data_9EF0
# 
_entry.id   9EF0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9EF0         pdb_00009ef0 10.2210/pdb9ef0/pdb 
WWPDB D_1000290308 ?            ?                   
EMDB  EMD-40857    ?            ?                   
# 
_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       2024-12-04 
# 
_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                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EF0 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          EMD-40857 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              galina.i.lepesheva@vanderbilt.edu 
_pdbx_contact_author.name_first         Galina 
_pdbx_contact_author.name_last          Lepesheva 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6975-1131 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lepesheva, G.I.' 1 0000-0002-6975-1131 
'Ren, Y.'         2 0000-0001-9550-2713 
# 
_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                     'Structural state of cytochrome P450 reductase in solution' 
_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 'Lepesheva, G.I.' 1 0000-0002-6975-1131 
primary 'Ren, Y.'         2 ?                   
# 
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 'NADPH--cytochrome P450 reductase' 77057.766 1 1.6.2.4 ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'            456.344   1 ?       ? ? ? 
3 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'      785.550   1 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        CPR,P450R 
# 
_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       
;MGDSHEDTSATMPEAVAEEVSLFSTTDMVLFSLIVGVLTYWFIFRKKKEEIPEFSKIQTTAPPVKESSFVEKMKKTGRNI
IVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETD
VDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEES
SIRQYELVVHEDMDVAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESGDHV
AVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQE
HLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEA
KSGRVNKGVATSWLRAKEPAGENGGRALVPMFVRKSQFRLPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGET
LLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEGGAHIYVCGDARNMAKDV
QNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGDSHEDTSATMPEAVAEEVSLFSTTDMVLFSLIVGVLTYWFIFRKKKEEIPEFSKIQTTAPPVKESSFVEKMKKTGRNI
IVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETD
VDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEES
SIRQYELVVHEDMDVAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESGDHV
AVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQE
HLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEA
KSGRVNKGVATSWLRAKEPAGENGGRALVPMFVRKSQFRLPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGET
LLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEGGAHIYVCGDARNMAKDV
QNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN MONONUCLEOTIDE'       FMN 
3 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   ASP n 
1 4   SER n 
1 5   HIS n 
1 6   GLU n 
1 7   ASP n 
1 8   THR n 
1 9   SER n 
1 10  ALA n 
1 11  THR n 
1 12  MET n 
1 13  PRO n 
1 14  GLU n 
1 15  ALA n 
1 16  VAL n 
1 17  ALA n 
1 18  GLU n 
1 19  GLU n 
1 20  VAL n 
1 21  SER n 
1 22  LEU n 
1 23  PHE n 
1 24  SER n 
1 25  THR n 
1 26  THR n 
1 27  ASP n 
1 28  MET n 
1 29  VAL n 
1 30  LEU n 
1 31  PHE n 
1 32  SER n 
1 33  LEU n 
1 34  ILE n 
1 35  VAL n 
1 36  GLY n 
1 37  VAL n 
1 38  LEU n 
1 39  THR n 
1 40  TYR n 
1 41  TRP n 
1 42  PHE n 
1 43  ILE n 
1 44  PHE n 
1 45  ARG n 
1 46  LYS n 
1 47  LYS n 
1 48  LYS n 
1 49  GLU n 
1 50  GLU n 
1 51  ILE n 
1 52  PRO n 
1 53  GLU n 
1 54  PHE n 
1 55  SER n 
1 56  LYS n 
1 57  ILE n 
1 58  GLN n 
1 59  THR n 
1 60  THR n 
1 61  ALA n 
1 62  PRO n 
1 63  PRO n 
1 64  VAL n 
1 65  LYS n 
1 66  GLU n 
1 67  SER n 
1 68  SER n 
1 69  PHE n 
1 70  VAL n 
1 71  GLU n 
1 72  LYS n 
1 73  MET n 
1 74  LYS n 
1 75  LYS n 
1 76  THR n 
1 77  GLY n 
1 78  ARG n 
1 79  ASN n 
1 80  ILE n 
1 81  ILE n 
1 82  VAL n 
1 83  PHE n 
1 84  TYR n 
1 85  GLY n 
1 86  SER n 
1 87  GLN n 
1 88  THR n 
1 89  GLY n 
1 90  THR n 
1 91  ALA n 
1 92  GLU n 
1 93  GLU n 
1 94  PHE n 
1 95  ALA n 
1 96  ASN n 
1 97  ARG n 
1 98  LEU n 
1 99  SER n 
1 100 LYS n 
1 101 ASP n 
1 102 ALA n 
1 103 HIS n 
1 104 ARG n 
1 105 TYR n 
1 106 GLY n 
1 107 MET n 
1 108 ARG n 
1 109 GLY n 
1 110 MET n 
1 111 SER n 
1 112 ALA n 
1 113 ASP n 
1 114 PRO n 
1 115 GLU n 
1 116 GLU n 
1 117 TYR n 
1 118 ASP n 
1 119 LEU n 
1 120 ALA n 
1 121 ASP n 
1 122 LEU n 
1 123 SER n 
1 124 SER n 
1 125 LEU n 
1 126 PRO n 
1 127 GLU n 
1 128 ILE n 
1 129 ASP n 
1 130 LYS n 
1 131 SER n 
1 132 LEU n 
1 133 VAL n 
1 134 VAL n 
1 135 PHE n 
1 136 CYS n 
1 137 MET n 
1 138 ALA n 
1 139 THR n 
1 140 TYR n 
1 141 GLY n 
1 142 GLU n 
1 143 GLY n 
1 144 ASP n 
1 145 PRO n 
1 146 THR n 
1 147 ASP n 
1 148 ASN n 
1 149 ALA n 
1 150 GLN n 
1 151 ASP n 
1 152 PHE n 
1 153 TYR n 
1 154 ASP n 
1 155 TRP n 
1 156 LEU n 
1 157 GLN n 
1 158 GLU n 
1 159 THR n 
1 160 ASP n 
1 161 VAL n 
1 162 ASP n 
1 163 LEU n 
1 164 THR n 
1 165 GLY n 
1 166 VAL n 
1 167 LYS n 
1 168 PHE n 
1 169 ALA n 
1 170 VAL n 
1 171 PHE n 
1 172 GLY n 
1 173 LEU n 
1 174 GLY n 
1 175 ASN n 
1 176 LYS n 
1 177 THR n 
1 178 TYR n 
1 179 GLU n 
1 180 HIS n 
1 181 PHE n 
1 182 ASN n 
1 183 ALA n 
1 184 MET n 
1 185 GLY n 
1 186 LYS n 
1 187 TYR n 
1 188 VAL n 
1 189 ASP n 
1 190 GLN n 
1 191 ARG n 
1 192 LEU n 
1 193 GLU n 
1 194 GLN n 
1 195 LEU n 
1 196 GLY n 
1 197 ALA n 
1 198 GLN n 
1 199 ARG n 
1 200 ILE n 
1 201 PHE n 
1 202 GLU n 
1 203 LEU n 
1 204 GLY n 
1 205 LEU n 
1 206 GLY n 
1 207 ASP n 
1 208 ASP n 
1 209 ASP n 
1 210 GLY n 
1 211 ASN n 
1 212 LEU n 
1 213 GLU n 
1 214 GLU n 
1 215 ASP n 
1 216 PHE n 
1 217 ILE n 
1 218 THR n 
1 219 TRP n 
1 220 ARG n 
1 221 GLU n 
1 222 GLN n 
1 223 PHE n 
1 224 TRP n 
1 225 PRO n 
1 226 ALA n 
1 227 VAL n 
1 228 CYS n 
1 229 GLU n 
1 230 PHE n 
1 231 PHE n 
1 232 GLY n 
1 233 VAL n 
1 234 GLU n 
1 235 ALA n 
1 236 THR n 
1 237 GLY n 
1 238 GLU n 
1 239 GLU n 
1 240 SER n 
1 241 SER n 
1 242 ILE n 
1 243 ARG n 
1 244 GLN n 
1 245 TYR n 
1 246 GLU n 
1 247 LEU n 
1 248 VAL n 
1 249 VAL n 
1 250 HIS n 
1 251 GLU n 
1 252 ASP n 
1 253 MET n 
1 254 ASP n 
1 255 VAL n 
1 256 ALA n 
1 257 LYS n 
1 258 VAL n 
1 259 TYR n 
1 260 THR n 
1 261 GLY n 
1 262 GLU n 
1 263 MET n 
1 264 GLY n 
1 265 ARG n 
1 266 LEU n 
1 267 LYS n 
1 268 SER n 
1 269 TYR n 
1 270 GLU n 
1 271 ASN n 
1 272 GLN n 
1 273 LYS n 
1 274 PRO n 
1 275 PRO n 
1 276 PHE n 
1 277 ASP n 
1 278 ALA n 
1 279 LYS n 
1 280 ASN n 
1 281 PRO n 
1 282 PHE n 
1 283 LEU n 
1 284 ALA n 
1 285 ALA n 
1 286 VAL n 
1 287 THR n 
1 288 ALA n 
1 289 ASN n 
1 290 ARG n 
1 291 LYS n 
1 292 LEU n 
1 293 ASN n 
1 294 GLN n 
1 295 GLY n 
1 296 THR n 
1 297 GLU n 
1 298 ARG n 
1 299 HIS n 
1 300 LEU n 
1 301 MET n 
1 302 HIS n 
1 303 LEU n 
1 304 GLU n 
1 305 LEU n 
1 306 ASP n 
1 307 ILE n 
1 308 SER n 
1 309 ASP n 
1 310 SER n 
1 311 LYS n 
1 312 ILE n 
1 313 ARG n 
1 314 TYR n 
1 315 GLU n 
1 316 SER n 
1 317 GLY n 
1 318 ASP n 
1 319 HIS n 
1 320 VAL n 
1 321 ALA n 
1 322 VAL n 
1 323 TYR n 
1 324 PRO n 
1 325 ALA n 
1 326 ASN n 
1 327 ASP n 
1 328 SER n 
1 329 ALA n 
1 330 LEU n 
1 331 VAL n 
1 332 ASN n 
1 333 GLN n 
1 334 ILE n 
1 335 GLY n 
1 336 GLU n 
1 337 ILE n 
1 338 LEU n 
1 339 GLY n 
1 340 ALA n 
1 341 ASP n 
1 342 LEU n 
1 343 ASP n 
1 344 VAL n 
1 345 ILE n 
1 346 MET n 
1 347 SER n 
1 348 LEU n 
1 349 ASN n 
1 350 ASN n 
1 351 LEU n 
1 352 ASP n 
1 353 GLU n 
1 354 GLU n 
1 355 SER n 
1 356 ASN n 
1 357 LYS n 
1 358 LYS n 
1 359 HIS n 
1 360 PRO n 
1 361 PHE n 
1 362 PRO n 
1 363 CYS n 
1 364 PRO n 
1 365 THR n 
1 366 THR n 
1 367 TYR n 
1 368 ARG n 
1 369 THR n 
1 370 ALA n 
1 371 LEU n 
1 372 THR n 
1 373 TYR n 
1 374 TYR n 
1 375 LEU n 
1 376 ASP n 
1 377 ILE n 
1 378 THR n 
1 379 ASN n 
1 380 PRO n 
1 381 PRO n 
1 382 ARG n 
1 383 THR n 
1 384 ASN n 
1 385 VAL n 
1 386 LEU n 
1 387 TYR n 
1 388 GLU n 
1 389 LEU n 
1 390 ALA n 
1 391 GLN n 
1 392 TYR n 
1 393 ALA n 
1 394 SER n 
1 395 GLU n 
1 396 PRO n 
1 397 SER n 
1 398 GLU n 
1 399 GLN n 
1 400 GLU n 
1 401 HIS n 
1 402 LEU n 
1 403 HIS n 
1 404 LYS n 
1 405 MET n 
1 406 ALA n 
1 407 SER n 
1 408 SER n 
1 409 SER n 
1 410 GLY n 
1 411 GLU n 
1 412 GLY n 
1 413 LYS n 
1 414 GLU n 
1 415 LEU n 
1 416 TYR n 
1 417 LEU n 
1 418 SER n 
1 419 TRP n 
1 420 VAL n 
1 421 VAL n 
1 422 GLU n 
1 423 ALA n 
1 424 ARG n 
1 425 ARG n 
1 426 HIS n 
1 427 ILE n 
1 428 LEU n 
1 429 ALA n 
1 430 ILE n 
1 431 LEU n 
1 432 GLN n 
1 433 ASP n 
1 434 TYR n 
1 435 PRO n 
1 436 SER n 
1 437 LEU n 
1 438 ARG n 
1 439 PRO n 
1 440 PRO n 
1 441 ILE n 
1 442 ASP n 
1 443 HIS n 
1 444 LEU n 
1 445 CYS n 
1 446 GLU n 
1 447 LEU n 
1 448 LEU n 
1 449 PRO n 
1 450 ARG n 
1 451 LEU n 
1 452 GLN n 
1 453 ALA n 
1 454 ARG n 
1 455 TYR n 
1 456 TYR n 
1 457 SER n 
1 458 ILE n 
1 459 ALA n 
1 460 SER n 
1 461 SER n 
1 462 SER n 
1 463 LYS n 
1 464 VAL n 
1 465 HIS n 
1 466 PRO n 
1 467 ASN n 
1 468 SER n 
1 469 VAL n 
1 470 HIS n 
1 471 ILE n 
1 472 CYS n 
1 473 ALA n 
1 474 VAL n 
1 475 ALA n 
1 476 VAL n 
1 477 GLU n 
1 478 TYR n 
1 479 GLU n 
1 480 ALA n 
1 481 LYS n 
1 482 SER n 
1 483 GLY n 
1 484 ARG n 
1 485 VAL n 
1 486 ASN n 
1 487 LYS n 
1 488 GLY n 
1 489 VAL n 
1 490 ALA n 
1 491 THR n 
1 492 SER n 
1 493 TRP n 
1 494 LEU n 
1 495 ARG n 
1 496 ALA n 
1 497 LYS n 
1 498 GLU n 
1 499 PRO n 
1 500 ALA n 
1 501 GLY n 
1 502 GLU n 
1 503 ASN n 
1 504 GLY n 
1 505 GLY n 
1 506 ARG n 
1 507 ALA n 
1 508 LEU n 
1 509 VAL n 
1 510 PRO n 
1 511 MET n 
1 512 PHE n 
1 513 VAL n 
1 514 ARG n 
1 515 LYS n 
1 516 SER n 
1 517 GLN n 
1 518 PHE n 
1 519 ARG n 
1 520 LEU n 
1 521 PRO n 
1 522 PHE n 
1 523 LYS n 
1 524 SER n 
1 525 THR n 
1 526 THR n 
1 527 PRO n 
1 528 VAL n 
1 529 ILE n 
1 530 MET n 
1 531 VAL n 
1 532 GLY n 
1 533 PRO n 
1 534 GLY n 
1 535 THR n 
1 536 GLY n 
1 537 ILE n 
1 538 ALA n 
1 539 PRO n 
1 540 PHE n 
1 541 MET n 
1 542 GLY n 
1 543 PHE n 
1 544 ILE n 
1 545 GLN n 
1 546 GLU n 
1 547 ARG n 
1 548 ALA n 
1 549 TRP n 
1 550 LEU n 
1 551 ARG n 
1 552 GLU n 
1 553 GLN n 
1 554 GLY n 
1 555 LYS n 
1 556 GLU n 
1 557 VAL n 
1 558 GLY n 
1 559 GLU n 
1 560 THR n 
1 561 LEU n 
1 562 LEU n 
1 563 TYR n 
1 564 TYR n 
1 565 GLY n 
1 566 CYS n 
1 567 ARG n 
1 568 ARG n 
1 569 SER n 
1 570 ASP n 
1 571 GLU n 
1 572 ASP n 
1 573 TYR n 
1 574 LEU n 
1 575 TYR n 
1 576 ARG n 
1 577 GLU n 
1 578 GLU n 
1 579 LEU n 
1 580 ALA n 
1 581 ARG n 
1 582 PHE n 
1 583 HIS n 
1 584 LYS n 
1 585 ASP n 
1 586 GLY n 
1 587 ALA n 
1 588 LEU n 
1 589 THR n 
1 590 GLN n 
1 591 LEU n 
1 592 ASN n 
1 593 VAL n 
1 594 ALA n 
1 595 PHE n 
1 596 SER n 
1 597 ARG n 
1 598 GLU n 
1 599 GLN n 
1 600 ALA n 
1 601 HIS n 
1 602 LYS n 
1 603 VAL n 
1 604 TYR n 
1 605 VAL n 
1 606 GLN n 
1 607 HIS n 
1 608 LEU n 
1 609 LEU n 
1 610 LYS n 
1 611 ARG n 
1 612 ASP n 
1 613 ARG n 
1 614 GLU n 
1 615 HIS n 
1 616 LEU n 
1 617 TRP n 
1 618 LYS n 
1 619 LEU n 
1 620 ILE n 
1 621 HIS n 
1 622 GLU n 
1 623 GLY n 
1 624 GLY n 
1 625 ALA n 
1 626 HIS n 
1 627 ILE n 
1 628 TYR n 
1 629 VAL n 
1 630 CYS n 
1 631 GLY n 
1 632 ASP n 
1 633 ALA n 
1 634 ARG n 
1 635 ASN n 
1 636 MET n 
1 637 ALA n 
1 638 LYS n 
1 639 ASP n 
1 640 VAL n 
1 641 GLN n 
1 642 ASN n 
1 643 THR n 
1 644 PHE n 
1 645 TYR n 
1 646 ASP n 
1 647 ILE n 
1 648 VAL n 
1 649 ALA n 
1 650 GLU n 
1 651 PHE n 
1 652 GLY n 
1 653 PRO n 
1 654 MET n 
1 655 GLU n 
1 656 HIS n 
1 657 THR n 
1 658 GLN n 
1 659 ALA n 
1 660 VAL n 
1 661 ASP n 
1 662 TYR n 
1 663 VAL n 
1 664 LYS n 
1 665 LYS n 
1 666 LEU n 
1 667 MET n 
1 668 THR n 
1 669 LYS n 
1 670 GLY n 
1 671 ARG n 
1 672 TYR n 
1 673 SER n 
1 674 LEU n 
1 675 ASP n 
1 676 VAL n 
1 677 TRP n 
1 678 SER 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                   678 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Por 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_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 
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 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE'       'RIBOFLAVIN MONOPHOSPHATE' 'C17 H21 N4 O9 P'   456.344 
GLN 'L-peptide linking' y GLUTAMINE                     ?                          'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ?                          'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ?                          'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ?                          'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                    ?                          'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ?                          'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ?                          'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ?                          'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                 ?                          'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ?                          'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ?                          'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ?                          'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ?                          'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ?                          'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ?                          'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLY 2   2   ?   ?   ?   A . n 
A 1 3   ASP 3   3   ?   ?   ?   A . n 
A 1 4   SER 4   4   ?   ?   ?   A . n 
A 1 5   HIS 5   5   ?   ?   ?   A . n 
A 1 6   GLU 6   6   ?   ?   ?   A . n 
A 1 7   ASP 7   7   ?   ?   ?   A . n 
A 1 8   THR 8   8   ?   ?   ?   A . n 
A 1 9   SER 9   9   ?   ?   ?   A . n 
A 1 10  ALA 10  10  ?   ?   ?   A . n 
A 1 11  THR 11  11  ?   ?   ?   A . n 
A 1 12  MET 12  12  ?   ?   ?   A . n 
A 1 13  PRO 13  13  ?   ?   ?   A . n 
A 1 14  GLU 14  14  ?   ?   ?   A . n 
A 1 15  ALA 15  15  ?   ?   ?   A . n 
A 1 16  VAL 16  16  ?   ?   ?   A . n 
A 1 17  ALA 17  17  ?   ?   ?   A . n 
A 1 18  GLU 18  18  ?   ?   ?   A . n 
A 1 19  GLU 19  19  ?   ?   ?   A . n 
A 1 20  VAL 20  20  ?   ?   ?   A . n 
A 1 21  SER 21  21  ?   ?   ?   A . n 
A 1 22  LEU 22  22  ?   ?   ?   A . n 
A 1 23  PHE 23  23  ?   ?   ?   A . n 
A 1 24  SER 24  24  ?   ?   ?   A . n 
A 1 25  THR 25  25  ?   ?   ?   A . n 
A 1 26  THR 26  26  ?   ?   ?   A . n 
A 1 27  ASP 27  27  ?   ?   ?   A . n 
A 1 28  MET 28  28  ?   ?   ?   A . n 
A 1 29  VAL 29  29  ?   ?   ?   A . n 
A 1 30  LEU 30  30  ?   ?   ?   A . n 
A 1 31  PHE 31  31  ?   ?   ?   A . n 
A 1 32  SER 32  32  ?   ?   ?   A . n 
A 1 33  LEU 33  33  ?   ?   ?   A . n 
A 1 34  ILE 34  34  ?   ?   ?   A . n 
A 1 35  VAL 35  35  ?   ?   ?   A . n 
A 1 36  GLY 36  36  ?   ?   ?   A . n 
A 1 37  VAL 37  37  ?   ?   ?   A . n 
A 1 38  LEU 38  38  ?   ?   ?   A . n 
A 1 39  THR 39  39  ?   ?   ?   A . n 
A 1 40  TYR 40  40  ?   ?   ?   A . n 
A 1 41  TRP 41  41  ?   ?   ?   A . n 
A 1 42  PHE 42  42  ?   ?   ?   A . n 
A 1 43  ILE 43  43  ?   ?   ?   A . n 
A 1 44  PHE 44  44  ?   ?   ?   A . n 
A 1 45  ARG 45  45  ?   ?   ?   A . n 
A 1 46  LYS 46  46  ?   ?   ?   A . n 
A 1 47  LYS 47  47  ?   ?   ?   A . n 
A 1 48  LYS 48  48  ?   ?   ?   A . n 
A 1 49  GLU 49  49  ?   ?   ?   A . n 
A 1 50  GLU 50  50  ?   ?   ?   A . n 
A 1 51  ILE 51  51  ?   ?   ?   A . n 
A 1 52  PRO 52  52  ?   ?   ?   A . n 
A 1 53  GLU 53  53  ?   ?   ?   A . n 
A 1 54  PHE 54  54  ?   ?   ?   A . n 
A 1 55  SER 55  55  ?   ?   ?   A . n 
A 1 56  LYS 56  56  ?   ?   ?   A . n 
A 1 57  ILE 57  57  ?   ?   ?   A . n 
A 1 58  GLN 58  58  ?   ?   ?   A . n 
A 1 59  THR 59  59  ?   ?   ?   A . n 
A 1 60  THR 60  60  ?   ?   ?   A . n 
A 1 61  ALA 61  61  ?   ?   ?   A . n 
A 1 62  PRO 62  62  ?   ?   ?   A . n 
A 1 63  PRO 63  63  ?   ?   ?   A . n 
A 1 64  VAL 64  64  ?   ?   ?   A . n 
