     1 
ATOM   4687 C CA    . VAL B 1 16  ? -13.647 -62.988 38.190  1.00 41.90  ? 14  VAL B CA    1 
ATOM   4688 C C     . VAL B 1 16  ? -13.359 -63.063 39.695  1.00 37.74  ? 14  VAL B C     1 
ATOM   4689 O O     . VAL B 1 16  ? -12.998 -64.153 40.183  1.00 40.62  ? 14  VAL B O     1 
ATOM   4690 C CB    . VAL B 1 16  ? -12.571 -62.184 37.439  1.00 39.81  ? 14  VAL B CB    1 
ATOM   4691 C CG1   . VAL B 1 16  ? -11.174 -62.563 37.898  1.00 43.03  ? 14  VAL B CG1   1 
ATOM   4692 C CG2   . VAL B 1 16  ? -12.708 -62.361 35.940  1.00 38.94  ? 14  VAL B CG2   1 
ATOM   4693 N N     . ARG B 1 17  ? -13.531 -61.955 40.405  1.00 40.25  ? 15  ARG B N     1 
ATOM   4694 C CA    . ARG B 1 17  ? -13.223 -61.857 41.862  1.00 41.56  ? 15  ARG B CA    1 
ATOM   4695 C C     . ARG B 1 17  ? -14.193 -62.722 42.664  1.00 42.02  ? 15  ARG B C     1 
ATOM   4696 O O     . ARG B 1 17  ? -13.758 -63.707 43.302  1.00 45.58  ? 15  ARG B O     1 
ATOM   4697 C CB    . ARG B 1 17  ? -13.284 -60.402 42.308  1.00 39.60  ? 15  ARG B CB    1 
ATOM   4698 C CG    . ARG B 1 17  ? -12.105 -59.593 41.793  1.00 41.56  ? 15  ARG B CG    1 
ATOM   4699 C CD    . ARG B 1 17  ? -12.137 -58.126 42.136  1.00 44.68  ? 15  ARG B CD    1 
ATOM   4700 N NE    . ARG B 1 17  ? -11.125 -57.717 43.106  1.00 52.48  ? 15  ARG B NE    1 
ATOM   4701 C CZ    . ARG B 1 17  ? -11.332 -57.578 44.407  1.00 61.29  ? 15  ARG B CZ    1 
ATOM   4702 N NH1   . ARG B 1 17  ? -12.503 -57.869 44.951  1.00 76.80  ? 15  ARG B NH1   1 
ATOM   4703 N NH2   . ARG B 1 17  ? -10.353 -57.162 45.179  1.00 64.12  ? 15  ARG B NH2   1 
ATOM   4704 N N     . ASP B 1 18  ? -15.482 -62.425 42.555  1.00 44.35  ? 16  ASP B N     1 
ATOM   4705 C CA    . ASP B 1 18  ? -16.519 -62.980 43.464  1.00 37.83  ? 16  ASP B CA    1 
ATOM   4706 C C     . ASP B 1 18  ? -16.812 -64.425 43.072  1.00 37.87  ? 16  ASP B C     1 
ATOM   4707 O O     . ASP B 1 18  ? -16.724 -65.270 43.950  1.00 43.99  ? 16  ASP B O     1 
ATOM   4708 C CB    . ASP B 1 18  ? -17.762 -62.098 43.498  1.00 32.80  ? 16  ASP B CB    1 
ATOM   4709 C CG    . ASP B 1 18  ? -17.429 -60.639 43.762  1.00 39.63  ? 16  ASP B CG    1 
ATOM   4710 O OD1   . ASP B 1 18  ? -16.371 -60.340 44.439  1.00 40.27  ? 16  ASP B OD1   1 
ATOM   4711 O OD2   . ASP B 1 18  ? -18.206 -59.799 43.279  1.00 42.34  ? 16  ASP B OD2   1 
ATOM   4712 N N     . GLU B 1 19  ? -17.078 -64.708 41.805  1.00 37.80  ? 17  GLU B N     1 
ATOM   4713 C CA    . GLU B 1 19  ? -17.664 -66.018 41.401  1.00 39.68  ? 17  GLU B CA    1 
ATOM   4714 C C     . GLU B 1 19  ? -16.549 -67.016 41.097  1.00 39.56  ? 17  GLU B C     1 
ATOM   4715 O O     . GLU B 1 19  ? -16.665 -68.165 41.561  1.00 43.58  ? 17  GLU B O     1 
ATOM   4716 C CB    . GLU B 1 19  ? -18.637 -65.897 40.212  1.00 39.51  ? 17  GLU B CB    1 
ATOM   4717 C CG    . GLU B 1 19  ? -19.632 -64.739 40.350  1.00 40.40  ? 17  GLU B CG    1 
ATOM   4718 C CD    . GLU B 1 19  ? -20.586 -64.564 39.184  1.00 39.82  ? 17  GLU B CD    1 
ATOM   4719 O OE1   . GLU B 1 19  ? -20.936 -63.398 38.903  1.00 42.04  ? 17  GLU B OE1   1 
ATOM   4720 O OE2   . GLU B 1 19  ? -20.969 -65.588 38.547  1.00 44.88  ? 17  GLU B OE2   1 
ATOM   4721 N N     . LEU B 1 20  ? -15.551 -66.636 40.296  1.00 42.06  ? 18  LEU B N     1 
ATOM   4722 C CA    . LEU B 1 20  ? -14.523 -67.611 39.839  1.00 40.19  ? 18  LEU B CA    1 
ATOM   4723 C C     . LEU B 1 20  ? -13.545 -67.862 40.992  1.00 38.53  ? 18  LEU B C     1 
ATOM   4724 O O     . LEU B 1 20  ? -13.266 -69.031 41.215  1.00 42.21  ? 18  LEU B O     1 
ATOM   4725 C CB    . LEU B 1 20  ? -13.793 -67.119 38.591  1.00 40.58  ? 18  LEU B CB    1 
ATOM   4726 C CG    . LEU B 1 20  ? -12.807 -68.108 37.972  1.00 39.71  ? 18  LEU B CG    1 
ATOM   4727 C CD1   . LEU B 1 20  ? -13.525 -69.228 37.256  1.00 40.74  ? 18  LEU B CD1   1 
ATOM   4728 C CD2   . LEU B 1 20  ? -11.871 -67.395 37.019  1.00 41.72  ? 18  LEU B CD2   1 
ATOM   4729 N N     . LEU B 1 21  ? -13.055 -66.836 41.691  1.00 35.22  ? 19  LEU B N     1 
ATOM   4730 C CA    . LEU B 1 21  ? -11.900 -67.009 42.617  1.00 41.78  ? 19  LEU B CA    1 
ATOM   4731 C C     . LEU B 1 21  ? -12.258 -66.799 44.113  1.00 40.95  ? 19  LEU B C     1 
ATOM   4732 O O     . LEU B 1 21  ? -11.318 -66.695 44.905  1.00 43.42  ? 19  LEU B O     1 
ATOM   4733 C CB    . LEU B 1 21  ? -10.794 -66.051 42.163  1.00 44.10  ? 19  LEU B CB    1 
ATOM   4734 C CG    . LEU B 1 21  ? -10.360 -66.173 40.698  1.00 44.87  ? 19  LEU B CG    1 
ATOM   4735 C CD1   . LEU B 1 21  ? -9.335  -65.094 40.369  1.00 43.73  ? 19  LEU B CD1   1 
ATOM   4736 C CD2   . LEU B 1 21  ? -9.831  -67.565 40.366  1.00 38.43  ? 19  LEU B CD2   1 
ATOM   4737 N N     . GLY B 1 22  ? -13.545 -66.775 44.497  1.00 45.14  ? 20  GLY B N     1 
ATOM   4738 C CA    . GLY B 1 22  ? -14.050 -66.791 45.890  1.00 42.77  ? 20  GLY B CA    1 
ATOM   4739 C C     . GLY B 1 22  ? -13.423 -65.709 46.759  1.00 41.66  ? 20  GLY B C     1 
ATOM   4740 O O     . GLY B 1 22  ? -12.870 -66.059 47.822  1.00 46.39  ? 20  GLY B O     1 
ATOM   4741 N N     . TYR B 1 23  ? -13.496 -64.438 46.347  1.00 41.67  ? 21  TYR B N     1 
ATOM   4742 C CA    . TYR B 1 23  ? -12.721 -63.332 46.978  1.00 43.67  ? 21  TYR B CA    1 
ATOM   4743 C C     . TYR B 1 23  ? -13.311 -62.937 48.328  1.00 43.70  ? 21  TYR B C     1 
ATOM   4744 O O     . TYR B 1 23  ? -12.585 -62.265 49.077  1.00 51.64  ? 21  TYR B O     1 
ATOM   4745 C CB    . TYR B 1 23  ? -12.626 -62.075 46.115  1.00 38.00  ? 21  TYR B CB    1 
ATOM   4746 C CG    . TYR B 1 23  ? -11.288 -61.890 45.445  1.00 36.64  ? 21  TYR B CG    1 
ATOM   4747 C CD1   . TYR B 1 23  ? -10.798 -62.826 44.545  1.00 36.11  ? 21  TYR B CD1   1 
ATOM   4748 C CD2   . TYR B 1 23  ? -10.530 -60.759 45.673  1.00 37.30  ? 21  TYR B CD2   1 
ATOM   4749 C CE1   . TYR B 1 23  ? -9.595  -62.630 43.886  1.00 36.48  ? 21  TYR B CE1   1 
ATOM   4750 C CE2   . TYR B 1 23  ? -9.311  -60.554 45.042  1.00 35.36  ? 21  TYR B CE2   1 
ATOM   4751 C CZ    . TYR B 1 23  ? -8.849  -61.493 44.145  1.00 36.81  ? 21  TYR B CZ    1 
ATOM   4752 O OH    . TYR B 1 23  ? -7.673  -61.273 43.511  1.00 36.41  ? 21  TYR B OH    1 
ATOM   4753 N N     . GLU B 1 24  ? -14.583 -63.262 48.579  1.00 51.08  ? 22  GLU B N     1 
ATOM   4754 C CA    . GLU B 1 24  ? -15.243 -63.077 49.902  1.00 49.76  ? 22  GLU B CA    1 
ATOM   4755 C C     . GLU B 1 24  ? -14.617 -64.058 50.902  1.00 41.64  ? 22  GLU B C     1 
ATOM   4756 O O     . GLU B 1 24  ? -14.045 -63.578 51.871  1.00 47.99  ? 22  GLU B O     1 
ATOM   4757 C CB    . GLU B 1 24  ? -16.763 -63.247 49.834  1.00 56.40  ? 22  GLU B CB    1 
ATOM   4758 C CG    . GLU B 1 24  ? -17.431 -62.662 51.066  1.00 63.15  ? 22  GLU B CG    1 
ATOM   4759 C CD    . GLU B 1 24  ? -18.939 -62.756 51.174  1.00 62.28  ? 22  GLU B CD    1 
ATOM   4760 O OE1   . GLU B 1 24  ? -19.444 -62.360 52.219  1.00 62.85  ? 22  GLU B OE1   1 
ATOM   4761 O OE2   . GLU B 1 24  ? -19.594 -63.212 50.234  1.00 54.17  ? 22  GLU B OE2   1 
ATOM   4762 N N     . ALA B 1 25  ? -14.627 -65.361 50.621  1.00 41.18  ? 23  ALA B N     1 
ATOM   4763 C CA    . ALA B 1 25  ? -13.949 -66.399 51.444  1.00 46.23  ? 23  ALA B CA    1 
ATOM   4764 C C     . ALA B 1 25  ? -12.482 -66.006 51.711  1.00 51.68  ? 23  ALA B C     1 
ATOM   4765 O O     . ALA B 1 25  ? -12.120 -65.936 52.896  1.00 62.71  ? 23  ALA B O     1 
ATOM   4766 C CB    . ALA B 1 25  ? -14.044 -67.760 50.789  1.00 40.22  ? 23  ALA B CB    1 
ATOM   4767 N N     . HIS B 1 26  ? -11.687 -65.780 50.651  1.00 50.28  ? 24  HIS B N     1 
ATOM   4768 C CA    . HIS B 1 26  ? -10.263 -65.335 50.659  1.00 44.90  ? 24  HIS B CA    1 
ATOM   4769 C C     . HIS B 1 26  ? -10.061 -64.166 51.643  1.00 47.09  ? 24  HIS B C     1 
ATOM   4770 O O     . HIS B 1 26  ? -9.130  -64.253 52.482  1.00 51.72  ? 24  HIS B O     1 
ATOM   4771 C CB    . HIS B 1 26  ? -9.825  -65.007 49.210  1.00 44.03  ? 24  HIS B CB    1 
ATOM   4772 C CG    . HIS B 1 26  ? -8.607  -64.142 49.065  1.00 42.89  ? 24  HIS B CG    1 
ATOM   4773 N ND1   . HIS B 1 26  ? -7.315  -64.655 49.103  1.00 41.38  ? 24  HIS B ND1   1 
ATOM   4774 C CD2   . HIS B 1 26  ? -8.475  -62.807 48.849  1.00 41.70  ? 24  HIS B CD2   1 
ATOM   4775 C CE1   . HIS B 1 26  ? -6.445  -63.666 48.958  1.00 41.20  ? 24  HIS B CE1   1 
ATOM   4776 N NE2   . HIS B 1 26  ? -7.131  -62.516 48.785  1.00 37.87  ? 24  HIS B NE2   1 
ATOM   4777 N N     . TYR B 1 27  ? -10.874 -63.106 51.555  1.00 47.23  ? 25  TYR B N     1 
ATOM   4778 C CA    . TYR B 1 27  ? -10.821 -61.929 52.465  1.00 51.35  ? 25  TYR B CA    1 
ATOM   4779 C C     . TYR B 1 27  ? -11.191 -62.316 53.909  1.00 50.36  ? 25  TYR B C     1 
ATOM   4780 O O     . TYR B 1 27  ? -10.546 -61.759 54.808  1.00 50.21  ? 25  TYR B O     1 
ATOM   4781 C CB    . TYR B 1 27  ? -11.711 -60.787 51.964  1.00 50.70  ? 25  TYR B CB    1 
ATOM   4782 C CG    . TYR B 1 27  ? -11.111 -59.942 50.869  1.00 56.06  ? 25  TYR B CG    1 
ATOM   4783 C CD1   . TYR B 1 27  ? -9.825  -60.165 50.398  1.00 53.69  ? 25  TYR B CD1   1 
ATOM   4784 C CD2   . TYR B 1 27  ? -11.825 -58.884 50.316  1.00 64.68  ? 25  TYR B CD2   1 
ATOM   4785 C CE1   . TYR B 1 27  ? -9.277  -59.387 49.391  1.00 54.22  ? 25  TYR B CE1   1 
ATOM   4786 C CE2   . TYR B 1 27  ? -11.300 -58.105 49.294  1.00 60.23  ? 25  TYR B CE2   1 
ATOM   4787 C CZ    . TYR B 1 27  ? -10.021 -58.364 48.829  1.00 57.32  ? 25  TYR B CZ    1 
ATOM   4788 O OH    . TYR B 1 27  ? -9.482  -57.610 47.830  1.00 54.97  ? 25  TYR B OH    1 
ATOM   4789 N N     . GLN B 1 28  ? -12.168 -63.215 54.118  1.00 55.46  ? 26  GLN B N     1 
ATOM   4790 C CA    . GLN B 1 28  ? -12.595 -63.721 55.461  1.00 62.00  ? 26  GLN B CA    1 
ATOM   4791 C C     . GLN B 1 28  ? -11.464 -64.521 56.117  1.00 56.41  ? 26  GLN B C     1 
ATOM   4792 O O     . GLN B 1 28  ? -11.379 -64.451 57.337  1.00 61.05  ? 26  GLN B O     1 
ATOM   4793 C CB    . GLN B 1 28  ? -13.836 -64.621 55.404  1.00 65.12  ? 26  GLN B CB    1 
ATOM   4794 C CG    . GLN B 1 28  ? -14.661 -64.582 56.689  1.00 69.35  ? 26  GLN B CG    1 
ATOM   4795 C CD    . GLN B 1 28  ? -15.608 -63.400 56.781  1.00 82.20  ? 26  GLN B CD    1 
ATOM   4796 O OE1   . GLN B 1 28  ? -15.600 -62.618 57.743  1.00 74.72  ? 26  GLN B OE1   1 
ATOM   4797 N NE2   . GLN B 1 28  ? -16.459 -63.261 55.774  1.00 83.27  ? 26  GLN B NE2   1 
ATOM   4798 N N     . SER B 1 29  ? -10.629 -65.211 55.330  1.00 51.32  ? 27  SER B N     1 
ATOM   4799 C CA    . SER B 1 29  ? -9.631  -66.208 55.793  1.00 54.06  ? 27  SER B CA    1 
ATOM   4800 C C     . SER B 1 29  ? -8.312  -65.531 56.172  1.00 56.55  ? 27  SER B C     1 
ATOM   4801 O O     . SER B 1 29  ? -7.335  -66.243 56.384  1.00 63.79  ? 27  SER B O     1 
ATOM   4802 C CB    . SER B 1 29  ? -9.418  -67.303 54.747  1.00 57.49  ? 27  SER B CB    1 
ATOM   4803 O OG    . SER B 1 29  ? -8.517  -66.908 53.714  1.00 60.81  ? 27  SER B OG    1 
ATOM   4804 N N     . LEU B 1 30  ? -8.270  -64.210 56.295  1.00 57.55  ? 28  LEU B N     1 
ATOM   4805 C CA    . LEU B 1 30  ? -7.021  -63.476 56.008  1.00 59.49  ? 28  LEU B CA    1 
ATOM   4806 C C     . LEU B 1 30  ? -6.961  -62.225 56.867  1.00 61.84  ? 28  LEU B C     1 
ATOM   4807 O O     . LEU B 1 30  ? -7.861  -61.391 56.779  1.00 60.87  ? 28  LEU B O     1 
ATOM   4808 C CB    . LEU B 1 30  ? -7.042  -63.191 54.505  1.00 69.37  ? 28  LEU B CB    1 
ATOM   4809 C CG    . LEU B 1 30  ? -5.841  -62.453 53.918  1.00 74.19  ? 28  LEU B CG    1 
ATOM   4810 C CD1   . LEU B 1 30  ? -5.413  -63.092 52.605  1.00 69.00  ? 28  LEU B CD1   1 
ATOM   4811 C CD2   . LEU B 1 30  ? -6.163  -60.976 53.721  1.00 74.27  ? 28  LEU B CD2   1 
ATOM   4812 N N     . PRO B 1 31  ? -5.916  -62.089 57.729  1.00 66.99  ? 29  PRO B N     1 
ATOM   4813 C CA    . PRO B 1 31  ? -5.810  -60.991 58.695  1.00 67.83  ? 29  PRO B CA    1 
ATOM   4814 C C     . PRO B 1 31  ? -5.793  -59.601 58.054  1.00 73.37  ? 29  PRO B C     1 
ATOM   4815 O O     . PRO B 1 31  ? -4.985  -59.392 57.169  1.00 80.18  ? 29  PRO B O     1 
ATOM   4816 C CB    . PRO B 1 31  ? -4.446  -61.175 59.382  1.00 62.80  ? 29  PRO B CB    1 
ATOM   4817 C CG    . PRO B 1 31  ? -4.077  -62.624 59.114  1.00 68.85  ? 29  PRO B CG    1 
ATOM   4818 C CD    . PRO B 1 31  ? -4.771  -63.011 57.823  1.00 66.65  ? 29  PRO B CD    1 
ATOM   4819 N N     . GLY B 1 32  ? -6.646  -58.700 58.545  1.00 74.26  ? 30  GLY B N     1 
ATOM   4820 C CA    . GLY B 1 32  ? -6.770  -57.309 58.068  1.00 79.46  ? 30  GLY B CA    1 
ATOM   4821 C C     . GLY B 1 32  ? -8.093  -57.112 57.353  1.00 87.60  ? 30  GLY B C     1 
ATOM   4822 O O     . GLY B 1 32  ? -8.682  -56.026 57.476  1.00 93.64  ? 30  GLY B O     1 
ATOM   4823 N N     . ALA B 1 33  ? -8.554  -58.145 56.645  1.00 93.87  ? 31  ALA B N     1 
ATOM   4824 C CA    . ALA B 1 33  ? -9.828  -58.164 55.893  1.00 89.64  ? 31  ALA B CA    1 
ATOM   4825 C C     . ALA B 1 33  ? -10.966 -58.577 56.842  1.00 90.39  ? 31  ALA B C     1 
ATOM   4826 O O     . ALA B 1 33  ? -11.416 -59.751 56.813  1.00 77.32  ? 31  ALA B O     1 
ATOM   4827 C CB    . ALA B 1 33  ? -9.684  -59.069 54.692  1.00 88.59  ? 31  ALA B CB    1 
ATOM   4828 N N     . GLU B 1 34  ? -11.334 -57.650 57.730  1.00 92.05  ? 32  GLU B N     1 
ATOM   4829 C CA    . GLU B 1 34  ? -12.643 -57.602 58.436  1.00 85.11  ? 32  GLU B CA    1 
ATOM   4830 C C     . GLU B 1 34  ? -13.366 -56.320 57.992  1.00 79.20  ? 32  GLU B C     1 
ATOM   4831 O O     . GLU B 1 34  ? -14.589 -56.316 58.018  1.00 85.67  ? 32  GLU B O     1 
ATOM   4832 C CB    . GLU B 1 34  ? -12.470 -57.657 59.961  1.00 82.41  ? 32  GLU B CB    1 
ATOM   4833 C CG    . GLU B 1 34  ? -11.672 -58.854 60.467  1.00 85.81  ? 32  GLU B CG    1 
ATOM   4834 C CD    . GLU B 1 34  ? -10.204 -58.598 60.800  1.00 90.49  ? 32  GLU B CD    1 
ATOM   4835 O OE1   . GLU B 1 34  ? -9.835  -57.414 60.899  1.00 93.01  ? 32  GLU B OE1   1 
ATOM   4836 O OE2   . GLU B 1 34  ? -9.424  -59.583 60.959  1.00 79.39  ? 32  GLU B OE2   1 
ATOM   4837 N N     . ASP B 1 35  ? -12.634 -55.281 57.580  1.00 80.20  ? 33  ASP B N     1 
ATOM   4838 C CA    . ASP B 1 35  ? -13.190 -53.984 57.103  1.00 80.12  ? 33  ASP B CA    1 
ATOM   4839 C C     . ASP B 1 35  ? -13.530 -54.069 55.614  1.00 80.20  ? 33  ASP B C     1 
ATOM   4840 O O     . ASP B 1 35  ? -14.239 -53.148 55.125  1.00 85.94  ? 33  ASP B O     1 
ATOM   4841 C CB    . ASP B 1 35  ? -12.202 -52.828 57.256  1.00 83.24  ? 33  ASP B CB    1 
ATOM   4842 C CG    . ASP B 1 35  ? -11.267 -52.992 58.434  1.00 92.55  ? 33  ASP B CG    1 
ATOM   4843 O OD1   . ASP B 1 35  ? -10.776 -54.122 58.628  1.00 96.59  ? 33  ASP B OD1   1 
ATOM   4844 O OD2   . ASP B 1 35  ? -11.042 -51.994 59.145  1.00 92.06  ? 33  ASP B OD2   1 
ATOM   4845 N N     . ALA B 1 36  ? -13.018 -55.100 54.925  1.00 74.01  ? 34  ALA B N     1 
ATOM   4846 C CA    . ALA B 1 36  ? -13.231 -55.371 53.481  1.00 69.71  ? 34  ALA B CA    1 
ATOM   4847 C C     . ALA B 1 36  ? -14.456 -56.280 53.295  1.00 65.54  ? 34  ALA B C     1 
ATOM   4848 O O     . ALA B 1 36  ? -14.337 -57.334 52.612  1.00 68.35  ? 34  ALA B O     1 
ATOM   4849 C CB    . ALA B 1 36  ? -11.991 -55.967 52.855  1.00 69.63  ? 34  ALA B CB    1 
ATOM   4850 N N     . THR B 1 37  ? -15.592 -55.848 53.853  1.00 63.13  ? 35  THR B N     1 
ATOM   4851 C CA    . THR B 1 37  ? -16.958 -56.394 53.626  1.00 66.08  ? 35  THR B CA    1 
ATOM   4852 C C     . THR B 1 37  ? -17.312 -56.306 52.151  1.00 59.53  ? 35  THR B C     1 
ATOM   4853 O O     . THR B 1 37  ? -17.035 -55.307 51.491  1.00 57.80  ? 35  THR B O     1 
ATOM   4854 C CB    . THR B 1 37  ? -18.007 -55.635 54.454  1.00 69.81  ? 35  THR B CB    1 
ATOM   4855 O OG1   . THR B 1 37  ? -18.117 -56.380 55.660  1.00 76.83  ? 35  THR B OG1   1 
ATOM   4856 C CG2   . THR B 1 37  ? -19.387 -55.535 53.845  1.00 69.75  ? 35  THR B CG2   1 
ATOM   4857 N N     . PRO B 1 38  ? -17.971 -57.347 51.614  1.00 55.64  ? 36  PRO B N     1 
ATOM   4858 C CA    . PRO B 1 38  ? -18.540 -57.287 50.267  1.00 56.47  ? 36  PRO B CA    1 
ATOM   4859 C C     . PRO B 1 38  ? -19.147 -55.929 49.856  1.00 60.44  ? 36  PRO B C     1 
ATOM   4860 O O     . PRO B 1 38  ? -18.802 -55.453 48.782  1.00 61.75  ? 36  PRO B O     1 
ATOM   4861 C CB    . PRO B 1 38  ? -19.587 -58.405 50.358  1.00 50.62  ? 36  PRO B CB    1 
ATOM   4862 C CG    . PRO B 1 38  ? -18.887 -59.452 51.199  1.00 50.19  ? 36  PRO B CG    1 
ATOM   4863 C CD    . PRO B 1 38  ? -18.156 -58.657 52.261  1.00 51.13  ? 36  PRO B CD    1 
ATOM   4864 N N     . ASP B 1 39  ? -20.013 -55.328 50.687  1.00 68.53  ? 37  ASP B N     1 
ATOM   4865 C CA    . ASP B 1 39  ? -20.701 -54.039 50.379  1.00 66.24  ? 37  ASP B CA    1 
ATOM   4866 C C     . ASP B 1 39  ? -19.660 -52.909 50.307  1.00 63.64  ? 37  ASP B C     1 
ATOM   4867 O O     . ASP B 1 39  ? -19.836 -52.021 49.452  1.00 60.54  ? 37  ASP B O     1 
ATOM   4868 C CB    . ASP B 1 39  ? -21.830 -53.707 51.370  1.00 71.27  ? 37  ASP B CB    1 
ATOM   4869 C CG    . ASP B 1 39  ? -23.048 -54.627 51.331  1.00 75.78  ? 37  ASP B CG    1 
ATOM   4870 O OD1   . ASP B 1 39  ? -22.864 -55.851 51.231  1.00 85.01  ? 37  ASP B OD1   1 
ATOM   4871 O OD2   . ASP B 1 39  ? -24.180 -54.118 51.446  1.00 81.39  ? 37  ASP B OD2   1 
ATOM   4872 N N     . MET B 1 40  ? -18.611 -52.936 51.140  1.00 55.53  ? 38  MET B N     1 
ATOM   4873 C CA    . MET B 1 40  ? -17.571 -51.870 51.158  1.00 60.47  ? 38  MET B CA    1 
ATOM   4874 C C     . MET B 1 40  ? -16.691 -51.963 49.894  1.00 58.79  ? 38  MET B C     1 
ATOM   4875 O O     . MET B 1 40  ? -16.415 -50.892 49.285  1.00 47.87  ? 38  MET B O     1 
ATOM   4876 C CB    . MET B 1 40  ? -16.704 -51.952 52.421  1.00 70.32  ? 38  MET B CB    1 
ATOM   4877 C CG    . MET B 1 40  ? -15.824 -50.709 52.682  1.00 78.45  ? 38  MET B CG    1 
ATOM   4878 S SD    . MET B 1 40  ? -16.469 -49.063 52.153  1.00 87.16  ? 38  MET B SD    1 
ATOM   4879 C CE    . MET B 1 40  ? -17.842 -48.769 53.275  1.00 86.48  ? 38  MET B CE    1 
ATOM   4880 N N     . VAL B 1 41  ? -16.293 -53.183 49.508  1.00 52.28  ? 39  VAL B N     1 
ATOM   4881 C CA    . VAL B 1 41  ? -15.537 -53.516 48.261  1.00 52.82  ? 39  VAL B CA    1 
ATOM   4882 C C     . VAL B 1 41  ? -16.304 -52.976 47.042  1.00 55.12  ? 39  VAL B C     1 
ATOM   4883 O O     . VAL B 1 41  ? -15.727 -52.170 46.237  1.00 52.13  ? 39  VAL B O     1 
ATOM   4884 C CB    . VAL B 1 41  ? -15.306 -55.039 48.161  1.00 62.22  ? 39  VAL B CB    1 
ATOM   4885 C CG1   . VAL B 1 41  ? -14.660 -55.452 46.840  1.00 66.14  ? 39  VAL B CG1   1 
ATOM   4886 C CG2   . VAL B 1 41  ? -14.478 -55.563 49.330  1.00 64.25  ? 39  VAL B CG2   1 
ATOM   4887 N N     . ASN B 1 42  ? -17.580 -53.348 46.932  1.00 52.67  ? 40  ASN B N     1 
ATOM   4888 C CA    . ASN B 1 42  ? -18.476 -52.902 45.830  1.00 50.27  ? 40  ASN B CA    1 
ATOM   4889 C C     . ASN B 1 42  ? -18.559 -51.376 45.741  1.00 45.94  ? 40  ASN B C     1 
ATOM   4890 O O     . ASN B 1 42  ? -18.556 -50.870 44.586  1.00 47.77  ? 40  ASN B O     1 
ATOM   4891 C CB    . ASN B 1 42  ? -19.842 -53.578 45.916  1.00 47.66  ? 40  ASN B CB    1 
ATOM   4892 C CG    . ASN B 1 42  ? -19.733 -54.960 45.319  1.00 47.53  ? 40  ASN B CG    1 
ATOM   4893 O OD1   . ASN B 1 42  ? -19.040 -55.147 44.320  1.00 48.81  ? 40  ASN B OD1   1 
ATOM   4894 N ND2   . ASN B 1 42  ? -20.342 -55.942 45.950  1.00 50.22  ? 40  ASN B ND2   1 
ATOM   4895 N N     . ALA B 1 43  ? -18.633 -50.668 46.873  1.00 44.94  ? 41  ALA B N     1 
ATOM   4896 C CA    . ALA B 1 43  ? -18.724 -49.189 46.917  1.00 42.65  ? 41  ALA B CA    1 
ATOM   4897 C C     . ALA B 1 43  ? -17.372 -48.588 46.514  1.00 45.66  ? 41  ALA B C     1 
ATOM   4898 O O     . ALA B 1 43  ? -17.352 -47.506 45.878  1.00 50.97  ? 41  ALA B O     1 
ATOM   4899 C CB    . ALA B 1 43  ? -19.103 -48.751 48.295  1.00 42.53  ? 41  ALA B CB    1 
ATOM   4900 N N     . ILE B 1 44  ? -16.273 -49.251 46.886  1.00 43.10  ? 42  ILE B N     1 
ATOM   4901 C CA    . ILE B 1 44  ? -14.905 -48.798 46.513  1.00 46.23  ? 42  ILE B CA    1 
ATOM   4902 C C     . ILE B 1 44  ? -14.693 -49.055 45.012  1.00 41.90  ? 42  ILE B C     1 
ATOM   4903 O O     . ILE B 1 44  ? -14.218 -48.137 44.342  1.00 37.92  ? 42  ILE B O     1 
ATOM   4904 C CB    . ILE B 1 44  ? -13.822 -49.428 47.412  1.00 45.32  ? 42  ILE B CB    1 
ATOM   4905 C CG1   . ILE B 1 44  ? -13.940 -48.917 48.848  1.00 44.42  ? 42  ILE B CG1   1 
ATOM   4906 C CG2   . ILE B 1 44  ? -12.418 -49.168 46.874  1.00 44.63  ? 42  ILE B CG2   1 
ATOM   4907 C CD1   . ILE B 1 44  ? -13.385 -49.883 49.858  1.00 42.33  ? 42  ILE B CD1   1 
ATOM   4908 N N     . LEU B 1 45  ? -15.055 -50.228 44.486  1.00 44.01  ? 43  LEU B N     1 
ATOM   4909 C CA    . LEU B 1 45  ? -15.029 -50.458 43.009  1.00 45.90  ? 43  LEU B CA    1 
ATOM   4910 C C     . LEU B 1 45  ? -15.826 -49.365 42.280  1.00 44.35  ? 43  LEU B C     1 
ATOM   4911 O O     . LEU B 1 45  ? -15.291 -48.799 41.301  1.00 47.11  ? 43  LEU B O     1 
ATOM   4912 C CB    . LEU B 1 45  ? -15.598 -51.843 42.697  1.00 47.54  ? 43  LEU B CB    1 
ATOM   4913 C CG    . LEU B 1 45  ? -14.751 -53.023 43.179  1.00 47.76  ? 43  LEU B CG    1 
ATOM   4914 C CD1   . LEU B 1 45  ? -15.280 -54.337 42.600  1.00 48.81  ? 43  LEU B CD1   1 
ATOM   4915 C CD2   . LEU B 1 45  ? -13.285 -52.819 42.818  1.00 44.07  ? 43  LEU B CD2   1 
ATOM   4916 N N     . GLU B 1 46  ? -17.046 -49.068 42.741  1.00 45.12  ? 44  GLU B N     1 
ATOM   4917 C CA    . GLU B 1 46  ? -18.000 -48.166 42.042  1.00 44.43  ? 44  GLU B CA    1 
ATOM   4918 C C     . GLU B 1 46  ? -17.473 -46.736 42.127  1.00 43.92  ? 44  GLU B C     1 
ATOM   4919 O O     . GLU B 1 46  ? -17.599 -46.011 41.127  1.00 43.41  ? 44  GLU B O     1 
ATOM   4920 C CB    . GLU B 1 46  ? -19.422 -48.324 42.597  1.00 49.93  ? 44  GLU B CB    1 
ATOM   4921 C CG    . GLU B 1 46  ? -20.237 -49.388 41.867  1.00 55.58  ? 44  GLU B CG    1 
ATOM   4922 C CD    . GLU B 1 46  ? -21.367 -50.025 42.662  1.00 69.09  ? 44  GLU B CD    1 
ATOM   4923 O OE1   . GLU B 1 46  ? -21.709 -51.207 42.391  1.00 72.55  ? 44  GLU B OE1   1 
ATOM   4924 O OE2   . GLU B 1 46  ? -21.905 -49.346 43.564  1.00 91.24  ? 44  GLU B OE2   1 
ATOM   4925 N N     . GLU B 1 47  ? -16.881 -46.349 43.258  1.00 46.16  ? 45  GLU B N     1 
ATOM   4926 C CA    . GLU B 1 47  ? -16.185 -45.037 43.429  1.00 48.93  ? 45  GLU B CA    1 
ATOM   4927 C C     . GLU B 1 47  ? -14.997 -44.925 42.470  1.00 42.60  ? 45  GLU B C     1 
ATOM   4928 O O     . GLU B 1 47  ? -14.754 -43.828 41.951  1.00 42.68  ? 45  GLU B O     1 
ATOM   4929 C CB    . GLU B 1 47  ? -15.605 -44.921 44.835  1.00 54.23  ? 45  GLU B CB    1 
ATOM   4930 C CG    . GLU B 1 47  ? -16.490 -44.197 45.802  1.00 67.35  ? 45  GLU B CG    1 
ATOM   4931 C CD    . GLU B 1 47  ? -16.319 -42.703 45.661  1.00 74.99  ? 45  GLU B CD    1 
ATOM   4932 O OE1   . GLU B 1 47  ? -17.040 -42.114 44.803  1.00 74.82  ? 45  GLU B OE1   1 
ATOM   4933 O OE2   . GLU B 1 47  ? -15.438 -42.148 46.379  1.00 72.82  ? 45  GLU B OE2   1 
ATOM   4934 N N     . GLY B 1 48  ? -14.223 -46.011 42.352  1.00 45.61  ? 46  GLY B N     1 
ATOM   4935 C CA    . GLY B 1 48  ? -13.022 -46.111 41.492  1.00 46.71  ? 46  GLY B CA    1 
ATOM   4936 C C     . GLY B 1 48  ? -13.406 -45.931 40.036  1.00 44.00  ? 46  GLY B C     1 
ATOM   4937 O O     . GLY B 1 48  ? -12.838 -45.031 39.383  1.00 43.14  ? 46  GLY B O     1 
ATOM   4938 N N     . ALA B 1 49  ? -14.413 -46.704 39.613  1.00 40.66  ? 47  ALA B N     1 
ATOM   4939 C CA    . ALA B 1 49  ? -15.045 -46.684 38.275  1.00 42.60  ? 47  ALA B CA    1 
ATOM   4940 C C     . ALA B 1 49  ? -15.432 -45.243 37.913  1.00 44.50  ? 47  ALA B C     1 
ATOM   4941 O O     . ALA B 1 49  ? -15.058 -44.769 36.811  1.00 44.09  ? 47  ALA B O     1 
ATOM   4942 C CB    . ALA B 1 49  ? -16.217 -47.636 38.260  1.00 35.14  ? 47  ALA B CB    1 
ATOM   4943 N N     . LYS B 1 50  ? -16.060 -44.520 38.840  1.00 46.10  ? 48  LYS B N     1 
ATOM   4944 C CA    . LYS B 1 50  ? -16.583 -43.156 38.570  1.00 45.98  ? 48  LYS B CA    1 
ATOM   4945 C C     . LYS B 1 50  ? -15.421 -42.188 38.315  1.00 43.01  ? 48  LYS B C     1 
ATOM   4946 O O     . LYS B 1 50  ? -15.446 -41.423 37.313  1.00 39.89  ? 48  LYS B O     1 
ATOM   4947 C CB    . LYS B 1 50  ? -17.445 -42.691 39.742  1.00 51.18  ? 48  LYS B CB    1 
ATOM   4948 C CG    . LYS B 1 50  ? -17.790 -41.212 39.687  1.00 57.06  ? 48  LYS B CG    1 
ATOM   4949 C CD    . LYS B 1 50  ? -18.445 -40.712 40.947  1.00 60.15  ? 48  LYS B CD    1 
ATOM   4950 C CE    . LYS B 1 50  ? -19.086 -39.360 40.742  1.00 58.96  ? 48  LYS B CE    1 
ATOM   4951 N NZ    . LYS B 1 50  ? -20.131 -39.131 41.753  1.00 57.95  ? 48  LYS B NZ    1 
ATOM   4952 N N     . PHE B 1 51  ? -14.413 -42.216 39.179  1.00 40.26  ? 49  PHE B N     1 
ATOM   4953 C CA    . PHE B 1 51  ? -13.201 -41.382 39.004  1.00 40.79  ? 49  PHE B CA    1 
ATOM   4954 C C     . PHE B 1 51  ? -12.536 -41.648 37.633  1.00 44.87  ? 49  PHE B C     1 
ATOM   4955 O O     . PHE B 1 51  ? -12.080 -40.696 36.920  1.00 38.83  ? 49  PHE B O     1 
ATOM   4956 C CB    . PHE B 1 51  ? -12.217 -41.679 40.123  1.00 40.18  ? 49  PHE B CB    1 
ATOM   4957 C CG    . PHE B 1 51  ? -10.976 -40.845 40.010  1.00 41.74  ? 49  PHE B CG    1 
ATOM   4958 C CD1   . PHE B 1 51  ? -10.964 -39.539 40.479  1.00 40.53  ? 49  PHE B CD1   1 
ATOM   4959 C CD2   . PHE B 1 51  ? -9.839  -41.362 39.408  1.00 38.90  ? 49  PHE B CD2   1 
ATOM   4960 C CE1   . PHE B 1 51  ? -9.824  -38.760 40.354  1.00 45.57  ? 49  PHE B CE1   1 
ATOM   4961 C CE2   . PHE B 1 51  ? -8.708  -40.569 39.270  1.00 43.95  ? 49  PHE B CE2   1 
ATOM   4962 C CZ    . PHE B 1 51  ? -8.700  -39.272 39.743  1.00 44.36  ? 49  PHE B CZ    1 
ATOM   4963 N N     . CYS B 1 52  ? -12.407 -42.927 37.294  1.00 38.98  ? 50  CYS B N     1 
ATOM   4964 C CA    . CYS B 1 52  ? -11.744 -43.400 36.060  1.00 40.09  ? 50  CYS B CA    1 
ATOM   4965 C C     . CYS B 1 52  ? -12.538 -42.898 34.849  1.00 38.73  ? 50  CYS B C     1 
ATOM   4966 O O     . CYS B 1 52  ? -11.916 -42.268 33.964  1.00 42.04  ? 50  CYS B O     1 
ATOM   4967 C CB    . CYS B 1 52  ? -11.584 -44.919 36.101  1.00 41.27  ? 50  CYS B CB    1 
ATOM   4968 S SG    . CYS B 1 52  ? -10.286 -45.428 37.254  1.00 37.92  ? 50  CYS B SG    1 
ATOM   4969 N N     . GLU B 1 53  ? -13.861 -43.104 34.841  1.00 39.13  ? 51  GLU B N     1 
ATOM   4970 C CA    . GLU B 1 53  ? -14.772 -42.710 33.722  1.00 38.49  ? 51  GLU B CA    1 
ATOM   4971 C C     . GLU B 1 53  ? -14.897 -41.183 33.612  1.00 37.61  ? 51  GLU B C     1 
ATOM   4972 O O     . GLU B 1 53  ? -14.850 -40.686 32.513  1.00 36.46  ? 51  GLU B O     1 
ATOM   4973 C CB    . GLU B 1 53  ? -16.146 -43.360 33.909  1.00 39.67  ? 51  GLU B CB    1 
ATOM   4974 C CG    . GLU B 1 53  ? -16.104 -44.890 33.854  1.00 41.11  ? 51  GLU B CG    1 
ATOM   4975 C CD    . GLU B 1 53  ? -17.389 -45.599 34.256  1.00 42.39  ? 51  GLU B CD    1 
ATOM   4976 O OE1   . GLU B 1 53  ? -17.464 -46.863 34.208  1.00 41.23  ? 51  GLU B OE1   1 
ATOM   4977 O OE2   . GLU B 1 53  ? -18.337 -44.878 34.575  1.00 47.37  ? 51  GLU B OE2   1 
ATOM   4978 N N     . GLN B 1 54  ? -14.983 -40.435 34.714  1.00 42.58  ? 52  GLN B N     1 
ATOM   4979 C CA    . GLN B 1 54  ? -15.427 -39.007 34.694  1.00 40.41  ? 52  GLN B CA    1 
ATOM   4980 C C     . GLN B 1 54  ? -14.241 -38.047 34.757  1.00 38.35  ? 52  GLN B C     1 
ATOM   4981 O O     . GLN B 1 54  ? -14.349 -36.967 34.171  1.00 38.62  ? 52  GLN B O     1 
ATOM   4982 C CB    . GLN B 1 54  ? -16.383 -38.732 35.857  1.00 44.07  ? 52  GLN B CB    1 
ATOM   4983 C CG    . GLN B 1 54  ? -17.819 -39.116 35.540  1.00 50.21  ? 52  GLN B CG    1 
ATOM   4984 C CD    . GLN B 1 54  ? -18.676 -39.422 36.748  1.00 57.34  ? 52  GLN B CD    1 
ATOM   4985 O OE1   . GLN B 1 54  ? -18.751 -38.669 37.719  1.00 60.14  ? 52  GLN B OE1   1 
ATOM   4986 N NE2   . GLN B 1 54  ? -19.350 -40.557 36.689  1.00 56.55  ? 52  GLN B NE2   1 
ATOM   4987 N N     . VAL B 1 55  ? -13.149 -38.412 35.434  1.00 38.37  ? 53  VAL B N     1 
ATOM   4988 C CA    . VAL B 1 55  ? -12.011 -37.481 35.695  1.00 34.30  ? 53  VAL B CA    1 
ATOM   4989 C C     . VAL B 1 55  ? -10.826 -37.805 34.772  1.00 34.18  ? 53  VAL B C     1 
ATOM   4990 O O     . VAL B 1 55  ? -10.341 -36.854 34.169  1.00 45.37  ? 53  VAL B O     1 
ATOM   4991 C CB    . VAL B 1 55  ? -11.593 -37.465 37.183  1.00 35.69  ? 53  VAL B CB    1 
ATOM   4992 C CG1   . VAL B 1 55  ? -10.552 -36.388 37.441  1.00 35.73  ? 53  VAL B CG1   1 
ATOM   4993 C CG2   . VAL B 1 55  ? -12.774 -37.289 38.146  1.00 36.09  ? 53  VAL B CG2   1 
ATOM   4994 N N     . ILE B 1 56  ? -10.292 -39.039 34.705  1.00 35.65  ? 54  ILE B N     1 
ATOM   4995 C CA    . ILE B 1 56  ? -8.970  -39.268 34.024  1.00 33.70  ? 54  ILE B CA    1 
ATOM   4996 C C     . ILE B 1 56  ? -9.137  -39.756 32.581  1.00 32.50  ? 54  ILE B C     1 
ATOM   4997 O O     . ILE B 1 56  ? -8.270  -39.385 31.754  1.00 31.07  ? 54  ILE B O     1 
ATOM   4998 C CB    . ILE B 1 56  ? -7.998  -40.181 34.801  1.00 34.00  ? 54  ILE B CB    1 
ATOM   4999 C CG1   . ILE B 1 56  ? -8.615  -41.529 35.189  1.00 31.42  ? 54  ILE B CG1   1 
ATOM   5000 C CG2   . ILE B 1 56  ? -7.424  -39.414 35.992  1.00 34.87  ? 54  ILE B CG2   1 
ATOM   5001 C CD1   . ILE B 1 56  ? -7.596  -42.510 35.754  1.00 32.12  ? 54  ILE B CD1   1 
ATOM   5002 N N     . ALA B 1 57  ? -10.170 -40.550 32.286  1.00 35.97  ? 55  ALA B N     1 
ATOM   5003 C CA    . ALA B 1 57  ? -10.478 -41.052 30.924  1.00 35.52  ? 55  ALA B CA    1 
ATOM   5004 C C     . ALA B 1 57  ? -10.584 -39.892 29.936  1.00 33.51  ? 55  ALA B C     1 
ATOM   5005 O O     . ALA B 1 57  ? -9.947  -39.941 28.884  1.00 31.32  ? 55  ALA B O     1 
ATOM   5006 C CB    . ALA B 1 57  ? -11.714 -41.922 30.925  1.00 39.09  ? 55  ALA B CB    1 
ATOM   5007 N N     . PRO B 1 58  ? -11.322 -38.794 30.232  1.00 35.45  ? 56  PRO B N     1 
ATOM   5008 C CA    . PRO B 1 58  ? -11.395 -37.643 29.321  1.00 33.85  ? 56  PRO B CA    1 
ATOM   5009 C C     . PRO B 1 58  ? -10.086 -36.878 29.103  1.00 37.27  ? 56  PRO B C     1 
ATOM   5010 O O     . PRO B 1 58  ? -10.013 -36.105 28.178  1.00 44.03  ? 56  PRO B O     1 
ATOM   5011 C CB    . PRO B 1 58  ? -12.421 -36.704 29.963  1.00 35.65  ? 56  PRO B CB    1 
ATOM   5012 C CG    . PRO B 1 58  ? -13.210 -37.604 30.891  1.00 37.70  ? 56  PRO B CG    1 
ATOM   5013 C CD    . PRO B 1 58  ? -12.208 -38.634 31.393  1.00 36.90  ? 56  PRO B CD    1 
ATOM   5014 N N     . LEU B 1 59  ? -9.064  -37.153 29.912  1.00 42.62  ? 57  LEU B N     1 
ATOM   5015 C CA    . LEU B 1 59  ? -7.723  -36.521 29.794  1.00 39.44  ? 57  LEU B CA    1 
ATOM   5016 C C     . LEU B 1 59  ? -6.808  -37.396 28.941  1.00 35.05  ? 57  LEU B C     1 
ATOM   5017 O O     . LEU B 1 59  ? -5.669  -36.960 28.620  1.00 31.38  ? 57  LEU B O     1 
ATOM   5018 C CB    . LEU B 1 59  ? -7.143  -36.321 31.196  1.00 40.15  ? 57  LEU B CB    1 
ATOM   5019 C CG    . LEU B 1 59  ? -8.001  -35.479 32.141  1.00 43.61  ? 57  LEU B CG    1 
ATOM   5020 C CD1   . LEU B 1 59  ? -7.297  -35.311 33.480  1.00 43.51  ? 57  LEU B CD1   1 
ATOM   5021 C CD2   . LEU B 1 59  ? -8.332  -34.126 31.521  1.00 42.21  ? 57  LEU B CD2   1 
ATOM   5022 N N     . ASN B 1 60  ? -7.255  -38.592 28.578  1.00 34.30  ? 58  ASN B N     1 
ATOM   5023 C CA    . ASN B 1 60  ? -6.353  -39.543 27.873  1.00 38.34  ? 58  ASN B CA    1 
ATOM   5024 C C     . ASN B 1 60  ? -5.872  -38.970 26.520  1.00 36.29  ? 58  ASN B C     1 
ATOM   5025 O O     . ASN B 1 60  ? -4.632  -39.023 26.271  1.00 30.30  ? 58  ASN B O     1 
ATOM   5026 C CB    . ASN B 1 60  ? -6.974  -40.924 27.691  1.00 37.69  ? 58  ASN B CB    1 
ATOM   5027 C CG    . ASN B 1 60  ? -5.890  -41.942 27.393  1.00 41.58  ? 58  ASN B CG    1 
ATOM   5028 O OD1   . ASN B 1 60  ? -4.725  -41.766 27.763  1.00 39.98  ? 58  ASN B OD1   1 
ATOM   5029 N ND2   . ASN B 1 60  ? -6.259  -43.005 26.721  1.00 39.30  ? 58  ASN B ND2   1 
ATOM   5030 N N     . ARG B 1 61  ? -6.783  -38.423 25.703  1.00 36.12  ? 59  ARG B N     1 
ATOM   5031 C CA    . ARG B 1 61  ? -6.455  -37.791 24.386  1.00 41.84  ? 59  ARG B CA    1 
ATOM   5032 C C     . ARG B 1 61  ? -5.609  -36.529 24.625  1.00 39.68  ? 59  ARG B C     1 
ATOM   5033 O O     . ARG B 1 61  ? -4.562  -36.371 23.906  1.00 36.15  ? 59  ARG B O     1 
ATOM   5034 C CB    . ARG B 1 61  ? -7.722  -37.481 23.571  1.00 44.20  ? 59  ARG B CB    1 
ATOM   5035 C CG    . ARG B 1 61  ? -8.478  -38.708 23.074  1.00 51.86  ? 59  ARG B CG    1 
ATOM   5036 C CD    . ARG B 1 61  ? -8.217  -39.125 21.621  1.00 58.92  ? 59  ARG B CD    1 
ATOM   5037 N NE    . ARG B 1 61  ? -6.811  -39.462 21.363  1.00 64.95  ? 59  ARG B NE    1 
ATOM   5038 C CZ    . ARG B 1 61  ? -5.944  -38.731 20.643  1.00 62.30  ? 59  ARG B CZ    1 
ATOM   5039 N NH1   . ARG B 1 61  ? -4.691  -39.133 20.504  1.00 56.85  ? 59  ARG B NH1   1 
ATOM   5040 N NH2   . ARG B 1 61  ? -6.317  -37.598 20.075  1.00 66.55  ? 59  ARG B NH2   1 
ATOM   5041 N N     . VAL B 1 62  ? -5.995  -35.696 25.609  1.00 40.22  ? 60  VAL B N     1 
ATOM   5042 C CA    . VAL B 1 62  ? -5.240  -34.454 26.008  1.00 40.29  ? 60  VAL B CA    1 
ATOM   5043 C C     . VAL B 1 62  ? -3.789  -34.845 26.253  1.00 33.63  ? 60  VAL B C     1 
ATOM   5044 O O     . VAL B 1 62  ? -2.902  -34.284 25.643  1.00 34.27  ? 60  VAL B O     1 
ATOM   5045 C CB    . VAL B 1 62  ? -5.780  -33.753 27.273  1.00 41.93  ? 60  VAL B CB    1 
ATOM   5046 C CG1   . VAL B 1 62  ? -5.128  -32.390 27.417  1.00 41.48  ? 60  VAL B CG1   1 
ATOM   5047 C CG2   . VAL B 1 62  ? -7.302  -33.630 27.308  1.00 41.84  ? 60  VAL B CG2   1 
ATOM   5048 N N     . GLY B 1 63  ? -3.585  -35.834 27.102  1.00 37.24  ? 61  GLY B N     1 
ATOM   5049 C CA    . GLY B 1 63  ? -2.232  -36.309 27.447  1.00 42.06  ? 61  GLY B CA    1 
ATOM   5050 C C     . GLY B 1 63  ? -1.433  -36.706 26.217  1.00 37.32  ? 61  GLY B C     1 
ATOM   5051 O O     . GLY B 1 63  ? -0.238  -36.386 26.148  1.00 36.45  ? 61  GLY B O     1 
ATOM   5052 N N     . ASP B 1 64  ? -2.045  -37.403 25.264  1.00 39.49  ? 62  ASP B N     1 
ATOM   5053 C CA    . ASP B 1 64  ? -1.340  -37.793 24.012  1.00 37.51  ? 62  ASP B CA    1 
ATOM   5054 C C     . ASP B 1 64  ? -0.994  -36.563 23.155  1.00 35.03  ? 62  ASP B C     1 
ATOM   5055 O O     . ASP B 1 64  ? 0.152   -36.493 22.719  1.00 34.09  ? 62  ASP B O     1 
ATOM   5056 C CB    . ASP B 1 64  ? -2.126  -38.820 23.201  1.00 38.72  ? 62  ASP B CB    1 
ATOM   5057 C CG    . ASP B 1 64  ? -1.324  -39.282 21.998  1.00 40.07  ? 62  ASP B CG    1 
ATOM   5058 O OD1   . ASP B 1 64  ? -0.221  -39.867 22.206  1.00 38.90  ? 62  ASP B OD1   1 
ATOM   5059 O OD2   . ASP B 1 64  ? -1.776  -39.003 20.875  1.00 35.43  ? 62  ASP B OD2   1 
ATOM   5060 N N     . LEU B 1 65  ? -1.925  -35.628 22.937  1.00 36.11  ? 63  LEU B N     1 
ATOM   5061 C CA    . LEU B 1 65  ? -1.723  -34.452 22.045  1.00 36.97  ? 63  LEU B CA    1 
ATOM   5062 C C     . LEU B 1 65  ? -0.732  -33.461 22.667  1.00 34.27  ? 63  LEU B C     1 
ATOM   5063 O O     . LEU B 1 65  ? 0.134   -33.019 21.935  1.00 33.35  ? 63  LEU B O     1 
ATOM   5064 C CB    . LEU B 1 65  ? -3.075  -33.776 21.775  1.00 42.21  ? 63  LEU B CB    1 
ATOM   5065 C CG    . LEU B 1 65  ? -4.116  -34.671 21.098  1.00 48.51  ? 63  LEU B CG    1 
ATOM   5066 C CD1   . LEU B 1 65  ? -5.507  -34.026 21.104  1.00 45.79  ? 63  LEU B CD1   1 
ATOM   5067 C CD2   . LEU B 1 65  ? -3.667  -35.021 19.681  1.00 47.18  ? 63  LEU B CD2   1 
ATOM   5068 N N     . GLU B 1 66  ? -0.836  -33.124 23.964  1.00 39.05  ? 64  GLU B N     1 
ATOM   5069 C CA    . GLU B 1 66  ? 0.026   -32.076 24.606  1.00 36.99  ? 64  GLU B CA    1 
ATOM   5070 C C     . GLU B 1 66  ? 1.370   -32.681 25.002  1.00 40.26  ? 64  GLU B C     1 
ATOM   5071 O O     . GLU B 1 66  ? 2.423   -32.023 24.816  1.00 38.71  ? 64  GLU B O     1 
ATOM   5072 C CB    . GLU B 1 66  ? -0.617  -31.469 25.849  1.00 38.22  ? 64  GLU B CB    1 
ATOM   5073 C CG    . GLU B 1 66  ? -1.881  -30.692 25.517  1.00 41.77  ? 64  GLU B CG    1 
ATOM   5074 C CD    . GLU B 1 66  ? -2.534  -29.946 26.665  1.00 41.61  ? 64  GLU B CD    1 
ATOM   5075 O OE1   . GLU B 1 66  ? -3.635  -29.400 26.453  1.00 42.75  ? 64  GLU B OE1   1 
ATOM   5076 O OE2   . GLU B 1 66  ? -1.960  -29.943 27.764  1.00 42.35  ? 64  GLU B OE2   1 
ATOM   5077 N N     . GLY B 1 67  ? 1.356   -33.895 25.540  1.00 38.74  ? 65  GLY B N     1 
ATOM   5078 C CA    . GLY B 1 67  ? 2.543   -34.417 26.228  1.00 40.73  ? 65  GLY B CA    1 
ATOM   5079 C C     . GLY B 1 67  ? 2.905   -33.462 27.355  1.00 42.20  ? 65  GLY B C     1 
ATOM   5080 O O     . GLY B 1 67  ? 2.030   -32.628 27.716  1.00 37.47  ? 65  GLY B O     1 
ATOM   5081 N N     . CYS B 1 68  ? 4.143   -33.562 27.850  1.00 37.66  ? 66  CYS B N     1 
ATOM   5082 C CA    . CYS B 1 68  ? 4.733   -32.741 28.930  1.00 36.27  ? 66  CYS B CA    1 
ATOM   5083 C C     . CYS B 1 68  ? 5.650   -31.704 28.282  1.00 36.48  ? 66  CYS B C     1 
ATOM   5084 O O     . CYS B 1 68  ? 6.047   -31.919 27.146  1.00 37.52  ? 66  CYS B O     1 
ATOM   5085 C CB    . CYS B 1 68  ? 5.477   -33.621 29.929  1.00 33.66  ? 66  CYS B CB    1 
ATOM   5086 S SG    . CYS B 1 68  ? 4.449   -34.891 30.703  1.00 39.47  ? 66  CYS B SG    1 
ATOM   5087 N N     . THR B 1 69  ? 5.939   -30.604 28.976  1.00 39.71  ? 67  THR B N     1 
ATOM   5088 C CA    . THR B 1 69  ? 6.810   -29.500 28.494  1.00 38.34  ? 67  THR B CA    1 
ATOM   5089 C C     . THR B 1 69  ? 7.959   -29.302 29.469  1.00 36.80  ? 67  THR B C     1 
ATOM   5090 O O     . THR B 1 69  ? 7.683   -28.979 30.640  1.00 37.58  ? 67  THR B O     1 
ATOM   5091 C CB    . THR B 1 69  ? 6.062   -28.170 28.391  1.00 38.29  ? 67  THR B CB    1 
ATOM   5092 O OG1   . THR B 1 69  ? 4.904   -28.554 27.661  1.00 34.15  ? 67  THR B OG1   1 
ATOM   5093 C CG2   . THR B 1 69  ? 6.856   -27.068 27.713  1.00 35.69  ? 67  THR B CG2   1 
ATOM   5094 N N     . TRP B 1 70  ? 9.176   -29.503 28.973  1.00 39.17  ? 68  TRP B N     1 
ATOM   5095 C CA    . TRP B 1 70  ? 10.432  -29.267 29.710  1.00 42.70  ? 68  TRP B CA    1 
ATOM   5096 C C     . TRP B 1 70  ? 10.752  -27.764 29.712  1.00 46.67  ? 68  TRP B C     1 
ATOM   5097 O O     . TRP B 1 70  ? 10.501  -27.115 28.701  1.00 38.75  ? 68  TRP B O     1 
ATOM   5098 C CB    . TRP B 1 70  ? 11.574  -30.072 29.090  1.00 43.29  ? 68  TRP B CB    1 
ATOM   5099 C CG    . TRP B 1 70  ? 12.857  -29.891 29.840  1.00 43.45  ? 68  TRP B CG    1 
ATOM   5100 C CD1   . TRP B 1 70  ? 13.293  -30.630 30.899  1.00 42.70  ? 68  TRP B CD1   1 
ATOM   5101 C CD2   . TRP B 1 70  ? 13.851  -28.875 29.621  1.00 42.87  ? 68  TRP B CD2   1 
ATOM   5102 N NE1   . TRP B 1 70  ? 14.504  -30.165 31.332  1.00 44.39  ? 68  TRP B NE1   1 
ATOM   5103 C CE2   . TRP B 1 70  ? 14.871  -29.083 30.575  1.00 43.95  ? 68  TRP B CE2   1 
ATOM   5104 C CE3   . TRP B 1 70  ? 13.984  -27.823 28.714  1.00 42.02  ? 68  TRP B CE3   1 
ATOM   5105 C CZ2   . TRP B 1 70  ? 16.000  -28.267 30.652  1.00 41.66  ? 68  TRP B CZ2   1 
ATOM   5106 C CZ3   . TRP B 1 70  ? 15.108  -27.028 28.774  1.00 44.16  ? 68  TRP B CZ3   1 
ATOM   5107 C CH2   . TRP B 1 70  ? 16.098  -27.238 29.741  1.00 44.63  ? 68  TRP B CH2   1 
ATOM   5108 N N     . SER B 1 71  ? 11.254  -27.243 30.838  1.00 47.40  ? 69  SER B N     1 
ATOM   5109 C CA    . SER B 1 71  ? 12.119  -26.038 30.912  1.00 47.56  ? 69  SER B CA    1 
ATOM   5110 C C     . SER B 1 71  ? 13.175  -26.294 31.992  1.00 52.46  ? 69  SER B C     1 
ATOM   5111 O O     . SER B 1 71  ? 13.086  -27.332 32.691  1.00 50.00  ? 69  SER B O     1 
ATOM   5112 C CB    . SER B 1 71  ? 11.315  -24.798 31.201  1.00 41.30  ? 69  SER B CB    1 
ATOM   5113 O OG    . SER B 1 71  ? 10.810  -24.868 32.509  1.00 44.69  ? 69  SER B OG    1 
ATOM   5114 N N     . ALA B 1 72  ? 14.128  -25.381 32.146  1.00 54.25  ? 70  ALA B N     1 
ATOM   5115 C CA    . ALA B 1 72  ? 15.200  -25.497 33.159  1.00 54.60  ? 70  ALA B CA    1 
ATOM   5116 C C     . ALA B 1 72  ? 14.558  -25.603 34.549  1.00 50.01  ? 70  ALA B C     1 
ATOM   5117 O O     . ALA B 1 72  ? 15.029  -26.424 35.333  1.00 58.23  ? 70  ALA B O     1 
ATOM   5118 C CB    . ALA B 1 72  ? 16.171  -24.344 33.025  1.00 55.02  ? 70  ALA B CB    1 
ATOM   5119 N N     . ASP B 1 73  ? 13.443  -24.910 34.795  1.00 55.55  ? 71  ASP B N     1 
ATOM   5120 C CA    . ASP B 1 73  ? 12.772  -24.824 36.128  1.00 56.13  ? 71  ASP B CA    1 
ATOM   5121 C C     . ASP B 1 73  ? 12.051  -26.125 36.502  1.00 51.18  ? 71  ASP B C     1 
ATOM   5122 O O     . ASP B 1 73  ? 11.741  -26.272 37.693  1.00 48.78  ? 71  ASP B O     1 
ATOM   5123 C CB    . ASP B 1 73  ? 11.719  -23.707 36.183  1.00 63.50  ? 71  ASP B CB    1 
ATOM   5124 C CG    . ASP B 1 73  ? 12.257  -22.309 35.919  1.00 72.23  ? 71  ASP B CG    1 
ATOM   5125 O OD1   . ASP B 1 73  ? 13.396  -22.026 36.349  1.00 73.71  ? 71  ASP B OD1   1 
ATOM   5126 O OD2   . ASP B 1 73  ? 11.539  -21.514 35.270  1.00 77.88  ? 71  ASP B OD2   1 
ATOM   5127 N N     . GLY B 1 74  ? 11.698  -26.988 35.544  1.00 47.27  ? 72  GLY B N     1 
ATOM   5128 C CA    . GLY B 1 74  ? 10.867  -28.182 35.821  1.00 44.17  ? 72  GLY B CA    1 
ATOM   5129 C C     . GLY B 1 74  ? 10.038  -28.639 34.625  1.00 44.85  ? 72  GLY B C     1 
ATOM   5130 O O     . GLY B 1 74  ? 10.450  -28.366 33.475  1.00 42.87  ? 72  GLY B O     1 
ATOM   5131 N N     . VAL B 1 75  ? 8.912   -29.323 34.882  1.00 40.72  ? 73  VAL B N     1 
ATOM   5132 C CA    . VAL B 1 75  ? 8.146   -30.061 33.838  1.00 40.35  ? 73  VAL B CA    1 
ATOM   5133 C C     . VAL B 1 75  ? 6.646   -29.836 34.039  1.00 36.22  ? 73  VAL B C     1 
ATOM   5134 O O     . VAL B 1 75  ? 6.095   -30.213 35.104  1.00 42.26  ? 73  VAL B O     1 
ATOM   5135 C CB    . VAL B 1 75  ? 8.511   -31.557 33.861  1.00 41.11  ? 73  VAL B CB    1 
ATOM   5136 C CG1   . VAL B 1 75  ? 7.499   -32.395 33.095  1.00 43.03  ? 73  VAL B CG1   1 
ATOM   5137 C CG2   . VAL B 1 75  ? 9.911   -31.798 33.323  1.00 37.45  ? 73  VAL B CG2   1 
ATOM   5138 N N     . LYS B 1 76  ? 6.005   -29.249 33.041  1.00 33.93  ? 74  LYS B N     1 
ATOM   5139 C CA    . LYS B 1 76  ? 4.536   -29.087 33.013  1.00 37.59  ? 74  LYS B CA    1 
ATOM   5140 C C     . LYS B 1 76  ? 3.900   -30.360 32.439  1.00 35.84  ? 74  LYS B C     1 
ATOM   5141 O O     . LYS B 1 76  ? 4.386   -30.880 31.440  1.00 42.00  ? 74  LYS B O     1 
ATOM   5142 C CB    . LYS B 1 76  ? 4.146   -27.855 32.197  1.00 41.31  ? 74  LYS B CB    1 
ATOM   5143 C CG    . LYS B 1 76  ? 2.658   -27.549 32.214  1.00 43.69  ? 74  LYS B CG    1 
ATOM   5144 C CD    . LYS B 1 76  ? 2.259   -26.412 31.275  1.00 46.17  ? 74  LYS B CD    1 
ATOM   5145 C CE    . LYS B 1 76  ? 0.822   -25.966 31.501  1.00 50.27  ? 74  LYS B CE    1 
ATOM   5146 N NZ    . LYS B 1 76  ? -0.079  -27.124 31.778  1.00 52.32  ? 74  LYS B NZ    1 
ATOM   5147 N N     . THR B 1 77  ? 2.855   -30.848 33.089  1.00 35.83  ? 75  THR B N     1 
ATOM   5148 C CA    . THR B 1 77  ? 2.046   -31.988 32.654  1.00 38.35  ? 75  THR B CA    1 
ATOM   5149 C C     . THR B 1 77  ? 0.866   -31.494 31.813  1.00 42.43  ? 75  THR B C     1 
ATOM   5150 O O     . THR B 1 77  ? 0.491   -30.331 31.839  1.00 43.06  ? 75  THR B O     1 
ATOM   5151 C CB    . THR B 1 77  ? 1.578   -32.805 33.860  1.00 35.25  ? 75  THR B CB    1 
ATOM   5152 O OG1   . THR B 1 77  ? 0.865   -31.919 34.720  1.00 33.14  ? 75  THR B OG1   1 
ATOM   5153 C CG2   . THR B 1 77  ? 2.738   -33.541 34.493  1.00 33.89  ? 75  THR B CG2   1 
ATOM   5154 N N     . PRO B 1 78  ? 0.249   -32.375 31.004  1.00 42.52  ? 76  PRO B N     1 
ATOM   5155 C CA    . PRO B 1 78  ? -0.873  -31.960 30.174  1.00 40.18  ? 76  PRO B CA    1 
ATOM   5156 C C     . PRO B 1 78  ? -1.990  -31.292 30.982  1.00 42.01  ? 76  PRO B C     1 
ATOM   5157 O O     . PRO B 1 78  ? -2.171  -31.618 32.161  1.00 41.47  ? 76  PRO B O     1 
ATOM   5158 C CB    . PRO B 1 78  ? -1.388  -33.283 29.619  1.00 40.55  ? 76  PRO B CB    1 
ATOM   5159 C CG    . PRO B 1 78  ? -0.165  -34.167 29.612  1.00 42.27  ? 76  PRO B CG    1 
ATOM   5160 C CD    . PRO B 1 78  ? 0.614   -33.789 30.839  1.00 38.38  ? 76  PRO B CD    1 
ATOM   5161 N N     . THR B 1 79  ? -2.753  -30.432 30.305  1.00 43.94  ? 77  THR B N     1 
ATOM   5162 C CA    . THR B 1 79  ? -3.942  -29.727 30.859  1.00 41.26  ? 77  THR B CA    1 
ATOM   5163 C C     . THR B 1 79  ? -4.796  -30.725 31.617  1.00 40.22  ? 77  THR B C     1 
ATOM   5164 O O     . THR B 1 79  ? -5.142  -31.752 30.996  1.00 41.81  ? 77  THR B O     1 
ATOM   5165 C CB    . THR B 1 79  ? -4.753  -29.086 29.734  1.00 39.47  ? 77  THR B CB    1 
ATOM   5166 O OG1   . THR B 1 79  ? -3.782  -28.243 29.120  1.00 40.19  ? 77  THR B OG1   1 
ATOM   5167 C CG2   . THR B 1 79  ? -5.960  -28.299 30.201  1.00 40.92  ? 77  THR B CG2   1 
ATOM   5168 N N     . GLY B 1 80  ? -5.081  -30.453 32.894  1.00 36.34  ? 78  GLY B N     1 
ATOM   5169 C CA    . GLY B 1 80  ? -6.039  -31.258 33.676  1.00 37.93  ? 78  GLY B CA    1 
ATOM   5170 C C     . GLY B 1 80  ? -5.412  -32.405 34.465  1.00 37.35  ? 78  GLY B C     1 
ATOM   5171 O O     . GLY B 1 80  ? -6.138  -32.967 35.297  1.00 39.55  ? 78  GLY B O     1 
ATOM   5172 N N     . PHE B 1 81  ? -4.142  -32.759 34.222  1.00 38.31  ? 79  PHE B N     1 
ATOM   5173 C CA    . PHE B 1 81  ? -3.451  -33.897 34.891  1.00 43.52  ? 79  PHE B CA    1 
ATOM   5174 C C     . PHE B 1 81  ? -3.328  -33.648 36.409  1.00 44.33  ? 79  PHE B C     1 
ATOM   5175 O O     . PHE B 1 81  ? -3.839  -34.484 37.184  1.00 40.04  ? 79  PHE B O     1 
ATOM   5176 C CB    . PHE B 1 81  ? -2.113  -34.196 34.197  1.00 43.68  ? 79  PHE B CB    1 
ATOM   5177 C CG    . PHE B 1 81  ? -2.209  -35.262 33.127  1.00 42.91  ? 79  PHE B CG    1 
ATOM   5178 C CD1   . PHE B 1 81  ? -3.314  -35.347 32.295  1.00 41.04  ? 79  PHE B CD1   1 
ATOM   5179 C CD2   . PHE B 1 81  ? -1.212  -36.207 32.973  1.00 43.25  ? 79  PHE B CD2   1 
ATOM   5180 C CE1   . PHE B 1 81  ? -3.402  -36.339 31.332  1.00 44.69  ? 79  PHE B CE1   1 
ATOM   5181 C CE2   . PHE B 1 81  ? -1.295  -37.193 32.004  1.00 43.08  ? 79  PHE B CE2   1 
ATOM   5182 C CZ    . PHE B 1 81  ? -2.388  -37.254 31.179  1.00 41.66  ? 79  PHE B CZ    1 
ATOM   5183 N N     . LYS B 1 82  ? -2.677  -32.557 36.828  1.00 45.43  ? 80  LYS B N     1 
ATOM   5184 C CA    . LYS B 1 82  ? -2.448  -32.224 38.266  1.00 47.24  ? 80  LYS B CA    1 
ATOM   5185 C C     . LYS B 1 82  ? -3.778  -32.035 38.999  1.00 49.12  ? 80  LYS B C     1 
ATOM   5186 O O     . LYS B 1 82  ? -3.853  -32.479 40.162  1.00 53.12  ? 80  LYS B O     1 
ATOM   5187 C CB    . LYS B 1 82  ? -1.576  -30.978 38.409  1.00 50.07  ? 80  LYS B CB    1 
ATOM   5188 C CG    . LYS B 1 82  ? -2.164  -29.711 37.824  1.00 59.98  ? 80  LYS B CG    1 
ATOM   5189 C CD    . LYS B 1 82  ? -1.122  -28.653 37.525  1.00 72.85  ? 80  LYS B CD    1 
ATOM   5190 C CE    . LYS B 1 82  ? -0.501  -28.072 38.780  1.00 78.85  ? 80  LYS B CE    1 
ATOM   5191 N NZ    . LYS B 1 82  ? 0.576   -27.103 38.462  1.00 83.53  ? 80  LYS B NZ    1 
ATOM   5192 N N     . GLU B 1 83  ? -4.804  -31.458 38.354  1.00 50.22  ? 81  GLU B N     1 
ATOM   5193 C CA    . GLU B 1 83  ? -6.116  -31.160 39.004  1.00 44.92  ? 81  GLU B CA    1 
ATOM   5194 C C     . GLU B 1 83  ? -6.835  -32.487 39.246  1.00 45.71  ? 81  GLU B C     1 
ATOM   5195 O O     . GLU B 1 83  ? -7.518  -32.615 40.285  1.00 53.21  ? 81  GLU B O     1 
ATOM   5196 C CB    . GLU B 1 83  ? -6.954  -30.178 38.184  1.00 46.13  ? 81  GLU B CB    1 
ATOM   5197 C CG    . GLU B 1 83  ? -6.256  -28.836 37.910  1.00 50.76  ? 81  GLU B CG    1 
ATOM   5198 C CD    . GLU B 1 83  ? -5.183  -28.747 36.820  1.00 55.63  ? 81  GLU B CD    1 
ATOM   5199 O OE1   . GLU B 1 83  ? -4.566  -27.646 36.652  1.00 52.54  ? 81  GLU B OE1   1 
ATOM   5200 O OE2   . GLU B 1 83  ? -4.943  -29.765 36.130  1.00 56.99  ? 81  GLU B OE2   1 
ATOM   5201 N N     . ALA B 1 84  ? -6.637  -33.477 38.363  1.00 41.37  ? 82  ALA B N     1 
ATOM   5202 C CA    . ALA B 1 84  ? -7.141  -34.865 38.550  1.00 38.08  ? 82  ALA B CA    1 
ATOM   5203 C C     . ALA B 1 84  ? -6.375  -35.539 39.704  1.00 37.60  ? 82  ALA B C     1 
ATOM   5204 O O     . ALA B 1 84  ? -7.008  -36.335 40.495  1.00 34.07  ? 82  ALA B O     1 
ATOM   5205 C CB    . ALA B 1 84  ? -7.019  -35.639 37.260  1.00 38.77  ? 82  ALA B CB    1 
ATOM   5206 N N     . TYR B 1 85  ? -5.069  -35.247 39.811  1.00 33.89  ? 83  TYR B N     1 
ATOM   5207 C CA    . TYR B 1 85  ? -4.201  -35.824 40.859  1.00 39.90  ? 83  TYR B CA    1 
ATOM   5208 C C     . TYR B 1 85  ? -4.647  -35.277 42.220  1.00 43.89  ? 83  TYR B C     1 
ATOM   5209 O O     . TYR B 1 85  ? -4.794  -36.130 43.117  1.00 41.61  ? 83  TYR B O     1 
ATOM   5210 C CB    . TYR B 1 85  ? -2.704  -35.653 40.585  1.00 40.10  ? 83  TYR B CB    1 
ATOM   5211 C CG    . TYR B 1 85  ? -1.884  -36.482 41.539  1.00 41.22  ? 83  TYR B CG    1 
ATOM   5212 C CD1   . TYR B 1 85  ? -1.856  -37.863 41.432  1.00 41.51  ? 83  TYR B CD1   1 
ATOM   5213 C CD2   . TYR B 1 85  ? -1.188  -35.892 42.587  1.00 43.17  ? 83  TYR B CD2   1 
ATOM   5214 C CE1   . TYR B 1 85  ? -1.150  -38.643 42.333  1.00 41.30  ? 83  TYR B CE1   1 
ATOM   5215 C CE2   . TYR B 1 85  ? -0.485  -36.656 43.506  1.00 40.71  ? 83  TYR B CE2   1 
ATOM   5216 C CZ    . TYR B 1 85  ? -0.478  -38.030 43.374  1.00 42.40  ? 83  TYR B CZ    1 
ATOM   5217 O OH    . TYR B 1 85  ? 0.205   -38.785 44.258  1.00 46.28  ? 83  TYR B OH    1 
ATOM   5218 N N     . GLN B 1 86  ? -4.915  -33.965 42.337  1.00 47.53  ? 84  GLN B N     1 
ATOM   5219 C CA    . GLN B 1 86  ? -5.437  -33.344 43.587  1.00 49.94  ? 84  GLN B CA    1 
ATOM   5220 C C     . GLN B 1 86  ? -6.712  -34.066 43.990  1.00 46.16  ? 84  GLN B C     1 
ATOM   5221 O O     . GLN B 1 86  ? -6.856  -34.355 45.185  1.00 52.00  ? 84  GLN B O     1 
ATOM   5222 C CB    . GLN B 1 86  ? -5.797  -31.870 43.466  1.00 58.80  ? 84  GLN B CB    1 
ATOM   5223 C CG    . GLN B 1 86  ? -4.616  -30.924 43.532  1.00 69.46  ? 84  GLN B CG    1 
ATOM   5224 C CD    . GLN B 1 86  ? -5.104  -29.559 43.116  1.00 77.93  ? 84  GLN B CD    1 
ATOM   5225 O OE1   . GLN B 1 86  ? -5.843  -28.913 43.853  1.00 90.01  ? 84  GLN B OE1   1 
ATOM   5226 N NE2   . GLN B 1 86  ? -4.761  -29.139 41.906  1.00 72.82  ? 84  GLN B NE2   1 
ATOM   5227 N N     . GLN B 1 87  ? -7.581  -34.364 43.028  1.00 42.53  ? 85  GLN B N     1 
ATOM   5228 C CA    . GLN B 1 87  ? -8.857  -35.077 43.298  1.00 42.89  ? 85  GLN B CA    1 
ATOM   5229 C C     . GLN B 1 87  ? -8.560  -36.512 43.718  1.00 42.82  ? 85  GLN B C     1 
ATOM   5230 O O     . GLN B 1 87  ? -9.236  -36.986 44.638  1.00 47.16  ? 85  GLN B O     1 
ATOM   5231 C CB    . GLN B 1 87  ? -9.798  -35.065 42.092  1.00 47.53  ? 85  GLN B CB    1 
ATOM   5232 C CG    . GLN B 1 87  ? -10.636 -33.798 41.989  1.00 53.24  ? 85  GLN B CG    1 
ATOM   5233 C CD    . GLN B 1 87  ? -11.219 -33.631 40.605  1.00 54.23  ? 85  GLN B CD    1 
ATOM   5234 O OE1   . GLN B 1 87  ? -12.202 -34.285 40.246  1.00 50.07  ? 85  GLN B OE1   1 
ATOM   5235 N NE2   . GLN B 1 87  ? -10.592 -32.772 39.811  1.00 55.30  ? 85  GLN B NE2   1 
ATOM   5236 N N     . PHE B 1 88  ? -7.614  -37.189 43.061  1.00 43.13  ? 86  PHE B N     1 
ATOM   5237 C CA    . PHE B 1 88  ? -7.164  -38.555 43.454  1.00 41.65  ? 86  PHE B CA    1 
ATOM   5238 C C     . PHE B 1 88  ? -6.672  -38.539 44.913  1.00 39.05  ? 86  PHE B C     1 
ATOM   5239 O O     . PHE B 1 88  ? -7.076  -39.445 45.676  1.00 41.91  ? 86  PHE B O     1 
ATOM   5240 C CB    . PHE B 1 88  ? -6.062  -39.044 42.513  1.00 42.03  ? 86  PHE B CB    1 
ATOM   5241 C CG    . PHE B 1 88  ? -5.778  -40.526 42.549  1.00 42.60  ? 86  PHE B CG    1 
ATOM   5242 C CD1   . PHE B 1 88  ? -6.743  -41.446 42.171  1.00 40.50  ? 86  PHE B CD1   1 
ATOM   5243 C CD2   . PHE B 1 88  ? -4.519  -41.001 42.901  1.00 43.19  ? 86  PHE B CD2   1 
ATOM   5244 C CE1   . PHE B 1 88  ? -6.465  -42.806 42.181  1.00 38.71  ? 86  PHE B CE1   1 
ATOM   5245 C CE2   . PHE B 1 88  ? -4.245  -42.360 42.902  1.00 42.05  ? 86  PHE B CE2   1 
ATOM   5246 C CZ    . PHE B 1 88  ? -5.222  -43.260 42.549  1.00 38.81  ? 86  PHE B CZ    1 
ATOM   5247 N N     . VAL B 1 89  ? -5.810  -37.573 45.276  1.00 38.64  ? 87  VAL B N     1 
ATOM   5248 C CA    . VAL B 1 89  ? -5.337  -37.340 46.676  1.00 42.15  ? 87  VAL B CA    1 
ATOM   5249 C C     . VAL B 1 89  ? -6.568  -37.200 47.602  1.00 44.68  ? 87  VAL B C     1 
ATOM   5250 O O     . VAL B 1 89  ? -6.762  -38.097 48.435  1.00 41.18  ? 87  VAL B O     1 
ATOM   5251 C CB    . VAL B 1 89  ? -4.386  -36.130 46.810  1.00 44.35  ? 87  VAL B CB    1 
ATOM   5252 C CG1   . VAL B 1 89  ? -4.023  -35.892 48.280  1.00 46.87  ? 87  VAL B CG1   1 
ATOM   5253 C CG2   . VAL B 1 89  ? -3.104  -36.241 45.979  1.00 40.73  ? 87  VAL B CG2   1 
ATOM   5254 N N     . GLU B 1 90  ? -7.430  -36.198 47.378  1.00 46.61  ? 88  GLU B N     1 
ATOM   5255 C CA    . GLU B 1 90  ? -8.581  -35.826 48.259  1.00 49.10  ? 88  GLU B CA    1 
ATOM   5256 C C     . GLU B 1 90  ? -9.540  -37.002 48.440  1.00 50.30  ? 88  GLU B C     1 
ATOM   5257 O O     . GLU B 1 90  ? -10.205 -37.026 49.480  1.00 64.78  ? 88  GLU B O     1 
ATOM   5258 C CB    . GLU B 1 90  ? -9.349  -34.605 47.733  1.00 52.96  ? 88  GLU B CB    1 
ATOM   5259 C CG    . GLU B 1 90  ? -8.640  -33.275 47.996  1.00 63.43  ? 88  GLU B CG    1 
ATOM   5260 C CD    . GLU B 1 90  ? -8.636  -32.225 46.881  1.00 69.02  ? 88  GLU B CD    1 
ATOM   5261 O OE1   . GLU B 1 90  ? -7.584  -31.558 46.687  1.00 79.79  ? 88  GLU B OE1   1 
ATOM   5262 O OE2   . GLU B 1 90  ? -9.664  -32.071 46.193  1.00 77.27  ? 88  GLU B OE2   1 
ATOM   5263 N N     . GLY B 1 91  ? -9.626  -37.934 47.486  1.00 46.29  ? 89  GLY B N     1 
ATOM   5264 C CA    . GLY B 1 91  ? -10.451 -39.160 47.616  1.00 40.58  ? 89  GLY B CA    1 
ATOM   5265 C C     . GLY B 1 91  ? -9.749  -40.237 48.432  1.00 42.97  ? 89  GLY B C     1 
ATOM   5266 O O     . GLY B 1 91  ? -10.329 -41.321 48.598  1.00 42.41  ? 89  GLY B O     1 
ATOM   5267 N N     . GLY B 1 92  ? -8.514  -39.962 48.879  1.00 47.18  ? 90  GLY B N     1 
ATOM   5268 C CA    . GLY B 1 92  ? -7.622  -40.873 49.628  1.00 44.09  ? 90  GLY B CA    1 
ATOM   5269 C C     . GLY B 1 92  ? -7.298  -42.163 48.893  1.00 46.48  ? 90  GLY B C     1 
ATOM   5270 O O     . GLY B 1 92  ? -7.054  -43.169 49.567  1.00 52.46  ? 90  GLY B O     1 
ATOM   5271 N N     . TRP B 1 93  ? -7.275  -42.175 47.562  1.00 45.16  ? 91  TRP B N     1 
ATOM   5272 C CA    . TRP B 1 93  ? -6.921  -43.402 46.795  1.00 42.78  ? 91  TRP B CA    1 
ATOM   5273 C C     . TRP B 1 93  ? -5.487  -43.843 47.091  1.00 39.11  ? 91  TRP B C     1 
ATOM   5274 O O     . TRP B 1 93  ? -5.258  -45.033 47.260  1.00 39.74  ? 91  TRP B O     1 
ATOM   5275 C CB    . TRP B 1 93  ? -7.170  -43.200 45.295  1.00 41.69  ? 91  TRP B CB    1 
ATOM   5276 C CG    . TRP B 1 93  ? -8.628  -43.041 44.992  1.00 37.54  ? 91  TRP B CG    1 
ATOM   5277 C CD1   . TRP B 1 93  ? -9.277  -41.883 44.691  1.00 33.65  ? 91  TRP B CD1   1 
ATOM   5278 C CD2   . TRP B 1 93  ? -9.629  -44.072 45.037  1.00 32.41  ? 91  TRP B CD2   1 
ATOM   5279 N NE1   . TRP B 1 93  ? -10.610 -42.130 44.529  1.00 35.73  ? 91  TRP B NE1   1 
ATOM   5280 C CE2   . TRP B 1 93  ? -10.856 -43.457 44.724  1.00 32.85  ? 91  TRP B CE2   1 
ATOM   5281 C CE3   . TRP B 1 93  ? -9.609  -45.445 45.307  1.00 33.59  ? 91  TRP B CE3   1 
ATOM   5282 C CZ2   . TRP B 1 93  ? -12.051 -44.168 44.658  1.00 34.42  ? 91  TRP B CZ2   1 
ATOM   5283 C CZ3   . TRP B 1 93  ? -10.788 -46.158 45.259  1.00 32.10  ? 91  TRP B CZ3   1 
ATOM   5284 C CH2   . TRP B 1 93  ? -11.994 -45.522 44.944  1.00 36.21  ? 91  TRP B CH2   1 
ATOM   5285 N N     . PRO B 1 94  ? -4.476  -42.942 47.165  1.00 36.75  ? 92  PRO B N     1 
ATOM   5286 C CA    . PRO B 1 94  ? -3.103  -43.363 47.440  1.00 41.96  ? 92  PRO B CA    1 
ATOM   5287 C C     . PRO B 1 94  ? -2.969  -44.254 48.687  1.00 45.92  ? 92  PRO B C     1 
ATOM   5288 O O     . PRO B 1 94  ? -2.175  -45.132 48.666  1.00 51.30  ? 92  PRO B O     1 
ATOM   5289 C CB    . PRO B 1 94  ? -2.312  -42.035 47.583  1.00 39.03  ? 92  PRO B CB    1 
ATOM   5290 C CG    . PRO B 1 94  ? -3.106  -41.033 46.767  1.00 37.76  ? 92  PRO B CG    1 
ATOM   5291 C CD    . PRO B 1 94  ? -4.552  -41.498 46.858  1.00 39.17  ? 92  PRO B CD    1 
ATOM   5292 N N     . SER B 1 95  ? -3.775  -44.035 49.723  1.00 52.18  ? 93  SER B N     1 
ATOM   5293 C CA    . SER B 1 95  ? -3.622  -44.684 51.050  1.00 52.90  ? 93  SER B CA    1 