A 1 65  LYS 65  65  ?   ?   ?   A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  PHE 69  69  69  PHE PHE A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ILE 81  81  81  ILE ILE A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  TYR 84  84  84  TYR TYR A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  GLN 87  87  87  GLN GLN A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 MET 107 107 107 MET MET A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 PRO 114 114 114 PRO PRO A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 ILE 128 128 128 ILE ILE A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 CYS 136 136 136 CYS CYS A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 ALA 138 138 138 ALA ALA A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 TYR 153 153 153 TYR TYR A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 TRP 155 155 155 TRP TRP A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 ASN 182 182 182 ASN ASN A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 MET 184 184 184 MET MET A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 TYR 187 187 187 TYR TYR A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 GLN 190 190 190 GLN GLN A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 GLN 194 194 194 GLN GLN A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 GLN 198 198 198 GLN GLN A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 GLY 206 206 206 GLY GLY A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ASP 209 209 209 ASP ASP A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 TRP 219 219 219 TRP TRP A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 GLN 222 222 222 GLN GLN A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 TRP 224 224 224 TRP TRP A . n 
A 1 225 PRO 225 225 225 PRO PRO A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 CYS 228 228 228 CYS CYS A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 VAL 248 248 248 VAL VAL A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 GLU 251 251 251 GLU GLU A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 MET 253 253 253 MET MET A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 TYR 259 259 259 TYR TYR A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 MET 263 263 263 MET MET A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 LYS 267 267 267 LYS LYS A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 PRO 274 274 274 PRO PRO A . n 
A 1 275 PRO 275 275 275 PRO PRO A . n 
A 1 276 PHE 276 276 276 PHE PHE A . n 
A 1 277 ASP 277 277 277 ASP ASP A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 ASN 280 280 280 ASN ASN A . n 
A 1 281 PRO 281 281 281 PRO PRO A . n 
A 1 282 PHE 282 282 282 PHE PHE A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 ARG 290 290 290 ARG ARG A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 THR 296 296 296 THR THR A . n 
A 1 297 GLU 297 297 297 GLU GLU A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 HIS 299 299 299 HIS HIS A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 MET 301 301 301 MET MET A . n 
A 1 302 HIS 302 302 302 HIS HIS A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 ASP 306 306 306 ASP ASP A . n 
A 1 307 ILE 307 307 307 ILE ILE A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 ARG 313 313 313 ARG ARG A . n 
A 1 314 TYR 314 314 314 TYR TYR A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 HIS 319 319 319 HIS HIS A . n 
A 1 320 VAL 320 320 320 VAL VAL A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 TYR 323 323 323 TYR TYR A . n 
A 1 324 PRO 324 324 324 PRO PRO A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 ASN 326 326 326 ASN ASN A . n 
A 1 327 ASP 327 327 327 ASP ASP A . n 
A 1 328 SER 328 328 328 SER SER A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 GLN 333 333 333 GLN GLN A . n 
A 1 334 ILE 334 334 334 ILE ILE A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 GLU 336 336 336 GLU GLU A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 ASP 341 341 341 ASP ASP A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 MET 346 346 346 MET MET A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 ASN 349 349 349 ASN ASN A . n 
A 1 350 ASN 350 350 350 ASN ASN A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 LYS 357 357 357 LYS LYS A . n 
A 1 358 LYS 358 358 358 LYS LYS A . n 
A 1 359 HIS 359 359 359 HIS HIS A . n 
A 1 360 PRO 360 360 360 PRO PRO A . n 
A 1 361 PHE 361 361 361 PHE PHE A . n 
A 1 362 PRO 362 362 362 PRO PRO A . n 
A 1 363 CYS 363 363 363 CYS CYS A . n 
A 1 364 PRO 364 364 364 PRO PRO A . n 
A 1 365 THR 365 365 365 THR THR A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 TYR 367 367 367 TYR TYR A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 THR 369 369 369 THR THR A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 THR 372 372 372 THR THR A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 TYR 374 374 374 TYR TYR A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 ASP 376 376 376 ASP ASP A . n 
A 1 377 ILE 377 377 377 ILE ILE A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 ASN 379 379 379 ASN ASN A . n 
A 1 380 PRO 380 380 380 PRO PRO A . n 
A 1 381 PRO 381 381 381 PRO PRO A . n 
A 1 382 ARG 382 382 382 ARG ARG A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 TYR 387 387 387 TYR TYR A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 GLN 391 391 391 GLN GLN A . n 
A 1 392 TYR 392 392 392 TYR TYR A . n 
A 1 393 ALA 393 393 393 ALA ALA A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 GLU 395 395 395 GLU GLU A . n 
A 1 396 PRO 396 396 396 PRO PRO A . n 
A 1 397 SER 397 397 397 SER SER A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 GLN 399 399 399 GLN GLN A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 HIS 401 401 401 HIS HIS A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 HIS 403 403 403 HIS HIS A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 MET 405 405 405 MET MET A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 SER 407 407 407 SER SER A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 GLU 411 411 411 GLU GLU A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 LYS 413 413 413 LYS LYS A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 LEU 415 415 415 LEU LEU A . n 
A 1 416 TYR 416 416 416 TYR TYR A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 SER 418 418 418 SER SER A . n 
A 1 419 TRP 419 419 419 TRP TRP A . n 
A 1 420 VAL 420 420 420 VAL VAL A . n 
A 1 421 VAL 421 421 421 VAL VAL A . n 
A 1 422 GLU 422 422 422 GLU GLU A . n 
A 1 423 ALA 423 423 423 ALA ALA A . n 
A 1 424 ARG 424 424 424 ARG ARG A . n 
A 1 425 ARG 425 425 425 ARG ARG A . n 
A 1 426 HIS 426 426 426 HIS HIS A . n 
A 1 427 ILE 427 427 427 ILE ILE A . n 
A 1 428 LEU 428 428 428 LEU LEU A . n 
A 1 429 ALA 429 429 429 ALA ALA A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 GLN 432 432 432 GLN GLN A . n 
A 1 433 ASP 433 433 433 ASP ASP A . n 
A 1 434 TYR 434 434 434 TYR TYR A . n 
A 1 435 PRO 435 435 435 PRO PRO A . n 
A 1 436 SER 436 436 436 SER SER A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 ARG 438 438 438 ARG ARG A . n 
A 1 439 PRO 439 439 439 PRO PRO A . n 
A 1 440 PRO 440 440 440 PRO PRO A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 ASP 442 442 442 ASP ASP A . n 
A 1 443 HIS 443 443 443 HIS HIS A . n 
A 1 444 LEU 444 444 444 LEU LEU A . n 
A 1 445 CYS 445 445 445 CYS CYS A . n 
A 1 446 GLU 446 446 446 GLU GLU A . n 
A 1 447 LEU 447 447 447 LEU LEU A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 ARG 450 450 450 ARG ARG A . n 
A 1 451 LEU 451 451 451 LEU LEU A . n 
A 1 452 GLN 452 452 452 GLN GLN A . n 
A 1 453 ALA 453 453 453 ALA ALA A . n 
A 1 454 ARG 454 454 454 ARG ARG A . n 
A 1 455 TYR 455 455 455 TYR TYR A . n 
A 1 456 TYR 456 456 456 TYR TYR A . n 
A 1 457 SER 457 457 457 SER SER A . n 
A 1 458 ILE 458 458 458 ILE ILE A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 SER 461 461 461 SER SER A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 LYS 463 463 463 LYS LYS A . n 
A 1 464 VAL 464 464 464 VAL VAL A . n 
A 1 465 HIS 465 465 465 HIS HIS A . n 
A 1 466 PRO 466 466 466 PRO PRO A . n 
A 1 467 ASN 467 467 467 ASN ASN A . n 
A 1 468 SER 468 468 468 SER SER A . n 
A 1 469 VAL 469 469 469 VAL VAL A . n 
A 1 470 HIS 470 470 470 HIS HIS A . n 
A 1 471 ILE 471 471 471 ILE ILE A . n 
A 1 472 CYS 472 472 472 CYS CYS A . n 
A 1 473 ALA 473 473 473 ALA ALA A . n 
A 1 474 VAL 474 474 474 VAL VAL A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 VAL 476 476 476 VAL VAL A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
A 1 478 TYR 478 478 478 TYR TYR A . n 
A 1 479 GLU 479 479 479 GLU GLU A . n 
A 1 480 ALA 480 480 480 ALA ALA A . n 
A 1 481 LYS 481 481 481 LYS LYS A . n 
A 1 482 SER 482 482 482 SER SER A . n 
A 1 483 GLY 483 483 483 GLY GLY A . n 
A 1 484 ARG 484 484 484 ARG ARG A . n 
A 1 485 VAL 485 485 485 VAL VAL A . n 
A 1 486 ASN 486 486 486 ASN ASN A . n 
A 1 487 LYS 487 487 487 LYS LYS A . n 
A 1 488 GLY 488 488 488 GLY GLY A . n 
A 1 489 VAL 489 489 489 VAL VAL A . n 
A 1 490 ALA 490 490 490 ALA ALA A . n 
A 1 491 THR 491 491 491 THR THR A . n 
A 1 492 SER 492 492 492 SER SER A . n 
A 1 493 TRP 493 493 493 TRP TRP A . n 
A 1 494 LEU 494 494 494 LEU LEU A . n 
A 1 495 ARG 495 495 495 ARG ARG A . n 
A 1 496 ALA 496 496 496 ALA ALA A . n 
A 1 497 LYS 497 497 497 LYS LYS A . n 
A 1 498 GLU 498 498 498 GLU GLU A . n 
A 1 499 PRO 499 499 499 PRO PRO A . n 
A 1 500 ALA 500 500 500 ALA ALA A . n 
A 1 501 GLY 501 501 501 GLY GLY A . n 
A 1 502 GLU 502 502 502 GLU GLU A . n 
A 1 503 ASN 503 503 503 ASN ASN A . n 
A 1 504 GLY 504 504 504 GLY ALA A . n 
A 1 505 GLY 505 505 505 GLY ALA A . n 
A 1 506 ARG 506 506 506 ARG ARG A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 LEU 508 508 508 LEU LEU A . n 
A 1 509 VAL 509 509 509 VAL VAL A . n 
A 1 510 PRO 510 510 510 PRO PRO A . n 
A 1 511 MET 511 511 511 MET MET A . n 
A 1 512 PHE 512 512 512 PHE PHE A . n 
A 1 513 VAL 513 513 513 VAL VAL A . n 
A 1 514 ARG 514 514 514 ARG ARG A . n 
A 1 515 LYS 515 515 515 LYS LYS A . n 
A 1 516 SER 516 516 516 SER SER A . n 
A 1 517 GLN 517 517 517 GLN GLN A . n 
A 1 518 PHE 518 518 518 PHE PHE A . n 
A 1 519 ARG 519 519 519 ARG ARG A . n 
A 1 520 LEU 520 520 520 LEU LEU A . n 
A 1 521 PRO 521 521 521 PRO PRO A . n 
A 1 522 PHE 522 522 522 PHE PHE A . n 
A 1 523 LYS 523 523 523 LYS LYS A . n 
A 1 524 SER 524 524 524 SER SER A . n 
A 1 525 THR 525 525 525 THR THR A . n 
A 1 526 THR 526 526 526 THR THR A . n 
A 1 527 PRO 527 527 527 PRO PRO A . n 
A 1 528 VAL 528 528 528 VAL VAL A . n 
A 1 529 ILE 529 529 529 ILE ILE A . n 
A 1 530 MET 530 530 530 MET MET A . n 
A 1 531 VAL 531 531 531 VAL VAL A . n 
A 1 532 GLY 532 532 532 GLY GLY A . n 
A 1 533 PRO 533 533 533 PRO PRO A . n 
A 1 534 GLY 534 534 534 GLY GLY A . n 
A 1 535 THR 535 535 535 THR THR A . n 
A 1 536 GLY 536 536 536 GLY GLY A . n 
A 1 537 ILE 537 537 537 ILE ILE A . n 
A 1 538 ALA 538 538 538 ALA ALA A . n 
A 1 539 PRO 539 539 539 PRO PRO A . n 
A 1 540 PHE 540 540 540 PHE PHE A . n 
A 1 541 MET 541 541 541 MET MET A . n 
A 1 542 GLY 542 542 542 GLY GLY A . n 
A 1 543 PHE 543 543 543 PHE PHE A . n 
A 1 544 ILE 544 544 544 ILE ILE A . n 
A 1 545 GLN 545 545 545 GLN GLN A . n 
A 1 546 GLU 546 546 546 GLU GLU A . n 
A 1 547 ARG 547 547 547 ARG ARG A . n 
A 1 548 ALA 548 548 548 ALA ALA A . n 
A 1 549 TRP 549 549 549 TRP TRP A . n 
A 1 550 LEU 550 550 550 LEU LEU A . n 
A 1 551 ARG 551 551 551 ARG ARG A . n 
A 1 552 GLU 552 552 552 GLU GLU A . n 
A 1 553 GLN 553 553 553 GLN GLN A . n 
A 1 554 GLY 554 554 554 GLY GLY A . n 
A 1 555 LYS 555 555 555 LYS LYS A . n 
A 1 556 GLU 556 556 556 GLU GLU A . n 
A 1 557 VAL 557 557 557 VAL VAL A . n 
A 1 558 GLY 558 558 558 GLY GLY A . n 
A 1 559 GLU 559 559 559 GLU GLU A . n 
A 1 560 THR 560 560 560 THR THR A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 LEU 562 562 562 LEU LEU A . n 
A 1 563 TYR 563 563 563 TYR TYR A . n 
A 1 564 TYR 564 564 564 TYR TYR A . n 
A 1 565 GLY 565 565 565 GLY GLY A . n 
A 1 566 CYS 566 566 566 CYS CYS A . n 
A 1 567 ARG 567 567 567 ARG ARG A . n 
A 1 568 ARG 568 568 568 ARG ARG A . n 
A 1 569 SER 569 569 569 SER SER A . n 
A 1 570 ASP 570 570 570 ASP ASP A . n 
A 1 571 GLU 571 571 571 GLU GLU A . n 
A 1 572 ASP 572 572 572 ASP ASP A . n 
A 1 573 TYR 573 573 573 TYR TYR A . n 
A 1 574 LEU 574 574 574 LEU LEU A . n 
A 1 575 TYR 575 575 575 TYR TYR A . n 
A 1 576 ARG 576 576 576 ARG ARG A . n 
A 1 577 GLU 577 577 577 GLU GLU A . n 
A 1 578 GLU 578 578 578 GLU GLU A . n 
A 1 579 LEU 579 579 579 LEU LEU A . n 
A 1 580 ALA 580 580 580 ALA ALA A . n 
A 1 581 ARG 581 581 581 ARG ARG A . n 
A 1 582 PHE 582 582 582 PHE PHE A . n 
A 1 583 HIS 583 583 583 HIS HIS A . n 
A 1 584 LYS 584 584 584 LYS LYS A . n 
A 1 585 ASP 585 585 585 ASP ASP A . n 
A 1 586 GLY 586 586 586 GLY GLY A . n 
A 1 587 ALA 587 587 587 ALA ALA A . n 
A 1 588 LEU 588 588 588 LEU LEU A . n 
A 1 589 THR 589 589 589 THR THR A . n 
A 1 590 GLN 590 590 590 GLN GLN A . n 
A 1 591 LEU 591 591 591 LEU LEU A . n 
A 1 592 ASN 592 592 592 ASN ASN A . n 
A 1 593 VAL 593 593 593 VAL VAL A . n 
A 1 594 ALA 594 594 594 ALA ALA A . n 
A 1 595 PHE 595 595 595 PHE PHE A . n 
A 1 596 SER 596 596 596 SER SER A . n 
A 1 597 ARG 597 597 597 ARG ARG A . n 
A 1 598 GLU 598 598 598 GLU GLU A . n 
A 1 599 GLN 599 599 599 GLN GLN A . n 
A 1 600 ALA 600 600 600 ALA ALA A . n 
A 1 601 HIS 601 601 601 HIS HIS A . n 
A 1 602 LYS 602 602 602 LYS LYS A . n 
A 1 603 VAL 603 603 603 VAL VAL A . n 
A 1 604 TYR 604 604 604 TYR TYR A . n 
A 1 605 VAL 605 605 605 VAL VAL A . n 
A 1 606 GLN 606 606 606 GLN GLN A . n 
A 1 607 HIS 607 607 607 HIS HIS A . n 
A 1 608 LEU 608 608 608 LEU LEU A . n 
A 1 609 LEU 609 609 609 LEU LEU A . n 
A 1 610 LYS 610 610 610 LYS LYS A . n 
A 1 611 ARG 611 611 611 ARG ARG A . n 
A 1 612 ASP 612 612 612 ASP ASP A . n 
A 1 613 ARG 613 613 613 ARG ARG A . n 
A 1 614 GLU 614 614 614 GLU GLU A . n 
A 1 615 HIS 615 615 615 HIS HIS A . n 
A 1 616 LEU 616 616 616 LEU LEU A . n 
A 1 617 TRP 617 617 617 TRP TRP A . n 
A 1 618 LYS 618 618 618 LYS LYS A . n 
A 1 619 LEU 619 619 619 LEU LEU A . n 
A 1 620 ILE 620 620 620 ILE ILE A . n 
A 1 621 HIS 621 621 621 HIS HIS A . n 
A 1 622 GLU 622 622 622 GLU GLU A . n 
A 1 623 GLY 623 623 623 GLY GLY A . n 
A 1 624 GLY 624 624 624 GLY GLY A . n 
A 1 625 ALA 625 625 625 ALA ALA A . n 
A 1 626 HIS 626 626 626 HIS HIS A . n 
A 1 627 ILE 627 627 627 ILE ILE A . n 
A 1 628 TYR 628 628 628 TYR TYR A . n 
A 1 629 VAL 629 629 629 VAL VAL A . n 
A 1 630 CYS 630 630 630 CYS CYS A . n 
A 1 631 GLY 631 631 631 GLY GLY A . n 
A 1 632 ASP 632 632 632 ASP ASP A . n 
A 1 633 ALA 633 633 633 ALA ALA A . n 
A 1 634 ARG 634 634 634 ARG ARG A . n 
A 1 635 ASN 635 635 635 ASN ASN A . n 
A 1 636 MET 636 636 636 MET MET A . n 
A 1 637 ALA 637 637 637 ALA ALA A . n 
A 1 638 LYS 638 638 638 LYS LYS A . n 
A 1 639 ASP 639 639 639 ASP ASP A . n 
A 1 640 VAL 640 640 640 VAL VAL A . n 
A 1 641 GLN 641 641 641 GLN GLN A . n 
A 1 642 ASN 642 642 642 ASN ASN A . n 
A 1 643 THR 643 643 643 THR THR A . n 
A 1 644 PHE 644 644 644 PHE PHE A . n 
A 1 645 TYR 645 645 645 TYR TYR A . n 
A 1 646 ASP 646 646 646 ASP ASP A . n 
A 1 647 ILE 647 647 647 ILE ILE A . n 
A 1 648 VAL 648 648 648 VAL VAL A . n 
A 1 649 ALA 649 649 649 ALA ALA A . n 
A 1 650 GLU 650 650 650 GLU GLU A . n 
A 1 651 PHE 651 651 651 PHE PHE A . n 
A 1 652 GLY 652 652 652 GLY GLY A . n 
A 1 653 PRO 653 653 653 PRO PRO A . n 
A 1 654 MET 654 654 654 MET MET A . n 
A 1 655 GLU 655 655 655 GLU GLU A . n 
A 1 656 HIS 656 656 656 HIS HIS A . n 
A 1 657 THR 657 657 657 THR THR A . n 
A 1 658 GLN 658 658 658 GLN GLN A . n 
A 1 659 ALA 659 659 659 ALA ALA A . n 
A 1 660 VAL 660 660 660 VAL VAL A . n 
A 1 661 ASP 661 661 661 ASP ASP A . n 
A 1 662 TYR 662 662 662 TYR TYR A . n 
A 1 663 VAL 663 663 663 VAL VAL A . n 
A 1 664 LYS 664 664 664 LYS LYS A . n 
A 1 665 LYS 665 665 665 LYS LYS A . n 
A 1 666 LEU 666 666 666 LEU LEU A . n 
A 1 667 MET 667 667 667 MET MET A . n 
A 1 668 THR 668 668 668 THR THR A . n 
A 1 669 LYS 669 669 669 LYS LYS A . n 
A 1 670 GLY 670 670 670 GLY GLY A . n 
A 1 671 ARG 671 671 671 ARG ARG A . n 
A 1 672 TYR 672 672 672 TYR TYR A . n 
A 1 673 SER 673 673 673 SER SER A . n 
A 1 674 LEU 674 674 674 LEU LEU A . n 
A 1 675 ASP 675 675 675 ASP ASP A . n 
A 1 676 VAL 676 676 676 VAL VAL A . n 
A 1 677 TRP 677 677 677 TRP TRP A . n 
A 1 678 SER 678 678 678 SER SER A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FMN 1 701 751 FMN FMN A . 
C 3 FAD 1 702 752 FAD FAD A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EF0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9EF0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EF0 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9EF0 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.002 ? 5171 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.522 ? 7026 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 9.243 ? 802  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.040 ? 738  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 901  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9EF0 
_struct.title                        'EM structure of cytochrome P450 reductase' 
_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        9EF0 
_struct_keywords.text            
'cytochrome P450 reductase, CPR, POR, electron transfer, endoplasmic reticulum, flavoprotein, oxidoreductase' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NCPR_RAT 
_struct_ref.pdbx_db_accession          P00388 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGDSHEDTSATMPEAVAEEVSLFSTTDMVLFSLIVGVLTYWFIFRKKKEEIPEFSKIQTTAPPVKESSFVEKMKKTGRNI
IVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETD
VDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEES
SIRQYELVVHEDMDVAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESGDHV
AVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQE
HLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEA
KSGRVNKGVATSWLRAKEPAGENGGRALVPMFVRKSQFRLPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGET
LLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEGGAHIYVCGDARNMAKDV
QNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EF0 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 678 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00388 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  678 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       678 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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 PHE A 69  ? GLY A 77  ? PHE A 69  GLY A 77  1 ? 9  
HELX_P HELX_P2  AA2 GLY A 89  ? ALA A 102 ? GLY A 89  ALA A 102 1 ? 14 
HELX_P HELX_P3  AA3 HIS A 103 ? GLY A 106 ? HIS A 103 GLY A 106 5 ? 4  
HELX_P HELX_P4  AA4 ASP A 118 ? SER A 123 ? ASP A 118 SER A 123 5 ? 6  
HELX_P HELX_P5  AA5 SER A 124 ? ILE A 128 ? SER A 124 ILE A 128 5 ? 5  
HELX_P HELX_P6  AA6 ALA A 149 ? THR A 159 ? ALA A 149 THR A 159 1 ? 11 
HELX_P HELX_P7  AA7 ASN A 182 ? GLY A 196 ? ASN A 182 GLY A 196 1 ? 15 
HELX_P HELX_P8  AA8 ASN A 211 ? GLY A 232 ? ASN A 211 GLY A 232 1 ? 22 
HELX_P HELX_P9  AA9 ASP A 254 ? VAL A 258 ? ASP A 254 VAL A 258 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 327 ? GLY A 339 ? ASP A 327 GLY A 339 1 ? 13 
HELX_P HELX_P11 AB2 THR A 366 ? TYR A 374 ? THR A 366 TYR A 374 1 ? 9  
HELX_P HELX_P12 AB3 ARG A 382 ? GLN A 391 ? ARG A 382 GLN A 391 1 ? 10 
HELX_P HELX_P13 AB4 GLU A 395 ? MET A 405 ? GLU A 395 MET A 405 1 ? 11 
HELX_P HELX_P14 AB5 GLY A 410 ? VAL A 420 ? GLY A 410 VAL A 420 1 ? 11 
HELX_P HELX_P15 AB6 HIS A 426 ? TYR A 434 ? HIS A 426 TYR A 434 1 ? 9  
HELX_P HELX_P16 AB7 PRO A 440 ? LEU A 448 ? PRO A 440 LEU A 448 1 ? 9  
HELX_P HELX_P17 AB8 VAL A 489 ? ALA A 496 ? VAL A 489 ALA A 496 1 ? 8  
HELX_P HELX_P18 AB9 PRO A 533 ? THR A 535 ? PRO A 533 THR A 535 5 ? 3  
HELX_P HELX_P19 AC1 GLY A 536 ? GLN A 553 ? GLY A 536 GLN A 553 1 ? 18 
HELX_P HELX_P20 AC2 TYR A 575 ? ASP A 585 ? TYR A 575 ASP A 585 1 ? 11 
HELX_P HELX_P21 AC3 TYR A 604 ? ASP A 612 ? TYR A 604 ASP A 612 1 ? 9  
HELX_P HELX_P22 AC4 ASP A 612 ? GLY A 624 ? ASP A 612 GLY A 624 1 ? 13 
HELX_P HELX_P23 AC5 ASN A 635 ? PHE A 651 ? ASN A 635 PHE A 651 1 ? 17 
HELX_P HELX_P24 AC6 GLU A 655 ? LYS A 669 ? GLU A 655 LYS A 669 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 274 A . ? PRO 274 A PRO 275 A ? PRO 275 A 1 -0.62 
2 CYS 363 A . ? CYS 363 A PRO 364 A ? PRO 364 A 1 5.52  
3 GLY 652 A . ? GLY 652 A PRO 653 A ? PRO 653 A 1 -7.58 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? 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 GLY A 109 ? ALA A 112 ? GLY A 109 ALA A 112 
AA1 2 ILE A 80  ? TYR A 84  ? ILE A 80  TYR A 84  
AA1 3 LEU A 132 ? MET A 137 ? LEU A 132 MET A 137 
AA1 4 LYS A 167 ? GLY A 174 ? LYS A 167 GLY A 174 
AA1 5 GLN A 198 ? ARG A 199 ? GLN A 198 ARG A 199 
AA2 1 GLY A 109 ? ALA A 112 ? GLY A 109 ALA A 112 
AA2 2 ILE A 80  ? TYR A 84  ? ILE A 80  TYR A 84  
AA2 3 LEU A 132 ? MET A 137 ? LEU A 132 MET A 137 
AA2 4 LYS A 167 ? GLY A 174 ? LYS A 167 GLY A 174 
AA2 5 GLY A 204 ? ASP A 207 ? GLY A 204 ASP A 207 
AA3 1 TYR A 245 ? LEU A 247 ? TYR A 245 LEU A 247 
AA3 2 LEU A 348 ? ASN A 350 ? LEU A 348 ASN A 350 
AA4 1 ARG A 454 ? SER A 457 ? ARG A 454 SER A 457 
AA4 2 HIS A 319 ? VAL A 322 ? HIS A 319 VAL A 322 
AA4 3 LEU A 508 ? ARG A 514 ? LEU A 508 ARG A 514 
AA4 4 PHE A 282 ? LYS A 291 ? PHE A 282 LYS A 291 
AA4 5 LEU A 300 ? ASP A 306 ? LEU A 300 ASP A 306 
AA4 6 SER A 468 ? VAL A 474 ? SER A 468 VAL A 474 
AA5 1 GLU A 477 ? GLU A 479 ? GLU A 477 GLU A 479 
AA5 2 VAL A 485 ? LYS A 487 ? VAL A 485 LYS A 487 
AA6 1 GLN A 590 ? PHE A 595 ? GLN A 590 PHE A 595 
AA6 2 THR A 560 ? CYS A 566 ? THR A 560 CYS A 566 
AA6 3 VAL A 528 ? VAL A 531 ? VAL A 528 VAL A 531 
AA6 4 HIS A 626 ? VAL A 629 ? HIS A 626 VAL A 629 
AA6 5 TYR A 672 ? LEU A 674 ? TYR A 672 LEU A 674 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O MET A 110 ? O MET A 110 N ILE A 80  ? N ILE A 80  
AA1 2 3 N PHE A 83  ? N PHE A 83  O VAL A 134 ? O VAL A 134 
AA1 3 4 N PHE A 135 ? N PHE A 135 O PHE A 171 ? O PHE A 171 
AA1 4 5 N PHE A 168 ? N PHE A 168 O GLN A 198 ? O GLN A 198 
AA2 1 2 O MET A 110 ? O MET A 110 N ILE A 80  ? N ILE A 80  
AA2 2 3 N PHE A 83  ? N PHE A 83  O VAL A 134 ? O VAL A 134 
AA2 3 4 N PHE A 135 ? N PHE A 135 O PHE A 171 ? O PHE A 171 
AA2 4 5 N GLY A 172 ? N GLY A 172 O GLY A 204 ? O GLY A 204 
AA3 1 2 N GLU A 246 ? N GLU A 246 O ASN A 349 ? O ASN A 349 
AA4 1 2 O TYR A 456 ? O TYR A 456 N VAL A 320 ? N VAL A 320 
AA4 2 3 N ALA A 321 ? N ALA A 321 O PHE A 512 ? O PHE A 512 
AA4 3 4 O VAL A 509 ? O VAL A 509 N ALA A 284 ? N ALA A 284 
AA4 4 5 N ALA A 285 ? N ALA A 285 O ASP A 306 ? O ASP A 306 
AA4 5 6 N LEU A 303 ? N LEU A 303 O ILE A 471 ? O ILE A 471 
AA5 1 2 N TYR A 478 ? N TYR A 478 O ASN A 486 ? O ASN A 486 
AA6 1 2 O ALA A 594 ? O ALA A 594 N TYR A 564 ? N TYR A 564 
AA6 2 3 O TYR A 563 ? O TYR A 563 N MET A 530 ? N MET A 530 
AA6 3 4 N ILE A 529 ? N ILE A 529 O HIS A 626 ? O HIS A 626 
AA6 4 5 N ILE A 627 ? N ILE A 627 O SER A 673 ? O SER A 673 
# 
_pdbx_entry_details.entry_id                   9EF0 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 142 ? ? -95.88  58.74   
2 1 ASP A 309 ? ? 59.55   15.51   
3 1 ASP A 318 ? ? -78.53  -169.21 
4 1 HIS A 465 ? ? -38.68  109.75  
5 1 ALA A 500 ? ? 56.58   -106.42 
6 1 GLU A 502 ? ? 60.50   -123.43 
7 1 ASP A 572 ? ? -141.59 24.26   
8 1 ASN A 635 ? ? -130.90 -30.28  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9EF0 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      'AB INITIO MODEL' 
# 
_em_3d_reconstruction.entry_id                    9EF0 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.33 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               671545 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       PBS 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Cytochrome P450 reductase' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9EF0 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               OTHER 
_em_imaging.mode                            OTHER 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             2400 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           130000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     90 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   90 
_em_imaging.recording_temperature_maximum   90 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            50 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   ? 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9EF0 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9EF0 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1  ? A MET 1  
2  1 Y 1 A GLY 2  ? A GLY 2  
3  1 Y 1 A ASP 3  ? A ASP 3  
4  1 Y 1 A SER 4  ? A SER 4  
5  1 Y 1 A HIS 5  ? A HIS 5  
6  1 Y 1 A GLU 6  ? A GLU 6  
7  1 Y 1 A ASP 7  ? A ASP 7  
8  1 Y 1 A THR 8  ? A THR 8  
9  1 Y 1 A SER 9  ? A SER 9  
10 1 Y 1 A ALA 10 ? A ALA 10 
11 1 Y 1 A THR 11 ? A THR 11 
12 1 Y 1 A MET 12 ? A MET 12 
13 1 Y 1 A PRO 13 ? A PRO 13 
14 1 Y 1 A GLU 14 ? A GLU 14 
15 1 Y 1 A ALA 15 ? A ALA 15 
16 1 Y 1 A VAL 16 ? A VAL 16 
17 1 Y 1 A ALA 17 ? A ALA 17 
18 1 Y 1 A GLU 18 ? A GLU 18 
19 1 Y 1 A GLU 19 ? A GLU 19 
20 1 Y 1 A VAL 20 ? A VAL 20 
21 1 Y 1 A SER 21 ? A SER 21 
22 1 Y 1 A LEU 22 ? A LEU 22 
23 1 Y 1 A PHE 23 ? A PHE 23 
24 1 Y 1 A SER 24 ? A SER 24 
25 1 Y 1 A THR 25 ? A THR 25 
26 1 Y 1 A THR 26 ? A THR 26 
27 1 Y 1 A ASP 27 ? A ASP 27 
28 1 Y 1 A MET 28 ? A MET 28 
29 1 Y 1 A VAL 29 ? A VAL 29 
30 1 Y 1 A LEU 30 ? A LEU 30 
31 1 Y 1 A PHE 31 ? A PHE 31 
32 1 Y 1 A SER 32 ? A SER 32 
33 1 Y 1 A LEU 33 ? A LEU 33 
34 1 Y 1 A ILE 34 ? A ILE 34 
35 1 Y 1 A VAL 35 ? A VAL 35 
36 1 Y 1 A GLY 36 ? A GLY 36 
37 1 Y 1 A VAL 37 ? A VAL 37 
38 1 Y 1 A LEU 38 ? A LEU 38 
39 1 Y 1 A THR 39 ? A THR 39 
40 1 Y 1 A TYR 40 ? A TYR 40 
41 1 Y 1 A TRP 41 ? A TRP 41 
42 1 Y 1 A PHE 42 ? A PHE 42 
43 1 Y 1 A ILE 43 ? A ILE 43 
44 1 Y 1 A PHE 44 ? A PHE 44 
45 1 Y 1 A ARG 45 ? A ARG 45 
46 1 Y 1 A LYS 46 ? A LYS 46 
47 1 Y 1 A LYS 47 ? A LYS 47 
48 1 Y 1 A LYS 48 ? A LYS 48 
49 1 Y 1 A GLU 49 ? A GLU 49 
50 1 Y 1 A GLU 50 ? A GLU 50 
51 1 Y 1 A ILE 51 ? A ILE 51 
52 1 Y 1 A PRO 52 ? A PRO 52 
53 1 Y 1 A GLU 53 ? A GLU 53 
54 1 Y 1 A PHE 54 ? A PHE 54 
55 1 Y 1 A SER 55 ? A SER 55 
56 1 Y 1 A LYS 56 ? A LYS 56 
57 1 Y 1 A ILE 57 ? A ILE 57 
58 1 Y 1 A GLN 58 ? A GLN 58 
59 1 Y 1 A THR 59 ? A THR 59 
60 1 Y 1 A THR 60 ? A THR 60 
61 1 Y 1 A ALA 61 ? A ALA 61 
62 1 Y 1 A PRO 62 ? A PRO 62 
63 1 Y 1 A PRO 63 ? A PRO 63 
64 1 Y 1 A VAL 64 ? A VAL 64 
65 1 Y 1 A LYS 65 ? A LYS 65 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
FMN N1     N N N 174 
FMN C2     C N N 175 
FMN O2     O N N 176 
FMN N3     N N N 177 
FMN C4     C N N 178 
FMN O4     O N N 179 
FMN C4A    C N N 180 
FMN N5     N N N 181 
FMN C5A    C Y N 182 
FMN C6     C Y N 183 
FMN C7     C Y N 184 
FMN C7M    C N N 185 
FMN C8     C Y N 186 
FMN C8M    C N N 187 
FMN C9     C Y N 188 
FMN C9A    C Y N 189 
FMN N10    N N N 190 
FMN C10    C N N 191 
FMN "C1'"  C N N 192 
FMN "C2'"  C N S 193 
FMN "O2'"  O N N 194 
FMN "C3'"  C N S 195 
FMN "O3'"  O N N 196 
FMN "C4'"  C N R 197 
FMN "O4'"  O N N 198 
FMN "C5'"  C N N 199 
FMN "O5'"  O N N 200 
FMN P      P N N 201 
FMN O1P    O N N 202 
FMN O2P    O N N 203 
FMN O3P    O N N 204 
FMN HN3    H N N 205 
FMN H6     H N N 206 
FMN HM71   H N N 207 
FMN HM72   H N N 208 
FMN HM73   H N N 209 
FMN HM81   H N N 210 
FMN HM82   H N N 211 
FMN HM83   H N N 212 
FMN H9     H N N 213 
FMN "H1'1" H N N 214 
FMN "H1'2" H N N 215 
FMN "H2'"  H N N 216 
FMN "HO2'" H N N 217 
FMN "H3'"  H N N 218 
FMN "HO3'" H N N 219 
FMN "H4'"  H N N 220 
FMN "HO4'" H N N 221 
FMN "H5'1" H N N 222 
FMN "H5'2" H N N 223 
FMN HOP2   H N N 224 
FMN HOP3   H N N 225 
GLN N      N N N 226 
GLN CA     C N S 227 
GLN C      C N N 228 
GLN O      O N N 229 
GLN CB     C N N 230 
GLN CG     C N N 231 
GLN CD     C N N 232 
GLN OE1    O N N 233 
GLN NE2    N N N 234 
GLN OXT    O N N 235 
GLN H      H N N 236 
GLN H2     H N N 237 
GLN HA     H N N 238 
GLN HB2    H N N 239 
GLN HB3    H N N 240 
GLN HG2    H N N 241 
GLN HG3    H N N 242 
GLN HE21   H N N 243 
GLN HE22   H N N 244 
GLN HXT    H N N 245 
GLU N      N N N 246 
GLU CA     C N S 247 
GLU C      C N N 248 
GLU O      O N N 249 
GLU CB     C N N 250 
GLU CG     C N N 251 
GLU CD     C N N 252 
GLU OE1    O N N 253 
GLU OE2    O N N 254 
GLU OXT    O N N 255 
GLU H      H N N 256 
GLU H2     H N N 257 
GLU HA     H N N 258 
GLU HB2    H N N 259 
GLU HB3    H N N 260 
GLU HG2    H N N 261 
GLU HG3    H N N 262 
GLU HE2    H N N 263 
GLU HXT    H N N 264 
GLY N      N N N 265 
GLY CA     C N N 266 
GLY C      C N N 267 
GLY O      O N N 268 
GLY OXT    O N N 269 
GLY H      H N N 270 
GLY H2     H N N 271 
GLY HA2    H N N 272 
GLY HA3    H N N 273 
GLY HXT    H N N 274 
HIS N      N N N 275 
HIS CA     C N S 276 
HIS C      C N N 277 
HIS O      O N N 278 
HIS CB     C N N 279 
HIS CG     C Y N 280 
HIS ND1    N Y N 281 
HIS CD2    C Y N 282 
HIS CE1    C Y N 283 
HIS NE2    N Y N 284 
HIS OXT    O N N 285 
HIS H      H N N 286 
HIS H2     H N N 287 
HIS HA     H N N 288 
HIS HB2    H N N 289 
HIS HB3    H N N 290 
HIS HD1    H N N 291 
HIS HD2    H N N 292 
HIS HE1    H N N 293 
HIS HE2    H N N 294 
HIS HXT    H N N 295 
ILE N      N N N 296 
ILE CA     C N S 297 
ILE C      C N N 298 
ILE O      O N N 299 
ILE CB     C N S 300 
ILE CG1    C N N 301 
ILE CG2    C N N 302 
ILE CD1    C N N 303 
ILE OXT    O N N 304 
ILE H      H N N 305 
ILE H2     H N N 306 
ILE HA     H N N 307 
ILE HB     H N N 308 
ILE HG12   H N N 309 
ILE HG13   H N N 310 
ILE HG21   H N N 311 
ILE HG22   H N N 312 
ILE HG23   H N N 313 
ILE HD11   H N N 314 
ILE HD12   H N N 315 
ILE HD13   H N N 316 
ILE HXT    H N N 317 
LEU N      N N N 318 
LEU CA     C N S 319 
LEU C      C N N 320 
LEU O      O N N 321 
LEU CB     C N N 322 
LEU CG     C N N 323 
LEU CD1    C N N 324 
LEU CD2    C N N 325 
LEU OXT    O N N 326 
LEU H      H N N 327 
LEU H2     H N N 328 
LEU HA     H N N 329 
LEU HB2    H N N 330 
LEU HB3    H N N 331 
LEU HG     H N N 332 
LEU HD11   H N N 333 
LEU HD12   H N N 334 
LEU HD13   H N N 335 
LEU HD21   H N N 336 
LEU HD22   H N N 337 
LEU HD23   H N N 338 
LEU HXT    H N N 339 
LYS N      N N N 340 
LYS CA     C N S 341 
LYS C      C N N 342 
LYS O      O N N 343 
LYS CB     C N N 344 
LYS CG     C N N 345 
LYS CD     C N N 346 
LYS CE     C N N 347 
LYS NZ     N N N 348 
LYS OXT    O N N 349 
LYS H      H N N 350 
LYS H2     H N N 351 
LYS HA     H N N 352 
LYS HB2    H N N 353 
LYS HB3    H N N 354 
LYS HG2    H N N 355 
LYS HG3    H N N 356 
LYS HD2    H N N 357 
LYS HD3    H N N 358 
LYS HE2    H N N 359 
LYS HE3    H N N 360 
LYS HZ1    H N N 361 
LYS HZ2    H N N 362 
LYS HZ3    H N N 363 
LYS HXT    H N N 364 
MET N      N N N 365 
MET CA     C N S 366 
MET C      C N N 367 
MET O      O N N 368 
MET CB     C N N 369 
MET CG     C N N 370 
MET SD     S N N 371 
MET CE     C N N 372 
MET OXT    O N N 373 
MET H      H N N 374 
MET H2     H N N 375 
MET HA     H N N 376 
MET HB2    H N N 377 
MET HB3    H N N 378 