ATOM   5294 C C     . SER B 1 95  ? -4.360  -46.032 51.150  1.00 52.40  ? 93  SER B C     1 
ATOM   5295 O O     . SER B 1 95  ? -4.205  -46.689 52.176  1.00 59.11  ? 93  SER B O     1 
ATOM   5296 C CB    . SER B 1 95  ? -4.052  -43.728 52.134  1.00 51.34  ? 93  SER B CB    1 
ATOM   5297 O OG    . SER B 1 95  ? -5.392  -43.315 51.964  1.00 49.59  ? 93  SER B OG    1 
ATOM   5298 N N     . LEU B 1 96  ? -5.078  -46.468 50.118  1.00 49.64  ? 94  LEU B N     1 
ATOM   5299 C CA    . LEU B 1 96  ? -5.999  -47.643 50.164  1.00 48.37  ? 94  LEU B CA    1 
ATOM   5300 C C     . LEU B 1 96  ? -5.315  -48.923 50.689  1.00 45.56  ? 94  LEU B C     1 
ATOM   5301 O O     . LEU B 1 96  ? -5.901  -49.571 51.614  1.00 44.45  ? 94  LEU B O     1 
ATOM   5302 C CB    . LEU B 1 96  ? -6.563  -47.861 48.755  1.00 46.60  ? 94  LEU B CB    1 
ATOM   5303 C CG    . LEU B 1 96  ? -7.812  -48.733 48.665  1.00 52.92  ? 94  LEU B CG    1 
ATOM   5304 C CD1   . LEU B 1 96  ? -9.053  -47.984 49.163  1.00 55.49  ? 94  LEU B CD1   1 
ATOM   5305 C CD2   . LEU B 1 96  ? -8.003  -49.199 47.229  1.00 56.44  ? 94  LEU B CD2   1 
ATOM   5306 N N     . ALA B 1 97  ? -4.183  -49.339 50.103  1.00 44.18  ? 95  ALA B N     1 
ATOM   5307 C CA    . ALA B 1 97  ? -3.558  -50.672 50.318  1.00 47.46  ? 95  ALA B CA    1 
ATOM   5308 C C     . ALA B 1 97  ? -2.266  -50.574 51.144  1.00 52.55  ? 95  ALA B C     1 
ATOM   5309 O O     . ALA B 1 97  ? -1.390  -51.411 50.953  1.00 63.78  ? 95  ALA B O     1 
ATOM   5310 C CB    . ALA B 1 97  ? -3.294  -51.333 48.994  1.00 47.34  ? 95  ALA B CB    1 
ATOM   5311 N N     . HIS B 1 98  ? -2.156  -49.595 52.042  1.00 51.17  ? 96  HIS B N     1 
ATOM   5312 C CA    . HIS B 1 98  ? -0.957  -49.355 52.884  1.00 51.14  ? 96  HIS B CA    1 
ATOM   5313 C C     . HIS B 1 98  ? -1.332  -49.529 54.367  1.00 52.33  ? 96  HIS B C     1 
ATOM   5314 O O     . HIS B 1 98  ? -2.535  -49.403 54.694  1.00 43.56  ? 96  HIS B O     1 
ATOM   5315 C CB    . HIS B 1 98  ? -0.358  -47.993 52.516  1.00 50.15  ? 96  HIS B CB    1 
ATOM   5316 C CG    . HIS B 1 98  ? 0.152   -47.992 51.117  1.00 55.81  ? 96  HIS B CG    1 
ATOM   5317 N ND1   . HIS B 1 98  ? 1.024   -48.956 50.656  1.00 55.39  ? 96  HIS B ND1   1 
ATOM   5318 C CD2   . HIS B 1 98  ? -0.141  -47.213 50.057  1.00 57.96  ? 96  HIS B CD2   1 
ATOM   5319 C CE1   . HIS B 1 98  ? 1.272   -48.746 49.380  1.00 56.08  ? 96  HIS B CE1   1 
ATOM   5320 N NE2   . HIS B 1 98  ? 0.568   -47.685 48.989  1.00 58.72  ? 96  HIS B NE2   1 
ATOM   5321 N N     . ASP B 1 99  ? -0.332  -49.842 55.203  1.00 56.04  ? 97  ASP B N     1 
ATOM   5322 C CA    . ASP B 1 99  ? -0.429  -50.095 56.672  1.00 55.66  ? 97  ASP B CA    1 
ATOM   5323 C C     . ASP B 1 99  ? -1.164  -48.930 57.353  1.00 53.70  ? 97  ASP B C     1 
ATOM   5324 O O     . ASP B 1 99  ? -0.907  -47.742 56.992  1.00 45.84  ? 97  ASP B O     1 
ATOM   5325 C CB    . ASP B 1 99  ? 0.956   -50.329 57.288  1.00 59.02  ? 97  ASP B CB    1 
ATOM   5326 C CG    . ASP B 1 99  ? 2.035   -49.373 56.787  1.00 80.41  ? 97  ASP B CG    1 
ATOM   5327 O OD1   . ASP B 1 99  ? 1.682   -48.405 56.052  1.00 88.19  ? 97  ASP B OD1   1 
ATOM   5328 O OD2   . ASP B 1 99  ? 3.230   -49.613 57.098  1.00 90.37  ? 97  ASP B OD2   1 
ATOM   5329 N N     . VAL B 1 100 ? -2.080  -49.259 58.273  1.00 59.60  ? 98  VAL B N     1 
ATOM   5330 C CA    . VAL B 1 100 ? -2.807  -48.259 59.113  1.00 63.67  ? 98  VAL B CA    1 
ATOM   5331 C C     . VAL B 1 100 ? -1.724  -47.506 59.890  1.00 60.10  ? 98  VAL B C     1 
ATOM   5332 O O     . VAL B 1 100 ? -1.835  -46.272 60.052  1.00 51.55  ? 98  VAL B O     1 
ATOM   5333 C CB    . VAL B 1 100 ? -3.870  -48.896 60.039  1.00 65.83  ? 98  VAL B CB    1 
ATOM   5334 C CG1   . VAL B 1 100 ? -4.712  -47.825 60.717  1.00 67.66  ? 98  VAL B CG1   1 
ATOM   5335 C CG2   . VAL B 1 100 ? -4.786  -49.880 59.309  1.00 65.47  ? 98  VAL B CG2   1 
ATOM   5336 N N     . GLU B 1 101 ? -0.677  -48.243 60.256  1.00 61.19  ? 99  GLU B N     1 
ATOM   5337 C CA    . GLU B 1 101 ? 0.556   -47.748 60.915  1.00 67.78  ? 99  GLU B CA    1 
ATOM   5338 C C     . GLU B 1 101 ? 1.011   -46.438 60.244  1.00 64.46  ? 99  GLU B C     1 
ATOM   5339 O O     . GLU B 1 101 ? 1.124   -45.451 60.970  1.00 60.28  ? 99  GLU B O     1 
ATOM   5340 C CB    . GLU B 1 101 ? 1.582   -48.884 60.905  1.00 76.77  ? 99  GLU B CB    1 
ATOM   5341 C CG    . GLU B 1 101 ? 2.685   -48.757 61.936  1.00 85.71  ? 99  GLU B CG    1 
ATOM   5342 C CD    . GLU B 1 101 ? 3.911   -49.617 61.632  1.00 94.65  ? 99  GLU B CD    1 
ATOM   5343 O OE1   . GLU B 1 101 ? 4.997   -49.361 62.210  1.00 89.17  ? 99  GLU B OE1   1 
ATOM   5344 O OE2   . GLU B 1 101 ? 3.785   -50.543 60.803  1.00 100.56 ? 99  GLU B OE2   1 
ATOM   5345 N N     . HIS B 1 102 ? 1.230   -46.379 58.921  1.00 66.18  ? 100 HIS B N     1 
ATOM   5346 C CA    . HIS B 1 102 ? 1.902   -45.211 58.271  1.00 57.59  ? 100 HIS B CA    1 
ATOM   5347 C C     . HIS B 1 102 ? 0.915   -44.321 57.500  1.00 56.52  ? 100 HIS B C     1 
ATOM   5348 O O     . HIS B 1 102 ? 1.353   -43.548 56.628  1.00 51.15  ? 100 HIS B O     1 
ATOM   5349 C CB    . HIS B 1 102 ? 3.080   -45.691 57.428  1.00 63.58  ? 100 HIS B CB    1 
ATOM   5350 C CG    . HIS B 1 102 ? 4.216   -46.214 58.242  1.00 67.37  ? 100 HIS B CG    1 
ATOM   5351 N ND1   . HIS B 1 102 ? 5.105   -45.370 58.896  1.00 69.68  ? 100 HIS B ND1   1 
ATOM   5352 C CD2   . HIS B 1 102 ? 4.632   -47.474 58.488  1.00 67.49  ? 100 HIS B CD2   1 
ATOM   5353 C CE1   . HIS B 1 102 ? 5.995   -46.095 59.541  1.00 75.15  ? 100 HIS B CE1   1 
ATOM   5354 N NE2   . HIS B 1 102 ? 5.724   -47.390 59.305  1.00 75.68  ? 100 HIS B NE2   1 
ATOM   5355 N N     . GLY B 1 103 ? -0.365  -44.354 57.870  1.00 55.99  ? 101 GLY B N     1 
ATOM   5356 C CA    . GLY B 1 103 ? -1.365  -43.351 57.457  1.00 50.15  ? 101 GLY B CA    1 
ATOM   5357 C C     . GLY B 1 103 ? -2.301  -43.919 56.414  1.00 55.92  ? 101 GLY B C     1 
ATOM   5358 O O     . GLY B 1 103 ? -2.930  -43.131 55.698  1.00 58.31  ? 101 GLY B O     1 
ATOM   5359 N N     . GLY B 1 104 ? -2.382  -45.243 56.323  1.00 51.49  ? 102 GLY B N     1 
ATOM   5360 C CA    . GLY B 1 104 ? -3.111  -45.928 55.247  1.00 54.88  ? 102 GLY B CA    1 
ATOM   5361 C C     . GLY B 1 104 ? -4.395  -46.520 55.768  1.00 53.15  ? 102 GLY B C     1 
ATOM   5362 O O     . GLY B 1 104 ? -4.548  -46.563 56.998  1.00 52.49  ? 102 GLY B O     1 
ATOM   5363 N N     . GLN B 1 105 ? -5.239  -47.015 54.856  1.00 51.51  ? 103 GLN B N     1 
ATOM   5364 C CA    . GLN B 1 105 ? -6.563  -47.639 55.145  1.00 48.84  ? 103 GLN B CA    1 
ATOM   5365 C C     . GLN B 1 105 ? -6.416  -49.152 55.417  1.00 45.70  ? 103 GLN B C     1 
ATOM   5366 O O     . GLN B 1 105 ? -7.384  -49.751 55.888  1.00 47.71  ? 103 GLN B O     1 
ATOM   5367 C CB    . GLN B 1 105 ? -7.536  -47.332 53.999  1.00 45.70  ? 103 GLN B CB    1 
ATOM   5368 C CG    . GLN B 1 105 ? -7.747  -45.837 53.729  1.00 45.19  ? 103 GLN B CG    1 
ATOM   5369 C CD    . GLN B 1 105 ? -8.631  -45.582 52.524  1.00 45.66  ? 103 GLN B CD    1 
ATOM   5370 O OE1   . GLN B 1 105 ? -9.719  -46.144 52.398  1.00 49.36  ? 103 GLN B OE1   1 
ATOM   5371 N NE2   . GLN B 1 105 ? -8.165  -44.751 51.602  1.00 41.20  ? 103 GLN B NE2   1 
ATOM   5372 N N     . GLY B 1 106 ? -5.262  -49.767 55.140  1.00 41.23  ? 104 GLY B N     1 
ATOM   5373 C CA    . GLY B 1 106 ? -5.028  -51.194 55.420  1.00 40.58  ? 104 GLY B CA    1 
ATOM   5374 C C     . GLY B 1 106 ? -5.882  -52.151 54.600  1.00 44.00  ? 104 GLY B C     1 
ATOM   5375 O O     . GLY B 1 106 ? -5.822  -53.345 54.852  1.00 40.41  ? 104 GLY B O     1 
ATOM   5376 N N     . LEU B 1 107 ? -6.596  -51.710 53.572  1.00 55.39  ? 105 LEU B N     1 
ATOM   5377 C CA    . LEU B 1 107 ? -7.328  -52.671 52.701  1.00 53.65  ? 105 LEU B CA    1 
ATOM   5378 C C     . LEU B 1 107 ? -6.311  -53.451 51.870  1.00 46.62  ? 105 LEU B C     1 
ATOM   5379 O O     . LEU B 1 107 ? -5.215  -52.964 51.630  1.00 42.18  ? 105 LEU B O     1 
ATOM   5380 C CB    . LEU B 1 107 ? -8.339  -51.910 51.844  1.00 55.14  ? 105 LEU B CB    1 
ATOM   5381 C CG    . LEU B 1 107 ? -9.401  -51.180 52.662  1.00 54.24  ? 105 LEU B CG    1 
ATOM   5382 C CD1   . LEU B 1 107 ? -9.971  -50.007 51.878  1.00 54.92  ? 105 LEU B CD1   1 
ATOM   5383 C CD2   . LEU B 1 107 ? -10.502 -52.137 53.108  1.00 51.65  ? 105 LEU B CD2   1 
ATOM   5384 N N     . PRO B 1 108 ? -6.627  -54.690 51.432  1.00 43.19  ? 106 PRO B N     1 
ATOM   5385 C CA    . PRO B 1 108 ? -5.646  -55.546 50.769  1.00 44.63  ? 106 PRO B CA    1 
ATOM   5386 C C     . PRO B 1 108 ? -5.144  -55.039 49.408  1.00 47.26  ? 106 PRO B C     1 
ATOM   5387 O O     . PRO B 1 108 ? -5.852  -54.310 48.729  1.00 42.94  ? 106 PRO B O     1 
ATOM   5388 C CB    . PRO B 1 108 ? -6.381  -56.873 50.531  1.00 41.11  ? 106 PRO B CB    1 
ATOM   5389 C CG    . PRO B 1 108 ? -7.592  -56.812 51.442  1.00 43.79  ? 106 PRO B CG    1 
ATOM   5390 C CD    . PRO B 1 108 ? -7.939  -55.337 51.547  1.00 44.28  ? 106 PRO B CD    1 
ATOM   5391 N N     . GLU B 1 109 ? -3.949  -55.492 49.038  1.00 50.14  ? 107 GLU B N     1 
ATOM   5392 C CA    . GLU B 1 109 ? -3.241  -55.148 47.773  1.00 56.76  ? 107 GLU B CA    1 
ATOM   5393 C C     . GLU B 1 109 ? -4.153  -55.465 46.575  1.00 50.72  ? 107 GLU B C     1 
ATOM   5394 O O     . GLU B 1 109 ? -4.209  -54.639 45.650  1.00 42.34  ? 107 GLU B O     1 
ATOM   5395 C CB    . GLU B 1 109 ? -1.915  -55.909 47.698  1.00 55.84  ? 107 GLU B CB    1 
ATOM   5396 C CG    . GLU B 1 109 ? -0.977  -55.407 46.615  1.00 63.98  ? 107 GLU B CG    1 
ATOM   5397 C CD    . GLU B 1 109 ? -0.082  -54.230 46.971  1.00 69.75  ? 107 GLU B CD    1 
ATOM   5398 O OE1   . GLU B 1 109 ? -0.140  -53.746 48.127  1.00 73.49  ? 107 GLU B OE1   1 
ATOM   5399 O OE2   . GLU B 1 109 ? 0.676   -53.797 46.074  1.00 72.18  ? 107 GLU B OE2   1 
ATOM   5400 N N     . SER B 1 110 ? -4.860  -56.599 46.634  1.00 46.95  ? 108 SER B N     1 
ATOM   5401 C CA    . SER B 1 110 ? -5.722  -57.136 45.546  1.00 48.37  ? 108 SER B CA    1 
ATOM   5402 C C     . SER B 1 110 ? -6.905  -56.200 45.252  1.00 45.31  ? 108 SER B C     1 
ATOM   5403 O O     . SER B 1 110 ? -7.498  -56.328 44.149  1.00 41.61  ? 108 SER B O     1 
ATOM   5404 C CB    . SER B 1 110 ? -6.207  -58.512 45.888  1.00 43.48  ? 108 SER B CB    1 
ATOM   5405 O OG    . SER B 1 110 ? -7.066  -58.447 47.007  1.00 49.45  ? 108 SER B OG    1 
ATOM   5406 N N     . LEU B 1 111 ? -7.291  -55.348 46.205  1.00 40.00  ? 109 LEU B N     1 
ATOM   5407 C CA    . LEU B 1 111 ? -8.412  -54.391 46.018  1.00 44.73  ? 109 LEU B CA    1 
ATOM   5408 C C     . LEU B 1 111 ? -7.807  -53.136 45.399  1.00 45.60  ? 109 LEU B C     1 
ATOM   5409 O O     . LEU B 1 111 ? -8.483  -52.528 44.546  1.00 52.54  ? 109 LEU B O     1 
ATOM   5410 C CB    . LEU B 1 111 ? -9.130  -54.108 47.346  1.00 47.65  ? 109 LEU B CB    1 
ATOM   5411 C CG    . LEU B 1 111 ? -10.238 -53.048 47.315  1.00 49.90  ? 109 LEU B CG    1 
ATOM   5412 C CD1   . LEU B 1 111 ? -11.368 -53.468 46.392  1.00 53.27  ? 109 LEU B CD1   1 
ATOM   5413 C CD2   . LEU B 1 111 ? -10.791 -52.777 48.707  1.00 51.06  ? 109 LEU B CD2   1 
ATOM   5414 N N     . GLY B 1 112 ? -6.574  -52.800 45.802  1.00 45.63  ? 110 GLY B N     1 
ATOM   5415 C CA    . GLY B 1 112 ? -5.714  -51.785 45.158  1.00 45.38  ? 110 GLY B CA    1 
ATOM   5416 C C     . GLY B 1 112 ? -5.553  -52.072 43.672  1.00 43.43  ? 110 GLY B C     1 
ATOM   5417 O O     . GLY B 1 112 ? -5.685  -51.120 42.876  1.00 42.07  ? 110 GLY B O     1 
ATOM   5418 N N     . LEU B 1 113 ? -5.354  -53.349 43.328  1.00 36.34  ? 111 LEU B N     1 
ATOM   5419 C CA    . LEU B 1 113 ? -5.047  -53.797 41.967  1.00 43.20  ? 111 LEU B CA    1 
ATOM   5420 C C     . LEU B 1 113 ? -6.293  -53.627 41.087  1.00 43.26  ? 111 LEU B C     1 
ATOM   5421 O O     . LEU B 1 113 ? -6.174  -53.190 39.937  1.00 38.47  ? 111 LEU B O     1 
ATOM   5422 C CB    . LEU B 1 113 ? -4.576  -55.248 42.032  1.00 52.41  ? 111 LEU B CB    1 
ATOM   5423 C CG    . LEU B 1 113 ? -3.712  -55.673 40.844  1.00 57.93  ? 111 LEU B CG    1 
ATOM   5424 C CD1   . LEU B 1 113 ? -2.253  -55.309 41.081  1.00 56.87  ? 111 LEU B CD1   1 
ATOM   5425 C CD2   . LEU B 1 113 ? -3.856  -57.163 40.562  1.00 64.57  ? 111 LEU B CD2   1 
ATOM   5426 N N     . ALA B 1 114 ? -7.475  -53.918 41.604  1.00 40.33  ? 112 ALA B N     1 
ATOM   5427 C CA    . ALA B 1 114 ? -8.728  -53.645 40.884  1.00 39.11  ? 112 ALA B CA    1 
ATOM   5428 C C     . ALA B 1 114 ? -8.825  -52.148 40.535  1.00 41.21  ? 112 ALA B C     1 
ATOM   5429 O O     . ALA B 1 114 ? -9.214  -51.806 39.354  1.00 35.95  ? 112 ALA B O     1 
ATOM   5430 C CB    . ALA B 1 114 ? -9.897  -54.133 41.693  1.00 41.94  ? 112 ALA B CB    1 
ATOM   5431 N N     . ILE B 1 115 ? -8.470  -51.253 41.459  1.00 41.87  ? 113 ILE B N     1 
ATOM   5432 C CA    . ILE B 1 115 ? -8.511  -49.790 41.142  1.00 41.63  ? 113 ILE B CA    1 
ATOM   5433 C C     . ILE B 1 115 ? -7.466  -49.468 40.056  1.00 39.47  ? 113 ILE B C     1 
ATOM   5434 O O     . ILE B 1 115 ? -7.768  -48.658 39.130  1.00 39.32  ? 113 ILE B O     1 
ATOM   5435 C CB    . ILE B 1 115 ? -8.359  -48.916 42.399  1.00 43.20  ? 113 ILE B CB    1 
ATOM   5436 C CG1   . ILE B 1 115 ? -9.478  -49.202 43.401  1.00 43.47  ? 113 ILE B CG1   1 
ATOM   5437 C CG2   . ILE B 1 115 ? -8.322  -47.439 42.026  1.00 43.94  ? 113 ILE B CG2   1 
ATOM   5438 C CD1   . ILE B 1 115 ? -10.861 -48.917 42.872  1.00 40.19  ? 113 ILE B CD1   1 
ATOM   5439 N N     . SER B 1 116 ? -6.277  -50.052 40.158  1.00 37.08  ? 114 SER B N     1 
ATOM   5440 C CA    . SER B 1 116 ? -5.181  -49.874 39.169  1.00 38.36  ? 114 SER B CA    1 
ATOM   5441 C C     . SER B 1 116 ? -5.624  -50.411 37.790  1.00 34.62  ? 114 SER B C     1 
ATOM   5442 O O     . SER B 1 116 ? -5.250  -49.793 36.772  1.00 33.42  ? 114 SER B O     1 
ATOM   5443 C CB    . SER B 1 116 ? -3.875  -50.501 39.673  1.00 36.16  ? 114 SER B CB    1 
ATOM   5444 O OG    . SER B 1 116 ? -3.311  -49.678 40.687  1.00 39.03  ? 114 SER B OG    1 
ATOM   5445 N N     . GLU B 1 117 ? -6.434  -51.479 37.740  1.00 34.73  ? 115 GLU B N     1 
ATOM   5446 C CA    . GLU B 1 117 ? -6.908  -52.060 36.455  1.00 36.41  ? 115 GLU B CA    1 
ATOM   5447 C C     . GLU B 1 117 ? -7.666  -50.968 35.702  1.00 36.30  ? 115 GLU B C     1 
ATOM   5448 O O     . GLU B 1 117 ? -7.426  -50.800 34.482  1.00 31.96  ? 115 GLU B O     1 
ATOM   5449 C CB    . GLU B 1 117 ? -7.803  -53.295 36.607  1.00 36.22  ? 115 GLU B CB    1 
ATOM   5450 C CG    . GLU B 1 117 ? -8.576  -53.602 35.319  1.00 34.31  ? 115 GLU B CG    1 
ATOM   5451 C CD    . GLU B 1 117 ? -9.379  -54.881 35.224  1.00 34.94  ? 115 GLU B CD    1 
ATOM   5452 O OE1   . GLU B 1 117 ? -9.983  -55.075 34.147  1.00 33.00  ? 115 GLU B OE1   1 
ATOM   5453 O OE2   . GLU B 1 117 ? -9.444  -55.663 36.230  1.00 32.95  ? 115 GLU B OE2   1 
ATOM   5454 N N     . MET B 1 118 ? -8.555  -50.277 36.416  1.00 34.90  ? 116 MET B N     1 
ATOM   5455 C CA    . MET B 1 118 ? -9.464  -49.258 35.844  1.00 38.18  ? 116 MET B CA    1 
ATOM   5456 C C     . MET B 1 118 ? -8.664  -47.975 35.578  1.00 38.98  ? 116 MET B C     1 
ATOM   5457 O O     . MET B 1 118 ? -8.909  -47.321 34.544  1.00 37.64  ? 116 MET B O     1 
ATOM   5458 C CB    . MET B 1 118 ? -10.643 -49.018 36.782  1.00 36.15  ? 116 MET B CB    1 
ATOM   5459 C CG    . MET B 1 118 ? -11.527 -50.246 36.870  1.00 42.26  ? 116 MET B CG    1 
ATOM   5460 S SD    . MET B 1 118 ? -13.049 -50.028 37.840  1.00 41.34  ? 116 MET B SD    1 
ATOM   5461 C CE    . MET B 1 118 ? -12.357 -49.958 39.494  1.00 43.70  ? 116 MET B CE    1 
ATOM   5462 N N     . VAL B 1 119 ? -7.714  -47.634 36.442  1.00 35.27  ? 117 VAL B N     1 
ATOM   5463 C CA    . VAL B 1 119 ? -6.895  -46.422 36.199  1.00 35.77  ? 117 VAL B CA    1 
ATOM   5464 C C     . VAL B 1 119 ? -6.089  -46.672 34.920  1.00 37.40  ? 117 VAL B C     1 
ATOM   5465 O O     . VAL B 1 119 ? -5.982  -45.752 34.093  1.00 37.00  ? 117 VAL B O     1 
ATOM   5466 C CB    . VAL B 1 119 ? -6.023  -46.052 37.407  1.00 39.14  ? 117 VAL B CB    1 
ATOM   5467 C CG1   . VAL B 1 119 ? -4.945  -45.031 37.057  1.00 38.40  ? 117 VAL B CG1   1 
ATOM   5468 C CG2   . VAL B 1 119 ? -6.892  -45.542 38.569  1.00 40.80  ? 117 VAL B CG2   1 
ATOM   5469 N N     . GLY B 1 120 ? -5.542  -47.864 34.732  1.00 32.75  ? 118 GLY B N     1 
ATOM   5470 C CA    . GLY B 1 120 ? -4.624  -48.067 33.601  1.00 33.45  ? 118 GLY B CA    1 
ATOM   5471 C C     . GLY B 1 120 ? -5.382  -48.019 32.274  1.00 32.38  ? 118 GLY B C     1 
ATOM   5472 O O     . GLY B 1 120 ? -4.825  -47.521 31.276  1.00 28.43  ? 118 GLY B O     1 
ATOM   5473 N N     . GLN B 1 121 ? -6.595  -48.560 32.277  1.00 30.34  ? 119 GLN B N     1 
ATOM   5474 C CA    . GLN B 1 121 ? -7.494  -48.586 31.102  1.00 33.80  ? 119 GLN B CA    1 
ATOM   5475 C C     . GLN B 1 121 ? -7.875  -47.161 30.703  1.00 35.95  ? 119 GLN B C     1 
ATOM   5476 O O     . GLN B 1 121 ? -7.820  -46.867 29.522  1.00 33.44  ? 119 GLN B O     1 
ATOM   5477 C CB    . GLN B 1 121 ? -8.696  -49.460 31.421  1.00 31.23  ? 119 GLN B CB    1 
ATOM   5478 C CG    . GLN B 1 121 ? -8.291  -50.914 31.490  1.00 31.52  ? 119 GLN B CG    1 
ATOM   5479 C CD    . GLN B 1 121 ? -9.354  -51.806 32.061  1.00 32.02  ? 119 GLN B CD    1 
ATOM   5480 O OE1   . GLN B 1 121 ? -10.476 -51.368 32.315  1.00 31.63  ? 119 GLN B OE1   1 
ATOM   5481 N NE2   . GLN B 1 121 ? -8.997  -53.076 32.232  1.00 32.92  ? 119 GLN B NE2   1 
ATOM   5482 N N     . ALA B 1 122 ? -8.201  -46.314 31.680  1.00 37.66  ? 120 ALA B N     1 
ATOM   5483 C CA    . ALA B 1 122 ? -8.789  -44.974 31.488  1.00 34.47  ? 120 ALA B CA    1 
ATOM   5484 C C     . ALA B 1 122 ? -7.706  -44.019 31.007  1.00 30.82  ? 120 ALA B C     1 
ATOM   5485 O O     . ALA B 1 122 ? -8.001  -43.168 30.179  1.00 34.52  ? 120 ALA B O     1 
ATOM   5486 C CB    . ALA B 1 122 ? -9.414  -44.508 32.785  1.00 37.61  ? 120 ALA B CB    1 
ATOM   5487 N N     . ASN B 1 123 ? -6.516  -44.091 31.587  1.00 27.25  ? 121 ASN B N     1 
ATOM   5488 C CA    . ASN B 1 123 ? -5.417  -43.160 31.232  1.00 27.42  ? 121 ASN B CA    1 
ATOM   5489 C C     . ASN B 1 123 ? -4.121  -43.738 31.797  1.00 30.60  ? 121 ASN B C     1 
ATOM   5490 O O     . ASN B 1 123 ? -3.815  -43.465 32.961  1.00 35.42  ? 121 ASN B O     1 
ATOM   5491 C CB    . ASN B 1 123 ? -5.702  -41.723 31.680  1.00 28.24  ? 121 ASN B CB    1 
ATOM   5492 C CG    . ASN B 1 123 ? -4.742  -40.684 31.142  1.00 28.68  ? 121 ASN B CG    1 
ATOM   5493 O OD1   . ASN B 1 123 ? -5.066  -39.502 31.116  1.00 30.32  ? 121 ASN B OD1   1 
ATOM   5494 N ND2   . ASN B 1 123 ? -3.557  -41.099 30.737  1.00 30.52  ? 121 ASN B ND2   1 
ATOM   5495 N N     . TRP B 1 124 ? -3.399  -44.506 30.982  1.00 30.29  ? 122 TRP B N     1 
ATOM   5496 C CA    . TRP B 1 124 ? -2.174  -45.168 31.498  1.00 32.62  ? 122 TRP B CA    1 
ATOM   5497 C C     . TRP B 1 124 ? -1.111  -44.134 31.866  1.00 30.23  ? 122 TRP B C     1 
ATOM   5498 O O     . TRP B 1 124 ? -0.506  -44.291 32.922  1.00 30.86  ? 122 TRP B O     1 
ATOM   5499 C CB    . TRP B 1 124 ? -1.614  -46.191 30.501  1.00 31.05  ? 122 TRP B CB    1 
ATOM   5500 C CG    . TRP B 1 124 ? -0.393  -46.868 31.038  1.00 33.29  ? 122 TRP B CG    1 
ATOM   5501 C CD1   . TRP B 1 124 ? 0.907   -46.550 30.779  1.00 30.93  ? 122 TRP B CD1   1 
ATOM   5502 C CD2   . TRP B 1 124 ? -0.361  -47.949 31.984  1.00 31.95  ? 122 TRP B CD2   1 
ATOM   5503 N NE1   . TRP B 1 124 ? 1.743   -47.371 31.482  1.00 34.24  ? 122 TRP B NE1   1 
ATOM   5504 C CE2   . TRP B 1 124 ? 0.996   -48.237 32.232  1.00 32.38  ? 122 TRP B CE2   1 
ATOM   5505 C CE3   . TRP B 1 124 ? -1.341  -48.703 32.636  1.00 34.77  ? 122 TRP B CE3   1 
ATOM   5506 C CZ2   . TRP B 1 124 ? 1.391   -49.251 33.101  1.00 35.64  ? 122 TRP B CZ2   1 
ATOM   5507 C CZ3   . TRP B 1 124 ? -0.949  -49.704 33.494  1.00 33.76  ? 122 TRP B CZ3   1 
ATOM   5508 C CH2   . TRP B 1 124 ? 0.399   -49.973 33.721  1.00 35.36  ? 122 TRP B CH2   1 
ATOM   5509 N N     . SER B 1 125 ? -0.887  -43.151 31.002  1.00 27.75  ? 123 SER B N     1 
ATOM   5510 C CA    . SER B 1 125 ? 0.180   -42.145 31.223  1.00 28.84  ? 123 SER B CA    1 
ATOM   5511 C C     . SER B 1 125 ? -0.046  -41.416 32.556  1.00 33.47  ? 123 SER B C     1 
ATOM   5512 O O     . SER B 1 125 ? 0.940   -41.197 33.263  1.00 31.21  ? 123 SER B O     1 
ATOM   5513 C CB    . SER B 1 125 ? 0.253   -41.221 30.041  1.00 28.44  ? 123 SER B CB    1 
ATOM   5514 O OG    . SER B 1 125 ? 0.587   -41.921 28.857  1.00 29.78  ? 123 SER B OG    1 
ATOM   5515 N N     . TRP B 1 126 ? -1.296  -41.095 32.886  1.00 33.07  ? 124 TRP B N     1 
ATOM   5516 C CA    . TRP B 1 126 ? -1.675  -40.435 34.165  1.00 32.87  ? 124 TRP B CA    1 
ATOM   5517 C C     . TRP B 1 126 ? -1.481  -41.423 35.320  1.00 35.60  ? 124 TRP B C     1 
ATOM   5518 O O     . TRP B 1 126 ? -0.940  -41.005 36.370  1.00 40.45  ? 124 TRP B O     1 
ATOM   5519 C CB    . TRP B 1 126 ? -3.117  -39.881 34.137  1.00 31.82  ? 124 TRP B CB    1 
ATOM   5520 C CG    . TRP B 1 126 ? -3.513  -39.138 35.382  1.00 34.21  ? 124 TRP B CG    1 
ATOM   5521 C CD1   . TRP B 1 126 ? -3.452  -37.790 35.623  1.00 34.17  ? 124 TRP B CD1   1 
ATOM   5522 C CD2   . TRP B 1 126 ? -4.005  -39.740 36.597  1.00 30.82  ? 124 TRP B CD2   1 
ATOM   5523 N NE1   . TRP B 1 126 ? -3.863  -37.523 36.911  1.00 35.20  ? 124 TRP B NE1   1 
ATOM   5524 C CE2   . TRP B 1 126 ? -4.220  -38.695 37.524  1.00 32.36  ? 124 TRP B CE2   1 
ATOM   5525 C CE3   . TRP B 1 126 ? -4.290  -41.058 36.977  1.00 30.18  ? 124 TRP B CE3   1 
ATOM   5526 C CZ2   . TRP B 1 126 ? -4.695  -38.934 38.817  1.00 32.93  ? 124 TRP B CZ2   1 
ATOM   5527 C CZ3   . TRP B 1 126 ? -4.773  -41.292 38.253  1.00 32.11  ? 124 TRP B CZ3   1 
ATOM   5528 C CH2   . TRP B 1 126 ? -4.982  -40.240 39.156  1.00 30.69  ? 124 TRP B CH2   1 
ATOM   5529 N N     . GLY B 1 127 ? -1.953  -42.657 35.157  1.00 33.09  ? 125 GLY B N     1 
ATOM   5530 C CA    . GLY B 1 127 ? -1.869  -43.727 36.171  1.00 34.16  ? 125 GLY B CA    1 
ATOM   5531 C C     . GLY B 1 127 ? -0.441  -44.068 36.604  1.00 33.82  ? 125 GLY B C     1 
ATOM   5532 O O     . GLY B 1 127 ? -0.276  -44.615 37.703  1.00 32.54  ? 125 GLY B O     1 
ATOM   5533 N N     . MET B 1 128 ? 0.548   -43.790 35.766  1.00 30.84  ? 126 MET B N     1 
ATOM   5534 C CA    . MET B 1 128 ? 1.962   -44.096 36.087  1.00 36.41  ? 126 MET B CA    1 
ATOM   5535 C C     . MET B 1 128 ? 2.462   -43.190 37.224  1.00 38.50  ? 126 MET B C     1 
ATOM   5536 O O     . MET B 1 128 ? 3.351   -43.624 37.953  1.00 31.65  ? 126 MET B O     1 
ATOM   5537 C CB    . MET B 1 128 ? 2.828   -43.906 34.838  1.00 33.96  ? 126 MET B CB    1 
ATOM   5538 C CG    . MET B 1 128 ? 2.631   -44.977 33.784  1.00 33.87  ? 126 MET B CG    1 
ATOM   5539 S SD    . MET B 1 128 ? 3.538   -44.640 32.256  1.00 36.23  ? 126 MET B SD    1 
ATOM   5540 C CE    . MET B 1 128 ? 5.208   -45.046 32.756  1.00 39.66  ? 126 MET B CE    1 
ATOM   5541 N N     . TYR B 1 129 ? 1.937   -41.974 37.327  1.00 33.23  ? 127 TYR B N     1 
ATOM   5542 C CA    . TYR B 1 129 ? 2.384   -41.044 38.389  1.00 35.84  ? 127 TYR B CA    1 
ATOM   5543 C C     . TYR B 1 129 ? 2.080   -41.716 39.735  1.00 37.28  ? 127 TYR B C     1 
ATOM   5544 O O     . TYR B 1 129 ? 3.022   -41.973 40.483  1.00 33.51  ? 127 TYR B O     1 
ATOM   5545 C CB    . TYR B 1 129 ? 1.800   -39.645 38.163  1.00 36.94  ? 127 TYR B CB    1 
ATOM   5546 C CG    . TYR B 1 129 ? 2.315   -38.919 36.947  1.00 35.45  ? 127 TYR B CG    1 
ATOM   5547 C CD1   . TYR B 1 129 ? 3.453   -38.135 37.012  1.00 33.85  ? 127 TYR B CD1   1 
ATOM   5548 C CD2   . TYR B 1 129 ? 1.655   -39.000 35.733  1.00 38.03  ? 127 TYR B CD2   1 
ATOM   5549 C CE1   . TYR B 1 129 ? 3.930   -37.461 35.902  1.00 33.94  ? 127 TYR B CE1   1 
ATOM   5550 C CE2   . TYR B 1 129 ? 2.117   -38.332 34.613  1.00 35.03  ? 127 TYR B CE2   1 
ATOM   5551 C CZ    . TYR B 1 129 ? 3.260   -37.560 34.697  1.00 36.12  ? 127 TYR B CZ    1 
ATOM   5552 O OH    . TYR B 1 129 ? 3.724   -36.897 33.600  1.00 35.74  ? 127 TYR B OH    1 
ATOM   5553 N N     . PRO B 1 130 ? 0.813   -42.051 40.058  1.00 35.39  ? 128 PRO B N     1 
ATOM   5554 C CA    . PRO B 1 130 ? 0.515   -42.809 41.270  1.00 34.79  ? 128 PRO B CA    1 
ATOM   5555 C C     . PRO B 1 130 ? 1.128   -44.214 41.260  1.00 39.01  ? 128 PRO B C     1 
ATOM   5556 O O     . PRO B 1 130 ? 1.559   -44.646 42.298  1.00 43.02  ? 128 PRO B O     1 
ATOM   5557 C CB    . PRO B 1 130 ? -1.014  -42.936 41.263  1.00 34.35  ? 128 PRO B CB    1 
ATOM   5558 C CG    . PRO B 1 130 ? -1.434  -42.634 39.849  1.00 33.62  ? 128 PRO B CG    1 
ATOM   5559 C CD    . PRO B 1 130 ? -0.392  -41.673 39.329  1.00 35.41  ? 128 PRO B CD    1 
ATOM   5560 N N     . GLY B 1 131 ? 1.161   -44.879 40.103  1.00 35.86  ? 129 GLY B N     1 
ATOM   5561 C CA    . GLY B 1 131 ? 1.653   -46.267 40.012  1.00 33.66  ? 129 GLY B CA    1 
ATOM   5562 C C     . GLY B 1 131 ? 3.074   -46.447 40.503  1.00 37.88  ? 129 GLY B C     1 
ATOM   5563 O O     . GLY B 1 131 ? 3.294   -47.310 41.356  1.00 43.79  ? 129 GLY B O     1 
ATOM   5564 N N     . LEU B 1 132 ? 4.006   -45.665 39.972  1.00 41.26  ? 130 LEU B N     1 
ATOM   5565 C CA    . LEU B 1 132 ? 5.424   -45.748 40.398  1.00 46.94  ? 130 LEU B CA    1 
ATOM   5566 C C     . LEU B 1 132 ? 5.507   -45.469 41.902  1.00 47.10  ? 130 LEU B C     1 
ATOM   5567 O O     . LEU B 1 132 ? 6.129   -46.248 42.623  1.00 50.00  ? 130 LEU B O     1 
ATOM   5568 C CB    . LEU B 1 132 ? 6.241   -44.755 39.571  1.00 47.10  ? 130 LEU B CB    1 
ATOM   5569 C CG    . LEU B 1 132 ? 6.266   -45.003 38.066  1.00 47.92  ? 130 LEU B CG    1 
ATOM   5570 C CD1   . LEU B 1 132 ? 6.428   -43.698 37.309  1.00 47.49  ? 130 LEU B CD1   1 
ATOM   5571 C CD2   . LEU B 1 132 ? 7.381   -45.963 37.698  1.00 56.21  ? 130 LEU B CD2   1 
ATOM   5572 N N     . SER B 1 133 ? 4.851   -44.415 42.353  1.00 51.97  ? 131 SER B N     1 
ATOM   5573 C CA    . SER B 1 133 ? 4.838   -44.085 43.792  1.00 61.26  ? 131 SER B CA    1 
ATOM   5574 C C     . SER B 1 133 ? 4.475   -45.330 44.607  1.00 68.41  ? 131 SER B C     1 
ATOM   5575 O O     . SER B 1 133 ? 5.234   -45.656 45.528  1.00 73.00  ? 131 SER B O     1 
ATOM   5576 C CB    . SER B 1 133 ? 3.891   -42.948 44.029  1.00 55.61  ? 131 SER B CB    1 
ATOM   5577 O OG    . SER B 1 133 ? 4.145   -41.885 43.129  1.00 51.94  ? 131 SER B OG    1 
ATOM   5578 N N     . HIS B 1 134 ? 3.377   -46.007 44.262  1.00 80.87  ? 132 HIS B N     1 
ATOM   5579 C CA    . HIS B 1 134 ? 2.898   -47.210 44.999  1.00 76.75  ? 132 HIS B CA    1 
ATOM   5580 C C     . HIS B 1 134 ? 4.028   -48.217 45.210  1.00 75.00  ? 132 HIS B C     1 
ATOM   5581 O O     . HIS B 1 134 ? 4.007   -48.905 46.248  1.00 66.24  ? 132 HIS B O     1 
ATOM   5582 C CB    . HIS B 1 134 ? 1.736   -47.870 44.252  1.00 74.29  ? 132 HIS B CB    1 
ATOM   5583 C CG    . HIS B 1 134 ? 1.232   -49.105 44.915  1.00 88.64  ? 132 HIS B CG    1 
ATOM   5584 N ND1   . HIS B 1 134 ? 0.456   -49.064 46.056  1.00 100.16 ? 132 HIS B ND1   1 
ATOM   5585 C CD2   . HIS B 1 134 ? 1.392   -50.409 44.612  1.00 88.84  ? 132 HIS B CD2   1 
ATOM   5586 C CE1   . HIS B 1 134 ? 0.157   -50.291 46.425  1.00 91.48  ? 132 HIS B CE1   1 
ATOM   5587 N NE2   . HIS B 1 134 ? 0.718   -51.132 45.555  1.00 91.10  ? 132 HIS B NE2   1 
ATOM   5588 N N     . GLY B 1 135 ? 4.958   -48.298 44.261  1.00 56.41  ? 133 GLY B N     1 
ATOM   5589 C CA    . GLY B 1 135 ? 6.106   -49.208 44.402  1.00 56.11  ? 133 GLY B CA    1 
ATOM   5590 C C     . GLY B 1 135 ? 7.133   -48.734 45.404  1.00 50.26  ? 133 GLY B C     1 
ATOM   5591 O O     . GLY B 1 135 ? 7.583   -49.568 46.180  1.00 58.62  ? 133 GLY B O     1 
ATOM   5592 N N     . ALA B 1 136 ? 7.518   -47.457 45.362  1.00 55.78  ? 134 ALA B N     1 
ATOM   5593 C CA    . ALA B 1 136 ? 8.571   -46.936 46.270  1.00 56.63  ? 134 ALA B CA    1 
ATOM   5594 C C     . ALA B 1 136 ? 8.103   -47.127 47.702  1.00 52.64  ? 134 ALA B C     1 
ATOM   5595 O O     . ALA B 1 136 ? 8.945   -47.287 48.585  1.00 55.34  ? 134 ALA B O     1 
ATOM   5596 C CB    . ALA B 1 136 ? 8.862   -45.489 45.993  1.00 56.86  ? 134 ALA B CB    1 
ATOM   5597 N N     . MET B 1 137 ? 6.795   -47.078 47.904  1.00 52.29  ? 135 MET B N     1 
ATOM   5598 C CA    . MET B 1 137 ? 6.247   -47.368 49.237  1.00 56.04  ? 135 MET B CA    1 
ATOM   5599 C C     . MET B 1 137 ? 6.620   -48.814 49.567  1.00 61.67  ? 135 MET B C     1 
ATOM   5600 O O     . MET B 1 137 ? 7.323   -49.027 50.563  1.00 64.16  ? 135 MET B O     1 
ATOM   5601 C CB    . MET B 1 137 ? 4.729   -47.204 49.192  1.00 54.50  ? 135 MET B CB    1 
ATOM   5602 C CG    . MET B 1 137 ? 4.283   -45.896 48.575  1.00 57.49  ? 135 MET B CG    1 
ATOM   5603 S SD    . MET B 1 137 ? 2.674   -45.353 49.188  1.00 63.81  ? 135 MET B SD    1 
ATOM   5604 C CE    . MET B 1 137 ? 1.881   -44.849 47.664  1.00 65.67  ? 135 MET B CE    1 
ATOM   5605 N N     . ASN B 1 138 ? 6.186   -49.756 48.737  1.00 53.81  ? 136 ASN B N     1 
ATOM   5606 C CA    . ASN B 1 138 ? 6.495   -51.192 48.927  1.00 53.21  ? 136 ASN B CA    1 
ATOM   5607 C C     . ASN B 1 138 ? 7.996   -51.368 49.183  1.00 54.50  ? 136 ASN B C     1 
ATOM   5608 O O     . ASN B 1 138 ? 8.331   -52.242 49.999  1.00 61.22  ? 136 ASN B O     1 
ATOM   5609 C CB    . ASN B 1 138 ? 5.973   -52.039 47.760  1.00 57.42  ? 136 ASN B CB    1 
ATOM   5610 C CG    . ASN B 1 138 ? 4.459   -52.041 47.668  1.00 59.67  ? 136 ASN B CG    1 
ATOM   5611 O OD1   . ASN B 1 138 ? 3.886   -52.449 46.663  1.00 71.56  ? 136 ASN B OD1   1 
ATOM   5612 N ND2   . ASN B 1 138 ? 3.783   -51.554 48.691  1.00 59.36  ? 136 ASN B ND2   1 
ATOM   5613 N N     . THR B 1 139 ? 8.871   -50.560 48.585  1.00 48.86  ? 137 THR B N     1 
ATOM   5614 C CA    . THR B 1 139 ? 10.337  -50.588 48.881  1.00 52.18  ? 137 THR B CA    1 
ATOM   5615 C C     . THR B 1 139 ? 10.668  -50.072 50.296  1.00 57.50  ? 137 THR B C     1 
ATOM   5616 O O     . THR B 1 139 ? 11.485  -50.734 51.005  1.00 56.58  ? 137 THR B O     1 
ATOM   5617 C CB    . THR B 1 139 ? 11.125  -49.691 47.920  1.00 59.53  ? 137 THR B CB    1 
ATOM   5618 O OG1   . THR B 1 139 ? 10.305  -49.515 46.765  1.00 61.32  ? 137 THR B OG1   1 
ATOM   5619 C CG2   . THR B 1 139 ? 12.486  -50.249 47.562  1.00 60.17  ? 137 THR B CG2   1 
ATOM   5620 N N     . LEU B 1 140 ? 10.184  -48.866 50.637  1.00 57.61  ? 138 LEU B N     1 
ATOM   5621 C CA    . LEU B 1 140 ? 10.401  -48.182 51.950  1.00 54.75  ? 138 LEU B CA    1 
ATOM   5622 C C     . LEU B 1 140 ? 9.813   -49.059 53.060  1.00 56.62  ? 138 LEU B C     1 
ATOM   5623 O O     . LEU B 1 140 ? 10.466  -49.221 54.108  1.00 51.25  ? 138 LEU B O     1 
ATOM   5624 C CB    . LEU B 1 140 ? 9.718   -46.808 51.953  1.00 50.80  ? 138 LEU B CB    1 
ATOM   5625 C CG    . LEU B 1 140 ? 10.552  -45.666 51.395  1.00 51.61  ? 138 LEU B CG    1 
ATOM   5626 C CD1   . LEU B 1 140 ? 9.693   -44.431 51.166  1.00 58.48  ? 138 LEU B CD1   1 
ATOM   5627 C CD2   . LEU B 1 140 ? 11.704  -45.348 52.326  1.00 53.22  ? 138 LEU B CD2   1 
ATOM   5628 N N     . HIS B 1 141 ? 8.627   -49.620 52.807  1.00 57.45  ? 139 HIS B N     1 
ATOM   5629 C CA    . HIS B 1 141 ? 7.880   -50.469 53.764  1.00 57.71  ? 139 HIS B CA    1 
ATOM   5630 C C     . HIS B 1 141 ? 8.722   -51.700 54.124  1.00 60.67  ? 139 HIS B C     1 
ATOM   5631 O O     . HIS B 1 141 ? 8.776   -52.047 55.312  1.00 56.75  ? 139 HIS B O     1 
ATOM   5632 C CB    . HIS B 1 141 ? 6.500   -50.848 53.209  1.00 54.12  ? 139 HIS B CB    1 
ATOM   5633 C CG    . HIS B 1 141 ? 5.704   -51.633 54.192  1.00 55.40  ? 139 HIS B CG    1 
ATOM   5634 N ND1   . HIS B 1 141 ? 5.411   -52.975 54.003  1.00 54.09  ? 139 HIS B ND1   1 
ATOM   5635 C CD2   . HIS B 1 141 ? 5.230   -51.291 55.410  1.00 55.52  ? 139 HIS B CD2   1 
ATOM   5636 C CE1   . HIS B 1 141 ? 4.739   -53.416 55.040  1.00 56.43  ? 139 HIS B CE1   1 
ATOM   5637 N NE2   . HIS B 1 141 ? 4.622   -52.395 55.927  1.00 60.23  ? 139 HIS B NE2   1 
ATOM   5638 N N     . ALA B 1 142 ? 9.370   -52.316 53.137  1.00 55.25  ? 140 ALA B N     1 
ATOM   5639 C CA    . ALA B 1 142 ? 10.051  -53.617 53.283  1.00 50.34  ? 140 ALA B CA    1 
ATOM   5640 C C     . ALA B 1 142 ? 11.483  -53.434 53.811  1.00 47.78  ? 140 ALA B C     1 
ATOM   5641 O O     . ALA B 1 142 ? 11.933  -54.357 54.469  1.00 49.42  ? 140 ALA B O     1 
ATOM   5642 C CB    . ALA B 1 142 ? 10.010  -54.367 51.970  1.00 49.53  ? 140 ALA B CB    1 
ATOM   5643 N N     . HIS B 1 143 ? 12.180  -52.325 53.541  1.00 46.97  ? 141 HIS B N     1 
ATOM   5644 C CA    . HIS B 1 143 ? 13.640  -52.196 53.818  1.00 46.37  ? 141 HIS B CA    1 
ATOM   5645 C C     . HIS B 1 143 ? 13.982  -50.882 54.523  1.00 46.82  ? 141 HIS B C     1 
ATOM   5646 O O     . HIS B 1 143 ? 15.141  -50.749 54.927  1.00 44.68  ? 141 HIS B O     1 
ATOM   5647 C CB    . HIS B 1 143 ? 14.472  -52.329 52.526  1.00 48.08  ? 141 HIS B CB    1 
ATOM   5648 C CG    . HIS B 1 143 ? 14.076  -53.507 51.700  1.00 51.56  ? 141 HIS B CG    1 
ATOM   5649 N ND1   . HIS B 1 143 ? 14.593  -54.771 51.918  1.00 50.01  ? 141 HIS B ND1   1 
ATOM   5650 C CD2   . HIS B 1 143 ? 13.189  -53.630 50.681  1.00 51.44  ? 141 HIS B CD2   1 
ATOM   5651 C CE1   . HIS B 1 143 ? 14.046  -55.622 51.065  1.00 51.89  ? 141 HIS B CE1   1 
ATOM   5652 N NE2   . HIS B 1 143 ? 13.179  -54.947 50.294  1.00 48.60  ? 141 HIS B NE2   1 
ATOM   5653 N N     . GLY B 1 144 ? 13.055  -49.935 54.673  1.00 43.55  ? 142 GLY B N     1 
ATOM   5654 C CA    . GLY B 1 144 ? 13.387  -48.649 55.326  1.00 50.28  ? 142 GLY B CA    1 
ATOM   5655 C C     . GLY B 1 144 ? 13.480  -48.779 56.850  1.00 50.60  ? 142 GLY B C     1 
ATOM   5656 O O     . GLY B 1 144 ? 12.738  -49.582 57.411  1.00 45.58  ? 142 GLY B O     1 
ATOM   5657 N N     . THR B 1 145 ? 14.340  -47.992 57.504  1.00 54.85  ? 143 THR B N     1 
ATOM   5658 C CA    . THR B 1 145 ? 14.354  -47.794 58.985  1.00 51.11  ? 143 THR B CA    1 
ATOM   5659 C C     . THR B 1 145 ? 13.057  -47.080 59.370  1.00 55.50  ? 143 THR B C     1 
ATOM   5660 O O     . THR B 1 145 ? 12.520  -46.347 58.530  1.00 60.52  ? 143 THR B O     1 
ATOM   5661 C CB    . THR B 1 145 ? 15.575  -46.976 59.449  1.00 51.76  ? 143 THR B CB    1 
ATOM   5662 O OG1   . THR B 1 145 ? 15.548  -45.610 59.005  1.00 47.39  ? 143 THR B OG1   1 
ATOM   5663 C CG2   . THR B 1 145 ? 16.885  -47.577 58.987  1.00 45.19  ? 143 THR B CG2   1 
ATOM   5664 N N     . ALA B 1 146 ? 12.583  -47.276 60.597  1.00 59.09  ? 144 ALA B N     1 
ATOM   5665 C CA    . ALA B 1 146 ? 11.352  -46.670 61.157  1.00 50.74  ? 144 ALA B CA    1 
ATOM   5666 C C     . ALA B 1 146 ? 11.292  -45.165 60.866  1.00 46.10  ? 144 ALA B C     1 
ATOM   5667 O O     . ALA B 1 146 ? 10.199  -44.689 60.525  1.00 56.35  ? 144 ALA B O     1 
ATOM   5668 C CB    . ALA B 1 146 ? 11.299  -46.944 62.641  1.00 52.63  ? 144 ALA B CB    1 
ATOM   5669 N N     . GLU B 1 147 ? 12.412  -44.452 61.002  1.00 46.17  ? 145 GLU B N     1 
ATOM   5670 C CA    . GLU B 1 147 ? 12.574  -42.989 60.739  1.00 50.53  ? 145 GLU B CA    1 
ATOM   5671 C C     . GLU B 1 147 ? 12.397  -42.679 59.233  1.00 56.23  ? 145 GLU B C     1 
ATOM   5672 O O     . GLU B 1 147 ? 11.771  -41.639 58.889  1.00 43.06  ? 145 GLU B O     1 
ATOM   5673 C CB    . GLU B 1 147 ? 13.969  -42.518 61.166  1.00 56.29  ? 145 GLU B CB    1 
ATOM   5674 C CG    . GLU B 1 147 ? 14.278  -42.713 62.651  1.00 74.01  ? 145 GLU B CG    1 
ATOM   5675 C CD    . GLU B 1 147 ? 14.551  -44.129 63.181  1.00 80.14  ? 145 GLU B CD    1 
ATOM   5676 O OE1   . GLU B 1 147 ? 14.846  -45.061 62.379  1.00 75.22  ? 145 GLU B OE1   1 
ATOM   5677 O OE2   . GLU B 1 147 ? 14.464  -44.307 64.419  1.00 75.89  ? 145 GLU B OE2   1 
ATOM   5678 N N     . GLN B 1 148 ? 12.957  -43.518 58.348  1.00 50.36  ? 146 GLN B N     1 
ATOM   5679 C CA    . GLN B 1 148 ? 12.782  -43.384 56.873  1.00 51.03  ? 146 GLN B CA    1 
ATOM   5680 C C     . GLN B 1 148 ? 11.287  -43.548 56.535  1.00 47.34  ? 146 GLN B C     1 
ATOM   5681 O O     . GLN B 1 148 ? 10.723  -42.664 55.855  1.00 43.67  ? 146 GLN B O     1 
ATOM   5682 C CB    . GLN B 1 148 ? 13.699  -44.377 56.146  1.00 48.94  ? 146 GLN B CB    1 
ATOM   5683 C CG    . GLN B 1 148 ? 15.166  -43.967 56.162  1.00 42.18  ? 146 GLN B CG    1 
ATOM   5684 C CD    . GLN B 1 148 ? 16.078  -45.025 55.584  1.00 44.40  ? 146 GLN B CD    1 
ATOM   5685 O OE1   . GLN B 1 148 ? 15.777  -46.231 55.534  1.00 42.85  ? 146 GLN B OE1   1 
ATOM   5686 N NE2   . GLN B 1 148 ? 17.242  -44.569 55.161  1.00 43.83  ? 146 GLN B NE2   1 
ATOM   5687 N N     . GLN B 1 149 ? 10.651  -44.604 57.044  1.00 43.06  ? 147 GLN B N     1 
ATOM   5688 C CA    . GLN B 1 149 ? 9.183   -44.799 56.960  1.00 45.62  ? 147 GLN B CA    1 
ATOM   5689 C C     . GLN B 1 149 ? 8.411   -43.573 57.477  1.00 48.85  ? 147 GLN B C     1 
ATOM   5690 O O     . GLN B 1 149 ? 7.424   -43.162 56.842  1.00 45.57  ? 147 GLN B O     1 
ATOM   5691 C CB    . GLN B 1 149 ? 8.793   -46.030 57.762  1.00 48.55  ? 147 GLN B CB    1 
ATOM   5692 C CG    . GLN B 1 149 ? 9.548   -47.268 57.325  1.00 48.02  ? 147 GLN B CG    1 
ATOM   5693 C CD    . GLN B 1 149 ? 8.774   -48.542 57.541  1.00 53.38  ? 147 GLN B CD    1 
ATOM   5694 O OE1   . GLN B 1 149 ? 7.551   -48.561 57.699  1.00 63.58  ? 147 GLN B OE1   1 
ATOM   5695 N NE2   . GLN B 1 149 ? 9.497   -49.646 57.494  1.00 59.48  ? 147 GLN B NE2   1 
ATOM   5696 N N     . ALA B 1 150 ? 8.805   -43.015 58.616  1.00 51.90  ? 148 ALA B N     1 
ATOM   5697 C CA    . ALA B 1 150 ? 8.089   -41.886 59.250  1.00 49.81  ? 148 ALA B CA    1 
ATOM   5698 C C     . ALA B 1 150 ? 8.197   -40.647 58.351  1.00 46.72  ? 148 ALA B C     1 
ATOM   5699 O O     . ALA B 1 150 ? 7.214   -39.916 58.225  1.00 46.81  ? 148 ALA B O     1 
ATOM   5700 C CB    . ALA B 1 150 ? 8.643   -41.650 60.637  1.00 47.24  ? 148 ALA B CB    1 
ATOM   5701 N N     . THR B 1 151 ? 9.343   -40.428 57.710  1.00 50.23  ? 149 THR B N     1 
ATOM   5702 C CA    . THR B 1 151 ? 9.630   -39.182 56.943  1.00 52.35  ? 149 THR B CA    1 
ATOM   5703 C C     . THR B 1 151 ? 9.059   -39.279 55.521  1.00 53.42  ? 149 THR B C     1 
ATOM   5704 O O     . THR B 1 151 ? 8.536   -38.246 55.015  1.00 52.94  ? 149 THR B O     1 
ATOM   5705 C CB    . THR B 1 151 ? 11.135  -38.895 56.888  1.00 50.59  ? 149 THR B CB    1 
ATOM   5706 O OG1   . THR B 1 151 ? 11.633  -39.025 58.213  1.00 55.93  ? 149 THR B OG1   1 
ATOM   5707 C CG2   . THR B 1 151 ? 11.484  -37.516 56.379  1.00 54.67  ? 149 THR B CG2   1 
ATOM   5708 N N     . TYR B 1 152 ? 9.176   -40.454 54.896  1.00 46.31  ? 150 TYR B N     1 
ATOM   5709 C CA    . TYR B 1 152 ? 9.060   -40.625 53.419  1.00 46.95  ? 150 TYR B CA    1 
ATOM   5710 C C     . TYR B 1 152 ? 7.755   -41.362 53.072  1.00 47.86  ? 150 TYR B C     1 
ATOM   5711 O O     . TYR B 1 152 ? 6.969   -40.809 52.279  1.00 49.38  ? 150 TYR B O     1 
ATOM   5712 C CB    . TYR B 1 152 ? 10.345  -41.273 52.890  1.00 44.28  ? 150 TYR B CB    1 
ATOM   5713 C CG    . TYR B 1 152 ? 11.528  -40.336 52.942  1.00 41.97  ? 150 TYR B CG    1 
ATOM   5714 C CD1   . TYR B 1 152 ? 11.530  -39.188 52.180  1.00 41.77  ? 150 TYR B CD1   1 
ATOM   5715 C CD2   . TYR B 1 152 ? 12.645  -40.579 53.731  1.00 40.57  ? 150 TYR B CD2   1 
ATOM   5716 C CE1   . TYR B 1 152 ? 12.588  -38.296 52.211  1.00 44.56  ? 150 TYR B CE1   1 
ATOM   5717 C CE2   . TYR B 1 152 ? 13.709  -39.685 53.787  1.00 37.35  ? 150 TYR B CE2   1 
ATOM   5718 C CZ    . TYR B 1 152 ? 13.685  -38.539 53.015  1.00 40.93  ? 150 TYR B CZ    1 
ATOM   5719 O OH    . TYR B 1 152 ? 14.690  -37.611 52.998  1.00 40.10  ? 150 TYR B OH    1 
ATOM   5720 N N     . LEU B 1 153 ? 7.510   -42.521 53.698  1.00 46.18  ? 151 LEU B N     1 
ATOM   5721 C CA    . LEU B 1 153 ? 6.356   -43.421 53.433  1.00 47.96  ? 151 LEU B CA    1 
ATOM   5722 C C     . LEU B 1 153 ? 5.041   -42.713 53.786  1.00 51.14  ? 151 LEU B C     1 
ATOM   5723 O O     . LEU B 1 153 ? 4.082   -42.813 52.999  1.00 56.41  ? 151 LEU B O     1 
ATOM   5724 C CB    . LEU B 1 153 ? 6.538   -44.720 54.227  1.00 47.53  ? 151 LEU B CB    1 
ATOM   5725 C CG    . LEU B 1 153 ? 5.799   -45.942 53.694  1.00 53.12  ? 151 LEU B CG    1 
ATOM   5726 C CD1   . LEU B 1 153 ? 6.436   -47.229 54.180  1.00 60.26  ? 151 LEU B CD1   1 
ATOM   5727 C CD2   . LEU B 1 153 ? 4.370   -45.924 54.141  1.00 64.63  ? 151 LEU B CD2   1 
ATOM   5728 N N     . THR B 1 154 ? 4.972   -42.029 54.926  1.00 52.13  ? 152 THR B N     1 
ATOM   5729 C CA    . THR B 1 154 ? 3.745   -41.316 55.371  1.00 53.18  ? 152 THR B CA    1 
ATOM   5730 C C     . THR B 1 154 ? 3.287   -40.367 54.257  1.00 49.20  ? 152 THR B C     1 
ATOM   5731 O O     . THR B 1 154 ? 2.102   -40.328 53.977  1.00 46.08  ? 152 THR B O     1 
ATOM   5732 C CB    . THR B 1 154 ? 4.005   -40.584 56.688  1.00 58.42  ? 152 THR B CB    1 
ATOM   5733 O OG1   . THR B 1 154 ? 5.166   -39.779 56.465  1.00 66.38  ? 152 THR B OG1   1 
ATOM   5734 C CG2   . THR B 1 154 ? 4.241   -41.538 57.837  1.00 61.49  ? 152 THR B CG2   1 
ATOM   5735 N N     . LYS B 1 155 ? 4.229   -39.650 53.651  1.00 48.62  ? 153 LYS B N     1 
ATOM   5736 C CA    . LYS B 1 155 ? 3.992   -38.644 52.593  1.00 49.17  ? 153 LYS B CA    1 
ATOM   5737 C C     . LYS B 1 155 ? 3.572   -39.322 51.279  1.00 50.16  ? 153 LYS B C     1 
ATOM   5738 O O     . LYS B 1 155 ? 2.722   -38.740 50.583  1.00 49.01  ? 153 LYS B O     1 
ATOM   5739 C CB    . LYS B 1 155 ? 5.264   -37.816 52.418  1.00 50.16  ? 153 LYS B CB    1 
ATOM   5740 C CG    . LYS B 1 155 ? 5.501   -36.787 53.505  1.00 47.62  ? 153 LYS B CG    1 
ATOM   5741 C CD    . LYS B 1 155 ? 4.564   -35.623 53.353  1.00 50.20  ? 153 LYS B CD    1 
ATOM   5742 C CE    . LYS B 1 155 ? 4.989   -34.414 54.144  1.00 52.71  ? 153 LYS B CE    1 
ATOM   5743 N NZ    . LYS B 1 155 ? 3.955   -34.075 55.135  1.00 59.81  ? 153 LYS B NZ    1 
ATOM   5744 N N     . LEU B 1 156 ? 4.150   -40.479 50.935  1.00 47.41  ? 154 LEU B N     1 
ATOM   5745 C CA    . LEU B 1 156 ? 3.783   -41.233 49.699  1.00 50.28  ? 154 LEU B CA    1 
ATOM   5746 C C     . LEU B 1 156 ? 2.385   -41.856 49.851  1.00 49.85  ? 154 LEU B C     1 
ATOM   5747 O O     . LEU B 1 156 ? 1.627   -41.850 48.865  1.00 64.70  ? 154 LEU B O     1 
ATOM   5748 C CB    . LEU B 1 156 ? 4.828   -42.312 49.415  1.00 47.44  ? 154 LEU B CB    1 
ATOM   5749 C CG    . LEU B 1 156 ? 6.242   -41.820 49.100  1.00 47.94  ? 154 LEU B CG    1 
ATOM   5750 C CD1   . LEU B 1 156 ? 7.153   -42.989 48.724  1.00 49.57  ? 154 LEU B CD1   1 
ATOM   5751 C CD2   . LEU B 1 156 ? 6.229   -40.783 47.999  1.00 49.12  ? 154 LEU B CD2   1 
ATOM   5752 N N     . VAL B 1 157 ? 2.045   -42.366 51.037  1.00 47.93  ? 155 VAL B N     1 
ATOM   5753 C CA    . VAL B 1 157 ? 0.746   -43.047 51.342  1.00 43.99  ? 155 VAL B CA    1 
ATOM   5754 C C     . VAL B 1 157 ? -0.384  -42.021 51.205  1.00 44.33  ? 155 VAL B C     1 
ATOM   5755 O O     . VAL B 1 157 ? -1.465  -42.397 50.772  1.00 49.34  ? 155 VAL B O     1 
ATOM   5756 C CB    . VAL B 1 157 ? 0.787   -43.690 52.744  1.00 43.56  ? 155 VAL B CB    1 
ATOM   5757 C CG1   . VAL B 1 157 ? -0.576  -44.118 53.261  1.00 41.92  ? 155 VAL B CG1   1 
ATOM   5758 C CG2   . VAL B 1 157 ? 1.740   -44.868 52.790  1.00 46.79  ? 155 VAL B CG2   1 
ATOM   5759 N N     . SER B 1 158 ? -0.111  -40.764 51.555  1.00 47.47  ? 156 SER B N     1 
ATOM   5760 C CA    . SER B 1 158 ? -1.054  -39.620 51.496  1.00 49.44  ? 156 SER B CA    1 
ATOM   5761 C C     . SER B 1 158 ? -1.162  -39.116 50.045  1.00 55.43  ? 156 SER B C     1 
ATOM   5762 O O     . SER B 1 158 ? -2.174  -38.453 49.708  1.00 56.13  ? 156 SER B O     1 
ATOM   5763 C CB    . SER B 1 158 ? -0.588  -38.530 52.439  1.00 46.84  ? 156 SER B CB    1 
ATOM   5764 O OG    . SER B 1 158 ? 0.437   -37.749 51.847  1.00 47.47  ? 156 SER B OG    1 
ATOM   5765 N N     . GLY B 1 159 ? -0.132  -39.386 49.228  1.00 54.17  ? 157 GLY B N     1 
ATOM   5766 C CA    . GLY B 1 159 ? -0.062  -38.992 47.809  1.00 53.05  ? 157 GLY B CA    1 
ATOM   5767 C C     . GLY B 1 159 ? 0.478   -37.586 47.616  1.00 45.95  ? 157 GLY B C     1 
ATOM   5768 O O     . GLY B 1 159 ? 0.662   -37.201 46.447  1.00 39.14  ? 157 GLY B O     1 
ATOM   5769 N N     . GLU B 1 160 ? 0.720   -36.846 48.704  1.00 42.37  ? 158 GLU B N     1 
ATOM   5770 C CA    . GLU B 1 160 ? 1.231   -35.448 48.663  1.00 46.05  ? 158 GLU B CA    1 
ATOM   5771 C C     . GLU B 1 160 ? 2.623   -35.471 48.032  1.00 42.03  ? 158 GLU B C     1 
ATOM   5772 O O     . GLU B 1 160 ? 3.021   -34.472 47.425  1.00 43.10  ? 158 GLU B O     1 
ATOM   5773 C CB    . GLU B 1 160 ? 1.394   -34.818 50.051  1.00 54.35  ? 158 GLU B CB    1 
ATOM   5774 C CG    . GLU B 1 160 ? 0.133   -34.615 50.876  1.00 61.74  ? 158 GLU B CG    1 
ATOM   5775 C CD    . GLU B 1 160 ? 0.477   -34.512 52.365  1.00 72.68  ? 158 GLU B CD    1 
ATOM   5776 O OE1   . GLU B 1 160 ? 1.046   -33.476 52.787  1.00 70.67  ? 158 GLU B OE1   1 
ATOM   5777 O OE2   . GLU B 1 160 ? 0.248   -35.496 53.103  1.00 80.37  ? 158 GLU B OE2   1 
ATOM   5778 N N     . TRP B 1 161 ? 3.345   -36.576 48.208  1.00 42.52  ? 159 TRP B N     1 
ATOM   5779 C CA    . TRP B 1 161 ? 4.674   -36.838 47.597  1.00 43.69  ? 159 TRP B CA    1 
ATOM   5780 C C     . TRP B 1 161 ? 4.570   -38.045 46.648  1.00 41.84  ? 159 TRP B C     1 
ATOM   5781 O O     . TRP B 1 161 ? 3.855   -39.015 46.981  1.00 35.84  ? 159 TRP B O     1 
ATOM   5782 C CB    . TRP B 1 161 ? 5.709   -37.101 48.702  1.00 50.18  ? 159 TRP B CB    1 
ATOM   5783 C CG    . TRP B 1 161 ? 6.095   -35.929 49.558  1.00 51.54  ? 159 TRP B CG    1 
ATOM   5784 C CD1   . TRP B 1 161 ? 5.526   -34.688 49.596  1.00 49.29  ? 159 TRP B CD1   1 
ATOM   5785 C CD2   . TRP B 1 161 ? 7.176   -35.901 50.504  1.00 49.13  ? 159 TRP B CD2   1 
ATOM   5786 N NE1   . TRP B 1 161 ? 6.196   -33.885 50.474  1.00 46.73  ? 159 TRP B NE1   1 
ATOM   5787 C CE2   . TRP B 1 161 ? 7.204   -34.603 51.053  1.00 49.80  ? 159 TRP B CE2   1 
ATOM   5788 C CE3   . TRP B 1 161 ? 8.127   -36.837 50.923  1.00 50.82  ? 159 TRP B CE3   1 
ATOM   5789 C CZ2   . TRP B 1 161 ? 8.138   -34.225 52.008  1.00 48.41  ? 159 TRP B CZ2   1 
ATOM   5790 C CZ3   . TRP B 1 161 ? 9.040   -36.468 51.884  1.00 50.60  ? 159 TRP B CZ3   1 
ATOM   5791 C CH2   . TRP B 1 161 ? 9.034   -35.182 52.421  1.00 49.84  ? 159 TRP B CH2   1 
ATOM   5792 N N     . THR B 1 162 ? 5.344   -38.002 45.564  1.00 39.83  ? 160 THR B N     1 
ATOM   5793 C CA    . THR B 1 162 ? 5.371   -39.093 44.561  1.00 41.24  ? 160 THR B CA    1 
ATOM   5794 C C     . THR B 1 162 ? 6.713   -39.818 44.623  1.00 41.14  ? 160 THR B C     1 
ATOM   5795 O O     . THR B 1 162 ? 7.670   -39.231 45.140  1.00 44.56  ? 160 THR B O     1 
ATOM   5796 C CB    . THR B 1 162 ? 5.179   -38.534 43.146  1.00 37.65  ? 160 THR B CB    1 
ATOM   5797 O OG1   . THR B 1 162 ? 6.128   -37.491 42.936  1.00 37.11  ? 160 THR B OG1   1 
ATOM   5798 C CG2   . THR B 1 162 ? 3.781   -38.009 42.908  1.00 40.83  ? 160 THR B CG2   1 
ATOM   5799 N N     . GLY B 1 163 ? 6.771   -41.032 44.082  1.00 39.86  ? 161 GLY B N     1 
ATOM   5800 C CA    . GLY B 1 163 ? 8.016   -41.814 44.066  1.00 39.55  ? 161 GLY B CA    1 
ATOM   5801 C C     . GLY B 1 163 ? 8.439   -42.317 42.696  1.00 40.45  ? 161 GLY B C     1 
ATOM   5802 O O     . GLY B 1 163 ? 7.556   -42.573 41.874  1.00 40.68  ? 161 GLY B O     1 
ATOM   5803 N N     . THR B 1 164 ? 9.743   -42.438 42.463  1.00 39.68  ? 162 THR B N     1 
ATOM   5804 C CA    . THR B 1 164 ? 10.335  -42.992 41.222  1.00 44.07  ? 162 THR B CA    1 
ATOM   5805 C C     . THR B 1 164 ? 11.302  -44.121 41.569  1.00 46.07  ? 162 THR B C     1 
ATOM   5806 O O     . THR B 1 164 ? 11.668  -44.265 42.758  1.00 49.54  ? 162 THR B O     1 
ATOM   5807 C CB    . THR B 1 164 ? 11.125  -41.927 40.452  1.00 46.10  ? 162 THR B CB    1 
ATOM   5808 O OG1   . THR B 1 164 ? 12.377  -41.754 41.125  1.00 45.44  ? 162 THR B OG1   1 
ATOM   5809 C CG2   . THR B 1 164 ? 10.372  -40.620 40.319  1.00 41.32  ? 162 THR B CG2   1 
ATOM   5810 N N     . MET B 1 165 ? 11.710  -44.863 40.550  1.00 41.58  ? 163 MET B N     1 
ATOM   5811 C CA    . MET B 1 165 ? 12.791  -45.875 40.609  1.00 46.35  ? 163 MET B CA    1 
ATOM   5812 C C     . MET B 1 165 ? 13.849  -45.458 39.582  1.00 44.75  ? 163 MET B C     1 
ATOM   5813 O O     . MET B 1 165 ? 13.505  -45.346 38.406  1.00 43.57  ? 163 MET B O     1 
ATOM   5814 C CB    . MET B 1 165 ? 12.256  -47.298 40.368  1.00 50.06  ? 163 MET B CB    1 
ATOM   5815 C CG    . MET B 1 165 ? 11.419  -47.500 39.087  1.00 58.97  ? 163 MET B CG    1 
ATOM   5816 S SD    . MET B 1 165 ? 10.582  -49.135 39.003  1.00 67.39  ? 163 MET B SD    1 
ATOM   5817 C CE    . MET B 1 165 ? 8.863   -48.651 39.013  1.00 73.83  ? 163 MET B CE    1 
ATOM   5818 N N     . CYS B 1 166 ? 15.058  -45.124 40.041  1.00 46.51  ? 164 CYS B N     1 
ATOM   5819 C CA    . CYS B 1 166 ? 16.173  -44.597 39.210  1.00 45.45  ? 164 CYS B CA    1 
ATOM   5820 C C     . CYS B 1 166 ? 17.264  -45.665 39.061  1.00 44.50  ? 164 CYS B C     1 
ATOM   5821 O O     . CYS B 1 166 ? 18.222  -45.669 39.828  1.00 47.91  ? 164 CYS B O     1 
ATOM   5822 C CB    . CYS B 1 166 ? 16.746  -43.308 39.781  1.00 43.16  ? 164 CYS B CB    1 
ATOM   5823 S SG    . CYS B 1 166 ? 15.535  -41.968 39.847  1.00 40.97  ? 164 CYS B SG    1 
ATOM   5824 N N     . LEU B 1 167 ? 17.115  -46.530 38.071  1.00 39.02  ? 165 LEU B N     1 
ATOM   5825 C CA    . LEU B 1 167 ? 18.111  -47.570 37.737  1.00 40.06  ? 165 LEU B CA    1 
ATOM   5826 C C     . LEU B 1 167 ? 18.905  -47.146 36.487  1.00 40.60  ? 165 LEU B C     1 
ATOM   5827 O O     . LEU B 1 167 ? 20.152  -47.010 36.555  1.00 40.90  ? 165 LEU B O     1 
ATOM   5828 C CB    . LEU B 1 167 ? 17.342  -48.874 37.504  1.00 42.16  ? 165 LEU B CB    1 
ATOM   5829 C CG    . LEU B 1 167 ? 16.443  -49.348 38.645  1.00 45.41  ? 165 LEU B CG    1 
ATOM   5830 C CD1   . LEU B 1 167 ? 15.173  -48.523 38.764  1.00 48.43  ? 165 LEU B CD1   1 
ATOM   5831 C CD2   . LEU B 1 167 ? 16.081  -50.812 38.448  1.00 45.21  ? 165 LEU B CD2   1 
ATOM   5832 N N     . THR B 1 168 ? 18.173  -47.010 35.385  1.00 41.46  ? 166 THR B N     1 
ATOM   5833 C CA    . THR B 1 168 ? 18.759  -46.888 34.029  1.00 36.80  ? 166 THR B CA    1 
ATOM   5834 C C     . THR B 1 168 ? 19.738  -45.749 33.755  1.00 36.82  ? 166 THR B C     1 
ATOM   5835 O O     . THR B 1 168 ? 19.453  -44.616 34.136  1.00 34.25  ? 166 THR B O     1 
ATOM   5836 C CB    . THR B 1 168 ? 17.619  -46.955 32.994  1.00 37.95  ? 166 THR B CB    1 
ATOM   5837 O OG1   . THR B 1 168 ? 16.807  -48.098 33.257  1.00 32.25  ? 166 THR B OG1   1 
ATOM   5838 C CG2   . THR B 1 168 ? 18.117  -47.006 31.567  1.00 39.07  ? 166 THR B CG2   1 
ATOM   5839 N N     . GLU B 1 169 ? 20.857  -46.100 33.130  1.00 36.80  ? 167 GLU B N     1 
ATOM   5840 C CA    . GLU B 1 169 ? 21.875  -45.146 32.607  1.00 37.01  ? 167 GLU B CA    1 
ATOM   5841 C C     . GLU B 1 169 ? 22.014  -45.386 31.092  1.00 38.72  ? 167 GLU B C     1 
ATOM   5842 O O     . GLU B 1 169 ? 21.525  -46.407 30.583  1.00 36.10  ? 167 GLU B O     1 
ATOM   5843 C CB    . GLU B 1 169 ? 23.180  -45.355 33.380  1.00 35.96  ? 167 GLU B CB    1 
ATOM   5844 C CG    . GLU B 1 169 ? 23.052  -45.061 34.870  1.00 38.52  ? 167 GLU B CG    1 
ATOM   5845 C CD    . GLU B 1 169 ? 24.236  -45.429 35.772  1.00 40.49  ? 167 GLU B CD    1 
ATOM   5846 O OE1   . GLU B 1 169 ? 24.049  -45.420 37.022  1.00 49.69  ? 167 GLU B OE1   1 
ATOM   5847 O OE2   . GLU B 1 169 ? 25.348  -45.710 35.261  1.00 35.51  ? 167 GLU B OE2   1 
ATOM   5848 N N     . PRO B 1 170 ? 22.658  -44.474 30.312  1.00 34.65  ? 168 PRO B N     1 
ATOM   5849 C CA    . PRO B 1 170 ? 22.764  -44.621 28.856  1.00 35.59  ? 168 PRO B CA    1 
ATOM   5850 C C     . PRO B 1 170 ? 23.318  -45.987 28.434  1.00 39.21  ? 168 PRO B C     1 
ATOM   5851 O O     . PRO B 1 170 ? 22.778  -46.532 27.526  1.00 34.35  ? 168 PRO B O     1 
ATOM   5852 C CB    . PRO B 1 170 ? 23.714  -43.505 28.436  1.00 30.36  ? 168 PRO B CB    1 
ATOM   5853 C CG    . PRO B 1 170 ? 23.426  -42.439 29.456  1.00 33.27  ? 168 PRO B CG    1 
ATOM   5854 C CD    . PRO B 1 170 ? 23.266  -43.213 30.752  1.00 36.65  ? 168 PRO B CD    1 
ATOM   5855 N N     . HIS B 1 171 ? 24.328  -46.503 29.143  1.00 39.08  ? 169 HIS B N     1 
ATOM   5856 C CA    . HIS B 1 171 ? 25.093  -47.719 28.759  1.00 39.41  ? 169 HIS B CA    1 
ATOM   5857 C C     . HIS B 1 171 ? 24.431  -48.986 29.349  1.00 39.67  ? 169 HIS B C     1 
ATOM   5858 O O     . HIS B 1 171 ? 24.872  -50.095 28.985  1.00 39.87  ? 169 HIS B O     1 
ATOM   5859 C CB    . HIS B 1 171 ? 26.567  -47.568 29.177  1.00 37.64  ? 169 HIS B CB    1 
ATOM   5860 C CG    . HIS B 1 171 ? 26.705  -47.565 30.660  1.00 42.83  ? 169 HIS B CG    1 
ATOM   5861 N ND1   . HIS B 1 171 ? 26.329  -46.464 31.440  1.00 47.25  ? 169 HIS B ND1   1 
ATOM   5862 C CD2   . HIS B 1 171 ? 27.088  -48.533 31.522  1.00 45.04  ? 169 HIS B CD2   1 
ATOM   5863 C CE1   . HIS B 1 171 ? 26.474  -46.765 32.710  1.00 49.75  ? 169 HIS B CE1   1 
ATOM   5864 N NE2   . HIS B 1 171 ? 26.946  -48.025 32.788  1.00 54.83  ? 169 HIS B NE2   1 
ATOM   5865 N N     . CYS B 1 172 ? 23.493  -48.833 30.286  1.00 39.43  ? 170 CYS B N     1 
ATOM   5866 C CA    . CYS B 1 172 ? 22.955  -50.023 31.005  1.00 40.21  ? 170 CYS B CA    1 
ATOM   5867 C C     . CYS B 1 172 ? 21.449  -49.936 31.290  1.00 35.57  ? 170 CYS B C     1 
ATOM   5868 O O     . CYS B 1 172 ? 21.010  -48.918 31.827  1.00 43.41  ? 170 CYS B O     1 
ATOM   5869 C CB    . CYS B 1 172 ? 23.729  -50.234 32.308  1.00 42.12  ? 170 CYS B CB    1 
ATOM   5870 S SG    . CYS B 1 172 ? 23.575  -48.912 33.527  1.00 42.97  ? 170 CYS B SG    1 
ATOM   5871 N N     . GLY B 1 173 ? 20.703  -50.985 30.956  1.00 34.89  ? 171 GLY B N     1 
ATOM   5872 C CA    . GLY B 1 173 ? 19.263  -51.060 31.264  1.00 36.63  ? 171 GLY B CA    1 
ATOM   5873 C C     . GLY B 1 173 ? 18.960  -52.419 31.852  1.00 34.68  ? 171 GLY B C     1 
ATOM   5874 O O     . GLY B 1 173 ? 18.503  -52.477 32.995  1.00 37.83  ? 171 GLY B O     1 
ATOM   5875 N N     . THR B 1 174 ? 19.241  -53.477 31.105  1.00 35.14  ? 172 THR B N     1 
ATOM   5876 C CA    . THR B 1 174 ? 19.119  -54.835 31.681  1.00 34.72  ? 172 THR B CA    1 
ATOM   5877 C C     . THR B 1 174 ? 20.341  -55.067 32.574  1.00 33.61  ? 172 THR B C     1 
ATOM   5878 O O     . THR B 1 174 ? 20.151  -55.518 33.703  1.00 31.76  ? 172 THR B O     1 
ATOM   5879 C CB    . THR B 1 174 ? 19.005  -55.890 30.578  1.00 35.20  ? 172 THR B CB    1 
ATOM   5880 O OG1   . THR B 1 174 ? 17.841  -55.627 29.796  1.00 35.61  ? 172 THR B OG1   1 
ATOM   5881 C CG2   . THR B 1 174 ? 18.967  -57.298 31.130  1.00 35.15  ? 172 THR B CG2   1 
ATOM   5882 N N     . ASP B 1 175 ? 21.532  -54.705 32.094  1.00 35.26  ? 173 ASP B N     1 
ATOM   5883 C CA    . ASP B 1 175 ? 22.807  -54.945 32.821  1.00 38.21  ? 173 ASP B CA    1 
ATOM   5884 C C     . ASP B 1 175 ? 23.036  -53.876 33.893  1.00 39.44  ? 173 ASP B C     1 
ATOM   5885 O O     . ASP B 1 175 ? 23.863  -52.988 33.663  1.00 43.35  ? 173 ASP B O     1 
ATOM   5886 C CB    . ASP B 1 175 ? 23.965  -55.019 31.825  1.00 40.92  ? 173 ASP B CB    1 
ATOM   5887 C CG    . ASP B 1 175 ? 25.154  -55.827 32.308  1.00 40.55  ? 173 ASP B CG    1 
ATOM   5888 O OD1   . ASP B 1 175 ? 25.258  -56.043 33.523  1.00 40.25  ? 173 ASP B OD1   1 
ATOM   5889 O OD2   . ASP B 1 175 ? 25.968  -56.225 31.461  1.00 39.21  ? 173 ASP B OD2   1 
ATOM   5890 N N     . LEU B 1 176 ? 22.358  -53.990 35.032  1.00 41.67  ? 174 LEU B N     1 
ATOM   5891 C CA    . LEU B 1 176 ? 22.460  -52.985 36.124  1.00 42.43  ? 174 LEU B CA    1 
ATOM   5892 C C     . LEU B 1 176 ? 23.820  -53.099 36.818  1.00 40.34  ? 174 LEU B C     1 
ATOM   5893 O O     . LEU B 1 176 ? 24.276  -52.098 37.359  1.00 40.21  ? 174 LEU B O     1 
ATOM   5894 C CB    . LEU B 1 176 ? 21.295  -53.213 37.088  1.00 44.89  ? 174 LEU B CB    1 
ATOM   5895 C CG    . LEU B 1 176 ? 19.906  -52.968 36.504  1.00 47.38  ? 174 LEU B CG    1 
ATOM   5896 C CD1   . LEU B 1 176 ? 18.831  -53.514 37.427  1.00 53.13  ? 174 LEU B CD1   1 
ATOM   5897 C CD2   . LEU B 1 176 ? 19.685  -51.487 36.250  1.00 46.68  ? 174 LEU B CD2   1 
ATOM   5898 N N     . GLY B 1 177 ? 24.460  -54.260 36.736  1.00 41.83  ? 175 GLY B N     1 
ATOM   5899 C CA    . GLY B 1 177 ? 25.812  -54.431 37.299  1.00 43.15  ? 175 GLY B CA    1 
ATOM   5900 C C     . GLY B 1 177 ? 26.815  -53.454 36.718  1.00 42.01  ? 175 GLY B C     1 
ATOM   5901 O O     . GLY B 1 177 ? 27.816  -53.195 37.383  1.00 39.52  ? 175 GLY B O     1 