MET HG2    H N N 379 
MET HG3    H N N 380 
MET HE1    H N N 381 
MET HE2    H N N 382 
MET HE3    H N N 383 
MET HXT    H N N 384 
PHE N      N N N 385 
PHE CA     C N S 386 
PHE C      C N N 387 
PHE O      O N N 388 
PHE CB     C N N 389 
PHE CG     C Y N 390 
PHE CD1    C Y N 391 
PHE CD2    C Y N 392 
PHE CE1    C Y N 393 
PHE CE2    C Y N 394 
PHE CZ     C Y N 395 
PHE OXT    O N N 396 
PHE H      H N N 397 
PHE H2     H N N 398 
PHE HA     H N N 399 
PHE HB2    H N N 400 
PHE HB3    H N N 401 
PHE HD1    H N N 402 
PHE HD2    H N N 403 
PHE HE1    H N N 404 
PHE HE2    H N N 405 
PHE HZ     H N N 406 
PHE HXT    H N N 407 
PRO N      N N N 408 
PRO CA     C N S 409 
PRO C      C N N 410 
PRO O      O N N 411 
PRO CB     C N N 412 
PRO CG     C N N 413 
PRO CD     C N N 414 
PRO OXT    O N N 415 
PRO H      H N N 416 
PRO HA     H N N 417 
PRO HB2    H N N 418 
PRO HB3    H N N 419 
PRO HG2    H N N 420 
PRO HG3    H N N 421 
PRO HD2    H N N 422 
PRO HD3    H N N 423 
PRO HXT    H N N 424 
SER N      N N N 425 
SER CA     C N S 426 
SER C      C N N 427 
SER O      O N N 428 
SER CB     C N N 429 
SER OG     O N N 430 
SER OXT    O N N 431 
SER H      H N N 432 
SER H2     H N N 433 
SER HA     H N N 434 
SER HB2    H N N 435 
SER HB3    H N N 436 
SER HG     H N N 437 
SER HXT    H N N 438 
THR N      N N N 439 
THR CA     C N S 440 
THR C      C N N 441 
THR O      O N N 442 
THR CB     C N R 443 
THR OG1    O N N 444 
THR CG2    C N N 445 
THR OXT    O N N 446 
THR H      H N N 447 
THR H2     H N N 448 
THR HA     H N N 449 
THR HB     H N N 450 
THR HG1    H N N 451 
THR HG21   H N N 452 
THR HG22   H N N 453 
THR HG23   H N N 454 
THR HXT    H N N 455 
TRP N      N N N 456 
TRP CA     C N S 457 
TRP C      C N N 458 
TRP O      O N N 459 
TRP CB     C N N 460 
TRP CG     C Y N 461 
TRP CD1    C Y N 462 
TRP CD2    C Y N 463 
TRP NE1    N Y N 464 
TRP CE2    C Y N 465 
TRP CE3    C Y N 466 
TRP CZ2    C Y N 467 
TRP CZ3    C Y N 468 
TRP CH2    C Y N 469 
TRP OXT    O N N 470 
TRP H      H N N 471 
TRP H2     H N N 472 
TRP HA     H N N 473 
TRP HB2    H N N 474 
TRP HB3    H N N 475 
TRP HD1    H N N 476 
TRP HE1    H N N 477 
TRP HE3    H N N 478 
TRP HZ2    H N N 479 
TRP HZ3    H N N 480 
TRP HH2    H N N 481 
TRP HXT    H N N 482 
TYR N      N N N 483 
TYR CA     C N S 484 
TYR C      C N N 485 
TYR O      O N N 486 
TYR CB     C N N 487 
TYR CG     C Y N 488 
TYR CD1    C Y N 489 
TYR CD2    C Y N 490 
TYR CE1    C Y N 491 
TYR CE2    C Y N 492 
TYR CZ     C Y N 493 
TYR OH     O N N 494 
TYR OXT    O N N 495 
TYR H      H N N 496 
TYR H2     H N N 497 
TYR HA     H N N 498 
TYR HB2    H N N 499 
TYR HB3    H N N 500 
TYR HD1    H N N 501 
TYR HD2    H N N 502 
TYR HE1    H N N 503 
TYR HE2    H N N 504 
TYR HH     H N N 505 
TYR HXT    H N N 506 
VAL N      N N N 507 
VAL CA     C N S 508 
VAL C      C N N 509 
VAL O      O N N 510 
VAL CB     C N N 511 
VAL CG1    C N N 512 
VAL CG2    C N N 513 
VAL OXT    O N N 514 
VAL H      H N N 515 
VAL H2     H N N 516 
VAL HA     H N N 517 
VAL HB     H N N 518 
VAL HG11   H N N 519 
VAL HG12   H N N 520 
VAL HG13   H N N 521 
VAL HG21   H N N 522 
VAL HG22   H N N 523 
VAL HG23   H N N 524 
VAL HXT    H N N 525 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
FMN N1    C2     sing N N 174 
FMN N1    C10    doub N N 175 
FMN C2    O2     doub N N 176 
FMN C2    N3     sing N N 177 
FMN N3    C4     sing N N 178 
FMN N3    HN3    sing N N 179 
FMN C4    O4     doub N N 180 
FMN C4    C4A    sing N N 181 
FMN C4A   N5     doub N N 182 
FMN C4A   C10    sing N N 183 
FMN N5    C5A    sing N N 184 
FMN C5A   C6     doub Y N 185 
FMN C5A   C9A    sing Y N 186 
FMN C6    C7     sing Y N 187 
FMN C6    H6     sing N N 188 
FMN C7    C7M    sing N N 189 
FMN C7    C8     doub Y N 190 
FMN C7M   HM71   sing N N 191 
FMN C7M   HM72   sing N N 192 
FMN C7M   HM73   sing N N 193 
FMN C8    C8M    sing N N 194 
FMN C8    C9     sing Y N 195 
FMN C8M   HM81   sing N N 196 
FMN C8M   HM82   sing N N 197 
FMN C8M   HM83   sing N N 198 
FMN C9    C9A    doub Y N 199 
FMN C9    H9     sing N N 200 
FMN C9A   N10    sing N N 201 
FMN N10   C10    sing N N 202 
FMN N10   "C1'"  sing N N 203 
FMN "C1'" "C2'"  sing N N 204 
FMN "C1'" "H1'1" sing N N 205 
FMN "C1'" "H1'2" sing N N 206 
FMN "C2'" "O2'"  sing N N 207 
FMN "C2'" "C3'"  sing N N 208 
FMN "C2'" "H2'"  sing N N 209 
FMN "O2'" "HO2'" sing N N 210 
FMN "C3'" "O3'"  sing N N 211 
FMN "C3'" "C4'"  sing N N 212 
FMN "C3'" "H3'"  sing N N 213 
FMN "O3'" "HO3'" sing N N 214 
FMN "C4'" "O4'"  sing N N 215 
FMN "C4'" "C5'"  sing N N 216 
FMN "C4'" "H4'"  sing N N 217 
FMN "O4'" "HO4'" sing N N 218 
FMN "C5'" "O5'"  sing N N 219 
FMN "C5'" "H5'1" sing N N 220 
FMN "C5'" "H5'2" sing N N 221 
FMN "O5'" P      sing N N 222 
FMN P     O1P    doub N N 223 
FMN P     O2P    sing N N 224 
FMN P     O3P    sing N N 225 
FMN O2P   HOP2   sing N N 226 
FMN O3P   HOP3   sing N N 227 
GLN N     CA     sing N N 228 
GLN N     H      sing N N 229 
GLN N     H2     sing N N 230 
GLN CA    C      sing N N 231 
GLN CA    CB     sing N N 232 
GLN CA    HA     sing N N 233 
GLN C     O      doub N N 234 
GLN C     OXT    sing N N 235 
GLN CB    CG     sing N N 236 
GLN CB    HB2    sing N N 237 
GLN CB    HB3    sing N N 238 
GLN CG    CD     sing N N 239 
GLN CG    HG2    sing N N 240 
GLN CG    HG3    sing N N 241 
GLN CD    OE1    doub N N 242 
GLN CD    NE2    sing N N 243 
GLN NE2   HE21   sing N N 244 
GLN NE2   HE22   sing N N 245 
GLN OXT   HXT    sing N N 246 
GLU N     CA     sing N N 247 
GLU N     H      sing N N 248 
GLU N     H2     sing N N 249 
GLU CA    C      sing N N 250 
GLU CA    CB     sing N N 251 
GLU CA    HA     sing N N 252 
GLU C     O      doub N N 253 
GLU C     OXT    sing N N 254 
GLU CB    CG     sing N N 255 
GLU CB    HB2    sing N N 256 
GLU CB    HB3    sing N N 257 
GLU CG    CD     sing N N 258 
GLU CG    HG2    sing N N 259 
GLU CG    HG3    sing N N 260 
GLU CD    OE1    doub N N 261 
GLU CD    OE2    sing N N 262 
GLU OE2   HE2    sing N N 263 
GLU OXT   HXT    sing N N 264 
GLY N     CA     sing N N 265 
GLY N     H      sing N N 266 
GLY N     H2     sing N N 267 
GLY CA    C      sing N N 268 
GLY CA    HA2    sing N N 269 
GLY CA    HA3    sing N N 270 
GLY C     O      doub N N 271 
GLY C     OXT    sing N N 272 
GLY OXT   HXT    sing N N 273 
HIS N     CA     sing N N 274 
HIS N     H      sing N N 275 
HIS N     H2     sing N N 276 
HIS CA    C      sing N N 277 
HIS CA    CB     sing N N 278 
HIS CA    HA     sing N N 279 
HIS C     O      doub N N 280 
HIS C     OXT    sing N N 281 
HIS CB    CG     sing N N 282 
HIS CB    HB2    sing N N 283 
HIS CB    HB3    sing N N 284 
HIS CG    ND1    sing Y N 285 
HIS CG    CD2    doub Y N 286 
HIS ND1   CE1    doub Y N 287 
HIS ND1   HD1    sing N N 288 
HIS CD2   NE2    sing Y N 289 
HIS CD2   HD2    sing N N 290 
HIS CE1   NE2    sing Y N 291 
HIS CE1   HE1    sing N N 292 
HIS NE2   HE2    sing N N 293 
HIS OXT   HXT    sing N N 294 
ILE N     CA     sing N N 295 
ILE N     H      sing N N 296 
ILE N     H2     sing N N 297 
ILE CA    C      sing N N 298 
ILE CA    CB     sing N N 299 
ILE CA    HA     sing N N 300 
ILE C     O      doub N N 301 
ILE C     OXT    sing N N 302 
ILE CB    CG1    sing N N 303 
ILE CB    CG2    sing N N 304 
ILE CB    HB     sing N N 305 
ILE CG1   CD1    sing N N 306 
ILE CG1   HG12   sing N N 307 
ILE CG1   HG13   sing N N 308 
ILE CG2   HG21   sing N N 309 
ILE CG2   HG22   sing N N 310 
ILE CG2   HG23   sing N N 311 
ILE CD1   HD11   sing N N 312 
ILE CD1   HD12   sing N N 313 
ILE CD1   HD13   sing N N 314 
ILE OXT   HXT    sing N N 315 
LEU N     CA     sing N N 316 
LEU N     H      sing N N 317 
LEU N     H2     sing N N 318 
LEU CA    C      sing N N 319 
LEU CA    CB     sing N N 320 
LEU CA    HA     sing N N 321 
LEU C     O      doub N N 322 
LEU C     OXT    sing N N 323 
LEU CB    CG     sing N N 324 
LEU CB    HB2    sing N N 325 
LEU CB    HB3    sing N N 326 
LEU CG    CD1    sing N N 327 
LEU CG    CD2    sing N N 328 
LEU CG    HG     sing N N 329 
LEU CD1   HD11   sing N N 330 
LEU CD1   HD12   sing N N 331 
LEU CD1   HD13   sing N N 332 
LEU CD2   HD21   sing N N 333 
LEU CD2   HD22   sing N N 334 
LEU CD2   HD23   sing N N 335 
LEU OXT   HXT    sing N N 336 
LYS N     CA     sing N N 337 
LYS N     H      sing N N 338 
LYS N     H2     sing N N 339 
LYS CA    C      sing N N 340 
LYS CA    CB     sing N N 341 
LYS CA    HA     sing N N 342 
LYS C     O      doub N N 343 
LYS C     OXT    sing N N 344 
LYS CB    CG     sing N N 345 
LYS CB    HB2    sing N N 346 
LYS CB    HB3    sing N N 347 
LYS CG    CD     sing N N 348 
LYS CG    HG2    sing N N 349 
LYS CG    HG3    sing N N 350 
LYS CD    CE     sing N N 351 
LYS CD    HD2    sing N N 352 
LYS CD    HD3    sing N N 353 
LYS CE    NZ     sing N N 354 
LYS CE    HE2    sing N N 355 
LYS CE    HE3    sing N N 356 
LYS NZ    HZ1    sing N N 357 
LYS NZ    HZ2    sing N N 358 
LYS NZ    HZ3    sing N N 359 
LYS OXT   HXT    sing N N 360 
MET N     CA     sing N N 361 
MET N     H      sing N N 362 
MET N     H2     sing N N 363 
MET CA    C      sing N N 364 
MET CA    CB     sing N N 365 
MET CA    HA     sing N N 366 
MET C     O      doub N N 367 
MET C     OXT    sing N N 368 
MET CB    CG     sing N N 369 
MET CB    HB2    sing N N 370 
MET CB    HB3    sing N N 371 
MET CG    SD     sing N N 372 
MET CG    HG2    sing N N 373 
MET CG    HG3    sing N N 374 
MET SD    CE     sing N N 375 
MET CE    HE1    sing N N 376 
MET CE    HE2    sing N N 377 
MET CE    HE3    sing N N 378 
MET OXT   HXT    sing N N 379 
PHE N     CA     sing N N 380 
PHE N     H      sing N N 381 
PHE N     H2     sing N N 382 
PHE CA    C      sing N N 383 
PHE CA    CB     sing N N 384 
PHE CA    HA     sing N N 385 
PHE C     O      doub N N 386 
PHE C     OXT    sing N N 387 
PHE CB    CG     sing N N 388 
PHE CB    HB2    sing N N 389 
PHE CB    HB3    sing N N 390 
PHE CG    CD1    doub Y N 391 
PHE CG    CD2    sing Y N 392 
PHE CD1   CE1    sing Y N 393 
PHE CD1   HD1    sing N N 394 
PHE CD2   CE2    doub Y N 395 
PHE CD2   HD2    sing N N 396 
PHE CE1   CZ     doub Y N 397 
PHE CE1   HE1    sing N N 398 
PHE CE2   CZ     sing Y N 399 
PHE CE2   HE2    sing N N 400 
PHE CZ    HZ     sing N N 401 
PHE OXT   HXT    sing N N 402 
PRO N     CA     sing N N 403 
PRO N     CD     sing N N 404 
PRO N     H      sing N N 405 
PRO CA    C      sing N N 406 
PRO CA    CB     sing N N 407 
PRO CA    HA     sing N N 408 
PRO C     O      doub N N 409 
PRO C     OXT    sing N N 410 
PRO CB    CG     sing N N 411 
PRO CB    HB2    sing N N 412 
PRO CB    HB3    sing N N 413 
PRO CG    CD     sing N N 414 
PRO CG    HG2    sing N N 415 
PRO CG    HG3    sing N N 416 
PRO CD    HD2    sing N N 417 
PRO CD    HD3    sing N N 418 
PRO OXT   HXT    sing N N 419 
SER N     CA     sing N N 420 
SER N     H      sing N N 421 
SER N     H2     sing N N 422 
SER CA    C      sing N N 423 
SER CA    CB     sing N N 424 
SER CA    HA     sing N N 425 
SER C     O      doub N N 426 
SER C     OXT    sing N N 427 
SER CB    OG     sing N N 428 
SER CB    HB2    sing N N 429 
SER CB    HB3    sing N N 430 
SER OG    HG     sing N N 431 
SER OXT   HXT    sing N N 432 
THR N     CA     sing N N 433 
THR N     H      sing N N 434 
THR N     H2     sing N N 435 
THR CA    C      sing N N 436 
THR CA    CB     sing N N 437 
THR CA    HA     sing N N 438 
THR C     O      doub N N 439 
THR C     OXT    sing N N 440 
THR CB    OG1    sing N N 441 
THR CB    CG2    sing N N 442 
THR CB    HB     sing N N 443 
THR OG1   HG1    sing N N 444 
THR CG2   HG21   sing N N 445 
THR CG2   HG22   sing N N 446 
THR CG2   HG23   sing N N 447 
THR OXT   HXT    sing N N 448 
TRP N     CA     sing N N 449 
TRP N     H      sing N N 450 
TRP N     H2     sing N N 451 
TRP CA    C      sing N N 452 
TRP CA    CB     sing N N 453 
TRP CA    HA     sing N N 454 
TRP C     O      doub N N 455 
TRP C     OXT    sing N N 456 
TRP CB    CG     sing N N 457 
TRP CB    HB2    sing N N 458 
TRP CB    HB3    sing N N 459 
TRP CG    CD1    doub Y N 460 
TRP CG    CD2    sing Y N 461 
TRP CD1   NE1    sing Y N 462 
TRP CD1   HD1    sing N N 463 
TRP CD2   CE2    doub Y N 464 
TRP CD2   CE3    sing Y N 465 
TRP NE1   CE2    sing Y N 466 
TRP NE1   HE1    sing N N 467 
TRP CE2   CZ2    sing Y N 468 
TRP CE3   CZ3    doub Y N 469 
TRP CE3   HE3    sing N N 470 
TRP CZ2   CH2    doub Y N 471 
TRP CZ2   HZ2    sing N N 472 
TRP CZ3   CH2    sing Y N 473 
TRP CZ3   HZ3    sing N N 474 
TRP CH2   HH2    sing N N 475 
TRP OXT   HXT    sing N N 476 
TYR N     CA     sing N N 477 
TYR N     H      sing N N 478 
TYR N     H2     sing N N 479 
TYR CA    C      sing N N 480 
TYR CA    CB     sing N N 481 
TYR CA    HA     sing N N 482 
TYR C     O      doub N N 483 
TYR C     OXT    sing N N 484 
TYR CB    CG     sing N N 485 
TYR CB    HB2    sing N N 486 
TYR CB    HB3    sing N N 487 
TYR CG    CD1    doub Y N 488 
TYR CG    CD2    sing Y N 489 
TYR CD1   CE1    sing Y N 490 
TYR CD1   HD1    sing N N 491 
TYR CD2   CE2    doub Y N 492 
TYR CD2   HD2    sing N N 493 
TYR CE1   CZ     doub Y N 494 
TYR CE1   HE1    sing N N 495 
TYR CE2   CZ     sing Y N 496 
TYR CE2   HE2    sing N N 497 
TYR CZ    OH     sing N N 498 
TYR OH    HH     sing N N 499 
TYR OXT   HXT    sing N N 500 
VAL N     CA     sing N N 501 
VAL N     H      sing N N 502 
VAL N     H2     sing N N 503 
VAL CA    C      sing N N 504 
VAL CA    CB     sing N N 505 
VAL CA    HA     sing N N 506 
VAL C     O      doub N N 507 
VAL C     OXT    sing N N 508 
VAL CB    CG1    sing N N 509 
VAL CB    CG2    sing N N 510 
VAL CB    HB     sing N N 511 
VAL CG1   HG11   sing N N 512 
VAL CG1   HG12   sing N N 513 
VAL CG1   HG13   sing N N 514 
VAL CG2   HG21   sing N N 515 
VAL CG2   HG22   sing N N 516 
VAL CG2   HG23   sing N N 517 
VAL OXT   HXT    sing N N 518 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.078 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          10116 
_em_entity_assembly_naturalsource.organism             'Rattus norvegicus' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               0.899 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         53 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    1 
_em_image_recording.num_real_images                     31000 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   30000000 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? cryoSPARC      4.6          
'IMAGE ACQUISITION'        ? 2  ? ? 1 EPU            2.1.4        
MASKING                    ? 3  ? ? ? ?              ?            