ATOM   5902 N N     . MET B 1 178 ? 26.543  -52.918 35.528  1.00 41.75  ? 176 MET B N     1 
ATOM   5903 C CA    . MET B 1 178 ? 27.476  -51.980 34.848  1.00 38.92  ? 176 MET B CA    1 
ATOM   5904 C C     . MET B 1 178 ? 27.198  -50.537 35.282  1.00 35.90  ? 176 MET B C     1 
ATOM   5905 O O     . MET B 1 178 ? 27.944  -49.648 34.859  1.00 33.99  ? 176 MET B O     1 
ATOM   5906 C CB    . MET B 1 178 ? 27.336  -52.076 33.328  1.00 39.10  ? 176 MET B CB    1 
ATOM   5907 C CG    . MET B 1 178 ? 27.956  -53.310 32.720  1.00 42.35  ? 176 MET B CG    1 
ATOM   5908 S SD    . MET B 1 178 ? 28.338  -53.049 30.973  1.00 49.19  ? 176 MET B SD    1 
ATOM   5909 C CE    . MET B 1 178 ? 26.698  -52.764 30.313  1.00 46.53  ? 176 MET B CE    1 
ATOM   5910 N N     . LEU B 1 179 ? 26.164  -50.323 36.093  1.00 40.07  ? 177 LEU B N     1 
ATOM   5911 C CA    . LEU B 1 179 ? 25.794  -48.946 36.519  1.00 44.33  ? 177 LEU B CA    1 
ATOM   5912 C C     . LEU B 1 179 ? 27.018  -48.252 37.121  1.00 47.31  ? 177 LEU B C     1 
ATOM   5913 O O     . LEU B 1 179 ? 27.887  -48.958 37.641  1.00 47.47  ? 177 LEU B O     1 
ATOM   5914 C CB    . LEU B 1 179 ? 24.600  -48.974 37.477  1.00 48.79  ? 177 LEU B CB    1 
ATOM   5915 C CG    . LEU B 1 179 ? 24.910  -49.036 38.972  1.00 50.20  ? 177 LEU B CG    1 
ATOM   5916 C CD1   . LEU B 1 179 ? 25.061  -47.643 39.560  1.00 51.85  ? 177 LEU B CD1   1 
ATOM   5917 C CD2   . LEU B 1 179 ? 23.807  -49.779 39.699  1.00 52.74  ? 177 LEU B CD2   1 
ATOM   5918 N N     . ARG B 1 180 ? 27.050  -46.924 37.089  1.00 50.52  ? 178 ARG B N     1 
ATOM   5919 C CA    . ARG B 1 180 ? 28.258  -46.149 37.502  1.00 51.10  ? 178 ARG B CA    1 
ATOM   5920 C C     . ARG B 1 180 ? 27.916  -44.902 38.360  1.00 47.06  ? 178 ARG B C     1 
ATOM   5921 O O     . ARG B 1 180 ? 28.851  -44.223 38.834  1.00 46.10  ? 178 ARG B O     1 
ATOM   5922 C CB    . ARG B 1 180 ? 29.030  -45.723 36.248  1.00 53.27  ? 178 ARG B CB    1 
ATOM   5923 C CG    . ARG B 1 180 ? 29.859  -46.797 35.552  1.00 56.19  ? 178 ARG B CG    1 
ATOM   5924 C CD    . ARG B 1 180 ? 30.886  -46.161 34.606  1.00 61.08  ? 178 ARG B CD    1 
ATOM   5925 N NE    . ARG B 1 180 ? 30.566  -44.745 34.346  1.00 77.14  ? 178 ARG B NE    1 
ATOM   5926 C CZ    . ARG B 1 180 ? 31.296  -43.652 34.697  1.00 75.78  ? 178 ARG B CZ    1 
ATOM   5927 N NH1   . ARG B 1 180 ? 32.478  -43.743 35.292  1.00 79.31  ? 178 ARG B NH1   1 
ATOM   5928 N NH2   . ARG B 1 180 ? 30.822  -42.441 34.444  1.00 65.67  ? 178 ARG B NH2   1 
ATOM   5929 N N     . THR B 1 181 ? 26.643  -44.574 38.577  1.00 46.42  ? 179 THR B N     1 
ATOM   5930 C CA    . THR B 1 181 ? 26.225  -43.534 39.557  1.00 49.74  ? 179 THR B CA    1 
ATOM   5931 C C     . THR B 1 181 ? 26.907  -43.864 40.897  1.00 47.48  ? 179 THR B C     1 
ATOM   5932 O O     . THR B 1 181 ? 26.863  -45.041 41.319  1.00 42.67  ? 179 THR B O     1 
ATOM   5933 C CB    . THR B 1 181 ? 24.691  -43.436 39.632  1.00 52.18  ? 179 THR B CB    1 
ATOM   5934 O OG1   . THR B 1 181 ? 24.225  -42.952 38.372  1.00 51.60  ? 179 THR B OG1   1 
ATOM   5935 C CG2   . THR B 1 181 ? 24.187  -42.515 40.720  1.00 52.11  ? 179 THR B CG2   1 
ATOM   5936 N N     . LYS B 1 182 ? 27.500  -42.854 41.532  1.00 46.45  ? 180 LYS B N     1 
ATOM   5937 C CA    . LYS B 1 182 ? 28.317  -42.982 42.770  1.00 48.05  ? 180 LYS B CA    1 
ATOM   5938 C C     . LYS B 1 182 ? 27.533  -42.458 43.972  1.00 47.30  ? 180 LYS B C     1 
ATOM   5939 O O     . LYS B 1 182 ? 26.925  -41.379 43.848  1.00 45.37  ? 180 LYS B O     1 
ATOM   5940 C CB    . LYS B 1 182 ? 29.620  -42.191 42.615  1.00 48.32  ? 180 LYS B CB    1 
ATOM   5941 C CG    . LYS B 1 182 ? 30.661  -42.893 41.764  1.00 51.34  ? 180 LYS B CG    1 
ATOM   5942 C CD    . LYS B 1 182 ? 31.847  -42.036 41.429  1.00 59.18  ? 180 LYS B CD    1 
ATOM   5943 C CE    . LYS B 1 182 ? 31.803  -41.513 40.008  1.00 69.94  ? 180 LYS B CE    1 
ATOM   5944 N NZ    . LYS B 1 182 ? 33.083  -41.750 39.298  1.00 72.96  ? 180 LYS B NZ    1 
ATOM   5945 N N     . ALA B 1 183 ? 27.563  -43.195 45.086  1.00 45.82  ? 181 ALA B N     1 
ATOM   5946 C CA    . ALA B 1 183 ? 27.230  -42.701 46.442  1.00 47.62  ? 181 ALA B CA    1 
ATOM   5947 C C     . ALA B 1 183 ? 28.529  -42.587 47.255  1.00 51.52  ? 181 ALA B C     1 
ATOM   5948 O O     . ALA B 1 183 ? 29.128  -43.650 47.510  1.00 46.07  ? 181 ALA B O     1 
ATOM   5949 C CB    . ALA B 1 183 ? 26.230  -43.614 47.108  1.00 45.20  ? 181 ALA B CB    1 
ATOM   5950 N N     . GLU B 1 184 ? 28.951  -41.351 47.582  1.00 51.53  ? 182 GLU B N     1 
ATOM   5951 C CA    . GLU B 1 184 ? 30.130  -41.027 48.428  1.00 57.18  ? 182 GLU B CA    1 
ATOM   5952 C C     . GLU B 1 184 ? 29.698  -40.725 49.868  1.00 60.49  ? 182 GLU B C     1 
ATOM   5953 O O     . GLU B 1 184 ? 29.095  -39.682 50.146  1.00 59.47  ? 182 GLU B O     1 
ATOM   5954 C CB    . GLU B 1 184 ? 30.898  -39.847 47.850  1.00 59.18  ? 182 GLU B CB    1 
ATOM   5955 C CG    . GLU B 1 184 ? 32.393  -39.969 48.088  1.00 72.98  ? 182 GLU B CG    1 
ATOM   5956 C CD    . GLU B 1 184 ? 33.237  -38.974 47.305  1.00 83.21  ? 182 GLU B CD    1 
ATOM   5957 O OE1   . GLU B 1 184 ? 34.406  -38.738 47.696  1.00 86.23  ? 182 GLU B OE1   1 
ATOM   5958 O OE2   . GLU B 1 184 ? 32.728  -38.434 46.302  1.00 90.58  ? 182 GLU B OE2   1 
ATOM   5959 N N     . PRO B 1 185 ? 30.032  -41.607 50.841  1.00 58.67  ? 183 PRO B N     1 
ATOM   5960 C CA    . PRO B 1 185 ? 29.548  -41.469 52.216  1.00 59.52  ? 183 PRO B CA    1 
ATOM   5961 C C     . PRO B 1 185 ? 30.087  -40.184 52.854  1.00 58.62  ? 183 PRO B C     1 
ATOM   5962 O O     . PRO B 1 185 ? 31.209  -39.800 52.547  1.00 51.97  ? 183 PRO B O     1 
ATOM   5963 C CB    . PRO B 1 185 ? 30.106  -42.693 52.952  1.00 57.88  ? 183 PRO B CB    1 
ATOM   5964 C CG    . PRO B 1 185 ? 31.290  -43.125 52.113  1.00 60.80  ? 183 PRO B CG    1 
ATOM   5965 C CD    . PRO B 1 185 ? 30.952  -42.744 50.689  1.00 59.58  ? 183 PRO B CD    1 
ATOM   5966 N N     . GLN B 1 186 ? 29.272  -39.532 53.680  1.00 61.76  ? 184 GLN B N     1 
ATOM   5967 C CA    . GLN B 1 186 ? 29.636  -38.243 54.330  1.00 63.65  ? 184 GLN B CA    1 
ATOM   5968 C C     . GLN B 1 186 ? 29.717  -38.470 55.850  1.00 64.26  ? 184 GLN B C     1 
ATOM   5969 O O     . GLN B 1 186 ? 28.991  -39.368 56.343  1.00 59.53  ? 184 GLN B O     1 
ATOM   5970 C CB    . GLN B 1 186 ? 28.620  -37.166 53.942  1.00 58.74  ? 184 GLN B CB    1 
ATOM   5971 C CG    . GLN B 1 186 ? 28.503  -36.946 52.449  1.00 57.39  ? 184 GLN B CG    1 
ATOM   5972 C CD    . GLN B 1 186 ? 29.612  -36.093 51.877  1.00 59.70  ? 184 GLN B CD    1 
ATOM   5973 O OE1   . GLN B 1 186 ? 29.720  -34.904 52.155  1.00 51.59  ? 184 GLN B OE1   1 
ATOM   5974 N NE2   . GLN B 1 186 ? 30.411  -36.678 50.998  1.00 62.97  ? 184 GLN B NE2   1 
ATOM   5975 N N     . ALA B 1 187 ? 30.540  -37.673 56.549  1.00 63.64  ? 185 ALA B N     1 
ATOM   5976 C CA    . ALA B 1 187 ? 30.702  -37.667 58.026  1.00 64.48  ? 185 ALA B CA    1 
ATOM   5977 C C     . ALA B 1 187 ? 29.356  -37.901 58.726  1.00 63.76  ? 185 ALA B C     1 
ATOM   5978 O O     . ALA B 1 187 ? 29.291  -38.783 59.608  1.00 66.66  ? 185 ALA B O     1 
ATOM   5979 C CB    . ALA B 1 187 ? 31.329  -36.371 58.479  1.00 65.35  ? 185 ALA B CB    1 
ATOM   5980 N N     . ASP B 1 188 ? 28.298  -37.175 58.357  1.00 58.68  ? 186 ASP B N     1 
ATOM   5981 C CA    . ASP B 1 188 ? 26.996  -37.286 59.078  1.00 60.82  ? 186 ASP B CA    1 
ATOM   5982 C C     . ASP B 1 188 ? 26.301  -38.621 58.761  1.00 56.37  ? 186 ASP B C     1 
ATOM   5983 O O     . ASP B 1 188 ? 25.155  -38.769 59.208  1.00 54.23  ? 186 ASP B O     1 
ATOM   5984 C CB    . ASP B 1 188 ? 26.099  -36.073 58.810  1.00 63.11  ? 186 ASP B CB    1 
ATOM   5985 C CG    . ASP B 1 188 ? 25.938  -35.737 57.337  1.00 70.70  ? 186 ASP B CG    1 
ATOM   5986 O OD1   . ASP B 1 188 ? 25.645  -36.668 56.553  1.00 74.58  ? 186 ASP B OD1   1 
ATOM   5987 O OD2   . ASP B 1 188 ? 26.127  -34.556 56.981  1.00 67.06  ? 186 ASP B OD2   1 
ATOM   5988 N N     . GLY B 1 189 ? 26.930  -39.525 57.986  1.00 58.40  ? 187 GLY B N     1 
ATOM   5989 C CA    . GLY B 1 189 ? 26.416  -40.877 57.656  1.00 62.26  ? 187 GLY B CA    1 
ATOM   5990 C C     . GLY B 1 189 ? 25.460  -40.922 56.455  1.00 65.16  ? 187 GLY B C     1 
ATOM   5991 O O     . GLY B 1 189 ? 24.998  -42.039 56.084  1.00 65.30  ? 187 GLY B O     1 
ATOM   5992 N N     . SER B 1 190 ? 25.135  -39.758 55.886  1.00 58.13  ? 188 SER B N     1 
ATOM   5993 C CA    . SER B 1 190 ? 24.410  -39.594 54.604  1.00 51.66  ? 188 SER B CA    1 
ATOM   5994 C C     . SER B 1 190 ? 25.428  -39.625 53.470  1.00 55.64  ? 188 SER B C     1 
ATOM   5995 O O     . SER B 1 190 ? 26.647  -39.546 53.767  1.00 49.67  ? 188 SER B O     1 
ATOM   5996 C CB    . SER B 1 190 ? 23.648  -38.287 54.564  1.00 45.63  ? 188 SER B CB    1 
ATOM   5997 O OG    . SER B 1 190 ? 24.521  -37.219 54.202  1.00 41.92  ? 188 SER B OG    1 
ATOM   5998 N N     . TYR B 1 191 ? 24.917  -39.607 52.231  1.00 58.06  ? 189 TYR B N     1 
ATOM   5999 C CA    . TYR B 1 191 ? 25.696  -39.762 50.981  1.00 54.87  ? 189 TYR B CA    1 
ATOM   6000 C C     . TYR B 1 191 ? 25.458  -38.585 50.047  1.00 50.87  ? 189 TYR B C     1 
ATOM   6001 O O     . TYR B 1 191 ? 24.426  -37.928 50.160  1.00 49.80  ? 189 TYR B O     1 
ATOM   6002 C CB    . TYR B 1 191 ? 25.328  -41.089 50.339  1.00 52.54  ? 189 TYR B CB    1 
ATOM   6003 C CG    . TYR B 1 191 ? 25.665  -42.257 51.224  1.00 51.62  ? 189 TYR B CG    1 
ATOM   6004 C CD1   . TYR B 1 191 ? 24.854  -42.630 52.290  1.00 52.95  ? 189 TYR B CD1   1 
ATOM   6005 C CD2   . TYR B 1 191 ? 26.840  -42.958 51.017  1.00 57.33  ? 189 TYR B CD2   1 
ATOM   6006 C CE1   . TYR B 1 191 ? 25.181  -43.715 53.091  1.00 51.80  ? 189 TYR B CE1   1 
ATOM   6007 C CE2   . TYR B 1 191 ? 27.182  -44.040 51.804  1.00 55.21  ? 189 TYR B CE2   1 
ATOM   6008 C CZ    . TYR B 1 191 ? 26.355  -44.412 52.843  1.00 51.36  ? 189 TYR B CZ    1 
ATOM   6009 O OH    . TYR B 1 191 ? 26.754  -45.485 53.572  1.00 54.17  ? 189 TYR B OH    1 
ATOM   6010 N N     . LYS B 1 192 ? 26.460  -38.304 49.218  1.00 49.61  ? 190 LYS B N     1 
ATOM   6011 C CA    . LYS B 1 192 ? 26.346  -37.419 48.039  1.00 54.19  ? 190 LYS B CA    1 
ATOM   6012 C C     . LYS B 1 192 ? 26.407  -38.287 46.775  1.00 53.28  ? 190 LYS B C     1 
ATOM   6013 O O     . LYS B 1 192 ? 27.449  -38.980 46.550  1.00 50.22  ? 190 LYS B O     1 
ATOM   6014 C CB    . LYS B 1 192 ? 27.387  -36.312 48.134  1.00 53.93  ? 190 LYS B CB    1 
ATOM   6015 C CG    . LYS B 1 192 ? 27.132  -35.432 49.339  1.00 54.19  ? 190 LYS B CG    1 
ATOM   6016 C CD    . LYS B 1 192 ? 27.900  -34.155 49.357  1.00 54.38  ? 190 LYS B CD    1 
ATOM   6017 C CE    . LYS B 1 192 ? 27.315  -33.235 50.396  1.00 52.63  ? 190 LYS B CE    1 
ATOM   6018 N NZ    . LYS B 1 192 ? 28.137  -32.017 50.530  1.00 55.94  ? 190 LYS B NZ    1 
ATOM   6019 N N     . VAL B 1 193 ? 25.280  -38.299 46.048  1.00 48.00  ? 191 VAL B N     1 
ATOM   6020 C CA    . VAL B 1 193 ? 25.033  -39.109 44.821  1.00 46.59  ? 191 VAL B CA    1 
ATOM   6021 C C     . VAL B 1 193 ? 25.387  -38.253 43.607  1.00 44.26  ? 191 VAL B C     1 
ATOM   6022 O O     . VAL B 1 193 ? 24.910  -37.102 43.517  1.00 42.97  ? 191 VAL B O     1 
ATOM   6023 C CB    . VAL B 1 193 ? 23.593  -39.647 44.783  1.00 47.56  ? 191 VAL B CB    1 
ATOM   6024 C CG1   . VAL B 1 193 ? 23.403  -40.668 43.661  1.00 44.39  ? 191 VAL B CG1   1 
ATOM   6025 C CG2   . VAL B 1 193 ? 23.225  -40.250 46.143  1.00 46.09  ? 191 VAL B CG2   1 
ATOM   6026 N N     . THR B 1 194 ? 26.317  -38.739 42.789  1.00 43.08  ? 192 THR B N     1 
ATOM   6027 C CA    . THR B 1 194 ? 26.716  -38.085 41.514  1.00 50.62  ? 192 THR B CA    1 
ATOM   6028 C C     . THR B 1 194 ? 26.483  -39.108 40.393  1.00 49.24  ? 192 THR B C     1 
ATOM   6029 O O     . THR B 1 194 ? 26.910  -40.276 40.553  1.00 48.75  ? 192 THR B O     1 
ATOM   6030 C CB    . THR B 1 194 ? 28.117  -37.462 41.627  1.00 47.02  ? 192 THR B CB    1 
ATOM   6031 O OG1   . THR B 1 194 ? 28.065  -36.517 42.699  1.00 51.97  ? 192 THR B OG1   1 
ATOM   6032 C CG2   . THR B 1 194 ? 28.568  -36.726 40.389  1.00 43.82  ? 192 THR B CG2   1 
ATOM   6033 N N     . GLY B 1 195 ? 25.743  -38.702 39.360  1.00 46.40  ? 193 GLY B N     1 
ATOM   6034 C CA    . GLY B 1 195 ? 25.400  -39.565 38.215  1.00 45.18  ? 193 GLY B CA    1 
ATOM   6035 C C     . GLY B 1 195 ? 24.276  -39.008 37.355  1.00 43.44  ? 193 GLY B C     1 
ATOM   6036 O O     . GLY B 1 195 ? 23.519  -38.095 37.786  1.00 37.52  ? 193 GLY B O     1 
ATOM   6037 N N     . THR B 1 196 ? 24.155  -39.559 36.155  1.00 46.07  ? 194 THR B N     1 
ATOM   6038 C CA    . THR B 1 196 ? 23.045  -39.272 35.212  1.00 41.61  ? 194 THR B CA    1 
ATOM   6039 C C     . THR B 1 196 ? 22.252  -40.568 35.060  1.00 37.56  ? 194 THR B C     1 
ATOM   6040 O O     . THR B 1 196 ? 22.869  -41.574 34.621  1.00 38.26  ? 194 THR B O     1 
ATOM   6041 C CB    . THR B 1 196 ? 23.596  -38.707 33.902  1.00 46.46  ? 194 THR B CB    1 
ATOM   6042 O OG1   . THR B 1 196 ? 24.351  -37.555 34.280  1.00 45.79  ? 194 THR B OG1   1 
ATOM   6043 C CG2   . THR B 1 196 ? 22.528  -38.329 32.892  1.00 47.31  ? 194 THR B CG2   1 
ATOM   6044 N N     . LYS B 1 197 ? 20.978  -40.538 35.473  1.00 33.78  ? 195 LYS B N     1 
ATOM   6045 C CA    . LYS B 1 197 ? 19.954  -41.591 35.224  1.00 37.03  ? 195 LYS B CA    1 
ATOM   6046 C C     . LYS B 1 197 ? 19.024  -41.132 34.087  1.00 41.50  ? 195 LYS B C     1 
ATOM   6047 O O     . LYS B 1 197 ? 18.695  -39.916 34.016  1.00 40.35  ? 195 LYS B O     1 
ATOM   6048 C CB    . LYS B 1 197 ? 19.160  -41.884 36.496  1.00 36.83  ? 195 LYS B CB    1 
ATOM   6049 C CG    . LYS B 1 197 ? 20.006  -42.422 37.634  1.00 37.88  ? 195 LYS B CG    1 
ATOM   6050 C CD    . LYS B 1 197 ? 20.464  -43.856 37.464  1.00 39.29  ? 195 LYS B CD    1 
ATOM   6051 C CE    . LYS B 1 197 ? 21.275  -44.340 38.651  1.00 36.19  ? 195 LYS B CE    1 
ATOM   6052 N NZ    . LYS B 1 197 ? 21.516  -45.794 38.593  1.00 34.07  ? 195 LYS B NZ    1 
ATOM   6053 N N     . ILE B 1 198 ? 18.652  -42.050 33.191  1.00 39.08  ? 196 ILE B N     1 
ATOM   6054 C CA    . ILE B 1 198 ? 17.819  -41.715 32.002  1.00 36.69  ? 196 ILE B CA    1 
ATOM   6055 C C     . ILE B 1 198 ? 16.569  -42.575 32.030  1.00 37.31  ? 196 ILE B C     1 
ATOM   6056 O O     . ILE B 1 198 ? 16.532  -43.618 32.737  1.00 36.61  ? 196 ILE B O     1 
ATOM   6057 C CB    . ILE B 1 198 ? 18.574  -41.881 30.672  1.00 35.43  ? 196 ILE B CB    1 
ATOM   6058 C CG1   . ILE B 1 198 ? 18.880  -43.344 30.339  1.00 37.64  ? 196 ILE B CG1   1 
ATOM   6059 C CG2   . ILE B 1 198 ? 19.833  -41.042 30.649  1.00 36.32  ? 196 ILE B CG2   1 
ATOM   6060 C CD1   . ILE B 1 198 ? 19.149  -43.579 28.859  1.00 38.02  ? 196 ILE B CD1   1 
ATOM   6061 N N     . PHE B 1 199 ? 15.598  -42.128 31.246  1.00 36.76  ? 197 PHE B N     1 
ATOM   6062 C CA    . PHE B 1 199 ? 14.268  -42.741 31.075  1.00 34.48  ? 197 PHE B CA    1 
ATOM   6063 C C     . PHE B 1 199 ? 13.541  -42.768 32.419  1.00 35.73  ? 197 PHE B C     1 
ATOM   6064 O O     . PHE B 1 199 ? 12.888  -43.782 32.669  1.00 35.51  ? 197 PHE B O     1 
ATOM   6065 C CB    . PHE B 1 199 ? 14.427  -44.143 30.478  1.00 35.98  ? 197 PHE B CB    1 
ATOM   6066 C CG    . PHE B 1 199 ? 14.967  -44.200 29.072  1.00 37.87  ? 197 PHE B CG    1 
ATOM   6067 C CD1   . PHE B 1 199 ? 14.955  -43.085 28.238  1.00 42.09  ? 197 PHE B CD1   1 
ATOM   6068 C CD2   . PHE B 1 199 ? 15.465  -45.392 28.562  1.00 37.97  ? 197 PHE B CD2   1 
ATOM   6069 C CE1   . PHE B 1 199 ? 15.443  -43.164 26.936  1.00 43.97  ? 197 PHE B CE1   1 
ATOM   6070 C CE2   . PHE B 1 199 ? 15.942  -45.469 27.263  1.00 38.43  ? 197 PHE B CE2   1 
ATOM   6071 C CZ    . PHE B 1 199 ? 15.934  -44.357 26.449  1.00 40.43  ? 197 PHE B CZ    1 
ATOM   6072 N N     . ILE B 1 200 ? 13.672  -41.745 33.277  1.00 34.73  ? 198 ILE B N     1 
ATOM   6073 C CA    . ILE B 1 200 ? 13.068  -41.809 34.644  1.00 36.35  ? 198 ILE B CA    1 
ATOM   6074 C C     . ILE B 1 200 ? 11.628  -41.293 34.580  1.00 33.28  ? 198 ILE B C     1 
ATOM   6075 O O     . ILE B 1 200 ? 11.401  -40.073 34.426  1.00 32.30  ? 198 ILE B O     1 
ATOM   6076 C CB    . ILE B 1 200 ? 13.945  -41.114 35.705  1.00 41.11  ? 198 ILE B CB    1 
ATOM   6077 C CG1   . ILE B 1 200 ? 15.352  -41.716 35.767  1.00 39.23  ? 198 ILE B CG1   1 
ATOM   6078 C CG2   . ILE B 1 200 ? 13.277  -41.165 37.070  1.00 42.62  ? 198 ILE B CG2   1 
ATOM   6079 C CD1   . ILE B 1 200 ? 15.364  -43.197 36.052  1.00 39.17  ? 198 ILE B CD1   1 
ATOM   6080 N N     . SER B 1 201 ? 10.695  -42.235 34.650  1.00 33.37  ? 199 SER B N     1 
ATOM   6081 C CA    . SER B 1 201 ? 9.241   -41.988 34.562  1.00 33.53  ? 199 SER B CA    1 
ATOM   6082 C C     . SER B 1 201 ? 8.851   -41.166 35.779  1.00 35.34  ? 199 SER B C     1 
ATOM   6083 O O     . SER B 1 201 ? 9.078   -41.642 36.914  1.00 33.88  ? 199 SER B O     1 
ATOM   6084 C CB    . SER B 1 201 ? 8.436   -43.275 34.485  1.00 33.71  ? 199 SER B CB    1 
ATOM   6085 O OG    . SER B 1 201 ? 8.857   -44.088 33.385  1.00 33.25  ? 199 SER B OG    1 
ATOM   6086 N N     . ALA B 1 202 ? 8.304   -39.976 35.542  1.00 38.79  ? 200 ALA B N     1 
ATOM   6087 C CA    . ALA B 1 202 ? 7.746   -39.104 36.595  1.00 42.31  ? 200 ALA B CA    1 
ATOM   6088 C C     . ALA B 1 202 ? 8.899   -38.493 37.392  1.00 42.01  ? 200 ALA B C     1 
ATOM   6089 O O     . ALA B 1 202 ? 8.666   -38.167 38.560  1.00 42.63  ? 200 ALA B O     1 
ATOM   6090 C CB    . ALA B 1 202 ? 6.810   -39.895 37.495  1.00 41.00  ? 200 ALA B CB    1 
ATOM   6091 N N     . GLY B 1 203 ? 10.081  -38.354 36.779  1.00 41.03  ? 201 GLY B N     1 
ATOM   6092 C CA    . GLY B 1 203 ? 11.297  -37.838 37.440  1.00 44.62  ? 201 GLY B CA    1 
ATOM   6093 C C     . GLY B 1 203 ? 11.173  -36.372 37.854  1.00 46.97  ? 201 GLY B C     1 
ATOM   6094 O O     . GLY B 1 203 ? 11.794  -35.952 38.871  1.00 48.47  ? 201 GLY B O     1 
ATOM   6095 N N     . GLU B 1 204 ? 10.439  -35.602 37.059  1.00 41.58  ? 202 GLU B N     1 
ATOM   6096 C CA    . GLU B 1 204 ? 10.172  -34.166 37.277  1.00 39.93  ? 202 GLU B CA    1 
ATOM   6097 C C     . GLU B 1 204 ? 8.766   -33.893 36.747  1.00 42.87  ? 202 GLU B C     1 
ATOM   6098 O O     . GLU B 1 204 ? 8.387   -34.474 35.695  1.00 45.07  ? 202 GLU B O     1 
ATOM   6099 C CB    . GLU B 1 204 ? 11.256  -33.356 36.578  1.00 39.31  ? 202 GLU B CB    1 
ATOM   6100 C CG    . GLU B 1 204 ? 11.150  -31.870 36.798  1.00 41.85  ? 202 GLU B CG    1 
ATOM   6101 C CD    . GLU B 1 204 ? 11.356  -31.410 38.240  1.00 45.03  ? 202 GLU B CD    1 
ATOM   6102 O OE1   . GLU B 1 204 ? 10.348  -31.462 39.003  1.00 44.89  ? 202 GLU B OE1   1 
ATOM   6103 O OE2   . GLU B 1 204 ? 12.527  -30.996 38.597  1.00 40.23  ? 202 GLU B OE2   1 
ATOM   6104 N N     . HIS B 1 205 ? 7.989   -33.104 37.477  1.00 41.42  ? 203 HIS B N     1 
ATOM   6105 C CA    . HIS B 1 205 ? 6.570   -32.821 37.146  1.00 41.74  ? 203 HIS B CA    1 
ATOM   6106 C C     . HIS B 1 205 ? 6.024   -31.845 38.184  1.00 42.74  ? 203 HIS B C     1 
ATOM   6107 O O     . HIS B 1 205 ? 6.799   -31.493 39.082  1.00 49.47  ? 203 HIS B O     1 
ATOM   6108 C CB    . HIS B 1 205 ? 5.758   -34.116 37.027  1.00 40.38  ? 203 HIS B CB    1 
ATOM   6109 C CG    . HIS B 1 205 ? 5.647   -34.897 38.290  1.00 42.83  ? 203 HIS B CG    1 
ATOM   6110 N ND1   . HIS B 1 205 ? 4.869   -34.477 39.347  1.00 42.15  ? 203 HIS B ND1   1 
ATOM   6111 C CD2   . HIS B 1 205 ? 6.184   -36.091 38.646  1.00 41.22  ? 203 HIS B CD2   1 
ATOM   6112 C CE1   . HIS B 1 205 ? 4.946   -35.375 40.314  1.00 45.72  ? 203 HIS B CE1   1 
ATOM   6113 N NE2   . HIS B 1 205 ? 5.763   -36.377 39.908  1.00 43.51  ? 203 HIS B NE2   1 
ATOM   6114 N N     . ASP B 1 206 ? 4.771   -31.420 38.021  1.00 40.63  ? 204 ASP B N     1 
ATOM   6115 C CA    . ASP B 1 206 ? 4.128   -30.280 38.728  1.00 37.42  ? 204 ASP B CA    1 
ATOM   6116 C C     . ASP B 1 206 ? 2.885   -30.812 39.429  1.00 39.97  ? 204 ASP B C     1 
ATOM   6117 O O     . ASP B 1 206 ? 1.991   -30.027 39.696  1.00 51.27  ? 204 ASP B O     1 
ATOM   6118 C CB    . ASP B 1 206 ? 3.780   -29.145 37.753  1.00 40.64  ? 204 ASP B CB    1 
ATOM   6119 C CG    . ASP B 1 206 ? 2.837   -29.525 36.593  1.00 47.54  ? 204 ASP B CG    1 
ATOM   6120 O OD1   . ASP B 1 206 ? 2.420   -30.735 36.504  1.00 44.26  ? 204 ASP B OD1   1 
ATOM   6121 O OD2   . ASP B 1 206 ? 2.520   -28.622 35.771  1.00 42.60  ? 204 ASP B OD2   1 
ATOM   6122 N N     . MET B 1 207 ? 2.856   -32.105 39.724  1.00 42.38  ? 205 MET B N     1 
ATOM   6123 C CA    . MET B 1 207 ? 1.680   -32.844 40.244  1.00 46.16  ? 205 MET B CA    1 
ATOM   6124 C C     . MET B 1 207 ? 1.681   -32.854 41.785  1.00 47.07  ? 205 MET B C     1 
ATOM   6125 O O     . MET B 1 207 ? 0.580   -32.995 42.359  1.00 47.13  ? 205 MET B O     1 
ATOM   6126 C CB    . MET B 1 207 ? 1.750   -34.284 39.732  1.00 51.86  ? 205 MET B CB    1 
ATOM   6127 C CG    . MET B 1 207 ? 0.406   -34.927 39.436  1.00 62.82  ? 205 MET B CG    1 
ATOM   6128 S SD    . MET B 1 207 ? 0.285   -35.553 37.723  1.00 54.74  ? 205 MET B SD    1 
ATOM   6129 C CE    . MET B 1 207 ? 0.410   -33.965 36.918  1.00 53.19  ? 205 MET B CE    1 
ATOM   6130 N N     . ALA B 1 208 ? 2.854   -32.746 42.433  1.00 43.17  ? 206 ALA B N     1 
ATOM   6131 C CA    . ALA B 1 208 ? 3.038   -33.024 43.883  1.00 44.75  ? 206 ALA B CA    1 
ATOM   6132 C C     . ALA B 1 208 ? 3.952   -32.005 44.568  1.00 41.75  ? 206 ALA B C     1 
ATOM   6133 O O     . ALA B 1 208 ? 4.482   -31.102 43.915  1.00 43.58  ? 206 ALA B O     1 
ATOM   6134 C CB    . ALA B 1 208 ? 3.577   -34.428 44.074  1.00 46.26  ? 206 ALA B CB    1 
ATOM   6135 N N     . ASP B 1 209 ? 4.137   -32.180 45.876  1.00 47.09  ? 207 ASP B N     1 
ATOM   6136 C CA    . ASP B 1 209 ? 4.850   -31.221 46.775  1.00 50.13  ? 207 ASP B CA    1 
ATOM   6137 C C     . ASP B 1 209 ? 6.331   -31.646 46.827  1.00 49.94  ? 207 ASP B C     1 
ATOM   6138 O O     . ASP B 1 209 ? 7.226   -30.781 47.060  1.00 53.25  ? 207 ASP B O     1 
ATOM   6139 C CB    . ASP B 1 209 ? 4.110   -31.118 48.127  1.00 46.98  ? 207 ASP B CB    1 
ATOM   6140 C CG    . ASP B 1 209 ? 2.680   -30.582 48.008  1.00 52.54  ? 207 ASP B CG    1 
ATOM   6141 O OD1   . ASP B 1 209 ? 2.522   -29.473 47.453  1.00 56.60  ? 207 ASP B OD1   1 
ATOM   6142 O OD2   . ASP B 1 209 ? 1.716   -31.295 48.411  1.00 59.22  ? 207 ASP B OD2   1 
ATOM   6143 N N     . ASN B 1 210 ? 6.593   -32.927 46.560  1.00 39.22  ? 208 ASN B N     1 
ATOM   6144 C CA    . ASN B 1 210 ? 7.957   -33.478 46.556  1.00 41.44  ? 208 ASN B CA    1 
ATOM   6145 C C     . ASN B 1 210 ? 7.937   -34.774 45.729  1.00 40.17  ? 208 ASN B C     1 
ATOM   6146 O O     . ASN B 1 210 ? 6.856   -35.413 45.605  1.00 31.46  ? 208 ASN B O     1 
ATOM   6147 C CB    . ASN B 1 210 ? 8.453   -33.675 48.005  1.00 41.44  ? 208 ASN B CB    1 
ATOM   6148 C CG    . ASN B 1 210 ? 9.962   -33.771 48.186  1.00 41.52  ? 208 ASN B CG    1 
ATOM   6149 O OD1   . ASN B 1 210 ? 10.744  -33.555 47.261  1.00 36.46  ? 208 ASN B OD1   1 
ATOM   6150 N ND2   . ASN B 1 210 ? 10.390  -34.093 49.402  1.00 47.29  ? 208 ASN B ND2   1 
ATOM   6151 N N     . ILE B 1 211 ? 9.127   -35.184 45.283  1.00 38.34  ? 209 ILE B N     1 
ATOM   6152 C CA    . ILE B 1 211 ? 9.397   -36.490 44.623  1.00 41.60  ? 209 ILE B CA    1 
ATOM   6153 C C     . ILE B 1 211 ? 10.569  -37.178 45.322  1.00 39.03  ? 209 ILE B C     1 
ATOM   6154 O O     . ILE B 1 211 ? 11.674  -36.578 45.414  1.00 35.82  ? 209 ILE B O     1 
ATOM   6155 C CB    . ILE B 1 211 ? 9.712   -36.322 43.120  1.00 45.37  ? 209 ILE B CB    1 
ATOM   6156 C CG1   . ILE B 1 211 ? 8.745   -35.364 42.405  1.00 43.70  ? 209 ILE B CG1   1 
ATOM   6157 C CG2   . ILE B 1 211 ? 9.763   -37.703 42.484  1.00 46.31  ? 209 ILE B CG2   1 
ATOM   6158 C CD1   . ILE B 1 211 ? 9.267   -34.831 41.076  1.00 47.82  ? 209 ILE B CD1   1 
ATOM   6159 N N     . VAL B 1 212 ? 10.348  -38.448 45.652  1.00 41.16  ? 210 VAL B N     1 
ATOM   6160 C CA    . VAL B 1 212 ? 11.315  -39.340 46.341  1.00 41.34  ? 210 VAL B CA    1 
ATOM   6161 C C     . VAL B 1 212 ? 11.909  -40.298 45.307  1.00 37.67  ? 210 VAL B C     1 
ATOM   6162 O O     . VAL B 1 212 ? 11.293  -41.327 44.985  1.00 37.98  ? 210 VAL B O     1 
ATOM   6163 C CB    . VAL B 1 212 ? 10.622  -40.095 47.495  1.00 42.99  ? 210 VAL B CB    1 
ATOM   6164 C CG1   . VAL B 1 212 ? 11.596  -41.013 48.224  1.00 43.49  ? 210 VAL B CG1   1 
ATOM   6165 C CG2   . VAL B 1 212 ? 9.934   -39.137 48.464  1.00 44.44  ? 210 VAL B CG2   1 
ATOM   6166 N N     . HIS B 1 213 ? 13.119  -40.023 44.868  1.00 36.60  ? 211 HIS B N     1 
ATOM   6167 C CA    . HIS B 1 213 ? 13.878  -40.968 44.016  1.00 38.82  ? 211 HIS B CA    1 
ATOM   6168 C C     . HIS B 1 213 ? 14.479  -42.090 44.879  1.00 39.92  ? 211 HIS B C     1 
ATOM   6169 O O     . HIS B 1 213 ? 15.330  -41.791 45.732  1.00 43.38  ? 211 HIS B O     1 
ATOM   6170 C CB    . HIS B 1 213 ? 14.918  -40.204 43.183  1.00 36.97  ? 211 HIS B CB    1 
ATOM   6171 C CG    . HIS B 1 213 ? 14.350  -39.032 42.456  1.00 37.80  ? 211 HIS B CG    1 
ATOM   6172 N ND1   . HIS B 1 213 ? 13.499  -39.179 41.373  1.00 38.96  ? 211 HIS B ND1   1 
ATOM   6173 C CD2   . HIS B 1 213 ? 14.520  -37.704 42.634  1.00 38.52  ? 211 HIS B CD2   1 
ATOM   6174 C CE1   . HIS B 1 213 ? 13.178  -37.982 40.917  1.00 42.07  ? 211 HIS B CE1   1 
ATOM   6175 N NE2   . HIS B 1 213 ? 13.782  -37.053 41.688  1.00 40.08  ? 211 HIS B NE2   1 
ATOM   6176 N N     . ILE B 1 214 ? 14.055  -43.332 44.637  1.00 40.94  ? 212 ILE B N     1 
ATOM   6177 C CA    . ILE B 1 214 ? 14.771  -44.582 45.030  1.00 41.74  ? 212 ILE B CA    1 
ATOM   6178 C C     . ILE B 1 214 ? 15.839  -44.892 43.962  1.00 42.02  ? 212 ILE B C     1 
ATOM   6179 O O     . ILE B 1 214 ? 15.485  -45.485 42.908  1.00 44.49  ? 212 ILE B O     1 
ATOM   6180 C CB    . ILE B 1 214 ? 13.756  -45.727 45.254  1.00 42.60  ? 212 ILE B CB    1 
ATOM   6181 C CG1   . ILE B 1 214 ? 12.670  -45.367 46.282  1.00 45.88  ? 212 ILE B CG1   1 
ATOM   6182 C CG2   . ILE B 1 214 ? 14.463  -47.017 45.638  1.00 44.01  ? 212 ILE B CG2   1 
ATOM   6183 C CD1   . ILE B 1 214 ? 13.163  -44.554 47.471  1.00 47.54  ? 212 ILE B CD1   1 
ATOM   6184 N N     . VAL B 1 215 ? 17.101  -44.512 44.213  1.00 41.94  ? 213 VAL B N     1 
ATOM   6185 C CA    . VAL B 1 215 ? 18.228  -44.538 43.219  1.00 42.90  ? 213 VAL B CA    1 
ATOM   6186 C C     . VAL B 1 215 ? 19.164  -45.725 43.484  1.00 48.32  ? 213 VAL B C     1 
ATOM   6187 O O     . VAL B 1 215 ? 19.608  -45.854 44.660  1.00 46.34  ? 213 VAL B O     1 
ATOM   6188 C CB    . VAL B 1 215 ? 19.046  -43.233 43.278  1.00 41.80  ? 213 VAL B CB    1 
ATOM   6189 C CG1   . VAL B 1 215 ? 20.060  -43.158 42.151  1.00 43.34  ? 213 VAL B CG1   1 
ATOM   6190 C CG2   . VAL B 1 215 ? 18.172  -41.984 43.311  1.00 40.28  ? 213 VAL B CG2   1 
ATOM   6191 N N     . LEU B 1 216 ? 19.523  -46.516 42.448  1.00 44.27  ? 214 LEU B N     1 
ATOM   6192 C CA    . LEU B 1 216 ? 20.649  -47.497 42.534  1.00 41.76  ? 214 LEU B CA    1 
ATOM   6193 C C     . LEU B 1 216 ? 21.969  -46.743 42.325  1.00 41.29  ? 214 LEU B C     1 
ATOM   6194 O O     . LEU B 1 216 ? 22.065  -46.075 41.310  1.00 38.36  ? 214 LEU B O     1 
ATOM   6195 C CB    . LEU B 1 216 ? 20.499  -48.611 41.496  1.00 42.01  ? 214 LEU B CB    1 
ATOM   6196 C CG    . LEU B 1 216 ? 19.350  -49.584 41.709  1.00 42.50  ? 214 LEU B CG    1 
ATOM   6197 C CD1   . LEU B 1 216 ? 19.269  -50.571 40.570  1.00 44.81  ? 214 LEU B CD1   1 
ATOM   6198 C CD2   . LEU B 1 216 ? 19.535  -50.356 42.994  1.00 52.51  ? 214 LEU B CD2   1 
ATOM   6199 N N     . ALA B 1 217 ? 22.926  -46.787 43.272  1.00 40.36  ? 215 ALA B N     1 
ATOM   6200 C CA    . ALA B 1 217 ? 24.316  -46.301 43.056  1.00 41.43  ? 215 ALA B CA    1 
ATOM   6201 C C     . ALA B 1 217 ? 25.321  -47.253 43.700  1.00 44.85  ? 215 ALA B C     1 
ATOM   6202 O O     . ALA B 1 217 ? 24.874  -48.204 44.402  1.00 48.19  ? 215 ALA B O     1 
ATOM   6203 C CB    . ALA B 1 217 ? 24.499  -44.904 43.585  1.00 41.98  ? 215 ALA B CB    1 
ATOM   6204 N N     . ARG B 1 218 ? 26.601  -46.951 43.493  1.00 47.21  ? 216 ARG B N     1 
ATOM   6205 C CA    . ARG B 1 218 ? 27.689  -47.801 44.016  1.00 50.52  ? 216 ARG B CA    1 
ATOM   6206 C C     . ARG B 1 218 ? 28.543  -47.038 45.022  1.00 54.10  ? 216 ARG B C     1 
ATOM   6207 O O     . ARG B 1 218 ? 28.908  -45.891 44.737  1.00 50.33  ? 216 ARG B O     1 
ATOM   6208 C CB    . ARG B 1 218 ? 28.623  -48.248 42.890  1.00 52.09  ? 216 ARG B CB    1 
ATOM   6209 C CG    . ARG B 1 218 ? 27.939  -48.630 41.588  1.00 55.57  ? 216 ARG B CG    1 
ATOM   6210 C CD    . ARG B 1 218 ? 29.001  -49.059 40.597  1.00 46.79  ? 216 ARG B CD    1 
ATOM   6211 N NE    . ARG B 1 218 ? 29.562  -50.350 40.957  1.00 49.34  ? 216 ARG B NE    1 
ATOM   6212 C CZ    . ARG B 1 218 ? 29.053  -51.515 40.582  1.00 53.76  ? 216 ARG B CZ    1 
ATOM   6213 N NH1   . ARG B 1 218 ? 27.973  -51.552 39.822  1.00 58.92  ? 216 ARG B NH1   1 
ATOM   6214 N NH2   . ARG B 1 218 ? 29.630  -52.640 40.959  1.00 56.12  ? 216 ARG B NH2   1 
ATOM   6215 N N     . LEU B 1 219 ? 28.853  -47.668 46.143  1.00 56.54  ? 217 LEU B N     1 
ATOM   6216 C CA    . LEU B 1 219 ? 29.749  -47.127 47.202  1.00 54.48  ? 217 LEU B CA    1 
ATOM   6217 C C     . LEU B 1 219 ? 31.200  -47.200 46.740  1.00 51.91  ? 217 LEU B C     1 
ATOM   6218 O O     . LEU B 1 219 ? 31.566  -48.166 46.079  1.00 49.87  ? 217 LEU B O     1 
ATOM   6219 C CB    . LEU B 1 219 ? 29.519  -47.960 48.458  1.00 52.08  ? 217 LEU B CB    1 
ATOM   6220 C CG    . LEU B 1 219 ? 28.120  -47.815 49.039  1.00 50.95  ? 217 LEU B CG    1 
ATOM   6221 C CD1   . LEU B 1 219 ? 27.865  -48.854 50.124  1.00 50.08  ? 217 LEU B CD1   1 
ATOM   6222 C CD2   . LEU B 1 219 ? 27.913  -46.391 49.546  1.00 51.66  ? 217 LEU B CD2   1 
ATOM   6223 N N     . PRO B 1 220 ? 32.066  -46.237 47.147  1.00 53.11  ? 218 PRO B N     1 
ATOM   6224 C CA    . PRO B 1 220 ? 33.342  -45.969 46.480  1.00 53.65  ? 218 PRO B CA    1 
ATOM   6225 C C     . PRO B 1 220 ? 34.277  -47.162 46.228  1.00 56.79  ? 218 PRO B C     1 
ATOM   6226 O O     . PRO B 1 220 ? 35.012  -47.108 45.234  1.00 63.65  ? 218 PRO B O     1 
ATOM   6227 C CB    . PRO B 1 220 ? 34.047  -44.984 47.427  1.00 54.08  ? 218 PRO B CB    1 
ATOM   6228 C CG    . PRO B 1 220 ? 32.913  -44.262 48.113  1.00 54.10  ? 218 PRO B CG    1 
ATOM   6229 C CD    . PRO B 1 220 ? 31.886  -45.360 48.317  1.00 57.70  ? 218 PRO B CD    1 
ATOM   6230 N N     . ASP B 1 221 ? 34.260  -48.192 47.075  1.00 52.97  ? 219 ASP B N     1 
ATOM   6231 C CA    . ASP B 1 221 ? 35.179  -49.347 46.889  1.00 60.38  ? 219 ASP B CA    1 
ATOM   6232 C C     . ASP B 1 221 ? 34.374  -50.629 47.022  1.00 62.76  ? 219 ASP B C     1 
ATOM   6233 O O     . ASP B 1 221 ? 34.866  -51.551 47.671  1.00 61.39  ? 219 ASP B O     1 
ATOM   6234 C CB    . ASP B 1 221 ? 36.371  -49.299 47.850  1.00 66.94  ? 219 ASP B CB    1 
ATOM   6235 C CG    . ASP B 1 221 ? 37.606  -48.650 47.239  1.00 72.00  ? 219 ASP B CG    1 
ATOM   6236 O OD1   . ASP B 1 221 ? 38.333  -49.347 46.497  1.00 74.77  ? 219 ASP B OD1   1 
ATOM   6237 O OD2   . ASP B 1 221 ? 37.832  -47.448 47.499  1.00 77.45  ? 219 ASP B OD2   1 
ATOM   6238 N N     . ALA B 1 222 ? 33.195  -50.653 46.395  1.00 59.98  ? 220 ALA B N     1 
ATOM   6239 C CA    . ALA B 1 222 ? 32.257  -51.795 46.365  1.00 53.28  ? 220 ALA B CA    1 
ATOM   6240 C C     . ALA B 1 222 ? 32.761  -52.831 45.364  1.00 50.10  ? 220 ALA B C     1 
ATOM   6241 O O     . ALA B 1 222 ? 33.544  -52.497 44.485  1.00 45.29  ? 220 ALA B O     1 
ATOM   6242 C CB    . ALA B 1 222 ? 30.876  -51.299 46.003  1.00 53.57  ? 220 ALA B CB    1 
ATOM   6243 N N     . PRO B 1 223 ? 32.304  -54.104 45.439  1.00 50.57  ? 221 PRO B N     1 
ATOM   6244 C CA    . PRO B 1 223 ? 32.633  -55.096 44.417  1.00 50.80  ? 221 PRO B CA    1 
ATOM   6245 C C     . PRO B 1 223 ? 32.038  -54.698 43.055  1.00 54.03  ? 221 PRO B C     1 
ATOM   6246 O O     . PRO B 1 223 ? 31.151  -53.834 43.017  1.00 49.19  ? 221 PRO B O     1 
ATOM   6247 C CB    . PRO B 1 223 ? 31.984  -56.421 44.884  1.00 52.10  ? 221 PRO B CB    1 
ATOM   6248 C CG    . PRO B 1 223 ? 31.422  -56.147 46.282  1.00 51.94  ? 221 PRO B CG    1 
ATOM   6249 C CD    . PRO B 1 223 ? 31.388  -54.638 46.465  1.00 51.20  ? 221 PRO B CD    1 
ATOM   6250 N N     . GLN B 1 224 ? 32.524  -55.344 41.993  1.00 51.50  ? 222 GLN B N     1 
ATOM   6251 C CA    . GLN B 1 224 ? 32.049  -55.217 40.591  1.00 52.57  ? 222 GLN B CA    1 
ATOM   6252 C C     . GLN B 1 224 ? 30.706  -55.928 40.413  1.00 47.33  ? 222 GLN B C     1 
ATOM   6253 O O     . GLN B 1 224 ? 30.350  -56.812 41.212  1.00 49.99  ? 222 GLN B O     1 
ATOM   6254 C CB    . GLN B 1 224 ? 33.077  -55.799 39.610  1.00 61.58  ? 222 GLN B CB    1 
ATOM   6255 C CG    . GLN B 1 224 ? 34.274  -54.882 39.377  1.00 68.68  ? 222 GLN B CG    1 
ATOM   6256 C CD    . GLN B 1 224 ? 33.823  -53.471 39.078  1.00 76.01  ? 222 GLN B CD    1 
ATOM   6257 O OE1   . GLN B 1 224 ? 33.145  -53.218 38.084  1.00 82.73  ? 222 GLN B OE1   1 
ATOM   6258 N NE2   . GLN B 1 224 ? 34.165  -52.537 39.950  1.00 74.46  ? 222 GLN B NE2   1 
ATOM   6259 N N     . GLY B 1 225 ? 29.926  -55.424 39.464  1.00 50.06  ? 223 GLY B N     1 
ATOM   6260 C CA    . GLY B 1 225 ? 28.634  -56.046 39.143  1.00 48.56  ? 223 GLY B CA    1 
ATOM   6261 C C     . GLY B 1 225 ? 27.524  -55.784 40.129  1.00 47.68  ? 223 GLY B C     1 
ATOM   6262 O O     . GLY B 1 225 ? 27.633  -54.839 40.916  1.00 47.19  ? 223 GLY B O     1 
ATOM   6263 N N     . THR B 1 226 ? 26.491  -56.611 40.064  1.00 45.01  ? 224 THR B N     1 
ATOM   6264 C CA    . THR B 1 226 ? 25.308  -56.478 40.930  1.00 51.02  ? 224 THR B CA    1 
ATOM   6265 C C     . THR B 1 226 ? 25.721  -56.405 42.391  1.00 57.84  ? 224 THR B C     1 
ATOM   6266 O O     . THR B 1 226 ? 25.075  -55.668 43.150  1.00 55.96  ? 224 THR B O     1 
ATOM   6267 C CB    . THR B 1 226 ? 24.448  -57.725 40.735  1.00 51.93  ? 224 THR B CB    1 
ATOM   6268 O OG1   . THR B 1 226 ? 23.714  -57.958 41.935  1.00 77.16  ? 224 THR B OG1   1 
ATOM   6269 C CG2   . THR B 1 226 ? 25.277  -58.949 40.421  1.00 54.20  ? 224 THR B CG2   1 
ATOM   6270 N N     . LYS B 1 227 ? 26.767  -57.139 42.757  1.00 59.38  ? 225 LYS B N     1 
ATOM   6271 C CA    . LYS B 1 227 ? 27.139  -57.216 44.189  1.00 53.98  ? 225 LYS B CA    1 
ATOM   6272 C C     . LYS B 1 227 ? 27.777  -55.905 44.666  1.00 50.54  ? 225 LYS B C     1 
ATOM   6273 O O     . LYS B 1 227 ? 28.106  -55.837 45.863  1.00 54.04  ? 225 LYS B O     1 
ATOM   6274 C CB    . LYS B 1 227 ? 28.060  -58.417 44.403  1.00 57.04  ? 225 LYS B CB    1 
ATOM   6275 C CG    . LYS B 1 227 ? 27.335  -59.713 44.769  1.00 60.13  ? 225 LYS B CG    1 
ATOM   6276 C CD    . LYS B 1 227 ? 27.523  -60.834 43.789  1.00 60.07  ? 225 LYS B CD    1 
ATOM   6277 C CE    . LYS B 1 227 ? 28.988  -61.132 43.535  1.00 62.18  ? 225 LYS B CE    1 
ATOM   6278 N NZ    . LYS B 1 227 ? 29.161  -62.289 42.624  1.00 62.04  ? 225 LYS B NZ    1 
ATOM   6279 N N     . GLY B 1 228 ? 27.898  -54.887 43.800  1.00 48.61  ? 226 GLY B N     1 
ATOM   6280 C CA    . GLY B 1 228 ? 28.429  -53.546 44.148  1.00 44.43  ? 226 GLY B CA    1 
ATOM   6281 C C     . GLY B 1 228 ? 27.361  -52.461 44.162  1.00 42.76  ? 226 GLY B C     1 
ATOM   6282 O O     . GLY B 1 228 ? 27.715  -51.285 44.279  1.00 41.27  ? 226 GLY B O     1 
ATOM   6283 N N     . ILE B 1 229 ? 26.098  -52.874 44.077  1.00 47.45  ? 227 ILE B N     1 
ATOM   6284 C CA    . ILE B 1 229 ? 24.975  -51.907 43.938  1.00 49.92  ? 227 ILE B CA    1 
ATOM   6285 C C     . ILE B 1 229 ? 24.251  -51.692 45.264  1.00 45.51  ? 227 ILE B C     1 
ATOM   6286 O O     . ILE B 1 229 ? 23.914  -52.675 45.918  1.00 40.22  ? 227 ILE B O     1 
ATOM   6287 C CB    . ILE B 1 229 ? 24.002  -52.381 42.836  1.00 51.07  ? 227 ILE B CB    1 
ATOM   6288 C CG1   . ILE B 1 229 ? 24.706  -52.594 41.495  1.00 54.26  ? 227 ILE B CG1   1 
ATOM   6289 C CG2   . ILE B 1 229 ? 22.830  -51.425 42.711  1.00 59.17  ? 227 ILE B CG2   1 
ATOM   6290 C CD1   . ILE B 1 229 ? 23.833  -53.254 40.457  1.00 56.27  ? 227 ILE B CD1   1 
ATOM   6291 N N     . SER B 1 230 ? 24.006  -50.433 45.600  1.00 48.60  ? 228 SER B N     1 
ATOM   6292 C CA    . SER B 1 230 ? 23.270  -50.055 46.834  1.00 48.87  ? 228 SER B CA    1 
ATOM   6293 C C     . SER B 1 230 ? 22.093  -49.130 46.477  1.00 48.86  ? 228 SER B C     1 
ATOM   6294 O O     . SER B 1 230 ? 22.113  -48.477 45.393  1.00 46.17  ? 228 SER B O     1 
ATOM   6295 C CB    . SER B 1 230 ? 24.227  -49.429 47.828  1.00 48.32  ? 228 SER B CB    1 
ATOM   6296 O OG    . SER B 1 230 ? 25.217  -50.367 48.267  1.00 46.56  ? 228 SER B OG    1 
ATOM   6297 N N     . LEU B 1 231 ? 21.100  -49.080 47.358  1.00 42.41  ? 229 LEU B N     1 
ATOM   6298 C CA    . LEU B 1 231 ? 19.832  -48.342 47.164  1.00 42.01  ? 229 LEU B CA    1 
ATOM   6299 C C     . LEU B 1 231 ? 19.857  -47.069 48.004  1.00 45.33  ? 229 LEU B C     1 
ATOM   6300 O O     . LEU B 1 231 ? 20.154  -47.177 49.200  1.00 51.64  ? 229 LEU B O     1 
ATOM   6301 C CB    . LEU B 1 231 ? 18.706  -49.269 47.615  1.00 47.02  ? 229 LEU B CB    1 
ATOM   6302 C CG    . LEU B 1 231 ? 17.366  -49.082 46.931  1.00 51.95  ? 229 LEU B CG    1 
ATOM   6303 C CD1   . LEU B 1 231 ? 17.561  -49.159 45.427  1.00 56.27  ? 229 LEU B CD1   1 
ATOM   6304 C CD2   . LEU B 1 231 ? 16.386  -50.146 47.401  1.00 52.67  ? 229 LEU B CD2   1 
ATOM   6305 N N     . PHE B 1 232 ? 19.509  -45.920 47.420  1.00 47.90  ? 230 PHE B N     1 
ATOM   6306 C CA    . PHE B 1 232 ? 19.526  -44.590 48.082  1.00 48.17  ? 230 PHE B CA    1 
ATOM   6307 C C     . PHE B 1 232 ? 18.168  -43.904 47.946  1.00 53.82  ? 230 PHE B C     1 
ATOM   6308 O O     . PHE B 1 232 ? 17.531  -44.032 46.878  1.00 58.52  ? 230 PHE B O     1 
ATOM   6309 C CB    . PHE B 1 232 ? 20.669  -43.740 47.534  1.00 47.69  ? 230 PHE B CB    1 
ATOM   6310 C CG    . PHE B 1 232 ? 21.988  -44.379 47.842  1.00 49.36  ? 230 PHE B CG    1 
ATOM   6311 C CD1   . PHE B 1 232 ? 22.507  -45.344 46.998  1.00 49.01  ? 230 PHE B CD1   1 
ATOM   6312 C CD2   . PHE B 1 232 ? 22.633  -44.117 49.042  1.00 52.17  ? 230 PHE B CD2   1 
ATOM   6313 C CE1   . PHE B 1 232 ? 23.706  -45.966 47.296  1.00 48.15  ? 230 PHE B CE1   1 
ATOM   6314 C CE2   . PHE B 1 232 ? 23.825  -44.755 49.347  1.00 50.52  ? 230 PHE B CE2   1 
ATOM   6315 C CZ    . PHE B 1 232 ? 24.355  -45.674 48.473  1.00 52.57  ? 230 PHE B CZ    1 
ATOM   6316 N N     . ILE B 1 233 ? 17.733  -43.254 49.034  1.00 49.38  ? 231 ILE B N     1 
ATOM   6317 C CA    . ILE B 1 233 ? 16.619  -42.268 49.053  1.00 46.72  ? 231 ILE B CA    1 
ATOM   6318 C C     . ILE B 1 233 ? 17.214  -40.904 48.733  1.00 46.34  ? 231 ILE B C     1 
ATOM   6319 O O     . ILE B 1 233 ? 18.020  -40.439 49.529  1.00 47.66  ? 231 ILE B O     1 
ATOM   6320 C CB    . ILE B 1 233 ? 15.893  -42.240 50.405  1.00 46.54  ? 231 ILE B CB    1 
ATOM   6321 C CG1   . ILE B 1 233 ? 15.350  -43.610 50.797  1.00 42.87  ? 231 ILE B CG1   1 
ATOM   6322 C CG2   . ILE B 1 233 ? 14.784  -41.194 50.395  1.00 48.46  ? 231 ILE B CG2   1 
ATOM   6323 C CD1   . ILE B 1 233 ? 14.903  -43.675 52.236  1.00 44.78  ? 231 ILE B CD1   1 
ATOM   6324 N N     . VAL B 1 234 ? 16.816  -40.308 47.608  1.00 48.70  ? 232 VAL B N     1 
ATOM   6325 C CA    . VAL B 1 234 ? 17.233  -38.940 47.175  1.00 47.94  ? 232 VAL B CA    1 
ATOM   6326 C C     . VAL B 1 234 ? 15.955  -38.160 46.880  1.00 56.27  ? 232 VAL B C     1 
ATOM   6327 O O     . VAL B 1 234 ? 15.328  -38.350 45.842  1.00 57.33  ? 232 VAL B O     1 
ATOM   6328 C CB    . VAL B 1 234 ? 18.150  -38.967 45.943  1.00 42.16  ? 232 VAL B CB    1 
ATOM   6329 C CG1   . VAL B 1 234 ? 18.837  -37.636 45.743  1.00 45.69  ? 232 VAL B CG1   1 
ATOM   6330 C CG2   . VAL B 1 234 ? 19.164  -40.093 45.988  1.00 42.05  ? 232 VAL B CG2   1 
ATOM   6331 N N     . PRO B 1 235 ? 15.496  -37.288 47.798  1.00 53.21  ? 233 PRO B N     1 
ATOM   6332 C CA    . PRO B 1 235 ? 14.282  -36.517 47.569  1.00 45.76  ? 233 PRO B CA    1 
ATOM   6333 C C     . PRO B 1 235 ? 14.627  -35.218 46.836  1.00 44.74  ? 233 PRO B C     1 
ATOM   6334 O O     . PRO B 1 235 ? 15.745  -34.705 46.964  1.00 41.06  ? 233 PRO B O     1 
ATOM   6335 C CB    . PRO B 1 235 ? 13.822  -36.302 49.003  1.00 47.47  ? 233 PRO B CB    1 
ATOM   6336 C CG    . PRO B 1 235 ? 15.119  -36.048 49.723  1.00 52.47  ? 233 PRO B CG    1 
ATOM   6337 C CD    . PRO B 1 235 ? 16.128  -36.982 49.088  1.00 53.11  ? 233 PRO B CD    1 
ATOM   6338 N N     . LYS B 1 236 ? 13.689  -34.731 46.037  1.00 42.41  ? 234 LYS B N     1 
ATOM   6339 C CA    . LYS B 1 236 ? 13.897  -33.492 45.249  1.00 44.60  ? 234 LYS B CA    1 
ATOM   6340 C C     . LYS B 1 236 ? 14.096  -32.346 46.253  1.00 44.01  ? 234 LYS B C     1 
ATOM   6341 O O     . LYS B 1 236 ? 15.020  -31.504 46.076  1.00 41.76  ? 234 LYS B O     1 
ATOM   6342 C CB    . LYS B 1 236 ? 12.695  -33.296 44.318  1.00 43.04  ? 234 LYS B CB    1 
ATOM   6343 C CG    . LYS B 1 236 ? 12.773  -32.093 43.391  1.00 46.94  ? 234 LYS B CG    1 
ATOM   6344 C CD    . LYS B 1 236 ? 11.433  -31.748 42.742  1.00 44.54  ? 234 LYS B CD    1 
ATOM   6345 C CE    . LYS B 1 236 ? 11.511  -30.485 41.915  1.00 39.34  ? 234 LYS B CE    1 
ATOM   6346 N NZ    . LYS B 1 236 ? 10.157  -30.116 41.465  1.00 40.21  ? 234 LYS B NZ    1 
ATOM   6347 N N     . PHE B 1 237 ? 13.247  -32.341 47.283  1.00 42.19  ? 235 PHE B N     1 
ATOM   6348 C CA    . PHE B 1 237 ? 13.307  -31.415 48.446  1.00 47.14  ? 235 PHE B CA    1 
ATOM   6349 C C     . PHE B 1 237 ? 13.614  -32.253 49.699  1.00 45.14  ? 235 PHE B C     1 
ATOM   6350 O O     . PHE B 1 237 ? 12.850  -33.216 49.960  1.00 42.63  ? 235 PHE B O     1 
ATOM   6351 C CB    . PHE B 1 237 ? 12.008  -30.613 48.619  1.00 43.47  ? 235 PHE B CB    1 
ATOM   6352 C CG    . PHE B 1 237 ? 11.685  -29.635 47.517  1.00 41.34  ? 235 PHE B CG    1 
ATOM   6353 C CD1   . PHE B 1 237 ? 12.363  -28.429 47.415  1.00 42.42  ? 235 PHE B CD1   1 
ATOM   6354 C CD2   . PHE B 1 237 ? 10.671  -29.903 46.602  1.00 44.38  ? 235 PHE B CD2   1 
ATOM   6355 C CE1   . PHE B 1 237 ? 12.058  -27.520 46.410  1.00 43.51  ? 235 PHE B CE1   1 
ATOM   6356 C CE2   . PHE B 1 237 ? 10.368  -29.001 45.589  1.00 44.19  ? 235 PHE B CE2   1 
ATOM   6357 C CZ    . PHE B 1 237 ? 11.056  -27.807 45.501  1.00 45.54  ? 235 PHE B CZ    1 
ATOM   6358 N N     . LEU B 1 238 ? 14.716  -31.936 50.399  1.00 41.83  ? 236 LEU B N     1 
ATOM   6359 C CA    . LEU B 1 238 ? 15.085  -32.559 51.703  1.00 43.27  ? 236 LEU B CA    1 
ATOM   6360 C C     . LEU B 1 238 ? 14.067  -32.081 52.716  1.00 38.74  ? 236 LEU B C     1 
ATOM   6361 O O     . LEU B 1 238 ? 13.712  -30.894 52.689  1.00 35.51  ? 236 LEU B O     1 
ATOM   6362 C CB    . LEU B 1 238 ? 16.486  -32.107 52.119  1.00 44.97  ? 236 LEU B CB    1 
ATOM   6363 C CG    . LEU B 1 238 ? 17.613  -32.587 51.204  1.00 44.04  ? 236 LEU B CG    1 
ATOM   6364 C CD1   . LEU B 1 238 ? 18.820  -31.657 51.259  1.00 43.14  ? 236 LEU B CD1   1 
ATOM   6365 C CD2   . LEU B 1 238 ? 17.982  -34.010 51.553  1.00 42.69  ? 236 LEU B CD2   1 
ATOM   6366 N N     . PRO B 1 239 ? 13.580  -32.967 53.611  1.00 40.79  ? 237 PRO B N     1 
ATOM   6367 C CA    . PRO B 1 239 ? 12.565  -32.581 54.595  1.00 51.36  ? 237 PRO B CA    1 
ATOM   6368 C C     . PRO B 1 239 ? 13.022  -31.387 55.455  1.00 47.67  ? 237 PRO B C     1 
ATOM   6369 O O     . PRO B 1 239 ? 14.226  -31.162 55.595  1.00 43.85  ? 237 PRO B O     1 
ATOM   6370 C CB    . PRO B 1 239 ? 12.356  -33.814 55.491  1.00 48.86  ? 237 PRO B CB    1 
ATOM   6371 C CG    . PRO B 1 239 ? 13.036  -34.958 54.750  1.00 46.77  ? 237 PRO B CG    1 
ATOM   6372 C CD    . PRO B 1 239 ? 14.072  -34.329 53.840  1.00 45.19  ? 237 PRO B CD    1 
ATOM   6373 N N     . ASN B 1 240 ? 12.058  -30.608 55.942  1.00 44.59  ? 238 ASN B N     1 
ATOM   6374 C CA    . ASN B 1 240 ? 12.284  -29.545 56.957  1.00 47.04  ? 238 ASN B CA    1 
ATOM   6375 C C     . ASN B 1 240 ? 11.921  -30.137 58.325  1.00 49.23  ? 238 ASN B C     1 
ATOM   6376 O O     . ASN B 1 240 ? 11.594  -31.358 58.374  1.00 51.97  ? 238 ASN B O     1 
ATOM   6377 C CB    . ASN B 1 240 ? 11.542  -28.259 56.582  1.00 40.93  ? 238 ASN B CB    1 
ATOM   6378 C CG    . ASN B 1 240 ? 10.035  -28.389 56.677  1.00 41.28  ? 238 ASN B CG    1 
ATOM   6379 O OD1   . ASN B 1 240 ? 9.489   -29.425 57.075  1.00 38.94  ? 238 ASN B OD1   1 
ATOM   6380 N ND2   . ASN B 1 240 ? 9.343   -27.334 56.297  1.00 41.89  ? 238 ASN B ND2   1 
ATOM   6381 N N     . ALA B 1 241 ? 11.969  -29.311 59.381  1.00 61.02  ? 239 ALA B N     1 
ATOM   6382 C CA    . ALA B 1 241 ? 11.742  -29.680 60.806  1.00 54.68  ? 239 ALA B CA    1 
ATOM   6383 C C     . ALA B 1 241 ? 10.368  -30.327 60.995  1.00 53.81  ? 239 ALA B C     1 
ATOM   6384 O O     . ALA B 1 241 ? 10.272  -31.212 61.857  1.00 61.34  ? 239 ALA B O     1 
ATOM   6385 C CB    . ALA B 1 241 ? 11.865  -28.465 61.689  1.00 55.52  ? 239 ALA B CB    1 
ATOM   6386 N N     . GLU B 1 242 ? 9.345   -29.913 60.232  1.00 55.19  ? 240 GLU B N     1 
ATOM   6387 C CA    . GLU B 1 242 ? 7.959   -30.457 60.353  1.00 54.50  ? 240 GLU B CA    1 
ATOM   6388 C C     . GLU B 1 242 ? 7.756   -31.666 59.415  1.00 52.62  ? 240 GLU B C     1 
ATOM   6389 O O     . GLU B 1 242 ? 6.673   -32.270 59.483  1.00 53.43  ? 240 GLU B O     1 
ATOM   6390 C CB    . GLU B 1 242 ? 6.922   -29.358 60.119  1.00 57.68  ? 240 GLU B CB    1 
ATOM   6391 C CG    . GLU B 1 242 ? 7.124   -28.127 60.987  1.00 61.43  ? 240 GLU B CG    1 
ATOM   6392 C CD    . GLU B 1 242 ? 7.953   -27.053 60.306  1.00 70.75  ? 240 GLU B CD    1 
ATOM   6393 O OE1   . GLU B 1 242 ? 9.117   -27.339 59.970  1.00 81.75  ? 240 GLU B OE1   1 
ATOM   6394 O OE2   . GLU B 1 242 ? 7.422   -25.955 60.062  1.00 77.02  ? 240 GLU B OE2   1 
ATOM   6395 N N     . GLY B 1 243 ? 8.750   -32.025 58.588  1.00 56.88  ? 241 GLY B N     1 
ATOM   6396 C CA    . GLY B 1 243 ? 8.687   -33.147 57.622  1.00 54.69  ? 241 GLY B CA    1 
ATOM   6397 C C     . GLY B 1 243 ? 8.182   -32.732 56.238  1.00 54.68  ? 241 GLY B C     1 
ATOM   6398 O O     . GLY B 1 243 ? 7.759   -33.613 55.469  1.00 55.26  ? 241 GLY B O     1 
ATOM   6399 N N     . ASN B 1 244 ? 8.246   -31.450 55.887  1.00 50.53  ? 242 ASN B N     1 
ATOM   6400 C CA    . ASN B 1 244 ? 7.633   -30.934 54.639  1.00 55.25  ? 242 ASN B CA    1 
ATOM   6401 C C     . ASN B 1 244 ? 8.729   -30.607 53.651  1.00 52.16  ? 242 ASN B C     1 
ATOM   6402 O O     . ASN B 1 244 ? 9.879   -30.494 54.078  1.00 53.09  ? 242 ASN B O     1 
ATOM   6403 C CB    . ASN B 1 244 ? 6.717   -29.741 54.901  1.00 52.59  ? 242 ASN B CB    1 
ATOM   6404 C CG    . ASN B 1 244 ? 5.548   -30.204 55.732  1.00 53.88  ? 242 ASN B CG    1 
ATOM   6405 O OD1   . ASN B 1 244 ? 5.205   -31.383 55.711  1.00 50.71  ? 242 ASN B OD1   1 
ATOM   6406 N ND2   . ASN B 1 244 ? 4.989   -29.313 56.521  1.00 61.15  ? 242 ASN B ND2   1 
ATOM   6407 N N     . ALA B 1 245 ? 8.380   -30.513 52.372  1.00 50.82  ? 243 ALA B N     1 
ATOM   6408 C CA    . ALA B 1 245 ? 9.380   -30.132 51.353  1.00 53.94  ? 243 ALA B CA    1 
ATOM   6409 C C     . ALA B 1 245 ? 10.218  -29.037 52.008  1.00 48.88  ? 243 ALA B C     1 
ATOM   6410 O O     . ALA B 1 245 ? 9.627   -28.105 52.486  1.00 48.37  ? 243 ALA B O     1 
ATOM   6411 C CB    . ALA B 1 245 ? 8.717   -29.677 50.069  1.00 49.07  ? 243 ALA B CB    1 
ATOM   6412 N N     . GLY B 1 246 ? 11.523  -29.214 52.130  1.00 52.86  ? 244 GLY B N     1 
ATOM   6413 C CA    . GLY B 1 246 ? 12.394  -28.186 52.704  1.00 52.42  ? 244 GLY B CA    1 
ATOM   6414 C C     . GLY B 1 246 ? 13.359  -27.690 51.662  1.00 56.96  ? 244 GLY B C     1 
ATOM   6415 O O     . GLY B 1 246 ? 12.903  -27.211 50.616  1.00 56.13  ? 244 GLY B O     1 
ATOM   6416 N N     . GLU B 1 247 ? 14.646  -27.862 51.947  1.00 57.01  ? 245 GLU B N     1 
ATOM   6417 C CA    . GLU B 1 247 ? 15.791  -27.407 51.133  1.00 54.51  ? 245 GLU B CA    1 
ATOM   6418 C C     . GLU B 1 247 ? 15.823  -28.181 49.802  1.00 58.88  ? 245 GLU B C     1 
ATOM   6419 O O     . GLU B 1 247 ? 15.751  -29.449 49.825  1.00 49.53  ? 245 GLU B O     1 
ATOM   6420 C CB    . GLU B 1 247 ? 17.046  -27.636 51.975  1.00 62.08  ? 245 GLU B CB    1 
ATOM   6421 C CG    . GLU B 1 247 ? 18.348  -27.354 51.253  1.00 70.80  ? 245 GLU B CG    1 
ATOM   6422 C CD    . GLU B 1 247 ? 18.747  -25.894 51.239  1.00 75.09  ? 245 GLU B CD    1 
ATOM   6423 O OE1   . GLU B 1 247 ? 17.863  -25.041 51.446  1.00 79.72  ? 245 GLU B OE1   1 
ATOM   6424 O OE2   . GLU B 1 247 ? 19.945  -25.621 51.042  1.00 82.76  ? 245 GLU B OE2   1 
ATOM   6425 N N     . ARG B 1 248 ? 15.997  -27.455 48.694  1.00 52.01  ? 246 ARG B N     1 
ATOM   6426 C CA    . ARG B 1 248 ? 16.067  -28.013 47.323  1.00 51.40  ? 246 ARG B CA    1 
ATOM   6427 C C     . ARG B 1 248 ? 17.381  -28.780 47.181  1.00 49.65  ? 246 ARG B C     1 
ATOM   6428 O O     . ARG B 1 248 ? 18.466  -28.149 47.171  1.00 45.09  ? 246 ARG B O     1 
ATOM   6429 C CB    . ARG B 1 248 ? 15.966  -26.908 46.260  1.00 57.15  ? 246 ARG B CB    1 
ATOM   6430 C CG    . ARG B 1 248 ? 16.049  -27.376 44.808  1.00 55.95  ? 246 ARG B CG    1 
ATOM   6431 C CD    . ARG B 1 248 ? 15.022  -28.450 44.428  1.00 63.26  ? 246 ARG B CD    1 
ATOM   6432 N NE    . ARG B 1 248 ? 15.390  -29.118 43.181  1.00 68.12  ? 246 ARG B NE    1 
ATOM   6433 C CZ    . ARG B 1 248 ? 15.043  -28.713 41.961  1.00 60.90  ? 246 ARG B CZ    1 
ATOM   6434 N NH1   . ARG B 1 248 ? 14.284  -27.644 41.809  1.00 65.06  ? 246 ARG B NH1   1 
ATOM   6435 N NH2   . ARG B 1 248 ? 15.461  -29.371 40.893  1.00 60.21  ? 246 ARG B NH2   1 
ATOM   6436 N N     . ASN B 1 249 ? 17.267  -30.090 46.996  1.00 42.65  ? 247 ASN B N     1 
ATOM   6437 C CA    . ASN B 1 249 ? 18.404  -31.010 46.754  1.00 44.15  ? 247 ASN B CA    1 
ATOM   6438 C C     . ASN B 1 249 ? 18.973  -30.750 45.332  1.00 46.79  ? 247 ASN B C     1 
ATOM   6439 O O     . ASN B 1 249 ? 18.266  -30.129 44.512  1.00 44.90  ? 247 ASN B O     1 
ATOM   6440 C CB    . ASN B 1 249 ? 17.878  -32.417 47.057  1.00 44.84  ? 247 ASN B CB    1 
ATOM   6441 C CG    . ASN B 1 249 ? 18.937  -33.409 47.448  1.00 42.26  ? 247 ASN B CG    1 
ATOM   6442 O OD1   . ASN B 1 249 ? 20.123  -33.109 47.408  1.00 46.13  ? 247 ASN B OD1   1 
ATOM   6443 N ND2   . ASN B 1 249 ? 18.506  -34.608 47.776  1.00 46.03  ? 247 ASN B ND2   1 
ATOM   6444 N N     . ALA B 1 250 ? 20.206  -31.177 45.016  1.00 48.17  ? 248 ALA B N     1 
ATOM   6445 C CA    . ALA B 1 250 ? 20.839  -30.954 43.689  1.00 50.77  ? 248 ALA B CA    1 
ATOM   6446 C C     . ALA B 1 250 ? 20.517  -32.146 42.764  1.00 51.17  ? 248 ALA B C     1 
ATOM   6447 O O     . ALA B 1 250 ? 21.444  -32.820 42.237  1.00 44.45  ? 248 ALA B O     1 
ATOM   6448 C CB    . ALA B 1 250 ? 22.316  -30.682 43.833  1.00 46.54  ? 248 ALA B CB    1 
ATOM   6449 N N     . VAL B 1 251 ? 19.211  -32.378 42.613  1.00 52.86  ? 249 VAL B N     1 
ATOM   6450 C CA    . VAL B 1 251 ? 18.537  -33.277 41.637  1.00 53.35  ? 249 VAL B CA    1 
ATOM   6451 C C     . VAL B 1 251 ? 17.835  -32.386 40.617  1.00 52.33  ? 249 VAL B C     1 
ATOM   6452 O O     . VAL B 1 251 ? 16.962  -31.588 41.057  1.00 48.67  ? 249 VAL B O     1 
ATOM   6453 C CB    . VAL B 1 251 ? 17.478  -34.155 42.323  1.00 56.24  ? 249 VAL B CB    1 
ATOM   6454 C CG1   . VAL B 1 251 ? 17.018  -35.261 41.389  1.00 61.61  ? 249 VAL B CG1   1 
ATOM   6455 C CG2   . VAL B 1 251 ? 17.961  -34.722 43.649  1.00 61.80  ? 249 VAL B CG2   1 
ATOM   6456 N N     . SER B 1 252 ? 18.152  -32.512 39.326  1.00 42.54  ? 250 SER B N     1 
ATOM   6457 C CA    . SER B 1 252 ? 17.413  -31.764 38.276  1.00 43.58  ? 250 SER B CA    1 
ATOM   6458 C C     . SER B 1 252 ? 17.224  -32.607 37.018  1.00 40.79  ? 250 SER B C     1 
ATOM   6459 O O     . SER B 1 252 ? 17.989  -33.577 36.779  1.00 36.64  ? 250 SER B O     1 
ATOM   6460 C CB    . SER B 1 252 ? 18.053  -30.456 37.948  1.00 39.27  ? 250 SER B CB    1 
ATOM   6461 O OG    . SER B 1 252 ? 19.374  -30.678 37.485  1.00 41.12  ? 250 SER B OG    1 
ATOM   6462 N N     . CYS B 1 253 ? 16.206  -32.212 36.261  1.00 41.22  ? 251 CYS B N     1 
ATOM   6463 C CA    . CYS B 1 253 ? 15.833  -32.810 34.962  1.00 40.56  ? 251 CYS B CA    1 
ATOM   6464 C C     . CYS B 1 253 ? 16.490  -31.977 33.858  1.00 36.01  ? 251 CYS B C     1 
ATOM   6465 O O     . CYS B 1 253 ? 16.181  -30.803 33.773  1.00 37.80  ? 251 CYS B O     1 
ATOM   6466 C CB    . CYS B 1 253 ? 14.321  -32.900 34.847  1.00 40.31  ? 251 CYS B CB    1 
ATOM   6467 S SG    . CYS B 1 253 ? 13.807  -33.568 33.242  1.00 44.58  ? 251 CYS B SG    1 
ATOM   6468 N N     . GLY B 1 254 ? 17.454  -32.545 33.136  1.00 38.65  ? 252 GLY B N     1 
ATOM   6469 C CA    . GLY B 1 254 ? 18.147  -31.899 32.002  1.00 39.10  ? 252 GLY B CA    1 
ATOM   6470 C C     . GLY B 1 254 ? 17.319  -31.958 30.719  1.00 44.65  ? 252 GLY B C     1 
ATOM   6471 O O     . GLY B 1 254 ? 17.607  -31.141 29.813  1.00 43.78  ? 252 GLY B O     1 
ATOM   6472 N N     . SER B 1 255 ? 16.333  -32.878 30.618  1.00 41.51  ? 253 SER B N     1 
ATOM   6473 C CA    . SER B 1 255 ? 15.459  -33.066 29.417  1.00 40.43  ? 253 SER B CA    1 
ATOM   6474 C C     . SER B 1 255 ? 14.438  -34.182 29.622  1.00 39.86  ? 253 SER B C     1 
ATOM   6475 O O     . SER B 1 255 ? 14.604  -35.031 30.556  1.00 36.03  ? 253 SER B O     1 
ATOM   6476 C CB    . SER B 1 255 ? 16.250  -33.345 28.148  1.00 38.06  ? 253 SER B CB    1 
ATOM   6477 O OG    . SER B 1 255 ? 17.101  -34.467 28.298  1.00 37.24  ? 253 SER B OG    1 
ATOM   6478 N N     . ILE B 1 256 ? 13.420  -34.166 28.759  1.00 37.51  ? 254 ILE B N     1 
ATOM   6479 C CA    . ILE B 1 256 ? 12.436  -35.277 28.646  1.00 34.53  ? 254 ILE B CA    1 
ATOM   6480 C C     . ILE B 1 256 ? 12.567  -35.881 27.254  1.00 33.23  ? 254 ILE B C     1 
ATOM   6481 O O     . ILE B 1 256 ? 13.229  -35.263 26.427  1.00 31.66  ? 254 ILE B O     1 
ATOM   6482 C CB    . ILE B 1 256 ? 11.026  -34.813 29.018  1.00 34.30  ? 254 ILE B CB    1 
ATOM   6483 C CG1   . ILE B 1 256 ? 10.419  -33.843 28.005  1.00 36.30  ? 254 ILE B CG1   1 
ATOM   6484 C CG2   . ILE B 1 256 ? 11.055  -34.220 30.423  1.00 35.21  ? 254 ILE B CG2   1 
ATOM   6485 C CD1   . ILE B 1 256 ? 8.925   -33.650 28.184  1.00 35.23  ? 254 ILE B CD1   1 
ATOM   6486 N N     . GLU B 1 257 ? 12.057  -37.095 27.056  1.00 32.51  ? 255 GLU B N     1 
ATOM   6487 C CA    . GLU B 1 257 ? 12.211  -37.827 25.781  1.00 34.27  ? 255 GLU B CA    1 
ATOM   6488 C C     . GLU B 1 257 ? 11.046  -37.453 24.867  1.00 31.82  ? 255 GLU B C     1 
ATOM   6489 O O     . GLU B 1 257 ? 9.963   -37.212 25.381  1.00 32.26  ? 255 GLU B O     1 
ATOM   6490 C CB    . GLU B 1 257 ? 12.274  -39.332 26.035  1.00 37.21  ? 255 GLU B CB    1 
ATOM   6491 C CG    . GLU B 1 257 ? 13.486  -39.755 26.840  1.00 37.66  ? 255 GLU B CG    1 
ATOM   6492 C CD    . GLU B 1 257 ? 14.860  -39.527 26.210  1.00 38.64  ? 255 GLU B CD    1 
ATOM   6493 O OE1   . GLU B 1 257 ? 15.811  -39.286 26.979  1.00 34.57  ? 255 GLU B OE1   1 
ATOM   6494 O OE2   . GLU B 1 257 ? 15.004  -39.640 24.969  1.00 35.00  ? 255 GLU B OE2   1 
ATOM   6495 N N     . HIS B 1 258 ? 11.293  -37.372 23.559  1.00 36.58  ? 256 HIS B N     1 
ATOM   6496 C CA    . HIS B 1 258 ? 10.248  -37.477 22.498  1.00 35.60  ? 256 HIS B CA    1 
ATOM   6497 C C     . HIS B 1 258 ? 10.062  -38.957 22.204  1.00 31.18  ? 256 HIS B C     1 
ATOM   6498 O O     . HIS B 1 258 ? 11.054  -39.595 21.787  1.00 30.37  ? 256 HIS B O     1 
ATOM   6499 C CB    . HIS B 1 258 ? 10.668  -36.728 21.238  1.00 44.75  ? 256 HIS B CB    1 
ATOM   6500 C CG    . HIS B 1 258 ? 11.160  -35.358 21.531  1.00 55.48  ? 256 HIS B CG    1 
ATOM   6501 N ND1   . HIS B 1 258 ? 10.295  -34.278 21.649  1.00 58.38  ? 256 HIS B ND1   1 
ATOM   6502 C CD2   . HIS B 1 258 ? 12.408  -34.896 21.764  1.00 59.83  ? 256 HIS B CD2   1 
ATOM   6503 C CE1   . HIS B 1 258 ? 10.997  -33.199 21.931  1.00 61.43  ? 256 HIS B CE1   1 
ATOM   6504 N NE2   . HIS B 1 258 ? 12.293  -33.554 22.013  1.00 64.69  ? 256 HIS B NE2   1 
ATOM   6505 N N     . LYS B 1 259 ? 8.870   -39.468 22.488  1.00 30.30  ? 257 LYS B N     1 
ATOM   6506 C CA    . LYS B 1 259 ? 8.624   -40.920 22.356  1.00 32.27  ? 257 LYS B CA    1 
ATOM   6507 C C     . LYS B 1 259 ? 7.422   -41.233 21.454  1.00 32.56  ? 257 LYS B C     1 
ATOM   6508 O O     . LYS B 1 259 ? 6.670   -40.309 21.144  1.00 31.68  ? 257 LYS B O     1 