'CTF CORRECTION'           ? 4  1 ? ? ?              ?            
'LAYERLINE INDEXING'       ? 5  ? ? ? ?              ?            
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?              ?            
'MODEL FITTING'            ? 7  ? 1 ? 'UCSF Chimera' 1.16         
OTHER                      ? 8  ? ? ? ?              ?            
'MODEL REFINEMENT'         ? 9  ? 1 ? PHENIX         1.21.1_5286: 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?              ?            
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ?              ?            
CLASSIFICATION             ? 12 1 ? ? cryoSPARC      4.6          
RECONSTRUCTION             ? 13 1 ? ? ?              ?            
# 
_em_specimen.concentration           0.23 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM151876 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9EF0 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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     . GLU A 1 66  ? 66.394  102.385 104.234 1.00 133.73 ? 66  GLU A N     1 
ATOM   2    C CA    . GLU A 1 66  ? 66.655  100.994 103.884 1.00 137.43 ? 66  GLU A CA    1 
ATOM   3    C C     . GLU A 1 66  ? 67.378  100.892 102.546 1.00 138.18 ? 66  GLU A C     1 
ATOM   4    O O     . GLU A 1 66  ? 68.336  100.132 102.405 1.00 137.85 ? 66  GLU A O     1 
ATOM   5    C CB    . GLU A 1 66  ? 65.349  100.198 103.837 1.00 138.35 ? 66  GLU A CB    1 
ATOM   6    C CG    . GLU A 1 66  ? 65.539  98.711  103.590 1.00 138.95 ? 66  GLU A CG    1 
ATOM   7    C CD    . GLU A 1 66  ? 64.226  97.958  103.527 1.00 143.20 ? 66  GLU A CD    1 
ATOM   8    O OE1   . GLU A 1 66  ? 63.409  98.260  102.632 1.00 144.65 ? 66  GLU A OE1   1 
ATOM   9    O OE2   . GLU A 1 66  ? 64.011  97.064  104.371 1.00 146.76 ? 66  GLU A OE2   1 
ATOM   10   N N     . SER A 1 67  ? 66.905  101.661 101.562 1.00 139.13 ? 67  SER A N     1 
ATOM   11   C CA    . SER A 1 67  ? 67.533  101.648 100.245 1.00 138.46 ? 67  SER A CA    1 
ATOM   12   C C     . SER A 1 67  ? 68.970  102.149 100.312 1.00 138.08 ? 67  SER A C     1 
ATOM   13   O O     . SER A 1 67  ? 69.868  101.570 99.689  1.00 136.55 ? 67  SER A O     1 
ATOM   14   C CB    . SER A 1 67  ? 66.715  102.491 99.267  1.00 134.89 ? 67  SER A CB    1 
ATOM   15   O OG    . SER A 1 67  ? 66.627  103.837 99.703  1.00 131.59 ? 67  SER A OG    1 
ATOM   16   N N     . SER A 1 68  ? 69.207  103.221 101.062 1.00 136.28 ? 68  SER A N     1 
ATOM   17   C CA    . SER A 1 68  ? 70.557  103.741 101.219 1.00 133.18 ? 68  SER A CA    1 
ATOM   18   C C     . SER A 1 68  ? 71.367  102.832 102.135 1.00 130.15 ? 68  SER A C     1 
ATOM   19   O O     . SER A 1 68  ? 70.851  102.297 103.120 1.00 128.71 ? 68  SER A O     1 
ATOM   20   C CB    . SER A 1 68  ? 70.514  105.161 101.780 1.00 132.91 ? 68  SER A CB    1 
ATOM   21   O OG    . SER A 1 68  ? 71.815  105.629 102.073 1.00 130.72 ? 68  SER A OG    1 
ATOM   22   N N     . PHE A 1 69  ? 72.647  102.654 101.806 1.00 126.42 ? 69  PHE A N     1 
ATOM   23   C CA    . PHE A 1 69  ? 73.490  101.708 102.524 1.00 124.11 ? 69  PHE A CA    1 
ATOM   24   C C     . PHE A 1 69  ? 74.408  102.357 103.553 1.00 124.81 ? 69  PHE A C     1 
ATOM   25   O O     . PHE A 1 69  ? 75.007  101.638 104.357 1.00 125.81 ? 69  PHE A O     1 
ATOM   26   C CB    . PHE A 1 69  ? 74.323  100.879 101.535 1.00 119.96 ? 69  PHE A CB    1 
ATOM   27   C CG    . PHE A 1 69  ? 75.556  101.574 101.036 1.00 114.78 ? 69  PHE A CG    1 
ATOM   28   C CD1   . PHE A 1 69  ? 75.464  102.597 100.110 1.00 116.27 ? 69  PHE A CD1   1 
ATOM   29   C CD2   . PHE A 1 69  ? 76.809  101.191 101.481 1.00 109.97 ? 69  PHE A CD2   1 
ATOM   30   C CE1   . PHE A 1 69  ? 76.599  103.230 99.644  1.00 116.49 ? 69  PHE A CE1   1 
ATOM   31   C CE2   . PHE A 1 69  ? 77.947  101.822 101.019 1.00 107.07 ? 69  PHE A CE2   1 
ATOM   32   C CZ    . PHE A 1 69  ? 77.841  102.843 100.100 1.00 110.64 ? 69  PHE A CZ    1 
ATOM   33   N N     . VAL A 1 70  ? 74.534  103.687 103.561 1.00 123.96 ? 70  VAL A N     1 
ATOM   34   C CA    . VAL A 1 70  ? 75.272  104.327 104.646 1.00 123.00 ? 70  VAL A CA    1 
ATOM   35   C C     . VAL A 1 70  ? 74.508  104.190 105.957 1.00 122.08 ? 70  VAL A C     1 
ATOM   36   O O     . VAL A 1 70  ? 75.111  104.028 107.026 1.00 119.11 ? 70  VAL A O     1 
ATOM   37   C CB    . VAL A 1 70  ? 75.573  105.800 104.316 1.00 125.85 ? 70  VAL A CB    1 
ATOM   38   C CG1   . VAL A 1 70  ? 76.813  105.902 103.440 1.00 125.55 ? 70  VAL A CG1   1 
ATOM   39   C CG2   . VAL A 1 70  ? 74.381  106.453 103.644 1.00 124.99 ? 70  VAL A CG2   1 
ATOM   40   N N     . GLU A 1 71  ? 73.176  104.249 105.903 1.00 123.80 ? 71  GLU A N     1 
ATOM   41   C CA    . GLU A 1 71  ? 72.381  103.965 107.093 1.00 125.26 ? 71  GLU A CA    1 
ATOM   42   C C     . GLU A 1 71  ? 72.596  102.531 107.559 1.00 125.81 ? 71  GLU A C     1 
ATOM   43   O O     . GLU A 1 71  ? 72.639  102.259 108.765 1.00 126.16 ? 71  GLU A O     1 
ATOM   44   C CB    . GLU A 1 71  ? 70.902  104.225 106.809 1.00 127.48 ? 71  GLU A CB    1 
ATOM   45   C CG    . GLU A 1 71  ? 70.576  105.677 106.499 1.00 128.39 ? 71  GLU A CG    1 
ATOM   46   C CD    . GLU A 1 71  ? 71.274  106.644 107.433 1.00 130.93 ? 71  GLU A CD    1 
ATOM   47   O OE1   . GLU A 1 71  ? 71.021  106.582 108.655 1.00 130.91 ? 71  GLU A OE1   1 
ATOM   48   O OE2   . GLU A 1 71  ? 72.077  107.467 106.946 1.00 131.62 ? 71  GLU A OE2   1 
ATOM   49   N N     . LYS A 1 72  ? 72.730  101.598 106.614 1.00 125.34 ? 72  LYS A N     1 
ATOM   50   C CA    . LYS A 1 72  ? 73.025  100.217 106.975 1.00 123.70 ? 72  LYS A CA    1 
ATOM   51   C C     . LYS A 1 72  ? 74.411  100.090 107.597 1.00 121.69 ? 72  LYS A C     1 
ATOM   52   O O     . LYS A 1 72  ? 74.606  99.277  108.507 1.00 123.28 ? 72  LYS A O     1 
ATOM   53   C CB    . LYS A 1 72  ? 72.880  99.319  105.746 1.00 120.03 ? 72  LYS A CB    1 
ATOM   54   C CG    . LYS A 1 72  ? 73.715  98.053  105.764 1.00 116.15 ? 72  LYS A CG    1 
ATOM   55   C CD    . LYS A 1 72  ? 73.667  97.364  104.412 1.00 114.48 ? 72  LYS A CD    1 
ATOM   56   C CE    . LYS A 1 72  ? 72.229  97.221  103.931 1.00 114.15 ? 72  LYS A CE    1 
ATOM   57   N NZ    . LYS A 1 72  ? 72.144  96.690  102.546 1.00 108.94 ? 72  LYS A NZ    1 
ATOM   58   N N     . MET A 1 73  ? 75.375  100.886 107.131 1.00 120.78 ? 73  MET A N     1 
ATOM   59   C CA    . MET A 1 73  ? 76.655  100.989 107.826 1.00 119.79 ? 73  MET A CA    1 
ATOM   60   C C     . MET A 1 73  ? 76.462  101.457 109.261 1.00 121.75 ? 73  MET A C     1 
ATOM   61   O O     . MET A 1 73  ? 77.048  100.900 110.196 1.00 120.28 ? 73  MET A O     1 
ATOM   62   C CB    . MET A 1 73  ? 77.581  101.954 107.088 1.00 120.93 ? 73  MET A CB    1 
ATOM   63   C CG    . MET A 1 73  ? 77.936  101.562 105.679 1.00 117.74 ? 73  MET A CG    1 
ATOM   64   S SD    . MET A 1 73  ? 79.350  100.458 105.729 1.00 118.26 ? 73  MET A SD    1 
ATOM   65   C CE    . MET A 1 73  ? 80.657  101.605 105.303 1.00 104.03 ? 73  MET A CE    1 
ATOM   66   N N     . LYS A 1 74  ? 75.649  102.497 109.447 1.00 122.98 ? 74  LYS A N     1 
ATOM   67   C CA    . LYS A 1 74  ? 75.444  103.053 110.781 1.00 122.35 ? 74  LYS A CA    1 
ATOM   68   C C     . LYS A 1 74  ? 74.829  102.024 111.722 1.00 120.69 ? 74  LYS A C     1 
ATOM   69   O O     . LYS A 1 74  ? 75.246  101.902 112.880 1.00 119.48 ? 74  LYS A O     1 
ATOM   70   C CB    . LYS A 1 74  ? 74.565  104.301 110.701 1.00 124.81 ? 74  LYS A CB    1 
ATOM   71   C CG    . LYS A 1 74  ? 75.195  105.455 109.939 1.00 124.71 ? 74  LYS A CG    1 
ATOM   72   C CD    . LYS A 1 74  ? 74.227  106.617 109.797 1.00 126.14 ? 74  LYS A CD    1 
ATOM   73   C CE    . LYS A 1 74  ? 74.939  107.871 109.317 1.00 125.72 ? 74  LYS A CE    1 
ATOM   74   N NZ    . LYS A 1 74  ? 74.019  109.040 109.251 1.00 123.31 ? 74  LYS A NZ    1 
ATOM   75   N N     . LYS A 1 75  ? 73.834  101.274 111.243 1.00 123.65 ? 75  LYS A N     1 
ATOM   76   C CA    . LYS A 1 75  ? 73.207  100.265 112.094 1.00 124.57 ? 75  LYS A CA    1 
ATOM   77   C C     . LYS A 1 75  ? 74.137  99.081  112.344 1.00 119.34 ? 75  LYS A C     1 
ATOM   78   O O     . LYS A 1 75  ? 74.237  98.596  113.476 1.00 114.26 ? 75  LYS A O     1 
ATOM   79   C CB    . LYS A 1 75  ? 71.886  99.790  111.487 1.00 125.19 ? 75  LYS A CB    1 
ATOM   80   C CG    . LYS A 1 75  ? 71.005  100.901 110.948 1.00 125.32 ? 75  LYS A CG    1 
ATOM   81   C CD    . LYS A 1 75  ? 69.628  100.382 110.568 1.00 124.03 ? 75  LYS A CD    1 
ATOM   82   C CE    . LYS A 1 75  ? 68.822  100.005 111.801 1.00 124.16 ? 75  LYS A CE    1 
ATOM   83   N NZ    . LYS A 1 75  ? 67.406  99.691  111.467 1.00 125.69 ? 75  LYS A NZ    1 
ATOM   84   N N     . THR A 1 76  ? 74.824  98.601  111.306 1.00 120.33 ? 76  THR A N     1 
ATOM   85   C CA    . THR A 1 76  ? 75.700  97.446  111.461 1.00 115.81 ? 76  THR A CA    1 
ATOM   86   C C     . THR A 1 76  ? 77.062  97.807  112.039 1.00 114.86 ? 76  THR A C     1 
ATOM   87   O O     . THR A 1 76  ? 77.793  96.909  112.470 1.00 114.60 ? 76  THR A O     1 
ATOM   88   C CB    . THR A 1 76  ? 75.892  96.741  110.116 1.00 118.24 ? 76  THR A CB    1 
ATOM   89   O OG1   . THR A 1 76  ? 76.328  97.689  109.133 1.00 122.55 ? 76  THR A OG1   1 
ATOM   90   C CG2   . THR A 1 76  ? 74.590  96.103  109.658 1.00 116.74 ? 76  THR A CG2   1 
ATOM   91   N N     . GLY A 1 77  ? 77.419  99.089  112.056 1.00 117.11 ? 77  GLY A N     1 
ATOM   92   C CA    . GLY A 1 77  ? 78.701  99.490  112.597 1.00 116.20 ? 77  GLY A CA    1 
ATOM   93   C C     . GLY A 1 77  ? 79.894  99.110  111.753 1.00 116.62 ? 77  GLY A C     1 
ATOM   94   O O     . GLY A 1 77  ? 81.008  99.024  112.276 1.00 114.77 ? 77  GLY A O     1 
ATOM   95   N N     . ARG A 1 78  ? 79.696  98.878  110.461 1.00 115.30 ? 78  ARG A N     1 
ATOM   96   C CA    . ARG A 1 78  ? 80.775  98.523  109.553 1.00 109.74 ? 78  ARG A CA    1 
ATOM   97   C C     . ARG A 1 78  ? 81.291  99.760  108.828 1.00 111.97 ? 78  ARG A C     1 
ATOM   98   O O     . ARG A 1 78  ? 80.584  100.759 108.671 1.00 116.66 ? 78  ARG A O     1 
ATOM   99   C CB    . ARG A 1 78  ? 80.310  97.468  108.547 1.00 107.27 ? 78  ARG A CB    1 
ATOM   100  C CG    . ARG A 1 78  ? 80.274  96.061  109.121 1.00 106.64 ? 78  ARG A CG    1 
ATOM   101  C CD    . ARG A 1 78  ? 79.063  95.284  108.638 1.00 106.10 ? 78  ARG A CD    1 
ATOM   102  N NE    . ARG A 1 78  ? 78.876  94.049  109.389 1.00 107.52 ? 78  ARG A NE    1 
ATOM   103  C CZ    . ARG A 1 78  ? 79.601  92.951  109.221 1.00 107.00 ? 78  ARG A CZ    1 
ATOM   104  N NH1   . ARG A 1 78  ? 80.573  92.894  108.325 1.00 104.43 ? 78  ARG A NH1   1 
ATOM   105  N NH2   . ARG A 1 78  ? 79.343  91.883  109.970 1.00 105.71 ? 78  ARG A NH2   1 
ATOM   106  N N     . ASN A 1 79  ? 82.546  99.681  108.386 1.00 108.71 ? 79  ASN A N     1 
ATOM   107  C CA    . ASN A 1 79  ? 83.241  100.837 107.833 1.00 109.42 ? 79  ASN A CA    1 
ATOM   108  C C     . ASN A 1 79  ? 83.862  100.620 106.460 1.00 104.15 ? 79  ASN A C     1 
ATOM   109  O O     . ASN A 1 79  ? 83.989  101.595 105.710 1.00 104.95 ? 79  ASN A O     1 
ATOM   110  C CB    . ASN A 1 79  ? 84.343  101.302 108.796 1.00 108.06 ? 79  ASN A CB    1 
ATOM   111  C CG    . ASN A 1 79  ? 85.541  100.378 108.792 1.00 106.68 ? 79  ASN A CG    1 
ATOM   112  O OD1   . ASN A 1 79  ? 85.443  99.219  109.192 1.00 100.57 ? 79  ASN A OD1   1 
ATOM   113  N ND2   . ASN A 1 79  ? 86.679  100.882 108.333 1.00 110.49 ? 79  ASN A ND2   1 
ATOM   114  N N     . ILE A 1 80  ? 84.246  99.399  106.099 1.00 97.97  ? 80  ILE A N     1 
ATOM   115  C CA    . ILE A 1 80  ? 84.941  99.127  104.845 1.00 90.91  ? 80  ILE A CA    1 
ATOM   116  C C     . ILE A 1 80  ? 83.976  98.432  103.896 1.00 86.38  ? 80  ILE A C     1 
ATOM   117  O O     . ILE A 1 80  ? 83.301  97.471  104.283 1.00 92.10  ? 80  ILE A O     1 
ATOM   118  C CB    . ILE A 1 80  ? 86.204  98.274  105.071 1.00 90.32  ? 80  ILE A CB    1 
ATOM   119  C CG1   . ILE A 1 80  ? 86.681  97.655  103.756 1.00 85.38  ? 80  ILE A CG1   1 
ATOM   120  C CG2   . ILE A 1 80  ? 85.948  97.201  106.114 1.00 94.32  ? 80  ILE A CG2   1 
ATOM   121  C CD1   . ILE A 1 80  ? 88.086  97.101  103.819 1.00 83.18  ? 80  ILE A CD1   1 
ATOM   122  N N     . ILE A 1 81  ? 83.903  98.922  102.661 1.00 80.30  ? 81  ILE A N     1 
ATOM   123  C CA    . ILE A 1 81  ? 83.046  98.349  101.632 1.00 79.57  ? 81  ILE A CA    1 
ATOM   124  C C     . ILE A 1 81  ? 83.903  97.966  100.437 1.00 79.38  ? 81  ILE A C     1 
ATOM   125  O O     . ILE A 1 81  ? 84.780  98.730  100.019 1.00 81.92  ? 81  ILE A O     1 
ATOM   126  C CB    . ILE A 1 81  ? 81.931  99.320  101.198 1.00 78.85  ? 81  ILE A CB    1 
ATOM   127  C CG1   . ILE A 1 81  ? 81.101  99.732  102.401 1.00 85.26  ? 81  ILE A CG1   1 
ATOM   128  C CG2   . ILE A 1 81  ? 81.025  98.658  100.186 1.00 79.18  ? 81  ILE A CG2   1 
ATOM   129  C CD1   . ILE A 1 81  ? 80.413  98.572  103.051 1.00 94.09  ? 81  ILE A CD1   1 
ATOM   130  N N     . VAL A 1 82  ? 83.650  96.781  99.891  1.00 76.75  ? 82  VAL A N     1 
ATOM   131  C CA    . VAL A 1 82  ? 84.285  96.328  98.662  1.00 74.91  ? 82  VAL A CA    1 
ATOM   132  C C     . VAL A 1 82  ? 83.187  96.105  97.633  1.00 74.80  ? 82  VAL A C     1 
ATOM   133  O O     . VAL A 1 82  ? 82.373  95.184  97.777  1.00 82.15  ? 82  VAL A O     1 
ATOM   134  C CB    . VAL A 1 82  ? 85.106  95.048  98.877  1.00 72.69  ? 82  VAL A CB    1 
ATOM   135  C CG1   . VAL A 1 82  ? 86.021  94.807  97.691  1.00 73.83  ? 82  VAL A CG1   1 
ATOM   136  C CG2   . VAL A 1 82  ? 85.906  95.143  100.163 1.00 73.21  ? 82  VAL A CG2   1 
ATOM   137  N N     . PHE A 1 83  ? 83.162  96.942  96.600  1.00 74.54  ? 83  PHE A N     1 
ATOM   138  C CA    . PHE A 1 83  ? 82.192  96.809  95.524  1.00 76.84  ? 83  PHE A CA    1 