ATOM   6509 C CB    . LYS B 1 259 ? 8.458   -41.524 23.755  1.00 31.27  ? 257 LYS B CB    1 
ATOM   6510 C CG    . LYS B 1 259 ? 9.262   -40.871 24.865  1.00 33.19  ? 257 LYS B CG    1 
ATOM   6511 C CD    . LYS B 1 259 ? 8.994   -41.491 26.213  1.00 33.10  ? 257 LYS B CD    1 
ATOM   6512 C CE    . LYS B 1 259 ? 7.546   -41.379 26.631  1.00 33.87  ? 257 LYS B CE    1 
ATOM   6513 N NZ    . LYS B 1 259 ? 7.208   -40.011 27.084  1.00 35.55  ? 257 LYS B NZ    1 
ATOM   6514 N N     . MET B 1 260 ? 7.257   -42.497 21.078  1.00 32.01  ? 258 MET B N     1 
ATOM   6515 C CA    . MET B 1 260 ? 6.189   -43.020 20.180  1.00 29.67  ? 258 MET B CA    1 
ATOM   6516 C C     . MET B 1 260 ? 4.841   -42.825 20.845  1.00 29.30  ? 258 MET B C     1 
ATOM   6517 O O     . MET B 1 260 ? 3.865   -42.573 20.119  1.00 28.65  ? 258 MET B O     1 
ATOM   6518 C CB    . MET B 1 260 ? 6.422   -44.512 19.935  1.00 31.78  ? 258 MET B CB    1 
ATOM   6519 C CG    . MET B 1 260 ? 5.310   -45.249 19.237  1.00 32.92  ? 258 MET B CG    1 
ATOM   6520 S SD    . MET B 1 260 ? 5.763   -46.984 19.238  1.00 37.15  ? 258 MET B SD    1 
ATOM   6521 C CE    . MET B 1 260 ? 5.051   -47.580 17.705  1.00 38.16  ? 258 MET B CE    1 
ATOM   6522 N N     . GLY B 1 261 ? 4.814   -43.009 22.170  1.00 28.77  ? 259 GLY B N     1 
ATOM   6523 C CA    . GLY B 1 261 ? 3.576   -42.922 22.955  1.00 27.55  ? 259 GLY B CA    1 
ATOM   6524 C C     . GLY B 1 261 ? 3.813   -42.585 24.423  1.00 31.37  ? 259 GLY B C     1 
ATOM   6525 O O     . GLY B 1 261 ? 4.907   -42.103 24.736  1.00 29.62  ? 259 GLY B O     1 
ATOM   6526 N N     . ILE B 1 262 ? 2.845   -42.876 25.295  1.00 27.55  ? 260 ILE B N     1 
ATOM   6527 C CA    . ILE B 1 262 ? 2.890   -42.449 26.729  1.00 30.46  ? 260 ILE B CA    1 
ATOM   6528 C C     . ILE B 1 262 ? 3.464   -41.024 26.823  1.00 32.05  ? 260 ILE B C     1 
ATOM   6529 O O     . ILE B 1 262 ? 4.316   -40.790 27.677  1.00 31.43  ? 260 ILE B O     1 
ATOM   6530 C CB    . ILE B 1 262 ? 3.546   -43.498 27.656  1.00 28.94  ? 260 ILE B CB    1 
ATOM   6531 C CG1   . ILE B 1 262 ? 5.006   -43.798 27.317  1.00 30.29  ? 260 ILE B CG1   1 
ATOM   6532 C CG2   . ILE B 1 262 ? 2.703   -44.764 27.696  1.00 26.88  ? 260 ILE B CG2   1 
ATOM   6533 C CD1   . ILE B 1 262 ? 5.761   -44.412 28.466  1.00 32.35  ? 260 ILE B CD1   1 
ATOM   6534 N N     . HIS B 1 263 ? 2.944   -40.107 26.004  1.00 29.31  ? 261 HIS B N     1 
ATOM   6535 C CA    . HIS B 1 263 ? 3.436   -38.706 25.965  1.00 33.17  ? 261 HIS B CA    1 
ATOM   6536 C C     . HIS B 1 263 ? 3.131   -37.963 27.271  1.00 33.03  ? 261 HIS B C     1 
ATOM   6537 O O     . HIS B 1 263 ? 3.949   -37.122 27.654  1.00 33.95  ? 261 HIS B O     1 
ATOM   6538 C CB    . HIS B 1 263 ? 2.830   -37.975 24.766  1.00 34.62  ? 261 HIS B CB    1 
ATOM   6539 C CG    . HIS B 1 263 ? 3.190   -38.533 23.432  1.00 34.07  ? 261 HIS B CG    1 
ATOM   6540 N ND1   . HIS B 1 263 ? 2.545   -38.139 22.282  1.00 29.12  ? 261 HIS B ND1   1 
ATOM   6541 C CD2   . HIS B 1 263 ? 4.122   -39.431 23.056  1.00 32.67  ? 261 HIS B CD2   1 
ATOM   6542 C CE1   . HIS B 1 263 ? 3.060   -38.774 21.255  1.00 32.16  ? 261 HIS B CE1   1 
ATOM   6543 N NE2   . HIS B 1 263 ? 4.023   -39.574 21.703  1.00 31.45  ? 261 HIS B NE2   1 
ATOM   6544 N N     . GLY B 1 264 ? 2.007   -38.267 27.914  1.00 31.64  ? 262 GLY B N     1 
ATOM   6545 C CA    . GLY B 1 264 ? 1.604   -37.602 29.169  1.00 36.33  ? 262 GLY B CA    1 
ATOM   6546 C C     . GLY B 1 264 ? 2.416   -38.022 30.384  1.00 34.83  ? 262 GLY B C     1 
ATOM   6547 O O     . GLY B 1 264 ? 2.157   -37.472 31.448  1.00 38.03  ? 262 GLY B O     1 
ATOM   6548 N N     . ASN B 1 265 ? 3.341   -38.970 30.237  1.00 32.96  ? 263 ASN B N     1 
ATOM   6549 C CA    . ASN B 1 265 ? 4.237   -39.352 31.357  1.00 34.31  ? 263 ASN B CA    1 
ATOM   6550 C C     . ASN B 1 265 ? 5.649   -38.843 31.064  1.00 38.34  ? 263 ASN B C     1 
ATOM   6551 O O     . ASN B 1 265 ? 6.290   -39.377 30.153  1.00 35.62  ? 263 ASN B O     1 
ATOM   6552 C CB    . ASN B 1 265 ? 4.206   -40.843 31.684  1.00 34.86  ? 263 ASN B CB    1 
ATOM   6553 C CG    . ASN B 1 265 ? 4.825   -41.135 33.033  1.00 35.88  ? 263 ASN B CG    1 
ATOM   6554 O OD1   . ASN B 1 265 ? 5.945   -41.625 33.113  1.00 31.93  ? 263 ASN B OD1   1 
ATOM   6555 N ND2   . ASN B 1 265 ? 4.114   -40.813 34.098  1.00 34.37  ? 263 ASN B ND2   1 
ATOM   6556 N N     . ALA B 1 266 ? 6.091   -37.834 31.813  1.00 35.40  ? 264 ALA B N     1 
ATOM   6557 C CA    . ALA B 1 266 ? 7.428   -37.240 31.614  1.00 34.94  ? 264 ALA B CA    1 
ATOM   6558 C C     . ALA B 1 266 ? 8.458   -38.354 31.808  1.00 34.17  ? 264 ALA B C     1 
ATOM   6559 O O     . ALA B 1 266 ? 8.399   -39.096 32.823  1.00 35.34  ? 264 ALA B O     1 
ATOM   6560 C CB    . ALA B 1 266 ? 7.637   -36.075 32.546  1.00 37.22  ? 264 ALA B CB    1 
ATOM   6561 N N     . THR B 1 267 ? 9.308   -38.528 30.805  1.00 34.82  ? 265 THR B N     1 
ATOM   6562 C CA    . THR B 1 267 ? 10.391  -39.534 30.770  1.00 31.45  ? 265 THR B CA    1 
ATOM   6563 C C     . THR B 1 267 ? 11.707  -38.762 30.831  1.00 33.44  ? 265 THR B C     1 
ATOM   6564 O O     . THR B 1 267 ? 12.091  -38.197 29.751  1.00 30.50  ? 265 THR B O     1 
ATOM   6565 C CB    . THR B 1 267 ? 10.253  -40.427 29.530  1.00 31.27  ? 265 THR B CB    1 
ATOM   6566 O OG1   . THR B 1 267 ? 8.914   -40.933 29.529  1.00 28.56  ? 265 THR B OG1   1 
ATOM   6567 C CG2   . THR B 1 267 ? 11.247  -41.567 29.536  1.00 30.22  ? 265 THR B CG2   1 
ATOM   6568 N N     . CYS B 1 268 ? 12.376  -38.741 32.006  1.00 30.62  ? 266 CYS B N     1 
ATOM   6569 C CA    . CYS B 1 268 ? 13.352  -37.664 32.344  1.00 33.64  ? 266 CYS B CA    1 
ATOM   6570 C C     . CYS B 1 268 ? 14.800  -38.138 32.421  1.00 35.34  ? 266 CYS B C     1 
ATOM   6571 O O     . CYS B 1 268 ? 15.063  -39.207 32.975  1.00 36.74  ? 266 CYS B O     1 
ATOM   6572 C CB    . CYS B 1 268 ? 13.015  -36.998 33.660  1.00 34.99  ? 266 CYS B CB    1 
ATOM   6573 S SG    . CYS B 1 268 ? 11.298  -36.443 33.733  1.00 41.62  ? 266 CYS B SG    1 
ATOM   6574 N N     . VAL B 1 269 ? 15.703  -37.325 31.867  1.00 39.46  ? 267 VAL B N     1 
ATOM   6575 C CA    . VAL B 1 269 ? 17.157  -37.364 32.178  1.00 38.59  ? 267 VAL B CA    1 
ATOM   6576 C C     . VAL B 1 269 ? 17.332  -36.629 33.525  1.00 40.54  ? 267 VAL B C     1 
ATOM   6577 O O     . VAL B 1 269 ? 17.086  -35.400 33.593  1.00 37.55  ? 267 VAL B O     1 
ATOM   6578 C CB    . VAL B 1 269 ? 17.984  -36.808 30.999  1.00 37.90  ? 267 VAL B CB    1 
ATOM   6579 C CG1   . VAL B 1 269 ? 19.479  -36.698 31.281  1.00 36.14  ? 267 VAL B CG1   1 
ATOM   6580 C CG2   . VAL B 1 269 ? 17.782  -37.677 29.760  1.00 38.46  ? 267 VAL B CG2   1 
ATOM   6581 N N     . MET B 1 270 ? 17.641  -37.393 34.576  1.00 39.51  ? 268 MET B N     1 
ATOM   6582 C CA    . MET B 1 270 ? 17.837  -36.907 35.966  1.00 39.63  ? 268 MET B CA    1 
ATOM   6583 C C     . MET B 1 270 ? 19.344  -36.855 36.295  1.00 36.85  ? 268 MET B C     1 
ATOM   6584 O O     . MET B 1 270 ? 20.027  -37.903 36.341  1.00 34.53  ? 268 MET B O     1 
ATOM   6585 C CB    . MET B 1 270 ? 17.077  -37.794 36.950  1.00 40.91  ? 268 MET B CB    1 
ATOM   6586 C CG    . MET B 1 270 ? 15.558  -37.842 36.704  1.00 39.49  ? 268 MET B CG    1 
ATOM   6587 S SD    . MET B 1 270 ? 14.721  -36.236 36.772  1.00 40.11  ? 268 MET B SD    1 
ATOM   6588 C CE    . MET B 1 270 ? 15.014  -35.728 38.468  1.00 43.24  ? 268 MET B CE    1 
ATOM   6589 N N     . ASN B 1 271 ? 19.847  -35.637 36.483  1.00 39.77  ? 269 ASN B N     1 
ATOM   6590 C CA    . ASN B 1 271 ? 21.244  -35.331 36.877  1.00 41.65  ? 269 ASN B CA    1 
ATOM   6591 C C     . ASN B 1 271 ? 21.320  -35.199 38.411  1.00 43.76  ? 269 ASN B C     1 
ATOM   6592 O O     . ASN B 1 271 ? 20.597  -34.383 38.976  1.00 44.69  ? 269 ASN B O     1 
ATOM   6593 C CB    . ASN B 1 271 ? 21.721  -34.080 36.149  1.00 40.15  ? 269 ASN B CB    1 
ATOM   6594 C CG    . ASN B 1 271 ? 21.608  -34.242 34.654  1.00 39.77  ? 269 ASN B CG    1 
ATOM   6595 O OD1   . ASN B 1 271 ? 22.297  -35.062 34.049  1.00 43.77  ? 269 ASN B OD1   1 
ATOM   6596 N ND2   . ASN B 1 271 ? 20.695  -33.506 34.060  1.00 42.49  ? 269 ASN B ND2   1 
ATOM   6597 N N     . PHE B 1 272 ? 22.138  -36.022 39.062  1.00 43.64  ? 270 PHE B N     1 
ATOM   6598 C CA    . PHE B 1 272 ? 22.423  -35.957 40.516  1.00 42.16  ? 270 PHE B CA    1 
ATOM   6599 C C     . PHE B 1 272 ? 23.810  -35.324 40.658  1.00 42.45  ? 270 PHE B C     1 
ATOM   6600 O O     . PHE B 1 272 ? 24.805  -35.954 40.225  1.00 39.91  ? 270 PHE B O     1 
ATOM   6601 C CB    . PHE B 1 272 ? 22.269  -37.347 41.145  1.00 42.03  ? 270 PHE B CB    1 
ATOM   6602 C CG    . PHE B 1 272 ? 20.882  -37.954 41.061  1.00 42.37  ? 270 PHE B CG    1 
ATOM   6603 C CD1   . PHE B 1 272 ? 19.939  -37.725 42.045  1.00 43.74  ? 270 PHE B CD1   1 
ATOM   6604 C CD2   . PHE B 1 272 ? 20.523  -38.777 40.007  1.00 45.61  ? 270 PHE B CD2   1 
ATOM   6605 C CE1   . PHE B 1 272 ? 18.676  -38.295 41.981  1.00 45.28  ? 270 PHE B CE1   1 
ATOM   6606 C CE2   . PHE B 1 272 ? 19.251  -39.324 39.928  1.00 48.71  ? 270 PHE B CE2   1 
ATOM   6607 C CZ    . PHE B 1 272 ? 18.329  -39.094 40.925  1.00 47.26  ? 270 PHE B CZ    1 
ATOM   6608 N N     . ASP B 1 273 ? 23.852  -34.072 41.135  1.00 47.05  ? 271 ASP B N     1 
ATOM   6609 C CA    . ASP B 1 273 ? 25.107  -33.310 41.348  1.00 52.22  ? 271 ASP B CA    1 
ATOM   6610 C C     . ASP B 1 273 ? 25.419  -33.299 42.846  1.00 48.69  ? 271 ASP B C     1 
ATOM   6611 O O     . ASP B 1 273 ? 25.062  -32.327 43.530  1.00 44.43  ? 271 ASP B O     1 
ATOM   6612 C CB    . ASP B 1 273 ? 25.006  -31.900 40.765  1.00 61.18  ? 271 ASP B CB    1 
ATOM   6613 C CG    . ASP B 1 273 ? 26.376  -31.338 40.411  1.00 75.25  ? 271 ASP B CG    1 
ATOM   6614 O OD1   . ASP B 1 273 ? 27.266  -32.152 40.057  1.00 87.64  ? 271 ASP B OD1   1 
ATOM   6615 O OD2   . ASP B 1 273 ? 26.554  -30.103 40.492  1.00 78.51  ? 271 ASP B OD2   1 
ATOM   6616 N N     . ALA B 1 274 ? 26.026  -34.365 43.360  1.00 50.20  ? 272 ALA B N     1 
ATOM   6617 C CA    . ALA B 1 274 ? 26.345  -34.484 44.806  1.00 52.57  ? 272 ALA B CA    1 
ATOM   6618 C C     . ALA B 1 274 ? 25.085  -34.128 45.606  1.00 52.64  ? 272 ALA B C     1 
ATOM   6619 O O     . ALA B 1 274 ? 25.151  -33.245 46.459  1.00 54.15  ? 272 ALA B O     1 
ATOM   6620 C CB    . ALA B 1 274 ? 27.506  -33.588 45.160  1.00 42.97  ? 272 ALA B CB    1 
ATOM   6621 N N     . ALA B 1 275 ? 23.960  -34.757 45.258  1.00 54.02  ? 273 ALA B N     1 
ATOM   6622 C CA    . ALA B 1 275 ? 22.650  -34.620 45.925  1.00 48.66  ? 273 ALA B CA    1 
ATOM   6623 C C     . ALA B 1 275 ? 22.681  -35.473 47.188  1.00 46.48  ? 273 ALA B C     1 
ATOM   6624 O O     . ALA B 1 275 ? 23.191  -36.603 47.127  1.00 41.09  ? 273 ALA B O     1 
ATOM   6625 C CB    . ALA B 1 275 ? 21.530  -35.051 45.005  1.00 47.81  ? 273 ALA B CB    1 
ATOM   6626 N N     . THR B 1 276 ? 22.111  -34.961 48.275  1.00 45.79  ? 274 THR B N     1 
ATOM   6627 C CA    . THR B 1 276 ? 22.018  -35.678 49.564  1.00 44.05  ? 274 THR B CA    1 
ATOM   6628 C C     . THR B 1 276 ? 21.079  -36.864 49.375  1.00 43.28  ? 274 THR B C     1 
ATOM   6629 O O     . THR B 1 276 ? 19.936  -36.657 48.947  1.00 46.14  ? 274 THR B O     1 
ATOM   6630 C CB    . THR B 1 276 ? 21.569  -34.768 50.719  1.00 45.37  ? 274 THR B CB    1 
ATOM   6631 O OG1   . THR B 1 276 ? 22.539  -33.721 50.834  1.00 45.01  ? 274 THR B OG1   1 
ATOM   6632 C CG2   . THR B 1 276 ? 21.429  -35.523 52.030  1.00 40.02  ? 274 THR B CG2   1 
ATOM   6633 N N     . GLY B 1 277 ? 21.569  -38.051 49.717  1.00 42.29  ? 275 GLY B N     1 
ATOM   6634 C CA    . GLY B 1 277 ? 20.799  -39.296 49.765  1.00 41.72  ? 275 GLY B CA    1 
ATOM   6635 C C     . GLY B 1 277 ? 21.157  -40.048 51.024  1.00 45.35  ? 275 GLY B C     1 
ATOM   6636 O O     . GLY B 1 277 ? 22.249  -39.788 51.571  1.00 48.30  ? 275 GLY B O     1 
ATOM   6637 N N     . PHE B 1 278 ? 20.294  -40.990 51.395  1.00 44.16  ? 276 PHE B N     1 
ATOM   6638 C CA    . PHE B 1 278 ? 20.352  -41.868 52.582  1.00 45.00  ? 276 PHE B CA    1 
ATOM   6639 C C     . PHE B 1 278 ? 20.290  -43.314 52.097  1.00 43.43  ? 276 PHE B C     1 
ATOM   6640 O O     . PHE B 1 278 ? 19.350  -43.648 51.396  1.00 41.31  ? 276 PHE B O     1 
ATOM   6641 C CB    . PHE B 1 278 ? 19.193  -41.491 53.518  1.00 40.08  ? 276 PHE B CB    1 
ATOM   6642 C CG    . PHE B 1 278 ? 19.048  -39.995 53.630  1.00 44.31  ? 276 PHE B CG    1 
ATOM   6643 C CD1   . PHE B 1 278 ? 19.901  -39.257 54.440  1.00 46.42  ? 276 PHE B CD1   1 
ATOM   6644 C CD2   . PHE B 1 278 ? 18.113  -39.313 52.868  1.00 42.56  ? 276 PHE B CD2   1 
ATOM   6645 C CE1   . PHE B 1 278 ? 19.786  -37.875 54.510  1.00 45.94  ? 276 PHE B CE1   1 
ATOM   6646 C CE2   . PHE B 1 278 ? 18.007  -37.933 52.938  1.00 41.79  ? 276 PHE B CE2   1 
ATOM   6647 C CZ    . PHE B 1 278 ? 18.849  -37.216 53.747  1.00 43.83  ? 276 PHE B CZ    1 
ATOM   6648 N N     . LEU B 1 279 ? 21.242  -44.157 52.493  1.00 46.47  ? 277 LEU B N     1 
ATOM   6649 C CA    . LEU B 1 279 ? 21.208  -45.612 52.188  1.00 45.06  ? 277 LEU B CA    1 
ATOM   6650 C C     . LEU B 1 279 ? 19.906  -46.220 52.704  1.00 42.84  ? 277 LEU B C     1 
ATOM   6651 O O     . LEU B 1 279 ? 19.571  -46.030 53.866  1.00 47.21  ? 277 LEU B O     1 
ATOM   6652 C CB    . LEU B 1 279 ? 22.409  -46.330 52.823  1.00 48.80  ? 277 LEU B CB    1 
ATOM   6653 C CG    . LEU B 1 279 ? 22.291  -47.855 52.796  1.00 55.40  ? 277 LEU B CG    1 
ATOM   6654 C CD1   . LEU B 1 279 ? 22.666  -48.389 51.418  1.00 56.05  ? 277 LEU B CD1   1 
ATOM   6655 C CD2   . LEU B 1 279 ? 23.111  -48.515 53.895  1.00 58.19  ? 277 LEU B CD2   1 
ATOM   6656 N N     . ILE B 1 280 ? 19.230  -47.032 51.909  1.00 46.53  ? 278 ILE B N     1 
ATOM   6657 C CA    . ILE B 1 280 ? 18.109  -47.846 52.456  1.00 44.99  ? 278 ILE B CA    1 
ATOM   6658 C C     . ILE B 1 280 ? 18.471  -49.303 52.215  1.00 45.47  ? 278 ILE B C     1 
ATOM   6659 O O     . ILE B 1 280 ? 18.892  -49.605 51.082  1.00 54.27  ? 278 ILE B O     1 
ATOM   6660 C CB    . ILE B 1 280 ? 16.750  -47.418 51.866  1.00 44.40  ? 278 ILE B CB    1 
ATOM   6661 C CG1   . ILE B 1 280 ? 15.689  -48.505 52.013  1.00 45.76  ? 278 ILE B CG1   1 
ATOM   6662 C CG2   . ILE B 1 280 ? 16.885  -46.972 50.424  1.00 43.71  ? 278 ILE B CG2   1 
ATOM   6663 C CD1   . ILE B 1 280 ? 14.286  -47.968 52.003  1.00 48.88  ? 278 ILE B CD1   1 
ATOM   6664 N N     . GLY B 1 281 ? 18.373  -50.132 53.266  1.00 47.23  ? 279 GLY B N     1 
ATOM   6665 C CA    . GLY B 1 281 ? 18.784  -51.553 53.288  1.00 44.95  ? 279 GLY B CA    1 
ATOM   6666 C C     . GLY B 1 281 ? 20.302  -51.722 53.364  1.00 44.72  ? 279 GLY B C     1 
ATOM   6667 O O     . GLY B 1 281 ? 21.060  -50.751 53.421  1.00 53.05  ? 279 GLY B O     1 
ATOM   6668 N N     . PRO B 1 282 ? 20.807  -52.973 53.367  1.00 47.25  ? 280 PRO B N     1 
ATOM   6669 C CA    . PRO B 1 282 ? 22.234  -53.225 53.586  1.00 48.38  ? 280 PRO B CA    1 
ATOM   6670 C C     . PRO B 1 282 ? 23.139  -52.719 52.464  1.00 51.40  ? 280 PRO B C     1 
ATOM   6671 O O     . PRO B 1 282 ? 22.781  -52.768 51.297  1.00 49.10  ? 280 PRO B O     1 
ATOM   6672 C CB    . PRO B 1 282 ? 22.318  -54.755 53.684  1.00 49.80  ? 280 PRO B CB    1 
ATOM   6673 C CG    . PRO B 1 282 ? 20.889  -55.201 53.980  1.00 48.53  ? 280 PRO B CG    1 
ATOM   6674 C CD    . PRO B 1 282 ? 20.027  -54.212 53.224  1.00 50.78  ? 280 PRO B CD    1 
ATOM   6675 N N     . PRO B 1 283 ? 24.353  -52.218 52.780  1.00 58.58  ? 281 PRO B N     1 
ATOM   6676 C CA    . PRO B 1 283 ? 25.327  -51.868 51.753  1.00 54.38  ? 281 PRO B CA    1 
ATOM   6677 C C     . PRO B 1 283 ? 25.475  -53.016 50.743  1.00 55.84  ? 281 PRO B C     1 
ATOM   6678 O O     . PRO B 1 283 ? 25.451  -54.149 51.155  1.00 56.64  ? 281 PRO B O     1 
ATOM   6679 C CB    . PRO B 1 283 ? 26.620  -51.657 52.549  1.00 52.57  ? 281 PRO B CB    1 
ATOM   6680 C CG    . PRO B 1 283 ? 26.157  -51.218 53.914  1.00 52.34  ? 281 PRO B CG    1 
ATOM   6681 C CD    . PRO B 1 283 ? 24.869  -51.982 54.137  1.00 56.32  ? 281 PRO B CD    1 
ATOM   6682 N N     . ASN B 1 284 ? 25.548  -52.692 49.451  1.00 50.49  ? 282 ASN B N     1 
ATOM   6683 C CA    . ASN B 1 284 ? 25.776  -53.661 48.342  1.00 50.77  ? 282 ASN B CA    1 
ATOM   6684 C C     . ASN B 1 284 ? 24.676  -54.731 48.256  1.00 46.69  ? 282 ASN B C     1 
ATOM   6685 O O     . ASN B 1 284 ? 24.940  -55.756 47.620  1.00 50.10  ? 282 ASN B O     1 
ATOM   6686 C CB    . ASN B 1 284 ? 27.169  -54.280 48.454  1.00 46.62  ? 282 ASN B CB    1 
ATOM   6687 C CG    . ASN B 1 284 ? 28.187  -53.208 48.771  1.00 50.16  ? 282 ASN B CG    1 
ATOM   6688 O OD1   . ASN B 1 284 ? 28.184  -52.116 48.192  1.00 55.14  ? 282 ASN B OD1   1 
ATOM   6689 N ND2   . ASN B 1 284 ? 29.036  -53.486 49.731  1.00 48.86  ? 282 ASN B ND2   1 
ATOM   6690 N N     . LYS B 1 285 ? 23.477  -54.493 48.797  1.00 47.96  ? 283 LYS B N     1 
ATOM   6691 C CA    . LYS B 1 285 ? 22.324  -55.427 48.692  1.00 53.60  ? 283 LYS B CA    1 
ATOM   6692 C C     . LYS B 1 285 ? 21.150  -54.694 48.027  1.00 50.35  ? 283 LYS B C     1 
ATOM   6693 O O     . LYS B 1 285 ? 19.991  -55.152 48.166  1.00 45.77  ? 283 LYS B O     1 
ATOM   6694 C CB    . LYS B 1 285 ? 21.992  -55.988 50.081  1.00 69.83  ? 283 LYS B CB    1 
ATOM   6695 C CG    . LYS B 1 285 ? 22.591  -57.359 50.382  1.00 75.85  ? 283 LYS B CG    1 
ATOM   6696 C CD    . LYS B 1 285 ? 21.899  -58.509 49.647  1.00 84.61  ? 283 LYS B CD    1 
ATOM   6697 C CE    . LYS B 1 285 ? 22.439  -59.880 50.016  1.00 90.48  ? 283 LYS B CE    1 
ATOM   6698 N NZ    . LYS B 1 285 ? 23.886  -60.006 49.711  1.00 89.50  ? 283 LYS B NZ    1 
ATOM   6699 N N     . GLY B 1 286 ? 21.469  -53.616 47.308  1.00 47.30  ? 284 GLY B N     1 
ATOM   6700 C CA    . GLY B 1 286 ? 20.526  -52.744 46.586  1.00 51.94  ? 284 GLY B CA    1 
ATOM   6701 C C     . GLY B 1 286 ? 19.723  -53.513 45.551  1.00 49.30  ? 284 GLY B C     1 
ATOM   6702 O O     . GLY B 1 286 ? 18.477  -53.389 45.546  1.00 40.11  ? 284 GLY B O     1 
ATOM   6703 N N     . LEU B 1 287 ? 20.373  -54.325 44.719  1.00 54.65  ? 285 LEU B N     1 
ATOM   6704 C CA    . LEU B 1 287 ? 19.586  -55.121 43.756  1.00 56.49  ? 285 LEU B CA    1 
ATOM   6705 C C     . LEU B 1 287 ? 18.583  -55.945 44.569  1.00 56.90  ? 285 LEU B C     1 
ATOM   6706 O O     . LEU B 1 287 ? 17.369  -55.838 44.267  1.00 66.75  ? 285 LEU B O     1 
ATOM   6707 C CB    . LEU B 1 287 ? 20.450  -55.986 42.841  1.00 58.24  ? 285 LEU B CB    1 
ATOM   6708 C CG    . LEU B 1 287 ? 19.623  -56.726 41.793  1.00 62.47  ? 285 LEU B CG    1 
ATOM   6709 C CD1   . LEU B 1 287 ? 18.828  -55.733 40.961  1.00 64.16  ? 285 LEU B CD1   1 
ATOM   6710 C CD2   . LEU B 1 287 ? 20.485  -57.610 40.910  1.00 65.85  ? 285 LEU B CD2   1 
ATOM   6711 N N     . ASN B 1 288 ? 19.021  -56.682 45.590  1.00 55.83  ? 286 ASN B N     1 
ATOM   6712 C CA    . ASN B 1 288 ? 18.060  -57.514 46.367  1.00 62.00  ? 286 ASN B CA    1 
ATOM   6713 C C     . ASN B 1 288 ? 16.866  -56.654 46.832  1.00 62.03  ? 286 ASN B C     1 
ATOM   6714 O O     . ASN B 1 288 ? 15.712  -57.060 46.560  1.00 65.86  ? 286 ASN B O     1 
ATOM   6715 C CB    . ASN B 1 288 ? 18.698  -58.268 47.529  1.00 63.03  ? 286 ASN B CB    1 
ATOM   6716 C CG    . ASN B 1 288 ? 17.668  -59.192 48.139  1.00 73.86  ? 286 ASN B CG    1 
ATOM   6717 O OD1   . ASN B 1 288 ? 16.716  -58.733 48.762  1.00 73.28  ? 286 ASN B OD1   1 
ATOM   6718 N ND2   . ASN B 1 288 ? 17.795  -60.487 47.904  1.00 79.02  ? 286 ASN B ND2   1 
ATOM   6719 N N     . CYS B 1 289 ? 17.110  -55.476 47.426  1.00 55.27  ? 287 CYS B N     1 
ATOM   6720 C CA    . CYS B 1 289 ? 16.049  -54.568 47.957  1.00 62.70  ? 287 CYS B CA    1 
ATOM   6721 C C     . CYS B 1 289 ? 15.179  -53.966 46.837  1.00 68.01  ? 287 CYS B C     1 
ATOM   6722 O O     . CYS B 1 289 ? 13.955  -53.787 47.082  1.00 66.28  ? 287 CYS B O     1 
ATOM   6723 C CB    . CYS B 1 289 ? 16.628  -53.416 48.772  1.00 59.08  ? 287 CYS B CB    1 
ATOM   6724 S SG    . CYS B 1 289 ? 17.654  -53.931 50.172  1.00 57.16  ? 287 CYS B SG    1 
ATOM   6725 N N     . MET B 1 290 ? 15.775  -53.605 45.684  1.00 72.54  ? 288 MET B N     1 
ATOM   6726 C CA    . MET B 1 290 ? 15.065  -52.951 44.539  1.00 65.56  ? 288 MET B CA    1 
ATOM   6727 C C     . MET B 1 290 ? 14.002  -53.924 44.009  1.00 67.98  ? 288 MET B C     1 
ATOM   6728 O O     . MET B 1 290 ? 12.982  -53.416 43.510  1.00 63.71  ? 288 MET B O     1 
ATOM   6729 C CB    . MET B 1 290 ? 16.016  -52.499 43.411  1.00 60.94  ? 288 MET B CB    1 
ATOM   6730 C CG    . MET B 1 290 ? 15.381  -51.661 42.268  1.00 60.07  ? 288 MET B CG    1 
ATOM   6731 S SD    . MET B 1 290 ? 14.144  -50.327 42.694  1.00 60.89  ? 288 MET B SD    1 
ATOM   6732 C CE    . MET B 1 290 ? 15.079  -48.824 42.413  1.00 59.02  ? 288 MET B CE    1 
ATOM   6733 N N     . PHE B 1 291 ? 14.165  -55.242 44.214  1.00 69.24  ? 289 PHE B N     1 
ATOM   6734 C CA    . PHE B 1 291 ? 13.273  -56.288 43.637  1.00 78.55  ? 289 PHE B CA    1 
ATOM   6735 C C     . PHE B 1 291 ? 11.901  -56.359 44.349  1.00 80.00  ? 289 PHE B C     1 
ATOM   6736 O O     . PHE B 1 291 ? 10.998  -57.092 43.857  1.00 86.30  ? 289 PHE B O     1 
ATOM   6737 C CB    . PHE B 1 291 ? 14.011  -57.628 43.521  1.00 81.92  ? 289 PHE B CB    1 
ATOM   6738 C CG    . PHE B 1 291 ? 14.380  -57.963 42.090  1.00 89.89  ? 289 PHE B CG    1 
ATOM   6739 C CD1   . PHE B 1 291 ? 13.395  -58.343 41.175  1.00 82.33  ? 289 PHE B CD1   1 
ATOM   6740 C CD2   . PHE B 1 291 ? 15.695  -57.861 41.643  1.00 83.93  ? 289 PHE B CD2   1 
ATOM   6741 C CE1   . PHE B 1 291 ? 13.720  -58.632 39.857  1.00 80.40  ? 289 PHE B CE1   1 
ATOM   6742 C CE2   . PHE B 1 291 ? 16.018  -58.156 40.324  1.00 85.92  ? 289 PHE B CE2   1 
ATOM   6743 C CZ    . PHE B 1 291 ? 15.031  -58.537 39.435  1.00 86.08  ? 289 PHE B CZ    1 
ATOM   6744 N N     . THR B 1 292 ? 11.695  -55.599 45.428  1.00 73.77  ? 290 THR B N     1 
ATOM   6745 C CA    . THR B 1 292 ? 10.340  -55.278 45.963  1.00 68.01  ? 290 THR B CA    1 
ATOM   6746 C C     . THR B 1 292 ? 9.662   -54.281 45.014  1.00 56.56  ? 290 THR B C     1 
ATOM   6747 O O     . THR B 1 292 ? 8.537   -54.592 44.594  1.00 52.21  ? 290 THR B O     1 
ATOM   6748 C CB    . THR B 1 292 ? 10.388  -54.731 47.398  1.00 67.95  ? 290 THR B CB    1 
ATOM   6749 O OG1   . THR B 1 292 ? 11.035  -55.714 48.211  1.00 71.08  ? 290 THR B OG1   1 
ATOM   6750 C CG2   . THR B 1 292 ? 9.012   -54.422 47.948  1.00 61.11  ? 290 THR B CG2   1 
ATOM   6751 N N     . PHE B 1 293 ? 10.327  -53.151 44.703  1.00 52.83  ? 291 PHE B N     1 
ATOM   6752 C CA    . PHE B 1 293 ? 9.879   -52.114 43.723  1.00 60.92  ? 291 PHE B CA    1 
ATOM   6753 C C     . PHE B 1 293 ? 9.590   -52.748 42.345  1.00 73.22  ? 291 PHE B C     1 
ATOM   6754 O O     . PHE B 1 293 ? 8.608   -52.307 41.688  1.00 75.56  ? 291 PHE B O     1 
ATOM   6755 C CB    . PHE B 1 293 ? 10.912  -50.990 43.531  1.00 63.83  ? 291 PHE B CB    1 
ATOM   6756 C CG    . PHE B 1 293 ? 10.396  -49.575 43.312  1.00 65.93  ? 291 PHE B CG    1 
ATOM   6757 C CD1   . PHE B 1 293 ? 9.151   -49.316 42.739  1.00 72.58  ? 291 PHE B CD1   1 
ATOM   6758 C CD2   . PHE B 1 293 ? 11.190  -48.481 43.652  1.00 65.58  ? 291 PHE B CD2   1 
ATOM   6759 C CE1   . PHE B 1 293 ? 8.703   -48.012 42.549  1.00 76.81  ? 291 PHE B CE1   1 
ATOM   6760 C CE2   . PHE B 1 293 ? 10.733  -47.182 43.479  1.00 75.40  ? 291 PHE B CE2   1 
ATOM   6761 C CZ    . PHE B 1 293 ? 9.492   -46.944 42.924  1.00 77.29  ? 291 PHE B CZ    1 
ATOM   6762 N N     . MET B 1 294 ? 10.400  -53.730 41.909  1.00 79.84  ? 292 MET B N     1 
ATOM   6763 C CA    . MET B 1 294 ? 10.326  -54.356 40.551  1.00 81.41  ? 292 MET B CA    1 
ATOM   6764 C C     . MET B 1 294 ? 9.153   -55.377 40.443  1.00 86.00  ? 292 MET B C     1 
ATOM   6765 O O     . MET B 1 294 ? 8.402   -55.219 39.457  1.00 92.46  ? 292 MET B O     1 
ATOM   6766 C CB    . MET B 1 294 ? 11.684  -54.951 40.126  1.00 76.36  ? 292 MET B CB    1 
ATOM   6767 C CG    . MET B 1 294 ? 12.730  -53.878 39.696  1.00 73.73  ? 292 MET B CG    1 
ATOM   6768 S SD    . MET B 1 294 ? 14.521  -54.319 39.921  1.00 66.17  ? 292 MET B SD    1 
ATOM   6769 C CE    . MET B 1 294 ? 14.818  -55.322 38.462  1.00 62.47  ? 292 MET B CE    1 
ATOM   6770 N N     . ASN B 1 295 ? 8.906   -56.317 41.390  1.00 81.90  ? 293 ASN B N     1 
ATOM   6771 C CA    . ASN B 1 295 ? 7.852   -57.385 41.253  1.00 79.66  ? 293 ASN B CA    1 
ATOM   6772 C C     . ASN B 1 295 ? 6.427   -56.834 41.487  1.00 71.53  ? 293 ASN B C     1 
ATOM   6773 O O     . ASN B 1 295 ? 5.436   -57.514 41.107  1.00 68.91  ? 293 ASN B O     1 
ATOM   6774 C CB    . ASN B 1 295 ? 8.085   -58.585 42.174  1.00 72.84  ? 293 ASN B CB    1 
ATOM   6775 C CG    . ASN B 1 295 ? 9.524   -59.036 42.178  1.00 79.88  ? 293 ASN B CG    1 
ATOM   6776 O OD1   . ASN B 1 295 ? 10.259  -58.812 41.221  1.00 74.76  ? 293 ASN B OD1   1 
ATOM   6777 N ND2   . ASN B 1 295 ? 9.945   -59.645 43.271  1.00 93.56  ? 293 ASN B ND2   1 
ATOM   6778 N N     . THR B 1 296 ? 6.309   -55.692 42.163  1.00 58.68  ? 294 THR B N     1 
ATOM   6779 C CA    . THR B 1 296 ? 5.077   -54.869 42.181  1.00 65.77  ? 294 THR B CA    1 
ATOM   6780 C C     . THR B 1 296 ? 4.784   -54.556 40.713  1.00 64.50  ? 294 THR B C     1 
ATOM   6781 O O     . THR B 1 296 ? 3.801   -55.114 40.179  1.00 65.29  ? 294 THR B O     1 
ATOM   6782 C CB    . THR B 1 296 ? 5.220   -53.567 43.002  1.00 63.63  ? 294 THR B CB    1 
ATOM   6783 O OG1   . THR B 1 296 ? 5.559   -53.827 44.364  1.00 73.98  ? 294 THR B OG1   1 
ATOM   6784 C CG2   . THR B 1 296 ? 3.968   -52.715 43.003  1.00 56.01  ? 294 THR B CG2   1 
ATOM   6785 N N     . ALA B 1 297 ? 5.694   -53.782 40.096  1.00 67.91  ? 295 ALA B N     1 
ATOM   6786 C CA    . ALA B 1 297 ? 5.579   -53.146 38.759  1.00 74.79  ? 295 ALA B CA    1 
ATOM   6787 C C     . ALA B 1 297 ? 5.607   -54.210 37.651  1.00 69.49  ? 295 ALA B C     1 
ATOM   6788 O O     . ALA B 1 297 ? 5.212   -53.833 36.521  1.00 72.64  ? 295 ALA B O     1 
ATOM   6789 C CB    . ALA B 1 297 ? 6.663   -52.100 38.549  1.00 68.31  ? 295 ALA B CB    1 
ATOM   6790 N N     . ARG B 1 298 ? 6.048   -55.450 37.942  1.00 58.92  ? 296 ARG B N     1 
ATOM   6791 C CA    . ARG B 1 298 ? 6.006   -56.582 36.970  1.00 65.94  ? 296 ARG B CA    1 
ATOM   6792 C C     . ARG B 1 298 ? 4.530   -56.927 36.799  1.00 57.37  ? 296 ARG B C     1 
ATOM   6793 O O     . ARG B 1 298 ? 4.065   -56.953 35.646  1.00 38.27  ? 296 ARG B O     1 
ATOM   6794 C CB    . ARG B 1 298 ? 6.758   -57.861 37.385  1.00 69.67  ? 296 ARG B CB    1 
ATOM   6795 C CG    . ARG B 1 298 ? 8.283   -57.766 37.483  1.00 78.32  ? 296 ARG B CG    1 
ATOM   6796 C CD    . ARG B 1 298 ? 9.024   -57.054 36.352  1.00 76.96  ? 296 ARG B CD    1 
ATOM   6797 N NE    . ARG B 1 298 ? 10.505  -56.953 36.361  1.00 70.96  ? 296 ARG B NE    1 
ATOM   6798 C CZ    . ARG B 1 298 ? 11.369  -57.977 36.272  1.00 61.55  ? 296 ARG B CZ    1 
ATOM   6799 N NH1   . ARG B 1 298 ? 12.670  -57.755 36.202  1.00 58.65  ? 296 ARG B NH1   1 
ATOM   6800 N NH2   . ARG B 1 298 ? 10.941  -59.225 36.261  1.00 71.17  ? 296 ARG B NH2   1 
ATOM   6801 N N     . LEU B 1 299 ? 3.833   -57.127 37.924  1.00 50.21  ? 297 LEU B N     1 
ATOM   6802 C CA    . LEU B 1 299 ? 2.377   -57.385 37.927  1.00 45.98  ? 297 LEU B CA    1 
ATOM   6803 C C     . LEU B 1 299 ? 1.636   -56.091 37.532  1.00 42.89  ? 297 LEU B C     1 
ATOM   6804 O O     . LEU B 1 299 ? 0.616   -56.177 36.817  1.00 42.53  ? 297 LEU B O     1 
ATOM   6805 C CB    . LEU B 1 299 ? 1.994   -57.916 39.305  1.00 47.92  ? 297 LEU B CB    1 
ATOM   6806 C CG    . LEU B 1 299 ? 0.759   -58.814 39.324  1.00 52.07  ? 297 LEU B CG    1 
ATOM   6807 C CD1   . LEU B 1 299 ? 0.949   -60.008 38.405  1.00 52.07  ? 297 LEU B CD1   1 
ATOM   6808 C CD2   . LEU B 1 299 ? 0.444   -59.286 40.742  1.00 53.71  ? 297 LEU B CD2   1 
ATOM   6809 N N     . GLY B 1 300 ? 2.158   -54.925 37.924  1.00 40.57  ? 298 GLY B N     1 
ATOM   6810 C CA    . GLY B 1 300 ? 1.629   -53.603 37.541  1.00 38.51  ? 298 GLY B CA    1 
ATOM   6811 C C     . GLY B 1 300 ? 1.724   -53.379 36.033  1.00 44.16  ? 298 GLY B C     1 
ATOM   6812 O O     . GLY B 1 300 ? 0.818   -52.734 35.475  1.00 44.40  ? 298 GLY B O     1 
ATOM   6813 N N     . THR B 1 301 ? 2.743   -53.945 35.367  1.00 43.65  ? 299 THR B N     1 
ATOM   6814 C CA    . THR B 1 301 ? 2.930   -53.829 33.894  1.00 39.79  ? 299 THR B CA    1 
ATOM   6815 C C     . THR B 1 301 ? 2.107   -54.916 33.200  1.00 33.13  ? 299 THR B C     1 
ATOM   6816 O O     . THR B 1 301 ? 1.574   -54.644 32.125  1.00 34.27  ? 299 THR B O     1 
ATOM   6817 C CB    . THR B 1 301 ? 4.421   -53.790 33.514  1.00 43.59  ? 299 THR B CB    1 
ATOM   6818 O OG1   . THR B 1 301 ? 5.040   -52.636 34.093  1.00 45.36  ? 299 THR B OG1   1 
ATOM   6819 C CG2   . THR B 1 301 ? 4.618   -53.664 32.025  1.00 48.94  ? 299 THR B CG2   1 
ATOM   6820 N N     . ALA B 1 302 ? 1.989   -56.108 33.767  1.00 29.64  ? 300 ALA B N     1 
ATOM   6821 C CA    . ALA B 1 302 ? 1.039   -57.132 33.269  1.00 35.43  ? 300 ALA B CA    1 
ATOM   6822 C C     . ALA B 1 302 ? -0.366  -56.507 33.164  1.00 34.63  ? 300 ALA B C     1 
ATOM   6823 O O     . ALA B 1 302 ? -1.125  -56.866 32.253  1.00 36.47  ? 300 ALA B O     1 
ATOM   6824 C CB    . ALA B 1 302 ? 1.048   -58.347 34.166  1.00 36.41  ? 300 ALA B CB    1 
ATOM   6825 N N     . LEU B 1 303 ? -0.675  -55.593 34.078  1.00 34.47  ? 301 LEU B N     1 
ATOM   6826 C CA    . LEU B 1 303 ? -1.929  -54.810 34.137  1.00 36.70  ? 301 LEU B CA    1 
ATOM   6827 C C     . LEU B 1 303 ? -2.016  -53.901 32.909  1.00 34.90  ? 301 LEU B C     1 
ATOM   6828 O O     . LEU B 1 303 ? -3.161  -53.680 32.428  1.00 30.95  ? 301 LEU B O     1 
ATOM   6829 C CB    . LEU B 1 303 ? -1.927  -53.988 35.423  1.00 40.75  ? 301 LEU B CB    1 
ATOM   6830 C CG    . LEU B 1 303 ? -3.288  -53.730 36.048  1.00 46.69  ? 301 LEU B CG    1 
ATOM   6831 C CD1   . LEU B 1 303 ? -4.057  -55.027 36.169  1.00 49.22  ? 301 LEU B CD1   1 
ATOM   6832 C CD2   . LEU B 1 303 ? -3.146  -53.088 37.419  1.00 44.44  ? 301 LEU B CD2   1 
ATOM   6833 N N     . GLN B 1 304 ? -0.880  -53.382 32.426  1.00 31.19  ? 302 GLN B N     1 
ATOM   6834 C CA    . GLN B 1 304 ? -0.866  -52.511 31.222  1.00 34.09  ? 302 GLN B CA    1 
ATOM   6835 C C     . GLN B 1 304 ? -1.347  -53.345 30.031  1.00 33.44  ? 302 GLN B C     1 
ATOM   6836 O O     . GLN B 1 304 ? -2.236  -52.869 29.289  1.00 32.61  ? 302 GLN B O     1 
ATOM   6837 C CB    . GLN B 1 304 ? 0.497   -51.898 30.940  1.00 34.85  ? 302 GLN B CB    1 
ATOM   6838 C CG    . GLN B 1 304 ? 0.420   -50.836 29.862  1.00 35.13  ? 302 GLN B CG    1 
ATOM   6839 C CD    . GLN B 1 304 ? 1.741   -50.147 29.636  1.00 36.98  ? 302 GLN B CD    1 
ATOM   6840 O OE1   . GLN B 1 304 ? 2.723   -50.356 30.355  1.00 30.92  ? 302 GLN B OE1   1 
ATOM   6841 N NE2   . GLN B 1 304 ? 1.774   -49.328 28.598  1.00 38.03  ? 302 GLN B NE2   1 
ATOM   6842 N N     . GLY B 1 305 ? -0.813  -54.562 29.915  1.00 32.27  ? 303 GLY B N     1 
ATOM   6843 C CA    . GLY B 1 305 ? -1.157  -55.526 28.863  1.00 32.30  ? 303 GLY B CA    1 
ATOM   6844 C C     . GLY B 1 305 ? -2.635  -55.808 28.882  1.00 31.25  ? 303 GLY B C     1 
ATOM   6845 O O     . GLY B 1 305 ? -3.250  -55.886 27.793  1.00 27.91  ? 303 GLY B O     1 
ATOM   6846 N N     . LEU B 1 306 ? -3.199  -55.946 30.076  1.00 30.32  ? 304 LEU B N     1 
ATOM   6847 C CA    . LEU B 1 306 ? -4.649  -56.193 30.198  1.00 33.15  ? 304 LEU B CA    1 
ATOM   6848 C C     . LEU B 1 306 ? -5.370  -54.941 29.702  1.00 32.30  ? 304 LEU B C     1 
ATOM   6849 O O     . LEU B 1 306 ? -6.345  -55.101 28.986  1.00 37.71  ? 304 LEU B O     1 
ATOM   6850 C CB    . LEU B 1 306 ? -5.052  -56.519 31.641  1.00 34.17  ? 304 LEU B CB    1 
ATOM   6851 C CG    . LEU B 1 306 ? -6.569  -56.590 31.867  1.00 32.58  ? 304 LEU B CG    1 
ATOM   6852 C CD1   . LEU B 1 306 ? -7.229  -57.709 31.059  1.00 31.24  ? 304 LEU B CD1   1 
ATOM   6853 C CD2   . LEU B 1 306 ? -6.872  -56.769 33.341  1.00 33.64  ? 304 LEU B CD2   1 
ATOM   6854 N N     . ALA B 1 307 ? -4.909  -53.751 30.077  1.00 29.08  ? 305 ALA B N     1 
ATOM   6855 C CA    . ALA B 1 307 ? -5.604  -52.481 29.754  1.00 32.40  ? 305 ALA B CA    1 
ATOM   6856 C C     . ALA B 1 307 ? -5.664  -52.283 28.223  1.00 32.03  ? 305 ALA B C     1 
ATOM   6857 O O     . ALA B 1 307 ? -6.699  -51.808 27.734  1.00 29.95  ? 305 ALA B O     1 
ATOM   6858 C CB    . ALA B 1 307 ? -4.937  -51.306 30.449  1.00 32.34  ? 305 ALA B CB    1 
ATOM   6859 N N     . HIS B 1 308 ? -4.605  -52.623 27.486  1.00 29.31  ? 306 HIS B N     1 
ATOM   6860 C CA    . HIS B 1 308 ? -4.544  -52.384 26.014  1.00 31.52  ? 306 HIS B CA    1 
ATOM   6861 C C     . HIS B 1 308 ? -5.509  -53.333 25.288  1.00 31.08  ? 306 HIS B C     1 
ATOM   6862 O O     . HIS B 1 308 ? -6.140  -52.886 24.311  1.00 32.71  ? 306 HIS B O     1 
ATOM   6863 C CB    . HIS B 1 308 ? -3.100  -52.410 25.506  1.00 27.62  ? 306 HIS B CB    1 
ATOM   6864 C CG    . HIS B 1 308 ? -2.297  -51.285 26.059  1.00 26.87  ? 306 HIS B CG    1 
ATOM   6865 N ND1   . HIS B 1 308 ? -2.677  -49.980 25.874  1.00 25.68  ? 306 HIS B ND1   1 
ATOM   6866 C CD2   . HIS B 1 308 ? -1.140  -51.260 26.774  1.00 27.21  ? 306 HIS B CD2   1 
ATOM   6867 C CE1   . HIS B 1 308 ? -1.776  -49.176 26.454  1.00 30.10  ? 306 HIS B CE1   1 
ATOM   6868 N NE2   . HIS B 1 308 ? -0.814  -49.936 27.027  1.00 27.56  ? 306 HIS B NE2   1 
ATOM   6869 N N     . ALA B 1 309 ? -5.688  -54.562 25.776  1.00 30.45  ? 307 ALA B N     1 
ATOM   6870 C CA    . ALA B 1 309 ? -6.660  -55.516 25.196  1.00 29.39  ? 307 ALA B CA    1 
ATOM   6871 C C     . ALA B 1 309 ? -8.076  -55.003 25.464  1.00 30.05  ? 307 ALA B C     1 
ATOM   6872 O O     . ALA B 1 309 ? -8.867  -54.976 24.504  1.00 30.33  ? 307 ALA B O     1 
ATOM   6873 C CB    . ALA B 1 309 ? -6.429  -56.929 25.690  1.00 30.02  ? 307 ALA B CB    1 
ATOM   6874 N N     . GLU B 1 310 ? -8.348  -54.539 26.691  1.00 32.02  ? 308 GLU B N     1 
ATOM   6875 C CA    . GLU B 1 310 ? -9.670  -54.008 27.134  1.00 32.50  ? 308 GLU B CA    1 
ATOM   6876 C C     . GLU B 1 310 ? -10.038 -52.749 26.344  1.00 31.18  ? 308 GLU B C     1 
ATOM   6877 O O     . GLU B 1 310 ? -11.157 -52.670 25.885  1.00 30.88  ? 308 GLU B O     1 
ATOM   6878 C CB    . GLU B 1 310 ? -9.682  -53.694 28.636  1.00 32.35  ? 308 GLU B CB    1 
ATOM   6879 C CG    . GLU B 1 310 ? -11.011 -53.157 29.149  1.00 31.22  ? 308 GLU B CG    1 
ATOM   6880 C CD    . GLU B 1 310 ? -12.213 -54.082 29.009  1.00 34.48  ? 308 GLU B CD    1 
ATOM   6881 O OE1   . GLU B 1 310 ? -13.325 -53.546 28.821  1.00 35.36  ? 308 GLU B OE1   1 
ATOM   6882 O OE2   . GLU B 1 310 ? -12.053 -55.336 29.124  1.00 30.85  ? 308 GLU B OE2   1 
ATOM   6883 N N     . VAL B 1 311 ? -9.139  -51.785 26.213  1.00 31.13  ? 309 VAL B N     1 
ATOM   6884 C CA    . VAL B 1 311 ? -9.447  -50.561 25.426  1.00 34.14  ? 309 VAL B CA    1 
ATOM   6885 C C     . VAL B 1 311 ? -9.678  -50.963 23.960  1.00 32.96  ? 309 VAL B C     1 
ATOM   6886 O O     . VAL B 1 311 ? -10.597 -50.448 23.352  1.00 36.55  ? 309 VAL B O     1 
ATOM   6887 C CB    . VAL B 1 311 ? -8.368  -49.471 25.576  1.00 31.76  ? 309 VAL B CB    1 
ATOM   6888 C CG1   . VAL B 1 311 ? -8.567  -48.317 24.586  1.00 29.61  ? 309 VAL B CG1   1 
ATOM   6889 C CG2   . VAL B 1 311 ? -8.347  -48.956 26.995  1.00 31.73  ? 309 VAL B CG2   1 
ATOM   6890 N N     . GLY B 1 312 ? -8.854  -51.839 23.414  1.00 31.79  ? 310 GLY B N     1 
ATOM   6891 C CA    . GLY B 1 312 ? -9.005  -52.314 22.027  1.00 30.75  ? 310 GLY B CA    1 
ATOM   6892 C C     . GLY B 1 312 ? -10.348 -52.982 21.808  1.00 31.17  ? 310 GLY B C     1 
ATOM   6893 O O     . GLY B 1 312 ? -10.940 -52.766 20.720  1.00 29.74  ? 310 GLY B O     1 
ATOM   6894 N N     . PHE B 1 313 ? -10.836 -53.748 22.795  1.00 30.95  ? 311 PHE B N     1 
ATOM   6895 C CA    . PHE B 1 313 ? -12.149 -54.430 22.704  1.00 32.83  ? 311 PHE B CA    1 
ATOM   6896 C C     . PHE B 1 313 ? -13.310 -53.417 22.815  1.00 34.25  ? 311 PHE B C     1 
ATOM   6897 O O     . PHE B 1 313 ? -14.277 -53.488 22.041  1.00 32.34  ? 311 PHE B O     1 
ATOM   6898 C CB    . PHE B 1 313 ? -12.249 -55.535 23.742  1.00 30.73  ? 311 PHE B CB    1 
ATOM   6899 C CG    . PHE B 1 313 ? -13.592 -56.196 23.720  1.00 31.13  ? 311 PHE B CG    1 
ATOM   6900 C CD1   . PHE B 1 313 ? -13.896 -57.108 22.734  1.00 31.05  ? 311 PHE B CD1   1 
ATOM   6901 C CD2   . PHE B 1 313 ? -14.558 -55.875 24.655  1.00 28.79  ? 311 PHE B CD2   1 
ATOM   6902 C CE1   . PHE B 1 313 ? -15.130 -57.737 22.716  1.00 30.99  ? 311 PHE B CE1   1 
ATOM   6903 C CE2   . PHE B 1 313 ? -15.789 -56.518 24.629  1.00 30.92  ? 311 PHE B CE2   1 
ATOM   6904 C CZ    . PHE B 1 313 ? -16.082 -57.426 23.635  1.00 29.23  ? 311 PHE B CZ    1 
ATOM   6905 N N     . GLN B 1 314 ? -13.227 -52.466 23.738  1.00 34.76  ? 312 GLN B N     1 
ATOM   6906 C CA    . GLN B 1 314 ? -14.329 -51.495 23.969  1.00 35.41  ? 312 GLN B CA    1 
ATOM   6907 C C     . GLN B 1 314 ? -14.580 -50.760 22.650  1.00 34.71  ? 312 GLN B C     1 
ATOM   6908 O O     . GLN B 1 314 ? -15.758 -50.712 22.219  1.00 32.65  ? 312 GLN B O     1 
ATOM   6909 C CB    . GLN B 1 314 ? -14.031 -50.542 25.127  1.00 31.75  ? 312 GLN B CB    1 
ATOM   6910 C CG    . GLN B 1 314 ? -14.148 -51.217 26.472  1.00 31.33  ? 312 GLN B CG    1 
ATOM   6911 C CD    . GLN B 1 314 ? -14.113 -50.253 27.638  1.00 34.66  ? 312 GLN B CD    1 
ATOM   6912 O OE1   . GLN B 1 314 ? -14.490 -49.092 27.532  1.00 36.11  ? 312 GLN B OE1   1 
ATOM   6913 N NE2   . GLN B 1 314 ? -13.697 -50.746 28.799  1.00 41.05  ? 312 GLN B NE2   1 
ATOM   6914 N N     . GLY B 1 315 ? -13.517 -50.246 22.028  1.00 30.23  ? 313 GLY B N     1 
ATOM   6915 C CA    . GLY B 1 315 ? -13.607 -49.556 20.721  1.00 31.94  ? 313 GLY B CA    1 
ATOM   6916 C C     . GLY B 1 315 ? -14.120 -50.495 19.624  1.00 29.98  ? 313 GLY B C     1 
ATOM   6917 O O     . GLY B 1 315 ? -15.128 -50.168 18.957  1.00 29.57  ? 313 GLY B O     1 
ATOM   6918 N N     . GLY B 1 316 ? -13.493 -51.658 19.479  1.00 26.62  ? 314 GLY B N     1 
ATOM   6919 C CA    . GLY B 1 316 ? -13.858 -52.633 18.439  1.00 29.73  ? 314 GLY B CA    1 
ATOM   6920 C C     . GLY B 1 316 ? -15.327 -52.996 18.502  1.00 31.00  ? 314 GLY B C     1 
ATOM   6921 O O     . GLY B 1 316 ? -15.974 -53.026 17.428  1.00 29.40  ? 314 GLY B O     1 
ATOM   6922 N N     . ILE B 1 317 ? -15.860 -53.359 19.670  1.00 31.51  ? 315 ILE B N     1 
ATOM   6923 C CA    . ILE B 1 317 ? -17.271 -53.851 19.729  1.00 32.40  ? 315 ILE B CA    1 
ATOM   6924 C C     . ILE B 1 317 ? -18.238 -52.726 19.326  1.00 33.34  ? 315 ILE B C     1 
ATOM   6925 O O     . ILE B 1 317 ? -19.166 -52.997 18.557  1.00 36.94  ? 315 ILE B O     1 
ATOM   6926 C CB    . ILE B 1 317 ? -17.613 -54.493 21.093  1.00 34.07  ? 315 ILE B CB    1 
ATOM   6927 C CG1   . ILE B 1 317 ? -18.970 -55.199 21.052  1.00 33.45  ? 315 ILE B CG1   1 
ATOM   6928 C CG2   . ILE B 1 317 ? -17.528 -53.486 22.228  1.00 30.81  ? 315 ILE B CG2   1 
ATOM   6929 C CD1   . ILE B 1 317 ? -19.168 -56.064 19.833  1.00 31.65  ? 315 ILE B CD1   1 
ATOM   6930 N N     . ALA B 1 318 ? -17.988 -51.508 19.788  1.00 30.90  ? 316 ALA B N     1 
ATOM   6931 C CA    . ALA B 1 318 ? -18.862 -50.364 19.455  1.00 34.52  ? 316 ALA B CA    1 
ATOM   6932 C C     . ALA B 1 318 ? -18.873 -50.105 17.941  1.00 36.54  ? 316 ALA B C     1 
ATOM   6933 O O     . ALA B 1 318 ? -19.968 -50.004 17.383  1.00 36.94  ? 316 ALA B O     1 
ATOM   6934 C CB    . ALA B 1 318 ? -18.396 -49.163 20.227  1.00 31.68  ? 316 ALA B CB    1 
ATOM   6935 N N     . TYR B 1 319 ? -17.700 -50.035 17.316  1.00 33.42  ? 317 TYR B N     1 
ATOM   6936 C CA    . TYR B 1 319 ? -17.589 -49.724 15.870  1.00 31.51  ? 317 TYR B CA    1 
ATOM   6937 C C     . TYR B 1 319 ? -18.155 -50.868 15.031  1.00 32.84  ? 317 TYR B C     1 
ATOM   6938 O O     . TYR B 1 319 ? -18.792 -50.578 14.023  1.00 33.98  ? 317 TYR B O     1 
ATOM   6939 C CB    . TYR B 1 319 ? -16.129 -49.437 15.519  1.00 31.39  ? 317 TYR B CB    1 
ATOM   6940 C CG    . TYR B 1 319 ? -15.904 -48.713 14.219  1.00 33.05  ? 317 TYR B CG    1 
ATOM   6941 C CD1   . TYR B 1 319 ? -16.096 -47.347 14.125  1.00 33.94  ? 317 TYR B CD1   1 
ATOM   6942 C CD2   . TYR B 1 319 ? -15.489 -49.389 13.086  1.00 33.09  ? 317 TYR B CD2   1 
ATOM   6943 C CE1   . TYR B 1 319 ? -15.888 -46.669 12.939  1.00 33.93  ? 317 TYR B CE1   1 
ATOM   6944 C CE2   . TYR B 1 319 ? -15.279 -48.727 11.889  1.00 36.20  ? 317 TYR B CE2   1 
ATOM   6945 C CZ    . TYR B 1 319 ? -15.479 -47.362 11.816  1.00 34.32  ? 317 TYR B CZ    1 
ATOM   6946 O OH    . TYR B 1 319 ? -15.276 -46.692 10.648  1.00 35.06  ? 317 TYR B OH    1 
ATOM   6947 N N     . ALA B 1 320 ? -17.942 -52.113 15.454  1.00 29.99  ? 318 ALA B N     1 
ATOM   6948 C CA    . ALA B 1 320 ? -18.384 -53.290 14.670  1.00 27.12  ? 318 ALA B CA    1 
ATOM   6949 C C     . ALA B 1 320 ? -19.909 -53.417 14.634  1.00 28.03  ? 318 ALA B C     1 
ATOM   6950 O O     . ALA B 1 320 ? -20.418 -53.841 13.599  1.00 33.63  ? 318 ALA B O     1 
ATOM   6951 C CB    . ALA B 1 320 ? -17.741 -54.537 15.205  1.00 23.28  ? 318 ALA B CB    1 
ATOM   6952 N N     A ARG B 1 321 ? -20.593 -52.768 15.578  0.50 30.78  ? 319 ARG B N     1 
ATOM   6953 N N     B ARG B 1 321 ? -20.591 -52.761 15.574  0.50 30.60  ? 319 ARG B N     1 
ATOM   6954 C CA    A ARG B 1 321 ? -22.078 -52.816 15.621  0.50 32.77  ? 319 ARG B CA    1 
ATOM   6955 C CA    B ARG B 1 321 ? -22.076 -52.815 15.616  0.50 32.41  ? 319 ARG B CA    1 
ATOM   6956 C C     A ARG B 1 321 ? -22.660 -51.551 14.979  0.50 33.89  ? 319 ARG B C     1 
ATOM   6957 C C     B ARG B 1 321 ? -22.666 -51.542 14.996  0.50 33.53  ? 319 ARG B C     1 
ATOM   6958 O O     A ARG B 1 321 ? -23.779 -51.640 14.463  0.50 37.46  ? 319 ARG B O     1 
ATOM   6959 O O     B ARG B 1 321 ? -23.786 -51.631 14.482  0.50 36.91  ? 319 ARG B O     1 
ATOM   6960 C CB    A ARG B 1 321 ? -22.570 -52.935 17.065  0.50 32.15  ? 319 ARG B CB    1 
ATOM   6961 C CB    B ARG B 1 321 ? -22.549 -53.007 17.058  0.50 31.60  ? 319 ARG B CB    1 
ATOM   6962 C CG    A ARG B 1 321 ? -22.240 -54.241 17.773  0.50 33.69  ? 319 ARG B CG    1 
ATOM   6963 C CG    B ARG B 1 321 ? -22.049 -54.286 17.714  0.50 32.92  ? 319 ARG B CG    1 
ATOM   6964 C CD    A ARG B 1 321 ? -22.550 -54.070 19.250  0.50 31.46  ? 319 ARG B CD    1 
ATOM   6965 C CD    B ARG B 1 321 ? -22.783 -54.569 19.009  0.50 31.80  ? 319 ARG B CD    1 
ATOM   6966 N NE    A ARG B 1 321 ? -22.459 -55.274 20.064  0.50 34.12  ? 319 ARG B NE    1 
ATOM   6967 N NE    B ARG B 1 321 ? -24.207 -54.736 18.765  0.50 32.55  ? 319 ARG B NE    1 
ATOM   6968 C CZ    A ARG B 1 321 ? -22.366 -55.278 21.392  0.50 28.99  ? 319 ARG B CZ    1 
ATOM   6969 C CZ    B ARG B 1 321 ? -25.114 -54.972 19.703  0.50 31.63  ? 319 ARG B CZ    1 
ATOM   6970 N NH1   A ARG B 1 321 ? -22.346 -54.136 22.058  0.50 23.18  ? 319 ARG B NH1   1 
ATOM   6971 N NH1   B ARG B 1 321 ? -24.750 -55.067 20.970  0.50 37.94  ? 319 ARG B NH1   1 
ATOM   6972 N NH2   A ARG B 1 321 ? -22.288 -56.422 22.050  0.50 26.29  ? 319 ARG B NH2   1 
ATOM   6973 N NH2   B ARG B 1 321 ? -26.385 -55.109 19.372  0.50 30.88  ? 319 ARG B NH2   1 
ATOM   6974 N N     . GLU B 1 322 ? -21.816 -50.546 14.733  1.00 35.36  ? 320 GLU B N     1 
ATOM   6975 C CA    . GLU B 1 322 ? -22.296 -49.263 14.155  1.00 40.53  ? 320 GLU B CA    1 
ATOM   6976 C C     . GLU B 1 322 ? -21.878 -49.097 12.684  1.00 36.40  ? 320 GLU B C     1 
ATOM   6977 O O     . GLU B 1 322 ? -22.668 -48.541 11.921  1.00 33.67  ? 320 GLU B O     1 
ATOM   6978 C CB    . GLU B 1 322 ? -21.796 -48.102 15.011  1.00 47.57  ? 320 GLU B CB    1 
ATOM   6979 C CG    . GLU B 1 322 ? -22.480 -48.035 16.363  1.00 60.84  ? 320 GLU B CG    1 
ATOM   6980 C CD    . GLU B 1 322 ? -21.836 -47.092 17.364  1.00 72.23  ? 320 GLU B CD    1 
ATOM   6981 O OE1   . GLU B 1 322 ? -21.229 -46.097 16.926  1.00 80.44  ? 320 GLU B OE1   1 
ATOM   6982 O OE2   . GLU B 1 322 ? -21.943 -47.356 18.579  1.00 76.82  ? 320 GLU B OE2   1 
ATOM   6983 N N     . ARG B 1 323 ? -20.691 -49.563 12.307  1.00 31.82  ? 321 ARG B N     1 
ATOM   6984 C CA    . ARG B 1 323 ? -20.193 -49.414 10.913  1.00 29.15  ? 321 ARG B CA    1 
ATOM   6985 C C     . ARG B 1 323 ? -20.885 -50.402 9.968   1.00 31.47  ? 321 ARG B C     1 
ATOM   6986 O O     . ARG B 1 323 ? -20.823 -51.608 10.220  1.00 31.88  ? 321 ARG B O     1 
ATOM   6987 C CB    . ARG B 1 323 ? -18.667 -49.540 10.824  1.00 26.70  ? 321 ARG B CB    1 
ATOM   6988 C CG    . ARG B 1 323 ? -18.107 -49.501 9.410   1.00 28.83  ? 321 ARG B CG    1 
ATOM   6989 C CD    . ARG B 1 323 ? -18.099 -48.111 8.808   1.00 28.95  ? 321 ARG B CD    1 
ATOM   6990 N NE    . ARG B 1 323 ? -17.298 -48.020 7.598   1.00 29.71  ? 321 ARG B NE    1 
ATOM   6991 C CZ    . ARG B 1 323 ? -17.101 -46.907 6.905   1.00 31.25  ? 321 ARG B CZ    1 
ATOM   6992 N NH1   . ARG B 1 323 ? -17.656 -45.775 7.296   1.00 30.39  ? 321 ARG B NH1   1 
ATOM   6993 N NH2   . ARG B 1 323 ? -16.353 -46.927 5.820   1.00 34.36  ? 321 ARG B NH2   1 
ATOM   6994 N N     . LEU B 1 324 ? -21.523 -49.881 8.930   1.00 29.95  ? 322 LEU B N     1 
ATOM   6995 C CA    . LEU B 1 324 ? -22.136 -50.712 7.884   1.00 30.55  ? 322 LEU B CA    1 
ATOM   6996 C C     . LEU B 1 324 ? -21.131 -50.759 6.737   1.00 33.49  ? 322 LEU B C     1 
ATOM   6997 O O     . LEU B 1 324 ? -20.632 -49.699 6.381   1.00 29.84  ? 322 LEU B O     1 
ATOM   6998 C CB    . LEU B 1 324 ? -23.475 -50.083 7.487   1.00 33.76  ? 322 LEU B CB    1 
ATOM   6999 C CG    . LEU B 1 324 ? -24.384 -49.592 8.625   1.00 31.64  ? 322 LEU B CG    1 
ATOM   7000 C CD1   . LEU B 1 324 ? -25.654 -48.979 8.041   1.00 29.02  ? 322 LEU B CD1   1 
ATOM   7001 C CD2   . LEU B 1 324 ? -24.734 -50.742 9.574   1.00 31.29  ? 322 LEU B CD2   1 
ATOM   7002 N N     . GLN B 1 325 ? -20.819 -51.970 6.257   1.00 35.84  ? 323 GLN B N     1 
ATOM   7003 C CA    . GLN B 1 325 ? -19.930 -52.189 5.088   1.00 30.58  ? 323 GLN B CA    1 
ATOM   7004 C C     . GLN B 1 325 ? -20.157 -53.600 4.543   1.00 27.13  ? 323 GLN B C     1 
ATOM   7005 O O     . GLN B 1 325 ? -19.988 -54.534 5.316   1.00 24.27  ? 323 GLN B O     1 
ATOM   7006 C CB    . GLN B 1 325 ? -18.439 -52.033 5.388   1.00 33.67  ? 323 GLN B CB    1 
ATOM   7007 C CG    . GLN B 1 325 ? -17.949 -50.606 5.545   1.00 38.68  ? 323 GLN B CG    1 
ATOM   7008 C CD    . GLN B 1 325 ? -17.916 -49.816 4.263   1.00 36.55  ? 323 GLN B CD    1 
ATOM   7009 O OE1   . GLN B 1 325 ? -17.121 -50.069 3.364   1.00 35.87  ? 323 GLN B OE1   1 
ATOM   7010 N NE2   . GLN B 1 325 ? -18.777 -48.821 4.187   1.00 34.68  ? 323 GLN B NE2   1 
ATOM   7011 N N     . MET B 1 326 ? -20.551 -53.725 3.277   1.00 27.56  ? 324 MET B N     1 
ATOM   7012 C CA    . MET B 1 326 ? -20.725 -54.996 2.545   1.00 31.95  ? 324 MET B CA    1 
ATOM   7013 C C     . MET B 1 326 ? -21.903 -55.732 3.168   1.00 30.12  ? 324 MET B C     1 
ATOM   7014 O O     . MET B 1 326 ? -22.621 -55.078 3.943   1.00 33.37  ? 324 MET B O     1 
ATOM   7015 C CB    . MET B 1 326 ? -19.424 -55.801 2.598   1.00 32.84  ? 324 MET B CB    1 
ATOM   7016 C CG    . MET B 1 326 ? -18.244 -55.001 2.014   1.00 35.19  ? 324 MET B CG    1 
ATOM   7017 S SD    . MET B 1 326 ? -18.453 -54.812 0.229   1.00 41.07  ? 324 MET B SD    1 
ATOM   7018 C CE    . MET B 1 326 ? -17.667 -56.301 -0.402  1.00 34.72  ? 324 MET B CE    1 
ATOM   7019 N N     . ARG B 1 327 ? -22.066 -57.016 2.860   1.00 29.17  ? 325 ARG B N     1 
ATOM   7020 C CA    . ARG B 1 327 ? -23.218 -57.830 3.314   1.00 30.96  ? 325 ARG B CA    1 
ATOM   7021 C C     . ARG B 1 327 ? -22.700 -59.165 3.841   1.00 33.37  ? 325 ARG B C     1 
ATOM   7022 O O     . ARG B 1 327 ? -21.611 -59.560 3.460   1.00 28.03  ? 325 ARG B O     1 
ATOM   7023 C CB    . ARG B 1 327 ? -24.208 -58.049 2.167   1.00 31.25  ? 325 ARG B CB    1 
ATOM   7024 C CG    . ARG B 1 327 ? -24.826 -56.768 1.622   1.00 31.86  ? 325 ARG B CG    1 
ATOM   7025 C CD    . ARG B 1 327 ? -25.673 -56.108 2.693   1.00 31.66  ? 325 ARG B CD    1 
ATOM   7026 N NE    . ARG B 1 327 ? -26.592 -55.181 2.090   1.00 32.90  ? 325 ARG B NE    1 
ATOM   7027 C CZ    . ARG B 1 327 ? -27.524 -54.499 2.730   1.00 32.32  ? 325 ARG B CZ    1 
ATOM   7028 N NH1   . ARG B 1 327 ? -27.669 -54.585 4.042   1.00 38.11  ? 325 ARG B NH1   1 
ATOM   7029 N NH2   . ARG B 1 327 ? -28.283 -53.684 2.046   1.00 28.86  ? 325 ARG B NH2   1 
ATOM   7030 N N     . SER B 1 328 ? -23.475 -59.799 4.716   1.00 36.50  ? 326 SER B N     1 
ATOM   7031 C CA    . SER B 1 328 ? -23.210 -61.154 5.258   1.00 35.35  ? 326 SER B CA    1 
ATOM   7032 C C     . SER B 1 328 ? -22.993 -62.112 4.087   1.00 37.29  ? 326 SER B C     1 
ATOM   7033 O O     . SER B 1 328 ? -23.601 -61.922 3.043   1.00 33.98  ? 326 SER B O     1 
ATOM   7034 C CB    . SER B 1 328 ? -24.344 -61.604 6.135   1.00 32.07  ? 326 SER B CB    1 
ATOM   7035 O OG    . SER B 1 328 ? -24.176 -62.955 6.528   1.00 35.57  ? 326 SER B OG    1 
ATOM   7036 N N     . LEU B 1 329 ? -22.225 -63.178 4.295   1.00 39.91  ? 327 LEU B N     1 
ATOM   7037 C CA    . LEU B 1 329 ? -22.015 -64.210 3.248   1.00 37.77  ? 327 LEU B CA    1 
ATOM   7038 C C     . LEU B 1 329 ? -23.266 -65.091 3.112   1.00 41.40  ? 327 LEU B C     1 
ATOM   7039 O O     . LEU B 1 329 ? -23.381 -65.757 2.080   1.00 38.86  ? 327 LEU B O     1 
ATOM   7040 C CB    . LEU B 1 329 ? -20.791 -65.028 3.653   1.00 35.31  ? 327 LEU B CB    1 
ATOM   7041 C CG    . LEU B 1 329 ? -19.463 -64.277 3.650   1.00 33.33  ? 327 LEU B CG    1 
ATOM   7042 C CD1   . LEU B 1 329 ? -18.393 -65.069 4.382   1.00 34.19  ? 327 LEU B CD1   1 
ATOM   7043 C CD2   . LEU B 1 329 ? -19.025 -63.978 2.229   1.00 32.24  ? 327 LEU B CD2   1 
ATOM   7044 N N     . THR B 1 330 ? -24.164 -65.083 4.105   1.00 42.50  ? 328 THR B N     1 
ATOM   7045 C CA    . THR B 1 330 ? -25.406 -65.917 4.106   1.00 40.96  ? 328 THR B CA    1 
ATOM   7046 C C     . THR B 1 330 ? -26.647 -65.045 3.879   1.00 42.48  ? 328 THR B C     1 
ATOM   7047 O O     . THR B 1 330 ? -27.705 -65.358 4.472   1.00 46.55  ? 328 THR B O     1 
ATOM   7048 C CB    . THR B 1 330 ? -25.572 -66.729 5.398   1.00 38.84  ? 328 THR B CB    1 
ATOM   7049 O OG1   . THR B 1 330 ? -25.521 -65.861 6.527   1.00 28.62  ? 328 THR B OG1   1 
ATOM   7050 C CG2   . THR B 1 330 ? -24.518 -67.796 5.520   1.00 37.60  ? 328 THR B CG2   1 
ATOM   7051 N N     . GLY B 1 331 ? -26.524 -64.034 3.022   1.00 40.00  ? 329 GLY B N     1 
ATOM   7052 C CA    . GLY B 1 331 ? -27.604 -63.102 2.663   1.00 38.91  ? 329 GLY B CA    1 
ATOM   7053 C C     . GLY B 1 331 ? -27.627 -61.875 3.571   1.00 39.72  ? 329 GLY B C     1 
ATOM   7054 O O     . GLY B 1 331 ? -27.255 -61.969 4.745   1.00 36.73  ? 329 GLY B O     1 
ATOM   7055 N N     . PRO B 1 332 ? -28.138 -60.723 3.065   1.00 35.19  ? 330 PRO B N     1 
ATOM   7056 C CA    . PRO B 1 332 ? -28.232 -59.485 3.843   1.00 38.60  ? 330 PRO B CA    1 
ATOM   7057 C C     . PRO B 1 332 ? -28.955 -59.623 5.199   1.00 38.28  ? 330 PRO B C     1 
ATOM   7058 O O     . PRO B 1 332 ? -30.040 -60.099 5.253   1.00 41.62  ? 330 PRO B O     1 
ATOM   7059 C CB    . PRO B 1 332 ? -29.008 -58.552 2.897   1.00 38.78  ? 330 PRO B CB    1 
ATOM   7060 C CG    . PRO B 1 332 ? -28.664 -59.045 1.507   1.00 35.02  ? 330 PRO B CG    1 
ATOM   7061 C CD    . PRO B 1 332 ? -28.621 -60.547 1.684   1.00 36.53  ? 330 PRO B CD    1 
ATOM   7062 N N     . LYS B 1 333 ? -28.319 -59.228 6.287   1.00 36.57  ? 331 LYS B N     1 
ATOM   7063 C CA    . LYS B 1 333 ? -28.904 -59.366 7.647   1.00 34.07  ? 331 LYS B CA    1 
ATOM   7064 C C     . LYS B 1 333 ? -29.653 -58.088 8.021   1.00 35.05  ? 331 LYS B C     1 
ATOM   7065 O O     . LYS B 1 333 ? -30.431 -58.141 8.930   1.00 35.90  ? 331 LYS B O     1 
ATOM   7066 C CB    . LYS B 1 333 ? -27.797 -59.619 8.666   1.00 33.19  ? 331 LYS B CB    1 
ATOM   7067 C CG    . LYS B 1 333 ? -27.087 -60.952 8.511   1.00 34.04  ? 331 LYS B CG    1 
ATOM   7068 C CD    . LYS B 1 333 ? -27.970 -62.137 8.807   1.00 31.07  ? 331 LYS B CD    1 
ATOM   7069 C CE    . LYS B 1 333 ? -27.280 -63.460 8.547   1.00 30.82  ? 331 LYS B CE    1 
ATOM   7070 N NZ    . LYS B 1 333 ? -27.416 -63.857 7.126   1.00 35.37  ? 331 LYS B NZ    1 
ATOM   7071 N N     . ALA B 1 334 ? -29.379 -56.963 7.370   1.00 40.07  ? 332 ALA B N     1 
ATOM   7072 C CA    . ALA B 1 334 ? -30.075 -55.681 7.616   1.00 39.49  ? 332 ALA B CA    1 
ATOM   7073 C C     . ALA B 1 334 ? -30.476 -55.105 6.266   1.00 38.06  ? 332 ALA B C     1 
ATOM   7074 O O     . ALA B 1 334 ? -29.949 -54.088 5.832   1.00 39.98  ? 332 ALA B O     1 
ATOM   7075 C CB    . ALA B 1 334 ? -29.204 -54.738 8.405   1.00 37.45  ? 332 ALA B CB    1 
ATOM   7076 N N     . PRO B 1 335 ? -31.438 -55.756 5.578   1.00 40.25  ? 333 PRO B N     1 
ATOM   7077 C CA    . PRO B 1 335 ? -31.809 -55.378 4.214   1.00 37.15  ? 333 PRO B CA    1 
ATOM   7078 C C     . PRO B 1 335 ? -32.489 -53.999 4.146   1.00 38.82  ? 333 PRO B C     1 
ATOM   7079 O O     . PRO B 1 335 ? -32.529 -53.456 3.080   1.00 35.50  ? 333 PRO B O     1 
ATOM   7080 C CB    . PRO B 1 335 ? -32.739 -56.515 3.771   1.00 36.61  ? 333 PRO B CB    1 
ATOM   7081 C CG    . PRO B 1 335 ? -33.319 -57.070 5.052   1.00 39.89  ? 333 PRO B CG    1 
ATOM   7082 C CD    . PRO B 1 335 ? -32.213 -56.905 6.081   1.00 42.90  ? 333 PRO B CD    1 
ATOM   7083 N N     . GLU B 1 336 ? -32.943 -53.468 5.288   1.00 33.88  ? 334 GLU B N     1 
ATOM   7084 C CA    . GLU B 1 336 ? -33.580 -52.131 5.450   1.00 35.13  ? 334 GLU B CA    1 
ATOM   7085 C C     . GLU B 1 336 ? -32.495 -51.037 5.595   1.00 37.09  ? 334 GLU B C     1 
ATOM   7086 O O     . GLU B 1 336 ? -32.857 -49.833 5.742   1.00 33.26  ? 334 GLU B O     1 
ATOM   7087 C CB    . GLU B 1 336 ? -34.586 -52.218 6.616   1.00 37.81  ? 334 GLU B CB    1 
ATOM   7088 C CG    . GLU B 1 336 ? -33.979 -52.296 8.026   1.00 41.67  ? 334 GLU B CG    1 
ATOM   7089 C CD    . GLU B 1 336 ? -33.102 -53.486 8.491   1.00 43.48  ? 334 GLU B CD    1 
ATOM   7090 O OE1   . GLU B 1 336 ? -32.386 -53.338 9.523   1.00 50.23  ? 334 GLU B OE1   1 
ATOM   7091 O OE2   . GLU B 1 336 ? -33.126 -54.561 7.885   1.00 39.99  ? 334 GLU B OE2   1 
ATOM   7092 N N     . LYS B 1 337 ? -31.205 -51.415 5.543   1.00 35.15  ? 335 LYS B N     1 
ATOM   7093 C CA    . LYS B 1 337 ? -30.048 -50.470 5.567   1.00 36.51  ? 335 LYS B CA    1 
ATOM   7094 C C     . LYS B 1 337 ? -29.191 -50.694 4.331   1.00 33.51  ? 335 LYS B C     1 
ATOM   7095 O O     . LYS B 1 337 ? -29.267 -51.756 3.722   1.00 40.71  ? 335 LYS B O     1 
ATOM   7096 C CB    . LYS B 1 337 ? -29.198 -50.702 6.818   1.00 37.63  ? 335 LYS B CB    1 
ATOM   7097 C CG    . LYS B 1 337 ? -29.989 -50.785 8.116   1.00 38.14  ? 335 LYS B CG    1 
ATOM   7098 C CD    . LYS B 1 337 ? -29.100 -51.026 9.297   1.00 36.76  ? 335 LYS B CD    1 
ATOM   7099 C CE    . LYS B 1 337 ? -29.866 -51.441 10.530  1.00 38.46  ? 335 LYS B CE    1 
ATOM   7100 N NZ    . LYS B 1 337 ? -29.078 -51.122 11.740  1.00 41.13  ? 335 LYS B NZ    1 
ATOM   7101 N N     . PRO B 1 338 ? -28.367 -49.716 3.907   1.00 31.51  ? 336 PRO B N     1 
ATOM   7102 C CA    . PRO B 1 338 ? -27.620 -49.854 2.658   1.00 30.90  ? 336 PRO B CA    1 
ATOM   7103 C C     . PRO B 1 338 ? -26.485 -50.882 2.782   1.00 35.93  ? 336 PRO B C     1 
ATOM   7104 O O     . PRO B 1 338 ? -25.998 -51.304 1.761   1.00 37.27  ? 336 PRO B O     1 
ATOM   7105 C CB    . PRO B 1 338 ? -27.101 -48.439 2.387   1.00 30.71  ? 336 PRO B CB    1 
ATOM   7106 C CG    . PRO B 1 338 ? -27.067 -47.780 3.770   1.00 33.47  ? 336 PRO B CG    1 
ATOM   7107 C CD    . PRO B 1 338 ? -28.220 -48.393 4.531   1.00 31.74  ? 336 PRO B CD    1 
ATOM   7108 N N     . ALA B 1 339 ? -26.117 -51.289 4.009   1.00 31.63  ? 337 ALA B N     1 
ATOM   7109 C CA    . ALA B 1 339 ? -25.071 -52.310 4.258   1.00 29.50  ? 337 ALA B CA    1 
ATOM   7110 C C     . ALA B 1 339 ? -25.339 -52.997 5.593   1.00 32.63  ? 337 ALA B C     1 
ATOM   7111 O O     . ALA B 1 339 ? -26.242 -52.543 6.337   1.00 37.26  ? 337 ALA B O     1 
ATOM   7112 C CB    . ALA B 1 339 ? -23.695 -51.682 4.206   1.00 28.60  ? 337 ALA B CB    1 
ATOM   7113 N N     . ASP B 1 340 ? -24.653 -54.110 5.850   1.00 29.80  ? 338 ASP B N     1 
ATOM   7114 C CA    . ASP B 1 340 ? -24.787 -54.857 7.123   1.00 30.42  ? 338 ASP B CA    1 
ATOM   7115 C C     . ASP B 1 340 ? -23.767 -54.276 8.089   1.00 30.78  ? 338 ASP B C     1 
ATOM   7116 O O     . ASP B 1 340 ? -22.723 -53.796 7.660   1.00 36.49  ? 338 ASP B O     1 
ATOM   7117 C CB    . ASP B 1 340 ? -24.598 -56.359 6.898   1.00 34.14  ? 338 ASP B CB    1 
ATOM   7118 C CG    . ASP B 1 340 ? -25.772 -57.049 6.214   1.00 36.07  ? 338 ASP B CG    1 
ATOM   7119 O OD1   . ASP B 1 340 ? -26.843 -56.368 6.017   1.00 35.61  ? 338 ASP B OD1   1 
ATOM   7120 O OD2   . ASP B 1 340 ? -25.636 -58.273 5.926   1.00 30.00  ? 338 ASP B OD2   1 
ATOM   7121 N N     . PRO B 1 341 ? -23.998 -54.377 9.421   1.00 29.44  ? 339 PRO B N     1 
ATOM   7122 C CA    . PRO B 1 341 ? -22.975 -53.995 10.390  1.00 26.51  ? 339 PRO B CA    1 
ATOM   7123 C C     . PRO B 1 341 ? -21.792 -54.953 10.181  1.00 27.60  ? 339 PRO B C     1 
ATOM   7124 O O     . PRO B 1 341 ? -22.025 -56.087 9.880   1.00 25.48  ? 339 PRO B O     1 
ATOM   7125 C CB    . PRO B 1 341 ? -23.676 -54.132 11.741  1.00 27.73  ? 339 PRO B CB    1 
ATOM   7126 C CG    . PRO B 1 341 ? -24.777 -55.122 11.495  1.00 27.57  ? 339 PRO B CG    1 
ATOM   7127 C CD    . PRO B 1 341 ? -25.231 -54.825 10.085  1.00 29.16  ? 339 PRO B CD    1 
ATOM   7128 N N     . ILE B 1 342 ? -20.564 -54.490 10.401  1.00 28.48  ? 340 ILE B N     1 
ATOM   7129 C CA    . ILE B 1 342 ? -19.364 -55.299 10.039  1.00 27.02  ? 340 ILE B CA    1 
ATOM   7130 C C     . ILE B 1 342 ? -19.195 -56.483 10.991  1.00 27.42  ? 340 ILE B C     1 
ATOM   7131 O O     . ILE B 1 342 ? -18.498 -57.440 10.595  1.00 28.43  ? 340 ILE B O     1 
ATOM   7132 C CB    . ILE B 1 342 ? -18.096 -54.438 9.907   1.00 25.51  ? 340 ILE B CB    1 
ATOM   7133 C CG1   . ILE B 1 342 ? -17.770 -53.634 11.165  1.00 25.08  ? 340 ILE B CG1   1 
ATOM   7134 C CG2   . ILE B 1 342 ? -18.229 -53.557 8.673   1.00 24.65  ? 340 ILE B CG2   1 
ATOM   7135 C CD1   . ILE B 1 342 ? -16.343 -53.140 11.200  1.00 23.27  ? 340 ILE B CD1   1 
ATOM   7136 N N     . ILE B 1 343 ? -19.943 -56.520 12.096  1.00 27.82  ? 341 ILE B N     1 
ATOM   7137 C CA    . ILE B 1 343 ? -19.952 -57.681 13.038  1.00 28.40  ? 341 ILE B CA    1 
ATOM   7138 C C     . ILE B 1 343 ? -20.448 -58.962 12.339  1.00 29.42  ? 341 ILE B C     1 
ATOM   7139 O O     . ILE B 1 343 ? -20.146 -60.030 12.837  1.00 28.40  ? 341 ILE B O     1 
ATOM   7140 C CB    . ILE B 1 343 ? -20.822 -57.366 14.274  1.00 27.35  ? 341 ILE B CB    1 
ATOM   7141 C CG1   . ILE B 1 343 ? -20.671 -58.434 15.361  1.00 29.35  ? 341 ILE B CG1   1 
ATOM   7142 C CG2   . ILE B 1 343 ? -22.274 -57.165 13.877  1.00 25.62  ? 341 ILE B CG2   1 
ATOM   7143 C CD1   . ILE B 1 343 ? -20.702 -57.894 16.767  1.00 33.87  ? 341 ILE B CD1   1 
ATOM   7144 N N     . VAL B 1 344 ? -21.186 -58.849 11.234  1.00 28.44  ? 342 VAL B N     1 
ATOM   7145 C CA    . VAL B 1 344 ? -21.740 -60.029 10.508  1.00 26.84  ? 342 VAL B CA    1 
ATOM   7146 C C     . VAL B 1 344 ? -20.621 -60.755 9.753   1.00 29.51  ? 342 VAL B C     1 
ATOM   7147 O O     . VAL B 1 344 ? -20.831 -61.902 9.356   1.00 29.75  ? 342 VAL B O     1 
ATOM   7148 C CB    . VAL B 1 344 ? -22.887 -59.605 9.575   1.00 29.62  ? 342 VAL B CB    1 
ATOM   7149 C CG1   . VAL B 1 344 ? -23.881 -58.692 10.271  1.00 30.81  ? 342 VAL B CG1   1 
ATOM   7150 C CG2   . VAL B 1 344 ? -22.380 -58.978 8.285   1.00 30.00  ? 342 VAL B CG2   1 
ATOM   7151 N N     . HIS B 1 345 ? -19.482 -60.093 9.563   1.00 33.31  ? 343 HIS B N     1 
ATOM   7152 C CA    . HIS B 1 345 ? -18.325 -60.699 8.858   1.00 32.34  ? 343 HIS B CA    1 
ATOM   7153 C C     . HIS B 1 345 ? -17.528 -61.596 9.816   1.00 32.23  ? 343 HIS B C     1 
ATOM   7154 O O     . HIS B 1 345 ? -17.181 -61.139 10.906  1.00 27.58  ? 343 HIS B O     1 
ATOM   7155 C CB    . HIS B 1 345 ? -17.464 -59.613 8.210   1.00 32.96  ? 343 HIS B CB    1 
ATOM   7156 C CG    . HIS B 1 345 ? -18.199 -58.680 7.311   1.00 36.65  ? 343 HIS B CG    1 
ATOM   7157 N ND1   . HIS B 1 345 ? -19.015 -59.122 6.295   1.00 35.28  ? 343 HIS B ND1   1 
ATOM   7158 C CD2   . HIS B 1 345 ? -18.223 -57.332 7.258   1.00 35.01  ? 343 HIS B CD2   1 
ATOM   7159 C CE1   . HIS B 1 345 ? -19.520 -58.087 5.661   1.00 38.48  ? 343 HIS B CE1   1 
ATOM   7160 N NE2   . HIS B 1 345 ? -19.048 -56.980 6.231   1.00 36.26  ? 343 HIS B NE2   1 
ATOM   7161 N N     . PRO B 1 346 ? -17.245 -62.858 9.431   1.00 30.59  ? 344 PRO B N     1 
ATOM   7162 C CA    . PRO B 1 346 ? -16.483 -63.792 10.282  1.00 31.93  ? 344 PRO B CA    1 
ATOM   7163 C C     . PRO B 1 346 ? -15.102 -63.297 10.771  1.00 32.83  ? 344 PRO B C     1 
ATOM   7164 O O     . PRO B 1 346 ? -14.778 -63.556 11.896  1.00 31.61  ? 344 PRO B O     1 
ATOM   7165 C CB    . PRO B 1 346 ? -16.378 -65.034 9.381   1.00 30.99  ? 344 PRO B CB    1 
ATOM   7166 C CG    . PRO B 1 346 ? -17.571 -64.944 8.469   1.00 28.73  ? 344 PRO B CG    1 
ATOM   7167 C CD    . PRO B 1 346 ? -17.686 -63.466 8.179   1.00 28.66  ? 344 PRO B CD    1 
ATOM   7168 N N     . ASP B 1 347 ? -14.366 -62.552 9.949   1.00 27.94  ? 345 ASP B N     1 
ATOM   7169 C CA    . ASP B 1 347 ? -13.032 -62.018 10.339  1.00 29.34  ? 345 ASP B CA    1 
ATOM   7170 C C     . ASP B 1 347 ? -13.141 -60.931 11.420  1.00 29.44  ? 345 ASP B C     1 
ATOM   7171 O O     . ASP B 1 347 ? -12.264 -60.894 12.277  1.00 27.30  ? 345 ASP B O     1 
ATOM   7172 C CB    . ASP B 1 347 ? -12.258 -61.498 9.131   1.00 29.77  ? 345 ASP B CB    1 
ATOM   7173 C CG    . ASP B 1 347 ? -10.789 -61.275 9.412   1.00 32.44  ? 345 ASP B CG    1 
ATOM   7174 O OD1   . ASP B 1 347 ? -10.108 -62.260 9.717   1.00 33.12  ? 345 ASP B OD1   1 
ATOM   7175 O OD2   . ASP B 1 347 ? -10.349 -60.120 9.327   1.00 33.15  ? 345 ASP B OD2   1 
ATOM   7176 N N     . VAL B 1 348 ? -14.155 -60.070 11.349  1.00 27.60  ? 346 VAL B N     1 
ATOM   7177 C CA    . VAL B 1 348 ? -14.375 -59.025 12.389  1.00 26.70  ? 346 VAL B CA    1 
ATOM   7178 C C     . VAL B 1 348 ? -14.661 -59.728 13.720  1.00 28.82  ? 346 VAL B C     1 
ATOM   7179 O O     . VAL B 1 348 ? -14.117 -59.300 14.731  1.00 25.96  ? 346 VAL B O     1 
ATOM   7180 C CB    . VAL B 1 348 ? -15.501 -58.053 11.991  1.00 27.80  ? 346 VAL B CB    1 
ATOM   7181 C CG1   . VAL B 1 348 ? -15.733 -56.978 13.039  1.00 27.56  ? 346 VAL B CG1   1 
ATOM   7182 C CG2   . VAL B 1 348 ? -15.253 -57.431 10.627  1.00 30.82  ? 346 VAL B CG2   1 
ATOM   7183 N N     . ARG B 1 349 ? -15.467 -60.785 13.688  1.00 27.16  ? 347 ARG B N     1 
ATOM   7184 C CA    . ARG B 1 349 ? -15.765 -61.580 14.902  1.00 30.22  ? 347 ARG B CA    1 
ATOM   7185 C C     . ARG B 1 349 ? -14.481 -62.255 15.401  1.00 31.40  ? 347 ARG B C     1 
ATOM   7186 O O     . ARG B 1 349 ? -14.264 -62.234 16.609  1.00 31.51  ? 347 ARG B O     1 
ATOM   7187 C CB    . ARG B 1 349 ? -16.905 -62.556 14.603  1.00 31.86  ? 347 ARG B CB    1 
ATOM   7188 C CG    . ARG B 1 349 ? -18.265 -61.883 14.501  1.00 31.79  ? 347 ARG B CG    1 
ATOM   7189 C CD    . ARG B 1 349 ? -19.241 -62.644 13.634  1.00 34.00  ? 347 ARG B CD    1 
ATOM   7190 N NE    . ARG B 1 349 ? -20.076 -63.505 14.449  1.00 47.26  ? 347 ARG B NE    1 
ATOM   7191 C CZ    . ARG B 1 349 ? -21.101 -63.099 15.184  1.00 42.97  ? 347 ARG B CZ    1 
ATOM   7192 N NH1   . ARG B 1 349 ? -21.447 -61.826 15.208  1.00 44.69  ? 347 ARG B NH1   1 
ATOM   7193 N NH2   . ARG B 1 349 ? -21.782 -63.975 15.892  1.00 52.59  ? 347 ARG B NH2   1 
ATOM   7194 N N     . ARG B 1 350 ? -13.653 -62.780 14.498  1.00 28.94  ? 348 ARG B N     1 
ATOM   7195 C CA    . ARG B 1 350 ? -12.356 -63.382 14.905  1.00 29.36  ? 348 ARG B CA    1 
ATOM   7196 C C     . ARG B 1 350 ? -11.522 -62.341 15.651  1.00 27.55  ? 348 ARG B C     1 
ATOM   7197 O O     . ARG B 1 350 ? -11.006 -62.665 16.721  1.00 33.69  ? 348 ARG B O     1 
ATOM   7198 C CB    . ARG B 1 350 ? -11.591 -63.926 13.699  1.00 31.84  ? 348 ARG B CB    1 
ATOM   7199 C CG    . ARG B 1 350 ? -10.151 -64.313 13.995  1.00 33.48  ? 348 ARG B CG    1 
ATOM   7200 C CD    . ARG B 1 350 ? -9.355  -64.612 12.740  1.00 36.47  ? 348 ARG B CD    1 
ATOM   7201 N NE    . ARG B 1 350 ? -9.105  -63.435 11.925  1.00 36.39  ? 348 ARG B NE    1 
ATOM   7202 C CZ    . ARG B 1 350 ? -8.180  -62.520 12.179  1.00 35.25  ? 348 ARG B CZ    1 
ATOM   7203 N NH1   . ARG B 1 350 ? -7.399  -62.641 13.237  1.00 36.24  ? 348 ARG B NH1   1 
ATOM   7204 N NH2   . ARG B 1 350 ? -8.036  -61.487 11.372  1.00 38.53  ? 348 ARG B NH2   1 
ATOM   7205 N N     . MET B 1 351 ? -11.460 -61.128 15.121  1.00 25.18  ? 349 MET B N     1 
ATOM   7206 C CA    . MET B 1 351 ? -10.673 -60.050 15.766  1.00 25.80  ? 349 MET B CA    1 
ATOM   7207 C C     . MET B 1 351 ? -11.304 -59.638 17.106  1.00 26.13  ? 349 MET B C     1 
ATOM   7208 O O     . MET B 1 351 ? -10.564 -59.505 18.076  1.00 30.10  ? 349 MET B O     1 
ATOM   7209 C CB    . MET B 1 351 ? -10.530 -58.852 14.828  1.00 25.11  ? 349 MET B CB    1 
ATOM   7210 C CG    . MET B 1 351 ? -9.634  -59.132 13.642  1.00 26.82  ? 349 MET B CG    1 
ATOM   7211 S SD    . MET B 1 351 ? -9.348  -57.687 12.601  1.00 29.80  ? 349 MET B SD    1 
ATOM   7212 C CE    . MET B 1 351 ? -10.894 -57.604 11.702  1.00 28.40  ? 349 MET B CE    1 
ATOM   7213 N N     . LEU B 1 352 ? -12.622 -59.497 17.160  1.00 27.49  ? 350 LEU B N     1 
ATOM   7214 C CA    . LEU B 1 352 ? -13.317 -59.148 18.424  1.00 30.35  ? 350 LEU B CA    1 
ATOM   7215 C C     . LEU B 1 352 ? -13.111 -60.257 19.462  1.00 29.21  ? 350 LEU B C     1 
ATOM   7216 O O     . LEU B 1 352 ? -12.784 -59.926 20.598  1.00 27.51  ? 350 LEU B O     1 
ATOM   7217 C CB    . LEU B 1 352 ? -14.809 -58.956 18.141  1.00 31.20  ? 350 LEU B CB    1 
ATOM   7218 C CG    . LEU B 1 352 ? -15.202 -57.710 17.353  1.00 33.54  ? 350 LEU B CG    1 
ATOM   7219 C CD1   . LEU B 1 352 ? -16.606 -57.867 16.790  1.00 34.51  ? 350 LEU B CD1   1 
ATOM   7220 C CD2   . LEU B 1 352 ? -15.117 -56.471 18.226  1.00 31.56  ? 350 LEU B CD2   1 
ATOM   7221 N N     . LEU B 1 353 ? -13.299 -61.515 19.066  1.00 27.40  ? 351 LEU B N     1 
ATOM   7222 C CA    . LEU B 1 353 ? -13.196 -62.648 20.017  1.00 30.65  ? 351 LEU B CA    1 
ATOM   7223 C C     . LEU B 1 353 ? -11.742 -62.819 20.478  1.00 33.09  ? 351 LEU B C     1 
ATOM   7224 O O     . LEU B 1 353 ? -11.542 -63.212 21.621  1.00 31.85  ? 351 LEU B O     1 
ATOM   7225 C CB    . LEU B 1 353 ? -13.746 -63.908 19.347  1.00 32.99  ? 351 LEU B CB    1 
ATOM   7226 C CG    . LEU B 1 353 ? -15.268 -63.983 19.241  1.00 35.99  ? 351 LEU B CG    1 
ATOM   7227 C CD1   . LEU B 1 353 ? -15.694 -65.178 18.405  1.00 37.79  ? 351 LEU B CD1   1 
ATOM   7228 C CD2   . LEU B 1 353 ? -15.907 -64.036 20.618  1.00 34.64  ? 351 LEU B CD2   1 
ATOM   7229 N N     . THR B 1 354 ? -10.774 -62.484 19.626  1.00 32.69  ? 352 THR B N     1 
ATOM   7230 C CA    . THR B 1 354 ? -9.360  -62.543 20.064  1.00 31.43  ? 352 THR B CA    1 
ATOM   7231 C C     . THR B 1 354 ? -9.162  -61.572 21.227  1.00 29.98  ? 352 THR B C     1 
ATOM   7232 O O     . THR B 1 354 ? -8.571  -61.943 22.236  1.00 25.33  ? 352 THR B O     1 
ATOM   7233 C CB    . THR B 1 354 ? -8.422  -62.224 18.904  1.00 28.56  ? 352 THR B CB    1 
ATOM   7234 O OG1   . THR B 1 354 ? -8.702  -63.196 17.900  1.00 30.04  ? 352 THR B OG1   1 
ATOM   7235 C CG2   . THR B 1 354 ? -6.975  -62.294 19.303  1.00 29.44  ? 352 THR B CG2   1 
ATOM   7236 N N     . MET B 1 355 ? -9.593  -60.334 21.055  1.00 29.12  ? 353 MET B N     1 
ATOM   7237 C CA    . MET B 1 355 ? -9.405  -59.296 22.090  1.00 29.10  ? 353 MET B CA    1 
ATOM   7238 C C     . MET B 1 355 ? -10.144 -59.736 23.363  1.00 29.01  ? 353 MET B C     1 
ATOM   7239 O O     . MET B 1 355 ? -9.554  -59.597 24.437  1.00 25.58  ? 353 MET B O     1 
ATOM   7240 C CB    . MET B 1 355 ? -9.916  -57.934 21.607  1.00 30.06  ? 353 MET B CB    1 
ATOM   7241 C CG    . MET B 1 355 ? -9.200  -57.432 20.377  1.00 30.92  ? 353 MET B CG    1 
ATOM   7242 S SD    . MET B 1 355 ? -9.642  -55.759 20.005  1.00 29.50  ? 353 MET B SD    1 
ATOM   7243 C CE    . MET B 1 355 ? -11.270 -56.017 19.322  1.00 32.28  ? 353 MET B CE    1 
ATOM   7244 N N     . LYS B 1 356 ? -11.358 -60.279 23.212  1.00 27.49  ? 354 LYS B N     1 
ATOM   7245 C CA    . LYS B 1 356 ? -12.241 -60.706 24.317  1.00 31.22  ? 354 LYS B CA    1 
ATOM   7246 C C     . LYS B 1 356 ? -11.596 -61.861 25.106  1.00 29.94  ? 354 LYS B C     1 
ATOM   7247 O O     . LYS B 1 356 ? -11.594 -61.791 26.354  1.00 29.56  ? 354 LYS B O     1 
ATOM   7248 C CB    . LYS B 1 356 ? -13.589 -61.128 23.721  1.00 31.62  ? 354 LYS B CB    1 
ATOM   7249 C CG    . LYS B 1 356 ? -14.742 -61.243 24.722  1.00 29.43  ? 354 LYS B CG    1 
ATOM   7250 C CD    . LYS B 1 356 ? -16.066 -61.682 24.058  1.00 28.81  ? 354 LYS B CD    1 
ATOM   7251 C CE    . LYS B 1 356 ? -17.213 -61.975 24.998  1.00 29.02  ? 354 LYS B CE    1 
ATOM   7252 N NZ    . LYS B 1 356 ? -17.296 -60.970 26.078  1.00 27.77  ? 354 LYS B NZ    1 
ATOM   7253 N N     . ALA B 1 357 ? -11.100 -62.890 24.405  1.00 30.64  ? 355 ALA B N     1 
ATOM   7254 C CA    . ALA B 1 357 ? -10.379 -64.055 24.973  1.00 29.55  ? 355 ALA B CA    1 
ATOM   7255 C C     . ALA B 1 357 ? -9.155  -63.564 25.747  1.00 30.17  ? 355 ALA B C     1 
ATOM   7256 O O     . ALA B 1 357 ? -9.003  -63.977 26.920  1.00 32.13  ? 355 ALA B O     1 
ATOM   7257 C CB    . ALA B 1 357 ? -10.032 -65.055 23.908  1.00 30.61  ? 355 ALA B CB    1 
ATOM   7258 N N     . PHE B 1 358 ? -8.402  -62.604 25.215  1.00 28.75  ? 356 PHE B N     1 
ATOM   7259 C CA    . PHE B 1 358 ? -7.201  -62.061 25.904  1.00 29.58  ? 356 PHE B CA    1 
ATOM   7260 C C     . PHE B 1 358 ? -7.587  -61.152 27.089  1.00 29.95  ? 356 PHE B C     1 
ATOM   7261 O O     . PHE B 1 358 ? -7.018  -61.325 28.193  1.00 29.02  ? 356 PHE B O     1 
ATOM   7262 C CB    . PHE B 1 358 ? -6.253  -61.378 24.917  1.00 29.85  ? 356 PHE B CB    1 
ATOM   7263 C CG    . PHE B 1 358 ? -5.542  -62.325 23.984  1.00 31.78  ? 356 PHE B CG    1 
ATOM   7264 C CD1   . PHE B 1 358 ? -4.998  -63.512 24.453  1.00 35.40  ? 356 PHE B CD1   1 
ATOM   7265 C CD2   . PHE B 1 358 ? -5.328  -61.992 22.661  1.00 31.66  ? 356 PHE B CD2   1 
ATOM   7266 C CE1   . PHE B 1 358 ? -4.296  -64.356 23.607  1.00 35.21  ? 356 PHE B CE1   1 
ATOM   7267 C CE2   . PHE B 1 358 ? -4.619  -62.837 21.819  1.00 34.94  ? 356 PHE B CE2   1 
ATOM   7268 C CZ    . PHE B 1 358 ? -4.104  -64.019 22.288  1.00 33.76  ? 356 PHE B CZ    1 
ATOM   7269 N N     . ALA B 1 359 ? -8.529  -60.227 26.921  1.00 30.76  ? 357 ALA B N     1 
ATOM   7270 C CA    . ALA B 1 359 ? -8.951  -59.331 28.020  1.00 32.62  ? 357 ALA B CA    1 
ATOM   7271 C C     . ALA B 1 359 ? -9.468  -60.169 29.206  1.00 35.51  ? 357 ALA B C     1 
ATOM   7272 O O     . ALA B 1 359 ? -8.914  -60.007 30.303  1.00 34.50  ? 357 ALA B O     1 
ATOM   7273 C CB    . ALA B 1 359 ? -9.971  -58.325 27.560  1.00 30.99  ? 357 ALA B CB    1 
ATOM   7274 N N     . GLU B 1 360 ? -10.454 -61.049 28.987  1.00 38.05  ? 358 GLU B N     1 
ATOM   7275 C CA    . GLU B 1 360 ? -11.192 -61.780 30.059  1.00 39.42  ? 358 GLU B CA    1 
ATOM   7276 C C     . GLU B 1 360 ? -10.307 -62.890 30.631  1.00 39.02  ? 358 GLU B C     1 
ATOM   7277 O O     . GLU B 1 360 ? -10.376 -63.134 31.831  1.00 45.78  ? 358 GLU B O     1 
ATOM   7278 C CB    . GLU B 1 360 ? -12.521 -62.321 29.517  1.00 37.01  ? 358 GLU B CB    1 
ATOM   7279 C CG    . GLU B 1 360 ? -13.530 -61.201 29.355  1.00 40.61  ? 358 GLU B CG    1 
ATOM   7280 C CD    . GLU B 1 360 ? -14.818 -61.519 28.623  1.00 42.04  ? 358 GLU B CD    1 
ATOM   7281 O OE1   . GLU B 1 360 ? -15.371 -60.577 28.026  1.00 38.09  ? 358 GLU B OE1   1 
ATOM   7282 O OE2   . GLU B 1 360 ? -15.256 -62.697 28.652  1.00 36.78  ? 358 GLU B OE2   1 
ATOM   7283 N N     . GLY B 1 361 ? -9.549  -63.559 29.773  1.00 38.27  ? 359 GLY B N     1 
ATOM   7284 C CA    . GLY B 1 361 ? -8.534  -64.554 30.157  1.00 36.23  ? 359 GLY B CA    1 
ATOM   7285 C C     . GLY B 1 361 ? -7.508  -63.945 31.085  1.00 32.56  ? 359 GLY B C     1 
ATOM   7286 O O     . GLY B 1 361 ? -7.269  -64.522 32.172  1.00 32.32  ? 359 GLY B O     1 
ATOM   7287 N N     . ASN B 1 362 ? -6.922  -62.815 30.691  1.00 29.55  ? 360 ASN B N     1 
ATOM   7288 C CA    . ASN B 1 362 ? -5.813  -62.205 31.467  1.00 32.00  ? 360 ASN B CA    1 
ATOM   7289 C C     . ASN B 1 362 ? -6.381  -61.576 32.737  1.00 33.00  ? 360 ASN B C     1 
ATOM   7290 O O     . ASN B 1 362 ? -5.616  -61.455 33.716  1.00 34.60  ? 360 ASN B O     1 
ATOM   7291 C CB    . ASN B 1 362 ? -4.988  -61.207 30.641  1.00 31.68  ? 360 ASN B CB    1 
ATOM   7292 C CG    . ASN B 1 362 ? -4.159  -61.880 29.565  1.00 32.26  ? 360 ASN B CG    1 
ATOM   7293 O OD1   . ASN B 1 362 ? -3.765  -63.041 29.691  1.00 30.48  ? 360 ASN B OD1   1 
ATOM   7294 N ND2   . ASN B 1 362 ? -3.863  -61.143 28.510  1.00 34.69  ? 360 ASN B ND2   1 
ATOM   7295 N N     . ARG B 1 363 ? -7.648  -61.142 32.728  1.00 35.04  ? 361 ARG B N     1 
ATOM   7296 C CA    . ARG B 1 363 ? -8.284  -60.599 33.950  1.00 36.85  ? 361 ARG B CA    1 
ATOM   7297 C C     . ARG B 1 363 ? -8.297  -61.725 35.007  1.00 37.85  ? 361 ARG B C     1 
ATOM   7298 O O     . ARG B 1 363 ? -7.916  -61.467 36.146  1.00 34.10  ? 361 ARG B O     1 
ATOM   7299 C CB    . ARG B 1 363 ? -9.667  -60.010 33.651  1.00 35.90  ? 361 ARG B CB    1 
ATOM   7300 C CG    . ARG B 1 363 ? -10.234 -59.233 34.830  1.00 36.00  ? 361 ARG B CG    1 
ATOM   7301 C CD    . ARG B 1 363 ? -11.446 -58.387 34.498  1.00 36.56  ? 361 ARG B CD    1 
ATOM   7302 N NE    . ARG B 1 363 ? -11.094 -57.244 33.673  1.00 34.86  ? 361 ARG B NE    1 
ATOM   7303 C CZ    . ARG B 1 363 ? -11.452 -57.097 32.393  1.00 34.78  ? 361 ARG B CZ    1 
ATOM   7304 N NH1   . ARG B 1 363 ? -12.208 -58.003 31.769  1.00 31.85  ? 361 ARG B NH1   1 
ATOM   7305 N NH2   . ARG B 1 363 ? -11.053 -56.019 31.741  1.00 32.85  ? 361 ARG B NH2   1 
ATOM   7306 N N     . ALA B 1 364 ? -8.678  -62.945 34.631  1.00 37.06  ? 362 ALA B N     1 
ATOM   7307 C CA    . ALA B 1 364 ? -8.733  -64.115 35.538  1.00 38.84  ? 362 ALA B CA    1 
ATOM   7308 C C     . ALA B 1 364 ? -7.337  -64.377 36.117  1.00 40.65  ? 362 ALA B C     1 
ATOM   7309 O O     . ALA B 1 364 ? -7.203  -64.389 37.349  1.00 42.32  ? 362 ALA B O     1 
ATOM   7310 C CB    . ALA B 1 364 ? -9.281  -65.328 34.816  1.00 38.25  ? 362 ALA B CB    1 
ATOM   7311 N N     . MET B 1 365 ? -6.331  -64.543 35.253  1.00 43.25  ? 363 MET B N     1 
ATOM   7312 C CA    . MET B 1 365 ? -4.922  -64.786 35.657  1.00 39.44  ? 363 MET B CA    1 
ATOM   7313 C C     . MET B 1 365 ? -4.453  -63.667 36.586  1.00 36.99  ? 363 MET B C     1 
ATOM   7314 O O     . MET B 1 365 ? -3.790  -63.943 37.579  1.00 37.19  ? 363 MET B O     1 
ATOM   7315 C CB    . MET B 1 365 ? -3.985  -64.880 34.456  1.00 39.96  ? 363 MET B CB    1 
ATOM   7316 C CG    . MET B 1 365 ? -2.517  -65.026 34.863  1.00 42.20  ? 363 MET B CG    1 
ATOM   7317 S SD    . MET B 1 365 ? -1.541  -66.024 33.726  1.00 40.79  ? 363 MET B SD    1 
ATOM   7318 C CE    . MET B 1 365 ? -1.685  -65.056 32.233  1.00 49.43  ? 363 MET B CE    1 
ATOM   7319 N N     . LEU B 1 366 ? -4.789  -62.428 36.291  1.00 40.71  ? 364 LEU B N     1 
ATOM   7320 C CA    . LEU B 1 366 ? -4.272  -61.303 37.093  1.00 41.78  ? 364 LEU B CA    1 
ATOM   7321 C C     . LEU B 1 366 ? -4.823  -61.377 38.536  1.00 45.44  ? 364 LEU B C     1 
ATOM   7322 O O     . LEU B 1 366 ? -4.026  -61.191 39.451  1.00 39.79  ? 364 LEU B O     1 
ATOM   7323 C CB    . LEU B 1 366 ? -4.671  -60.010 36.400  1.00 44.94  ? 364 LEU B CB    1 
ATOM   7324 C CG    . LEU B 1 366 ? -4.346  -58.762 37.203  1.00 51.08  ? 364 LEU B CG    1 
ATOM   7325 C CD1   . LEU B 1 366 ? -2.931  -58.293 36.893  1.00 50.19  ? 364 LEU B CD1   1 
ATOM   7326 C CD2   . LEU B 1 366 ? -5.391  -57.689 36.936  1.00 52.63  ? 364 LEU B CD2   1 
ATOM   7327 N N     . TYR B 1 367 ? -6.127  -61.625 38.750  1.00 42.19  ? 365 TYR B N     1 
ATOM   7328 C CA    . TYR B 1 367 ? -6.745  -61.615 40.102  1.00 40.32  ? 365 TYR B CA    1 
ATOM   7329 C C     . TYR B 1 367 ? -6.476  -62.960 40.796  1.00 42.35  ? 365 TYR B C     1 
ATOM   7330 O O     . TYR B 1 367 ? -6.582  -63.032 42.054  1.00 46.13  ? 365 TYR B O     1 
ATOM   7331 C CB    . TYR B 1 367 ? -8.237  -61.258 40.076  1.00 40.88  ? 365 TYR B CB    1 
ATOM   7332 C CG    . TYR B 1 367 ? -8.505  -59.809 39.789  1.00 38.53  ? 365 TYR B CG    1 
ATOM   7333 C CD1   . TYR B 1 367 ? -8.017  -58.822 40.612  1.00 41.97  ? 365 TYR B CD1   1 
ATOM   7334 C CD2   . TYR B 1 367 ? -9.181  -59.421 38.648  1.00 43.58  ? 365 TYR B CD2   1 
ATOM   7335 C CE1   . TYR B 1 367 ? -8.193  -57.481 40.309  1.00 44.71  ? 365 TYR B CE1   1 
ATOM   7336 C CE2   . TYR B 1 367 ? -9.375  -58.084 38.335  1.00 42.61  ? 365 TYR B CE2   1 
ATOM   7337 C CZ    . TYR B 1 367 ? -8.874  -57.105 39.166  1.00 43.73  ? 365 TYR B CZ    1 
ATOM   7338 O OH    . TYR B 1 367 ? -9.036  -55.782 38.858  1.00 42.99  ? 365 TYR B OH    1 
ATOM   7339 N N     . PHE B 1 368 ? -6.119  -63.996 40.043  1.00 40.56  ? 366 PHE B N     1 
ATOM   7340 C CA    . PHE B 1 368 ? -5.579  -65.249 40.630  1.00 44.81  ? 366 PHE B CA    1 
ATOM   7341 C C     . PHE B 1 368 ? -4.222  -64.940 41.276  1.00 46.72  ? 366 PHE B C     1 
ATOM   7342 O O     . PHE B 1 368 ? -3.999  -65.364 42.453  1.00 49.23  ? 366 PHE B O     1 
ATOM   7343 C CB    . PHE B 1 368 ? -5.474  -66.362 39.587  1.00 44.95  ? 366 PHE B CB    1 
ATOM   7344 C CG    . PHE B 1 368 ? -4.828  -67.630 40.086  1.00 42.68  ? 366 PHE B CG    1 
ATOM   7345 C CD1   . PHE B 1 368 ? -3.448  -67.777 40.049  1.00 39.86  ? 366 PHE B CD1   1 
ATOM   7346 C CD2   . PHE B 1 368 ? -5.604  -68.679 40.552  1.00 42.34  ? 366 PHE B CD2   1 
ATOM   7347 C CE1   . PHE B 1 368 ? -2.852  -68.947 40.483  1.00 43.66  ? 366 PHE B CE1   1 
ATOM   7348 C CE2   . PHE B 1 368 ? -5.009  -69.852 40.997  1.00 45.69  ? 366 PHE B CE2   1 
ATOM   7349 C CZ    . PHE B 1 368 ? -3.632  -69.973 40.975  1.00 47.59  ? 366 PHE B CZ    1 
ATOM   7350 N N     . ALA B 1 369 ? -3.363  -64.204 40.558  1.00 40.79  ? 367 ALA B N     1 
ATOM   7351 C CA    . ALA B 1 369 ? -2.012  -63.809 41.026  1.00 36.17  ? 367 ALA B CA    1 
ATOM   7352 C C     . ALA B 1 369 ? -2.170  -62.897 42.222  1.00 37.06  ? 367 ALA B C     1 
ATOM   7353 O O     . ALA B 1 369 ? -1.336  -62.980 43.150  1.00 41.99  ? 367 ALA B O     1 
ATOM   7354 C CB    . ALA B 1 369 ? -1.228  -63.090 39.960  1.00 36.85  ? 367 ALA B CB    1 
ATOM   7355 N N     . ALA B 1 370 ? -3.171  -62.014 42.178  1.00 35.80  ? 368 ALA B N     1 
ATOM   7356 C CA    . ALA B 1 370 ? -3.334  -60.968 43.211  1.00 37.21  ? 368 ALA B CA    1 
ATOM   7357 C C     . ALA B 1 370 ? -3.694  -61.615 44.550  1.00 38.88  ? 368 ALA B C     1 
ATOM   7358 O O     . ALA B 1 370 ? -3.318  -61.065 45.577  1.00 43.86  ? 368 ALA B O     1 
ATOM   7359 C CB    . ALA B 1 370 ? -4.349  -59.949 42.786  1.00 36.86  ? 368 ALA B CB    1 
ATOM   7360 N N     . LYS B 1 371 ? -4.390  -62.745 44.534  1.00 41.87  ? 369 LYS B N     1 
ATOM   7361 C CA    . LYS B 1 371 ? -4.700  -63.509 45.767  1.00 45.09  ? 369 LYS B CA    1 
ATOM   7362 C C     . LYS B 1 371 ? -3.395  -63.993 46.390  1.00 45.24  ? 369 LYS B C     1 
ATOM   7363 O O     . LYS B 1 371 ? -3.291  -63.925 47.621  1.00 46.17  ? 369 LYS B O     1 
ATOM   7364 C CB    . LYS B 1 371 ? -5.603  -64.704 45.475  1.00 43.81  ? 369 LYS B CB    1 
ATOM   7365 C CG    . LYS B 1 371 ? -7.075  -64.361 45.435  1.00 42.95  ? 369 LYS B CG    1 
ATOM   7366 C CD    . LYS B 1 371 ? -7.876  -65.462 44.821  1.00 44.16  ? 369 LYS B CD    1 
ATOM   7367 C CE    . LYS B 1 371 ? -8.127  -66.625 45.736  1.00 42.84  ? 369 LYS B CE    1 
ATOM   7368 N NZ    . LYS B 1 371 ? -8.673  -67.751 44.954  1.00 47.47  ? 369 LYS B NZ    1 
ATOM   7369 N N     . GLN B 1 372 ? -2.445  -64.444 45.563  1.00 42.75  ? 370 GLN B N     1 
ATOM   7370 C CA    . GLN B 1 372 ? -1.105  -64.888 46.030  1.00 40.92  ? 370 GLN B CA    1 
ATOM   7371 C C     . GLN B 1 372 ? -0.408  -63.719 46.708  1.00 39.40  ? 370 GLN B C     1 
ATOM   7372 O O     . GLN B 1 372 ? 0.105   -63.914 47.801  1.00 37.66  ? 370 GLN B O     1 
ATOM   7373 C CB    . GLN B 1 372 ? -0.245  -65.379 44.876  1.00 44.50  ? 370 GLN B CB    1 
ATOM   7374 C CG    . GLN B 1 372 ? -0.928  -66.439 44.032  1.00 45.44  ? 370 GLN B CG    1 
ATOM   7375 C CD    . GLN B 1 372 ? -1.615  -67.489 44.860  1.00 48.70  ? 370 GLN B CD    1 
ATOM   7376 O OE1   . GLN B 1 372 ? -1.083  -68.013 45.840  1.00 53.16  ? 370 GLN B OE1   1 
ATOM   7377 N NE2   . GLN B 1 372 ? -2.837  -67.783 44.471  1.00 58.96  ? 370 GLN B NE2   1 
ATOM   7378 N N     . VAL B 1 373 ? -0.444  -62.538 46.100  1.00 38.13  ? 371 VAL B N     1 
ATOM   7379 C CA    . VAL B 1 373 ? 0.214   -61.325 46.662  1.00 39.49  ? 371 VAL B CA    1 
ATOM   7380 C C     . VAL B 1 373 ? -0.344  -61.028 48.064  1.00 42.96  ? 371 VAL B C     1 
ATOM   7381 O O     . VAL B 1 373 ? 0.464   -60.714 48.946  1.00 41.18  ? 371 VAL B O     1 
ATOM   7382 C CB    . VAL B 1 373 ? 0.061   -60.138 45.699  1.00 36.66  ? 371 VAL B CB    1 
ATOM   7383 C CG1   . VAL B 1 373 ? 0.494   -58.811 46.309  1.00 38.73  ? 371 VAL B CG1   1 
ATOM   7384 C CG2   . VAL B 1 373 ? 0.824   -60.401 44.419  1.00 39.05  ? 371 VAL B CG2   1 
ATOM   7385 N N     . ASP B 1 374 ? -1.667  -61.099 48.257  1.00 46.00  ? 372 ASP B N     1 
ATOM   7386 C CA    . ASP B 1 374 ? -2.359  -60.887 49.566  1.00 51.08  ? 372 ASP B CA    1 
ATOM   7387 C C     . ASP B 1 374 ? -1.820  -61.864 50.627  1.00 45.87  ? 372 ASP B C     1 
ATOM   7388 O O     . ASP B 1 374 ? -1.493  -61.425 51.712  1.00 49.44  ? 372 ASP B O     1 
ATOM   7389 C CB    . ASP B 1 374 ? -3.867  -61.132 49.450  1.00 50.87  ? 372 ASP B CB    1 
ATOM   7390 C CG    . ASP B 1 374 ? -4.662  -60.032 48.774  1.00 51.35  ? 372 ASP B CG    1 
ATOM   7391 O OD1   . ASP B 1 374 ? -4.179  -58.859 48.769  1.00 51.70  ? 372 ASP B OD1   1 
ATOM   7392 O OD2   . ASP B 1 374 ? -5.792  -60.353 48.320  1.00 46.58  ? 372 ASP B OD2   1 
ATOM   7393 N N     . ILE B 1 375 ? -1.798  -63.154 50.306  1.00 46.73  ? 373 ILE B N     1 
ATOM   7394 C CA    . ILE B 1 375 ? -1.263  -64.262 51.149  1.00 50.68  ? 373 ILE B CA    1 
ATOM   7395 C C     . ILE B 1 375 ? 0.174   -63.939 51.594  1.00 53.94  ? 373 ILE B C     1 
ATOM   7396 O O     . ILE B 1 375 ? 0.431   -63.919 52.816  1.00 61.88  ? 373 ILE B O     1 
ATOM   7397 C CB    . ILE B 1 375 ? -1.363  -65.587 50.373  1.00 48.53  ? 373 ILE B CB    1 
ATOM   7398 C CG1   . ILE B 1 375 ? -2.824  -66.032 50.226  1.00 45.52  ? 373 ILE B CG1   1 
ATOM   7399 C CG2   . ILE B 1 375 ? -0.493  -66.655 51.017  1.00 49.75  ? 373 ILE B CG2   1 
ATOM   7400 C CD1   . ILE B 1 375 ? -2.999  -67.332 49.448  1.00 43.26  ? 373 ILE B CD1   1 
ATOM   7401 N N     . VAL B 1 376 ? 1.079   -63.657 50.660  1.00 50.07  ? 374 VAL B N     1 
ATOM   7402 C CA    . VAL B 1 376 ? 2.504   -63.326 50.976  1.00 47.49  ? 374 VAL B CA    1 
ATOM   7403 C C     . VAL B 1 376 ? 2.567   -62.116 51.910  1.00 48.46  ? 374 VAL B C     1 
ATOM   7404 O O     . VAL B 1 376 ? 3.423   -62.141 52.815  1.00 49.90  ? 374 VAL B O     1 
ATOM   7405 C CB    . VAL B 1 376 ? 3.343   -63.104 49.706  1.00 44.18  ? 374 VAL B CB    1 
ATOM   7406 C CG1   . VAL B 1 376 ? 4.708   -62.495 50.005  1.00 41.64  ? 374 VAL B CG1   1 
ATOM   7407 C CG2   . VAL B 1 376 ? 3.482   -64.406 48.917  1.00 43.55  ? 374 VAL B CG2   1 
ATOM   7408 N N     . GLN B 1 377 ? 1.693   -61.124 51.742  1.00 47.49  ? 375 GLN B N     1 
ATOM   7409 C CA    . GLN B 1 377 ? 1.716   -59.897 52.589  1.00 56.03  ? 375 GLN B CA    1 
ATOM   7410 C C     . GLN B 1 377 ? 1.076   -60.110 53.974  1.00 51.80  ? 375 GLN B C     1 
ATOM   7411 O O     . GLN B 1 377 ? 1.427   -59.311 54.848  1.00 45.03  ? 375 GLN B O     1 
ATOM   7412 C CB    . GLN B 1 377 ? 1.071   -58.707 51.882  1.00 57.58  ? 375 GLN B CB    1 
ATOM   7413 C CG    . GLN B 1 377 ? 2.058   -57.984 50.979  1.00 69.94  ? 375 GLN B CG    1 
ATOM   7414 C CD    . GLN B 1 377 ? 1.360   -57.079 49.993  1.00 85.20  ? 375 GLN B CD    1 
ATOM   7415 O OE1   . GLN B 1 377 ? 0.303   -56.517 50.277  1.00 97.71  ? 375 GLN B OE1   1 
ATOM   7416 N NE2   . GLN B 1 377 ? 1.947   -56.933 48.815  1.00 88.59  ? 375 GLN B NE2   1 
ATOM   7417 N N     . ARG B 1 378 ? 0.216   -61.120 54.189  1.00 53.61  ? 376 ARG B N     1 
ATOM   7418 C CA    . ARG B 1 378 ? -0.706  -61.157 55.364  1.00 52.73  ? 376 ARG B CA    1 
ATOM   7419 C C     . ARG B 1 378 ? -0.892  -62.534 56.016  1.00 54.14  ? 376 ARG B C     1 
ATOM   7420 O O     . ARG B 1 378 ? -1.356  -62.544 57.153  1.00 53.99  ? 376 ARG B O     1 
ATOM   7421 C CB    . ARG B 1 378 ? -2.098  -60.690 54.956  1.00 54.66  ? 376 ARG B CB    1 
ATOM   7422 C CG    . ARG B 1 378 ? -2.196  -59.190 54.788  1.00 57.94  ? 376 ARG B CG    1 
ATOM   7423 C CD    . ARG B 1 378 ? -3.485  -58.870 54.076  1.00 56.44  ? 376 ARG B CD    1 
ATOM   7424 N NE    . ARG B 1 378 ? -3.583  -57.436 53.934  1.00 60.17  ? 376 ARG B NE    1 
ATOM   7425 C CZ    . ARG B 1 378 ? -4.601  -56.693 54.346  1.00 61.14  ? 376 ARG B CZ    1 
ATOM   7426 N NH1   . ARG B 1 378 ? -5.656  -57.246 54.912  1.00 68.59  ? 376 ARG B NH1   1 
ATOM   7427 N NH2   . ARG B 1 378 ? -4.585  -55.389 54.141  1.00 60.89  ? 376 ARG B NH2   1 
ATOM   7428 N N     . SER B 1 379 ? -0.653  -63.656 55.345  1.00 55.61  ? 377 SER B N     1 
ATOM   7429 C CA    . SER B 1 379 ? -0.851  -64.985 55.975  1.00 56.15  ? 377 SER B CA    1 
ATOM   7430 C C     . SER B 1 379 ? 0.130   -65.139 57.137  1.00 62.01  ? 377 SER B C     1 
ATOM   7431 O O     . SER B 1 379 ? 1.178   -64.462 57.122  1.00 61.75  ? 377 SER B O     1 
ATOM   7432 C CB    . SER B 1 379 ? -0.705  -66.118 55.011  1.00 57.06  ? 377 SER B CB    1 
ATOM   7433 O OG    . SER B 1 379 ? -1.316  -67.285 55.536  1.00 54.05  ? 377 SER B OG    1 
ATOM   7434 N N     . GLN B 1 380 ? -0.236  -65.991 58.099  1.00 69.70  ? 378 GLN B N     1 
ATOM   7435 C CA    . GLN B 1 380 ? 0.564   -66.385 59.286  1.00 70.75  ? 378 GLN B CA    1 
ATOM   7436 C C     . GLN B 1 380 ? 1.200   -67.748 59.024  1.00 67.03  ? 378 GLN B C     1 
ATOM   7437 O O     . GLN B 1 380 ? 2.315   -67.993 59.512  1.00 70.10  ? 378 GLN B O     1 
ATOM   7438 C CB    . GLN B 1 380 ? -0.339  -66.469 60.517  1.00 73.30  ? 378 GLN B CB    1 
ATOM   7439 C CG    . GLN B 1 380 ? -1.130  -65.196 60.772  1.00 76.09  ? 378 GLN B CG    1 
ATOM   7440 C CD    . GLN B 1 380 ? -0.255  -64.043 61.205  1.00 83.25  ? 378 GLN B CD    1 
ATOM   7441 O OE1   . GLN B 1 380 ? 0.935   -63.965 60.880  1.00 76.04  ? 378 GLN B OE1   1 
ATOM   7442 N NE2   . GLN B 1 380 ? -0.847  -63.127 61.962  1.00 83.12  ? 378 GLN B NE2   1 
ATOM   7443 N N     . ASP B 1 381 ? 0.500   -68.590 58.269  1.00 62.25  ? 379 ASP B N     1 
ATOM   7444 C CA    . ASP B 1 381 ? 0.930   -69.966 57.907  1.00 65.75  ? 379 ASP B CA    1 
ATOM   7445 C C     . ASP B 1 381 ? 2.103   -69.875 56.910  1.00 73.27  ? 379 ASP B C     1 
ATOM   7446 O O     . ASP B 1 381 ? 1.901   -69.305 55.824  1.00 77.12  ? 379 ASP B O     1 
ATOM   7447 C CB    . ASP B 1 381 ? -0.297  -70.742 57.414  1.00 58.14  ? 379 ASP B CB    1 
ATOM   7448 C CG    . ASP B 1 381 ? 0.010   -72.144 56.945  1.00 60.64  ? 379 ASP B CG    1 
ATOM   7449 O OD1   . ASP B 1 381 ? 1.212   -72.447 56.813  1.00 61.63  ? 379 ASP B OD1   1 
ATOM   7450 O OD2   . ASP B 1 381 ? -0.950  -72.905 56.697  1.00 57.63  ? 379 ASP B OD2   1 
ATOM   7451 N N     . GLU B 1 382 ? 3.287   -70.396 57.269  1.00 79.12  ? 380 GLU B N     1 
ATOM   7452 C CA    . GLU B 1 382 ? 4.542   -70.309 56.460  1.00 73.61  ? 380 GLU B CA    1 
ATOM   7453 C C     . GLU B 1 382 ? 4.479   -71.304 55.293  1.00 68.34  ? 380 GLU B C     1 
ATOM   7454 O O     . GLU B 1 382 ? 5.144   -71.060 54.289  1.00 68.51  ? 380 GLU B O     1 
ATOM   7455 C CB    . GLU B 1 382 ? 5.796   -70.573 57.303  1.00 76.84  ? 380 GLU B CB    1 
ATOM   7456 C CG    . GLU B 1 382 ? 5.906   -69.721 58.563  1.00 84.03  ? 380 GLU B CG    1 
ATOM   7457 C CD    . GLU B 1 382 ? 5.930   -68.207 58.395  1.00 90.81  ? 380 GLU B CD    1 
ATOM   7458 O OE1   . GLU B 1 382 ? 4.938   -67.546 58.788  1.00 100.64 ? 380 GLU B OE1   1 
ATOM   7459 O OE2   . GLU B 1 382 ? 6.952   -67.679 57.912  1.00 85.41  ? 380 GLU B OE2   1 
ATOM   7460 N N     . GLU B 1 383 ? 3.712   -72.387 55.425  1.00 67.19  ? 381 GLU B N     1 
ATOM   7461 C CA    . GLU B 1 383 ? 3.417   -73.336 54.313  1.00 76.32  ? 381 GLU B CA    1 
ATOM   7462 C C     . GLU B 1 383 ? 2.658   -72.588 53.216  1.00 75.10  ? 381 GLU B C     1 
ATOM   7463 O O     . GLU B 1 383 ? 2.961   -72.791 52.026  1.00 72.52  ? 381 GLU B O     1 
ATOM   7464 C CB    . GLU B 1 383 ? 2.542   -74.520 54.750  1.00 80.98  ? 381 GLU B CB    1 
ATOM   7465 C CG    . GLU B 1 383 ? 3.000   -75.225 56.020  1.00 92.65  ? 381 GLU B CG    1 
ATOM   7466 C CD    . GLU B 1 383 ? 4.497   -75.475 56.130  1.00 92.82  ? 381 GLU B CD    1 
ATOM   7467 O OE1   . GLU B 1 383 ? 5.073   -75.205 57.215  1.00 94.33  ? 381 GLU B OE1   1 
ATOM   7468 O OE2   . GLU B 1 383 ? 5.084   -75.935 55.134  1.00 81.85  ? 381 GLU B OE2   1 
ATOM   7469 N N     . GLN B 1 384 ? 1.682   -71.784 53.634  1.00 76.87  ? 382 GLN B N     1 
ATOM   7470 C CA    . GLN B 1 384 ? 0.755   -71.039 52.754  1.00 70.37  ? 382 GLN B CA    1 
ATOM   7471 C C     . GLN B 1 384 ? 1.479   -69.822 52.151  1.00 65.76  ? 382 GLN B C     1 
ATOM   7472 O O     . GLN B 1 384 ? 1.249   -69.569 50.974  1.00 66.91  ? 382 GLN B O     1 
ATOM   7473 C CB    . GLN B 1 384 ? -0.486  -70.647 53.544  1.00 69.52  ? 382 GLN B CB    1 
ATOM   7474 C CG    . GLN B 1 384 ? -1.750  -70.696 52.709  1.00 80.35  ? 382 GLN B CG    1 
ATOM   7475 C CD    . GLN B 1 384 ? -2.829  -69.804 53.268  1.00 83.81  ? 382 GLN B CD    1 
ATOM   7476 O OE1   . GLN B 1 384 ? -2.679  -69.206 54.333  1.00 88.93  ? 382 GLN B OE1   1 
ATOM   7477 N NE2   . GLN B 1 384 ? -3.931  -69.709 52.543  1.00 77.76  ? 382 GLN B NE2   1 
ATOM   7478 N N     . LYS B 1 385 ? 2.329   -69.104 52.900  1.00 60.49  ? 383 LYS B N     1 
ATOM   7479 C CA    . LYS B 1 385 ? 3.145   -67.982 52.352  1.00 60.01  ? 383 LYS B CA    1 
ATOM   7480 C C     . LYS B 1 385 ? 4.106   -68.549 51.309  1.00 64.20  ? 383 LYS B C     1 
ATOM   7481 O O     . LYS B 1 385 ? 4.258   -67.920 50.252  1.00 61.09  ? 383 LYS B O     1 
ATOM   7482 C CB    . LYS B 1 385 ? 4.017   -67.249 53.377  1.00 57.03  ? 383 LYS B CB    1 
ATOM   7483 C CG    . LYS B 1 385 ? 3.312   -66.312 54.343  1.00 64.10  ? 383 LYS B CG    1 
ATOM   7484 C CD    . LYS B 1 385 ? 4.234   -65.787 55.449  1.00 72.06  ? 383 LYS B CD    1 
ATOM   7485 C CE    . LYS B 1 385 ? 4.575   -64.315 55.322  1.00 82.32  ? 383 LYS B CE    1 
ATOM   7486 N NZ    . LYS B 1 385 ? 3.393   -63.452 55.609  1.00 83.52  ? 383 LYS B NZ    1 
ATOM   7487 N N     . LYS B 1 386 ? 4.754   -69.678 51.610  1.00 66.60  ? 384 LYS B N     1 
ATOM   7488 C CA    . LYS B 1 386 ? 5.864   -70.193 50.771  1.00 61.85  ? 384 LYS B CA    1 
ATOM   7489 C C     . LYS B 1 386 ? 5.288   -70.734 49.460  1.00 54.07  ? 384 LYS B C     1 
ATOM   7490 O O     . LYS B 1 386 ? 5.943   -70.566 48.428  1.00 54.83  ? 384 LYS B O     1 
ATOM   7491 C CB    . LYS B 1 386 ? 6.696   -71.254 51.496  1.00 66.40  ? 384 LYS B CB    1 
ATOM   7492 C CG    . LYS B 1 386 ? 8.201   -71.053 51.352  1.00 77.42  ? 384 LYS B CG    1 
ATOM   7493 C CD    . LYS B 1 386 ? 9.016   -72.308 51.601  1.00 80.16  ? 384 LYS B CD    1 
ATOM   7494 C CE    . LYS B 1 386 ? 8.988   -73.262 50.425  1.00 74.80  ? 384 LYS B CE    1 
ATOM   7495 N NZ    . LYS B 1 386 ? 9.138   -74.665 50.872  1.00 72.41  ? 384 LYS B NZ    1 
ATOM   7496 N N     . ALA B 1 387 ? 4.113   -71.356 49.492  1.00 46.80  ? 385 ALA B N     1 
ATOM   7497 C CA    . ALA B 1 387 ? 3.433   -71.862 48.274  1.00 50.61  ? 385 ALA B CA    1 
ATOM   7498 C C     . ALA B 1 387 ? 2.906   -70.682 47.424  1.00 52.20  ? 385 ALA B C     1 
ATOM   7499 O O     . ALA B 1 387 ? 2.918   -70.793 46.175  1.00 48.06  ? 385 ALA B O     1 
ATOM   7500 C CB    . ALA B 1 387 ? 2.327   -72.818 48.633  1.00 45.96  ? 385 ALA B CB    1 
ATOM   7501 N N     . ALA B 1 388 ? 2.447   -69.603 48.072  1.00 47.98  ? 386 ALA B N     1 
ATOM   7502 C CA    . ALA B 1 388 ? 2.005   -68.353 47.424  1.00 47.92  ? 386 ALA B CA    1 
ATOM   7503 C C     . ALA B 1 388 ? 3.219   -67.678 46.784  1.00 48.46  ? 386 ALA B C     1 
ATOM   7504 O O     . ALA B 1 388 ? 3.071   -67.178 45.658  1.00 45.30  ? 386 ALA B O     1 
ATOM   7505 C CB    . ALA B 1 388 ? 1.330   -67.437 48.408  1.00 44.94  ? 386 ALA B CB    1 
ATOM   7506 N N     . ASP B 1 389 ? 4.364   -67.693 47.473  1.00 47.48  ? 387 ASP B N     1 
ATOM   7507 C CA    . ASP B 1 389 ? 5.599   -66.986 47.045  1.00 49.61  ? 387 ASP B CA    1 
ATOM   7508 C C     . ASP B 1 389 ? 6.208   -67.668 45.815  1.00 50.29  ? 387 ASP B C     1 
ATOM   7509 O O     . ASP B 1 389 ? 6.695   -66.966 44.908  1.00 52.53  ? 387 ASP B O     1 
ATOM   7510 C CB    . ASP B 1 389 ? 6.629   -66.920 48.161  1.00 50.52  ? 387 ASP B CB    1 
ATOM   7511 C CG    . ASP B 1 389 ? 7.713   -65.941 47.797  1.00 54.80  ? 387 ASP B CG    1 
ATOM   7512 O OD1   . ASP B 1 389 ? 7.477   -64.722 47.963  1.00 60.73  ? 387 ASP B OD1   1 
ATOM   7513 O OD2   . ASP B 1 389 ? 8.741   -66.405 47.265  1.00 65.03  ? 387 ASP B OD2   1 
ATOM   7514 N N     . SER B 1 390 ? 6.195   -68.990 45.786  1.00 47.22  ? 388 SER B N     1 
ATOM   7515 C CA    . SER B 1 390 ? 6.678   -69.784 44.641  1.00 48.12  ? 388 SER B CA    1 
ATOM   7516 C C     . SER B 1 390 ? 5.717   -69.624 43.446  1.00 53.25  ? 388 SER B C     1 
ATOM   7517 O O     . SER B 1 390 ? 6.196   -69.725 42.287  1.00 58.04  ? 388 SER B O     1 
ATOM   7518 C CB    . SER B 1 390 ? 6.814   -71.210 45.058  1.00 51.19  ? 388 SER B CB    1 
ATOM   7519 O OG    . SER B 1 390 ? 5.546   -71.833 44.972  1.00 58.11  ? 388 SER B OG    1 
ATOM   7520 N N     . MET B 1 391 ? 4.407   -69.460 43.698  1.00 51.88  ? 389 MET B N     1 
ATOM   7521 C CA    . MET B 1 391 ? 3.383   -69.257 42.635  1.00 50.64  ? 389 MET B CA    1 
ATOM   7522 C C     . MET B 1 391 ? 3.573   -67.872 41.992  1.00 47.62  ? 389 MET B C     1 
ATOM   7523 O O     . MET B 1 391 ? 3.604   -67.798 40.759  1.00 45.34  ? 389 MET B O     1 
ATOM   7524 C CB    . MET B 1 391 ? 1.962   -69.361 43.189  1.00 51.13  ? 389 MET B CB    1 
ATOM   7525 C CG    . MET B 1 391 ? 0.875   -69.268 42.106  1.00 55.17  ? 389 MET B CG    1 
ATOM   7526 S SD    . MET B 1 391 ? 0.902   -70.652 40.918  1.00 52.59  ? 389 MET B SD    1 
ATOM   7527 C CE    . MET B 1 391 ? 0.380   -72.012 41.966  1.00 49.44  ? 389 MET B CE    1 
ATOM   7528 N N     . LEU B 1 392 ? 3.696   -66.815 42.795  1.00 42.99  ? 390 LEU B N     1 
ATOM   7529 C CA    . LEU B 1 392 ? 4.026   -65.449 42.320  1.00 45.96  ? 390 LEU B CA    1 
ATOM   7530 C C     . LEU B 1 392 ? 5.286   -65.464 41.462  1.00 47.35  ? 390 LEU B C     1 
ATOM   7531 O O     . LEU B 1 392 ? 5.284   -64.757 40.444  1.00 49.70  ? 390 LEU B O     1 
ATOM   7532 C CB    . LEU B 1 392 ? 4.233   -64.492 43.490  1.00 52.44  ? 390 LEU B CB    1 
ATOM   7533 C CG    . LEU B 1 392 ? 2.954   -63.930 44.084  1.00 60.67  ? 390 LEU B CG    1 
ATOM   7534 C CD1   . LEU B 1 392 ? 3.281   -62.931 45.174  1.00 64.75  ? 390 LEU B CD1   1 
ATOM   7535 C CD2   . LEU B 1 392 ? 2.087   -63.298 43.004  1.00 63.77  ? 390 LEU B CD2   1 
ATOM   7536 N N     . ALA B 1 393 ? 6.324   -66.196 41.866  1.00 44.25  ? 391 ALA B N     1 
ATOM   7537 C CA    . ALA B 1 393 ? 7.635   -66.201 41.180  1.00 44.16  ? 391 ALA B CA    1 
ATOM   7538 C C     . ALA B 1 393 ? 7.492   -66.891 39.816  1.00 47.01  ? 391 ALA B C     1 
ATOM   7539 O O     . ALA B 1 393 ? 8.184   -66.497 38.875  1.00 53.85  ? 391 ALA B O     1 
ATOM   7540 C CB    . ALA B 1 393 ? 8.676   -66.863 42.043  1.00 47.20  ? 391 ALA B CB    1 
ATOM   7541 N N     . PHE B 1 394 ? 6.602   -67.873 39.701  1.00 42.54  ? 392 PHE B N     1 
ATOM   7542 C CA    . PHE B 1 394 ? 6.278   -68.524 38.415  1.00 38.77  ? 392 PHE B CA    1 
ATOM   7543 C C     . PHE B 1 394 ? 5.383   -67.605 37.546  1.00 41.43  ? 392 PHE B C     1 
ATOM   7544 O O     . PHE B 1 394 ? 5.643   -67.480 36.342  1.00 45.35  ? 392 PHE B O     1 
ATOM   7545 C CB    . PHE B 1 394 ? 5.642   -69.880 38.692  1.00 38.25  ? 392 PHE B CB    1 
ATOM   7546 C CG    . PHE B 1 394 ? 5.156   -70.577 37.450  1.00 43.78  ? 392 PHE B CG    1 
ATOM   7547 C CD1   . PHE B 1 394 ? 6.060   -71.133 36.555  1.00 43.22  ? 392 PHE B CD1   1 
ATOM   7548 C CD2   . PHE B 1 394 ? 3.801   -70.644 37.158  1.00 42.38  ? 392 PHE B CD2   1 
ATOM   7549 C CE1   . PHE B 1 394 ? 5.617   -71.765 35.409  1.00 44.59  ? 392 PHE B CE1   1 
ATOM   7550 C CE2   . PHE B 1 394 ? 3.363   -71.301 36.021  1.00 41.53  ? 392 PHE B CE2   1 
ATOM   7551 C CZ    . PHE B 1 394 ? 4.271   -71.844 35.143  1.00 45.60  ? 392 PHE B CZ    1 
ATOM   7552 N N     . LEU B 1 395 ? 4.348   -66.973 38.110  1.00 39.99  ? 393 LEU B N     1 
ATOM   7553 C CA    . LEU B 1 395 ? 3.304   -66.276 37.314  1.00 40.38  ? 393 LEU B CA    1 
ATOM   7554 C C     . LEU B 1 395 ? 3.738   -64.844 36.955  1.00 41.86  ? 393 LEU B C     1 
ATOM   7555 O O     . LEU B 1 395 ? 3.287   -64.331 35.898  1.00 41.65  ? 393 LEU B O     1 
ATOM   7556 C CB    . LEU B 1 395 ? 1.985   -66.273 38.083  1.00 41.88  ? 393 LEU B CB    1 
ATOM   7557 C CG    . LEU B 1 395 ? 1.197   -67.577 38.081  1.00 41.47  ? 393 LEU B CG    1 
ATOM   7558 C CD1   . LEU B 1 395 ? -0.142  -67.342 38.754  1.00 42.82  ? 393 LEU B CD1   1 
ATOM   7559 C CD2   . LEU B 1 395 ? 1.004   -68.127 36.669  1.00 39.89  ? 393 LEU B CD2   1 
ATOM   7560 N N     . THR B 1 396 ? 4.575   -64.208 37.767  1.00 33.19  ? 394 THR B N     1 
ATOM   7561 C CA    . THR B 1 396 ? 4.959   -62.785 37.587  1.00 35.16  ? 394 THR B CA    1 
ATOM   7562 C C     . THR B 1 396 ? 5.551   -62.550 36.201  1.00 38.42  ? 394 THR B C     1 
ATOM   7563 O O     . THR B 1 396 ? 5.104   -61.626 35.522  1.00 42.06  ? 394 THR B O     1 
ATOM   7564 C CB    . THR B 1 396 ? 5.914   -62.320 38.696  1.00 38.72  ? 394 THR B CB    1 
ATOM   7565 O OG1   . THR B 1 396 ? 5.042   -62.213 39.820  1.00 41.45  ? 394 THR B OG1   1 
ATOM   7566 C CG2   . THR B 1 396 ? 6.629   -61.012 38.425  1.00 41.29  ? 394 THR B CG2   1 
ATOM   7567 N N     . PRO B 1 397 ? 6.636   -63.252 35.789  1.00 39.66  ? 395 PRO B N     1 
ATOM   7568 C CA    . PRO B 1 397 ? 7.199   -63.064 34.453  1.00 38.44  ? 395 PRO B CA    1 
ATOM   7569 C C     . PRO B 1 397 ? 6.247   -63.492 33.317  1.00 40.30  ? 395 PRO B C     1 
ATOM   7570 O O     . PRO B 1 397 ? 6.286   -62.892 32.226  1.00 35.54  ? 395 PRO B O     1 
ATOM   7571 C CB    . PRO B 1 397 ? 8.451   -63.956 34.458  1.00 43.73  ? 395 PRO B CB    1 
ATOM   7572 C CG    . PRO B 1 397 ? 8.199   -64.966 35.562  1.00 40.42  ? 395 PRO B CG    1 
ATOM   7573 C CD    . PRO B 1 397 ? 7.433   -64.190 36.606  1.00 40.15  ? 395 PRO B CD    1 
ATOM   7574 N N     . ILE B 1 398 ? 5.438   -64.529 33.540  1.00 36.42  ? 396 ILE B N     1 
ATOM   7575 C CA    . ILE B 1 398 ? 4.472   -65.000 32.505  1.00 37.74  ? 396 ILE B CA    1 
ATOM   7576 C C     . ILE B 1 398 ? 3.487   -63.847 32.275  1.00 39.17  ? 396 ILE B C     1 
ATOM   7577 O O     . ILE B 1 398 ? 3.295   -63.439 31.115  1.00 38.28  ? 396 ILE B O     1 
ATOM   7578 C CB    . ILE B 1 398 ? 3.756   -66.297 32.929  1.00 38.59  ? 396 ILE B CB    1 
ATOM   7579 C CG1   . ILE B 1 398 ? 4.675   -67.519 32.835  1.00 39.61  ? 396 ILE B CG1   1 
ATOM   7580 C CG2   . ILE B 1 398 ? 2.481   -66.476 32.130  1.00 38.04  ? 396 ILE B CG2   1 
ATOM   7581 C CD1   . ILE B 1 398 ? 4.103   -68.766 33.491  1.00 38.42  ? 396 ILE B CD1   1 
ATOM   7582 N N     . ALA B 1 399 ? 2.914   -63.323 33.357  1.00 36.15  ? 397 ALA B N     1 
ATOM   7583 C CA    . ALA B 1 399 ? 1.891   -62.270 33.309  1.00 35.60  ? 397 ALA B CA    1 
ATOM   7584 C C     . ALA B 1 399 ? 2.509   -61.061 32.607  1.00 38.04  ? 397 ALA B C     1 
ATOM   7585 O O     . ALA B 1 399 ? 1.924   -60.612 31.586  1.00 41.46  ? 397 ALA B O     1 
ATOM   7586 C CB    . ALA B 1 399 ? 1.388   -61.952 34.681  1.00 36.20  ? 397 ALA B CB    1 
ATOM   7587 N N     . LYS B 1 400 ? 3.681   -60.606 33.055  1.00 32.64  ? 398 LYS B N     1 
ATOM   7588 C CA    . LYS B 1 400 ? 4.286   -59.381 32.482  1.00 34.90  ? 398 LYS B CA    1 
ATOM   7589 C C     . LYS B 1 400 ? 4.487   -59.558 30.959  1.00 32.83  ? 398 LYS B C     1 
ATOM   7590 O O     . LYS B 1 400 ? 3.891   -58.804 30.204  1.00 27.23  ? 398 LYS B O     1 
ATOM   7591 C CB    . LYS B 1 400 ? 5.562   -59.014 33.231  1.00 36.29  ? 398 LYS B CB    1 
ATOM   7592 C CG    . LYS B 1 400 ? 6.059   -57.604 32.963  1.00 36.78  ? 398 LYS B CG    1 
ATOM   7593 C CD    . LYS B 1 400 ? 6.868   -57.499 31.688  1.00 37.74  ? 398 LYS B CD    1 
ATOM   7594 C CE    . LYS B 1 400 ? 7.048   -56.060 31.246  1.00 38.51  ? 398 LYS B CE    1 
ATOM   7595 N NZ    . LYS B 1 400 ? 7.923   -55.938 30.060  1.00 39.46  ? 398 LYS B NZ    1 
ATOM   7596 N N     . ALA B 1 401 ? 5.274   -60.528 30.504  1.00 34.54  ? 399 ALA B N     1 
ATOM   7597 C CA    . ALA B 1 401 ? 5.636   -60.666 29.071  1.00 34.67  ? 399 ALA B CA    1 
ATOM   7598 C C     . ALA B 1 401 ? 4.414   -61.069 28.236  1.00 35.10  ? 399 ALA B C     1 
ATOM   7599 O O     . ALA B 1 401 ? 4.229   -60.480 27.125  1.00 31.96  ? 399 ALA B O     1 
ATOM   7600 C CB    . ALA B 1 401 ? 6.743   -61.660 28.880  1.00 32.87  ? 399 ALA B CB    1 
ATOM   7601 N N     . PHE B 1 402 ? 3.645   -62.065 28.680  1.00 31.56  ? 400 PHE B N     1 
ATOM   7602 C CA    . PHE B 1 402 ? 2.524   -62.618 27.874  1.00 29.24  ? 400 PHE B CA    1 
ATOM   7603 C C     . PHE B 1 402 ? 1.374   -61.607 27.780  1.00 31.02  ? 400 PHE B C     1 
ATOM   7604 O O     . PHE B 1 402 ? 0.775   -61.427 26.704  1.00 31.37  ? 400 PHE B O     1 
ATOM   7605 C CB    . PHE B 1 402 ? 2.040   -63.937 28.456  1.00 29.51  ? 400 PHE B CB    1 
ATOM   7606 C CG    . PHE B 1 402 ? 0.869   -64.563 27.756  1.00 30.59  ? 400 PHE B CG    1 
ATOM   7607 C CD1   . PHE B 1 402 ? 1.058   -65.324 26.617  1.00 33.60  ? 400 PHE B CD1   1 
ATOM   7608 C CD2   . PHE B 1 402 ? -0.416  -64.391 28.233  1.00 32.92  ? 400 PHE B CD2   1 
ATOM   7609 C CE1   . PHE B 1 402 ? -0.014  -65.917 25.984  1.00 30.98  ? 400 PHE B CE1   1 
ATOM   7610 C CE2   . PHE B 1 402 ? -1.491  -64.973 27.585  1.00 31.76  ? 400 PHE B CE2   1 
ATOM   7611 C CZ    . PHE B 1 402 ? -1.284  -65.749 26.479  1.00 31.62  ? 400 PHE B CZ    1 
ATOM   7612 N N     . MET B 1 403 ? 1.002   -60.972 28.875  1.00 31.80  ? 401 MET B N     1 
ATOM   7613 C CA    . MET B 1 403 ? -0.168  -60.060 28.804  1.00 32.59  ? 401 MET B CA    1 
ATOM   7614 C C     . MET B 1 403 ? 0.171   -58.829 27.938  1.00 34.28  ? 401 MET B C     1 
ATOM   7615 O O     . MET B 1 403 ? -0.768  -58.342 27.216  1.00 32.08  ? 401 MET B O     1 
ATOM   7616 C CB    . MET B 1 403 ? -0.656  -59.631 30.187  1.00 31.89  ? 401 MET B CB    1 
ATOM   7617 C CG    . MET B 1 403 ? -1.102  -60.778 31.058  1.00 32.58  ? 401 MET B CG    1 
ATOM   7618 S SD    . MET B 1 403 ? -1.980  -60.194 32.543  1.00 36.07  ? 401 MET B SD    1 
ATOM   7619 C CE    . MET B 1 403 ? -2.363  -61.768 33.310  1.00 36.81  ? 401 MET B CE    1 
ATOM   7620 N N     . THR B 1 404 ? 1.414   -58.313 27.984  1.00 31.21  ? 402 THR B N     1 
ATOM   7621 C CA    . THR B 1 404 ? 1.817   -57.128 27.177  1.00 30.55  ? 402 THR B CA    1 
ATOM   7622 C C     . THR B 1 404 ? 1.857   -57.538 25.696  1.00 33.22  ? 402 THR B C     1 
ATOM   7623 O O     . THR B 1 404 ? 1.188   -56.908 24.858  1.00 33.75  ? 402 THR B O     1 
ATOM   7624 C CB    . THR B 1 404 ? 3.107   -56.504 27.700  1.00 29.25  ? 402 THR B CB    1 
ATOM   7625 O OG1   . THR B 1 404 ? 4.113   -57.511 27.711  1.00 29.88  ? 402 THR B OG1   1 
ATOM   7626 C CG2   . THR B 1 404 ? 2.923   -55.932 29.086  1.00 30.00  ? 402 THR B CG2   1 
ATOM   7627 N N     . GLU B 1 405 ? 2.527   -58.636 25.390  1.00 31.37  ? 403 GLU B N     1 
ATOM   7628 C CA    . GLU B 1 405 ? 2.624   -59.134 24.009  1.00 29.12  ? 403 GLU B CA    1 
ATOM   7629 C C     . GLU B 1 405 ? 1.211   -59.279 23.423  1.00 31.03  ? 403 GLU B C     1 
ATOM   7630 O O     . GLU B 1 405 ? 0.981   -58.752 22.321  1.00 31.15  ? 403 GLU B O     1 
ATOM   7631 C CB    . GLU B 1 405 ? 3.396   -60.458 23.945  1.00 28.72  ? 403 GLU B CB    1 
ATOM   7632 C CG    . GLU B 1 405 ? 4.912   -60.320 24.106  1.00 29.88  ? 403 GLU B CG    1 
ATOM   7633 C CD    . GLU B 1 405 ? 5.680   -59.643 22.977  1.00 31.37  ? 403 GLU B CD    1 
ATOM   7634 O OE1   . GLU B 1 405 ? 6.781   -59.109 23.255  1.00 29.93  ? 403 GLU B OE1   1 
ATOM   7635 O OE2   . GLU B 1 405 ? 5.216   -59.703 21.814  1.00 33.09  ? 403 GLU B OE2   1 
ATOM   7636 N N     . VAL B 1 406 ? 0.292   -59.992 24.067  1.00 28.32  ? 404 VAL B N     1 
ATOM   7637 C CA    . VAL B 1 406 ? -1.044  -60.212 23.438  1.00 28.69  ? 404 VAL B CA    1 
ATOM   7638 C C     . VAL B 1 406 ? -1.918  -58.961 23.624  1.00 27.51  ? 404 VAL B C     1 
ATOM   7639 O O     . VAL B 1 406 ? -2.879  -58.804 22.878  1.00 26.74  ? 404 VAL B O     1 
ATOM   7640 C CB    . VAL B 1 406 ? -1.727  -61.482 23.964  1.00 28.85  ? 404 VAL B CB    1 
ATOM   7641 C CG1   . VAL B 1 406 ? -0.795  -62.698 23.830  1.00 29.27  ? 404 VAL B CG1   1 
ATOM   7642 C CG2   . VAL B 1 406 ? -2.215  -61.283 25.395  1.00 28.74  ? 404 VAL B CG2   1 
ATOM   7643 N N     . GLY B 1 407 ? -1.619  -58.111 24.597  1.00 30.90  ? 405 GLY B N     1 
ATOM   7644 C CA    . GLY B 1 407 ? -2.278  -56.792 24.738  1.00 31.27  ? 405 GLY B CA    1 
ATOM   7645 C C     . GLY B 1 407 ? -1.998  -55.926 23.511  1.00 31.05  ? 405 GLY B C     1 
ATOM   7646 O O     . GLY B 1 407 ? -2.927  -55.332 22.961  1.00 30.32  ? 405 GLY B O     1 
ATOM   7647 N N     . PHE B 1 408 ? -0.763  -55.928 23.039  1.00 28.24  ? 406 PHE B N     1 
ATOM   7648 C CA    . PHE B 1 408 ? -0.333  -55.156 21.852  1.00 29.97  ? 406 PHE B CA    1 
ATOM   7649 C C     . PHE B 1 408 ? -0.955  -55.756 20.588  1.00 28.44  ? 406 PHE B C     1 
ATOM   7650 O O     . PHE B 1 408 ? -1.410  -54.992 19.704  1.00 31.11  ? 406 PHE B O     1 
ATOM   7651 C CB    . PHE B 1 408 ? 1.190   -55.086 21.787  1.00 26.08  ? 406 PHE B CB    1 
ATOM   7652 C CG    . PHE B 1 408 ? 1.722   -54.414 20.560  1.00 24.81  ? 406 PHE B CG    1 
ATOM   7653 C CD1   . PHE B 1 408 ? 1.752   -53.031 20.479  1.00 24.04  ? 406 PHE B CD1   1 
ATOM   7654 C CD2   . PHE B 1 408 ? 2.199   -55.172 19.494  1.00 23.56  ? 406 PHE B CD2   1 
ATOM   7655 C CE1   . PHE B 1 408 ? 2.259   -52.399 19.345  1.00 25.82  ? 406 PHE B CE1   1 
ATOM   7656 C CE2   . PHE B 1 408 ? 2.720   -54.538 18.383  1.00 25.35  ? 406 PHE B CE2   1 
ATOM   7657 C CZ    . PHE B 1 408 ? 2.742   -53.152 18.307  1.00 24.97  ? 406 PHE B CZ    1 
ATOM   7658 N N     . GLU B 1 409 ? -0.970  -57.077 20.475  1.00 27.55  ? 407 GLU B N     1 
ATOM   7659 C CA    . GLU B 1 409 ? -1.733  -57.748 19.390  1.00 28.18  ? 407 GLU B CA    1 
ATOM   7660 C C     . GLU B 1 409 ? -3.201  -57.291 19.451  1.00 27.89  ? 407 GLU B C     1 
ATOM   7661 O O     . GLU B 1 409 ? -3.765  -56.955 18.380  1.00 25.94  ? 407 GLU B O     1 
ATOM   7662 C CB    . GLU B 1 409 ? -1.698  -59.276 19.504  1.00 29.81  ? 407 GLU B CB    1 
ATOM   7663 C CG    . GLU B 1 409 ? -2.430  -59.965 18.347  1.00 29.92  ? 407 GLU B CG    1 
ATOM   7664 C CD    . GLU B 1 409 ? -2.740  -61.437 18.569  1.00 34.60  ? 407 GLU B CD    1 
ATOM   7665 O OE1   . GLU B 1 409 ? -3.662  -61.950 17.906  1.00 32.86  ? 407 GLU B OE1   1 
ATOM   7666 O OE2   . GLU B 1 409 ? -2.074  -62.063 19.414  1.00 31.78  ? 407 GLU B OE2   1 
ATOM   7667 N N     . SER B 1 410 ? -3.782  -57.234 20.654  1.00 25.80  ? 408 SER B N     1 
ATOM   7668 C CA    . SER B 1 410 ? -5.227  -56.959 20.850  1.00 27.11  ? 408 SER B CA    1 
ATOM   7669 C C     . SER B 1 410 ? -5.495  -55.517 20.426  1.00 27.14  ? 408 SER B C     1 
ATOM   7670 O O     . SER B 1 410 ? -6.525  -55.268 19.804  1.00 27.06  ? 408 SER B O     1 
ATOM   7671 C CB    . SER B 1 410 ? -5.693  -57.239 22.274  1.00 24.68  ? 408 SER B CB    1 
ATOM   7672 O OG    . SER B 1 410 ? -5.714  -58.638 22.506  1.00 22.73  ? 408 SER B OG    1 
ATOM   7673 N N     . ALA B 1 411 ? -4.559  -54.619 20.724  1.00 26.46  ? 409 ALA B N     1 
ATOM   7674 C CA    . ALA B 1 411 ? -4.673  -53.183 20.407  1.00 26.66  ? 409 ALA B CA    1 
ATOM   7675 C C     . ALA B 1 411 ? -4.720  -53.038 18.882  1.00 26.75  ? 409 ALA B C     1 
ATOM   7676 O O     . ALA B 1 411 ? -5.506  -52.203 18.413  1.00 25.28  ? 409 ALA B O     1 
ATOM   7677 C CB    . ALA B 1 411 ? -3.532  -52.393 21.009  1.00 27.02  ? 409 ALA B CB    1 
ATOM   7678 N N     . ASN B 1 412 ? -3.912  -53.831 18.176  1.00 24.66  ? 410 ASN B N     1 
ATOM   7679 C CA    . ASN B 1 412 ? -3.828  -53.797 16.704  1.00 25.98  ? 410 ASN B CA    1 
ATOM   7680 C C     . ASN B 1 412 ? -5.120  -54.341 16.092  1.00 27.24  ? 410 ASN B C     1 
ATOM   7681 O O     . ASN B 1 412 ? -5.572  -53.715 15.091  1.00 28.40  ? 410 ASN B O     1 
ATOM   7682 C CB    . ASN B 1 412 ? -2.529  -54.413 16.225  1.00 22.61  ? 410 ASN B CB    1 
ATOM   7683 C CG    . ASN B 1 412 ? -1.423  -53.404 16.383  1.00 26.69  ? 410 ASN B CG    1 
ATOM   7684 O OD1   . ASN B 1 412 ? -1.418  -52.381 15.684  1.00 25.20  ? 410 ASN B OD1   1 
ATOM   7685 N ND2   . ASN B 1 412 ? -0.558  -53.631 17.371  1.00 27.99  ? 410 ASN B ND2   1 
ATOM   7686 N N     . HIS B 1 413 ? -5.747  -55.371 16.665  1.00 29.36  ? 411 HIS B N     1 
ATOM   7687 C CA    . HIS B 1 413 ? -7.080  -55.847 16.190  1.00 30.64  ? 411 HIS B CA    1 
ATOM   7688 C C     . HIS B 1 413 ? -8.079  -54.688 16.283  1.00 30.53  ? 411 HIS B C     1 
ATOM   7689 O O     . HIS B 1 413 ? -8.825  -54.495 15.327  1.00 31.57  ? 411 HIS B O     1 
ATOM   7690 C CB    . HIS B 1 413 ? -7.540  -57.054 17.006  1.00 30.68  ? 411 HIS B CB    1 
ATOM   7691 C CG    . HIS B 1 413 ? -6.751  -58.296 16.772  1.00 30.17  ? 411 HIS B CG    1 
ATOM   7692 N ND1   . HIS B 1 413 ? -6.521  -58.796 15.512  1.00 30.29  ? 411 HIS B ND1   1 
ATOM   7693 C CD2   . HIS B 1 413 ? -6.152  -59.144 17.631  1.00 26.48  ? 411 HIS B CD2   1 
ATOM   7694 C CE1   . HIS B 1 413 ? -5.806  -59.894 15.603  1.00 28.26  ? 411 HIS B CE1   1 
ATOM   7695 N NE2   . HIS B 1 413 ? -5.571  -60.128 16.889  1.00 28.04  ? 411 HIS B NE2   1 
ATOM   7696 N N     . GLY B 1 414 ? -8.122  -54.000 17.421  1.00 32.67  ? 412 GLY B N     1 
ATOM   7697 C CA    . GLY B 1 414 ? -8.926  -52.766 17.601  1.00 30.45  ? 412 GLY B CA    1 
ATOM   7698 C C     . GLY B 1 414 ? -8.808  -51.821 16.419  1.00 29.35  ? 412 GLY B C     1 
ATOM   7699 O O     . GLY B 1 414 ? -9.850  -51.443 15.832  1.00 28.48  ? 412 GLY B O     1 
ATOM   7700 N N     . VAL B 1 415 ? -7.583  -51.427 16.079  1.00 28.07  ? 413 VAL B N     1 
ATOM   7701 C CA    . VAL B 1 415 ? -7.309  -50.557 14.900  1.00 31.16  ? 413 VAL B CA    1 
ATOM   7702 C C     . VAL B 1 415 ? -7.867  -51.236 13.643  1.00 31.72  ? 413 VAL B C     1 
ATOM   7703 O O     . VAL B 1 415 ? -8.670  -50.577 12.929  1.00 30.28  ? 413 VAL B O     1 
ATOM   7704 C CB    . VAL B 1 415 ? -5.810  -50.234 14.782  1.00 32.10  ? 413 VAL B CB    1 
ATOM   7705 C CG1   . VAL B 1 415 ? -5.446  -49.661 13.424  1.00 32.14  ? 413 VAL B CG1   1 
ATOM   7706 C CG2   . VAL B 1 415 ? -5.360  -49.309 15.913  1.00 30.16  ? 413 VAL B CG2   1 
ATOM   7707 N N     . GLN B 1 416 ? -7.509  -52.499 13.373  1.00 30.64  ? 414 GLN B N     1 
ATOM   7708 C CA    . GLN B 1 416 ? -7.916  -53.222 12.128  1.00 29.50  ? 414 GLN B CA    1 
ATOM   7709 C C     . GLN B 1 416 ? -9.433  -53.185 11.926  1.00 28.09  ? 414 GLN B C     1 
ATOM   7710 O O     . GLN B 1 416 ? -9.857  -52.996 10.787  1.00 27.22  ? 414 GLN B O     1 
ATOM   7711 C CB    . GLN B 1 416 ? -7.414  -54.669 12.149  1.00 27.58  ? 414 GLN B CB    1 
ATOM   7712 C CG    . GLN B 1 416 ? -7.319  -55.307 10.774  1.00 24.38  ? 414 GLN B CG    1 
ATOM   7713 C CD    . GLN B 1 416 ? -6.259  -54.659 9.918   1.00 27.28  ? 414 GLN B CD    1 
ATOM   7714 O OE1   . GLN B 1 416 ? -5.293  -54.094 10.417  1.00 29.14  ? 414 GLN B OE1   1 
ATOM   7715 N NE2   . GLN B 1 416 ? -6.434  -54.743 8.612   1.00 26.46  ? 414 GLN B NE2   1 
ATOM   7716 N N     . ILE B 1 417 ? -10.191 -53.381 12.994  1.00 25.97  ? 415 ILE B N     1 
ATOM   7717 C CA    . ILE B 1 417 ? -11.682 -53.336 12.941  1.00 28.82  ? 415 ILE B CA    1 
ATOM   7718 C C     . ILE B 1 417 ? -12.170 -51.975 12.413  1.00 28.11  ? 415 ILE B C     1 
ATOM   7719 O O     . ILE B 1 417 ? -13.205 -51.964 11.714  1.00 26.81  ? 415 ILE B O     1 
ATOM   7720 C CB    . ILE B 1 417 ? -12.276 -53.695 14.319  1.00 27.88  ? 415 ILE B CB    1 
ATOM   7721 C CG1   . ILE B 1 417 ? -12.123 -55.205 14.542  1.00 30.88  ? 415 ILE B CG1   1 
ATOM   7722 C CG2   . ILE B 1 417 ? -13.734 -53.270 14.433  1.00 24.54  ? 415 ILE B CG2   1 
ATOM   7723 C CD1   . ILE B 1 417 ? -12.350 -55.696 15.957  1.00 31.74  ? 415 ILE B CD1   1 