ATOM   139  C C     . PHE A 1 83  ? 82.706  95.834  94.476  1.00 78.33  ? 83  PHE A C     1 
ATOM   140  O O     . PHE A 1 83  ? 83.915  95.708  94.267  1.00 80.46  ? 83  PHE A O     1 
ATOM   141  C CB    . PHE A 1 83  ? 81.906  98.160  94.869  1.00 80.89  ? 83  PHE A CB    1 
ATOM   142  C CG    . PHE A 1 83  ? 80.999  99.048  95.667  1.00 82.76  ? 83  PHE A CG    1 
ATOM   143  C CD1   . PHE A 1 83  ? 81.490  99.811  96.709  1.00 82.83  ? 83  PHE A CD1   1 
ATOM   144  C CD2   . PHE A 1 83  ? 79.649  99.116  95.374  1.00 90.76  ? 83  PHE A CD2   1 
ATOM   145  C CE1   . PHE A 1 83  ? 80.652  100.632 97.436  1.00 89.93  ? 83  PHE A CE1   1 
ATOM   146  C CE2   . PHE A 1 83  ? 78.807  99.930  96.101  1.00 95.66  ? 83  PHE A CE2   1 
ATOM   147  C CZ    . PHE A 1 83  ? 79.309  100.688 97.134  1.00 95.29  ? 83  PHE A CZ    1 
ATOM   148  N N     . TYR A 1 84  ? 81.779  95.143  93.819  1.00 79.76  ? 84  TYR A N     1 
ATOM   149  C CA    . TYR A 1 84  ? 82.110  94.221  92.743  1.00 82.57  ? 84  TYR A CA    1 
ATOM   150  C C     . TYR A 1 84  ? 81.225  94.489  91.536  1.00 89.10  ? 84  TYR A C     1 
ATOM   151  O O     . TYR A 1 84  ? 80.028  94.755  91.676  1.00 90.94  ? 84  TYR A O     1 
ATOM   152  C CB    . TYR A 1 84  ? 81.961  92.751  93.165  1.00 82.66  ? 84  TYR A CB    1 
ATOM   153  C CG    . TYR A 1 84  ? 80.627  92.367  93.773  1.00 81.08  ? 84  TYR A CG    1 
ATOM   154  C CD1   . TYR A 1 84  ? 80.225  92.862  95.006  1.00 87.64  ? 84  TYR A CD1   1 
ATOM   155  C CD2   . TYR A 1 84  ? 79.758  91.526  93.095  1.00 79.34  ? 84  TYR A CD2   1 
ATOM   156  C CE1   . TYR A 1 84  ? 79.010  92.506  95.554  1.00 91.49  ? 84  TYR A CE1   1 
ATOM   157  C CE2   . TYR A 1 84  ? 78.542  91.167  93.635  1.00 84.53  ? 84  TYR A CE2   1 
ATOM   158  C CZ    . TYR A 1 84  ? 78.172  91.661  94.863  1.00 90.92  ? 84  TYR A CZ    1 
ATOM   159  O OH    . TYR A 1 84  ? 76.958  91.305  95.401  1.00 97.01  ? 84  TYR A OH    1 
ATOM   160  N N     . GLY A 1 85  ? 81.824  94.415  90.352  1.00 89.45  ? 85  GLY A N     1 
ATOM   161  C CA    . GLY A 1 85  ? 81.087  94.538  89.110  1.00 88.66  ? 85  GLY A CA    1 
ATOM   162  C C     . GLY A 1 85  ? 81.076  93.233  88.345  1.00 89.08  ? 85  GLY A C     1 
ATOM   163  O O     . GLY A 1 85  ? 81.264  93.214  87.126  1.00 95.71  ? 85  GLY A O     1 
ATOM   164  N N     . SER A 1 86  ? 80.868  92.131  89.057  1.00 87.36  ? 86  SER A N     1 
ATOM   165  C CA    . SER A 1 86  ? 81.015  90.808  88.474  1.00 91.19  ? 86  SER A CA    1 
ATOM   166  C C     . SER A 1 86  ? 79.828  90.443  87.592  1.00 94.63  ? 86  SER A C     1 
ATOM   167  O O     . SER A 1 86  ? 78.714  90.945  87.764  1.00 94.29  ? 86  SER A O     1 
ATOM   168  C CB    . SER A 1 86  ? 81.167  89.753  89.568  1.00 94.13  ? 86  SER A CB    1 
ATOM   169  O OG    . SER A 1 86  ? 81.745  88.572  89.046  1.00 92.34  ? 86  SER A OG    1 
ATOM   170  N N     . GLN A 1 87  ? 80.087  89.554  86.635  1.00 96.57  ? 87  GLN A N     1 
ATOM   171  C CA    . GLN A 1 87  ? 79.031  88.917  85.861  1.00 97.56  ? 87  GLN A CA    1 
ATOM   172  C C     . GLN A 1 87  ? 79.210  87.404  85.889  1.00 96.49  ? 87  GLN A C     1 
ATOM   173  O O     . GLN A 1 87  ? 78.226  86.657  85.896  1.00 93.34  ? 87  GLN A O     1 
ATOM   174  C CB    . GLN A 1 87  ? 79.020  89.437  84.423  1.00 97.10  ? 87  GLN A CB    1 
ATOM   175  C CG    . GLN A 1 87  ? 78.184  90.689  84.230  1.00 101.45 ? 87  GLN A CG    1 
ATOM   176  C CD    . GLN A 1 87  ? 77.711  90.860  82.801  1.00 107.31 ? 87  GLN A CD    1 
ATOM   177  O OE1   . GLN A 1 87  ? 77.177  91.907  82.433  1.00 108.08 ? 87  GLN A OE1   1 
ATOM   178  N NE2   . GLN A 1 87  ? 77.905  89.831  81.986  1.00 110.89 ? 87  GLN A NE2   1 
ATOM   179  N N     . THR A 1 88  ? 80.461  86.944  85.905  1.00 94.55  ? 88  THR A N     1 
ATOM   180  C CA    . THR A 1 88  ? 80.766  85.522  85.974  1.00 90.36  ? 88  THR A CA    1 
ATOM   181  C C     . THR A 1 88  ? 81.213  85.068  87.358  1.00 91.16  ? 88  THR A C     1 
ATOM   182  O O     . THR A 1 88  ? 81.608  83.908  87.513  1.00 92.15  ? 88  THR A O     1 
ATOM   183  C CB    . THR A 1 88  ? 81.837  85.154  84.941  1.00 92.18  ? 88  THR A CB    1 
ATOM   184  O OG1   . THR A 1 88  ? 83.008  85.949  85.155  1.00 98.14  ? 88  THR A OG1   1 
ATOM   185  C CG2   . THR A 1 88  ? 81.319  85.396  83.533  1.00 93.59  ? 88  THR A CG2   1 
ATOM   186  N N     . GLY A 1 89  ? 81.172  85.943  88.363  1.00 91.02  ? 89  GLY A N     1 
ATOM   187  C CA    . GLY A 1 89  ? 81.322  85.555  89.750  1.00 91.07  ? 89  GLY A CA    1 
ATOM   188  C C     . GLY A 1 89  ? 82.678  85.833  90.368  1.00 91.02  ? 89  GLY A C     1 
ATOM   189  O O     . GLY A 1 89  ? 82.785  85.832  91.601  1.00 96.57  ? 89  GLY A O     1 
ATOM   190  N N     . THR A 1 90  ? 83.719  86.064  89.563  1.00 86.50  ? 90  THR A N     1 
ATOM   191  C CA    . THR A 1 90  ? 85.057  86.215  90.132  1.00 86.59  ? 90  THR A CA    1 
ATOM   192  C C     . THR A 1 90  ? 85.173  87.482  90.973  1.00 84.39  ? 90  THR A C     1 
ATOM   193  O O     . THR A 1 90  ? 85.742  87.456  92.070  1.00 86.20  ? 90  THR A O     1 
ATOM   194  C CB    . THR A 1 90  ? 86.110  86.210  89.026  1.00 86.65  ? 90  THR A CB    1 
ATOM   195  O OG1   . THR A 1 90  ? 86.018  87.422  88.271  1.00 91.85  ? 90  THR A OG1   1 
ATOM   196  C CG2   . THR A 1 90  ? 85.905  85.022  88.101  1.00 87.93  ? 90  THR A CG2   1 
ATOM   197  N N     . ALA A 1 91  ? 84.642  88.603  90.478  1.00 81.55  ? 91  ALA A N     1 
ATOM   198  C CA    . ALA A 1 91  ? 84.724  89.847  91.238  1.00 78.53  ? 91  ALA A CA    1 
ATOM   199  C C     . ALA A 1 91  ? 83.902  89.768  92.516  1.00 80.70  ? 91  ALA A C     1 
ATOM   200  O O     . ALA A 1 91  ? 84.294  90.322  93.548  1.00 84.87  ? 91  ALA A O     1 
ATOM   201  C CB    . ALA A 1 91  ? 84.265  91.028  90.384  1.00 81.28  ? 91  ALA A CB    1 
ATOM   202  N N     . GLU A 1 92  ? 82.751  89.096  92.462  1.00 79.88  ? 92  GLU A N     1 
ATOM   203  C CA    . GLU A 1 92  ? 81.939  88.920  93.662  1.00 79.38  ? 92  GLU A CA    1 
ATOM   204  C C     . GLU A 1 92  ? 82.703  88.141  94.723  1.00 80.38  ? 92  GLU A C     1 
ATOM   205  O O     . GLU A 1 92  ? 82.711  88.515  95.902  1.00 81.71  ? 92  GLU A O     1 
ATOM   206  C CB    . GLU A 1 92  ? 80.632  88.212  93.306  1.00 85.26  ? 92  GLU A CB    1 
ATOM   207  C CG    . GLU A 1 92  ? 79.837  87.732  94.503  1.00 92.49  ? 92  GLU A CG    1 
ATOM   208  C CD    . GLU A 1 92  ? 78.482  87.179  94.113  1.00 98.12  ? 92  GLU A CD    1 
ATOM   209  O OE1   . GLU A 1 92  ? 77.610  87.971  93.699  1.00 97.66  ? 92  GLU A OE1   1 
ATOM   210  O OE2   . GLU A 1 92  ? 78.288  85.950  94.217  1.00 105.83 ? 92  GLU A OE2   1 
ATOM   211  N N     . GLU A 1 93  ? 83.363  87.056  94.315  1.00 78.59  ? 93  GLU A N     1 
ATOM   212  C CA    . GLU A 1 93  ? 84.153  86.276  95.258  1.00 79.49  ? 93  GLU A CA    1 
ATOM   213  C C     . GLU A 1 93  ? 85.330  87.078  95.795  1.00 76.10  ? 93  GLU A C     1 
ATOM   214  O O     . GLU A 1 93  ? 85.655  86.977  96.982  1.00 75.73  ? 93  GLU A O     1 
ATOM   215  C CB    . GLU A 1 93  ? 84.630  84.983  94.595  1.00 85.42  ? 93  GLU A CB    1 
ATOM   216  C CG    . GLU A 1 93  ? 86.059  84.588  94.921  1.00 87.71  ? 93  GLU A CG    1 
ATOM   217  C CD    . GLU A 1 93  ? 86.470  83.295  94.248  1.00 95.26  ? 93  GLU A CD    1 
ATOM   218  O OE1   . GLU A 1 93  ? 86.009  83.035  93.117  1.00 89.94  ? 93  GLU A OE1   1 
ATOM   219  O OE2   . GLU A 1 93  ? 87.247  82.532  94.857  1.00 99.58  ? 93  GLU A OE2   1 
ATOM   220  N N     . PHE A 1 94  ? 85.970  87.883  94.945  1.00 76.13  ? 94  PHE A N     1 
ATOM   221  C CA    . PHE A 1 94  ? 87.088  88.707  95.398  1.00 74.24  ? 94  PHE A CA    1 
ATOM   222  C C     . PHE A 1 94  ? 86.633  89.736  96.427  1.00 71.21  ? 94  PHE A C     1 
ATOM   223  O O     . PHE A 1 94  ? 87.300  89.942  97.449  1.00 73.60  ? 94  PHE A O     1 
ATOM   224  C CB    . PHE A 1 94  ? 87.736  89.395  94.198  1.00 72.23  ? 94  PHE A CB    1 
ATOM   225  C CG    . PHE A 1 94  ? 88.699  88.524  93.443  1.00 74.07  ? 94  PHE A CG    1 
ATOM   226  C CD1   . PHE A 1 94  ? 88.665  87.147  93.579  1.00 80.41  ? 94  PHE A CD1   1 
ATOM   227  C CD2   . PHE A 1 94  ? 89.614  89.079  92.569  1.00 75.83  ? 94  PHE A CD2   1 
ATOM   228  C CE1   . PHE A 1 94  ? 89.542  86.345  92.879  1.00 82.75  ? 94  PHE A CE1   1 
ATOM   229  C CE2   . PHE A 1 94  ? 90.489  88.281  91.863  1.00 78.27  ? 94  PHE A CE2   1 
ATOM   230  C CZ    . PHE A 1 94  ? 90.455  86.914  92.020  1.00 81.40  ? 94  PHE A CZ    1 
ATOM   231  N N     . ALA A 1 95  ? 85.495  90.385  96.175  1.00 69.20  ? 95  ALA A N     1 
ATOM   232  C CA    . ALA A 1 95  ? 84.966  91.358  97.124  1.00 68.80  ? 95  ALA A CA    1 
ATOM   233  C C     . ALA A 1 95  ? 84.567  90.692  98.434  1.00 71.04  ? 95  ALA A C     1 
ATOM   234  O O     . ALA A 1 95  ? 84.809  91.239  99.517  1.00 74.83  ? 95  ALA A O     1 
ATOM   235  C CB    . ALA A 1 95  ? 83.776  92.093  96.511  1.00 74.94  ? 95  ALA A CB    1 
ATOM   236  N N     . ASN A 1 96  ? 83.948  89.511  98.357  1.00 74.41  ? 96  ASN A N     1 
ATOM   237  C CA    . ASN A 1 96  ? 83.593  88.786  99.572  1.00 74.30  ? 96  ASN A CA    1 
ATOM   238  C C     . ASN A 1 96  ? 84.837  88.411  100.366 1.00 70.76  ? 96  ASN A C     1 
ATOM   239  O O     . ASN A 1 96  ? 84.854  88.518  101.599 1.00 70.27  ? 96  ASN A O     1 
ATOM   240  C CB    . ASN A 1 96  ? 82.782  87.540  99.219  1.00 74.31  ? 96  ASN A CB    1 
ATOM   241  C CG    . ASN A 1 96  ? 81.356  87.866  98.818  1.00 75.43  ? 96  ASN A CG    1 
ATOM   242  O OD1   . ASN A 1 96  ? 80.980  89.032  98.714  1.00 79.52  ? 96  ASN A OD1   1 
ATOM   243  N ND2   . ASN A 1 96  ? 80.556  86.833  98.589  1.00 75.49  ? 96  ASN A ND2   1 
ATOM   244  N N     . ARG A 1 97  ? 85.891  87.973  99.675  1.00 68.71  ? 97  ARG A N     1 
ATOM   245  C CA    . ARG A 1 97  ? 87.134  87.630  100.353 1.00 69.24  ? 97  ARG A CA    1 
ATOM   246  C C     . ARG A 1 97  ? 87.752  88.849  101.024 1.00 73.12  ? 97  ARG A C     1 
ATOM   247  O O     . ARG A 1 97  ? 88.252  88.756  102.149 1.00 76.66  ? 97  ARG A O     1 
ATOM   248  C CB    . ARG A 1 97  ? 88.118  87.009  99.365  1.00 66.62  ? 97  ARG A CB    1 
ATOM   249  C CG    . ARG A 1 97  ? 89.424  86.572  99.999  1.00 70.44  ? 97  ARG A CG    1 
ATOM   250  C CD    . ARG A 1 97  ? 90.470  86.263  98.949  1.00 67.25  ? 97  ARG A CD    1 
ATOM   251  N NE    . ARG A 1 97  ? 89.885  85.652  97.763  1.00 66.94  ? 97  ARG A NE    1 
ATOM   252  C CZ    . ARG A 1 97  ? 90.589  85.134  96.767  1.00 74.54  ? 97  ARG A CZ    1 
ATOM   253  N NH1   . ARG A 1 97  ? 91.912  85.132  96.784  1.00 73.19  ? 97  ARG A NH1   1 
ATOM   254  N NH2   . ARG A 1 97  ? 89.950  84.603  95.728  1.00 78.92  ? 97  ARG A NH2   1 
ATOM   255  N N     . LEU A 1 98  ? 87.734  90.001  100.349 1.00 73.81  ? 98  LEU A N     1 
ATOM   256  C CA    . LEU A 1 98  ? 88.280  91.212  100.957 1.00 72.03  ? 98  LEU A CA    1 
ATOM   257  C C     . LEU A 1 98  ? 87.477  91.626  102.185 1.00 75.35  ? 98  LEU A C     1 
ATOM   258  O O     . LEU A 1 98  ? 88.051  92.008  103.214 1.00 80.78  ? 98  LEU A O     1 
ATOM   259  C CB    . LEU A 1 98  ? 88.316  92.346  99.933  1.00 69.24  ? 98  LEU A CB    1 
ATOM   260  C CG    . LEU A 1 98  ? 89.610  92.508  99.134  1.00 65.92  ? 98  LEU A CG    1 
ATOM   261  C CD1   . LEU A 1 98  ? 89.610  93.827  98.384  1.00 63.56  ? 98  LEU A CD1   1 
ATOM   262  C CD2   . LEU A 1 98  ? 90.824  92.405  100.040 1.00 69.49  ? 98  LEU A CD2   1 
ATOM   263  N N     . SER A 1 99  ? 86.147  91.555  102.099 1.00 75.92  ? 99  SER A N     1 
ATOM   264  C CA    . SER A 1 99  ? 85.314  91.909  103.244 1.00 74.82  ? 99  SER A CA    1 
ATOM   265  C C     . SER A 1 99  ? 85.557  90.968  104.416 1.00 77.54  ? 99  SER A C     1 
ATOM   266  O O     . SER A 1 99  ? 85.589  91.402  105.573 1.00 77.19  ? 99  SER A O     1 
ATOM   267  C CB    . SER A 1 99  ? 83.840  91.903  102.844 1.00 75.08  ? 99  SER A CB    1 
ATOM   268  O OG    . SER A 1 99  ? 83.583  92.866  101.839 1.00 80.11  ? 99  SER A OG    1 
ATOM   269  N N     . LYS A 1 100 ? 85.718  89.672  104.139 1.00 81.97  ? 100 LYS A N     1 
ATOM   270  C CA    . LYS A 1 100 ? 86.041  88.725  105.203 1.00 83.41  ? 100 LYS A CA    1 
ATOM   271  C C     . LYS A 1 100 ? 87.414  89.009  105.800 1.00 83.94  ? 100 LYS A C     1 
ATOM   272  O O     . LYS A 1 100 ? 87.592  88.942  107.022 1.00 85.30  ? 100 LYS A O     1 
ATOM   273  C CB    . LYS A 1 100 ? 85.974  87.295  104.670 1.00 81.35  ? 100 LYS A CB    1 
ATOM   274  C CG    . LYS A 1 100 ? 84.686  86.564  105.005 1.00 80.09  ? 100 LYS A CG    1 
ATOM   275  C CD    . LYS A 1 100 ? 84.326  85.569  103.918 1.00 77.07  ? 100 LYS A CD    1 
ATOM   276  C CE    . LYS A 1 100 ? 85.209  84.337  103.989 1.00 70.79  ? 100 LYS A CE    1 
ATOM   277  N NZ    . LYS A 1 100 ? 85.267  83.627  102.683 1.00 71.15  ? 100 LYS A NZ    1 
ATOM   278  N N     . ASP A 1 101 ? 88.397  89.327  104.955 1.00 82.77  ? 101 ASP A N     1 
ATOM   279  C CA    . ASP A 1 101 ? 89.746  89.604  105.429 1.00 87.80  ? 101 ASP A CA    1 
ATOM   280  C C     . ASP A 1 101 ? 89.823  90.892  106.232 1.00 92.58  ? 101 ASP A C     1 
ATOM   281  O O     . ASP A 1 101 ? 90.754  91.056  107.029 1.00 97.90  ? 101 ASP A O     1 
ATOM   282  C CB    . ASP A 1 101 ? 90.709  89.672  104.243 1.00 92.14  ? 101 ASP A CB    1 
ATOM   283  C CG    . ASP A 1 101 ? 92.073  89.100  104.566 1.00 104.35 ? 101 ASP A CG    1 
ATOM   284  O OD1   . ASP A 1 101 ? 92.351  88.859  105.760 1.00 110.24 ? 101 ASP A OD1   1 
ATOM   285  O OD2   . ASP A 1 101 ? 92.866  88.890  103.626 1.00 103.40 ? 101 ASP A OD2   1 
ATOM   286  N N     . ALA A 1 102 ? 88.876  91.811  106.032 1.00 92.39  ? 102 ALA A N     1 
ATOM   287  C CA    . ALA A 1 102 ? 88.858  93.042  106.817 1.00 94.72  ? 102 ALA A CA    1 