ATOM   7724 N N     . PHE B 1 418 ? -11.460 -50.880 12.690  1.00 25.66  ? 416 PHE B N     1 
ATOM   7725 C CA    . PHE B 1 418 ? -11.845 -49.530 12.202  1.00 27.52  ? 416 PHE B CA    1 
ATOM   7726 C C     . PHE B 1 418 ? -11.385 -49.359 10.750  1.00 29.19  ? 416 PHE B C     1 
ATOM   7727 O O     . PHE B 1 418 ? -11.645 -48.321 10.187  1.00 30.36  ? 416 PHE B O     1 
ATOM   7728 C CB    . PHE B 1 418 ? -11.240 -48.411 13.064  1.00 27.68  ? 416 PHE B CB    1 
ATOM   7729 C CG    . PHE B 1 418 ? -11.923 -48.148 14.377  1.00 27.99  ? 416 PHE B CG    1 
ATOM   7730 C CD1   . PHE B 1 418 ? -11.910 -49.093 15.386  1.00 28.39  ? 416 PHE B CD1   1 
ATOM   7731 C CD2   . PHE B 1 418 ? -12.544 -46.935 14.628  1.00 31.48  ? 416 PHE B CD2   1 
ATOM   7732 C CE1   . PHE B 1 418 ? -12.521 -48.851 16.602  1.00 29.63  ? 416 PHE B CE1   1 
ATOM   7733 C CE2   . PHE B 1 418 ? -13.147 -46.684 15.857  1.00 28.61  ? 416 PHE B CE2   1 
ATOM   7734 C CZ    . PHE B 1 418 ? -13.169 -47.655 16.828  1.00 28.50  ? 416 PHE B CZ    1 
ATOM   7735 N N     . GLY B 1 419 ? -10.629 -50.300 10.185  1.00 28.51  ? 417 GLY B N     1 
ATOM   7736 C CA    . GLY B 1 419 ? -10.056 -50.110 8.844   1.00 27.36  ? 417 GLY B CA    1 
ATOM   7737 C C     . GLY B 1 419 ? -9.183  -48.875 8.809   1.00 27.72  ? 417 GLY B C     1 
ATOM   7738 O O     . GLY B 1 419 ? -8.527  -48.608 9.818   1.00 26.01  ? 417 GLY B O     1 
ATOM   7739 N N     . GLY B 1 420 ? -9.152  -48.164 7.674   1.00 27.93  ? 418 GLY B N     1 
ATOM   7740 C CA    . GLY B 1 420 ? -8.436  -46.883 7.514   1.00 27.88  ? 418 GLY B CA    1 
ATOM   7741 C C     . GLY B 1 420 ? -8.637  -45.945 8.694   1.00 27.93  ? 418 GLY B C     1 
ATOM   7742 O O     . GLY B 1 420 ? -7.659  -45.425 9.211   1.00 32.76  ? 418 GLY B O     1 
ATOM   7743 N N     . HIS B 1 421 ? -9.886  -45.705 9.060   1.00 30.92  ? 419 HIS B N     1 
ATOM   7744 C CA    . HIS B 1 421 ? -10.323 -44.850 10.194  1.00 31.40  ? 419 HIS B CA    1 
ATOM   7745 C C     . HIS B 1 421 ? -9.481  -45.136 11.458  1.00 32.97  ? 419 HIS B C     1 
ATOM   7746 O O     . HIS B 1 421 ? -9.229  -44.166 12.239  1.00 29.22  ? 419 HIS B O     1 
ATOM   7747 C CB    . HIS B 1 421 ? -11.839 -45.030 10.401  1.00 30.05  ? 419 HIS B CB    1 
ATOM   7748 C CG    . HIS B 1 421 ? -12.669 -44.369 9.343   1.00 35.63  ? 419 HIS B CG    1 
ATOM   7749 N ND1   . HIS B 1 421 ? -13.119 -45.043 8.217   1.00 40.56  ? 419 HIS B ND1   1 
ATOM   7750 C CD2   . HIS B 1 421 ? -13.138 -43.106 9.231   1.00 36.62  ? 419 HIS B CD2   1 
ATOM   7751 C CE1   . HIS B 1 421 ? -13.805 -44.211 7.455   1.00 39.55  ? 419 HIS B CE1   1 
ATOM   7752 N NE2   . HIS B 1 421 ? -13.799 -43.015 8.029   1.00 37.06  ? 419 HIS B NE2   1 
ATOM   7753 N N     . GLY B 1 422 ? -9.054  -46.388 11.684  1.00 30.58  ? 420 GLY B N     1 
ATOM   7754 C CA    . GLY B 1 422 ? -8.233  -46.744 12.866  1.00 31.56  ? 420 GLY B CA    1 
ATOM   7755 C C     . GLY B 1 422 ? -6.883  -46.013 12.909  1.00 31.81  ? 420 GLY B C     1 
ATOM   7756 O O     . GLY B 1 422 ? -6.276  -45.918 14.007  1.00 31.72  ? 420 GLY B O     1 
ATOM   7757 N N     . PHE B 1 423 ? -6.380  -45.554 11.771  1.00 26.92  ? 421 PHE B N     1 
ATOM   7758 C CA    . PHE B 1 423 ? -5.037  -44.924 11.675  1.00 31.42  ? 421 PHE B CA    1 
ATOM   7759 C C     . PHE B 1 423 ? -5.122  -43.459 12.097  1.00 30.21  ? 421 PHE B C     1 
ATOM   7760 O O     . PHE B 1 423 ? -4.070  -42.823 12.205  1.00 30.62  ? 421 PHE B O     1 
ATOM   7761 C CB    . PHE B 1 423 ? -4.507  -45.034 10.243  1.00 29.13  ? 421 PHE B CB    1 
ATOM   7762 C CG    . PHE B 1 423 ? -3.023  -44.822 10.084  1.00 29.82  ? 421 PHE B CG    1 
ATOM   7763 C CD1   . PHE B 1 423 ? -2.114  -45.694 10.660  1.00 27.47  ? 421 PHE B CD1   1 
ATOM   7764 C CD2   . PHE B 1 423 ? -2.534  -43.783 9.292   1.00 31.33  ? 421 PHE B CD2   1 
ATOM   7765 C CE1   . PHE B 1 423 ? -0.749  -45.496 10.500  1.00 29.01  ? 421 PHE B CE1   1 
ATOM   7766 C CE2   . PHE B 1 423 ? -1.168  -43.624 9.086   1.00 29.22  ? 421 PHE B CE2   1 
ATOM   7767 C CZ    . PHE B 1 423 ? -0.274  -44.481 9.695   1.00 28.49  ? 421 PHE B CZ    1 
ATOM   7768 N N     . ILE B 1 424 ? -6.340  -42.936 12.226  1.00 31.93  ? 422 ILE B N     1 
ATOM   7769 C CA    . ILE B 1 424 ? -6.623  -41.480 12.419  1.00 33.62  ? 422 ILE B CA    1 
ATOM   7770 C C     . ILE B 1 424 ? -6.714  -41.227 13.920  1.00 34.27  ? 422 ILE B C     1 
ATOM   7771 O O     . ILE B 1 424 ? -7.451  -41.976 14.581  1.00 34.43  ? 422 ILE B O     1 
ATOM   7772 C CB    . ILE B 1 424 ? -7.939  -41.078 11.715  1.00 33.96  ? 422 ILE B CB    1 
ATOM   7773 C CG1   . ILE B 1 424 ? -7.979  -41.514 10.246  1.00 35.75  ? 422 ILE B CG1   1 
ATOM   7774 C CG2   . ILE B 1 424 ? -8.199  -39.586 11.867  1.00 34.59  ? 422 ILE B CG2   1 
ATOM   7775 C CD1   . ILE B 1 424 ? -6.733  -41.118 9.453   1.00 36.09  ? 422 ILE B CD1   1 
ATOM   7776 N N     . ALA B 1 425 ? -6.058  -40.172 14.401  1.00 37.01  ? 423 ALA B N     1 
ATOM   7777 C CA    . ALA B 1 425 ? -5.840  -39.845 15.837  1.00 41.10  ? 423 ALA B CA    1 
ATOM   7778 C C     . ALA B 1 425 ? -7.143  -39.767 16.656  1.00 44.18  ? 423 ALA B C     1 
ATOM   7779 O O     . ALA B 1 425 ? -7.200  -40.307 17.777  1.00 50.46  ? 423 ALA B O     1 
ATOM   7780 C CB    . ALA B 1 425 ? -5.104  -38.544 15.922  1.00 41.99  ? 423 ALA B CB    1 
ATOM   7781 N N     . GLU B 1 426 ? -8.149  -39.103 16.119  1.00 43.09  ? 424 GLU B N     1 
ATOM   7782 C CA    . GLU B 1 426 ? -9.416  -38.732 16.803  1.00 44.64  ? 424 GLU B CA    1 
ATOM   7783 C C     . GLU B 1 426 ? -10.134 -39.956 17.378  1.00 46.24  ? 424 GLU B C     1 
ATOM   7784 O O     . GLU B 1 426 ? -10.873 -39.772 18.314  1.00 53.29  ? 424 GLU B O     1 
ATOM   7785 C CB    . GLU B 1 426 ? -10.354 -38.005 15.828  1.00 46.31  ? 424 GLU B CB    1 
ATOM   7786 C CG    . GLU B 1 426 ? -9.921  -36.569 15.523  1.00 50.60  ? 424 GLU B CG    1 
ATOM   7787 C CD    . GLU B 1 426 ? -8.622  -36.332 14.738  1.00 58.70  ? 424 GLU B CD    1 
ATOM   7788 O OE1   . GLU B 1 426 ? -8.373  -37.047 13.739  1.00 52.68  ? 424 GLU B OE1   1 
ATOM   7789 O OE2   . GLU B 1 426 ? -7.846  -35.397 15.112  1.00 74.58  ? 424 GLU B OE2   1 
ATOM   7790 N N     . HIS B 1 427 ? -9.957  -41.169 16.863  1.00 47.17  ? 425 HIS B N     1 
ATOM   7791 C CA    . HIS B 1 427 ? -10.701 -42.347 17.386  1.00 40.22  ? 425 HIS B CA    1 
ATOM   7792 C C     . HIS B 1 427 ? -9.927  -43.023 18.544  1.00 40.02  ? 425 HIS B C     1 
ATOM   7793 O O     . HIS B 1 427 ? -10.451 -43.990 19.123  1.00 36.49  ? 425 HIS B O     1 
ATOM   7794 C CB    . HIS B 1 427 ? -11.029 -43.296 16.230  1.00 46.61  ? 425 HIS B CB    1 
ATOM   7795 C CG    . HIS B 1 427 ? -11.714 -42.665 15.058  1.00 46.66  ? 425 HIS B CG    1 
ATOM   7796 N ND1   . HIS B 1 427 ? -13.096 -42.552 14.977  1.00 48.26  ? 425 HIS B ND1   1 
ATOM   7797 C CD2   . HIS B 1 427 ? -11.220 -42.154 13.903  1.00 46.80  ? 425 HIS B CD2   1 
ATOM   7798 C CE1   . HIS B 1 427 ? -13.423 -41.981 13.829  1.00 49.24  ? 425 HIS B CE1   1 
ATOM   7799 N NE2   . HIS B 1 427 ? -12.280 -41.729 13.144  1.00 49.17  ? 425 HIS B NE2   1 
ATOM   7800 N N     . GLY B 1 428 ? -8.722  -42.563 18.912  1.00 37.62  ? 426 GLY B N     1 
ATOM   7801 C CA    . GLY B 1 428 ? -8.022  -43.082 20.111  1.00 39.04  ? 426 GLY B CA    1 
ATOM   7802 C C     . GLY B 1 428 ? -7.487  -44.519 19.974  1.00 34.69  ? 426 GLY B C     1 
ATOM   7803 O O     . GLY B 1 428 ? -6.733  -44.969 20.845  1.00 30.07  ? 426 GLY B O     1 
ATOM   7804 N N     . MET B 1 429 ? -7.790  -45.230 18.898  1.00 30.08  ? 427 MET B N     1 
ATOM   7805 C CA    . MET B 1 429 ? -7.408  -46.649 18.775  1.00 31.23  ? 427 MET B CA    1 
ATOM   7806 C C     . MET B 1 429 ? -5.909  -46.741 18.484  1.00 29.66  ? 427 MET B C     1 
ATOM   7807 O O     . MET B 1 429 ? -5.237  -47.657 19.005  1.00 31.05  ? 427 MET B O     1 
ATOM   7808 C CB    . MET B 1 429 ? -8.244  -47.318 17.687  1.00 32.84  ? 427 MET B CB    1 
ATOM   7809 C CG    . MET B 1 429 ? -9.714  -47.443 18.087  1.00 35.61  ? 427 MET B CG    1 
ATOM   7810 S SD    . MET B 1 429 ? -9.981  -48.774 19.309  1.00 41.54  ? 427 MET B SD    1 
ATOM   7811 C CE    . MET B 1 429 ? -10.395 -47.666 20.640  1.00 40.40  ? 427 MET B CE    1 
ATOM   7812 N N     . GLU B 1 430 ? -5.391  -45.792 17.725  1.00 29.64  ? 428 GLU B N     1 
ATOM   7813 C CA    . GLU B 1 430 ? -3.967  -45.788 17.339  1.00 32.40  ? 428 GLU B CA    1 
ATOM   7814 C C     . GLU B 1 430 ? -3.124  -45.345 18.538  1.00 30.50  ? 428 GLU B C     1 
ATOM   7815 O O     . GLU B 1 430 ? -2.043  -45.918 18.710  1.00 34.25  ? 428 GLU B O     1 
ATOM   7816 C CB    . GLU B 1 430 ? -3.760  -44.967 16.068  1.00 33.16  ? 428 GLU B CB    1 
ATOM   7817 C CG    . GLU B 1 430 ? -4.051  -43.498 16.230  1.00 34.71  ? 428 GLU B CG    1 
ATOM   7818 C CD    . GLU B 1 430 ? -2.850  -42.655 16.636  1.00 33.41  ? 428 GLU B CD    1 
ATOM   7819 O OE1   . GLU B 1 430 ? -3.071  -41.518 17.069  1.00 34.87  ? 428 GLU B OE1   1 
ATOM   7820 O OE2   . GLU B 1 430 ? -1.713  -43.126 16.504  1.00 28.79  ? 428 GLU B OE2   1 
ATOM   7821 N N     . GLN B 1 431 ? -3.605  -44.413 19.361  1.00 31.48  ? 429 GLN B N     1 
ATOM   7822 C CA    . GLN B 1 431 ? -2.942  -44.037 20.642  1.00 30.89  ? 429 GLN B CA    1 
ATOM   7823 C C     . GLN B 1 431 ? -2.783  -45.290 21.513  1.00 28.54  ? 429 GLN B C     1 
ATOM   7824 O O     . GLN B 1 431 ? -1.699  -45.495 22.049  1.00 30.68  ? 429 GLN B O     1 
ATOM   7825 C CB    . GLN B 1 431 ? -3.707  -42.976 21.424  1.00 28.86  ? 429 GLN B CB    1 
ATOM   7826 C CG    . GLN B 1 431 ? -2.950  -42.552 22.669  1.00 30.55  ? 429 GLN B CG    1 
ATOM   7827 C CD    . GLN B 1 431 ? -3.789  -41.682 23.579  1.00 30.49  ? 429 GLN B CD    1 
ATOM   7828 O OE1   . GLN B 1 431 ? -4.608  -40.891 23.133  1.00 33.13  ? 429 GLN B OE1   1 
ATOM   7829 N NE2   . GLN B 1 431 ? -3.578  -41.803 24.875  1.00 31.86  ? 429 GLN B NE2   1 
ATOM   7830 N N     . ASN B 1 432 ? -3.826  -46.102 21.629  1.00 27.10  ? 430 ASN B N     1 
ATOM   7831 C CA    . ASN B 1 432 ? -3.782  -47.366 22.399  1.00 27.28  ? 430 ASN B CA    1 
ATOM   7832 C C     . ASN B 1 432 ? -2.591  -48.234 21.941  1.00 28.70  ? 430 ASN B C     1 
ATOM   7833 O O     . ASN B 1 432 ? -1.820  -48.721 22.808  1.00 28.17  ? 430 ASN B O     1 
ATOM   7834 C CB    . ASN B 1 432 ? -5.095  -48.111 22.248  1.00 26.51  ? 430 ASN B CB    1 
ATOM   7835 C CG    . ASN B 1 432 ? -5.229  -49.216 23.259  1.00 27.53  ? 430 ASN B CG    1 
ATOM   7836 O OD1   . ASN B 1 432 ? -4.916  -49.029 24.435  1.00 29.94  ? 430 ASN B OD1   1 
ATOM   7837 N ND2   . ASN B 1 432 ? -5.789  -50.330 22.824  1.00 28.07  ? 430 ASN B ND2   1 
ATOM   7838 N N     . VAL B 1 433 ? -2.422  -48.430 20.636  1.00 25.20  ? 431 VAL B N     1 
ATOM   7839 C CA    . VAL B 1 433 ? -1.271  -49.209 20.089  1.00 26.08  ? 431 VAL B CA    1 
ATOM   7840 C C     . VAL B 1 433 ? 0.065   -48.573 20.513  1.00 26.25  ? 431 VAL B C     1 
ATOM   7841 O O     . VAL B 1 433 ? 1.002   -49.311 20.968  1.00 25.50  ? 431 VAL B O     1 
ATOM   7842 C CB    . VAL B 1 433 ? -1.354  -49.329 18.551  1.00 24.30  ? 431 VAL B CB    1 
ATOM   7843 C CG1   . VAL B 1 433 ? -0.054  -49.878 17.984  1.00 22.78  ? 431 VAL B CG1   1 
ATOM   7844 C CG2   . VAL B 1 433 ? -2.543  -50.196 18.130  1.00 24.92  ? 431 VAL B CG2   1 
ATOM   7845 N N     . ARG B 1 434 ? 0.204   -47.269 20.276  1.00 26.23  ? 432 ARG B N     1 
ATOM   7846 C CA    . ARG B 1 434 ? 1.429   -46.495 20.612  1.00 27.96  ? 432 ARG B CA    1 
ATOM   7847 C C     . ARG B 1 434 ? 1.754   -46.631 22.121  1.00 28.56  ? 432 ARG B C     1 
ATOM   7848 O O     . ARG B 1 434 ? 2.914   -46.919 22.444  1.00 28.43  ? 432 ARG B O     1 
ATOM   7849 C CB    . ARG B 1 434 ? 1.268   -45.052 20.129  1.00 28.02  ? 432 ARG B CB    1 
ATOM   7850 C CG    . ARG B 1 434 ? 1.504   -44.906 18.632  1.00 29.95  ? 432 ARG B CG    1 
ATOM   7851 C CD    . ARG B 1 434 ? 1.541   -43.465 18.152  1.00 28.27  ? 432 ARG B CD    1 
ATOM   7852 N NE    . ARG B 1 434 ? 0.269   -42.779 18.385  1.00 31.09  ? 432 ARG B NE    1 
ATOM   7853 C CZ    . ARG B 1 434 ? 0.052   -41.864 19.336  1.00 31.16  ? 432 ARG B CZ    1 
ATOM   7854 N NH1   . ARG B 1 434 ? 1.014   -41.548 20.186  1.00 31.20  ? 432 ARG B NH1   1 
ATOM   7855 N NH2   . ARG B 1 434 ? -1.131  -41.282 19.444  1.00 29.48  ? 432 ARG B NH2   1 
ATOM   7856 N N     . ASP B 1 435 ? 0.761   -46.469 22.987  1.00 26.45  ? 433 ASP B N     1 
ATOM   7857 C CA    . ASP B 1 435 ? 0.952   -46.585 24.455  1.00 30.38  ? 433 ASP B CA    1 
ATOM   7858 C C     . ASP B 1 435 ? 1.286   -48.035 24.825  1.00 31.79  ? 433 ASP B C     1 
ATOM   7859 O O     . ASP B 1 435 ? 2.030   -48.239 25.780  1.00 28.68  ? 433 ASP B O     1 
ATOM   7860 C CB    . ASP B 1 435 ? -0.282  -46.065 25.192  1.00 28.46  ? 433 ASP B CB    1 
ATOM   7861 C CG    . ASP B 1 435 ? -0.506  -44.567 25.074  1.00 31.24  ? 433 ASP B CG    1 
ATOM   7862 O OD1   . ASP B 1 435 ? 0.384   -43.880 24.552  1.00 26.67  ? 433 ASP B OD1   1 
ATOM   7863 O OD2   . ASP B 1 435 ? -1.570  -44.105 25.513  1.00 28.20  ? 433 ASP B OD2   1 
ATOM   7864 N N     . SER B 1 436 ? 0.766   -48.993 24.065  1.00 31.01  ? 434 SER B N     1 
ATOM   7865 C CA    . SER B 1 436 ? 0.996   -50.427 24.350  1.00 30.56  ? 434 SER B CA    1 
ATOM   7866 C C     . SER B 1 436 ? 2.458   -50.781 24.061  1.00 32.02  ? 434 SER B C     1 
ATOM   7867 O O     . SER B 1 436 ? 3.004   -51.628 24.791  1.00 28.70  ? 434 SER B O     1 
ATOM   7868 C CB    . SER B 1 436 ? 0.057   -51.308 23.585  1.00 30.94  ? 434 SER B CB    1 
ATOM   7869 O OG    . SER B 1 436 ? 0.352   -52.666 23.841  1.00 32.58  ? 434 SER B OG    1 
ATOM   7870 N N     . ARG B 1 437 ? 3.081   -50.165 23.058  1.00 30.74  ? 435 ARG B N     1 
ATOM   7871 C CA    . ARG B 1 437 ? 4.388   -50.667 22.557  1.00 30.84  ? 435 ARG B CA    1 
ATOM   7872 C C     . ARG B 1 437 ? 5.481   -50.643 23.654  1.00 31.39  ? 435 ARG B C     1 
ATOM   7873 O O     . ARG B 1 437 ? 6.381   -51.541 23.623  1.00 26.30  ? 435 ARG B O     1 
ATOM   7874 C CB    . ARG B 1 437 ? 4.874   -49.891 21.334  1.00 27.05  ? 435 ARG B CB    1 
ATOM   7875 C CG    . ARG B 1 437 ? 6.090   -50.531 20.677  1.00 27.57  ? 435 ARG B CG    1 
ATOM   7876 C CD    . ARG B 1 437 ? 5.763   -51.947 20.216  1.00 26.31  ? 435 ARG B CD    1 
ATOM   7877 N NE    . ARG B 1 437 ? 6.896   -52.696 19.710  1.00 25.89  ? 435 ARG B NE    1 
ATOM   7878 C CZ    . ARG B 1 437 ? 7.815   -53.328 20.446  1.00 24.84  ? 435 ARG B CZ    1 
ATOM   7879 N NH1   . ARG B 1 437 ? 7.789   -53.273 21.763  1.00 26.39  ? 435 ARG B NH1   1 
ATOM   7880 N NH2   . ARG B 1 437 ? 8.777   -54.020 19.855  1.00 24.65  ? 435 ARG B NH2   1 
ATOM   7881 N N     . ILE B 1 438 ? 5.497   -49.671 24.562  1.00 31.11  ? 436 ILE B N     1 
ATOM   7882 C CA    . ILE B 1 438 ? 6.585   -49.589 25.587  1.00 31.03  ? 436 ILE B CA    1 
ATOM   7883 C C     . ILE B 1 438 ? 6.449   -50.744 26.581  1.00 30.14  ? 436 ILE B C     1 
ATOM   7884 O O     . ILE B 1 438 ? 7.463   -51.136 27.141  1.00 30.48  ? 436 ILE B O     1 
ATOM   7885 C CB    . ILE B 1 438 ? 6.525   -48.241 26.341  1.00 29.95  ? 436 ILE B CB    1 
ATOM   7886 C CG1   . ILE B 1 438 ? 7.691   -48.067 27.315  1.00 27.62  ? 436 ILE B CG1   1 
ATOM   7887 C CG2   . ILE B 1 438 ? 5.187   -48.068 27.041  1.00 28.40  ? 436 ILE B CG2   1 
ATOM   7888 C CD1   . ILE B 1 438 ? 9.027   -48.421 26.729  1.00 29.61  ? 436 ILE B CD1   1 
ATOM   7889 N N     . SER B 1 439 ? 5.250   -51.281 26.745  1.00 28.78  ? 437 SER B N     1 
ATOM   7890 C CA    . SER B 1 439 ? 4.942   -52.274 27.798  1.00 30.96  ? 437 SER B CA    1 
ATOM   7891 C C     . SER B 1 439 ? 5.771   -53.546 27.610  1.00 33.28  ? 437 SER B C     1 
ATOM   7892 O O     . SER B 1 439 ? 5.937   -54.246 28.618  1.00 30.71  ? 437 SER B O     1 
ATOM   7893 C CB    . SER B 1 439 ? 3.457   -52.577 27.875  1.00 31.63  ? 437 SER B CB    1 
ATOM   7894 O OG    . SER B 1 439 ? 3.027   -53.448 26.846  1.00 28.65  ? 437 SER B OG    1 
ATOM   7895 N N     . MET B 1 440 ? 6.264   -53.826 26.398  1.00 28.24  ? 438 MET B N     1 
ATOM   7896 C CA    . MET B 1 440 ? 7.104   -55.015 26.098  1.00 29.74  ? 438 MET B CA    1 
ATOM   7897 C C     . MET B 1 440 ? 8.592   -54.655 26.214  1.00 31.92  ? 438 MET B C     1 
ATOM   7898 O O     . MET B 1 440 ? 9.433   -55.553 26.018  1.00 31.80  ? 438 MET B O     1 
ATOM   7899 C CB    . MET B 1 440 ? 6.833   -55.529 24.679  1.00 31.72  ? 438 MET B CB    1 
ATOM   7900 C CG    . MET B 1 440 ? 5.451   -56.109 24.468  1.00 34.88  ? 438 MET B CG    1 
ATOM   7901 S SD    . MET B 1 440 ? 4.667   -55.378 23.005  1.00 46.51  ? 438 MET B SD    1 
ATOM   7902 C CE    . MET B 1 440 ? 4.006   -53.982 23.889  1.00 42.97  ? 438 MET B CE    1 
ATOM   7903 N N     . LEU B 1 441 ? 8.927   -53.388 26.459  1.00 30.85  ? 439 LEU B N     1 
ATOM   7904 C CA    . LEU B 1 441 ? 10.346  -52.936 26.554  1.00 32.75  ? 439 LEU B CA    1 
ATOM   7905 C C     . LEU B 1 441 ? 10.747  -52.628 28.012  1.00 30.62  ? 439 LEU B C     1 
ATOM   7906 O O     . LEU B 1 441 ? 11.854  -52.975 28.403  1.00 34.70  ? 439 LEU B O     1 
ATOM   7907 C CB    . LEU B 1 441 ? 10.570  -51.705 25.663  1.00 31.19  ? 439 LEU B CB    1 
ATOM   7908 C CG    . LEU B 1 441 ? 10.098  -51.797 24.210  1.00 29.51  ? 439 LEU B CG    1 
ATOM   7909 C CD1   . LEU B 1 441 ? 10.023  -50.420 23.593  1.00 28.90  ? 439 LEU B CD1   1 
ATOM   7910 C CD2   . LEU B 1 441 ? 10.982  -52.691 23.378  1.00 30.19  ? 439 LEU B CD2   1 
ATOM   7911 N N     . TYR B 1 442 ? 9.869   -51.980 28.759  1.00 28.76  ? 440 TYR B N     1 
ATOM   7912 C CA    . TYR B 1 442 ? 10.267  -51.567 30.123  1.00 28.70  ? 440 TYR B CA    1 
ATOM   7913 C C     . TYR B 1 442 ? 9.828   -52.582 31.179  1.00 29.47  ? 440 TYR B C     1 
ATOM   7914 O O     . TYR B 1 442 ? 9.082   -53.508 30.859  1.00 27.34  ? 440 TYR B O     1 
ATOM   7915 C CB    . TYR B 1 442 ? 9.865   -50.117 30.408  1.00 29.56  ? 440 TYR B CB    1 
ATOM   7916 C CG    . TYR B 1 442 ? 8.407   -49.761 30.549  1.00 29.08  ? 440 TYR B CG    1 
ATOM   7917 C CD1   . TYR B 1 442 ? 7.390   -50.688 30.402  1.00 28.39  ? 440 TYR B CD1   1 
ATOM   7918 C CD2   . TYR B 1 442 ? 8.054   -48.455 30.835  1.00 31.08  ? 440 TYR B CD2   1 
ATOM   7919 C CE1   . TYR B 1 442 ? 6.061   -50.322 30.537  1.00 27.58  ? 440 TYR B CE1   1 
ATOM   7920 C CE2   . TYR B 1 442 ? 6.733   -48.072 30.970  1.00 30.77  ? 440 TYR B CE2   1 
ATOM   7921 C CZ    . TYR B 1 442 ? 5.732   -49.010 30.824  1.00 29.01  ? 440 TYR B CZ    1 
ATOM   7922 O OH    . TYR B 1 442 ? 4.438   -48.611 30.963  1.00 29.11  ? 440 TYR B OH    1 
ATOM   7923 N N     . GLU B 1 443 ? 10.296  -52.378 32.406  1.00 37.10  ? 441 GLU B N     1 
ATOM   7924 C CA    . GLU B 1 443 ? 10.054  -53.293 33.552  1.00 34.67  ? 441 GLU B CA    1 
ATOM   7925 C C     . GLU B 1 443 ? 10.489  -54.710 33.163  1.00 31.05  ? 441 GLU B C     1 
ATOM   7926 O O     . GLU B 1 443 ? 9.710   -55.633 33.376  1.00 33.13  ? 441 GLU B O     1 
ATOM   7927 C CB    . GLU B 1 443 ? 8.587   -53.235 34.003  1.00 40.04  ? 441 GLU B CB    1 
ATOM   7928 C CG    . GLU B 1 443 ? 8.423   -53.478 35.500  1.00 50.69  ? 441 GLU B CG    1 
ATOM   7929 C CD    . GLU B 1 443 ? 9.444   -52.759 36.381  1.00 61.96  ? 441 GLU B CD    1 
ATOM   7930 O OE1   . GLU B 1 443 ? 9.375   -51.490 36.429  1.00 62.97  ? 441 GLU B OE1   1 
ATOM   7931 O OE2   . GLU B 1 443 ? 10.346  -53.464 36.968  1.00 62.51  ? 441 GLU B OE2   1 
ATOM   7932 N N     . GLY B 1 444 ? 11.667  -54.843 32.557  1.00 32.68  ? 442 GLY B N     1 
ATOM   7933 C CA    . GLY B 1 444 ? 12.190  -56.118 32.025  1.00 35.79  ? 442 GLY B CA    1 
ATOM   7934 C C     . GLY B 1 444 ? 11.607  -56.444 30.657  1.00 33.36  ? 442 GLY B C     1 
ATOM   7935 O O     . GLY B 1 444 ? 10.384  -56.681 30.581  1.00 30.08  ? 442 GLY B O     1 
ATOM   7936 N N     . THR B 1 445 ? 12.442  -56.502 29.620  1.00 31.32  ? 443 THR B N     1 
ATOM   7937 C CA    . THR B 1 445 ? 11.979  -56.748 28.229  1.00 31.22  ? 443 THR B CA    1 
ATOM   7938 C C     . THR B 1 445 ? 11.364  -58.134 28.159  1.00 33.66  ? 443 THR B C     1 
ATOM   7939 O O     . THR B 1 445 ? 11.759  -58.969 28.966  1.00 36.36  ? 443 THR B O     1 
ATOM   7940 C CB    . THR B 1 445 ? 13.106  -56.710 27.203  1.00 31.85  ? 443 THR B CB    1 
ATOM   7941 O OG1   . THR B 1 445 ? 13.931  -57.864 27.378  1.00 30.39  ? 443 THR B OG1   1 
ATOM   7942 C CG2   . THR B 1 445 ? 13.914  -55.435 27.300  1.00 33.58  ? 443 THR B CG2   1 
ATOM   7943 N N     . THR B 1 446 ? 10.490  -58.375 27.188  1.00 31.12  ? 444 THR B N     1 
ATOM   7944 C CA    . THR B 1 446 ? 9.924   -59.710 26.923  1.00 30.22  ? 444 THR B CA    1 
ATOM   7945 C C     . THR B 1 446 ? 11.055  -60.723 27.026  1.00 30.28  ? 444 THR B C     1 
ATOM   7946 O O     . THR B 1 446 ? 10.851  -61.723 27.672  1.00 31.19  ? 444 THR B O     1 
ATOM   7947 C CB    . THR B 1 446 ? 9.241   -59.780 25.552  1.00 34.72  ? 444 THR B CB    1 
ATOM   7948 O OG1   . THR B 1 446 ? 8.250   -58.748 25.479  1.00 33.00  ? 444 THR B OG1   1 
ATOM   7949 C CG2   . THR B 1 446 ? 8.622   -61.139 25.295  1.00 32.11  ? 444 THR B CG2   1 
ATOM   7950 N N     . GLY B 1 447 ? 12.199  -60.455 26.404  1.00 31.24  ? 445 GLY B N     1 
ATOM   7951 C CA    . GLY B 1 447 ? 13.291  -61.439 26.280  1.00 31.08  ? 445 GLY B CA    1 
ATOM   7952 C C     . GLY B 1 447 ? 13.933  -61.713 27.619  1.00 35.23  ? 445 GLY B C     1 
ATOM   7953 O O     . GLY B 1 447 ? 14.287  -62.897 27.901  1.00 36.34  ? 445 GLY B O     1 
ATOM   7954 N N     . VAL B 1 448 ? 14.076  -60.666 28.431  1.00 31.86  ? 446 VAL B N     1 
ATOM   7955 C CA    . VAL B 1 448 ? 14.705  -60.771 29.777  1.00 34.80  ? 446 VAL B CA    1 
ATOM   7956 C C     . VAL B 1 448 ? 13.755  -61.516 30.707  1.00 35.86  ? 446 VAL B C     1 
ATOM   7957 O O     . VAL B 1 448 ? 14.220  -62.377 31.487  1.00 39.17  ? 446 VAL B O     1 
ATOM   7958 C CB    . VAL B 1 448 ? 15.081  -59.380 30.303  1.00 37.75  ? 446 VAL B CB    1 
ATOM   7959 C CG1   . VAL B 1 448 ? 15.300  -59.359 31.811  1.00 37.93  ? 446 VAL B CG1   1 
ATOM   7960 C CG2   . VAL B 1 448 ? 16.304  -58.880 29.551  1.00 38.02  ? 446 VAL B CG2   1 
ATOM   7961 N N     . GLN B 1 449 ? 12.463  -61.223 30.611  1.00 36.43  ? 447 GLN B N     1 
ATOM   7962 C CA    . GLN B 1 449 ? 11.421  -61.931 31.397  1.00 34.76  ? 447 GLN B CA    1 
ATOM   7963 C C     . GLN B 1 449 ? 11.438  -63.409 31.024  1.00 33.66  ? 447 GLN B C     1 
ATOM   7964 O O     . GLN B 1 449 ? 11.253  -64.236 31.879  1.00 34.65  ? 447 GLN B O     1 
ATOM   7965 C CB    . GLN B 1 449 ? 10.046  -61.345 31.098  1.00 37.22  ? 447 GLN B CB    1 
ATOM   7966 C CG    . GLN B 1 449 ? 9.912   -59.883 31.497  1.00 39.78  ? 447 GLN B CG    1 
ATOM   7967 C CD    . GLN B 1 449 ? 9.760   -59.690 32.989  1.00 38.42  ? 447 GLN B CD    1 
ATOM   7968 O OE1   . GLN B 1 449 ? 9.438   -60.617 33.733  1.00 36.60  ? 447 GLN B OE1   1 
ATOM   7969 N NE2   . GLN B 1 449 ? 9.949   -58.454 33.420  1.00 35.37  ? 447 GLN B NE2   1 
ATOM   7970 N N     . ALA B 1 450 ? 11.566  -63.729 29.747  1.00 35.82  ? 448 ALA B N     1 
ATOM   7971 C CA    . ALA B 1 450 ? 11.471  -65.126 29.306  1.00 34.53  ? 448 ALA B CA    1 
ATOM   7972 C C     . ALA B 1 450 ? 12.670  -65.852 29.917  1.00 41.85  ? 448 ALA B C     1 
ATOM   7973 O O     . ALA B 1 450 ? 12.495  -66.958 30.485  1.00 39.21  ? 448 ALA B O     1 
ATOM   7974 C CB    . ALA B 1 450 ? 11.446  -65.210 27.815  1.00 30.74  ? 448 ALA B CB    1 
ATOM   7975 N N     . LEU B 1 451 ? 13.837  -65.217 29.819  1.00 43.75  ? 449 LEU B N     1 
ATOM   7976 C CA    . LEU B 1 451 ? 15.109  -65.774 30.340  1.00 48.51  ? 449 LEU B CA    1 
ATOM   7977 C C     . LEU B 1 451 ? 14.942  -65.996 31.851  1.00 46.12  ? 449 LEU B C     1 
ATOM   7978 O O     . LEU B 1 451 ? 15.299  -67.066 32.326  1.00 46.01  ? 449 LEU B O     1 
ATOM   7979 C CB    . LEU B 1 451 ? 16.255  -64.819 29.988  1.00 51.04  ? 449 LEU B CB    1 
ATOM   7980 C CG    . LEU B 1 451 ? 17.662  -65.337 30.275  1.00 51.44  ? 449 LEU B CG    1 
ATOM   7981 C CD1   . LEU B 1 451 ? 17.916  -66.634 29.533  1.00 49.72  ? 449 LEU B CD1   1 
ATOM   7982 C CD2   . LEU B 1 451 ? 18.711  -64.292 29.904  1.00 48.61  ? 449 LEU B CD2   1 
ATOM   7983 N N     . ASP B 1 452 ? 14.337  -65.052 32.562  1.00 45.78  ? 450 ASP B N     1 
ATOM   7984 C CA    . ASP B 1 452 ? 14.066  -65.170 34.018  1.00 49.08  ? 450 ASP B CA    1 
ATOM   7985 C C     . ASP B 1 452 ? 13.178  -66.396 34.270  1.00 48.82  ? 450 ASP B C     1 
ATOM   7986 O O     . ASP B 1 452 ? 13.526  -67.243 35.096  1.00 54.88  ? 450 ASP B O     1 
ATOM   7987 C CB    . ASP B 1 452 ? 13.394  -63.903 34.558  1.00 48.65  ? 450 ASP B CB    1 
ATOM   7988 C CG    . ASP B 1 452 ? 13.287  -63.895 36.072  1.00 56.39  ? 450 ASP B CG    1 
ATOM   7989 O OD1   . ASP B 1 452 ? 14.360  -63.905 36.730  1.00 65.91  ? 450 ASP B OD1   1 
ATOM   7990 O OD2   . ASP B 1 452 ? 12.139  -63.899 36.583  1.00 51.07  ? 450 ASP B OD2   1 
ATOM   7991 N N     . LEU B 1 453 ? 12.052  -66.496 33.580  1.00 44.94  ? 451 LEU B N     1 
ATOM   7992 C CA    . LEU B 1 453 ? 11.112  -67.616 33.787  1.00 41.97  ? 451 LEU B CA    1 
ATOM   7993 C C     . LEU B 1 453 ? 11.855  -68.936 33.543  1.00 42.66  ? 451 LEU B C     1 
ATOM   7994 O O     . LEU B 1 453 ? 11.780  -69.808 34.410  1.00 43.85  ? 451 LEU B O     1 
ATOM   7995 C CB    . LEU B 1 453 ? 9.901   -67.464 32.863  1.00 41.12  ? 451 LEU B CB    1 
ATOM   7996 C CG    . LEU B 1 453 ? 8.949   -68.660 32.786  1.00 41.38  ? 451 LEU B CG    1 
ATOM   7997 C CD1   . LEU B 1 453 ? 8.234   -68.905 34.121  1.00 42.48  ? 451 LEU B CD1   1 
ATOM   7998 C CD2   . LEU B 1 453 ? 7.943   -68.460 31.671  1.00 38.71  ? 451 LEU B CD2   1 
ATOM   7999 N N     . LEU B 1 454 ? 12.503  -69.127 32.399  1.00 38.46  ? 452 LEU B N     1 
ATOM   8000 C CA    . LEU B 1 454 ? 12.936  -70.507 32.034  1.00 41.88  ? 452 LEU B CA    1 
ATOM   8001 C C     . LEU B 1 454 ? 14.215  -70.894 32.788  1.00 44.66  ? 452 LEU B C     1 
ATOM   8002 O O     . LEU B 1 454 ? 14.267  -72.003 33.280  1.00 51.37  ? 452 LEU B O     1 
ATOM   8003 C CB    . LEU B 1 454 ? 13.168  -70.623 30.536  1.00 37.67  ? 452 LEU B CB    1 
ATOM   8004 C CG    . LEU B 1 454 ? 13.548  -72.019 30.084  1.00 39.69  ? 452 LEU B CG    1 
ATOM   8005 C CD1   . LEU B 1 454 ? 12.477  -73.013 30.497  1.00 40.94  ? 452 LEU B CD1   1 
ATOM   8006 C CD2   . LEU B 1 454 ? 13.774  -72.037 28.591  1.00 37.02  ? 452 LEU B CD2   1 
ATOM   8007 N N     . GLY B 1 455 ? 15.190  -69.991 32.874  1.00 46.92  ? 453 GLY B N     1 
ATOM   8008 C CA    . GLY B 1 455 ? 16.539  -70.262 33.394  1.00 48.80  ? 453 GLY B CA    1 
ATOM   8009 C C     . GLY B 1 455 ? 16.588  -70.192 34.909  1.00 49.82  ? 453 GLY B C     1 
ATOM   8010 O O     . GLY B 1 455 ? 16.970  -71.191 35.525  1.00 52.37  ? 453 GLY B O     1 
ATOM   8011 N N     . ARG B 1 456 ? 16.197  -69.056 35.482  1.00 47.97  ? 454 ARG B N     1 
ATOM   8012 C CA    . ARG B 1 456 ? 16.325  -68.768 36.930  1.00 50.75  ? 454 ARG B CA    1 
ATOM   8013 C C     . ARG B 1 456 ? 15.188  -69.481 37.691  1.00 51.89  ? 454 ARG B C     1 
ATOM   8014 O O     . ARG B 1 456 ? 15.477  -70.071 38.735  1.00 67.87  ? 454 ARG B O     1 
ATOM   8015 C CB    . ARG B 1 456 ? 16.438  -67.255 37.153  1.00 53.43  ? 454 ARG B CB    1 
ATOM   8016 C CG    . ARG B 1 456 ? 15.705  -66.774 38.397  1.00 66.03  ? 454 ARG B CG    1 
ATOM   8017 C CD    . ARG B 1 456 ? 16.071  -65.395 38.904  1.00 70.32  ? 454 ARG B CD    1 
ATOM   8018 N NE    . ARG B 1 456 ? 15.863  -65.368 40.348  1.00 71.34  ? 454 ARG B NE    1 
ATOM   8019 C CZ    . ARG B 1 456 ? 16.828  -65.283 41.262  1.00 71.15  ? 454 ARG B CZ    1 
ATOM   8020 N NH1   . ARG B 1 456 ? 18.093  -65.171 40.904  1.00 74.62  ? 454 ARG B NH1   1 
ATOM   8021 N NH2   . ARG B 1 456 ? 16.524  -65.279 42.546  1.00 76.75  ? 454 ARG B NH2   1 
ATOM   8022 N N     . LYS B 1 457 ? 13.945  -69.462 37.204  1.00 50.75  ? 455 LYS B N     1 
ATOM   8023 C CA    . LYS B 1 457 ? 12.764  -69.925 37.983  1.00 44.88  ? 455 LYS B CA    1 
ATOM   8024 C C     . LYS B 1 457 ? 12.493  -71.418 37.748  1.00 46.23  ? 455 LYS B C     1 
ATOM   8025 O O     . LYS B 1 457 ? 12.281  -72.154 38.737  1.00 46.47  ? 455 LYS B O     1 
ATOM   8026 C CB    . LYS B 1 457 ? 11.529  -69.108 37.606  1.00 47.85  ? 455 LYS B CB    1 
ATOM   8027 C CG    . LYS B 1 457 ? 11.629  -67.616 37.883  1.00 47.95  ? 455 LYS B CG    1 
ATOM   8028 C CD    . LYS B 1 457 ? 11.865  -67.288 39.328  1.00 47.87  ? 455 LYS B CD    1 
ATOM   8029 C CE    . LYS B 1 457 ? 12.127  -65.809 39.532  1.00 50.88  ? 455 LYS B CE    1 
ATOM   8030 N NZ    . LYS B 1 457 ? 10.953  -64.991 39.133  1.00 48.09  ? 455 LYS B NZ    1 
ATOM   8031 N N     . VAL B 1 458 ? 12.453  -71.849 36.491  1.00 40.33  ? 456 VAL B N     1 
ATOM   8032 C CA    . VAL B 1 458 ? 12.011  -73.221 36.127  1.00 41.85  ? 456 VAL B CA    1 
ATOM   8033 C C     . VAL B 1 458 ? 13.251  -74.113 36.160  1.00 40.85  ? 456 VAL B C     1 
ATOM   8034 O O     . VAL B 1 458 ? 13.305  -74.927 37.056  1.00 41.88  ? 456 VAL B O     1 
ATOM   8035 C CB    . VAL B 1 458 ? 11.232  -73.248 34.796  1.00 40.36  ? 456 VAL B CB    1 
ATOM   8036 C CG1   . VAL B 1 458 ? 11.006  -74.659 34.255  1.00 38.11  ? 456 VAL B CG1   1 
ATOM   8037 C CG2   . VAL B 1 458 ? 9.911   -72.522 34.974  1.00 41.54  ? 456 VAL B CG2   1 
ATOM   8038 N N     . LEU B 1 459 ? 14.236  -73.898 35.290  1.00 42.85  ? 457 LEU B N     1 
ATOM   8039 C CA    . LEU B 1 459 ? 15.386  -74.834 35.117  1.00 46.83  ? 457 LEU B CA    1 
ATOM   8040 C C     . LEU B 1 459 ? 16.263  -74.879 36.380  1.00 47.04  ? 457 LEU B C     1 
ATOM   8041 O O     . LEU B 1 459 ? 16.801  -75.983 36.667  1.00 48.05  ? 457 LEU B O     1 
ATOM   8042 C CB    . LEU B 1 459 ? 16.188  -74.432 33.878  1.00 42.63  ? 457 LEU B CB    1 
ATOM   8043 C CG    . LEU B 1 459 ? 15.525  -74.746 32.540  1.00 41.14  ? 457 LEU B CG    1 
ATOM   8044 C CD1   . LEU B 1 459 ? 16.554  -74.670 31.425  1.00 42.27  ? 457 LEU B CD1   1 
ATOM   8045 C CD2   . LEU B 1 459 ? 14.827  -76.101 32.535  1.00 40.91  ? 457 LEU B CD2   1 
ATOM   8046 N N     . MET B 1 460 ? 16.316  -73.768 37.132  1.00 48.62  ? 458 MET B N     1 
ATOM   8047 C CA    . MET B 1 460 ? 17.131  -73.600 38.367  1.00 49.54  ? 458 MET B CA    1 
ATOM   8048 C C     . MET B 1 460 ? 16.430  -74.265 39.564  1.00 47.85  ? 458 MET B C     1 
ATOM   8049 O O     . MET B 1 460 ? 17.114  -74.485 40.566  1.00 42.87  ? 458 MET B O     1 
ATOM   8050 C CB    . MET B 1 460 ? 17.415  -72.123 38.683  1.00 53.94  ? 458 MET B CB    1 
ATOM   8051 C CG    . MET B 1 460 ? 18.867  -71.823 39.114  1.00 65.16  ? 458 MET B CG    1 
ATOM   8052 S SD    . MET B 1 460 ? 20.090  -72.323 37.838  1.00 75.10  ? 458 MET B SD    1 
ATOM   8053 C CE    . MET B 1 460 ? 20.223  -70.818 36.873  1.00 77.98  ? 458 MET B CE    1 
ATOM   8054 N N     . THR B 1 461 ? 15.127  -74.554 39.489  1.00 45.25  ? 459 THR B N     1 
ATOM   8055 C CA    . THR B 1 461 ? 14.381  -75.338 40.513  1.00 41.56  ? 459 THR B CA    1 
ATOM   8056 C C     . THR B 1 461 ? 14.150  -76.764 39.979  1.00 40.04  ? 459 THR B C     1 
ATOM   8057 O O     . THR B 1 461 ? 13.326  -77.519 40.545  1.00 41.21  ? 459 THR B O     1 
ATOM   8058 C CB    . THR B 1 461 ? 13.094  -74.612 40.938  1.00 43.16  ? 459 THR B CB    1 
ATOM   8059 O OG1   . THR B 1 461 ? 12.117  -74.584 39.883  1.00 41.85  ? 459 THR B OG1   1 
ATOM   8060 C CG2   . THR B 1 461 ? 13.389  -73.222 41.455  1.00 37.85  ? 459 THR B CG2   1 
ATOM   8061 N N     . GLN B 1 462 ? 14.840  -77.112 38.902  1.00 40.00  ? 460 GLN B N     1 
ATOM   8062 C CA    . GLN B 1 462 ? 14.715  -78.415 38.208  1.00 46.13  ? 460 GLN B CA    1 
ATOM   8063 C C     . GLN B 1 462 ? 13.251  -78.762 37.984  1.00 44.08  ? 460 GLN B C     1 
ATOM   8064 O O     . GLN B 1 462 ? 12.939  -79.957 37.968  1.00 47.63  ? 460 GLN B O     1 
ATOM   8065 C CB    . GLN B 1 462 ? 15.459  -79.480 39.005  1.00 53.98  ? 460 GLN B CB    1 
ATOM   8066 C CG    . GLN B 1 462 ? 16.935  -79.145 39.097  1.00 57.42  ? 460 GLN B CG    1 
ATOM   8067 C CD    . GLN B 1 462 ? 17.691  -80.132 39.937  1.00 62.67  ? 460 GLN B CD    1 
ATOM   8068 O OE1   . GLN B 1 462 ? 17.284  -81.278 40.108  1.00 61.63  ? 460 GLN B OE1   1 
ATOM   8069 N NE2   . GLN B 1 462 ? 18.815  -79.680 40.455  1.00 71.37  ? 460 GLN B NE2   1 
ATOM   8070 N N     . GLY B 1 463 ? 12.431  -77.746 37.713  1.00 45.33  ? 461 GLY B N     1 
ATOM   8071 C CA    . GLY B 1 463 ? 11.044  -77.888 37.240  1.00 44.07  ? 461 GLY B CA    1 
ATOM   8072 C C     . GLY B 1 463 ? 10.027  -77.685 38.351  1.00 43.88  ? 461 GLY B C     1 
ATOM   8073 O O     . GLY B 1 463 ? 8.831   -77.741 38.030  1.00 45.07  ? 461 GLY B O     1 
ATOM   8074 N N     . GLU B 1 464 ? 10.459  -77.468 39.602  1.00 42.27  ? 462 GLU B N     1 
ATOM   8075 C CA    . GLU B 1 464 ? 9.538   -77.406 40.772  1.00 45.89  ? 462 GLU B CA    1 
ATOM   8076 C C     . GLU B 1 464 ? 8.645   -76.176 40.655  1.00 44.82  ? 462 GLU B C     1 
ATOM   8077 O O     . GLU B 1 464 ? 7.470   -76.290 41.035  1.00 46.94  ? 462 GLU B O     1 
ATOM   8078 C CB    . GLU B 1 464 ? 10.232  -77.363 42.145  1.00 52.82  ? 462 GLU B CB    1 
ATOM   8079 C CG    . GLU B 1 464 ? 10.846  -78.687 42.636  1.00 60.13  ? 462 GLU B CG    1 
ATOM   8080 C CD    . GLU B 1 464 ? 10.220  -80.027 42.236  1.00 64.91  ? 462 GLU B CD    1 
ATOM   8081 O OE1   . GLU B 1 464 ? 11.001  -80.917 41.837  1.00 62.61  ? 462 GLU B OE1   1 
ATOM   8082 O OE2   . GLU B 1 464 ? 8.967   -80.209 42.346  1.00 65.92  ? 462 GLU B OE2   1 
ATOM   8083 N N     . ALA B 1 465 ? 9.183   -75.047 40.182  1.00 47.32  ? 463 ALA B N     1 
ATOM   8084 C CA    . ALA B 1 465 ? 8.436   -73.772 40.013  1.00 48.25  ? 463 ALA B CA    1 
ATOM   8085 C C     . ALA B 1 465 ? 7.169   -73.990 39.158  1.00 43.84  ? 463 ALA B C     1 
ATOM   8086 O O     . ALA B 1 465 ? 6.188   -73.285 39.419  1.00 48.51  ? 463 ALA B O     1 
ATOM   8087 C CB    . ALA B 1 465 ? 9.340   -72.711 39.434  1.00 48.21  ? 463 ALA B CB    1 
ATOM   8088 N N     . LEU B 1 466 ? 7.174   -74.942 38.211  1.00 43.08  ? 464 LEU B N     1 
ATOM   8089 C CA    . LEU B 1 466 ? 6.045   -75.226 37.267  1.00 44.04  ? 464 LEU B CA    1 
ATOM   8090 C C     . LEU B 1 466 ? 4.965   -76.028 38.006  1.00 46.60  ? 464 LEU B C     1 
ATOM   8091 O O     . LEU B 1 466 ? 3.770   -75.796 37.746  1.00 47.00  ? 464 LEU B O     1 
ATOM   8092 C CB    . LEU B 1 466 ? 6.569   -75.968 36.025  1.00 39.48  ? 464 LEU B CB    1 
ATOM   8093 C CG    . LEU B 1 466 ? 5.532   -76.427 34.993  1.00 40.05  ? 464 LEU B CG    1 
ATOM   8094 C CD1   . LEU B 1 466 ? 4.743   -75.253 34.427  1.00 44.05  ? 464 LEU B CD1   1 
ATOM   8095 C CD2   . LEU B 1 466 ? 6.177   -77.180 33.839  1.00 41.33  ? 464 LEU B CD2   1 
ATOM   8096 N N     . LYS B 1 467 ? 5.383   -76.848 38.975  1.00 54.60  ? 465 LYS B N     1 
ATOM   8097 C CA    . LYS B 1 467 ? 4.579   -77.944 39.578  1.00 53.14  ? 465 LYS B CA    1 
ATOM   8098 C C     . LYS B 1 467 ? 3.398   -77.378 40.375  1.00 51.52  ? 465 LYS B C     1 
ATOM   8099 O O     . LYS B 1 467 ? 2.312   -78.003 40.327  1.00 55.63  ? 465 LYS B O     1 
ATOM   8100 C CB    . LYS B 1 467 ? 5.449   -78.840 40.460  1.00 58.14  ? 465 LYS B CB    1 
ATOM   8101 C CG    . LYS B 1 467 ? 5.274   -80.323 40.167  1.00 64.91  ? 465 LYS B CG    1 
ATOM   8102 C CD    . LYS B 1 467 ? 6.218   -80.821 39.107  1.00 67.58  ? 465 LYS B CD    1 
ATOM   8103 C CE    . LYS B 1 467 ? 5.690   -82.031 38.369  1.00 70.44  ? 465 LYS B CE    1 
ATOM   8104 N NZ    . LYS B 1 467 ? 6.751   -83.056 38.241  1.00 71.56  ? 465 LYS B NZ    1 
ATOM   8105 N N     . GLY B 1 468 ? 3.605   -76.270 41.093  1.00 49.69  ? 466 GLY B N     1 
ATOM   8106 C CA    . GLY B 1 468 ? 2.542   -75.509 41.781  1.00 47.51  ? 466 GLY B CA    1 
ATOM   8107 C C     . GLY B 1 468 ? 1.323   -75.338 40.880  1.00 49.80  ? 466 GLY B C     1 
ATOM   8108 O O     . GLY B 1 468 ? 0.207   -75.706 41.311  1.00 53.58  ? 466 GLY B O     1 
ATOM   8109 N N     . PHE B 1 469 ? 1.538   -74.869 39.643  1.00 47.46  ? 467 PHE B N     1 
ATOM   8110 C CA    . PHE B 1 469 ? 0.470   -74.549 38.660  1.00 42.64  ? 467 PHE B CA    1 
ATOM   8111 C C     . PHE B 1 469 ? -0.060  -75.835 38.003  1.00 36.62  ? 467 PHE B C     1 
ATOM   8112 O O     . PHE B 1 469 ? -1.281  -75.986 37.941  1.00 38.40  ? 467 PHE B O     1 
ATOM   8113 C CB    . PHE B 1 469 ? 0.921   -73.498 37.638  1.00 42.55  ? 467 PHE B CB    1 
ATOM   8114 C CG    . PHE B 1 469 ? -0.259  -72.888 36.914  1.00 46.71  ? 467 PHE B CG    1 
ATOM   8115 C CD1   . PHE B 1 469 ? -0.981  -71.848 37.485  1.00 45.15  ? 467 PHE B CD1   1 
ATOM   8116 C CD2   . PHE B 1 469 ? -0.717  -73.428 35.718  1.00 44.85  ? 467 PHE B CD2   1 
ATOM   8117 C CE1   . PHE B 1 469 ? -2.102  -71.330 36.852  1.00 46.55  ? 467 PHE B CE1   1 
ATOM   8118 C CE2   . PHE B 1 469 ? -1.843  -72.908 35.090  1.00 46.48  ? 467 PHE B CE2   1 
ATOM   8119 C CZ    . PHE B 1 469 ? -2.534  -71.861 35.658  1.00 45.20  ? 467 PHE B CZ    1 
ATOM   8120 N N     . THR B 1 470 ? 0.796   -76.730 37.524  1.00 35.57  ? 468 THR B N     1 
ATOM   8121 C CA    . THR B 1 470 ? 0.370   -77.961 36.808  1.00 40.62  ? 468 THR B CA    1 
ATOM   8122 C C     . THR B 1 470 ? -0.351  -78.915 37.773  1.00 44.04  ? 468 THR B C     1 
ATOM   8123 O O     . THR B 1 470 ? -1.159  -79.746 37.296  1.00 44.67  ? 468 THR B O     1 
ATOM   8124 C CB    . THR B 1 470 ? 1.549   -78.638 36.096  1.00 42.21  ? 468 THR B CB    1 
ATOM   8125 O OG1   . THR B 1 470 ? 2.623   -78.810 37.018  1.00 42.41  ? 468 THR B OG1   1 
ATOM   8126 C CG2   . THR B 1 470 ? 2.058   -77.838 34.919  1.00 40.45  ? 468 THR B CG2   1 
ATOM   8127 N N     . LYS B 1 471 ? -0.094  -78.789 39.080  1.00 51.80  ? 469 LYS B N     1 
ATOM   8128 C CA    . LYS B 1 471 ? -0.887  -79.460 40.138  1.00 49.18  ? 469 LYS B CA    1 
ATOM   8129 C C     . LYS B 1 471 ? -2.350  -78.979 40.058  1.00 46.21  ? 469 LYS B C     1 
ATOM   8130 O O     . LYS B 1 471 ? -3.220  -79.852 39.866  1.00 48.40  ? 469 LYS B O     1 
ATOM   8131 C CB    . LYS B 1 471 ? -0.263  -79.201 41.510  1.00 56.09  ? 469 LYS B CB    1 
ATOM   8132 C CG    . LYS B 1 471 ? -1.008  -79.854 42.666  1.00 65.87  ? 469 LYS B CG    1 
ATOM   8133 C CD    . LYS B 1 471 ? -0.240  -79.834 43.961  1.00 70.81  ? 469 LYS B CD    1 
ATOM   8134 C CE    . LYS B 1 471 ? -0.869  -80.692 45.035  1.00 71.51  ? 469 LYS B CE    1 
ATOM   8135 N NZ    . LYS B 1 471 ? 0.179   -81.137 45.980  1.00 73.01  ? 469 LYS B NZ    1 
ATOM   8136 N N     . ILE B 1 472 ? -2.625  -77.666 40.195  1.00 43.15  ? 470 ILE B N     1 
ATOM   8137 C CA    . ILE B 1 472 ? -4.003  -77.079 40.110  1.00 40.48  ? 470 ILE B CA    1 
ATOM   8138 C C     . ILE B 1 472 ? -4.679  -77.532 38.813  1.00 39.99  ? 470 ILE B C     1 
ATOM   8139 O O     . ILE B 1 472 ? -5.846  -77.981 38.884  1.00 51.95  ? 470 ILE B O     1 
ATOM   8140 C CB    . ILE B 1 472 ? -4.031  -75.544 40.251  1.00 45.01  ? 470 ILE B CB    1 
ATOM   8141 C CG1   . ILE B 1 472 ? -3.575  -75.093 41.642  1.00 46.43  ? 470 ILE B CG1   1 
ATOM   8142 C CG2   . ILE B 1 472 ? -5.423  -74.997 39.925  1.00 40.64  ? 470 ILE B CG2   1 
ATOM   8143 C CD1   . ILE B 1 472 ? -3.131  -73.639 41.727  1.00 45.22  ? 470 ILE B CD1   1 
ATOM   8144 N N     . VAL B 1 473 ? -3.982  -77.507 37.680  1.00 37.81  ? 471 VAL B N     1 
ATOM   8145 C CA    . VAL B 1 473 ? -4.598  -77.907 36.383  1.00 37.45  ? 471 VAL B CA    1 
ATOM   8146 C C     . VAL B 1 473 ? -4.975  -79.381 36.442  1.00 41.25  ? 471 VAL B C     1 
ATOM   8147 O O     . VAL B 1 473 ? -6.063  -79.727 35.950  1.00 45.67  ? 471 VAL B O     1 
ATOM   8148 C CB    . VAL B 1 473 ? -3.671  -77.634 35.189  1.00 37.65  ? 471 VAL B CB    1 
ATOM   8149 C CG1   . VAL B 1 473 ? -4.309  -78.056 33.880  1.00 34.76  ? 471 VAL B CG1   1 
ATOM   8150 C CG2   . VAL B 1 473 ? -3.252  -76.169 35.144  1.00 39.59  ? 471 VAL B CG2   1 
ATOM   8151 N N     . HIS B 1 474 ? -4.071  -80.228 36.939  1.00 44.33  ? 472 HIS B N     1 
ATOM   8152 C CA    . HIS B 1 474 ? -4.298  -81.691 37.007  1.00 46.08  ? 472 HIS B CA    1 
ATOM   8153 C C     . HIS B 1 474 ? -5.494  -81.991 37.920  1.00 42.77  ? 472 HIS B C     1 
ATOM   8154 O O     . HIS B 1 474 ? -6.278  -82.851 37.563  1.00 41.27  ? 472 HIS B O     1 
ATOM   8155 C CB    . HIS B 1 474 ? -3.039  -82.423 37.454  1.00 47.59  ? 472 HIS B CB    1 
ATOM   8156 C CG    . HIS B 1 474 ? -3.253  -83.896 37.539  1.00 51.50  ? 472 HIS B CG    1 
ATOM   8157 N ND1   . HIS B 1 474 ? -3.476  -84.667 36.414  1.00 53.55  ? 472 HIS B ND1   1 
ATOM   8158 C CD2   . HIS B 1 474 ? -3.313  -84.732 38.599  1.00 50.64  ? 472 HIS B CD2   1 
ATOM   8159 C CE1   . HIS B 1 474 ? -3.653  -85.918 36.769  1.00 51.91  ? 472 HIS B CE1   1 
ATOM   8160 N NE2   . HIS B 1 474 ? -3.534  -85.988 38.103  1.00 52.90  ? 472 HIS B NE2   1 
ATOM   8161 N N     . LYS B 1 475 ? -5.639  -81.278 39.037  1.00 47.44  ? 473 LYS B N     1 
ATOM   8162 C CA    . LYS B 1 475 ? -6.807  -81.409 39.953  1.00 53.78  ? 473 LYS B CA    1 
ATOM   8163 C C     . LYS B 1 475 ? -8.105  -80.994 39.249  1.00 51.48  ? 473 LYS B C     1 
ATOM   8164 O O     . LYS B 1 475 ? -9.104  -81.657 39.497  1.00 53.03  ? 473 LYS B O     1 
ATOM   8165 C CB    . LYS B 1 475 ? -6.614  -80.577 41.223  1.00 59.45  ? 473 LYS B CB    1 
ATOM   8166 C CG    . LYS B 1 475 ? -5.537  -81.100 42.156  1.00 70.11  ? 473 LYS B CG    1 
ATOM   8167 C CD    . LYS B 1 475 ? -5.746  -80.716 43.604  1.00 80.40  ? 473 LYS B CD    1 
ATOM   8168 C CE    . LYS B 1 475 ? -6.953  -81.389 44.223  1.00 79.48  ? 473 LYS B CE    1 
ATOM   8169 N NZ    . LYS B 1 475 ? -6.564  -82.129 45.445  1.00 82.54  ? 473 LYS B NZ    1 
ATOM   8170 N N     . PHE B 1 476 ? -8.091  -79.962 38.393  1.00 51.22  ? 474 PHE B N     1 
ATOM   8171 C CA    . PHE B 1 476 ? -9.286  -79.486 37.636  1.00 47.78  ? 474 PHE B CA    1 
ATOM   8172 C C     . PHE B 1 476 ? -9.737  -80.575 36.642  1.00 48.69  ? 474 PHE B C     1 
ATOM   8173 O O     . PHE B 1 476 ? -10.938 -80.883 36.534  1.00 48.50  ? 474 PHE B O     1 
ATOM   8174 C CB    . PHE B 1 476 ? -9.003  -78.126 36.969  1.00 48.53  ? 474 PHE B CB    1 
ATOM   8175 C CG    . PHE B 1 476 ? -10.083 -77.619 36.039  1.00 45.04  ? 474 PHE B CG    1 
ATOM   8176 C CD1   . PHE B 1 476 ? -10.167 -78.067 34.731  1.00 44.24  ? 474 PHE B CD1   1 
ATOM   8177 C CD2   . PHE B 1 476 ? -11.047 -76.729 36.488  1.00 42.04  ? 474 PHE B CD2   1 
ATOM   8178 C CE1   . PHE B 1 476 ? -11.194 -77.637 33.900  1.00 48.98  ? 474 PHE B CE1   1 
ATOM   8179 C CE2   . PHE B 1 476 ? -12.058 -76.292 35.655  1.00 41.67  ? 474 PHE B CE2   1 
ATOM   8180 C CZ    . PHE B 1 476 ? -12.136 -76.746 34.362  1.00 43.11  ? 474 PHE B CZ    1 
ATOM   8181 N N     . CYS B 1 477 ? -8.811  -81.148 35.879  1.00 53.26  ? 475 CYS B N     1 
ATOM   8182 C CA    . CYS B 1 477 ? -9.137  -82.173 34.848  1.00 52.67  ? 475 CYS B CA    1 
ATOM   8183 C C     . CYS B 1 477 ? -9.689  -83.447 35.513  1.00 54.57  ? 475 CYS B C     1 
ATOM   8184 O O     . CYS B 1 477 ? -10.485 -84.174 34.856  1.00 50.62  ? 475 CYS B O     1 
ATOM   8185 C CB    . CYS B 1 477 ? -7.916  -82.474 33.990  1.00 48.36  ? 475 CYS B CB    1 
ATOM   8186 S SG    . CYS B 1 477 ? -7.285  -80.976 33.205  1.00 49.69  ? 475 CYS B SG    1 
ATOM   8187 N N     . GLN B 1 478 ? -9.287  -83.712 36.761  1.00 53.00  ? 476 GLN B N     1 
ATOM   8188 C CA    . GLN B 1 478 ? -9.737  -84.900 37.539  1.00 52.42  ? 476 GLN B CA    1 
ATOM   8189 C C     . GLN B 1 478 ? -11.152 -84.666 38.068  1.00 46.20  ? 476 GLN B C     1 
ATOM   8190 O O     . GLN B 1 478 ? -12.020 -85.522 37.859  1.00 52.54  ? 476 GLN B O     1 
ATOM   8191 C CB    . GLN B 1 478 ? -8.778  -85.175 38.690  1.00 55.08  ? 476 GLN B CB    1 
ATOM   8192 C CG    . GLN B 1 478 ? -7.575  -86.008 38.284  1.00 57.33  ? 476 GLN B CG    1 
ATOM   8193 C CD    . GLN B 1 478 ? -6.780  -86.387 39.506  1.00 67.24  ? 476 GLN B CD    1 
ATOM   8194 O OE1   . GLN B 1 478 ? -6.575  -85.572 40.406  1.00 79.11  ? 476 GLN B OE1   1 
ATOM   8195 N NE2   . GLN B 1 478 ? -6.340  -87.635 39.558  1.00 69.53  ? 476 GLN B NE2   1 
ATOM   8196 N N     . ALA B 1 479 ? -11.396 -83.513 38.674  1.00 44.09  ? 477 ALA B N     1 
ATOM   8197 C CA    . ALA B 1 479 ? -12.699 -83.185 39.280  1.00 41.28  ? 477 ALA B CA    1 
ATOM   8198 C C     . ALA B 1 479 ? -13.759 -82.979 38.195  1.00 47.71  ? 477 ALA B C     1 
ATOM   8199 O O     . ALA B 1 479 ? -14.960 -83.065 38.523  1.00 52.83  ? 477 ALA B O     1 
ATOM   8200 C CB    . ALA B 1 479 ? -12.545 -81.972 40.148  1.00 40.52  ? 477 ALA B CB    1 
ATOM   8201 N N     . ASN B 1 480 ? -13.351 -82.692 36.956  1.00 51.17  ? 478 ASN B N     1 
ATOM   8202 C CA    . ASN B 1 480 ? -14.276 -82.260 35.876  1.00 49.27  ? 478 ASN B CA    1 
ATOM   8203 C C     . ASN B 1 480 ? -14.163 -83.182 34.672  1.00 51.76  ? 478 ASN B C     1 
ATOM   8204 O O     . ASN B 1 480 ? -14.759 -82.831 33.661  1.00 48.59  ? 478 ASN B O     1 
ATOM   8205 C CB    . ASN B 1 480 ? -13.974 -80.844 35.399  1.00 48.81  ? 478 ASN B CB    1 
ATOM   8206 C CG    . ASN B 1 480 ? -14.414 -79.788 36.384  1.00 47.93  ? 478 ASN B CG    1 
ATOM   8207 O OD1   . ASN B 1 480 ? -15.600 -79.453 36.421  1.00 48.41  ? 478 ASN B OD1   1 
ATOM   8208 N ND2   . ASN B 1 480 ? -13.469 -79.230 37.138  1.00 44.04  ? 478 ASN B ND2   1 
ATOM   8209 N N     . GLU B 1 481 ? -13.445 -84.303 34.787  1.00 53.95  ? 479 GLU B N     1 
ATOM   8210 C CA    . GLU B 1 481 ? -13.229 -85.238 33.660  1.00 56.74  ? 479 GLU B CA    1 
ATOM   8211 C C     . GLU B 1 481 ? -14.571 -85.764 33.138  1.00 57.25  ? 479 GLU B C     1 
ATOM   8212 O O     . GLU B 1 481 ? -14.678 -85.991 31.915  1.00 59.41  ? 479 GLU B O     1 
ATOM   8213 C CB    . GLU B 1 481 ? -12.386 -86.441 34.078  1.00 66.60  ? 479 GLU B CB    1 
ATOM   8214 C CG    . GLU B 1 481 ? -12.273 -87.442 32.945  1.00 75.36  ? 479 GLU B CG    1 
ATOM   8215 C CD    . GLU B 1 481 ? -11.430 -88.663 33.218  1.00 84.34  ? 479 GLU B CD    1 
ATOM   8216 O OE1   . GLU B 1 481 ? -11.729 -89.709 32.607  1.00 85.03  ? 479 GLU B OE1   1 
ATOM   8217 O OE2   . GLU B 1 481 ? -10.479 -88.556 34.023  1.00 84.19  ? 479 GLU B OE2   1 
ATOM   8218 N N     . ALA B 1 482 ? -15.523 -86.051 34.032  1.00 54.43  ? 480 ALA B N     1 
ATOM   8219 C CA    . ALA B 1 482 ? -16.839 -86.649 33.688  1.00 59.58  ? 480 ALA B CA    1 
ATOM   8220 C C     . ALA B 1 482 ? -17.960 -85.585 33.745  1.00 58.82  ? 480 ALA B C     1 
ATOM   8221 O O     . ALA B 1 482 ? -19.143 -85.956 33.642  1.00 62.68  ? 480 ALA B O     1 
ATOM   8222 C CB    . ALA B 1 482 ? -17.115 -87.841 34.578  1.00 54.81  ? 480 ALA B CB    1 
ATOM   8223 N N     . ASN B 1 483 ? -17.600 -84.303 33.842  1.00 53.86  ? 481 ASN B N     1 
ATOM   8224 C CA    . ASN B 1 483 ? -18.505 -83.142 33.635  1.00 50.13  ? 481 ASN B CA    1 
ATOM   8225 C C     . ASN B 1 483 ? -18.770 -82.956 32.141  1.00 48.83  ? 481 ASN B C     1 
ATOM   8226 O O     . ASN B 1 483 ? -17.872 -82.505 31.440  1.00 52.53  ? 481 ASN B O     1 
ATOM   8227 C CB    . ASN B 1 483 ? -17.892 -81.878 34.215  1.00 48.83  ? 481 ASN B CB    1 
ATOM   8228 C CG    . ASN B 1 483 ? -18.849 -80.708 34.249  1.00 49.95  ? 481 ASN B CG    1 
ATOM   8229 O OD1   . ASN B 1 483 ? -19.893 -80.702 33.597  1.00 47.15  ? 481 ASN B OD1   1 
ATOM   8230 N ND2   . ASN B 1 483 ? -18.483 -79.696 35.011  1.00 48.74  ? 481 ASN B ND2   1 
ATOM   8231 N N     . GLU B 1 484 ? -19.977 -83.284 31.690  1.00 57.33  ? 482 GLU B N     1 
ATOM   8232 C CA    . GLU B 1 484 ? -20.391 -83.314 30.255  1.00 62.93  ? 482 GLU B CA    1 
ATOM   8233 C C     . GLU B 1 484 ? -20.256 -81.936 29.579  1.00 53.43  ? 482 GLU B C     1 
ATOM   8234 O O     . GLU B 1 484 ? -19.980 -81.927 28.367  1.00 49.63  ? 482 GLU B O     1 
ATOM   8235 C CB    . GLU B 1 484 ? -21.835 -83.813 30.129  1.00 75.51  ? 482 GLU B CB    1 
ATOM   8236 C CG    . GLU B 1 484 ? -21.953 -85.326 30.083  1.00 83.20  ? 482 GLU B CG    1 
ATOM   8237 C CD    . GLU B 1 484 ? -21.616 -85.897 28.717  1.00 85.79  ? 482 GLU B CD    1 
ATOM   8238 O OE1   . GLU B 1 484 ? -22.330 -85.574 27.736  1.00 79.77  ? 482 GLU B OE1   1 
ATOM   8239 O OE2   . GLU B 1 484 ? -20.624 -86.631 28.634  1.00 91.09  ? 482 GLU B OE2   1 
ATOM   8240 N N     . ALA B 1 485 ? -20.472 -80.831 30.303  1.00 45.58  ? 483 ALA B N     1 
ATOM   8241 C CA    . ALA B 1 485 ? -20.495 -79.457 29.740  1.00 47.18  ? 483 ALA B CA    1 
ATOM   8242 C C     . ALA B 1 485 ? -19.073 -78.992 29.388  1.00 49.84  ? 483 ALA B C     1 
ATOM   8243 O O     . ALA B 1 485 ? -18.926 -78.174 28.460  1.00 55.28  ? 483 ALA B O     1 
ATOM   8244 C CB    . ALA B 1 485 ? -21.176 -78.514 30.712  1.00 46.62  ? 483 ALA B CB    1 
ATOM   8245 N N     . VAL B 1 486 ? -18.044 -79.479 30.089  1.00 52.53  ? 484 VAL B N     1 
ATOM   8246 C CA    . VAL B 1 486 ? -16.634 -79.051 29.840  1.00 50.72  ? 484 VAL B CA    1 
ATOM   8247 C C     . VAL B 1 486 ? -15.764 -80.252 29.449  1.00 54.09  ? 484 VAL B C     1 
ATOM   8248 O O     . VAL B 1 486 ? -14.535 -80.139 29.560  1.00 57.30  ? 484 VAL B O     1 
ATOM   8249 C CB    . VAL B 1 486 ? -16.052 -78.277 31.040  1.00 46.86  ? 484 VAL B CB    1 
ATOM   8250 C CG1   . VAL B 1 486 ? -16.924 -77.087 31.404  1.00 51.69  ? 484 VAL B CG1   1 
ATOM   8251 C CG2   . VAL B 1 486 ? -15.814 -79.161 32.245  1.00 46.41  ? 484 VAL B CG2   1 
ATOM   8252 N N     . LYS B 1 487 ? -16.365 -81.345 28.978  1.00 57.97  ? 485 LYS B N     1 
ATOM   8253 C CA    . LYS B 1 487 ? -15.637 -82.495 28.381  1.00 59.46  ? 485 LYS B CA    1 
ATOM   8254 C C     . LYS B 1 487 ? -14.635 -81.983 27.347  1.00 58.61  ? 485 LYS B C     1 
ATOM   8255 O O     . LYS B 1 487 ? -13.466 -82.424 27.381  1.00 57.07  ? 485 LYS B O     1 
ATOM   8256 C CB    . LYS B 1 487 ? -16.592 -83.453 27.659  1.00 64.60  ? 485 LYS B CB    1 
ATOM   8257 C CG    . LYS B 1 487 ? -16.420 -84.913 28.045  1.00 74.33  ? 485 LYS B CG    1 
ATOM   8258 C CD    . LYS B 1 487 ? -16.750 -85.176 29.517  1.00 79.77  ? 485 LYS B CD    1 
ATOM   8259 C CE    . LYS B 1 487 ? -16.839 -86.647 29.876  1.00 75.00  ? 485 LYS B CE    1 
ATOM   8260 N NZ    . LYS B 1 487 ? -17.906 -87.333 29.115  1.00 70.37  ? 485 LYS B NZ    1 
ATOM   8261 N N     . GLU B 1 488 ? -15.109 -81.114 26.450  1.00 53.55  ? 486 GLU B N     1 
ATOM   8262 C CA    . GLU B 1 488 ? -14.362 -80.639 25.258  1.00 54.14  ? 486 GLU B CA    1 
ATOM   8263 C C     . GLU B 1 488 ? -13.153 -79.789 25.680  1.00 47.47  ? 486 GLU B C     1 
ATOM   8264 O O     . GLU B 1 488 ? -12.199 -79.773 24.916  1.00 49.10  ? 486 GLU B O     1 
ATOM   8265 C CB    . GLU B 1 488 ? -15.289 -79.859 24.321  1.00 57.30  ? 486 GLU B CB    1 
ATOM   8266 C CG    . GLU B 1 488 ? -15.948 -78.656 24.972  1.00 59.36  ? 486 GLU B CG    1 
ATOM   8267 C CD    . GLU B 1 488 ? -16.814 -77.823 24.040  1.00 62.94  ? 486 GLU B CD    1 
ATOM   8268 O OE1   . GLU B 1 488 ? -17.939 -77.481 24.457  1.00 50.70  ? 486 GLU B OE1   1 
ATOM   8269 O OE2   . GLU B 1 488 ? -16.354 -77.491 22.912  1.00 65.09  ? 486 GLU B OE2   1 
ATOM   8270 N N     . PHE B 1 489 ? -13.210 -79.107 26.829  1.00 45.61  ? 487 PHE B N     1 
ATOM   8271 C CA    . PHE B 1 489 ? -12.130 -78.257 27.404  1.00 47.27  ? 487 PHE B CA    1 
ATOM   8272 C C     . PHE B 1 489 ? -11.139 -79.131 28.183  1.00 47.77  ? 487 PHE B C     1 
ATOM   8273 O O     . PHE B 1 489 ? -9.920  -78.943 28.024  1.00 47.07  ? 487 PHE B O     1 
ATOM   8274 C CB    . PHE B 1 489 ? -12.696 -77.132 28.281  1.00 43.81  ? 487 PHE B CB    1 
ATOM   8275 C CG    . PHE B 1 489 ? -13.686 -76.262 27.555  1.00 49.32  ? 487 PHE B CG    1 
ATOM   8276 C CD1   . PHE B 1 489 ? -13.292 -75.517 26.450  1.00 51.31  ? 487 PHE B CD1   1 
ATOM   8277 C CD2   . PHE B 1 489 ? -15.028 -76.242 27.911  1.00 47.86  ? 487 PHE B CD2   1 
ATOM   8278 C CE1   . PHE B 1 489 ? -14.213 -74.750 25.747  1.00 47.80  ? 487 PHE B CE1   1 
ATOM   8279 C CE2   . PHE B 1 489 ? -15.950 -75.488 27.197  1.00 44.68  ? 487 PHE B CE2   1 
ATOM   8280 C CZ    . PHE B 1 489 ? -15.541 -74.745 26.117  1.00 47.87  ? 487 PHE B CZ    1 
ATOM   8281 N N     . VAL B 1 490 ? -11.628 -80.071 28.998  1.00 55.60  ? 488 VAL B N     1 
ATOM   8282 C CA    . VAL B 1 490 ? -10.771 -80.873 29.936  1.00 50.27  ? 488 VAL B CA    1 
ATOM   8283 C C     . VAL B 1 490 ? -9.813  -81.762 29.126  1.00 46.01  ? 488 VAL B C     1 
ATOM   8284 O O     . VAL B 1 490 ? -8.639  -81.802 29.465  1.00 47.60  ? 488 VAL B O     1 
ATOM   8285 C CB    . VAL B 1 490 ? -11.631 -81.673 30.927  1.00 46.32  ? 488 VAL B CB    1 
ATOM   8286 C CG1   . VAL B 1 490 ? -10.847 -82.782 31.601  1.00 48.44  ? 488 VAL B CG1   1 
ATOM   8287 C CG2   . VAL B 1 490 ? -12.263 -80.746 31.958  1.00 46.01  ? 488 VAL B CG2   1 
ATOM   8288 N N     . ALA B 1 491 ? -10.282 -82.403 28.059  1.00 44.35  ? 489 ALA B N     1 
ATOM   8289 C CA    . ALA B 1 491 ? -9.472  -83.345 27.257  1.00 46.85  ? 489 ALA B CA    1 
ATOM   8290 C C     . ALA B 1 491 ? -8.196  -82.644 26.792  1.00 43.85  ? 489 ALA B C     1 
ATOM   8291 O O     . ALA B 1 491 ? -7.112  -83.025 27.230  1.00 47.46  ? 489 ALA B O     1 
ATOM   8292 C CB    . ALA B 1 491 ? -10.281 -83.910 26.107  1.00 49.22  ? 489 ALA B CB    1 
ATOM   8293 N N     . PRO B 1 492 ? -8.270  -81.614 25.910  1.00 43.49  ? 490 PRO B N     1 
ATOM   8294 C CA    . PRO B 1 492 ? -7.069  -80.900 25.460  1.00 41.62  ? 490 PRO B CA    1 
ATOM   8295 C C     . PRO B 1 492 ? -6.310  -80.183 26.584  1.00 39.72  ? 490 PRO B C     1 
ATOM   8296 O O     . PRO B 1 492 ? -5.131  -79.997 26.424  1.00 41.84  ? 490 PRO B O     1 
ATOM   8297 C CB    . PRO B 1 492 ? -7.554  -79.860 24.440  1.00 41.56  ? 490 PRO B CB    1 
ATOM   8298 C CG    . PRO B 1 492 ? -9.077  -79.834 24.582  1.00 41.91  ? 490 PRO B CG    1 
ATOM   8299 C CD    . PRO B 1 492 ? -9.481  -81.158 25.203  1.00 43.31  ? 490 PRO B CD    1 
ATOM   8300 N N     . LEU B 1 493 ? -6.975  -79.808 27.680  1.00 38.05  ? 491 LEU B N     1 
ATOM   8301 C CA    . LEU B 1 493 ? -6.293  -79.171 28.836  1.00 41.53  ? 491 LEU B CA    1 
ATOM   8302 C C     . LEU B 1 493 ? -5.391  -80.210 29.526  1.00 42.59  ? 491 LEU B C     1 
ATOM   8303 O O     . LEU B 1 493 ? -4.185  -79.887 29.802  1.00 39.32  ? 491 LEU B O     1 
ATOM   8304 C CB    . LEU B 1 493 ? -7.301  -78.553 29.812  1.00 40.85  ? 491 LEU B CB    1 
ATOM   8305 C CG    . LEU B 1 493 ? -6.657  -77.792 30.974  1.00 43.03  ? 491 LEU B CG    1 
ATOM   8306 C CD1   . LEU B 1 493 ? -5.792  -76.645 30.470  1.00 44.47  ? 491 LEU B CD1   1 
ATOM   8307 C CD2   . LEU B 1 493 ? -7.691  -77.284 31.966  1.00 42.78  ? 491 LEU B CD2   1 
ATOM   8308 N N     . ALA B 1 494 ? -5.910  -81.417 29.777  1.00 43.66  ? 492 ALA B N     1 
ATOM   8309 C CA    . ALA B 1 494 ? -5.120  -82.524 30.382  1.00 42.69  ? 492 ALA B CA    1 
ATOM   8310 C C     . ALA B 1 494 ? -3.930  -82.805 29.460  1.00 42.29  ? 492 ALA B C     1 
ATOM   8311 O O     . ALA B 1 494 ? -2.810  -82.837 29.945  1.00 38.81  ? 492 ALA B O     1 
ATOM   8312 C CB    . ALA B 1 494 ? -5.969  -83.756 30.611  1.00 41.90  ? 492 ALA B CB    1 
ATOM   8313 N N     . GLN B 1 495 ? -4.169  -82.931 28.156  1.00 42.30  ? 493 GLN B N     1 
ATOM   8314 C CA    . GLN B 1 495 ? -3.083  -83.217 27.186  1.00 47.32  ? 493 GLN B CA    1 
ATOM   8315 C C     . GLN B 1 495 ? -2.006  -82.124 27.256  1.00 42.59  ? 493 GLN B C     1 
ATOM   8316 O O     . GLN B 1 495 ? -0.839  -82.460 27.352  1.00 44.94  ? 493 GLN B O     1 
ATOM   8317 C CB    . GLN B 1 495 ? -3.656  -83.376 25.785  1.00 47.30  ? 493 GLN B CB    1 
ATOM   8318 C CG    . GLN B 1 495 ? -2.664  -83.959 24.802  1.00 52.82  ? 493 GLN B CG    1 
ATOM   8319 C CD    . GLN B 1 495 ? -3.398  -84.292 23.530  1.00 65.47  ? 493 GLN B CD    1 
ATOM   8320 O OE1   . GLN B 1 495 ? -4.280  -85.151 23.505  1.00 77.70  ? 493 GLN B OE1   1 
ATOM   8321 N NE2   . GLN B 1 495 ? -3.076  -83.577 22.467  1.00 63.51  ? 493 GLN B NE2   1 
ATOM   8322 N N     . LEU B 1 496 ? -2.390  -80.859 27.238  1.00 38.61  ? 494 LEU B N     1 
ATOM   8323 C CA    . LEU B 1 496 ? -1.444  -79.722 27.252  1.00 36.80  ? 494 LEU B CA    1 
ATOM   8324 C C     . LEU B 1 496 ? -0.712  -79.685 28.599  1.00 34.74  ? 494 LEU B C     1 
ATOM   8325 O O     . LEU B 1 496 ? 0.505   -79.310 28.642  1.00 31.73  ? 494 LEU B O     1 
ATOM   8326 C CB    . LEU B 1 496 ? -2.251  -78.441 27.032  1.00 39.29  ? 494 LEU B CB    1 
ATOM   8327 C CG    . LEU B 1 496 ? -1.425  -77.215 26.667  1.00 40.68  ? 494 LEU B CG    1 
ATOM   8328 C CD1   . LEU B 1 496 ? -0.972  -77.299 25.215  1.00 38.52  ? 494 LEU B CD1   1 
ATOM   8329 C CD2   . LEU B 1 496 ? -2.211  -75.948 26.927  1.00 41.05  ? 494 LEU B CD2   1 
ATOM   8330 N N     . ASN B 1 497 ? -1.407  -80.038 29.680  1.00 36.00  ? 495 ASN B N     1 