ATOM   288  C C     . ALA A 1 102 ? 88.752  92.778  108.314 1.00 98.39  ? 102 ALA A C     1 
ATOM   289  O O     . ALA A 1 102 ? 89.181  93.619  109.111 1.00 100.91 ? 102 ALA A O     1 
ATOM   290  C CB    . ALA A 1 102 ? 87.704  93.937  106.368 1.00 94.25  ? 102 ALA A CB    1 
ATOM   291  N N     . HIS A 1 103 ? 88.190  91.635  108.713 1.00 104.40 ? 103 HIS A N     1 
ATOM   292  C CA    . HIS A 1 103 ? 88.084  91.312  110.133 1.00 108.32 ? 103 HIS A CA    1 
ATOM   293  C C     . HIS A 1 103 ? 89.444  91.023  110.755 1.00 109.61 ? 103 HIS A C     1 
ATOM   294  O O     . HIS A 1 103 ? 89.632  91.242  111.957 1.00 108.96 ? 103 HIS A O     1 
ATOM   295  C CB    . HIS A 1 103 ? 87.151  90.117  110.329 1.00 106.74 ? 103 HIS A CB    1 
ATOM   296  C CG    . HIS A 1 103 ? 86.751  89.891  111.753 1.00 111.84 ? 103 HIS A CG    1 
ATOM   297  N ND1   . HIS A 1 103 ? 85.806  90.663  112.393 1.00 118.16 ? 103 HIS A ND1   1 
ATOM   298  C CD2   . HIS A 1 103 ? 87.168  88.977  112.661 1.00 116.09 ? 103 HIS A CD2   1 
ATOM   299  C CE1   . HIS A 1 103 ? 85.659  90.235  113.634 1.00 121.37 ? 103 HIS A CE1   1 
ATOM   300  N NE2   . HIS A 1 103 ? 86.474  89.213  113.822 1.00 120.46 ? 103 HIS A NE2   1 
ATOM   301  N N     . ARG A 1 104 ? 90.398  90.532  109.962 1.00 111.71 ? 104 ARG A N     1 
ATOM   302  C CA    . ARG A 1 104 ? 91.705  90.165  110.494 1.00 113.84 ? 104 ARG A CA    1 
ATOM   303  C C     . ARG A 1 104 ? 92.506  91.370  110.973 1.00 114.35 ? 104 ARG A C     1 
ATOM   304  O O     . ARG A 1 104 ? 93.466  91.197  111.730 1.00 116.09 ? 104 ARG A O     1 
ATOM   305  C CB    . ARG A 1 104 ? 92.496  89.395  109.433 1.00 114.68 ? 104 ARG A CB    1 
ATOM   306  C CG    . ARG A 1 104 ? 93.645  88.566  109.980 1.00 118.84 ? 104 ARG A CG    1 
ATOM   307  C CD    . ARG A 1 104 ? 94.988  89.175  109.611 1.00 120.68 ? 104 ARG A CD    1 
ATOM   308  N NE    . ARG A 1 104 ? 95.307  88.983  108.202 1.00 125.64 ? 104 ARG A NE    1 
ATOM   309  C CZ    . ARG A 1 104 ? 95.861  87.887  107.702 1.00 130.88 ? 104 ARG A CZ    1 
ATOM   310  N NH1   . ARG A 1 104 ? 96.174  86.858  108.472 1.00 130.26 ? 104 ARG A NH1   1 
ATOM   311  N NH2   . ARG A 1 104 ? 96.108  87.821  106.397 1.00 128.35 ? 104 ARG A NH2   1 
ATOM   312  N N     . TYR A 1 105 ? 92.135  92.582  110.559 1.00 113.65 ? 105 TYR A N     1 
ATOM   313  C CA    . TYR A 1 105 ? 92.861  93.793  110.920 1.00 114.67 ? 105 TYR A CA    1 
ATOM   314  C C     . TYR A 1 105 ? 92.042  94.707  111.827 1.00 115.35 ? 105 TYR A C     1 
ATOM   315  O O     . TYR A 1 105 ? 92.200  95.929  111.792 1.00 114.15 ? 105 TYR A O     1 
ATOM   316  C CB    . TYR A 1 105 ? 93.305  94.542  109.665 1.00 108.36 ? 105 TYR A CB    1 
ATOM   317  C CG    . TYR A 1 105 ? 94.347  93.805  108.854 1.00 109.69 ? 105 TYR A CG    1 
ATOM   318  C CD1   . TYR A 1 105 ? 93.988  92.772  108.000 1.00 110.14 ? 105 TYR A CD1   1 
ATOM   319  C CD2   . TYR A 1 105 ? 95.690  94.139  108.947 1.00 110.38 ? 105 TYR A CD2   1 
ATOM   320  C CE1   . TYR A 1 105 ? 94.937  92.094  107.260 1.00 112.39 ? 105 TYR A CE1   1 
ATOM   321  C CE2   . TYR A 1 105 ? 96.646  93.467  108.211 1.00 112.50 ? 105 TYR A CE2   1 
ATOM   322  C CZ    . TYR A 1 105 ? 96.265  92.445  107.370 1.00 114.21 ? 105 TYR A CZ    1 
ATOM   323  O OH    . TYR A 1 105 ? 97.213  91.773  106.634 1.00 116.26 ? 105 TYR A OH    1 
ATOM   324  N N     . GLY A 1 106 ? 91.160  94.128  112.638 1.00 115.11 ? 106 GLY A N     1 
ATOM   325  C CA    . GLY A 1 106 ? 90.407  94.906  113.602 1.00 114.59 ? 106 GLY A CA    1 
ATOM   326  C C     . GLY A 1 106 ? 89.280  95.733  113.033 1.00 115.13 ? 106 GLY A C     1 
ATOM   327  O O     . GLY A 1 106 ? 88.683  96.525  113.768 1.00 116.06 ? 106 GLY A O     1 
ATOM   328  N N     . MET A 1 107 ? 88.965  95.578  111.753 1.00 114.82 ? 107 MET A N     1 
ATOM   329  C CA    . MET A 1 107 ? 87.901  96.328  111.105 1.00 111.64 ? 107 MET A CA    1 
ATOM   330  C C     . MET A 1 107 ? 86.766  95.387  110.721 1.00 111.42 ? 107 MET A C     1 
ATOM   331  O O     . MET A 1 107 ? 86.900  94.162  110.761 1.00 110.01 ? 107 MET A O     1 
ATOM   332  C CB    . MET A 1 107 ? 88.435  97.064  109.871 1.00 108.86 ? 107 MET A CB    1 
ATOM   333  C CG    . MET A 1 107 ? 88.428  98.575  110.000 1.00 109.32 ? 107 MET A CG    1 
ATOM   334  S SD    . MET A 1 107 ? 89.415  99.382  108.728 1.00 131.88 ? 107 MET A SD    1 
ATOM   335  C CE    . MET A 1 107 ? 91.065  98.900  109.227 1.00 126.19 ? 107 MET A CE    1 
ATOM   336  N N     . ARG A 1 108 ? 85.632  95.975  110.349 1.00 110.32 ? 108 ARG A N     1 
ATOM   337  C CA    . ARG A 1 108 ? 84.463  95.189  109.982 1.00 108.79 ? 108 ARG A CA    1 
ATOM   338  C C     . ARG A 1 108 ? 83.781  95.825  108.781 1.00 105.18 ? 108 ARG A C     1 
ATOM   339  O O     . ARG A 1 108 ? 83.602  97.045  108.735 1.00 105.47 ? 108 ARG A O     1 
ATOM   340  C CB    . ARG A 1 108 ? 83.480  95.069  111.151 1.00 110.67 ? 108 ARG A CB    1 
ATOM   341  C CG    . ARG A 1 108 ? 83.347  96.331  111.986 1.00 112.22 ? 108 ARG A CG    1 
ATOM   342  C CD    . ARG A 1 108 ? 82.447  96.099  113.189 1.00 111.54 ? 108 ARG A CD    1 
ATOM   343  N NE    . ARG A 1 108 ? 81.048  95.958  112.807 1.00 115.40 ? 108 ARG A NE    1 
ATOM   344  C CZ    . ARG A 1 108 ? 80.343  94.843  112.944 1.00 116.55 ? 108 ARG A CZ    1 
ATOM   345  N NH1   . ARG A 1 108 ? 80.881  93.742  113.443 1.00 112.89 ? 108 ARG A NH1   1 
ATOM   346  N NH2   . ARG A 1 108 ? 79.067  94.831  112.568 1.00 117.00 ? 108 ARG A NH2   1 
ATOM   347  N N     . GLY A 1 109 ? 83.402  94.992  107.819 1.00 99.06  ? 109 GLY A N     1 
ATOM   348  C CA    . GLY A 1 109 ? 82.731  95.474  106.625 1.00 97.08  ? 109 GLY A CA    1 
ATOM   349  C C     . GLY A 1 109 ? 82.208  94.317  105.808 1.00 87.60  ? 109 GLY A C     1 
ATOM   350  O O     . GLY A 1 109 ? 82.521  93.151  106.067 1.00 88.73  ? 109 GLY A O     1 
ATOM   351  N N     . MET A 1 110 ? 81.400  94.657  104.806 1.00 82.17  ? 110 MET A N     1 
ATOM   352  C CA    . MET A 1 110 ? 80.803  93.660  103.933 1.00 84.29  ? 110 MET A CA    1 
ATOM   353  C C     . MET A 1 110 ? 80.862  94.146  102.492 1.00 81.53  ? 110 MET A C     1 
ATOM   354  O O     . MET A 1 110 ? 80.975  95.344  102.222 1.00 85.51  ? 110 MET A O     1 
ATOM   355  C CB    . MET A 1 110 ? 79.352  93.345  104.331 1.00 94.46  ? 110 MET A CB    1 
ATOM   356  C CG    . MET A 1 110 ? 78.366  94.490  104.131 1.00 94.56  ? 110 MET A CG    1 
ATOM   357  S SD    . MET A 1 110 ? 76.646  94.053  104.441 1.00 84.66  ? 110 MET A SD    1 
ATOM   358  C CE    . MET A 1 110 ? 76.239  93.184  102.932 1.00 101.72 ? 110 MET A CE    1 
ATOM   359  N N     . SER A 1 111 ? 80.790  93.193  101.567 1.00 78.77  ? 111 SER A N     1 
ATOM   360  C CA    . SER A 1 111 ? 80.774  93.490  100.142 1.00 79.71  ? 111 SER A CA    1 
ATOM   361  C C     . SER A 1 111 ? 79.333  93.604  99.663  1.00 80.71  ? 111 SER A C     1 
ATOM   362  O O     . SER A 1 111 ? 78.518  92.711  99.914  1.00 81.60  ? 111 SER A O     1 
ATOM   363  C CB    . SER A 1 111 ? 81.509  92.406  99.355  1.00 75.88  ? 111 SER A CB    1 
ATOM   364  O OG    . SER A 1 111 ? 80.752  91.211  99.316  1.00 77.50  ? 111 SER A OG    1 
ATOM   365  N N     . ALA A 1 112 ? 79.026  94.698  98.973  1.00 85.80  ? 112 ALA A N     1 
ATOM   366  C CA    . ALA A 1 112 ? 77.671  94.996  98.536  1.00 89.87  ? 112 ALA A CA    1 
ATOM   367  C C     . ALA A 1 112 ? 77.639  95.218  97.031  1.00 93.78  ? 112 ALA A C     1 
ATOM   368  O O     . ALA A 1 112 ? 78.536  95.853  96.469  1.00 93.22  ? 112 ALA A O     1 
ATOM   369  C CB    . ALA A 1 112 ? 77.121  96.230  99.255  1.00 99.26  ? 112 ALA A CB    1 
ATOM   370  N N     . ASP A 1 113 ? 76.605  94.689  96.387  1.00 100.05 ? 113 ASP A N     1 
ATOM   371  C CA    . ASP A 1 113 ? 76.446  94.881  94.954  1.00 102.84 ? 113 ASP A CA    1 
ATOM   372  C C     . ASP A 1 113 ? 76.007  96.315  94.663  1.00 106.73 ? 113 ASP A C     1 
ATOM   373  O O     . ASP A 1 113 ? 75.100  96.835  95.320  1.00 111.31 ? 113 ASP A O     1 
ATOM   374  C CB    . ASP A 1 113 ? 75.428  93.894  94.391  1.00 103.74 ? 113 ASP A CB    1 
ATOM   375  C CG    . ASP A 1 113 ? 75.244  94.036  92.898  1.00 112.66 ? 113 ASP A CG    1 
ATOM   376  O OD1   . ASP A 1 113 ? 76.208  93.774  92.149  1.00 115.65 ? 113 ASP A OD1   1 
ATOM   377  O OD2   . ASP A 1 113 ? 74.131  94.404  92.473  1.00 117.59 ? 113 ASP A OD2   1 
ATOM   378  N N     . PRO A 1 114 ? 76.621  96.976  93.678  1.00 104.43 ? 114 PRO A N     1 
ATOM   379  C CA    . PRO A 1 114 ? 76.325  98.395  93.439  1.00 106.48 ? 114 PRO A CA    1 
ATOM   380  C C     . PRO A 1 114 ? 75.025  98.657  92.698  1.00 110.49 ? 114 PRO A C     1 
ATOM   381  O O     . PRO A 1 114 ? 74.656  99.829  92.542  1.00 116.18 ? 114 PRO A O     1 
ATOM   382  C CB    . PRO A 1 114 ? 77.526  98.858  92.605  1.00 100.51 ? 114 PRO A CB    1 
ATOM   383  C CG    . PRO A 1 114 ? 77.949  97.636  91.872  1.00 99.08  ? 114 PRO A CG    1 
ATOM   384  C CD    . PRO A 1 114 ? 77.689  96.477  92.796  1.00 100.32 ? 114 PRO A CD    1 
ATOM   385  N N     . GLU A 1 115 ? 74.322  97.625  92.229  1.00 107.74 ? 115 GLU A N     1 
ATOM   386  C CA    . GLU A 1 115 ? 73.121  97.870  91.436  1.00 111.96 ? 115 GLU A CA    1 
ATOM   387  C C     . GLU A 1 115 ? 71.973  98.376  92.301  1.00 115.75 ? 115 GLU A C     1 
ATOM   388  O O     . GLU A 1 115 ? 71.280  99.327  91.922  1.00 118.29 ? 115 GLU A O     1 
ATOM   389  C CB    . GLU A 1 115 ? 72.712  96.602  90.687  1.00 114.69 ? 115 GLU A CB    1 
ATOM   390  C CG    . GLU A 1 115 ? 71.508  96.778  89.774  1.00 117.94 ? 115 GLU A CG    1 
ATOM   391  C CD    . GLU A 1 115 ? 71.161  95.515  89.012  1.00 119.78 ? 115 GLU A CD    1 
ATOM   392  O OE1   . GLU A 1 115 ? 71.837  94.486  89.223  1.00 120.69 ? 115 GLU A OE1   1 
ATOM   393  O OE2   . GLU A 1 115 ? 70.213  95.551  88.200  1.00 117.72 ? 115 GLU A OE2   1 
ATOM   394  N N     . GLU A 1 116 ? 71.755  97.763  93.465  1.00 114.06 ? 116 GLU A N     1 
ATOM   395  C CA    . GLU A 1 116 ? 70.618  98.134  94.298  1.00 115.52 ? 116 GLU A CA    1 
ATOM   396  C C     . GLU A 1 116 ? 70.887  99.347  95.179  1.00 115.54 ? 116 GLU A C     1 
ATOM   397  O O     . GLU A 1 116 ? 69.956  99.834  95.829  1.00 116.20 ? 116 GLU A O     1 
ATOM   398  C CB    . GLU A 1 116 ? 70.193  96.957  95.179  1.00 117.49 ? 116 GLU A CB    1 
ATOM   399  C CG    . GLU A 1 116 ? 70.352  95.597  94.528  1.00 119.27 ? 116 GLU A CG    1 
ATOM   400  C CD    . GLU A 1 116 ? 71.475  94.793  95.145  1.00 116.52 ? 116 GLU A CD    1 
ATOM   401  O OE1   . GLU A 1 116 ? 72.490  95.399  95.546  1.00 115.80 ? 116 GLU A OE1   1 
ATOM   402  O OE2   . GLU A 1 116 ? 71.341  93.554  95.231  1.00 114.14 ? 116 GLU A OE2   1 
ATOM   403  N N     . TYR A 1 117 ? 72.120  99.842  95.222  1.00 115.15 ? 117 TYR A N     1 
ATOM   404  C CA    . TYR A 1 117 ? 72.473  101.006 96.022  1.00 118.34 ? 117 TYR A CA    1 
ATOM   405  C C     . TYR A 1 117 ? 72.969  102.115 95.109  1.00 122.22 ? 117 TYR A C     1 
ATOM   406  O O     . TYR A 1 117 ? 73.851  101.886 94.274  1.00 121.48 ? 117 TYR A O     1 
ATOM   407  C CB    . TYR A 1 117 ? 73.552  100.667 97.055  1.00 117.14 ? 117 TYR A CB    1 
ATOM   408  C CG    . TYR A 1 117 ? 73.240  99.467  97.914  1.00 117.50 ? 117 TYR A CG    1 
ATOM   409  C CD1   . TYR A 1 117 ? 72.111  99.442  98.722  1.00 119.55 ? 117 TYR A CD1   1 
ATOM   410  C CD2   . TYR A 1 117 ? 74.079  98.362  97.926  1.00 112.55 ? 117 TYR A CD2   1 
ATOM   411  C CE1   . TYR A 1 117 ? 71.825  98.348  99.512  1.00 117.08 ? 117 TYR A CE1   1 
ATOM   412  C CE2   . TYR A 1 117 ? 73.800  97.265  98.713  1.00 111.33 ? 117 TYR A CE2   1 
ATOM   413  C CZ    . TYR A 1 117 ? 72.673  97.263  99.503  1.00 114.77 ? 117 TYR A CZ    1 
ATOM   414  O OH    . TYR A 1 117 ? 72.392  96.170  100.289 1.00 118.79 ? 117 TYR A OH    1 
ATOM   415  N N     . ASP A 1 118 ? 72.410  103.310 95.268  1.00 125.23 ? 118 ASP A N     1 
ATOM   416  C CA    . ASP A 1 118 ? 72.938  104.460 94.554  1.00 124.76 ? 118 ASP A CA    1 
ATOM   417  C C     . ASP A 1 118 ? 74.311  104.840 95.099  1.00 127.15 ? 118 ASP A C     1 
ATOM   418  O O     . ASP A 1 118 ? 74.668  104.512 96.234  1.00 131.60 ? 118 ASP A O     1 
ATOM   419  C CB    . ASP A 1 118 ? 71.935  105.629 94.597  1.00 128.81 ? 118 ASP A CB    1 
ATOM   420  C CG    . ASP A 1 118 ? 71.916  106.397 95.929  1.00 132.78 ? 118 ASP A CG    1 
ATOM   421  O OD1   . ASP A 1 118 ? 72.698  106.124 96.861  1.00 133.69 ? 118 ASP A OD1   1 
ATOM   422  O OD2   . ASP A 1 118 ? 71.075  107.315 96.039  1.00 132.45 ? 118 ASP A OD2   1 
ATOM   423  N N     . LEU A 1 119 ? 75.103  105.499 94.261  1.00 124.70 ? 119 LEU A N     1 
ATOM   424  C CA    . LEU A 1 119 ? 76.463  105.862 94.632  1.00 124.25 ? 119 LEU A CA    1 
ATOM   425  C C     . LEU A 1 119 ? 76.567  107.276 95.185  1.00 123.75 ? 119 LEU A C     1 
ATOM   426  O O     . LEU A 1 119 ? 77.676  107.724 95.494  1.00 121.23 ? 119 LEU A O     1 
ATOM   427  C CB    . LEU A 1 119 ? 77.402  105.698 93.434  1.00 121.19 ? 119 LEU A CB    1 
ATOM   428  C CG    . LEU A 1 119 ? 77.943  104.286 93.183  1.00 113.10 ? 119 LEU A CG    1 
ATOM   429  C CD1   . LEU A 1 119 ? 78.614  103.733 94.431  1.00 105.50 ? 119 LEU A CD1   1 
ATOM   430  C CD2   . LEU A 1 119 ? 76.860  103.338 92.686  1.00 113.16 ? 119 LEU A CD2   1 
ATOM   431  N N     . ALA A 1 120 ? 75.445  107.985 95.320  1.00 125.36 ? 120 ALA A N     1 
ATOM   432  C CA    . ALA A 1 120 ? 75.454  109.296 95.953  1.00 126.54 ? 120 ALA A CA    1 
ATOM   433  C C     . ALA A 1 120 ? 75.758  109.223 97.442  1.00 125.78 ? 120 ALA A C     1 
ATOM   434  O O     . ALA A 1 120 ? 76.015  110.264 98.056  1.00 127.64 ? 120 ALA A O     1 
ATOM   435  C CB    . ALA A 1 120 ? 74.112  109.995 95.732  1.00 125.97 ? 120 ALA A CB    1 
ATOM   436  N N     . ASP A 1 121 ? 75.737  108.029 98.031  1.00 122.77 ? 121 ASP A N     1 