ATOM   8331 C CA    . ASN B 1 497 ? -0.790  -80.019 31.032  1.00 38.10  ? 495 ASN B CA    1 
ATOM   8332 C C     . ASN B 1 497 ? 0.355   -81.042 31.047  1.00 40.35  ? 495 ASN B C     1 
ATOM   8333 O O     . ASN B 1 497 ? 1.434   -80.721 31.536  1.00 45.01  ? 495 ASN B O     1 
ATOM   8334 C CB    . ASN B 1 497 ? -1.816  -80.225 32.144  1.00 37.06  ? 495 ASN B CB    1 
ATOM   8335 C CG    . ASN B 1 497 ? -1.354  -79.671 33.478  1.00 38.47  ? 495 ASN B CG    1 
ATOM   8336 O OD1   . ASN B 1 497 ? -0.751  -78.600 33.564  1.00 37.57  ? 495 ASN B OD1   1 
ATOM   8337 N ND2   . ASN B 1 497 ? -1.613  -80.409 34.542  1.00 38.74  ? 495 ASN B ND2   1 
ATOM   8338 N N     . LYS B 1 498 ? 0.162   -82.205 30.447  1.00 38.06  ? 496 LYS B N     1 
ATOM   8339 C CA    . LYS B 1 498 ? 1.232   -83.212 30.351  1.00 43.29  ? 496 LYS B CA    1 
ATOM   8340 C C     . LYS B 1 498 ? 2.400   -82.598 29.565  1.00 42.84  ? 496 LYS B C     1 
ATOM   8341 O O     . LYS B 1 498 ? 3.554   -82.617 30.051  1.00 43.06  ? 496 LYS B O     1 
ATOM   8342 C CB    . LYS B 1 498 ? 0.694   -84.504 29.722  1.00 48.08  ? 496 LYS B CB    1 
ATOM   8343 C CG    . LYS B 1 498 ? 1.513   -85.755 30.042  1.00 55.51  ? 496 LYS B CG    1 
ATOM   8344 C CD    . LYS B 1 498 ? 0.952   -87.076 29.484  1.00 64.49  ? 496 LYS B CD    1 
ATOM   8345 C CE    . LYS B 1 498 ? 0.893   -87.173 27.966  1.00 68.01  ? 496 LYS B CE    1 
ATOM   8346 N NZ    . LYS B 1 498 ? 2.150   -87.696 27.360  1.00 59.67  ? 496 LYS B NZ    1 
ATOM   8347 N N     . GLU B 1 499 ? 2.106   -82.076 28.380  1.00 42.34  ? 497 GLU B N     1 
ATOM   8348 C CA    . GLU B 1 499 ? 3.119   -81.679 27.379  1.00 40.96  ? 497 GLU B CA    1 
ATOM   8349 C C     . GLU B 1 499 ? 3.937   -80.552 28.013  1.00 40.26  ? 497 GLU B C     1 
ATOM   8350 O O     . GLU B 1 499 ? 5.177   -80.550 27.884  1.00 45.06  ? 497 GLU B O     1 
ATOM   8351 C CB    . GLU B 1 499 ? 2.401   -81.376 26.063  1.00 37.94  ? 497 GLU B CB    1 
ATOM   8352 C CG    . GLU B 1 499 ? 3.325   -80.988 24.914  1.00 39.12  ? 497 GLU B CG    1 
ATOM   8353 C CD    . GLU B 1 499 ? 2.652   -80.062 23.908  1.00 37.55  ? 497 GLU B CD    1 
ATOM   8354 O OE1   . GLU B 1 499 ? 2.963   -80.183 22.731  1.00 34.68  ? 497 GLU B OE1   1 
ATOM   8355 O OE2   . GLU B 1 499 ? 1.815   -79.202 24.303  1.00 36.43  ? 497 GLU B OE2   1 
ATOM   8356 N N     . TRP B 1 500 ? 3.278   -79.659 28.736  1.00 38.84  ? 498 TRP B N     1 
ATOM   8357 C CA    . TRP B 1 500 ? 3.958   -78.559 29.475  1.00 40.16  ? 498 TRP B CA    1 
ATOM   8358 C C     . TRP B 1 500 ? 5.173   -79.092 30.256  1.00 38.44  ? 498 TRP B C     1 
ATOM   8359 O O     . TRP B 1 500 ? 6.277   -78.504 30.156  1.00 43.53  ? 498 TRP B O     1 
ATOM   8360 C CB    . TRP B 1 500 ? 2.949   -77.892 30.412  1.00 39.18  ? 498 TRP B CB    1 
ATOM   8361 C CG    . TRP B 1 500 ? 3.261   -76.476 30.755  1.00 36.03  ? 498 TRP B CG    1 
ATOM   8362 C CD1   . TRP B 1 500 ? 4.398   -75.779 30.475  1.00 35.19  ? 498 TRP B CD1   1 
ATOM   8363 C CD2   . TRP B 1 500 ? 2.389   -75.582 31.455  1.00 35.08  ? 498 TRP B CD2   1 
ATOM   8364 N NE1   . TRP B 1 500 ? 4.305   -74.514 30.974  1.00 34.09  ? 498 TRP B NE1   1 
ATOM   8365 C CE2   . TRP B 1 500 ? 3.075   -74.364 31.581  1.00 36.56  ? 498 TRP B CE2   1 
ATOM   8366 C CE3   . TRP B 1 500 ? 1.091   -75.693 31.962  1.00 38.79  ? 498 TRP B CE3   1 
ATOM   8367 C CZ2   . TRP B 1 500 ? 2.488   -73.253 32.189  1.00 36.66  ? 498 TRP B CZ2   1 
ATOM   8368 C CZ3   . TRP B 1 500 ? 0.523   -74.612 32.593  1.00 39.34  ? 498 TRP B CZ3   1 
ATOM   8369 C CH2   . TRP B 1 500 ? 1.213   -73.400 32.686  1.00 42.19  ? 498 TRP B CH2   1 
ATOM   8370 N N     . GLY B 1 501 ? 4.961   -80.136 31.060  1.00 41.67  ? 499 GLY B N     1 
ATOM   8371 C CA    . GLY B 1 501 ? 5.987   -80.776 31.917  1.00 40.57  ? 499 GLY B CA    1 
ATOM   8372 C C     . GLY B 1 501 ? 7.006   -81.510 31.071  1.00 40.76  ? 499 GLY B C     1 
ATOM   8373 O O     . GLY B 1 501 ? 8.201   -81.367 31.368  1.00 40.67  ? 499 GLY B O     1 
ATOM   8374 N N     . ASP B 1 502 ? 6.563   -82.213 30.015  1.00 40.34  ? 500 ASP B N     1 
ATOM   8375 C CA    . ASP B 1 502 ? 7.461   -82.974 29.095  1.00 44.19  ? 500 ASP B CA    1 
ATOM   8376 C C     . ASP B 1 502 ? 8.460   -82.004 28.461  1.00 47.02  ? 500 ASP B C     1 
ATOM   8377 O O     . ASP B 1 502 ? 9.678   -82.312 28.511  1.00 44.24  ? 500 ASP B O     1 
ATOM   8378 C CB    . ASP B 1 502 ? 6.674   -83.796 28.069  1.00 41.10  ? 500 ASP B CB    1 
ATOM   8379 C CG    . ASP B 1 502 ? 5.950   -84.942 28.761  1.00 48.26  ? 500 ASP B CG    1 
ATOM   8380 O OD1   . ASP B 1 502 ? 6.302   -85.235 29.911  1.00 65.90  ? 500 ASP B OD1   1 
ATOM   8381 O OD2   . ASP B 1 502 ? 5.027   -85.521 28.185  1.00 50.30  ? 500 ASP B OD2   1 
ATOM   8382 N N     . LEU B 1 503 ? 7.951   -80.893 27.899  1.00 46.28  ? 501 LEU B N     1 
ATOM   8383 C CA    . LEU B 1 503 ? 8.744   -79.836 27.222  1.00 41.97  ? 501 LEU B CA    1 
ATOM   8384 C C     . LEU B 1 503 ? 9.764   -79.297 28.214  1.00 37.78  ? 501 LEU B C     1 
ATOM   8385 O O     . LEU B 1 503 ? 10.901  -79.020 27.800  1.00 33.09  ? 501 LEU B O     1 
ATOM   8386 C CB    . LEU B 1 503 ? 7.823   -78.707 26.752  1.00 45.11  ? 501 LEU B CB    1 
ATOM   8387 C CG    . LEU B 1 503 ? 6.922   -79.033 25.567  1.00 46.26  ? 501 LEU B CG    1 
ATOM   8388 C CD1   . LEU B 1 503 ? 5.987   -77.870 25.286  1.00 53.08  ? 501 LEU B CD1   1 
ATOM   8389 C CD2   . LEU B 1 503 ? 7.731   -79.367 24.336  1.00 46.87  ? 501 LEU B CD2   1 
ATOM   8390 N N     . THR B 1 504 ? 9.342   -79.096 29.464  1.00 40.57  ? 502 THR B N     1 
ATOM   8391 C CA    . THR B 1 504 ? 10.193  -78.482 30.521  1.00 41.50  ? 502 THR B CA    1 
ATOM   8392 C C     . THR B 1 504 ? 11.423  -79.393 30.677  1.00 46.50  ? 502 THR B C     1 
ATOM   8393 O O     . THR B 1 504 ? 12.585  -78.876 30.667  1.00 43.01  ? 502 THR B O     1 
ATOM   8394 C CB    . THR B 1 504 ? 9.386   -78.227 31.802  1.00 36.70  ? 502 THR B CB    1 
ATOM   8395 O OG1   . THR B 1 504 ? 8.343   -77.322 31.442  1.00 34.47  ? 502 THR B OG1   1 
ATOM   8396 C CG2   . THR B 1 504 ? 10.223  -77.701 32.950  1.00 34.93  ? 502 THR B CG2   1 
ATOM   8397 N N     . MET B 1 505 ? 11.171  -80.706 30.735  1.00 46.44  ? 503 MET B N     1 
ATOM   8398 C CA    . MET B 1 505 ? 12.203  -81.771 30.870  1.00 49.13  ? 503 MET B CA    1 
ATOM   8399 C C     . MET B 1 505 ? 13.113  -81.799 29.620  1.00 46.82  ? 503 MET B C     1 
ATOM   8400 O O     . MET B 1 505 ? 14.362  -81.817 29.802  1.00 42.83  ? 503 MET B O     1 
ATOM   8401 C CB    . MET B 1 505 ? 11.543  -83.140 31.119  1.00 49.92  ? 503 MET B CB    1 
ATOM   8402 C CG    . MET B 1 505 ? 10.807  -83.261 32.482  1.00 48.76  ? 503 MET B CG    1 
ATOM   8403 S SD    . MET B 1 505 ? 11.510  -82.229 33.849  1.00 61.96  ? 503 MET B SD    1 
ATOM   8404 C CE    . MET B 1 505 ? 13.025  -83.116 34.221  1.00 60.42  ? 503 MET B CE    1 
ATOM   8405 N N     . LYS B 1 506 ? 12.546  -81.802 28.399  1.00 46.81  ? 504 LYS B N     1 
ATOM   8406 C CA    . LYS B 1 506 ? 13.335  -81.873 27.126  1.00 46.72  ? 504 LYS B CA    1 
ATOM   8407 C C     . LYS B 1 506 ? 14.278  -80.661 27.019  1.00 43.06  ? 504 LYS B C     1 
ATOM   8408 O O     . LYS B 1 506 ? 15.424  -80.817 26.598  1.00 42.99  ? 504 LYS B O     1 
ATOM   8409 C CB    . LYS B 1 506 ? 12.392  -81.985 25.929  1.00 48.68  ? 504 LYS B CB    1 
ATOM   8410 C CG    . LYS B 1 506 ? 11.656  -83.309 25.867  1.00 53.35  ? 504 LYS B CG    1 
ATOM   8411 C CD    . LYS B 1 506 ? 10.459  -83.312 24.950  1.00 57.25  ? 504 LYS B CD    1 
ATOM   8412 C CE    . LYS B 1 506 ? 10.605  -84.331 23.846  1.00 60.89  ? 504 LYS B CE    1 
ATOM   8413 N NZ    . LYS B 1 506 ? 9.289   -84.701 23.286  1.00 64.84  ? 504 LYS B NZ    1 
ATOM   8414 N N     . VAL B 1 507 ? 13.805  -79.494 27.436  1.00 43.61  ? 505 VAL B N     1 
ATOM   8415 C CA    . VAL B 1 507 ? 14.551  -78.211 27.384  1.00 43.31  ? 505 VAL B CA    1 
ATOM   8416 C C     . VAL B 1 507 ? 15.696  -78.263 28.412  1.00 42.03  ? 505 VAL B C     1 
ATOM   8417 O O     . VAL B 1 507 ? 16.805  -77.834 28.037  1.00 38.94  ? 505 VAL B O     1 
ATOM   8418 C CB    . VAL B 1 507 ? 13.592  -77.012 27.557  1.00 41.35  ? 505 VAL B CB    1 
ATOM   8419 C CG1   . VAL B 1 507 ? 14.322  -75.749 27.940  1.00 41.87  ? 505 VAL B CG1   1 
ATOM   8420 C CG2   . VAL B 1 507 ? 12.771  -76.781 26.292  1.00 38.76  ? 505 VAL B CG2   1 
ATOM   8421 N N     . GLY B 1 508 ? 15.466  -78.784 29.628  1.00 39.25  ? 506 GLY B N     1 
ATOM   8422 C CA    . GLY B 1 508 ? 16.518  -79.006 30.643  1.00 40.14  ? 506 GLY B CA    1 
ATOM   8423 C C     . GLY B 1 508 ? 17.622  -79.930 30.129  1.00 40.50  ? 506 GLY B C     1 
ATOM   8424 O O     . GLY B 1 508 ? 18.832  -79.656 30.386  1.00 39.35  ? 506 GLY B O     1 
ATOM   8425 N N     . MET B 1 509 ? 17.219  -80.984 29.417  1.00 42.96  ? 507 MET B N     1 
ATOM   8426 C CA    . MET B 1 509 ? 18.104  -81.987 28.754  1.00 42.87  ? 507 MET B CA    1 
ATOM   8427 C C     . MET B 1 509 ? 18.958  -81.296 27.677  1.00 39.56  ? 507 MET B C     1 
ATOM   8428 O O     . MET B 1 509 ? 20.182  -81.548 27.624  1.00 40.14  ? 507 MET B O     1 
ATOM   8429 C CB    . MET B 1 509 ? 17.267  -83.121 28.137  1.00 38.29  ? 507 MET B CB    1 
ATOM   8430 C CG    . MET B 1 509 ? 18.076  -84.285 27.605  1.00 43.67  ? 507 MET B CG    1 
ATOM   8431 S SD    . MET B 1 509 ? 19.018  -85.209 28.888  1.00 42.87  ? 507 MET B SD    1 
ATOM   8432 C CE    . MET B 1 509 ? 17.692  -86.172 29.597  1.00 49.21  ? 507 MET B CE    1 
ATOM   8433 N N     . ALA B 1 510 ? 18.326  -80.509 26.808  1.00 38.81  ? 508 ALA B N     1 
ATOM   8434 C CA    . ALA B 1 510 ? 18.982  -79.827 25.674  1.00 37.54  ? 508 ALA B CA    1 
ATOM   8435 C C     . ALA B 1 510 ? 19.994  -78.854 26.285  1.00 38.35  ? 508 ALA B C     1 
ATOM   8436 O O     . ALA B 1 510 ? 21.145  -78.776 25.778  1.00 36.58  ? 508 ALA B O     1 
ATOM   8437 C CB    . ALA B 1 510 ? 17.954  -79.123 24.809  1.00 35.79  ? 508 ALA B CB    1 
ATOM   8438 N N     . ALA B 1 511 ? 19.568  -78.175 27.356  1.00 36.23  ? 509 ALA B N     1 
ATOM   8439 C CA    . ALA B 1 511 ? 20.338  -77.124 28.055  1.00 39.32  ? 509 ALA B CA    1 
ATOM   8440 C C     . ALA B 1 511 ? 21.570  -77.742 28.726  1.00 40.62  ? 509 ALA B C     1 
ATOM   8441 O O     . ALA B 1 511 ? 22.633  -77.072 28.742  1.00 38.90  ? 509 ALA B O     1 
ATOM   8442 C CB    . ALA B 1 511 ? 19.462  -76.386 29.031  1.00 39.36  ? 509 ALA B CB    1 
ATOM   8443 N N     . MET B 1 512 ? 21.464  -78.988 29.206  1.00 44.58  ? 510 MET B N     1 
ATOM   8444 C CA    . MET B 1 512 ? 22.627  -79.723 29.788  1.00 43.59  ? 510 MET B CA    1 
ATOM   8445 C C     . MET B 1 512 ? 23.709  -79.922 28.707  1.00 39.12  ? 510 MET B C     1 
ATOM   8446 O O     . MET B 1 512 ? 24.842  -79.744 29.027  1.00 39.59  ? 510 MET B O     1 
ATOM   8447 C CB    . MET B 1 512 ? 22.200  -81.052 30.425  1.00 45.14  ? 510 MET B CB    1 
ATOM   8448 C CG    . MET B 1 512 ? 23.350  -81.976 30.865  1.00 43.19  ? 510 MET B CG    1 
ATOM   8449 S SD    . MET B 1 512 ? 22.835  -83.699 30.678  1.00 48.74  ? 510 MET B SD    1 
ATOM   8450 C CE    . MET B 1 512 ? 22.829  -83.825 28.891  1.00 44.45  ? 510 MET B CE    1 
ATOM   8451 N N     . LYS B 1 513 ? 23.366  -80.202 27.454  1.00 44.07  ? 511 LYS B N     1 
ATOM   8452 C CA    . LYS B 1 513 ? 24.342  -80.365 26.341  1.00 49.91  ? 511 LYS B CA    1 
ATOM   8453 C C     . LYS B 1 513 ? 24.862  -79.002 25.880  1.00 43.36  ? 511 LYS B C     1 
ATOM   8454 O O     . LYS B 1 513 ? 26.044  -78.935 25.603  1.00 43.52  ? 511 LYS B O     1 
ATOM   8455 C CB    . LYS B 1 513 ? 23.715  -81.080 25.140  1.00 58.62  ? 511 LYS B CB    1 
ATOM   8456 C CG    . LYS B 1 513 ? 23.188  -82.480 25.429  1.00 73.78  ? 511 LYS B CG    1 
ATOM   8457 C CD    . LYS B 1 513 ? 24.280  -83.538 25.653  1.00 79.90  ? 511 LYS B CD    1 
ATOM   8458 C CE    . LYS B 1 513 ? 25.196  -83.728 24.462  1.00 73.96  ? 511 LYS B CE    1 
ATOM   8459 N NZ    . LYS B 1 513 ? 24.432  -83.727 23.191  1.00 71.71  ? 511 LYS B NZ    1 
ATOM   8460 N N     . ASP B 1 514 ? 23.993  -77.989 25.763  1.00 44.65  ? 512 ASP B N     1 
ATOM   8461 C CA    . ASP B 1 514 ? 24.314  -76.632 25.229  1.00 45.23  ? 512 ASP B CA    1 
ATOM   8462 C C     . ASP B 1 514 ? 23.495  -75.555 25.967  1.00 41.87  ? 512 ASP B C     1 
ATOM   8463 O O     . ASP B 1 514 ? 22.304  -75.486 25.737  1.00 37.60  ? 512 ASP B O     1 
ATOM   8464 C CB    . ASP B 1 514 ? 24.082  -76.604 23.716  1.00 46.30  ? 512 ASP B CB    1 
ATOM   8465 C CG    . ASP B 1 514 ? 24.319  -75.260 23.061  1.00 48.02  ? 512 ASP B CG    1 
ATOM   8466 O OD1   . ASP B 1 514 ? 25.000  -74.433 23.674  1.00 50.08  ? 512 ASP B OD1   1 
ATOM   8467 O OD2   . ASP B 1 514 ? 23.809  -75.057 21.942  1.00 48.80  ? 512 ASP B OD2   1 
ATOM   8468 N N     . ARG B 1 515 ? 24.149  -74.745 26.803  1.00 42.33  ? 513 ARG B N     1 
ATOM   8469 C CA    . ARG B 1 515 ? 23.581  -73.613 27.582  1.00 45.52  ? 513 ARG B CA    1 
ATOM   8470 C C     . ARG B 1 515 ? 22.850  -72.597 26.686  1.00 43.57  ? 513 ARG B C     1 
ATOM   8471 O O     . ARG B 1 515 ? 21.975  -71.880 27.202  1.00 40.19  ? 513 ARG B O     1 
ATOM   8472 C CB    . ARG B 1 515 ? 24.709  -72.909 28.346  1.00 49.42  ? 513 ARG B CB    1 
ATOM   8473 C CG    . ARG B 1 515 ? 25.141  -73.623 29.616  1.00 57.03  ? 513 ARG B CG    1 
ATOM   8474 C CD    . ARG B 1 515 ? 23.949  -74.277 30.296  1.00 64.93  ? 513 ARG B CD    1 
ATOM   8475 N NE    . ARG B 1 515 ? 24.229  -74.746 31.646  1.00 73.27  ? 513 ARG B NE    1 
ATOM   8476 C CZ    . ARG B 1 515 ? 23.936  -74.088 32.770  1.00 74.17  ? 513 ARG B CZ    1 
ATOM   8477 N NH1   . ARG B 1 515 ? 23.337  -72.906 32.741  1.00 71.99  ? 513 ARG B NH1   1 
ATOM   8478 N NH2   . ARG B 1 515 ? 24.245  -74.628 33.936  1.00 71.08  ? 513 ARG B NH2   1 
ATOM   8479 N N     . GLU B 1 516 ? 23.203  -72.515 25.406  1.00 40.59  ? 514 GLU B N     1 
ATOM   8480 C CA    . GLU B 1 516 ? 22.564  -71.594 24.422  1.00 43.30  ? 514 GLU B CA    1 
ATOM   8481 C C     . GLU B 1 516 ? 21.065  -71.924 24.322  1.00 41.22  ? 514 GLU B C     1 
ATOM   8482 O O     . GLU B 1 516 ? 20.290  -70.997 24.034  1.00 38.50  ? 514 GLU B O     1 
ATOM   8483 C CB    . GLU B 1 516 ? 23.285  -71.690 23.074  1.00 48.42  ? 514 GLU B CB    1 
ATOM   8484 C CG    . GLU B 1 516 ? 23.826  -70.383 22.530  1.00 55.04  ? 514 GLU B CG    1 
ATOM   8485 C CD    . GLU B 1 516 ? 24.752  -69.595 23.432  1.00 53.21  ? 514 GLU B CD    1 
ATOM   8486 O OE1   . GLU B 1 516 ? 25.913  -69.385 23.061  1.00 49.64  ? 514 GLU B OE1   1 
ATOM   8487 O OE2   . GLU B 1 516 ? 24.272  -69.120 24.457  1.00 68.66  ? 514 GLU B OE2   1 
ATOM   8488 N N     . GLU B 1 517 ? 20.674  -73.165 24.649  1.00 35.92  ? 515 GLU B N     1 
ATOM   8489 C CA    . GLU B 1 517 ? 19.276  -73.657 24.646  1.00 38.40  ? 515 GLU B CA    1 
ATOM   8490 C C     . GLU B 1 517 ? 18.373  -72.854 25.598  1.00 38.12  ? 515 GLU B C     1 
ATOM   8491 O O     . GLU B 1 517 ? 17.200  -72.703 25.293  1.00 43.64  ? 515 GLU B O     1 
ATOM   8492 C CB    . GLU B 1 517 ? 19.229  -75.132 25.052  1.00 38.85  ? 515 GLU B CB    1 
ATOM   8493 C CG    . GLU B 1 517 ? 19.771  -76.077 23.998  1.00 40.95  ? 515 GLU B CG    1 
ATOM   8494 C CD    . GLU B 1 517 ? 19.026  -76.069 22.677  1.00 45.28  ? 515 GLU B CD    1 
ATOM   8495 O OE1   . GLU B 1 517 ? 19.614  -76.567 21.679  1.00 45.15  ? 515 GLU B OE1   1 
ATOM   8496 O OE2   . GLU B 1 517 ? 17.871  -75.546 22.645  1.00 49.60  ? 515 GLU B OE2   1 
ATOM   8497 N N     . VAL B 1 518 ? 18.855  -72.403 26.740  1.00 36.09  ? 516 VAL B N     1 
ATOM   8498 C CA    . VAL B 1 518 ? 17.974  -71.698 27.700  1.00 39.82  ? 516 VAL B CA    1 
ATOM   8499 C C     . VAL B 1 518 ? 17.459  -70.442 26.988  1.00 43.82  ? 516 VAL B C     1 
ATOM   8500 O O     . VAL B 1 518 ? 16.242  -70.161 27.041  1.00 39.67  ? 516 VAL B O     1 
ATOM   8501 C CB    . VAL B 1 518 ? 18.718  -71.363 29.004  1.00 41.00  ? 516 VAL B CB    1 
ATOM   8502 C CG1   . VAL B 1 518 ? 17.867  -70.494 29.902  1.00 40.11  ? 516 VAL B CG1   1 
ATOM   8503 C CG2   . VAL B 1 518 ? 19.177  -72.620 29.736  1.00 42.96  ? 516 VAL B CG2   1 
ATOM   8504 N N     . GLY B 1 519 ? 18.369  -69.718 26.341  1.00 39.65  ? 517 GLY B N     1 
ATOM   8505 C CA    . GLY B 1 519 ? 18.028  -68.535 25.548  1.00 37.00  ? 517 GLY B CA    1 
ATOM   8506 C C     . GLY B 1 519 ? 17.213  -68.914 24.324  1.00 35.32  ? 517 GLY B C     1 
ATOM   8507 O O     . GLY B 1 519 ? 16.272  -68.208 24.036  1.00 36.61  ? 517 GLY B O     1 
ATOM   8508 N N     . ALA B 1 520 ? 17.577  -69.970 23.609  1.00 29.66  ? 518 ALA B N     1 
ATOM   8509 C CA    . ALA B 1 520 ? 16.928  -70.366 22.342  1.00 32.48  ? 518 ALA B CA    1 
ATOM   8510 C C     . ALA B 1 520 ? 15.443  -70.713 22.538  1.00 33.88  ? 518 ALA B C     1 
ATOM   8511 O O     . ALA B 1 520 ? 14.657  -70.572 21.589  1.00 36.51  ? 518 ALA B O     1 
ATOM   8512 C CB    . ALA B 1 520 ? 17.661  -71.518 21.739  1.00 33.42  ? 518 ALA B CB    1 
ATOM   8513 N N     . ALA B 1 521 ? 15.057  -71.195 23.707  1.00 33.65  ? 519 ALA B N     1 
ATOM   8514 C CA    . ALA B 1 521 ? 13.712  -71.737 23.959  1.00 32.76  ? 519 ALA B CA    1 
ATOM   8515 C C     . ALA B 1 521 ? 12.874  -70.716 24.706  1.00 31.43  ? 519 ALA B C     1 
ATOM   8516 O O     . ALA B 1 521 ? 11.638  -70.881 24.712  1.00 32.71  ? 519 ALA B O     1 
ATOM   8517 C CB    . ALA B 1 521 ? 13.831  -72.994 24.769  1.00 34.88  ? 519 ALA B CB    1 
ATOM   8518 N N     . SER B 1 522 ? 13.535  -69.736 25.321  1.00 32.74  ? 520 SER B N     1 
ATOM   8519 C CA    . SER B 1 522 ? 13.010  -68.930 26.450  1.00 35.65  ? 520 SER B CA    1 
ATOM   8520 C C     . SER B 1 522 ? 11.683  -68.244 26.066  1.00 37.61  ? 520 SER B C     1 
ATOM   8521 O O     . SER B 1 522 ? 10.670  -68.454 26.782  1.00 37.86  ? 520 SER B O     1 
ATOM   8522 C CB    . SER B 1 522 ? 14.037  -67.927 26.947  1.00 36.65  ? 520 SER B CB    1 
ATOM   8523 O OG    . SER B 1 522 ? 14.555  -67.108 25.905  1.00 34.60  ? 520 SER B OG    1 
ATOM   8524 N N     . VAL B 1 523 ? 11.645  -67.455 24.991  1.00 32.56  ? 521 VAL B N     1 
ATOM   8525 C CA    . VAL B 1 523 ? 10.418  -66.666 24.680  1.00 33.85  ? 521 VAL B CA    1 
ATOM   8526 C C     . VAL B 1 523 ? 9.326   -67.613 24.168  1.00 34.30  ? 521 VAL B C     1 
ATOM   8527 O O     . VAL B 1 523 ? 8.176   -67.496 24.604  1.00 35.97  ? 521 VAL B O     1 
ATOM   8528 C CB    . VAL B 1 523 ? 10.692  -65.515 23.714  1.00 30.96  ? 521 VAL B CB    1 
ATOM   8529 C CG1   . VAL B 1 523 ? 9.385   -64.843 23.344  1.00 33.80  ? 521 VAL B CG1   1 
ATOM   8530 C CG2   . VAL B 1 523 ? 11.647  -64.508 24.334  1.00 31.15  ? 521 VAL B CG2   1 
ATOM   8531 N N     . ASP B 1 524 ? 9.697   -68.569 23.333  1.00 33.99  ? 522 ASP B N     1 
ATOM   8532 C CA    . ASP B 1 524 ? 8.785   -69.639 22.874  1.00 31.60  ? 522 ASP B CA    1 
ATOM   8533 C C     . ASP B 1 524 ? 8.178   -70.340 24.085  1.00 33.89  ? 522 ASP B C     1 
ATOM   8534 O O     . ASP B 1 524 ? 6.966   -70.603 24.058  1.00 35.37  ? 522 ASP B O     1 
ATOM   8535 C CB    . ASP B 1 524 ? 9.521   -70.591 21.945  1.00 32.44  ? 522 ASP B CB    1 
ATOM   8536 C CG    . ASP B 1 524 ? 9.490   -70.072 20.528  1.00 33.94  ? 522 ASP B CG    1 
ATOM   8537 O OD1   . ASP B 1 524 ? 8.421   -69.611 20.152  1.00 32.55  ? 522 ASP B OD1   1 
ATOM   8538 O OD2   . ASP B 1 524 ? 10.542  -70.089 19.831  1.00 39.71  ? 522 ASP B OD2   1 
ATOM   8539 N N     . TYR B 1 525 ? 8.976   -70.611 25.117  1.00 34.05  ? 523 TYR B N     1 
ATOM   8540 C CA    . TYR B 1 525 ? 8.505   -71.293 26.346  1.00 32.73  ? 523 TYR B CA    1 
ATOM   8541 C C     . TYR B 1 525 ? 7.559   -70.383 27.141  1.00 30.60  ? 523 TYR B C     1 
ATOM   8542 O O     . TYR B 1 525 ? 6.525   -70.863 27.686  1.00 29.85  ? 523 TYR B O     1 
ATOM   8543 C CB    . TYR B 1 525 ? 9.697   -71.746 27.176  1.00 32.76  ? 523 TYR B CB    1 
ATOM   8544 C CG    . TYR B 1 525 ? 9.320   -72.546 28.389  1.00 32.96  ? 523 TYR B CG    1 
ATOM   8545 C CD1   . TYR B 1 525 ? 9.116   -73.908 28.319  1.00 35.22  ? 523 TYR B CD1   1 
ATOM   8546 C CD2   . TYR B 1 525 ? 9.139   -71.931 29.608  1.00 36.06  ? 523 TYR B CD2   1 
ATOM   8547 C CE1   . TYR B 1 525 ? 8.764   -74.645 29.443  1.00 35.32  ? 523 TYR B CE1   1 
ATOM   8548 C CE2   . TYR B 1 525 ? 8.786   -72.651 30.736  1.00 35.63  ? 523 TYR B CE2   1 
ATOM   8549 C CZ    . TYR B 1 525 ? 8.612   -74.017 30.657  1.00 34.79  ? 523 TYR B CZ    1 
ATOM   8550 O OH    . TYR B 1 525 ? 8.291   -74.724 31.785  1.00 39.78  ? 523 TYR B OH    1 
ATOM   8551 N N     . LEU B 1 526 ? 7.906   -69.106 27.263  1.00 29.01  ? 524 LEU B N     1 
ATOM   8552 C CA    . LEU B 1 526 ? 7.107   -68.166 28.082  1.00 29.71  ? 524 LEU B CA    1 
ATOM   8553 C C     . LEU B 1 526 ? 5.736   -67.971 27.435  1.00 29.20  ? 524 LEU B C     1 
ATOM   8554 O O     . LEU B 1 526 ? 4.709   -67.971 28.181  1.00 31.28  ? 524 LEU B O     1 
ATOM   8555 C CB    . LEU B 1 526 ? 7.854   -66.847 28.263  1.00 29.84  ? 524 LEU B CB    1 
ATOM   8556 C CG    . LEU B 1 526 ? 7.072   -65.840 29.095  1.00 32.30  ? 524 LEU B CG    1 
ATOM   8557 C CD1   . LEU B 1 526 ? 8.015   -64.875 29.776  1.00 34.33  ? 524 LEU B CD1   1 
ATOM   8558 C CD2   . LEU B 1 526 ? 6.050   -65.090 28.238  1.00 32.86  ? 524 LEU B CD2   1 
ATOM   8559 N N     . MET B 1 527 ? 5.708   -67.918 26.100  1.00 28.70  ? 525 MET B N     1 
ATOM   8560 C CA    . MET B 1 527 ? 4.464   -67.693 25.332  1.00 30.40  ? 525 MET B CA    1 
ATOM   8561 C C     . MET B 1 527 ? 3.572   -68.930 25.414  1.00 29.96  ? 525 MET B C     1 
ATOM   8562 O O     . MET B 1 527 ? 2.369   -68.753 25.720  1.00 30.75  ? 525 MET B O     1 
ATOM   8563 C CB    . MET B 1 527 ? 4.771   -67.289 23.889  1.00 32.40  ? 525 MET B CB    1 
ATOM   8564 C CG    . MET B 1 527 ? 5.424   -65.909 23.811  1.00 32.92  ? 525 MET B CG    1 
ATOM   8565 S SD    . MET B 1 527 ? 4.369   -64.540 24.425  1.00 35.60  ? 525 MET B SD    1 
ATOM   8566 C CE    . MET B 1 527 ? 3.055   -64.640 23.212  1.00 34.74  ? 525 MET B CE    1 
ATOM   8567 N N     . TYR B 1 528 ? 4.127   -70.121 25.192  1.00 29.62  ? 526 TYR B N     1 
ATOM   8568 C CA    . TYR B 1 528 ? 3.448   -71.416 25.482  1.00 33.47  ? 526 TYR B CA    1 
ATOM   8569 C C     . TYR B 1 528 ? 2.852   -71.439 26.899  1.00 33.69  ? 526 TYR B C     1 
ATOM   8570 O O     . TYR B 1 528 ? 1.639   -71.720 27.027  1.00 37.35  ? 526 TYR B O     1 
ATOM   8571 C CB    . TYR B 1 528 ? 4.410   -72.582 25.319  1.00 31.76  ? 526 TYR B CB    1 
ATOM   8572 C CG    . TYR B 1 528 ? 3.799   -73.930 25.570  1.00 31.50  ? 526 TYR B CG    1 
ATOM   8573 C CD1   . TYR B 1 528 ? 3.639   -74.400 26.855  1.00 31.86  ? 526 TYR B CD1   1 
ATOM   8574 C CD2   . TYR B 1 528 ? 3.409   -74.738 24.531  1.00 31.39  ? 526 TYR B CD2   1 
ATOM   8575 C CE1   . TYR B 1 528 ? 3.152   -75.660 27.106  1.00 33.89  ? 526 TYR B CE1   1 
ATOM   8576 C CE2   . TYR B 1 528 ? 2.856   -75.977 24.771  1.00 34.61  ? 526 TYR B CE2   1 
ATOM   8577 C CZ    . TYR B 1 528 ? 2.741   -76.450 26.061  1.00 35.66  ? 526 TYR B CZ    1 
ATOM   8578 O OH    . TYR B 1 528 ? 2.238   -77.693 26.327  1.00 43.96  ? 526 TYR B OH    1 
ATOM   8579 N N     . SER B 1 529 ? 3.654   -71.146 27.924  1.00 33.83  ? 527 SER B N     1 
ATOM   8580 C CA    . SER B 1 529 ? 3.208   -71.039 29.344  1.00 34.53  ? 527 SER B CA    1 
ATOM   8581 C C     . SER B 1 529 ? 1.996   -70.093 29.466  1.00 35.91  ? 527 SER B C     1 
ATOM   8582 O O     . SER B 1 529 ? 1.050   -70.394 30.241  1.00 32.32  ? 527 SER B O     1 
ATOM   8583 C CB    . SER B 1 529 ? 4.325   -70.588 30.250  1.00 31.47  ? 527 SER B CB    1 
ATOM   8584 O OG    . SER B 1 529 ? 5.385   -71.531 30.252  1.00 31.23  ? 527 SER B OG    1 
ATOM   8585 N N     . GLY B 1 530 ? 2.028   -68.967 28.755  1.00 36.31  ? 528 GLY B N     1 
ATOM   8586 C CA    . GLY B 1 530 ? 0.931   -67.983 28.789  1.00 32.63  ? 528 GLY B CA    1 
ATOM   8587 C C     . GLY B 1 530 ? -0.346  -68.577 28.217  1.00 30.55  ? 528 GLY B C     1 
ATOM   8588 O O     . GLY B 1 530 ? -1.391  -68.429 28.860  1.00 30.86  ? 528 GLY B O     1 
ATOM   8589 N N     . TYR B 1 531 ? -0.285  -69.256 27.065  1.00 30.11  ? 529 TYR B N     1 
ATOM   8590 C CA    . TYR B 1 531 ? -1.492  -69.850 26.430  1.00 32.00  ? 529 TYR B CA    1 
ATOM   8591 C C     . TYR B 1 531 ? -2.016  -70.982 27.325  1.00 34.35  ? 529 TYR B C     1 
ATOM   8592 O O     . TYR B 1 531 ? -3.201  -71.255 27.272  1.00 42.05  ? 529 TYR B O     1 
ATOM   8593 C CB    . TYR B 1 531 ? -1.232  -70.323 24.996  1.00 31.00  ? 529 TYR B CB    1 
ATOM   8594 C CG    . TYR B 1 531 ? -0.958  -69.217 24.005  1.00 34.96  ? 529 TYR B CG    1 
ATOM   8595 C CD1   . TYR B 1 531 ? -1.926  -68.269 23.676  1.00 33.67  ? 529 TYR B CD1   1 
ATOM   8596 C CD2   . TYR B 1 531 ? 0.282   -69.101 23.396  1.00 37.20  ? 529 TYR B CD2   1 
ATOM   8597 C CE1   . TYR B 1 531 ? -1.663  -67.235 22.791  1.00 31.10  ? 529 TYR B CE1   1 
ATOM   8598 C CE2   . TYR B 1 531 ? 0.562   -68.078 22.505  1.00 35.93  ? 529 TYR B CE2   1 
ATOM   8599 C CZ    . TYR B 1 531 ? -0.420  -67.155 22.194  1.00 35.43  ? 529 TYR B CZ    1 
ATOM   8600 O OH    . TYR B 1 531 ? -0.109  -66.159 21.340  1.00 30.76  ? 529 TYR B OH    1 
ATOM   8601 N N     . ALA B 1 532 ? -1.151  -71.650 28.092  1.00 36.56  ? 530 ALA B N     1 
ATOM   8602 C CA    . ALA B 1 532 ? -1.495  -72.849 28.897  1.00 38.29  ? 530 ALA B CA    1 
ATOM   8603 C C     . ALA B 1 532 ? -2.203  -72.373 30.155  1.00 32.71  ? 530 ALA B C     1 
ATOM   8604 O O     . ALA B 1 532 ? -3.233  -72.919 30.455  1.00 34.24  ? 530 ALA B O     1 
ATOM   8605 C CB    . ALA B 1 532 ? -0.258  -73.647 29.236  1.00 41.36  ? 530 ALA B CB    1 
ATOM   8606 N N     . CYS B 1 533 ? -1.669  -71.354 30.821  1.00 33.67  ? 531 CYS B N     1 
ATOM   8607 C CA    . CYS B 1 533 ? -2.369  -70.614 31.911  1.00 39.60  ? 531 CYS B CA    1 
ATOM   8608 C C     . CYS B 1 533 ? -3.809  -70.223 31.503  1.00 39.12  ? 531 CYS B C     1 
ATOM   8609 O O     . CYS B 1 533 ? -4.738  -70.496 32.266  1.00 40.05  ? 531 CYS B O     1 
ATOM   8610 C CB    . CYS B 1 533 ? -1.587  -69.364 32.299  1.00 42.22  ? 531 CYS B CB    1 
ATOM   8611 S SG    . CYS B 1 533 ? -0.034  -69.723 33.172  1.00 42.48  ? 531 CYS B SG    1 
ATOM   8612 N N     . LEU B 1 534 ? -3.992  -69.618 30.327  1.00 38.83  ? 532 LEU B N     1 
ATOM   8613 C CA    . LEU B 1 534 ? -5.293  -69.074 29.855  1.00 33.90  ? 532 LEU B CA    1 
ATOM   8614 C C     . LEU B 1 534 ? -6.202  -70.222 29.399  1.00 35.85  ? 532 LEU B C     1 
ATOM   8615 O O     . LEU B 1 534 ? -7.451  -70.070 29.517  1.00 36.24  ? 532 LEU B O     1 
ATOM   8616 C CB    . LEU B 1 534 ? -5.042  -68.052 28.741  1.00 34.85  ? 532 LEU B CB    1 
ATOM   8617 C CG    . LEU B 1 534 ? -5.342  -66.589 29.083  1.00 37.18  ? 532 LEU B CG    1 
ATOM   8618 C CD1   . LEU B 1 534 ? -4.495  -66.035 30.237  1.00 34.55  ? 532 LEU B CD1   1 
ATOM   8619 C CD2   . LEU B 1 534 ? -5.150  -65.743 27.847  1.00 37.89  ? 532 LEU B CD2   1 
ATOM   8620 N N     . ALA B 1 535 ? -5.640  -71.344 28.944  1.00 33.36  ? 533 ALA B N     1 
ATOM   8621 C CA    . ALA B 1 535 ? -6.425  -72.570 28.652  1.00 36.04  ? 533 ALA B CA    1 
ATOM   8622 C C     . ALA B 1 535 ? -7.104  -73.023 29.956  1.00 35.46  ? 533 ALA B C     1 
ATOM   8623 O O     . ALA B 1 535 ? -8.322  -73.250 29.963  1.00 38.45  ? 533 ALA B O     1 
ATOM   8624 C CB    . ALA B 1 535 ? -5.547  -73.644 28.073  1.00 37.07  ? 533 ALA B CB    1 
ATOM   8625 N N     . TYR B 1 536 ? -6.358  -73.049 31.046  1.00 34.43  ? 534 TYR B N     1 
ATOM   8626 C CA    . TYR B 1 536 ? -6.898  -73.405 32.380  1.00 37.50  ? 534 TYR B CA    1 
ATOM   8627 C C     . TYR B 1 536 ? -7.947  -72.370 32.810  1.00 37.58  ? 534 TYR B C     1 
ATOM   8628 O O     . TYR B 1 536 ? -8.977  -72.775 33.369  1.00 40.80  ? 534 TYR B O     1 
ATOM   8629 C CB    . TYR B 1 536 ? -5.796  -73.513 33.434  1.00 35.84  ? 534 TYR B CB    1 
ATOM   8630 C CG    . TYR B 1 536 ? -6.321  -73.454 34.845  1.00 35.96  ? 534 TYR B CG    1 
ATOM   8631 C CD1   . TYR B 1 536 ? -7.102  -74.477 35.341  1.00 36.98  ? 534 TYR B CD1   1 
ATOM   8632 C CD2   . TYR B 1 536 ? -6.104  -72.354 35.660  1.00 36.98  ? 534 TYR B CD2   1 
ATOM   8633 C CE1   . TYR B 1 536 ? -7.633  -74.424 36.621  1.00 37.98  ? 534 TYR B CE1   1 
ATOM   8634 C CE2   . TYR B 1 536 ? -6.629  -72.282 36.944  1.00 36.89  ? 534 TYR B CE2   1 
ATOM   8635 C CZ    . TYR B 1 536 ? -7.395  -73.329 37.426  1.00 38.73  ? 534 TYR B CZ    1 
ATOM   8636 O OH    . TYR B 1 536 ? -7.914  -73.327 38.686  1.00 41.14  ? 534 TYR B OH    1 
ATOM   8637 N N     . PHE B 1 537 ? -7.709  -71.071 32.622  1.00 34.29  ? 535 PHE B N     1 
ATOM   8638 C CA    . PHE B 1 537 ? -8.629  -70.055 33.190  1.00 33.60  ? 535 PHE B CA    1 
ATOM   8639 C C     . PHE B 1 537 ? -9.935  -70.046 32.406  1.00 32.06  ? 535 PHE B C     1 
ATOM   8640 O O     . PHE B 1 537 ? -10.999 -69.822 33.059  1.00 31.62  ? 535 PHE B O     1 
ATOM   8641 C CB    . PHE B 1 537 ? -7.993  -68.676 33.317  1.00 34.33  ? 535 PHE B CB    1 
ATOM   8642 C CG    . PHE B 1 537 ? -7.000  -68.569 34.443  1.00 37.93  ? 535 PHE B CG    1 
ATOM   8643 C CD1   . PHE B 1 537 ? -7.401  -68.754 35.753  1.00 43.28  ? 535 PHE B CD1   1 
ATOM   8644 C CD2   . PHE B 1 537 ? -5.660  -68.305 34.189  1.00 40.35  ? 535 PHE B CD2   1 
ATOM   8645 C CE1   . PHE B 1 537 ? -6.484  -68.654 36.791  1.00 46.92  ? 535 PHE B CE1   1 
ATOM   8646 C CE2   . PHE B 1 537 ? -4.748  -68.200 35.221  1.00 39.06  ? 535 PHE B CE2   1 
ATOM   8647 C CZ    . PHE B 1 537 ? -5.158  -68.379 36.520  1.00 46.05  ? 535 PHE B CZ    1 
ATOM   8648 N N     . TRP B 1 538 ? -9.860  -70.343 31.106  1.00 32.59  ? 536 TRP B N     1 
ATOM   8649 C CA    . TRP B 1 538 ? -11.030 -70.453 30.203  1.00 33.75  ? 536 TRP B CA    1 
ATOM   8650 C C     . TRP B 1 538 ? -11.795 -71.761 30.432  1.00 35.50  ? 536 TRP B C     1 
ATOM   8651 O O     . TRP B 1 538 ? -13.038 -71.732 30.288  1.00 37.84  ? 536 TRP B O     1 
ATOM   8652 C CB    . TRP B 1 538 ? -10.633 -70.300 28.721  1.00 31.58  ? 536 TRP B CB    1 
ATOM   8653 C CG    . TRP B 1 538 ? -10.602 -68.859 28.336  1.00 31.96  ? 536 TRP B CG    1 
ATOM   8654 C CD1   . TRP B 1 538 ? -9.533  -68.138 27.897  1.00 31.87  ? 536 TRP B CD1   1 
ATOM   8655 C CD2   . TRP B 1 538 ? -11.699 -67.940 28.432  1.00 31.15  ? 536 TRP B CD2   1 
ATOM   8656 N NE1   . TRP B 1 538 ? -9.901  -66.839 27.681  1.00 32.70  ? 536 TRP B NE1   1 
ATOM   8657 C CE2   . TRP B 1 538 ? -11.218 -66.683 28.002  1.00 31.65  ? 536 TRP B CE2   1 
ATOM   8658 C CE3   . TRP B 1 538 ? -13.037 -68.060 28.816  1.00 30.39  ? 536 TRP B CE3   1 
ATOM   8659 C CZ2   . TRP B 1 538 ? -12.015 -65.537 28.012  1.00 30.53  ? 536 TRP B CZ2   1 
ATOM   8660 C CZ3   . TRP B 1 538 ? -13.834 -66.936 28.810  1.00 29.81  ? 536 TRP B CZ3   1 
ATOM   8661 C CH2   . TRP B 1 538 ? -13.327 -65.695 28.412  1.00 30.94  ? 536 TRP B CH2   1 
ATOM   8662 N N     . ALA B 1 539 ? -11.112 -72.874 30.684  1.00 34.83  ? 537 ALA B N     1 
ATOM   8663 C CA    . ALA B 1 539 ? -11.776 -74.145 31.050  1.00 35.89  ? 537 ALA B CA    1 
ATOM   8664 C C     . ALA B 1 539 ? -12.531 -73.952 32.381  1.00 35.46  ? 537 ALA B C     1 
ATOM   8665 O O     . ALA B 1 539 ? -13.676 -74.406 32.465  1.00 41.42  ? 537 ALA B O     1 
ATOM   8666 C CB    . ALA B 1 539 ? -10.772 -75.258 31.126  1.00 38.08  ? 537 ALA B CB    1 
ATOM   8667 N N     . ASP B 1 540 ? -11.982 -73.190 33.320  1.00 33.07  ? 538 ASP B N     1 
ATOM   8668 C CA    . ASP B 1 540 ? -12.593 -72.953 34.653  1.00 37.07  ? 538 ASP B CA    1 
ATOM   8669 C C     . ASP B 1 540 ? -13.729 -71.924 34.549  1.00 39.80  ? 538 ASP B C     1 
ATOM   8670 O O     . ASP B 1 540 ? -14.754 -72.124 35.208  1.00 40.53  ? 538 ASP B O     1 
ATOM   8671 C CB    . ASP B 1 540 ? -11.538 -72.530 35.674  1.00 40.85  ? 538 ASP B CB    1 
ATOM   8672 C CG    . ASP B 1 540 ? -11.907 -72.724 37.147  1.00 40.72  ? 538 ASP B CG    1 
ATOM   8673 O OD1   . ASP B 1 540 ? -12.460 -73.782 37.499  1.00 44.57  ? 538 ASP B OD1   1 
ATOM   8674 O OD2   . ASP B 1 540 ? -11.637 -71.806 37.928  1.00 38.57  ? 538 ASP B OD2   1 
ATOM   8675 N N     . MET B 1 541 ? -13.590 -70.870 33.746  1.00 39.37  ? 539 MET B N     1 
ATOM   8676 C CA    . MET B 1 541 ? -14.700 -69.896 33.565  1.00 39.12  ? 539 MET B CA    1 
ATOM   8677 C C     . MET B 1 541 ? -15.864 -70.629 32.864  1.00 38.80  ? 539 MET B C     1 
ATOM   8678 O O     . MET B 1 541 ? -17.012 -70.418 33.263  1.00 40.76  ? 539 MET B O     1 
ATOM   8679 C CB    . MET B 1 541 ? -14.257 -68.645 32.789  1.00 40.35  ? 539 MET B CB    1 
ATOM   8680 C CG    . MET B 1 541 ? -13.400 -67.714 33.610  1.00 41.06  ? 539 MET B CG    1 
ATOM   8681 S SD    . MET B 1 541 ? -13.066 -66.070 32.893  1.00 40.03  ? 539 MET B SD    1 
ATOM   8682 C CE    . MET B 1 541 ? -11.893 -66.541 31.619  1.00 49.02  ? 539 MET B CE    1 
ATOM   8683 N N     . ALA B 1 542 ? -15.563 -71.521 31.920  1.00 37.46  ? 540 ALA B N     1 
ATOM   8684 C CA    . ALA B 1 542 ? -16.536 -72.382 31.216  1.00 39.73  ? 540 ALA B CA    1 
ATOM   8685 C C     . ALA B 1 542 ? -17.260 -73.300 32.224  1.00 45.22  ? 540 ALA B C     1 
ATOM   8686 O O     . ALA B 1 542 ? -18.504 -73.375 32.183  1.00 48.95  ? 540 ALA B O     1 
ATOM   8687 C CB    . ALA B 1 542 ? -15.833 -73.149 30.115  1.00 35.17  ? 540 ALA B CB    1 
ATOM   8688 N N     . ARG B 1 543 ? -16.515 -73.974 33.101  1.00 45.91  ? 541 ARG B N     1 
ATOM   8689 C CA    . ARG B 1 543 ? -17.068 -74.789 34.216  1.00 42.25  ? 541 ARG B CA    1 
ATOM   8690 C C     . ARG B 1 543 ? -18.035 -73.946 35.069  1.00 37.23  ? 541 ARG B C     1 
ATOM   8691 O O     . ARG B 1 543 ? -19.129 -74.404 35.328  1.00 38.89  ? 541 ARG B O     1 
ATOM   8692 C CB    . ARG B 1 543 ? -15.949 -75.354 35.100  1.00 39.35  ? 541 ARG B CB    1 
ATOM   8693 C CG    . ARG B 1 543 ? -16.475 -76.211 36.243  1.00 38.69  ? 541 ARG B CG    1 
ATOM   8694 C CD    . ARG B 1 543 ? -15.660 -76.129 37.509  1.00 39.38  ? 541 ARG B CD    1 
ATOM   8695 N NE    . ARG B 1 543 ? -15.229 -74.784 37.896  1.00 40.05  ? 541 ARG B NE    1 
ATOM   8696 C CZ    . ARG B 1 543 ? -15.857 -73.979 38.750  1.00 40.67  ? 541 ARG B CZ    1 
ATOM   8697 N NH1   . ARG B 1 543 ? -17.009 -74.317 39.300  1.00 45.72  ? 541 ARG B NH1   1 
ATOM   8698 N NH2   . ARG B 1 543 ? -15.337 -72.806 39.044  1.00 46.38  ? 541 ARG B NH2   1 
ATOM   8699 N N     . LEU B 1 544 ? -17.635 -72.771 35.528  1.00 36.95  ? 542 LEU B N     1 
ATOM   8700 C CA    . LEU B 1 544 ? -18.498 -71.900 36.354  1.00 37.01  ? 542 LEU B CA    1 
ATOM   8701 C C     . LEU B 1 544 ? -19.732 -71.496 35.542  1.00 43.29  ? 542 LEU B C     1 
ATOM   8702 O O     . LEU B 1 544 ? -20.832 -71.453 36.102  1.00 49.79  ? 542 LEU B O     1 
ATOM   8703 C CB    . LEU B 1 544 ? -17.690 -70.678 36.787  1.00 37.86  ? 542 LEU B CB    1 
ATOM   8704 C CG    . LEU B 1 544 ? -18.458 -69.658 37.631  1.00 40.56  ? 542 LEU B CG    1 
ATOM   8705 C CD1   . LEU B 1 544 ? -19.216 -70.330 38.770  1.00 42.50  ? 542 LEU B CD1   1 
ATOM   8706 C CD2   . LEU B 1 544 ? -17.528 -68.598 38.194  1.00 43.16  ? 542 LEU B CD2   1 
ATOM   8707 N N     . ALA B 1 545 ? -19.544 -71.187 34.263  1.00 48.91  ? 543 ALA B N     1 
ATOM   8708 C CA    . ALA B 1 545 ? -20.614 -70.720 33.352  1.00 47.17  ? 543 ALA B CA    1 
ATOM   8709 C C     . ALA B 1 545 ? -21.688 -71.801 33.260  1.00 44.60  ? 543 ALA B C     1 
ATOM   8710 O O     . ALA B 1 545 ? -22.854 -71.442 33.436  1.00 39.26  ? 543 ALA B O     1 
ATOM   8711 C CB    . ALA B 1 545 ? -20.059 -70.364 31.988  1.00 42.12  ? 543 ALA B CB    1 
ATOM   8712 N N     . ALA B 1 546 ? -21.280 -73.051 33.007  1.00 41.98  ? 544 ALA B N     1 
ATOM   8713 C CA    . ALA B 1 546 ? -22.147 -74.252 32.905  1.00 41.83  ? 544 ALA B CA    1 
ATOM   8714 C C     . ALA B 1 546 ? -22.843 -74.555 34.243  1.00 42.58  ? 544 ALA B C     1 
ATOM   8715 O O     . ALA B 1 546 ? -24.002 -74.969 34.207  1.00 50.84  ? 544 ALA B O     1 
ATOM   8716 C CB    . ALA B 1 546 ? -21.337 -75.434 32.450  1.00 38.84  ? 544 ALA B CB    1 
ATOM   8717 N N     . GLU B 1 547 ? -22.165 -74.367 35.375  1.00 47.27  ? 545 GLU B N     1 
ATOM   8718 C CA    . GLU B 1 547 ? -22.735 -74.511 36.750  1.00 48.96  ? 545 GLU B CA    1 
ATOM   8719 C C     . GLU B 1 547 ? -23.893 -73.526 36.939  1.00 47.72  ? 545 GLU B C     1 
ATOM   8720 O O     . GLU B 1 547 ? -24.960 -73.959 37.430  1.00 50.65  ? 545 GLU B O     1 
ATOM   8721 C CB    . GLU B 1 547 ? -21.648 -74.216 37.782  1.00 52.08  ? 545 GLU B CB    1 
ATOM   8722 C CG    . GLU B 1 547 ? -21.975 -74.545 39.227  1.00 57.78  ? 545 GLU B CG    1 
ATOM   8723 C CD    . GLU B 1 547 ? -20.746 -74.338 40.100  1.00 61.06  ? 545 GLU B CD    1 
ATOM   8724 O OE1   . GLU B 1 547 ? -19.759 -75.080 39.908  1.00 65.87  ? 545 GLU B OE1   1 
ATOM   8725 O OE2   . GLU B 1 547 ? -20.732 -73.373 40.894  1.00 65.24  ? 545 GLU B OE2   1 
ATOM   8726 N N     . LYS B 1 548 ? -23.676 -72.263 36.581  1.00 42.73  ? 546 LYS B N     1 
ATOM   8727 C CA    . LYS B 1 548 ? -24.708 -71.222 36.779  1.00 43.43  ? 546 LYS B CA    1 
ATOM   8728 C C     . LYS B 1 548 ? -25.880 -71.485 35.843  1.00 50.03  ? 546 LYS B C     1 
ATOM   8729 O O     . LYS B 1 548 ? -27.025 -71.333 36.285  1.00 51.43  ? 546 LYS B O     1 
ATOM   8730 C CB    . LYS B 1 548 ? -24.105 -69.843 36.509  1.00 43.29  ? 546 LYS B CB    1 
ATOM   8731 C CG    . LYS B 1 548 ? -23.004 -69.416 37.466  1.00 46.08  ? 546 LYS B CG    1 
ATOM   8732 C CD    . LYS B 1 548 ? -23.511 -68.567 38.604  1.00 44.46  ? 546 LYS B CD    1 
ATOM   8733 C CE    . LYS B 1 548 ? -22.670 -68.695 39.854  1.00 46.44  ? 546 LYS B CE    1 
ATOM   8734 N NZ    . LYS B 1 548 ? -22.494 -67.390 40.530  1.00 48.56  ? 546 LYS B NZ    1 
ATOM   8735 N N     . LEU B 1 549 ? -25.594 -71.892 34.610  1.00 48.15  ? 547 LEU B N     1 
ATOM   8736 C CA    . LEU B 1 549 ? -26.668 -72.057 33.608  1.00 47.97  ? 547 LEU B CA    1 
ATOM   8737 C C     . LEU B 1 549 ? -27.546 -73.246 33.997  1.00 53.24  ? 547 LEU B C     1 
ATOM   8738 O O     . LEU B 1 549 ? -28.756 -73.186 33.745  1.00 57.83  ? 547 LEU B O     1 
ATOM   8739 C CB    . LEU B 1 549 ? -26.019 -72.229 32.232  1.00 45.97  ? 547 LEU B CB    1 
ATOM   8740 C CG    . LEU B 1 549 ? -25.614 -70.931 31.537  1.00 44.73  ? 547 LEU B CG    1 
ATOM   8741 C CD1   . LEU B 1 549 ? -24.696 -71.206 30.360  1.00 42.25  ? 547 LEU B CD1   1 
ATOM   8742 C CD2   . LEU B 1 549 ? -26.838 -70.153 31.087  1.00 45.22  ? 547 LEU B CD2   1 
ATOM   8743 N N     . ALA B 1 550 ? -26.956 -74.267 34.611  1.00 52.04  ? 548 ALA B N     1 
ATOM   8744 C CA    . ALA B 1 550 ? -27.716 -75.474 34.993  1.00 51.59  ? 548 ALA B CA    1 
ATOM   8745 C C     . ALA B 1 550 ? -28.545 -75.201 36.248  1.00 52.64  ? 548 ALA B C     1 
ATOM   8746 O O     . ALA B 1 550 ? -29.518 -75.926 36.470  1.00 60.93  ? 548 ALA B O     1 
ATOM   8747 C CB    . ALA B 1 550 ? -26.766 -76.608 35.223  1.00 50.42  ? 548 ALA B CB    1 
ATOM   8748 N N     . ALA B 1 551 ? -28.171 -74.190 37.022  1.00 49.89  ? 549 ALA B N     1 
ATOM   8749 C CA    . ALA B 1 551 ? -28.873 -73.894 38.283  1.00 46.40  ? 549 ALA B CA    1 
ATOM   8750 C C     . ALA B 1 551 ? -29.876 -72.767 38.065  1.00 51.69  ? 549 ALA B C     1 
ATOM   8751 O O     . ALA B 1 551 ? -30.451 -72.303 39.060  1.00 55.87  ? 549 ALA B O     1 
ATOM   8752 C CB    . ALA B 1 551 ? -27.863 -73.503 39.313  1.00 42.00  ? 549 ALA B CB    1 
ATOM   8753 N N     . GLY B 1 552 ? -30.066 -72.342 36.819  1.00 48.63  ? 550 GLY B N     1 
ATOM   8754 C CA    . GLY B 1 552 ? -30.950 -71.199 36.544  1.00 44.31  ? 550 GLY B CA    1 
ATOM   8755 C C     . GLY B 1 552 ? -30.301 -69.887 36.927  1.00 45.62  ? 550 GLY B C     1 
ATOM   8756 O O     . GLY B 1 552 ? -29.649 -69.836 37.973  1.00 48.28  ? 550 GLY B O     1 
ATOM   8757 N N     . THR B 1 553 ? -30.482 -68.852 36.108  1.00 49.88  ? 551 THR B N     1 
ATOM   8758 C CA    . THR B 1 553 ? -29.773 -67.580 36.382  1.00 52.76  ? 551 THR B CA    1 
ATOM   8759 C C     . THR B 1 553 ? -30.431 -66.369 35.731  1.00 49.95  ? 551 THR B C     1 
ATOM   8760 O O     . THR B 1 553 ? -30.914 -66.498 34.603  1.00 50.28  ? 551 THR B O     1 
ATOM   8761 C CB    . THR B 1 553 ? -28.326 -67.618 35.870  1.00 52.74  ? 551 THR B CB    1 
ATOM   8762 O OG1   . THR B 1 553 ? -27.772 -66.311 36.022  1.00 49.65  ? 551 THR B OG1   1 
ATOM   8763 C CG2   . THR B 1 553 ? -28.216 -68.059 34.427  1.00 48.58  ? 551 THR B CG2   1 
ATOM   8764 N N     . GLY B 1 554 ? -30.484 -65.252 36.452  1.00 55.92  ? 552 GLY B N     1 
ATOM   8765 C CA    . GLY B 1 554 ? -30.915 -63.979 35.840  1.00 59.18  ? 552 GLY B CA    1 
ATOM   8766 C C     . GLY B 1 554 ? -30.123 -63.607 34.586  1.00 54.70  ? 552 GLY B C     1 
ATOM   8767 O O     . GLY B 1 554 ? -30.589 -62.742 33.866  1.00 53.59  ? 552 GLY B O     1 
ATOM   8768 N N     . GLU B 1 555 ? -28.949 -64.196 34.325  1.00 53.82  ? 553 GLU B N     1 
ATOM   8769 C CA    . GLU B 1 555 ? -27.998 -63.642 33.319  1.00 48.46  ? 553 GLU B CA    1 
ATOM   8770 C C     . GLU B 1 555 ? -27.569 -64.730 32.330  1.00 43.15  ? 553 GLU B C     1 
ATOM   8771 O O     . GLU B 1 555 ? -26.358 -64.939 32.176  1.00 48.54  ? 553 GLU B O     1 
ATOM   8772 C CB    . GLU B 1 555 ? -26.817 -63.017 34.058  1.00 47.18  ? 553 GLU B CB    1 
ATOM   8773 C CG    . GLU B 1 555 ? -27.209 -61.783 34.830  1.00 50.63  ? 553 GLU B CG    1 
ATOM   8774 C CD    . GLU B 1 555 ? -26.090 -61.184 35.665  1.00 55.77  ? 553 GLU B CD    1 
ATOM   8775 O OE1   . GLU B 1 555 ? -25.855 -59.964 35.535  1.00 61.12  ? 553 GLU B OE1   1 
ATOM   8776 O OE2   . GLU B 1 555 ? -25.473 -61.928 36.453  1.00 53.62  ? 553 GLU B OE2   1 
ATOM   8777 N N     . GLU B 1 556 ? -28.523 -65.384 31.667  1.00 43.90  ? 554 GLU B N     1 
ATOM   8778 C CA    . GLU B 1 556 ? -28.239 -66.496 30.716  1.00 46.93  ? 554 GLU B CA    1 
ATOM   8779 C C     . GLU B 1 556 ? -27.148 -66.044 29.740  1.00 47.14  ? 554 GLU B C     1 
ATOM   8780 O O     . GLU B 1 556 ? -26.170 -66.809 29.534  1.00 46.94  ? 554 GLU B O     1 
ATOM   8781 C CB    . GLU B 1 556 ? -29.484 -66.965 29.954  1.00 48.11  ? 554 GLU B CB    1 
ATOM   8782 C CG    . GLU B 1 556 ? -30.079 -68.246 30.512  1.00 59.53  ? 554 GLU B CG    1 
ATOM   8783 C CD    . GLU B 1 556 ? -31.466 -68.636 30.001  1.00 65.67  ? 554 GLU B CD    1 
ATOM   8784 O OE1   . GLU B 1 556 ? -32.263 -69.102 30.820  1.00 71.84  ? 554 GLU B OE1   1 
ATOM   8785 O OE2   . GLU B 1 556 ? -31.743 -68.506 28.787  1.00 72.38  ? 554 GLU B OE2   1 
ATOM   8786 N N     . ALA B 1 557 ? -27.316 -64.861 29.140  1.00 43.21  ? 555 ALA B N     1 
ATOM   8787 C CA    . ALA B 1 557 ? -26.476 -64.418 28.009  1.00 42.76  ? 555 ALA B CA    1 
ATOM   8788 C C     . ALA B 1 557 ? -25.030 -64.240 28.518  1.00 43.55  ? 555 ALA B C     1 
ATOM   8789 O O     . ALA B 1 557 ? -24.113 -64.649 27.800  1.00 40.24  ? 555 ALA B O     1 
ATOM   8790 C CB    . ALA B 1 557 ? -27.050 -63.183 27.354  1.00 39.13  ? 555 ALA B CB    1 
ATOM   8791 N N     . PHE B 1 558 ? -24.851 -63.757 29.753  1.00 41.27  ? 556 PHE B N     1 
ATOM   8792 C CA    . PHE B 1 558 ? -23.528 -63.498 30.359  1.00 40.74  ? 556 PHE B CA    1 
ATOM   8793 C C     . PHE B 1 558 ? -22.730 -64.813 30.334  1.00 43.18  ? 556 PHE B C     1 
ATOM   8794 O O     . PHE B 1 558 ? -21.624 -64.831 29.765  1.00 44.45  ? 556 PHE B O     1 
ATOM   8795 C CB    . PHE B 1 558 ? -23.666 -62.855 31.744  1.00 40.05  ? 556 PHE B CB    1 
ATOM   8796 C CG    . PHE B 1 558 ? -22.316 -62.568 32.358  1.00 42.71  ? 556 PHE B CG    1 
ATOM   8797 C CD1   . PHE B 1 558 ? -21.626 -61.398 32.054  1.00 45.23  ? 556 PHE B CD1   1 
ATOM   8798 C CD2   . PHE B 1 558 ? -21.677 -63.515 33.138  1.00 35.60  ? 556 PHE B CD2   1 
ATOM   8799 C CE1   . PHE B 1 558 ? -20.356 -61.158 32.560  1.00 39.69  ? 556 PHE B CE1   1 
ATOM   8800 C CE2   . PHE B 1 558 ? -20.411 -63.275 33.637  1.00 38.07  ? 556 PHE B CE2   1 
ATOM   8801 C CZ    . PHE B 1 558 ? -19.752 -62.098 33.354  1.00 40.32  ? 556 PHE B CZ    1 
ATOM   8802 N N     . TYR B 1 559 ? -23.303 -65.900 30.856  1.00 41.84  ? 557 TYR B N     1 
ATOM   8803 C CA    . TYR B 1 559 ? -22.625 -67.212 31.004  1.00 38.79  ? 557 TYR B CA    1 
ATOM   8804 C C     . TYR B 1 559 ? -22.530 -67.944 29.652  1.00 37.04  ? 557 TYR B C     1 
ATOM   8805 O O     . TYR B 1 559 ? -21.534 -68.607 29.385  1.00 36.99  ? 557 TYR B O     1 
ATOM   8806 C CB    . TYR B 1 559 ? -23.292 -67.980 32.150  1.00 37.78  ? 557 TYR B CB    1 
ATOM   8807 C CG    . TYR B 1 559 ? -23.189 -67.267 33.485  1.00 39.72  ? 557 TYR B CG    1 
ATOM   8808 C CD1   . TYR B 1 559 ? -21.974 -67.126 34.156  1.00 37.00  ? 557 TYR B CD1   1 
ATOM   8809 C CD2   . TYR B 1 559 ? -24.310 -66.684 34.067  1.00 38.41  ? 557 TYR B CD2   1 
ATOM   8810 C CE1   . TYR B 1 559 ? -21.884 -66.465 35.382  1.00 36.44  ? 557 TYR B CE1   1 
ATOM   8811 C CE2   . TYR B 1 559 ? -24.232 -66.014 35.279  1.00 37.88  ? 557 TYR B CE2   1 
ATOM   8812 C CZ    . TYR B 1 559 ? -23.027 -65.926 35.946  1.00 35.06  ? 557 TYR B CZ    1 
ATOM   8813 O OH    . TYR B 1 559 ? -23.018 -65.249 37.115  1.00 37.60  ? 557 TYR B OH    1 
ATOM   8814 N N     . LYS B 1 560 ? -23.499 -67.813 28.756  1.00 39.51  ? 558 LYS B N     1 
ATOM   8815 C CA    . LYS B 1 560 ? -23.361 -68.427 27.404  1.00 39.98  ? 558 LYS B CA    1 
ATOM   8816 C C     . LYS B 1 560 ? -22.176 -67.801 26.650  1.00 39.00  ? 558 LYS B C     1 
ATOM   8817 O O     . LYS B 1 560 ? -21.485 -68.532 25.928  1.00 36.51  ? 558 LYS B O     1 
ATOM   8818 C CB    . LYS B 1 560 ? -24.656 -68.307 26.602  1.00 42.34  ? 558 LYS B CB    1 
ATOM   8819 C CG    . LYS B 1 560 ? -25.591 -69.496 26.770  1.00 47.66  ? 558 LYS B CG    1 
ATOM   8820 C CD    . LYS B 1 560 ? -26.973 -69.292 26.199  1.00 51.63  ? 558 LYS B CD    1 
ATOM   8821 C CE    . LYS B 1 560 ? -27.801 -70.555 26.319  1.00 60.74  ? 558 LYS B CE    1 
ATOM   8822 N NZ    . LYS B 1 560 ? -29.207 -70.234 26.661  1.00 66.70  ? 558 LYS B NZ    1 
ATOM   8823 N N     . ALA B 1 561 ? -21.956 -66.497 26.815  1.00 36.23  ? 559 ALA B N     1 
ATOM   8824 C CA    . ALA B 1 561 ? -20.846 -65.748 26.204  1.00 35.27  ? 559 ALA B CA    1 
ATOM   8825 C C     . ALA B 1 561 ? -19.529 -66.321 26.714  1.00 35.21  ? 559 ALA B C     1 
ATOM   8826 O O     . ALA B 1 561 ? -18.650 -66.565 25.878  1.00 37.78  ? 559 ALA B O     1 
ATOM   8827 C CB    . ALA B 1 561 ? -20.959 -64.291 26.537  1.00 37.84  ? 559 ALA B CB    1 
ATOM   8828 N N     . LYS B 1 562 ? -19.424 -66.589 28.020  1.00 35.45  ? 560 LYS B N     1 
ATOM   8829 C CA    . LYS B 1 562 ? -18.212 -67.217 28.621  1.00 34.81  ? 560 LYS B CA    1 
ATOM   8830 C C     . LYS B 1 562 ? -17.928 -68.571 27.954  1.00 36.91  ? 560 LYS B C     1 
ATOM   8831 O O     . LYS B 1 562 ? -16.759 -68.803 27.568  1.00 32.31  ? 560 LYS B O     1 
ATOM   8832 C CB    . LYS B 1 562 ? -18.360 -67.344 30.128  1.00 34.84  ? 560 LYS B CB    1 
ATOM   8833 C CG    . LYS B 1 562 ? -18.316 -66.028 30.887  1.00 37.08  ? 560 LYS B CG    1 
ATOM   8834 C CD    . LYS B 1 562 ? -16.924 -65.366 30.960  1.00 39.92  ? 560 LYS B CD    1 
ATOM   8835 C CE    . LYS B 1 562 ? -16.992 -63.942 31.494  1.00 39.37  ? 560 LYS B CE    1 
ATOM   8836 N NZ    . LYS B 1 562 ? -15.662 -63.285 31.524  1.00 41.93  ? 560 LYS B NZ    1 
ATOM   8837 N N     . LEU B 1 563 ? -18.949 -69.400 27.739  1.00 34.16  ? 561 LEU B N     1 
ATOM   8838 C CA    . LEU B 1 563 ? -18.737 -70.708 27.076  1.00 38.23  ? 561 LEU B CA    1 
ATOM   8839 C C     . LEU B 1 563 ? -18.282 -70.493 25.635  1.00 36.67  ? 561 LEU B C     1 
ATOM   8840 O O     . LEU B 1 563 ? -17.338 -71.216 25.188  1.00 34.96  ? 561 LEU B O     1 
ATOM   8841 C CB    . LEU B 1 563 ? -19.996 -71.570 27.138  1.00 39.93  ? 561 LEU B CB    1 
ATOM   8842 C CG    . LEU B 1 563 ? -20.166 -72.292 28.469  1.00 45.07  ? 561 LEU B CG    1 
ATOM   8843 C CD1   . LEU B 1 563 ? -21.621 -72.693 28.661  1.00 47.10  ? 561 LEU B CD1   1 
ATOM   8844 C CD2   . LEU B 1 563 ? -19.228 -73.493 28.568  1.00 41.61  ? 561 LEU B CD2   1 
ATOM   8845 N N     . GLN B 1 564 ? -18.869 -69.514 24.950  1.00 37.51  ? 562 GLN B N     1 
ATOM   8846 C CA    . GLN B 1 564 ? -18.557 -69.245 23.515  1.00 37.95  ? 562 GLN B CA    1 
ATOM   8847 C C     . GLN B 1 564 ? -17.159 -68.639 23.379  1.00 36.02  ? 562 GLN B C     1 
ATOM   8848 O O     . GLN B 1 564 ? -16.473 -69.017 22.430  1.00 34.47  ? 562 GLN B O     1 
ATOM   8849 C CB    . GLN B 1 564 ? -19.632 -68.368 22.890  1.00 39.78  ? 562 GLN B CB    1 
ATOM   8850 C CG    . GLN B 1 564 ? -20.862 -69.170 22.498  1.00 41.10  ? 562 GLN B CG    1 
ATOM   8851 C CD    . GLN B 1 564 ? -22.145 -68.385 22.591  1.00 49.47  ? 562 GLN B CD    1 
ATOM   8852 O OE1   . GLN B 1 564 ? -22.196 -67.206 22.967  1.00 44.79  ? 562 GLN B OE1   1 
ATOM   8853 N NE2   . GLN B 1 564 ? -23.217 -69.065 22.229  1.00 58.59  ? 562 GLN B NE2   1 
ATOM   8854 N N     . THR B 1 565 ? -16.731 -67.774 24.302  1.00 30.83  ? 563 THR B N     1 
ATOM   8855 C CA    . THR B 1 565 ? -15.343 -67.280 24.297  1.00 35.92  ? 563 THR B CA    1 
ATOM   8856 C C     . THR B 1 565 ? -14.358 -68.431 24.616  1.00 37.99  ? 563 THR B C     1 
ATOM   8857 O O     . THR B 1 565 ? -13.388 -68.607 23.853  1.00 43.38  ? 563 THR B O     1 
ATOM   8858 C CB    . THR B 1 565 ? -15.174 -66.063 25.205  1.00 36.51  ? 563 THR B CB    1 
ATOM   8859 O OG1   . THR B 1 565 ? -16.252 -65.184 24.891  1.00 36.42  ? 563 THR B OG1   1 
ATOM   8860 C CG2   . THR B 1 565 ? -13.830 -65.385 25.015  1.00 32.47  ? 563 THR B CG2   1 
ATOM   8861 N N     . ALA B 1 566 ? -14.566 -69.202 25.674  1.00 36.86  ? 564 ALA B N     1 
ATOM   8862 C CA    . ALA B 1 566 ? -13.715 -70.373 25.989  1.00 37.49  ? 564 ALA B CA    1 
ATOM   8863 C C     . ALA B 1 566 ? -13.513 -71.249 24.739  1.00 36.78  ? 564 ALA B C     1 
ATOM   8864 O O     . ALA B 1 566 ? -12.370 -71.631 24.465  1.00 35.08  ? 564 ALA B O     1 
ATOM   8865 C CB    . ALA B 1 566 ? -14.325 -71.168 27.101  1.00 38.99  ? 564 ALA B CB    1 
ATOM   8866 N N     . ARG B 1 567 ? -14.574 -71.574 23.998  1.00 35.79  ? 565 ARG B N     1 
ATOM   8867 C CA    . ARG B 1 567 ? -14.483 -72.499 22.837  1.00 34.76  ? 565 ARG B CA    1 
ATOM   8868 C C     . ARG B 1 567 ? -13.674 -71.841 21.714  1.00 36.24  ? 565 ARG B C     1 
ATOM   8869 O O     . ARG B 1 567 ? -12.975 -72.546 20.956  1.00 39.44  ? 565 ARG B O     1 
ATOM   8870 C CB    . ARG B 1 567 ? -15.887 -72.882 22.363  1.00 35.84  ? 565 ARG B CB    1 
ATOM   8871 C CG    . ARG B 1 567 ? -15.925 -73.772 21.125  1.00 37.69  ? 565 ARG B CG    1 
ATOM   8872 C CD    . ARG B 1 567 ? -17.180 -74.635 21.114  1.00 44.02  ? 565 ARG B CD    1 
ATOM   8873 N NE    . ARG B 1 567 ? -18.347 -73.884 21.585  1.00 54.17  ? 565 ARG B NE    1 
ATOM   8874 C CZ    . ARG B 1 567 ? -19.063 -74.093 22.695  1.00 49.87  ? 565 ARG B CZ    1 
ATOM   8875 N NH1   . ARG B 1 567 ? -18.790 -75.095 23.505  1.00 52.60  ? 565 ARG B NH1   1 
ATOM   8876 N NH2   . ARG B 1 567 ? -20.063 -73.274 22.990  1.00 51.74  ? 565 ARG B NH2   1 
ATOM   8877 N N     . PHE B 1 568 ? -13.842 -70.534 21.537  1.00 37.16  ? 566 PHE B N     1 
ATOM   8878 C CA    . PHE B 1 568 ? -13.053 -69.748 20.565  1.00 33.51  ? 566 PHE B CA    1 
ATOM   8879 C C     . PHE B 1 568 ? -11.586 -69.834 20.993  1.00 32.65  ? 566 PHE B C     1 
ATOM   8880 O O     . PHE B 1 568 ? -10.753 -70.065 20.124  1.00 33.62  ? 566 PHE B O     1 
ATOM   8881 C CB    . PHE B 1 568 ? -13.509 -68.291 20.505  1.00 32.30  ? 566 PHE B CB    1 
ATOM   8882 C CG    . PHE B 1 568 ? -12.600 -67.441 19.657  1.00 33.30  ? 566 PHE B CG    1 
ATOM   8883 C CD1   . PHE B 1 568 ? -12.708 -67.445 18.276  1.00 31.53  ? 566 PHE B CD1   1 
ATOM   8884 C CD2   . PHE B 1 568 ? -11.593 -66.691 20.240  1.00 34.77  ? 566 PHE B CD2   1 
ATOM   8885 C CE1   . PHE B 1 568 ? -11.836 -66.705 17.501  1.00 33.33  ? 566 PHE B CE1   1 
ATOM   8886 C CE2   . PHE B 1 568 ? -10.735 -65.940 19.459  1.00 34.39  ? 566 PHE B CE2   1 
ATOM   8887 C CZ    . PHE B 1 568 ? -10.854 -65.953 18.093  1.00 31.54  ? 566 PHE B CZ    1 
ATOM   8888 N N     . TYR B 1 569 ? -11.302 -69.663 22.291  1.00 27.08  ? 567 TYR B N     1 
ATOM   8889 C CA    . TYR B 1 569 ? -9.918  -69.647 22.790  1.00 30.06  ? 567 TYR B CA    1 
ATOM   8890 C C     . TYR B 1 569 ? -9.282  -70.978 22.418  1.00 32.99  ? 567 TYR B C     1 
ATOM   8891 O O     . TYR B 1 569 ? -8.235  -70.927 21.750  1.00 34.10  ? 567 TYR B O     1 
ATOM   8892 C CB    . TYR B 1 569 ? -9.791  -69.372 24.282  1.00 32.86  ? 567 TYR B CB    1 
ATOM   8893 C CG    . TYR B 1 569 ? -8.348  -69.372 24.694  1.00 35.08  ? 567 TYR B CG    1 
ATOM   8894 C CD1   . TYR B 1 569 ? -7.518  -68.319 24.353  1.00 33.57  ? 567 TYR B CD1   1 
ATOM   8895 C CD2   . TYR B 1 569 ? -7.786  -70.477 25.316  1.00 36.69  ? 567 TYR B CD2   1 
ATOM   8896 C CE1   . TYR B 1 569 ? -6.183  -68.322 24.697  1.00 34.63  ? 567 TYR B CE1   1 
ATOM   8897 C CE2   . TYR B 1 569 ? -6.448  -70.497 25.667  1.00 34.34  ? 567 TYR B CE2   1 
ATOM   8898 C CZ    . TYR B 1 569 ? -5.653  -69.412 25.365  1.00 35.23  ? 567 TYR B CZ    1 
ATOM   8899 O OH    . TYR B 1 569 ? -4.336  -69.447 25.695  1.00 36.74  ? 567 TYR B OH    1 
ATOM   8900 N N     . PHE B 1 570 ? -9.936  -72.103 22.727  1.00 34.24  ? 568 PHE B N     1 
ATOM   8901 C CA    . PHE B 1 570 ? -9.324  -73.452 22.598  1.00 31.89  ? 568 PHE B CA    1 
ATOM   8902 C C     . PHE B 1 570 ? -9.160  -73.745 21.125  1.00 32.07  ? 568 PHE B C     1 
ATOM   8903 O O     . PHE B 1 570 ? -8.153  -74.298 20.747  1.00 34.75  ? 568 PHE B O     1 
ATOM   8904 C CB    . PHE B 1 570 ? -10.135 -74.567 23.272  1.00 33.19  ? 568 PHE B CB    1 
ATOM   8905 C CG    . PHE B 1 570 ? -9.802  -74.800 24.727  1.00 32.02  ? 568 PHE B CG    1 
ATOM   8906 C CD1   . PHE B 1 570 ? -10.060 -73.826 25.678  1.00 30.99  ? 568 PHE B CD1   1 
ATOM   8907 C CD2   . PHE B 1 570 ? -9.223  -75.984 25.148  1.00 32.14  ? 568 PHE B CD2   1 
ATOM   8908 C CE1   . PHE B 1 570 ? -9.738  -74.026 27.014  1.00 32.54  ? 568 PHE B CE1   1 
ATOM   8909 C CE2   . PHE B 1 570 ? -8.921  -76.187 26.488  1.00 31.61  ? 568 PHE B CE2   1 
ATOM   8910 C CZ    . PHE B 1 570 ? -9.179  -75.208 27.420  1.00 32.05  ? 568 PHE B CZ    1 
ATOM   8911 N N     . GLN B 1 571 ? -10.141 -73.433 20.299  1.00 37.11  ? 569 GLN B N     1 
ATOM   8912 C CA    . GLN B 1 571 ? -10.073 -73.910 18.895  1.00 34.38  ? 569 GLN B CA    1 
ATOM   8913 C C     . GLN B 1 571 ? -9.319  -72.980 17.949  1.00 35.30  ? 569 GLN B C     1 
ATOM   8914 O O     . GLN B 1 571 ? -8.869  -73.475 16.910  1.00 34.85  ? 569 GLN B O     1 
ATOM   8915 C CB    . GLN B 1 571 ? -11.495 -74.099 18.371  1.00 33.06  ? 569 GLN B CB    1 
ATOM   8916 C CG    . GLN B 1 571 ? -12.314 -75.111 19.154  1.00 36.28  ? 569 GLN B CG    1 
ATOM   8917 C CD    . GLN B 1 571 ? -13.685 -75.315 18.560  1.00 39.60  ? 569 GLN B CD    1 
ATOM   8918 O OE1   . GLN B 1 571 ? -14.058 -74.692 17.572  1.00 39.48  ? 569 GLN B OE1   1 
ATOM   8919 N NE2   . GLN B 1 571 ? -14.454 -76.203 19.165  1.00 44.95  ? 569 GLN B NE2   1 
ATOM   8920 N N     . ARG B 1 572 ? -9.133  -71.720 18.308  1.00 29.76  ? 570 ARG B N     1 
ATOM   8921 C CA    . ARG B 1 572 ? -8.604  -70.755 17.318  1.00 30.08  ? 570 ARG B CA    1 
ATOM   8922 C C     . ARG B 1 572 ? -7.332  -70.080 17.807  1.00 29.42  ? 570 ARG B C     1 
ATOM   8923 O O     . ARG B 1 572 ? -6.560  -69.684 16.931  1.00 30.81  ? 570 ARG B O     1 
ATOM   8924 C CB    . ARG B 1 572 ? -9.670  -69.742 16.934  1.00 31.44  ? 570 ARG B CB    1 
ATOM   8925 C CG    . ARG B 1 572 ? -10.693 -70.320 15.978  1.00 32.55  ? 570 ARG B CG    1 
ATOM   8926 C CD    . ARG B 1 572 ? -11.237 -69.217 15.128  1.00 34.04  ? 570 ARG B CD    1 
ATOM   8927 N NE    . ARG B 1 572 ? -12.219 -69.745 14.213  1.00 30.53  ? 570 ARG B NE    1 
ATOM   8928 C CZ    . ARG B 1 572 ? -12.101 -69.820 12.903  1.00 33.03  ? 570 ARG B CZ    1 
ATOM   8929 N NH1   . ARG B 1 572 ? -11.018 -69.385 12.273  1.00 34.66  ? 570 ARG B NH1   1 
ATOM   8930 N NH2   . ARG B 1 572 ? -13.102 -70.333 12.213  1.00 34.03  ? 570 ARG B NH2   1 
ATOM   8931 N N     . ILE B 1 573 ? -7.102  -70.019 19.118  1.00 31.87  ? 571 ILE B N     1 
ATOM   8932 C CA    . ILE B 1 573 ? -5.959  -69.288 19.729  1.00 33.22  ? 571 ILE B CA    1 
ATOM   8933 C C     . ILE B 1 573 ? -4.961  -70.293 20.309  1.00 34.85  ? 571 ILE B C     1 
ATOM   8934 O O     . ILE B 1 573 ? -3.783  -70.174 19.966  1.00 37.06  ? 571 ILE B O     1 
ATOM   8935 C CB    . ILE B 1 573 ? -6.471  -68.221 20.719  1.00 34.50  ? 571 ILE B CB    1 
ATOM   8936 C CG1   . ILE B 1 573 ? -7.287  -67.172 19.955  1.00 38.33  ? 571 ILE B CG1   1 
ATOM   8937 C CG2   . ILE B 1 573 ? -5.336  -67.549 21.481  1.00 33.67  ? 571 ILE B CG2   1 
ATOM   8938 C CD1   . ILE B 1 573 ? -7.983  -66.194 20.852  1.00 48.97  ? 571 ILE B CD1   1 
ATOM   8939 N N     . LEU B 1 574 ? -5.398  -71.266 21.105  1.00 36.18  ? 572 LEU B N     1 
ATOM   8940 C CA    . LEU B 1 574 ? -4.486  -72.194 21.822  1.00 36.99  ? 572 LEU B CA    1 
ATOM   8941 C C     . LEU B 1 574 ? -3.598  -72.964 20.840  1.00 36.36  ? 572 LEU B C     1 
ATOM   8942 O O     . LEU B 1 574 ? -2.453  -73.231 21.198  1.00 34.57  ? 572 LEU B O     1 
ATOM   8943 C CB    . LEU B 1 574 ? -5.318  -73.144 22.689  1.00 40.40  ? 572 LEU B CB    1 
ATOM   8944 C CG    . LEU B 1 574 ? -4.544  -74.087 23.607  1.00 38.00  ? 572 LEU B CG    1 
ATOM   8945 C CD1   . LEU B 1 574 ? -3.608  -73.319 24.515  1.00 42.61  ? 572 LEU B CD1   1 
ATOM   8946 C CD2   . LEU B 1 574 ? -5.511  -74.908 24.449  1.00 42.80  ? 572 LEU B CD2   1 
ATOM   8947 N N     . PRO B 1 575 ? -4.031  -73.314 19.587  1.00 35.94  ? 573 PRO B N     1 
ATOM   8948 C CA    . PRO B 1 575 ? -3.171  -74.047 18.647  1.00 31.88  ? 573 PRO B CA    1 
ATOM   8949 C C     . PRO B 1 575 ? -1.870  -73.317 18.268  1.00 34.43  ? 573 PRO B C     1 
ATOM   8950 O O     . PRO B 1 575 ? -0.967  -73.969 17.761  1.00 37.45  ? 573 PRO B O     1 
ATOM   8951 C CB    . PRO B 1 575 ? -4.076  -74.306 17.431  1.00 28.36  ? 573 PRO B CB    1 
ATOM   8952 C CG    . PRO B 1 575 ? -5.482  -74.266 18.005  1.00 27.37  ? 573 PRO B CG    1 
ATOM   8953 C CD    . PRO B 1 575 ? -5.384  -73.137 19.019  1.00 32.73  ? 573 PRO B CD    1 
ATOM   8954 N N     . ARG B 1 576 ? -1.752  -72.020 18.565  1.00 31.98  ? 574 ARG B N     1 
ATOM   8955 C CA    . ARG B 1 576 ? -0.460  -71.276 18.441  1.00 33.50  ? 574 ARG B CA    1 
ATOM   8956 C C     . ARG B 1 576 ? 0.624   -71.993 19.271  1.00 35.15  ? 574 ARG B C     1 
ATOM   8957 O O     . ARG B 1 576 ? 1.827   -71.863 18.921  1.00 27.78  ? 574 ARG B O     1 
ATOM   8958 C CB    . ARG B 1 576 ? -0.575  -69.824 18.916  1.00 31.38  ? 574 ARG B CB    1 
ATOM   8959 C CG    . ARG B 1 576 ? -1.429  -68.921 18.036  1.00 31.05  ? 574 ARG B CG    1 
ATOM   8960 C CD    . ARG B 1 576 ? -1.864  -67.743 18.896  1.00 32.95  ? 574 ARG B CD    1 
ATOM   8961 N NE    . ARG B 1 576 ? -2.608  -66.770 18.122  1.00 31.32  ? 574 ARG B NE    1 
ATOM   8962 C CZ    . ARG B 1 576 ? -2.745  -65.484 18.413  1.00 29.19  ? 574 ARG B CZ    1 
ATOM   8963 N NH1   . ARG B 1 576 ? -2.187  -64.961 19.483  1.00 29.11  ? 574 ARG B NH1   1 
ATOM   8964 N NH2   . ARG B 1 576 ? -3.458  -64.710 17.617  1.00 32.51  ? 574 ARG B NH2   1 
ATOM   8965 N N     . THR B 1 577 ? 0.215   -72.754 20.301  1.00 35.60  ? 575 THR B N     1 
ATOM   8966 C CA    . THR B 1 577 ? 1.126   -73.648 21.069  1.00 36.84  ? 575 THR B CA    1 
ATOM   8967 C C     . THR B 1 577 ? 1.932   -74.534 20.101  1.00 35.57  ? 575 THR B C     1 
ATOM   8968 O O     . THR B 1 577 ? 3.123   -74.730 20.354  1.00 39.32  ? 575 THR B O     1 
ATOM   8969 C CB    . THR B 1 577 ? 0.389   -74.440 22.155  1.00 34.89  ? 575 THR B CB    1 
ATOM   8970 O OG1   . THR B 1 577 ? -0.698  -75.172 21.596  1.00 36.34  ? 575 THR B OG1   1 
ATOM   8971 C CG2   . THR B 1 577 ? -0.092  -73.542 23.262  1.00 34.84  ? 575 THR B CG2   1 
ATOM   8972 N N     . ARG B 1 578 ? 1.346   -74.995 18.999  1.00 37.71  ? 576 ARG B N     1 
ATOM   8973 C CA    . ARG B 1 578 ? 2.033   -75.941 18.086  1.00 37.42  ? 576 ARG B CA    1 
ATOM   8974 C C     . ARG B 1 578 ? 3.326   -75.296 17.569  1.00 39.37  ? 576 ARG B C     1 
ATOM   8975 O O     . ARG B 1 578 ? 4.378   -76.000 17.489  1.00 38.42  ? 576 ARG B O     1 
ATOM   8976 C CB    . ARG B 1 578 ? 1.107   -76.369 16.945  1.00 36.37  ? 576 ARG B CB    1 
ATOM   8977 C CG    . ARG B 1 578 ? -0.089  -77.233 17.350  1.00 38.95  ? 576 ARG B CG    1 
ATOM   8978 C CD    . ARG B 1 578 ? 0.154   -78.350 18.351  1.00 34.97  ? 576 ARG B CD    1 
ATOM   8979 N NE    . ARG B 1 578 ? 0.048   -77.859 19.732  1.00 37.69  ? 576 ARG B NE    1 
ATOM   8980 C CZ    . ARG B 1 578 ? 0.726   -78.348 20.779  1.00 38.92  ? 576 ARG B CZ    1 
ATOM   8981 N NH1   . ARG B 1 578 ? 1.564   -79.355 20.629  1.00 46.33  ? 576 ARG B NH1   1 
ATOM   8982 N NH2   . ARG B 1 578 ? 0.577   -77.845 21.991  1.00 37.31  ? 576 ARG B NH2   1 
ATOM   8983 N N     . ALA B 1 579 ? 3.277   -74.003 17.230  1.00 43.07  ? 577 ALA B N     1 
ATOM   8984 C CA    . ALA B 1 579 ? 4.435   -73.281 16.640  1.00 37.07  ? 577 ALA B CA    1 
ATOM   8985 C C     . ALA B 1 579 ? 5.459   -73.001 17.740  1.00 33.73  ? 577 ALA B C     1 
ATOM   8986 O O     . ALA B 1 579 ? 6.665   -73.126 17.467  1.00 35.77  ? 577 ALA B O     1 
ATOM   8987 C CB    . ALA B 1 579 ? 4.008   -72.010 15.945  1.00 36.61  ? 577 ALA B CB    1 
ATOM   8988 N N     . HIS B 1 580 ? 5.015   -72.643 18.948  1.00 34.34  ? 578 HIS B N     1 
ATOM   8989 C CA    . HIS B 1 580 ? 5.939   -72.436 20.094  1.00 33.85  ? 578 HIS B CA    1 
ATOM   8990 C C     . HIS B 1 580 ? 6.674   -73.748 20.401  1.00 35.02  ? 578 HIS B C     1 
ATOM   8991 O O     . HIS B 1 580 ? 7.927   -73.706 20.491  1.00 33.49  ? 578 HIS B O     1 
ATOM   8992 C CB    . HIS B 1 580 ? 5.211   -71.786 21.256  1.00 31.81  ? 578 HIS B CB    1 
ATOM   8993 C CG    . HIS B 1 580 ? 4.814   -70.392 20.926  1.00 33.43  ? 578 HIS B CG    1 
ATOM   8994 N ND1   . HIS B 1 580 ? 5.737   -69.419 20.625  1.00 33.61  ? 578 HIS B ND1   1 
ATOM   8995 C CD2   . HIS B 1 580 ? 3.600   -69.814 20.835  1.00 35.24  ? 578 HIS B CD2   1 
ATOM   8996 C CE1   . HIS B 1 580 ? 5.115   -68.288 20.402  1.00 39.59  ? 578 HIS B CE1   1 
ATOM   8997 N NE2   . HIS B 1 580 ? 3.789   -68.508 20.522  1.00 36.84  ? 578 HIS B NE2   1 
ATOM   8998 N N     . VAL B 1 581 ? 5.961   -74.875 20.444  1.00 33.17  ? 579 VAL B N     1 
ATOM   8999 C CA    . VAL B 1 581 ? 6.586   -76.215 20.667  1.00 39.68  ? 579 VAL B CA    1 
ATOM   9000 C C     . VAL B 1 581 ? 7.638   -76.526 19.571  1.00 38.29  ? 579 VAL B C     1 
ATOM   9001 O O     . VAL B 1 581 ? 8.803   -76.884 19.941  1.00 40.05  ? 579 VAL B O     1 
ATOM   9002 C CB    . VAL B 1 581 ? 5.513   -77.318 20.780  1.00 40.76  ? 579 VAL B CB    1 
ATOM   9003 C CG1   . VAL B 1 581 ? 6.063   -78.701 20.460  1.00 39.90  ? 579 VAL B CG1   1 
ATOM   9004 C CG2   . VAL B 1 581 ? 4.885   -77.306 22.162  1.00 35.66  ? 579 VAL B CG2   1 
ATOM   9005 N N     . ALA B 1 582 ? 7.259   -76.449 18.293  1.00 33.22  ? 580 ALA B N     1 
ATOM   9006 C CA    . ALA B 1 582 ? 8.127   -76.787 17.149  1.00 31.51  ? 580 ALA B CA    1 
ATOM   9007 C C     . ALA B 1 582 ? 9.399   -75.934 17.213  1.00 33.11  ? 580 ALA B C     1 
ATOM   9008 O O     . ALA B 1 582 ? 10.490  -76.505 17.117  1.00 33.96  ? 580 ALA B O     1 
ATOM   9009 C CB    . ALA B 1 582 ? 7.386   -76.585 15.862  1.00 31.77  ? 580 ALA B CB    1 
ATOM   9010 N N     . ALA B 1 583 ? 9.263   -74.622 17.428  1.00 34.84  ? 581 ALA B N     1 
ATOM   9011 C CA    . ALA B 1 583 ? 10.390  -73.658 17.480  1.00 35.03  ? 581 ALA B CA    1 
ATOM   9012 C C     . ALA B 1 583 ? 11.324  -74.014 18.645  1.00 38.54  ? 581 ALA B C     1 
ATOM   9013 O O     . ALA B 1 583 ? 12.567  -74.077 18.417  1.00 34.68  ? 581 ALA B O     1 
ATOM   9014 C CB    . ALA B 1 583 ? 9.876   -72.242 17.576  1.00 32.72  ? 581 ALA B CB    1 
ATOM   9015 N N     . MET B 1 584 ? 10.762  -74.292 19.832  1.00 40.42  ? 582 MET B N     1 
ATOM   9016 C CA    . MET B 1 584 ? 11.580  -74.529 21.042  1.00 46.59  ? 582 MET B CA    1 
ATOM   9017 C C     . MET B 1 584 ? 12.297  -75.886 20.952  1.00 45.28  ? 582 MET B C     1 
ATOM   9018 O O     . MET B 1 584 ? 13.499  -75.880 21.246  1.00 49.80  ? 582 MET B O     1 
ATOM   9019 C CB    . MET B 1 584 ? 10.804  -74.301 22.353  1.00 50.45  ? 582 MET B CB    1 
ATOM   9020 C CG    . MET B 1 584 ? 9.839   -75.371 22.805  1.00 52.87  ? 582 MET B CG    1 
ATOM   9021 S SD    . MET B 1 584 ? 9.147   -74.887 24.442  1.00 49.23  ? 582 MET B SD    1 
ATOM   9022 C CE    . MET B 1 584 ? 7.648   -74.034 23.967  1.00 48.35  ? 582 MET B CE    1 
ATOM   9023 N N     . LEU B 1 585 ? 11.679  -76.932 20.388  1.00 47.72  ? 583 LEU B N     1 
ATOM   9024 C CA    . LEU B 1 585 ? 12.340  -78.255 20.135  1.00 43.14  ? 583 LEU B CA    1 
ATOM   9025 C C     . LEU B 1 585 ? 13.345  -78.201 18.975  1.00 40.87  ? 583 LEU B C     1 
ATOM   9026 O O     . LEU B 1 585 ? 14.043  -79.197 18.802  1.00 45.08  ? 583 LEU B O     1 
ATOM   9027 C CB    . LEU B 1 585 ? 11.296  -79.314 19.783  1.00 43.98  ? 583 LEU B CB    1 
ATOM   9028 C CG    . LEU B 1 585 ? 10.333  -79.691 20.899  1.00 45.81  ? 583 LEU B CG    1 
ATOM   9029 C CD1   . LEU B 1 585 ? 9.394   -80.809 20.435  1.00 45.89  ? 583 LEU B CD1   1 
ATOM   9030 C CD2   . LEU B 1 585 ? 11.093  -80.070 22.150  1.00 41.08  ? 583 LEU B CD2   1 
ATOM   9031 N N     . SER B 1 586 ? 13.400  -77.134 18.174  1.00 36.88  ? 584 SER B N     1 
ATOM   9032 C CA    . SER B 1 586 ? 14.261  -77.067 16.963  1.00 36.08  ? 584 SER B CA    1 
ATOM   9033 C C     . SER B 1 586 ? 15.742  -76.911 17.349  1.00 34.92  ? 584 SER B C     1 
ATOM   9034 O O     . SER B 1 586 ? 16.566  -77.171 16.521  1.00 33.93  ? 584 SER B O     1 
ATOM   9035 C CB    . SER B 1 586 ? 13.802  -75.983 16.013  1.00 37.90  ? 584 SER B CB    1 
ATOM   9036 O OG    . SER B 1 586 ? 14.125  -74.681 16.493  1.00 36.95  ? 584 SER B OG    1 
ATOM   9037 N N     . GLY B 1 587 ? 16.053  -76.474 18.566  1.00 39.21  ? 585 GLY B N     1 
ATOM   9038 C CA    . GLY B 1 587 ? 17.431  -76.363 19.094  1.00 40.42  ? 585 GLY B CA    1 
ATOM   9039 C C     . GLY B 1 587 ? 18.114  -75.037 18.766  1.00 39.96  ? 585 GLY B C     1 
ATOM   9040 O O     . GLY B 1 587 ? 17.689  -74.328 17.805  1.00 40.61  ? 585 GLY B O     1 
ATOM   9041 N N     . ALA B 1 588 ? 19.186  -74.739 19.498  1.00 38.22  ? 586 ALA B N     1 
ATOM   9042 C CA    . ALA B 1 588 ? 19.876  -73.426 19.497  1.00 39.60  ? 586 ALA B CA    1 
ATOM   9043 C C     . ALA B 1 588 ? 20.691  -73.237 18.227  1.00 36.81  ? 586 ALA B C     1 
ATOM   9044 O O     . ALA B 1 588 ? 20.949  -72.080 17.898  1.00 35.37  ? 586 ALA B O     1 
ATOM   9045 C CB    . ALA B 1 588 ? 20.778  -73.294 20.695  1.00 38.01  ? 586 ALA B CB    1 
ATOM   9046 N N     . ASN B 1 589 ? 21.078  -74.316 17.551  1.00 38.91  ? 587 ASN B N     1 
ATOM   9047 C CA    . ASN B 1 589 ? 22.004  -74.229 16.390  1.00 41.32  ? 587 ASN B CA    1 
ATOM   9048 C C     . ASN B 1 589 ? 21.437  -73.391 15.246  1.00 37.50  ? 587 ASN B C     1 
ATOM   9049 O O     . ASN B 1 589 ? 22.270  -72.769 14.552  1.00 37.84  ? 587 ASN B O     1 
ATOM   9050 C CB    . ASN B 1 589 ? 22.474  -75.590 15.878  1.00 45.57  ? 587 ASN B CB    1 
ATOM   9051 C CG    . ASN B 1 589 ? 23.665  -76.059 16.695  1.00 50.16  ? 587 ASN B CG    1 
ATOM   9052 O OD1   . ASN B 1 589 ? 24.474  -75.255 17.155  1.00 50.70  ? 587 ASN B OD1   1 
ATOM   9053 N ND2   . ASN B 1 589 ? 23.768  -77.352 16.927  1.00 49.32  ? 587 ASN B ND2   1 
ATOM   9054 N N     . ASN B 1 590 ? 20.115  -73.353 15.041  1.00 32.98  ? 588 ASN B N     1 
ATOM   9055 C CA    . ASN B 1 590 ? 19.561  -72.658 13.856  1.00 33.45  ? 588 ASN B CA    1 
ATOM   9056 C C     . ASN B 1 590 ? 19.597  -71.149 14.139  1.00 33.84  ? 588 ASN B C     1 
ATOM   9057 O O     . ASN B 1 590 ? 19.533  -70.367 13.145  1.00 29.65  ? 588 ASN B O     1 
ATOM   9058 C CB    . ASN B 1 590 ? 18.216  -73.234 13.439  1.00 35.64  ? 588 ASN B CB    1 
ATOM   9059 C CG    . ASN B 1 590 ? 17.235  -73.284 14.582  1.00 35.62  ? 588 ASN B CG    1 
ATOM   9060 O OD1   . ASN B 1 590 ? 17.260  -72.435 15.478  1.00 36.42  ? 588 ASN B OD1   1 
ATOM   9061 N ND2   . ASN B 1 590 ? 16.370  -74.279 14.548  1.00 36.67  ? 588 ASN B ND2   1 
ATOM   9062 N N     . LEU B 1 591 ? 19.779  -70.762 15.417  1.00 32.88  ? 589 LEU B N     1 
ATOM   9063 C CA    . LEU B 1 591 ? 19.987  -69.352 15.842  1.00 32.44  ? 589 LEU B CA    1 
ATOM   9064 C C     . LEU B 1 591 ? 21.472  -69.005 15.881  1.00 34.97  ? 589 LEU B C     1 
ATOM   9065 O O     . LEU B 1 591 ? 21.792  -67.848 15.610  1.00 40.50  ? 589 LEU B O     1 
ATOM   9066 C CB    . LEU B 1 591 ? 19.391  -69.122 17.231  1.00 33.77  ? 589 LEU B CB    1 
ATOM   9067 C CG    . LEU B 1 591 ? 17.884  -69.339 17.365  1.00 34.76  ? 589 LEU B CG    1 
ATOM   9068 C CD1   . LEU B 1 591 ? 17.432  -69.028 18.781  1.00 37.14  ? 589 LEU B CD1   1 
ATOM   9069 C CD2   . LEU B 1 591 ? 17.099  -68.506 16.385  1.00 35.56  ? 589 LEU B CD2   1 
ATOM   9070 N N     . MET B 1 592 ? 22.345  -69.927 16.280  1.00 39.26  ? 590 MET B N     1 
ATOM   9071 C CA    . MET B 1 592 ? 23.723  -69.576 16.743  1.00 41.49  ? 590 MET B CA    1 
ATOM   9072 C C     . MET B 1 592 ? 24.763  -69.847 15.650  1.00 37.72  ? 590 MET B C     1 
ATOM   9073 O O     . MET B 1 592 ? 25.866  -69.385 15.807  1.00 34.29  ? 590 MET B O     1 
ATOM   9074 C CB    . MET B 1 592 ? 24.115  -70.347 18.010  1.00 36.80  ? 590 MET B CB    1 
ATOM   9075 C CG    . MET B 1 592 ? 23.101  -70.236 19.123  1.00 38.29  ? 590 MET B CG    1 
ATOM   9076 S SD    . MET B 1 592 ? 22.711  -68.529 19.630  1.00 37.86  ? 590 MET B SD    1 
ATOM   9077 C CE    . MET B 1 592 ? 24.358  -67.835 19.793  1.00 44.08  ? 590 MET B CE    1 
ATOM   9078 N N     . GLU B 1 593 ? 24.437  -70.556 14.580  1.00 43.90  ? 591 GLU B N     1 
ATOM   9079 C CA    . GLU B 1 593 ? 25.484  -71.004 13.625  1.00 48.18  ? 591 GLU B CA    1 
ATOM   9080 C C     . GLU B 1 593 ? 25.973  -69.832 12.783  1.00 45.17  ? 591 GLU B C     1 
ATOM   9081 O O     . GLU B 1 593 ? 27.152  -69.849 12.428  1.00 48.64  ? 591 GLU B O     1 
ATOM   9082 C CB    . GLU B 1 593 ? 25.026  -72.175 12.759  1.00 55.16  ? 591 GLU B CB    1 
ATOM   9083 C CG    . GLU B 1 593 ? 25.421  -73.502 13.386  1.00 66.35  ? 591 GLU B CG    1 
ATOM   9084 C CD    . GLU B 1 593 ? 24.754  -74.740 12.834  1.00 69.24  ? 591 GLU B CD    1 
ATOM   9085 O OE1   . GLU B 1 593 ? 24.080  -74.637 11.789  1.00 80.87  ? 591 GLU B OE1   1 
ATOM   9086 O OE2   . GLU B 1 593 ? 24.902  -75.789 13.474  1.00 67.56  ? 591 GLU B OE2   1 
ATOM   9087 N N     . MET B 1 594 ? 25.100  -68.882 12.463  1.00 44.98  ? 592 MET B N     1 
ATOM   9088 C CA    . MET B 1 594 ? 25.476  -67.753 11.575  1.00 41.24  ? 592 MET B CA    1 
ATOM   9089 C C     . MET B 1 594 ? 26.466  -66.831 12.286  1.00 43.64  ? 592 MET B C     1 
ATOM   9090 O O     . MET B 1 594 ? 26.221  -66.475 13.442  1.00 35.62  ? 592 MET B O     1 
ATOM   9091 C CB    . MET B 1 594 ? 24.257  -66.938 11.136  1.00 40.12  ? 592 MET B CB    1 
ATOM   9092 C CG    . MET B 1 594 ? 24.583  -65.872 10.113  1.00 40.97  ? 592 MET B CG    1 
ATOM   9093 S SD    . MET B 1 594 ? 23.107  -65.044 9.493   1.00 43.63  ? 592 MET B SD    1 
ATOM   9094 C CE    . MET B 1 594 ? 22.313  -66.396 8.630   1.00 40.11  ? 592 MET B CE    1 
ATOM   9095 N N     . ALA B 1 595 ? 27.540  -66.468 11.588  1.00 40.99  ? 593 ALA B N     1 
ATOM   9096 C CA    . ALA B 1 595 ? 28.541  -65.547 12.156  1.00 38.67  ? 593 ALA B CA    1 
ATOM   9097 C C     . ALA B 1 595 ? 27.974  -64.132 12.185  1.00 36.14  ? 593 ALA B C     1 
ATOM   9098 O O     . ALA B 1 595 ? 27.207  -63.788 11.295  1.00 34.08  ? 593 ALA B O     1 
ATOM   9099 C CB    . ALA B 1 595 ? 29.812  -65.618 11.360  1.00 37.09  ? 593 ALA B CB    1 
ATOM   9100 N N     . GLU B 1 596 ? 28.366  -63.348 13.183  1.00 38.93  ? 594 GLU B N     1 
ATOM   9101 C CA    . GLU B 1 596 ? 27.877  -61.957 13.319  1.00 40.92  ? 594 GLU B CA    1 
ATOM   9102 C C     . GLU B 1 596 ? 28.150  -61.180 12.036  1.00 41.21  ? 594 GLU B C     1 
ATOM   9103 O O     . GLU B 1 596 ? 27.266  -60.428 11.624  1.00 41.13  ? 594 GLU B O     1 
ATOM   9104 C CB    . GLU B 1 596 ? 28.591  -61.278 14.481  1.00 44.98  ? 594 GLU B CB    1 
ATOM   9105 C CG    . GLU B 1 596 ? 28.885  -62.199 15.648  1.00 61.00  ? 594 GLU B CG    1 
ATOM   9106 C CD    . GLU B 1 596 ? 29.480  -61.497 16.858  1.00 62.90  ? 594 GLU B CD    1 
ATOM   9107 O OE1   . GLU B 1 596 ? 29.961  -60.356 16.700  1.00 56.64  ? 594 GLU B OE1   1 
ATOM   9108 O OE2   . GLU B 1 596 ? 29.460  -62.092 17.952  1.00 58.49  ? 594 GLU B OE2   1 
ATOM   9109 N N     . GLU B 1 597 ? 29.316  -61.383 11.428  1.00 40.46  ? 595 GLU B N     1 
ATOM   9110 C CA    . GLU B 1 597 ? 29.732  -60.618 10.224  1.00 42.36  ? 595 GLU B CA    1 
ATOM   9111 C C     . GLU B 1 597 ? 29.020  -61.098 8.963   1.00 37.06  ? 595 GLU B C     1 
ATOM   9112 O O     . GLU B 1 597 ? 29.233  -60.484 7.925   1.00 34.62  ? 595 GLU B O     1 
ATOM   9113 C CB    . GLU B 1 597 ? 31.231  -60.802 10.018  1.00 48.06  ? 595 GLU B CB    1 
ATOM   9114 C CG    . GLU B 1 597 ? 31.993  -61.010 11.310  1.00 60.69  ? 595 GLU B CG    1 
ATOM   9115 C CD    . GLU B 1 597 ? 32.245  -62.468 11.647  1.00 65.19  ? 595 GLU B CD    1 
ATOM   9116 O OE1   . GLU B 1 597 ? 32.090  -62.832 12.824  1.00 61.78  ? 595 GLU B OE1   1 
ATOM   9117 O OE2   . GLU B 1 597 ? 32.588  -63.232 10.726  1.00 68.67  ? 595 GLU B OE2   1 
ATOM   9118 N N     . ASP B 1 598 ? 28.199  -62.136 9.062   1.00 37.91  ? 596 ASP B N     1 
ATOM   9119 C CA    . ASP B 1 598 ? 27.548  -62.730 7.867   1.00 40.49  ? 596 ASP B CA    1 
ATOM   9120 C C     . ASP B 1 598 ? 26.039  -62.452 7.843   1.00 37.92  ? 596 ASP B C     1 
ATOM   9121 O O     . ASP B 1 598 ? 25.374  -62.981 6.952   1.00 41.70  ? 596 ASP B O     1 
ATOM   9122 C CB    . ASP B 1 598 ? 27.845  -64.227 7.808   1.00 43.81  ? 596 ASP B CB    1 
ATOM   9123 C CG    . ASP B 1 598 ? 29.305  -64.549 7.558   1.00 44.20  ? 596 ASP B CG    1 
ATOM   9124 O OD1   . ASP B 1 598 ? 30.041  -63.640 7.141   1.00 40.86  ? 596 ASP B OD1   1 
ATOM   9125 O OD2   . ASP B 1 598 ? 29.687  -65.708 7.780   1.00 41.77  ? 596 ASP B OD2   1 
ATOM   9126 N N     . PHE B 1 599 ? 25.532  -61.646 8.772   1.00 36.54  ? 597 PHE B N     1 
ATOM   9127 C CA    . PHE B 1 599 ? 24.074  -61.357 8.856   1.00 39.98  ? 597 PHE B CA    1 
ATOM   9128 C C     . PHE B 1 599 ? 23.640  -60.333 7.806   1.00 36.11  ? 597 PHE B C     1 
ATOM   9129 O O     . PHE B 1 599 ? 22.481  -60.389 7.404   1.00 38.92  ? 597 PHE B O     1 
ATOM   9130 C CB    . PHE B 1 599 ? 23.689  -60.832 10.243  1.00 36.38  ? 597 PHE B CB    1 
ATOM   9131 C CG    . PHE B 1 599 ? 23.391  -61.866 11.295  1.00 34.45  ? 597 PHE B CG    1 
ATOM   9132 C CD1   . PHE B 1 599 ? 24.413  -62.574 11.903  1.00 36.92  ? 597 PHE B CD1   1 
ATOM   9133 C CD2   . PHE B 1 599 ? 22.090  -62.105 11.704  1.00 34.93  ? 597 PHE B CD2   1 
ATOM   9134 C CE1   . PHE B 1 599 ? 24.137  -63.517 12.880  1.00 36.47  ? 597 PHE B CE1   1 
ATOM   9135 C CE2   . PHE B 1 599 ? 21.816  -63.044 12.683  1.00 33.79  ? 597 PHE B CE2   1 
ATOM   9136 C CZ    . PHE B 1 599 ? 22.840  -63.748 13.269  1.00 34.41  ? 597 PHE B CZ    1 
ATOM   9137 N N     . ALA B 1 600 ? 24.540  -59.457 7.362   1.00 36.23  ? 598 ALA B N     1 
ATOM   9138 C CA    . ALA B 1 600 ? 24.141  -58.354 6.459   1.00 38.99  ? 598 ALA B CA    1 
ATOM   9139 C C     . ALA B 1 600 ? 25.079  -58.228 5.256   1.00 42.58  ? 598 ALA B C     1 
ATOM   9140 O O     . ALA B 1 600 ? 25.598  -57.131 5.037   1.00 40.88  ? 598 ALA B O     1 
ATOM   9141 C CB    . ALA B 1 600 ? 24.106  -57.076 7.247   1.00 37.63  ? 598 ALA B CB    1 
ATOM   9142 N N     . LEU B 1 601 ? 25.251  -59.303 4.493   1.00 41.13  ? 599 LEU B N     1 
ATOM   9143 C CA    . LEU B 1 601 ? 26.152  -59.309 3.300   1.00 42.31  ? 599 LEU B CA    1 
ATOM   9144 C C     . LEU B 1 601 ? 25.420  -58.866 2.014   1.00 44.32  ? 599 LEU B C     1 
ATOM   9145 O O     . LEU B 1 601 ? 26.070  -58.870 0.945   1.00 39.25  ? 599 LEU B O     1 
ATOM   9146 C CB    . LEU B 1 601 ? 26.772  -60.706 3.162   1.00 40.66  ? 599 LEU B CB    1 
ATOM   9147 C CG    . LEU B 1 601 ? 27.590  -61.145 4.376   1.00 38.33  ? 599 LEU B CG    1 
ATOM   9148 C CD1   . LEU B 1 601 ? 28.115  -62.561 4.233   1.00 36.74  ? 599 LEU B CD1   1 
ATOM   9149 C CD2   . LEU B 1 601 ? 28.726  -60.180 4.619   1.00 37.04  ? 599 LEU B CD2   1 
ATOM   9150 N N     . GLY B 1 602 ? 24.141  -58.460 2.100   1.00 45.83  ? 600 GLY B N     1 
ATOM   9151 C CA    . GLY B 1 602 ? 23.299  -58.133 0.929   1.00 42.74  ? 600 GLY B CA    1 
ATOM   9152 C C     . GLY B 1 602 ? 23.328  -56.655 0.555   1.00 40.89  ? 600 GLY B C     1 
ATOM   9153 O O     . GLY B 1 602 ? 22.410  -56.229 -0.190  1.00 38.33  ? 600 GLY B O     1 
ATOM   9154 N N     . TYR B 1 603 ? 24.339  -55.898 1.013   1.00 39.89  ? 601 TYR B N     1 
ATOM   9155 C CA    . TYR B 1 603 ? 24.463  -54.425 0.806   1.00 39.61  ? 601 TYR B CA    1 
ATOM   9156 C C     . TYR B 1 603 ? 25.688  -54.186 -0.087  1.00 39.90  ? 601 TYR B C     1 
ATOM   9157 O O     . TYR B 1 603 ? 25.408  -54.255 -1.311  1.00 41.87  ? 601 TYR B O     1 
ATOM   9158 C CB    . TYR B 1 603 ? 24.446  -53.694 2.161   1.00 38.79  ? 601 TYR B CB    1 
ATOM   9159 C CG    . TYR B 1 603 ? 23.214  -54.030 2.963   1.00 39.44  ? 601 TYR B CG    1 
ATOM   9160 C CD1   . TYR B 1 603 ? 22.041  -53.300 2.850   1.00 39.05  ? 601 TYR B CD1   1 
ATOM   9161 C CD2   . TYR B 1 603 ? 23.180  -55.182 3.724   1.00 39.02  ? 601 TYR B CD2   1 
ATOM   9162 C CE1   . TYR B 1 603 ? 20.887  -53.691 3.518   1.00 41.99  ? 601 TYR B CE1   1 
ATOM   9163 C CE2   . TYR B 1 603 ? 22.050  -55.572 4.415   1.00 38.50  ? 601 TYR B CE2   1 
ATOM   9164 C CZ    . TYR B 1 603 ? 20.892  -54.836 4.304   1.00 38.31  ? 601 TYR B CZ    1 
ATOM   9165 O OH    . TYR B 1 603 ? 19.781  -55.314 4.943   1.00 35.66  ? 601 TYR B OH    1 
HETATM 9166 P PA    . FAD C 2 .   ? -14.251 -50.454 6.095   1.00 34.46  ? 701 FAD A PA    1 
HETATM 9167 O O1A   . FAD C 2 .   ? -15.383 -49.829 6.827   1.00 31.16  ? 701 FAD A O1A   1 
HETATM 9168 O O2A   . FAD C 2 .   ? -14.404 -50.724 4.642   1.00 40.79  ? 701 FAD A O2A   1 
HETATM 9169 O O5B   . FAD C 2 .   ? -13.810 -51.793 6.842   1.00 34.64  ? 701 FAD A O5B   1 
HETATM 9170 C C5B   . FAD C 2 .   ? -13.825 -51.823 8.287   1.00 30.32  ? 701 FAD A C5B   1 
HETATM 9171 C C4B   . FAD C 2 .   ? -13.470 -53.209 8.763   1.00 30.62  ? 701 FAD A C4B   1 
HETATM 9172 O O4B   . FAD C 2 .   ? -14.461 -54.149 8.275   1.00 29.17  ? 701 FAD A O4B   1 
HETATM 9173 C C3B   . FAD C 2 .   ? -12.117 -53.761 8.295   1.00 28.70  ? 701 FAD A C3B   1 
HETATM 9174 O O3B   . FAD C 2 .   ? -11.532 -54.592 9.287   1.00 25.73  ? 701 FAD A O3B   1 
HETATM 9175 C C2B   . FAD C 2 .   ? -12.514 -54.572 7.063   1.00 27.57  ? 701 FAD A C2B   1 
HETATM 9176 O O2B   . FAD C 2 .   ? -11.581 -55.565 6.706   1.00 27.28  ? 701 FAD A O2B   1 
HETATM 9177 C C1B   . FAD C 2 .   ? -13.819 -55.176 7.560   1.00 30.24  ? 701 FAD A C1B   1 
HETATM 9178 N N9A   . FAD C 2 .   ? -14.686 -55.609 6.488   1.00 30.62  ? 701 FAD A N9A   1 
HETATM 9179 C C8A   . FAD C 2 .   ? -15.457 -54.841 5.660   1.00 31.81  ? 701 FAD A C8A   1 
HETATM 9180 N N7A   . FAD C 2 .   ? -16.118 -55.555 4.782   1.00 30.35  ? 701 FAD A N7A   1 
HETATM 9181 C C5A   . FAD C 2 .   ? -15.754 -56.868 5.050   1.00 30.70  ? 701 FAD A C5A   1 
HETATM 9182 C C6A   . FAD C 2 .   ? -16.112 -58.098 4.469   1.00 27.41  ? 701 FAD A C6A   1 
HETATM 9183 N N6A   . FAD C 2 .   ? -16.953 -58.219 3.448   1.00 30.61  ? 701 FAD A N6A   1 
HETATM 9184 N N1A   . FAD C 2 .   ? -15.556 -59.214 4.990   1.00 26.78  ? 701 FAD A N1A   1 
HETATM 9185 C C2A   . FAD C 2 .   ? -14.707 -59.090 6.017   1.00 32.85  ? 701 FAD A C2A   1 
HETATM 9186 N N3A   . FAD C 2 .   ? -14.301 -57.992 6.643   1.00 27.99  ? 701 FAD A N3A   1 
HETATM 9187 C C4A   . FAD C 2 .   ? -14.869 -56.906 6.102   1.00 28.58  ? 701 FAD A C4A   1 
HETATM 9188 N N1    . FAD C 2 .   ? -8.611  -44.308 -0.531  1.00 34.04  ? 701 FAD A N1    1 
HETATM 9189 C C2    . FAD C 2 .   ? -8.495  -43.815 -1.770  1.00 31.67  ? 701 FAD A C2    1 
HETATM 9190 O O2    . FAD C 2 .   ? -9.382  -43.981 -2.589  1.00 27.91  ? 701 FAD A O2    1 
HETATM 9191 N N3    . FAD C 2 .   ? -7.382  -43.175 -2.192  1.00 31.15  ? 701 FAD A N3    1 
HETATM 9192 C C4    . FAD C 2 .   ? -6.311  -42.964 -1.367  1.00 30.10  ? 701 FAD A C4    1 
HETATM 9193 O O4    . FAD C 2 .   ? -5.343  -42.354 -1.781  1.00 26.88  ? 701 FAD A O4    1 
HETATM 9194 C C4X   . FAD C 2 .   ? -6.419  -43.395 -0.038  1.00 31.13  ? 701 FAD A C4X   1 
HETATM 9195 N N5    . FAD C 2 .   ? -5.433  -43.152 0.786   1.00 29.29  ? 701 FAD A N5    1 
HETATM 9196 C C5X   . FAD C 2 .   ? -5.613  -43.506 2.095   1.00 30.76  ? 701 FAD A C5X   1 
HETATM 9197 C C6    . FAD C 2 .   ? -4.607  -43.191 3.023   1.00 30.65  ? 701 FAD A C6    1 
HETATM 9198 C C7    . FAD C 2 .   ? -4.755  -43.479 4.358   1.00 30.81  ? 701 FAD A C7    1 
HETATM 9199 C C7M   . FAD C 2 .   ? -3.672  -43.099 5.332   1.00 36.66  ? 701 FAD A C7M   1 
HETATM 9200 C C8    . FAD C 2 .   ? -5.919  -44.151 4.800   1.00 32.73  ? 701 FAD A C8    1 
HETATM 9201 C C8M   . FAD C 2 .   ? -6.116  -44.500 6.251   1.00 35.25  ? 701 FAD A C8M   1 
HETATM 9202 C C9    . FAD C 2 .   ? -6.869  -44.524 3.895   1.00 33.31  ? 701 FAD A C9    1 
HETATM 9203 C C9A   . FAD C 2 .   ? -6.761  -44.182 2.542   1.00 30.02  ? 701 FAD A C9A   1 
HETATM 9204 N N10   . FAD C 2 .   ? -7.751  -44.490 1.619   1.00 32.57  ? 701 FAD A N10   1 
HETATM 9205 C C10   . FAD C 2 .   ? -7.638  -44.072 0.316   1.00 32.68  ? 701 FAD A C10   1 
HETATM 9206 C "C1'" . FAD C 2 .   ? -8.955  -45.210 2.064   1.00 31.22  ? 701 FAD A "C1'" 1 
HETATM 9207 C "C2'" . FAD C 2 .   ? -8.610  -46.669 2.399   1.00 32.66  ? 701 FAD A "C2'" 1 
HETATM 9208 O "O2'" . FAD C 2 .   ? -8.353  -47.426 1.221   1.00 29.57  ? 701 FAD A "O2'" 1 
HETATM 9209 C "C3'" . FAD C 2 .   ? -9.707  -47.342 3.228   1.00 35.53  ? 701 FAD A "C3'" 1 
HETATM 9210 O "O3'" . FAD C 2 .   ? -9.452  -47.074 4.590   1.00 33.17  ? 701 FAD A "O3'" 1 
HETATM 9211 C "C4'" . FAD C 2 .   ? -9.809  -48.858 3.062   1.00 39.85  ? 701 FAD A "C4'" 1 
HETATM 9212 O "O4'" . FAD C 2 .   ? -10.283 -49.169 1.751   1.00 37.35  ? 701 FAD A "O4'" 1 
HETATM 9213 C "C5'" . FAD C 2 .   ? -10.710 -49.488 4.099   1.00 38.92  ? 701 FAD A "C5'" 1 
HETATM 9214 O "O5'" . FAD C 2 .   ? -11.968 -48.762 4.164   1.00 36.73  ? 701 FAD A "O5'" 1 
HETATM 9215 P P     . FAD C 2 .   ? -12.501 -48.201 5.564   1.00 32.88  ? 701 FAD A P     1 
HETATM 9216 O O1P   . FAD C 2 .   ? -11.386 -47.583 6.325   1.00 33.91  ? 701 FAD A O1P   1 
HETATM 9217 O O2P   . FAD C 2 .   ? -13.708 -47.381 5.283   1.00 35.75  ? 701 FAD A O2P   1 
HETATM 9218 O O3P   . FAD C 2 .   ? -12.957 -49.544 6.295   1.00 36.35  ? 701 FAD A O3P   1 
HETATM 9219 C C1    . PEG D 3 .   ? -0.866  -56.269 -10.482 1.00 69.51  ? 702 PEG A C1    1 
HETATM 9220 O O1    . PEG D 3 .   ? -0.435  -56.214 -9.114  1.00 61.88  ? 702 PEG A O1    1 
HETATM 9221 C C2    . PEG D 3 .   ? -1.443  -57.626 -10.854 1.00 67.70  ? 702 PEG A C2    1 
HETATM 9222 O O2    . PEG D 3 .   ? -2.809  -57.532 -11.262 1.00 69.01  ? 702 PEG A O2    1 
HETATM 9223 C C3    . PEG D 3 .   ? -3.441  -58.796 -11.520 1.00 61.21  ? 702 PEG A C3    1 
HETATM 9224 C C4    . PEG D 3 .   ? -3.815  -59.485 -10.217 1.00 61.71  ? 702 PEG A C4    1 
HETATM 9225 O O4    . PEG D 3 .   ? -5.231  -59.521 -9.965  1.00 62.43  ? 702 PEG A O4    1 
HETATM 9226 N N1A   . CO8 E 4 .   ? -8.551  -57.970 -9.543  1.00 67.14  ? 703 CO8 A N1A   1 
HETATM 9227 C C2A   . CO8 E 4 .   ? -9.049  -57.337 -10.612 1.00 63.34  ? 703 CO8 A C2A   1 
HETATM 9228 N N3A   . CO8 E 4 .   ? -10.289 -56.913 -10.837 1.00 63.36  ? 703 CO8 A N3A   1 
HETATM 9229 C C4A   . CO8 E 4 .   ? -11.083 -57.207 -9.797  1.00 76.69  ? 703 CO8 A C4A   1 
HETATM 9230 C C5A   . CO8 E 4 .   ? -10.725 -57.855 -8.637  1.00 72.68  ? 703 CO8 A C5A   1 
HETATM 9231 C C6A   . CO8 E 4 .   ? -9.382  -58.256 -8.514  1.00 65.03  ? 703 CO8 A C6A   1 
HETATM 9232 N N6A   . CO8 E 4 .   ? -8.890  -58.884 -7.451  1.00 60.29  ? 703 CO8 A N6A   1 
HETATM 9233 N N7A   . CO8 E 4 .   ? -11.825 -57.975 -7.798  1.00 70.16  ? 703 CO8 A N7A   1 
HETATM 9234 C C8A   . CO8 E 4 .   ? -12.807 -57.405 -8.455  1.00 66.51  ? 703 CO8 A C8A   1 
HETATM 9235 N N9A   . CO8 E 4 .   ? -12.416 -56.927 -9.678  1.00 77.28  ? 703 CO8 A N9A   1 
HETATM 9236 C C1B   . CO8 E 4 .   ? -13.222 -56.222 -10.666 1.00 82.77  ? 703 CO8 A C1B   1 
HETATM 9237 C C2B   . CO8 E 4 .   ? -13.791 -57.097 -11.779 1.00 87.83  ? 703 CO8 A C2B   1 
HETATM 9238 O O2B   . CO8 E 4 .   ? -13.905 -56.374 -12.986 1.00 74.44  ? 703 CO8 A O2B   1 
HETATM 9239 C C3B   . CO8 E 4 .   ? -15.154 -57.499 -11.219 1.00 89.05  ? 703 CO8 A C3B   1 
HETATM 9240 O O3B   . CO8 E 4 .   ? -16.082 -57.690 -12.280 1.00 99.55  ? 703 CO8 A O3B   1 
HETATM 9241 P P3B   . CO8 E 4 .   ? -16.267 -59.247 -12.653 1.00 93.02  ? 703 CO8 A P3B   1 
HETATM 9242 O O7A   . CO8 E 4 .   ? -17.389 -59.302 -13.667 1.00 78.22  ? 703 CO8 A O7A   1 
HETATM 9243 O O8A   . CO8 E 4 .   ? -14.953 -59.715 -13.234 1.00 99.11  ? 703 CO8 A O8A   1 
HETATM 9244 O O9A   . CO8 E 4 .   ? -16.616 -59.969 -11.369 1.00 84.35  ? 703 CO8 A O9A   1 
HETATM 9245 C C4B   . CO8 E 4 .   ? -15.555 -56.278 -10.404 1.00 89.17  ? 703 CO8 A C4B   1 
HETATM 9246 O O4B   . CO8 E 4 .   ? -14.317 -55.645 -9.995  1.00 84.24  ? 703 CO8 A O4B   1 
HETATM 9247 C C5B   . CO8 E 4 .   ? -16.376 -56.580 -9.177  1.00 84.62  ? 703 CO8 A C5B   1 
HETATM 9248 O O5B   . CO8 E 4 .   ? -15.919 -57.823 -8.600  1.00 91.10  ? 703 CO8 A O5B   1 
HETATM 9249 P P1A   . CO8 E 4 .   ? -16.787 -58.458 -7.417  1.00 84.25  ? 703 CO8 A P1A   1 
HETATM 9250 O O1A   . CO8 E 4 .   ? -18.226 -58.453 -7.805  1.00 96.08  ? 703 CO8 A O1A   1 
HETATM 9251 O O2A   . CO8 E 4 .   ? -16.169 -59.741 -6.978  1.00 78.18  ? 703 CO8 A O2A   1 
HETATM 9252 O O3A   . CO8 E 4 .   ? -16.570 -57.362 -6.276  1.00 94.65  ? 703 CO8 A O3A   1 
HETATM 9253 P P2A   . CO8 E 4 .   ? -17.564 -56.284 -5.638  1.00 79.62  ? 703 CO8 A P2A   1 
HETATM 9254 O O4A   . CO8 E 4 .   ? -18.241 -55.550 -6.742  1.00 79.17  ? 703 CO8 A O4A   1 
HETATM 9255 O O5A   . CO8 E 4 .   ? -18.390 -56.936 -4.583  1.00 79.37  ? 703 CO8 A O5A   1 
HETATM 9256 O O6A   . CO8 E 4 .   ? -16.517 -55.306 -4.924  1.00 94.52  ? 703 CO8 A O6A   1 
HETATM 9257 C CBP   . CO8 E 4 .   ? -14.452 -54.068 -4.706  1.00 104.23 ? 703 CO8 A CBP   1 
HETATM 9258 C CCP   . CO8 E 4 .   ? -15.275 -54.982 -5.606  1.00 103.35 ? 703 CO8 A CCP   1 
HETATM 9259 C CDP   . CO8 E 4 .   ? -15.389 -53.276 -3.793  1.00 102.05 ? 703 CO8 A CDP   1 
HETATM 9260 C CEP   . CO8 E 4 .   ? -13.659 -53.082 -5.563  1.00 104.72 ? 703 CO8 A CEP   1 
HETATM 9261 C CAP   . CO8 E 4 .   ? -13.475 -54.905 -3.876  1.00 107.14 ? 703 CO8 A CAP   1 
HETATM 9262 O OAP   . CO8 E 4 .   ? -12.333 -55.154 -4.677  1.00 126.80 ? 703 CO8 A OAP   1 
HETATM 9263 C C9P   . CO8 E 4 .   ? -13.053 -54.259 -2.568  1.00 91.77  ? 703 CO8 A C9P   1 
HETATM 9264 O O9P   . CO8 E 4 .   ? -13.636 -54.561 -1.533  1.00 100.34 ? 703 CO8 A O9P   1 
HETATM 9265 N N8P   . CO8 E 4 .   ? -12.046 -53.399 -2.609  1.00 77.15  ? 703 CO8 A N8P   1 
HETATM 9266 C C7P   . CO8 E 4 .   ? -11.784 -52.422 -1.560  1.00 71.21  ? 703 CO8 A C7P   1 
HETATM 9267 C C6P   . CO8 E 4 .   ? -11.598 -51.024 -2.107  1.00 62.11  ? 703 CO8 A C6P   1 
HETATM 9268 C C5P   . CO8 E 4 .   ? -10.146 -50.601 -2.206  1.00 65.61  ? 703 CO8 A C5P   1 
HETATM 9269 O O5P   . CO8 E 4 .   ? -9.243  -51.432 -2.222  1.00 57.28  ? 703 CO8 A O5P   1 
HETATM 9270 N N4P   . CO8 E 4 .   ? -9.900  -49.290 -2.297  1.00 64.71  ? 703 CO8 A N4P   1 
HETATM 9271 C C3P   . CO8 E 4 .   ? -8.755  -48.634 -1.686  1.00 61.31  ? 703 CO8 A C3P   1 
HETATM 9272 C C2P   . CO8 E 4 .   ? -7.697  -48.266 -2.698  1.00 65.02  ? 703 CO8 A C2P   1 
HETATM 9273 S S1P   . CO8 E 4 .   ? -7.193  -46.527 -2.649  1.00 51.57  ? 703 CO8 A S1P   1 
HETATM 9274 C "C1'" . CO8 E 4 .   ? -5.921  -46.566 -1.438  1.00 51.49  ? 703 CO8 A "C1'" 1 
HETATM 9275 O "O1'" . CO8 E 4 .   ? -6.055  -47.066 -0.348  1.00 48.93  ? 703 CO8 A "O1'" 1 
HETATM 9276 C "C2'" . CO8 E 4 .   ? -4.659  -45.912 -1.906  1.00 51.41  ? 703 CO8 A "C2'" 1 
HETATM 9277 C "C3'" . CO8 E 4 .   ? -3.635  -45.711 -0.842  1.00 55.27  ? 703 CO8 A "C3'" 1 
HETATM 9278 C "C4'" . CO8 E 4 .   ? -2.454  -46.653 -0.978  1.00 61.89  ? 703 CO8 A "C4'" 1 
HETATM 9279 C "C5'" . CO8 E 4 .   ? -1.139  -45.964 -1.218  1.00 65.32  ? 703 CO8 A "C5'" 1 
HETATM 9280 C "C6'" . CO8 E 4 .   ? -0.116  -46.812 -1.930  1.00 66.30  ? 703 CO8 A "C6'" 1 
HETATM 9281 C "C7'" . CO8 E 4 .   ? 0.715   -46.055 -2.932  1.00 63.51  ? 703 CO8 A "C7'" 1 
HETATM 9282 C "C8'" . CO8 E 4 .   ? 1.610   -46.930 -3.775  1.00 59.88  ? 703 CO8 A "C8'" 1 
HETATM 9283 C C1    . PEG F 3 .   ? 6.092   -39.361 17.747  1.00 56.89  ? 704 PEG A C1    1 
HETATM 9284 O O1    . PEG F 3 .   ? 7.145   -40.353 17.857  1.00 48.03  ? 704 PEG A O1    1 
HETATM 9285 C C2    . PEG F 3 .   ? 4.788   -39.724 18.478  1.00 50.74  ? 704 PEG A C2    1 
HETATM 9286 O O2    . PEG F 3 .   ? 3.689   -39.864 17.566  1.00 55.40  ? 704 PEG A O2    1 
HETATM 9287 C C3    . PEG F 3 .   ? 3.395   -38.681 16.818  1.00 52.14  ? 704 PEG A C3    1 
HETATM 9288 C C4    . PEG F 3 .   ? 1.929   -38.627 16.507  1.00 54.06  ? 704 PEG A C4    1 
HETATM 9289 O O4    . PEG F 3 .   ? 1.470   -39.761 15.806  1.00 39.70  ? 704 PEG A O4    1 
HETATM 9290 P PA    . FAD G 2 .   ? 18.970  -53.365 26.676  1.00 34.04  ? 701 FAD B PA    1 
HETATM 9291 O O1A   . FAD G 2 .   ? 19.005  -53.780 28.104  1.00 35.59  ? 701 FAD B O1A   1 
HETATM 9292 O O2A   . FAD G 2 .   ? 20.228  -52.900 26.037  1.00 28.79  ? 701 FAD B O2A   1 
HETATM 9293 O O5B   . FAD G 2 .   ? 18.323  -54.528 25.799  1.00 29.44  ? 701 FAD B O5B   1 
HETATM 9294 C C5B   . FAD G 2 .   ? 18.357  -54.412 24.362  1.00 30.57  ? 701 FAD B C5B   1 
HETATM 9295 C C4B   . FAD G 2 .   ? 17.904  -55.715 23.756  1.00 30.60  ? 701 FAD B C4B   1 
HETATM 9296 O O4B   . FAD G 2 .   ? 18.805  -56.769 24.182  1.00 31.36  ? 701 FAD B O4B   1 
HETATM 9297 C C3B   . FAD G 2 .   ? 16.501  -56.190 24.153  1.00 31.48  ? 701 FAD B C3B   1 
HETATM 9298 O O3B   . FAD G 2 .   ? 15.871  -56.855 23.068  1.00 38.35  ? 701 FAD B O3B   1 
HETATM 9299 C C2B   . FAD G 2 .   ? 16.799  -57.157 25.298  1.00 33.26  ? 701 FAD B C2B   1 
HETATM 9300 O O2B   . FAD G 2 .   ? 15.779  -58.102 25.519  1.00 35.48  ? 701 FAD B O2B   1 
HETATM 9301 C C1B   . FAD G 2 .   ? 18.065  -57.812 24.766  1.00 33.00  ? 701 FAD B C1B   1 
HETATM 9302 N N9A   . FAD G 2 .   ? 18.874  -58.430 25.791  1.00 33.18  ? 701 FAD B N9A   1 
HETATM 9303 C C8A   . FAD G 2 .   ? 19.722  -57.826 26.677  1.00 34.62  ? 701 FAD B C8A   1 
HETATM 9304 N N7A   . FAD G 2 .   ? 20.309  -58.683 27.477  1.00 34.38  ? 701 FAD B N7A   1 
HETATM 9305 C C5A   . FAD G 2 .   ? 19.811  -59.920 27.092  1.00 35.81  ? 701 FAD B C5A   1 
HETATM 9306 C C6A   . FAD G 2 .   ? 20.040  -61.228 27.553  1.00 40.60  ? 701 FAD B C6A   1 
HETATM 9307 N N6A   . FAD G 2 .   ? 20.868  -61.529 28.548  1.00 41.63  ? 701 FAD B N6A   1 
HETATM 9308 N N1A   . FAD G 2 .   ? 19.371  -62.228 26.936  1.00 37.50  ? 701 FAD B N1A   1 
HETATM 9309 C C2A   . FAD G 2 .   ? 18.537  -61.923 25.935  1.00 36.15  ? 701 FAD B C2A   1 
HETATM 9310 N N3A   . FAD G 2 .   ? 18.246  -60.735 25.418  1.00 32.43  ? 701 FAD B N3A   1 
HETATM 9311 C C4A   . FAD G 2 .   ? 18.925  -59.769 26.051  1.00 33.97  ? 701 FAD B C4A   1 
HETATM 9312 N N1    . FAD G 2 .   ? 14.159  -47.294 33.846  1.00 37.36  ? 701 FAD B N1    1 
HETATM 9313 C C2    . FAD G 2 .   ? 14.115  -46.968 35.147  1.00 36.97  ? 701 FAD B C2    1 
HETATM 9314 O O2    . FAD G 2 .   ? 14.989  -47.345 35.915  1.00 30.80  ? 701 FAD B O2    1 
HETATM 9315 N N3    . FAD G 2 .   ? 13.093  -46.256 35.676  1.00 34.37  ? 701 FAD B N3    1 
HETATM 9316 C C4    . FAD G 2 .   ? 12.048  -45.809 34.913  1.00 33.18  ? 701 FAD B C4    1 
HETATM 9317 O O4    . FAD G 2 .   ? 11.165  -45.147 35.430  1.00 27.22  ? 701 FAD B O4    1 
HETATM 9318 C C4X   . FAD G 2 .   ? 12.085  -46.076 33.537  1.00 33.16  ? 701 FAD B C4X   1 
HETATM 9319 N N5    . FAD G 2 .   ? 11.123  -45.616 32.779  1.00 32.76  ? 701 FAD B N5    1 
HETATM 9320 C C5X   . FAD G 2 .   ? 11.232  -45.829 31.431  1.00 36.21  ? 701 FAD B C5X   1 
HETATM 9321 C C6    . FAD G 2 .   ? 10.248  -45.292 30.586  1.00 34.33  ? 701 FAD B C6    1 
HETATM 9322 C C7    . FAD G 2 .   ? 10.325  -45.434 29.222  1.00 35.37  ? 701 FAD B C7    1 
HETATM 9323 C C7M   . FAD G 2 .   ? 9.268   -44.822 28.341  1.00 40.25  ? 701 FAD B C7M   1 
HETATM 9324 C C8    . FAD G 2 .   ? 11.390  -46.172 28.658  1.00 33.51  ? 701 FAD B C8    1 
HETATM 9325 C C8M   . FAD G 2 .   ? 11.491  -46.363 27.168  1.00 33.38  ? 701 FAD B C8M   1 
HETATM 9326 C C9    . FAD G 2 .   ? 12.320  -46.753 29.477  1.00 32.65  ? 701 FAD B C9    1 
HETATM 9327 C C9A   . FAD G 2 .   ? 12.283  -46.572 30.865  1.00 32.84  ? 701 FAD B C9A   1 
HETATM 9328 N N10   . FAD G 2 .   ? 13.250  -47.097 31.713  1.00 38.20  ? 701 FAD B N10   1 
HETATM 9329 C C10   . FAD G 2 .   ? 13.208  -46.840 33.064  1.00 35.31  ? 701 FAD B C10   1 
HETATM 9330 C "C1'" . FAD G 2 .   ? 14.357  -47.883 31.146  1.00 36.07  ? 701 FAD B "C1'" 1 
HETATM 9331 C "C2'" . FAD G 2 .   ? 13.872  -49.273 30.747  1.00 38.67  ? 701 FAD B "C2'" 1 
HETATM 9332 O "O2'" . FAD G 2 .   ? 13.614  -50.060 31.902  1.00 35.37  ? 701 FAD B "O2'" 1 
HETATM 9333 C "C3'" . FAD G 2 .   ? 14.881  -49.985 29.843  1.00 38.29  ? 701 FAD B "C3'" 1 
HETATM 9334 O "O3'" . FAD G 2 .   ? 14.746  -49.472 28.535  1.00 33.72  ? 701 FAD B "O3'" 1 
HETATM 9335 C "C4'" . FAD G 2 .   ? 14.715  -51.502 29.766  1.00 38.80  ? 701 FAD B "C4'" 1 
HETATM 9336 O "O4'" . FAD G 2 .   ? 15.134  -52.094 30.996  1.00 41.36  ? 701 FAD B "O4'" 1 
HETATM 9337 C "C5'" . FAD G 2 .   ? 15.505  -52.100 28.626  1.00 41.45  ? 701 FAD B "C5'" 1 
HETATM 9338 O "O5'" . FAD G 2 .   ? 16.882  -51.648 28.716  1.00 40.69  ? 701 FAD B "O5'" 1 
HETATM 9339 P P     . FAD G 2 .   ? 17.580  -50.960 27.454  1.00 39.97  ? 701 FAD B P     1 
HETATM 9340 O O1P   . FAD G 2 .   ? 16.614  -50.062 26.768  1.00 39.68  ? 701 FAD B O1P   1 
HETATM 9341 O O2P   . FAD G 2 .   ? 18.873  -50.395 27.923  1.00 33.35  ? 701 FAD B O2P   1 
HETATM 9342 O O3P   . FAD G 2 .   ? 17.872  -52.221 26.524  1.00 33.36  ? 701 FAD B O3P   1 
HETATM 9343 N N1A   . CO8 H 4 .   ? 12.553  -61.830 41.772  1.00 74.18  ? 702 CO8 B N1A   1 
HETATM 9344 C C2A   . CO8 H 4 .   ? 13.133  -61.392 42.898  1.00 77.79  ? 702 CO8 B C2A   1 
HETATM 9345 N N3A   . CO8 H 4 .   ? 14.412  -61.112 43.132  1.00 84.81  ? 702 CO8 B N3A   1 
HETATM 9346 C C4A   . CO8 H 4 .   ? 15.151  -61.328 42.032  1.00 103.26 ? 702 CO8 B C4A   1 
HETATM 9347 C C5A   . CO8 H 4 .   ? 14.706  -61.777 40.809  1.00 98.12  ? 702 CO8 B C5A   1 
HETATM 9348 C C6A   . CO8 H 4 .   ? 13.330  -62.039 40.683  1.00 78.53  ? 702 CO8 B C6A   1 
HETATM 9349 N N6A   . CO8 H 4 .   ? 12.760  -62.468 39.563  1.00 66.95  ? 702 CO8 B N6A   1 
HETATM 9350 N N7A   . CO8 H 4 .   ? 15.769  -61.875 39.920  1.00 90.65  ? 702 CO8 B N7A   1 
HETATM 9351 C C8A   . CO8 H 4 .   ? 16.816  -61.490 40.611  1.00 91.02  ? 702 CO8 B C8A   1 
HETATM 9352 N N9A   . CO8 H 4 .   ? 16.500  -61.150 41.900  1.00 104.79 ? 702 CO8 B N9A   1 
HETATM 9353 C C1B   . CO8 H 4 .   ? 17.392  -60.666 42.941  1.00 110.96 ? 702 CO8 B C1B   1 
HETATM 9354 C C2B   . CO8 H 4 .   ? 17.756  -61.712 43.991  1.00 105.62 ? 702 CO8 B C2B   1 
HETATM 9355 O O2B   . CO8 H 4 .   ? 17.971  -61.095 45.240  1.00 89.85  ? 702 CO8 B O2B   1 
HETATM 9356 C C3B   . CO8 H 4 .   ? 19.026  -62.322 43.403  1.00 106.59 ? 702 CO8 B C3B   1 
HETATM 9357 O O3B   . CO8 H 4 .   ? 19.855  -62.840 44.438  1.00 108.34 ? 702 CO8 B O3B   1 
HETATM 9358 P P3B   . CO8 H 4 .   ? 20.237  -64.384 44.179  1.00 99.21  ? 702 CO8 B P3B   1 
HETATM 9359 O O7A   . CO8 H 4 .   ? 18.940  -65.134 43.973  1.00 107.13 ? 702 CO8 B O7A   1 
HETATM 9360 O O8A   . CO8 H 4 .   ? 21.120  -64.424 42.952  1.00 114.13 ? 702 CO8 B O8A   1 
HETATM 9361 O O9A   . CO8 H 4 .   ? 20.971  -64.847 45.419  1.00 98.74  ? 702 CO8 B O9A   1 
HETATM 9362 C C4B   . CO8 H 4 .   ? 19.686  -61.116 42.750  1.00 108.74 ? 702 CO8 B C4B   1 
HETATM 9363 O O4B   . CO8 H 4 .   ? 18.595  -60.258 42.332  1.00 110.79 ? 702 CO8 B O4B   1 
HETATM 9364 C C5B   . CO8 H 4 .   ? 20.533  -61.441 41.546  1.00 96.68  ? 702 CO8 B C5B   1 
HETATM 9365 O O5B   . CO8 H 4 .   ? 19.828  -62.400 40.731  1.00 93.91  ? 702 CO8 B O5B   1 
HETATM 9366 P P1A   . CO8 H 4 .   ? 20.537  -62.898 39.389  1.00 86.30  ? 702 CO8 B P1A   1 
HETATM 9367 O O1A   . CO8 H 4 .   ? 21.933  -63.319 39.699  1.00 92.18  ? 702 CO8 B O1A   1 
HETATM 9368 O O2A   . CO8 H 4 .   ? 19.638  -63.856 38.686  1.00 70.41  ? 702 CO8 B O2A   1 
HETATM 9369 O O3A   . CO8 H 4 .   ? 20.593  -61.527 38.566  1.00 96.58  ? 702 CO8 B O3A   1 
HETATM 9370 P P2A   . CO8 H 4 .   ? 21.816  -60.661 38.000  1.00 100.11 ? 702 CO8 B P2A   1 
HETATM 9371 O O4A   . CO8 H 4 .   ? 22.725  -60.299 39.124  1.00 83.76  ? 702 CO8 B O4A   1 
HETATM 9372 O O5A   . CO8 H 4 .   ? 22.379  -61.338 36.795  1.00 91.45  ? 702 CO8 B O5A   1 
HETATM 9373 O O6A   . CO8 H 4 .   ? 21.067  -59.333 37.518  1.00 87.21  ? 702 CO8 B O6A   1 
HETATM 9374 C CBP   . CO8 H 4 .   ? 19.256  -58.326 36.304  1.00 86.58  ? 702 CO8 B CBP   1 
HETATM 9375 C CCP   . CO8 H 4 .   ? 20.404  -59.325 36.228  1.00 87.47  ? 702 CO8 B CCP   1 
HETATM 9376 C CDP   . CO8 H 4 .   ? 19.824  -56.950 36.659  1.00 80.45  ? 702 CO8 B CDP   1 
HETATM 9377 C CEP   . CO8 H 4 .   ? 18.297  -58.757 37.417  1.00 81.44  ? 702 CO8 B CEP   1 
HETATM 9378 C CAP   . CO8 H 4 .   ? 18.503  -58.241 34.970  1.00 82.42  ? 702 CO8 B CAP   1 
HETATM 9379 O OAP   . CO8 H 4 .   ? 18.265  -59.526 34.422  1.00 61.34  ? 702 CO8 B OAP   1 
HETATM 9380 C C9P   . CO8 H 4 .   ? 17.194  -57.483 35.092  1.00 78.91  ? 702 CO8 B C9P   1 
HETATM 9381 O O9P   . CO8 H 4 .   ? 16.169  -58.077 35.415  1.00 69.55  ? 702 CO8 B O9P   1 
HETATM 9382 N N8P   . CO8 H 4 .   ? 17.226  -56.184 34.835  1.00 81.40  ? 702 CO8 B N8P   1 
HETATM 9383 C C7P   . CO8 H 4 .   ? 16.570  -55.595 33.678  1.00 84.57  ? 702 CO8 B C7P   1 
HETATM 9384 C C6P   . CO8 H 4 .   ? 15.087  -55.852 33.680  1.00 90.46  ? 702 CO8 B C6P   1 
HETATM 9385 C C5P   . CO8 H 4 .   ? 14.398  -55.005 34.726  1.00 91.52  ? 702 CO8 B C5P   1 
HETATM 9386 O O5P   . CO8 H 4 .   ? 13.352  -55.372 35.254  1.00 95.56  ? 702 CO8 B O5P   1 
HETATM 9387 N N4P   . CO8 H 4 .   ? 14.978  -53.848 35.041  1.00 87.42  ? 702 CO8 B N4P   1 
HETATM 9388 C C3P   . CO8 H 4 .   ? 14.301  -52.823 35.817  1.00 92.66  ? 702 CO8 B C3P   1 
HETATM 9389 C C2P   . CO8 H 4 .   ? 13.340  -52.029 34.976  1.00 85.49  ? 702 CO8 B C2P   1 
HETATM 9390 S S1P   . CO8 H 4 .   ? 13.783  -50.279 35.081  1.00 99.42  ? 702 CO8 B S1P   1 
HETATM 9391 C "C1'" . CO8 H 4 .   ? 12.202  -49.544 35.272  1.00 64.69  ? 702 CO8 B "C1'" 1 
HETATM 9392 O "O1'" . CO8 H 4 .   ? 11.894  -48.902 36.242  1.00 45.81  ? 702 CO8 B "O1'" 1 
HETATM 9393 C "C2'" . CO8 H 4 .   ? 11.291  -49.799 34.107  1.00 59.61  ? 702 CO8 B "C2'" 1 
HETATM 9394 C "C3'" . CO8 H 4 .   ? 10.304  -48.710 33.842  1.00 65.66  ? 702 CO8 B "C3'" 1 
HETATM 9395 C "C4'" . CO8 H 4 .   ? 9.180   -48.651 34.859  1.00 69.28  ? 702 CO8 B "C4'" 1 
HETATM 9396 C "C5'" . CO8 H 4 .   ? 7.891   -48.092 34.325  1.00 72.65  ? 702 CO8 B "C5'" 1 
HETATM 9397 C "C6'" . CO8 H 4 .   ? 6.739   -49.064 34.355  1.00 81.62  ? 702 CO8 B "C6'" 1 
HETATM 9398 C "C7'" . CO8 H 4 .   ? 5.395   -48.426 34.590  1.00 77.70  ? 702 CO8 B "C7'" 1 
HETATM 9399 C "C8'" . CO8 H 4 .   ? 4.633   -48.998 35.760  1.00 68.60  ? 702 CO8 B "C8'" 1 
HETATM 9400 O O     . HOH I 5 .   ? -3.292  -65.004 -23.574 1.00 44.95  ? 801 HOH A O     1 
HETATM 9401 O O     . HOH I 5 .   ? 2.927   -46.259 -20.754 1.00 42.96  ? 802 HOH A O     1 
HETATM 9402 O O     . HOH I 5 .   ? -2.129  -40.468 -27.508 1.00 43.54  ? 803 HOH A O     1 
HETATM 9403 O O     . HOH I 5 .   ? 19.214  -57.268 -11.975 1.00 37.17  ? 804 HOH A O     1 
HETATM 9404 O O     . HOH I 5 .   ? -5.619  -58.334 -7.323  1.00 31.16  ? 805 HOH A O     1 
HETATM 9405 O O     . HOH I 5 .   ? -23.087 -63.362 8.747   1.00 28.56  ? 806 HOH A O     1 
HETATM 9406 O O     . HOH I 5 .   ? -2.585  -56.081 4.371   1.00 20.69  ? 807 HOH A O     1 
HETATM 9407 O O     . HOH I 5 .   ? 15.669  -60.223 23.939  1.00 29.27  ? 808 HOH A O     1 
HETATM 9408 O O     . HOH I 5 .   ? -8.759  -67.858 13.069  1.00 28.10  ? 809 HOH A O     1 
HETATM 9409 O O     . HOH I 5 .   ? 11.770  -73.932 -8.947  1.00 34.50  ? 810 HOH A O     1 
HETATM 9410 O O     . HOH I 5 .   ? -21.008 -63.070 7.007   1.00 37.28  ? 811 HOH A O     1 
HETATM 9411 O O     . HOH I 5 .   ? 1.166   -65.704 11.050  1.00 28.50  ? 812 HOH A O     1 
HETATM 9412 O O     . HOH I 5 .   ? -8.852  -37.094 4.567   1.00 32.14  ? 813 HOH A O     1 
HETATM 9413 O O     . HOH I 5 .   ? -21.959 -44.121 -13.388 1.00 41.79  ? 814 HOH A O     1 
HETATM 9414 O O     . HOH I 5 .   ? 20.985  -64.683 3.679   1.00 36.71  ? 815 HOH A O     1 
HETATM 9415 O O     . HOH I 5 .   ? 19.165  -50.800 24.205  1.00 28.65  ? 816 HOH A O     1 
HETATM 9416 O O     . HOH I 5 .   ? -25.453 -59.358 14.082  1.00 35.22  ? 817 HOH A O     1 
HETATM 9417 O O     . HOH I 5 .   ? 4.016   -53.373 6.667   1.00 24.87  ? 818 HOH A O     1 
HETATM 9418 O O     . HOH I 5 .   ? -19.412 -71.257 20.374  1.00 43.96  ? 819 HOH A O     1 
HETATM 9419 O O     . HOH I 5 .   ? 4.393   -28.874 6.948   1.00 33.28  ? 820 HOH A O     1 
HETATM 9420 O O     . HOH I 5 .   ? -11.860 -47.296 -1.095  1.00 40.57  ? 821 HOH A O     1 
HETATM 9421 O O     . HOH I 5 .   ? -20.122 -60.959 26.982  1.00 29.58  ? 822 HOH A O     1 
HETATM 9422 O O     . HOH I 5 .   ? 30.303  -56.461 17.789  1.00 30.00  ? 823 HOH A O     1 
HETATM 9423 O O     . HOH I 5 .   ? -14.537 -44.955 4.622   1.00 31.38  ? 824 HOH A O     1 
HETATM 9424 O O     . HOH I 5 .   ? 16.862  -62.686 -0.976  1.00 27.61  ? 825 HOH A O     1 
HETATM 9425 O O     . HOH I 5 .   ? 7.657   -57.878 4.745   1.00 26.81  ? 826 HOH A O     1 
HETATM 9426 O O     . HOH I 5 .   ? 24.287  -66.416 24.467  1.00 41.24  ? 827 HOH A O     1 
HETATM 9427 O O     . HOH I 5 .   ? -11.574 -57.871 8.058   1.00 26.14  ? 828 HOH A O     1 
HETATM 9428 O O     . HOH I 5 .   ? -1.752  -40.602 2.580   1.00 35.91  ? 829 HOH A O     1 
HETATM 9429 O O     . HOH I 5 .   ? 11.430  -50.827 13.159  1.00 29.90  ? 830 HOH A O     1 
HETATM 9430 O O     . HOH I 5 .   ? 23.337  -63.737 2.464   1.00 38.27  ? 831 HOH A O     1 
HETATM 9431 O O     . HOH I 5 .   ? 1.320   -29.241 -6.755  1.00 31.31  ? 832 HOH A O     1 
HETATM 9432 O O     . HOH I 5 .   ? 24.498  -51.597 -9.356  1.00 30.00  ? 833 HOH A O     1 
HETATM 9433 O O     . HOH I 5 .   ? 0.418   -38.321 -6.436  1.00 33.38  ? 834 HOH A O     1 
HETATM 9434 O O     . HOH I 5 .   ? 8.745   -29.505 0.506   1.00 30.00  ? 835 HOH A O     1 
HETATM 9435 O O     . HOH I 5 .   ? -9.032  -66.826 9.323   1.00 30.00  ? 836 HOH A O     1 
HETATM 9436 O O     . HOH I 5 .   ? -24.685 -65.197 22.239  1.00 33.14  ? 837 HOH A O     1 
HETATM 9437 O O     . HOH I 5 .   ? -7.402  -66.249 1.784   1.00 42.54  ? 838 HOH A O     1 
HETATM 9438 O O     . HOH I 5 .   ? -0.670  -35.914 -6.253  1.00 37.29  ? 839 HOH A O     1 
HETATM 9439 O O     . HOH I 5 .   ? -21.612 -70.312 10.857  1.00 31.86  ? 840 HOH A O     1 
HETATM 9440 O O     . HOH I 5 .   ? -10.528 -52.692 2.134   1.00 28.01  ? 841 HOH A O     1 
HETATM 9441 O O     . HOH I 5 .   ? -15.668 -45.382 -16.583 1.00 41.48  ? 842 HOH A O     1 
HETATM 9442 O O     . HOH I 5 .   ? -17.294 -69.871 19.935  1.00 34.09  ? 843 HOH A O     1 
HETATM 9443 O O     . HOH I 5 .   ? 6.459   -39.331 7.131   1.00 23.27  ? 844 HOH A O     1 
HETATM 9444 O O     . HOH I 5 .   ? -10.670 -64.739 8.497   1.00 30.31  ? 845 HOH A O     1 
HETATM 9445 O O     . HOH I 5 .   ? -16.695 -74.161 14.899  1.00 30.00  ? 846 HOH A O     1 
HETATM 9446 O O     . HOH I 5 .   ? 11.230  -42.863 14.995  1.00 37.13  ? 847 HOH A O     1 
HETATM 9447 O O     . HOH I 5 .   ? -4.503  -41.047 -4.082  1.00 31.75  ? 848 HOH A O     1 
HETATM 9448 O O     . HOH I 5 .   ? 13.181  -45.675 17.559  1.00 33.95  ? 849 HOH A O     1 
HETATM 9449 O O     . HOH I 5 .   ? 7.804   -42.429 5.573   1.00 25.45  ? 850 HOH A O     1 
HETATM 9450 O O     . HOH I 5 .   ? -22.209 -72.758 16.933  1.00 49.63  ? 851 HOH A O     1 
HETATM 9451 O O     . HOH I 5 .   ? 5.704   -40.489 9.362   1.00 26.60  ? 852 HOH A O     1 
HETATM 9452 O O     . HOH I 5 .   ? -25.178 -38.333 -11.221 1.00 42.69  ? 853 HOH A O     1 
HETATM 9453 O O     . HOH I 5 .   ? -12.027 -61.926 5.706   1.00 35.42  ? 854 HOH A O     1 
HETATM 9454 O O     . HOH I 5 .   ? 26.793  -50.509 24.151  1.00 34.25  ? 855 HOH A O     1 
HETATM 9455 O O     . HOH I 5 .   ? -18.862 -52.562 -3.120  1.00 30.11  ? 856 HOH A O     1 
HETATM 9456 O O     . HOH I 5 .   ? 8.861   -39.016 5.933   1.00 26.62  ? 857 HOH A O     1 
HETATM 9457 O O     . HOH I 5 .   ? -2.505  -35.843 6.363   1.00 29.08  ? 858 HOH A O     1 
HETATM 9458 O O     . HOH I 5 .   ? 19.113  -39.218 -9.972  1.00 30.76  ? 859 HOH A O     1 
HETATM 9459 O O     . HOH I 5 .   ? -18.087 -50.313 -12.607 1.00 28.55  ? 860 HOH A O     1 
HETATM 9460 O O     . HOH I 5 .   ? 21.239  -49.995 -22.282 1.00 35.02  ? 861 HOH A O     1 
HETATM 9461 O O     . HOH I 5 .   ? 21.814  -61.480 1.860   1.00 36.15  ? 862 HOH A O     1 
HETATM 9462 O O     . HOH I 5 .   ? -16.472 -61.999 4.916   1.00 30.00  ? 863 HOH A O     1 
HETATM 9463 O O     . HOH I 5 .   ? 27.171  -63.923 18.428  1.00 26.00  ? 864 HOH A O     1 
HETATM 9464 O O     . HOH I 5 .   ? -19.657 -37.874 -0.601  1.00 49.87  ? 865 HOH A O     1 
HETATM 9465 O O     . HOH I 5 .   ? -2.439  -28.700 9.040   1.00 33.84  ? 866 HOH A O     1 
HETATM 9466 O O     . HOH I 5 .   ? 30.478  -63.372 1.053   1.00 31.92  ? 867 HOH A O     1 
HETATM 9467 O O     . HOH I 5 .   ? 10.678  -52.018 -0.374  1.00 35.90  ? 868 HOH A O     1 
HETATM 9468 O O     . HOH I 5 .   ? 19.297  -65.294 -17.021 1.00 36.12  ? 869 HOH A O     1 
HETATM 9469 O O     . HOH I 5 .   ? -18.977 -67.450 18.693  1.00 36.55  ? 870 HOH A O     1 
HETATM 9470 O O     . HOH I 5 .   ? 1.824   -27.432 -16.802 1.00 30.98  ? 871 HOH A O     1 
HETATM 9471 O O     . HOH I 5 .   ? 25.780  -55.531 -20.410 1.00 43.39  ? 872 HOH A O     1 
HETATM 9472 O O     . HOH I 5 .   ? 18.151  -65.152 24.856  1.00 31.82  ? 873 HOH A O     1 
HETATM 9473 O O     . HOH I 5 .   ? -0.449  -36.918 9.741   1.00 19.44  ? 874 HOH A O     1 
HETATM 9474 O O     . HOH I 5 .   ? -5.214  -58.005 -4.948  1.00 46.95  ? 875 HOH A O     1 
HETATM 9475 O O     . HOH I 5 .   ? 16.506  -42.524 -15.371 1.00 30.00  ? 876 HOH A O     1 
HETATM 9476 O O     . HOH I 5 .   ? 23.395  -48.418 15.650  1.00 30.00  ? 877 HOH A O     1 
HETATM 9477 O O     . HOH I 5 .   ? 10.469  -64.974 -18.566 1.00 30.00  ? 878 HOH A O     1 
HETATM 9478 O O     . HOH J 5 .   ? 14.976  -29.233 54.421  1.00 45.71  ? 801 HOH B O     1 
HETATM 9479 O O     . HOH J 5 .   ? 8.045   -45.531 61.244  1.00 30.00  ? 802 HOH B O     1 
HETATM 9480 O O     . HOH J 5 .   ? -7.754  -36.358 11.455  1.00 33.96  ? 803 HOH B O     1 
HETATM 9481 O O     . HOH J 5 .   ? 19.988  -71.254 10.878  1.00 36.28  ? 804 HOH B O     1 
HETATM 9482 O O     . HOH J 5 .   ? 14.216  -32.199 39.959  1.00 37.78  ? 805 HOH B O     1 
HETATM 9483 O O     . HOH J 5 .   ? 27.226  -50.056 46.833  1.00 41.36  ? 806 HOH B O     1 
HETATM 9484 O O     . HOH J 5 .   ? -3.389  -58.331 27.312  1.00 23.95  ? 807 HOH B O     1 
HETATM 9485 O O     . HOH J 5 .   ? 11.759  -69.178 17.834  1.00 28.05  ? 808 HOH B O     1 
HETATM 9486 O O     . HOH J 5 .   ? 10.381  -68.774 29.271  1.00 46.67  ? 809 HOH B O     1 
HETATM 9487 O O     . HOH J 5 .   ? -1.474  -30.930 34.930  1.00 35.60  ? 810 HOH B O     1 
HETATM 9488 O O     . HOH J 5 .   ? -13.293 -57.569 29.272  1.00 29.94  ? 811 HOH B O     1 
HETATM 9489 O O     . HOH J 5 .   ? -13.415 -62.700 32.669  1.00 38.32  ? 812 HOH B O     1 
HETATM 9490 O O     . HOH J 5 .   ? 2.436   -66.380 20.041  1.00 29.63  ? 813 HOH B O     1 
HETATM 9491 O O     . HOH J 5 .   ? 7.732   -42.488 31.197  1.00 35.88  ? 814 HOH B O     1 
HETATM 9492 O O     . HOH J 5 .   ? -14.061 -48.083 8.845   1.00 28.94  ? 815 HOH B O     1 
HETATM 9493 O O     . HOH J 5 .   ? -25.600 -53.461 14.720  1.00 30.00  ? 816 HOH B O     1 
HETATM 9494 O O     . HOH J 5 .   ? 13.701  -38.202 22.978  1.00 32.95  ? 817 HOH B O     1 
HETATM 9495 O O     . HOH J 5 .   ? -1.310  -39.870 16.028  1.00 35.23  ? 818 HOH B O     1 
HETATM 9496 O O     . HOH J 5 .   ? 2.866   -41.409 46.525  1.00 33.62  ? 819 HOH B O     1 
HETATM 9497 O O     . HOH J 5 .   ? 16.961  -50.597 34.084  1.00 28.72  ? 820 HOH B O     1 
HETATM 9498 O O     . HOH J 5 .   ? 5.819   -41.255 40.371  1.00 42.16  ? 821 HOH B O     1 
HETATM 9499 O O     . HOH J 5 .   ? -20.057 -62.732 29.348  1.00 37.49  ? 822 HOH B O     1 
HETATM 9500 O O     . HOH J 5 .   ? 0.394   -54.395 25.865  1.00 27.62  ? 823 HOH B O     1 
HETATM 9501 O O     . HOH J 5 .   ? 0.166   -28.211 34.591  1.00 41.42  ? 824 HOH B O     1 
HETATM 9502 O O     . HOH J 5 .   ? 15.282  -55.535 30.549  1.00 31.94  ? 825 HOH B O     1 
HETATM 9503 O O     . HOH J 5 .   ? 27.781  -67.608 9.182   1.00 43.22  ? 826 HOH B O     1 
HETATM 9504 O O     . HOH J 5 .   ? 7.284   -38.851 40.750  1.00 30.00  ? 827 HOH B O     1 
HETATM 9505 O O     . HOH J 5 .   ? -7.436  -64.075 15.698  1.00 33.74  ? 828 HOH B O     1 
HETATM 9506 O O     . HOH J 5 .   ? -5.359  -42.080 18.618  1.00 23.24  ? 829 HOH B O     1 
HETATM 9507 O O     . HOH J 5 .   ? 19.901  -64.863 26.802  1.00 27.55  ? 830 HOH B O     1 
HETATM 9508 O O     . HOH J 5 .   ? -3.973  -28.304 34.077  1.00 45.99  ? 831 HOH B O     1 
HETATM 9509 O O     . HOH J 5 .   ? 10.231  -44.121 37.745  1.00 39.60  ? 832 HOH B O     1 
HETATM 9510 O O     . HOH J 5 .   ? 0.430   -41.043 24.553  1.00 31.09  ? 833 HOH B O     1 
HETATM 9511 O O     . HOH J 5 .   ? 15.779  -64.696 25.993  1.00 41.39  ? 834 HOH B O     1 
HETATM 9512 O O     . HOH J 5 .   ? -9.561  -39.342 26.260  1.00 34.66  ? 835 HOH B O     1 
HETATM 9513 O O     . HOH J 5 .   ? 8.524   -29.785 37.833  1.00 38.30  ? 836 HOH B O     1 
HETATM 9514 O O     . HOH J 5 .   ? 15.172  -39.625 29.620  1.00 27.62  ? 837 HOH B O     1 
HETATM 9515 O O     . HOH J 5 .   ? -7.365  -44.445 16.056  1.00 26.71  ? 838 HOH B O     1 
HETATM 9516 O O     . HOH J 5 .   ? -19.357 -73.443 19.064  1.00 49.46  ? 839 HOH B O     1 
HETATM 9517 O O     . HOH J 5 .   ? 20.103  -48.030 28.622  1.00 29.92  ? 840 HOH B O     1 
HETATM 9518 O O     . HOH J 5 .   ? 22.010  -69.230 12.719  1.00 36.04  ? 841 HOH B O     1 
HETATM 9519 O O     . HOH J 5 .   ? -6.509  -50.079 19.865  1.00 29.41  ? 842 HOH B O     1 
HETATM 9520 O O     . HOH J 5 .   ? 12.059  -58.745 45.803  1.00 46.13  ? 843 HOH B O     1 
HETATM 9521 O O     . HOH J 5 .   ? -2.867  -39.516 28.360  1.00 27.44  ? 844 HOH B O     1 
HETATM 9522 O O     . HOH J 5 .   ? -5.840  -57.467 13.157  1.00 31.74  ? 845 HOH B O     1 
HETATM 9523 O O     . HOH J 5 .   ? 26.731  -66.753 22.603  1.00 36.27  ? 846 HOH B O     1 
HETATM 9524 O O     . HOH J 5 .   ? 7.052   -57.938 27.876  1.00 29.06  ? 847 HOH B O     1 
HETATM 9525 O O     . HOH J 5 .   ? 23.930  -62.075 4.729   1.00 28.10  ? 848 HOH B O     1 
HETATM 9526 O O     . HOH J 5 .   ? -0.251  -39.722 27.108  1.00 28.89  ? 849 HOH B O     1 
HETATM 9527 O O     . HOH J 5 .   ? -20.845 -57.736 0.412   1.00 37.56  ? 850 HOH B O     1 
HETATM 9528 O O     . HOH J 5 .   ? 20.914  -51.091 49.773  1.00 43.76  ? 851 HOH B O     1 
HETATM 9529 O O     . HOH J 5 .   ? 12.888  -34.428 41.018  1.00 37.53  ? 852 HOH B O     1 
HETATM 9530 O O     . HOH J 5 .   ? -5.790  -52.782 33.072  1.00 40.23  ? 853 HOH B O     1 
HETATM 9531 O O     . HOH J 5 .   ? -5.821  -59.659 11.155  1.00 30.00  ? 854 HOH B O     1 
HETATM 9532 O O     . HOH J 5 .   ? 13.227  -58.444 24.219  1.00 28.42  ? 855 HOH B O     1 
HETATM 9533 O O     . HOH J 5 .   ? 13.561  -29.755 34.401  1.00 30.00  ? 856 HOH B O     1 
HETATM 9534 O O     . HOH J 5 .   ? -10.559 -44.181 49.118  1.00 33.66  ? 857 HOH B O     1 
HETATM 9535 O O     . HOH J 5 .   ? -23.414 -60.787 13.253  1.00 21.58  ? 858 HOH B O     1 
HETATM 9536 O O     . HOH J 5 .   ? 21.932  -59.211 4.009   1.00 36.55  ? 859 HOH B O     1 
HETATM 9537 O O     . HOH J 5 .   ? -8.859  -56.407 7.923   1.00 24.44  ? 860 HOH B O     1 
HETATM 9538 O O     . HOH J 5 .   ? 5.429   -31.008 51.826  1.00 26.35  ? 861 HOH B O     1 
HETATM 9539 O O     . HOH J 5 .   ? -2.834  -77.084 20.450  1.00 27.99  ? 862 HOH B O     1 
HETATM 9540 O O     . HOH J 5 .   ? -14.630 -62.553 6.872   1.00 27.78  ? 863 HOH B O     1 
HETATM 9541 O O     . HOH J 5 .   ? -17.257 -77.526 19.379  1.00 39.48  ? 864 HOH B O     1 
HETATM 9542 O O     . HOH J 5 .   ? 6.788   -37.977 24.447  1.00 18.50  ? 865 HOH B O     1 
HETATM 9543 O O     . HOH J 5 .   ? 30.000  -47.296 32.035  1.00 37.64  ? 866 HOH B O     1 
HETATM 9544 O O     . HOH J 5 .   ? 4.837   -35.803 23.581  1.00 36.71  ? 867 HOH B O     1 
HETATM 9545 O O     . HOH J 5 .   ? -6.850  -77.934 17.649  1.00 30.00  ? 868 HOH B O     1 
# 