ATOM   437  C CA    . ASP A 1 121 ? 76.044  107.851 99.443  1.00 126.08 ? 121 ASP A CA    1 
ATOM   438  C C     . ASP A 1 121 ? 77.535  107.931 99.738  1.00 125.58 ? 121 ASP A C     1 
ATOM   439  O O     . ASP A 1 121 ? 77.923  107.887 100.910 1.00 127.80 ? 121 ASP A O     1 
ATOM   440  C CB    . ASP A 1 121 ? 75.490  106.513 99.936  1.00 129.88 ? 121 ASP A CB    1 
ATOM   441  C CG    . ASP A 1 121 ? 73.976  106.503 100.011 1.00 134.07 ? 121 ASP A CG    1 
ATOM   442  O OD1   . ASP A 1 121 ? 73.374  107.597 100.032 1.00 134.37 ? 121 ASP A OD1   1 
ATOM   443  O OD2   . ASP A 1 121 ? 73.389  105.401 100.052 1.00 136.41 ? 121 ASP A OD2   1 
ATOM   444  N N     . LEU A 1 122 ? 78.381  108.035 98.712  1.00 122.00 ? 122 LEU A N     1 
ATOM   445  C CA    . LEU A 1 122 ? 79.797  108.276 98.955  1.00 120.30 ? 122 LEU A CA    1 
ATOM   446  C C     . LEU A 1 122 ? 80.034  109.622 99.626  1.00 121.98 ? 122 LEU A C     1 
ATOM   447  O O     . LEU A 1 122 ? 81.084  109.818 100.245 1.00 119.34 ? 122 LEU A O     1 
ATOM   448  C CB    . LEU A 1 122 ? 80.580  108.190 97.645  1.00 114.80 ? 122 LEU A CB    1 
ATOM   449  C CG    . LEU A 1 122 ? 81.176  106.822 97.304  1.00 107.94 ? 122 LEU A CG    1 
ATOM   450  C CD1   . LEU A 1 122 ? 80.079  105.813 97.023  1.00 108.25 ? 122 LEU A CD1   1 
ATOM   451  C CD2   . LEU A 1 122 ? 82.123  106.926 96.121  1.00 108.54 ? 122 LEU A CD2   1 
ATOM   452  N N     . SER A 1 123 ? 79.084  110.554 99.509  1.00 124.86 ? 123 SER A N     1 
ATOM   453  C CA    . SER A 1 123 ? 79.179  111.811 100.243 1.00 123.24 ? 123 SER A CA    1 
ATOM   454  C C     . SER A 1 123 ? 78.994  111.599 101.739 1.00 123.55 ? 123 SER A C     1 
ATOM   455  O O     . SER A 1 123 ? 79.672  112.244 102.546 1.00 122.92 ? 123 SER A O     1 
ATOM   456  C CB    . SER A 1 123 ? 78.146  112.806 99.716  1.00 120.96 ? 123 SER A CB    1 
ATOM   457  O OG    . SER A 1 123 ? 76.864  112.210 99.631  1.00 123.50 ? 123 SER A OG    1 
ATOM   458  N N     . SER A 1 124 ? 78.076  110.713 102.128 1.00 123.24 ? 124 SER A N     1 
ATOM   459  C CA    . SER A 1 124 ? 77.875  110.386 103.534 1.00 123.17 ? 124 SER A CA    1 
ATOM   460  C C     . SER A 1 124 ? 78.869  109.352 104.044 1.00 122.81 ? 124 SER A C     1 
ATOM   461  O O     . SER A 1 124 ? 78.954  109.145 105.259 1.00 125.35 ? 124 SER A O     1 
ATOM   462  C CB    . SER A 1 124 ? 76.449  109.878 103.757 1.00 121.58 ? 124 SER A CB    1 
ATOM   463  O OG    . SER A 1 124 ? 75.502  110.910 103.544 1.00 122.78 ? 124 SER A OG    1 
ATOM   464  N N     . LEU A 1 125 ? 79.597  108.693 103.146 1.00 120.97 ? 125 LEU A N     1 
ATOM   465  C CA    . LEU A 1 125 ? 80.586  107.703 103.568 1.00 121.72 ? 125 LEU A CA    1 
ATOM   466  C C     . LEU A 1 125 ? 81.628  108.259 104.538 1.00 122.86 ? 125 LEU A C     1 
ATOM   467  O O     . LEU A 1 125 ? 81.933  107.565 105.524 1.00 122.74 ? 125 LEU A O     1 
ATOM   468  C CB    . LEU A 1 125 ? 81.234  107.086 102.316 1.00 121.29 ? 125 LEU A CB    1 
ATOM   469  C CG    . LEU A 1 125 ? 82.161  105.859 102.292 1.00 114.00 ? 125 LEU A CG    1 
ATOM   470  C CD1   . LEU A 1 125 ? 82.575  105.590 100.856 1.00 111.38 ? 125 LEU A CD1   1 
ATOM   471  C CD2   . LEU A 1 125 ? 83.409  105.985 103.155 1.00 106.56 ? 125 LEU A CD2   1 
ATOM   472  N N     . PRO A 1 126 ? 82.205  109.453 104.344 1.00 123.11 ? 126 PRO A N     1 
ATOM   473  C CA    . PRO A 1 126 ? 83.191  109.947 105.324 1.00 122.98 ? 126 PRO A CA    1 
ATOM   474  C C     . PRO A 1 126 ? 82.625  110.173 106.716 1.00 122.70 ? 126 PRO A C     1 
ATOM   475  O O     . PRO A 1 126 ? 83.406  110.280 107.670 1.00 119.99 ? 126 PRO A O     1 
ATOM   476  C CB    . PRO A 1 126 ? 83.680  111.262 104.702 1.00 122.62 ? 126 PRO A CB    1 
ATOM   477  C CG    . PRO A 1 126 ? 83.413  111.114 103.255 1.00 123.45 ? 126 PRO A CG    1 
ATOM   478  C CD    . PRO A 1 126 ? 82.138  110.338 103.168 1.00 121.36 ? 126 PRO A CD    1 
ATOM   479  N N     . GLU A 1 127 ? 81.300  110.256 106.868 1.00 124.95 ? 127 GLU A N     1 
ATOM   480  C CA    . GLU A 1 127 ? 80.713  110.436 108.192 1.00 123.20 ? 127 GLU A CA    1 
ATOM   481  C C     . GLU A 1 127 ? 81.002  109.264 109.120 1.00 124.58 ? 127 GLU A C     1 
ATOM   482  O O     . GLU A 1 127 ? 80.861  109.405 110.339 1.00 125.92 ? 127 GLU A O     1 
ATOM   483  C CB    . GLU A 1 127 ? 79.203  110.650 108.072 1.00 123.40 ? 127 GLU A CB    1 
ATOM   484  C CG    . GLU A 1 127 ? 78.791  112.082 107.751 1.00 123.51 ? 127 GLU A CG    1 
ATOM   485  C CD    . GLU A 1 127 ? 78.873  112.411 106.271 1.00 126.71 ? 127 GLU A CD    1 
ATOM   486  O OE1   . GLU A 1 127 ? 79.802  111.924 105.593 1.00 125.36 ? 127 GLU A OE1   1 
ATOM   487  O OE2   . GLU A 1 127 ? 78.001  113.161 105.783 1.00 130.19 ? 127 GLU A OE2   1 
ATOM   488  N N     . ILE A 1 128 ? 81.398  108.118 108.577 1.00 125.47 ? 128 ILE A N     1 
ATOM   489  C CA    . ILE A 1 128 ? 81.820  106.979 109.382 1.00 123.77 ? 128 ILE A CA    1 
ATOM   490  C C     . ILE A 1 128 ? 83.310  107.114 109.660 1.00 120.91 ? 128 ILE A C     1 
ATOM   491  O O     . ILE A 1 128 ? 84.115  107.252 108.731 1.00 118.43 ? 128 ILE A O     1 
ATOM   492  C CB    . ILE A 1 128 ? 81.508  105.653 108.669 1.00 119.05 ? 128 ILE A CB    1 
ATOM   493  C CG1   . ILE A 1 128 ? 80.001  105.388 108.667 1.00 116.88 ? 128 ILE A CG1   1 
ATOM   494  C CG2   . ILE A 1 128 ? 82.252  104.503 109.330 1.00 113.70 ? 128 ILE A CG2   1 
ATOM   495  C CD1   . ILE A 1 128 ? 79.380  105.372 110.047 1.00 116.17 ? 128 ILE A CD1   1 
ATOM   496  N N     . ASP A 1 129 ? 83.679  107.089 110.936 1.00 121.06 ? 129 ASP A N     1 
ATOM   497  C CA    . ASP A 1 129 ? 85.081  107.193 111.307 1.00 122.46 ? 129 ASP A CA    1 
ATOM   498  C C     . ASP A 1 129 ? 85.832  105.926 110.916 1.00 117.82 ? 129 ASP A C     1 
ATOM   499  O O     . ASP A 1 129 ? 85.293  104.817 110.968 1.00 114.82 ? 129 ASP A O     1 
ATOM   500  C CB    . ASP A 1 129 ? 85.221  107.443 112.809 1.00 126.18 ? 129 ASP A CB    1 
ATOM   501  C CG    . ASP A 1 129 ? 86.628  107.848 113.204 1.00 125.62 ? 129 ASP A CG    1 
ATOM   502  O OD1   . ASP A 1 129 ? 87.426  108.187 112.305 1.00 124.78 ? 129 ASP A OD1   1 
ATOM   503  O OD2   . ASP A 1 129 ? 86.936  107.827 114.414 1.00 125.72 ? 129 ASP A OD2   1 
ATOM   504  N N     . LYS A 1 130 ? 87.095  106.105 110.520 1.00 116.93 ? 130 LYS A N     1 
ATOM   505  C CA    . LYS A 1 130 ? 87.968  104.996 110.135 1.00 114.13 ? 130 LYS A CA    1 
ATOM   506  C C     . LYS A 1 130 ? 87.354  104.180 108.998 1.00 113.29 ? 130 LYS A C     1 
ATOM   507  O O     . LYS A 1 130 ? 87.376  102.948 109.009 1.00 115.28 ? 130 LYS A O     1 
ATOM   508  C CB    . LYS A 1 130 ? 88.285  104.108 111.342 1.00 115.82 ? 130 LYS A CB    1 
ATOM   509  C CG    . LYS A 1 130 ? 89.580  103.323 111.236 1.00 116.59 ? 130 LYS A CG    1 
ATOM   510  C CD    . LYS A 1 130 ? 90.294  103.246 112.575 1.00 118.97 ? 130 LYS A CD    1 
ATOM   511  C CE    . LYS A 1 130 ? 91.802  103.187 112.391 1.00 119.41 ? 130 LYS A CE    1 
ATOM   512  N NZ    . LYS A 1 130 ? 92.505  102.806 113.648 1.00 116.73 ? 130 LYS A NZ    1 
ATOM   513  N N     . SER A 1 131 ? 86.798  104.873 108.010 1.00 110.48 ? 131 SER A N     1 
ATOM   514  C CA    . SER A 1 131 ? 86.074  104.242 106.917 1.00 107.78 ? 131 SER A CA    1 
ATOM   515  C C     . SER A 1 131 ? 86.948  104.113 105.674 1.00 102.35 ? 131 SER A C     1 
ATOM   516  O O     . SER A 1 131 ? 87.998  104.747 105.549 1.00 102.62 ? 131 SER A O     1 
ATOM   517  C CB    . SER A 1 131 ? 84.810  105.034 106.579 1.00 110.76 ? 131 SER A CB    1 
ATOM   518  O OG    . SER A 1 131 ? 85.132  106.229 105.890 1.00 111.95 ? 131 SER A OG    1 
ATOM   519  N N     . LEU A 1 132 ? 86.487  103.275 104.748 1.00 99.68  ? 132 LEU A N     1 
ATOM   520  C CA    . LEU A 1 132 ? 87.181  103.023 103.493 1.00 92.43  ? 132 LEU A CA    1 
ATOM   521  C C     . LEU A 1 132 ? 86.200  102.373 102.529 1.00 88.92  ? 132 LEU A C     1 
ATOM   522  O O     . LEU A 1 132 ? 85.225  101.742 102.944 1.00 95.07  ? 132 LEU A O     1 
ATOM   523  C CB    . LEU A 1 132 ? 88.412  102.133 103.707 1.00 90.06  ? 132 LEU A CB    1 
ATOM   524  C CG    . LEU A 1 132 ? 89.288  101.785 102.502 1.00 87.14  ? 132 LEU A CG    1 
ATOM   525  C CD1   . LEU A 1 132 ? 89.908  103.036 101.911 1.00 95.89  ? 132 LEU A CD1   1 
ATOM   526  C CD2   . LEU A 1 132 ? 90.362  100.785 102.892 1.00 79.49  ? 132 LEU A CD2   1 
ATOM   527  N N     . VAL A 1 133 ? 86.462  102.543 101.235 1.00 85.54  ? 133 VAL A N     1 
ATOM   528  C CA    . VAL A 1 133 ? 85.696  101.883 100.186 1.00 86.63  ? 133 VAL A CA    1 
ATOM   529  C C     . VAL A 1 133 ? 86.670  101.305 99.168  1.00 83.92  ? 133 VAL A C     1 
ATOM   530  O O     . VAL A 1 133 ? 87.711  101.904 98.879  1.00 88.38  ? 133 VAL A O     1 
ATOM   531  C CB    . VAL A 1 133 ? 84.683  102.840 99.518  1.00 85.71  ? 133 VAL A CB    1 
ATOM   532  C CG1   . VAL A 1 133 ? 85.385  103.898 98.688  1.00 87.79  ? 133 VAL A CG1   1 
ATOM   533  C CG2   . VAL A 1 133 ? 83.695  102.061 98.668  1.00 85.75  ? 133 VAL A CG2   1 
ATOM   534  N N     . VAL A 1 134 ? 86.354  100.117 98.659  1.00 77.28  ? 134 VAL A N     1 
ATOM   535  C CA    . VAL A 1 134 ? 87.202  99.412  97.706  1.00 76.64  ? 134 VAL A CA    1 
ATOM   536  C C     . VAL A 1 134 ? 86.348  99.011  96.512  1.00 80.89  ? 134 VAL A C     1 
ATOM   537  O O     . VAL A 1 134 ? 85.183  98.632  96.672  1.00 85.12  ? 134 VAL A O     1 
ATOM   538  C CB    . VAL A 1 134 ? 87.870  98.174  98.343  1.00 74.08  ? 134 VAL A CB    1 
ATOM   539  C CG1   . VAL A 1 134 ? 88.798  97.493  97.352  1.00 73.61  ? 134 VAL A CG1   1 
ATOM   540  C CG2   . VAL A 1 134 ? 88.628  98.564  99.601  1.00 74.51  ? 134 VAL A CG2   1 
ATOM   541  N N     . PHE A 1 135 ? 86.919  99.111  95.315  1.00 81.78  ? 135 PHE A N     1 
ATOM   542  C CA    . PHE A 1 135 ? 86.220  98.774  94.083  1.00 80.32  ? 135 PHE A CA    1 
ATOM   543  C C     . PHE A 1 135 ? 86.964  97.658  93.365  1.00 79.90  ? 135 PHE A C     1 
ATOM   544  O O     . PHE A 1 135 ? 88.174  97.760  93.137  1.00 84.14  ? 135 PHE A O     1 
ATOM   545  C CB    . PHE A 1 135 ? 86.088  99.997  93.170  1.00 82.39  ? 135 PHE A CB    1 
ATOM   546  C CG    . PHE A 1 135 ? 85.153  101.050 93.695  1.00 84.30  ? 135 PHE A CG    1 
ATOM   547  C CD1   . PHE A 1 135 ? 85.523  101.863 94.753  1.00 85.30  ? 135 PHE A CD1   1 
ATOM   548  C CD2   . PHE A 1 135 ? 83.903  101.227 93.131  1.00 88.80  ? 135 PHE A CD2   1 
ATOM   549  C CE1   . PHE A 1 135 ? 84.664  102.830 95.235  1.00 87.40  ? 135 PHE A CE1   1 
ATOM   550  C CE2   . PHE A 1 135 ? 83.041  102.192 93.610  1.00 89.71  ? 135 PHE A CE2   1 
ATOM   551  C CZ    . PHE A 1 135 ? 83.422  102.994 94.662  1.00 91.33  ? 135 PHE A CZ    1 
ATOM   552  N N     . CYS A 1 136 ? 86.240  96.595  93.014  1.00 79.46  ? 136 CYS A N     1 
ATOM   553  C CA    . CYS A 1 136 ? 86.778  95.463  92.259  1.00 79.46  ? 136 CYS A CA    1 
ATOM   554  C C     . CYS A 1 136 ? 85.875  95.268  91.045  1.00 84.98  ? 136 CYS A C     1 
ATOM   555  O O     . CYS A 1 136 ? 84.870  94.558  91.120  1.00 89.11  ? 136 CYS A O     1 
ATOM   556  C CB    . CYS A 1 136 ? 86.851  94.205  93.119  1.00 77.73  ? 136 CYS A CB    1 
ATOM   557  S SG    . CYS A 1 136 ? 88.024  94.298  94.488  1.00 92.32  ? 136 CYS A SG    1 
ATOM   558  N N     . MET A 1 137 ? 86.237  95.889  89.926  1.00 79.50  ? 137 MET A N     1 
ATOM   559  C CA    . MET A 1 137 ? 85.382  95.928  88.750  1.00 83.08  ? 137 MET A CA    1 
ATOM   560  C C     . MET A 1 137 ? 86.089  95.340  87.537  1.00 85.98  ? 137 MET A C     1 
ATOM   561  O O     . MET A 1 137 ? 87.315  95.410  87.411  1.00 84.94  ? 137 MET A O     1 
ATOM   562  C CB    . MET A 1 137 ? 84.935  97.361  88.443  1.00 86.22  ? 137 MET A CB    1 
ATOM   563  C CG    . MET A 1 137 ? 84.380  98.096  89.646  1.00 85.45  ? 137 MET A CG    1 
ATOM   564  S SD    . MET A 1 137 ? 82.634  97.728  89.897  1.00 101.42 ? 137 MET A SD    1 
ATOM   565  C CE    . MET A 1 137 ? 82.152  99.069  90.975  1.00 100.02 ? 137 MET A CE    1 
ATOM   566  N N     . ALA A 1 138 ? 85.292  94.753  86.650  1.00 87.60  ? 138 ALA A N     1 
ATOM   567  C CA    . ALA A 1 138 ? 85.737  94.204  85.377  1.00 92.30  ? 138 ALA A CA    1 
ATOM   568  C C     . ALA A 1 138 ? 85.029  94.948  84.245  1.00 102.51 ? 138 ALA A C     1 
ATOM   569  O O     . ALA A 1 138 ? 84.333  95.942  84.468  1.00 106.14 ? 138 ALA A O     1 
ATOM   570  C CB    . ALA A 1 138 ? 85.475  92.698  85.319  1.00 94.77  ? 138 ALA A CB    1 
ATOM   571  N N     . THR A 1 139 ? 85.210  94.459  83.020  1.00 109.71 ? 139 THR A N     1 
ATOM   572  C CA    . THR A 1 139 ? 84.587  95.085  81.862  1.00 112.12 ? 139 THR A CA    1 
ATOM   573  C C     . THR A 1 139 ? 84.447  94.061  80.745  1.00 111.13 ? 139 THR A C     1 
ATOM   574  O O     . THR A 1 139 ? 85.100  93.014  80.752  1.00 111.75 ? 139 THR A O     1 
ATOM   575  C CB    . THR A 1 139 ? 85.389  96.297  81.381  1.00 111.93 ? 139 THR A CB    1 
ATOM   576  O OG1   . THR A 1 139 ? 84.950  96.672  80.070  1.00 118.36 ? 139 THR A OG1   1 
ATOM   577  C CG2   . THR A 1 139 ? 86.872  95.972  81.346  1.00 109.67 ? 139 THR A CG2   1 
ATOM   578  N N     . TYR A 1 140 ? 83.583  94.382  79.783  1.00 113.15 ? 140 TYR A N     1 
ATOM   579  C CA    . TYR A 1 140 ? 83.338  93.523  78.634  1.00 116.34 ? 140 TYR A CA    1 
ATOM   580  C C     . TYR A 1 140 ? 83.257  94.361  77.366  1.00 119.47 ? 140 TYR A C     1 
ATOM   581  O O     . TYR A 1 140 ? 83.053  95.577  77.409  1.00 121.88 ? 140 TYR A O     1 
ATOM   582  C CB    . TYR A 1 140 ? 82.051  92.700  78.789  1.00 115.62 ? 140 TYR A CB    1 
ATOM   583  C CG    . TYR A 1 140 ? 82.046  91.764  79.973  1.00 116.49 ? 140 TYR A CG    1 
ATOM   584  C CD1   . TYR A 1 140 ? 82.972  90.735  80.071  1.00 118.98 ? 140 TYR A CD1   1 
ATOM   585  C CD2   . TYR A 1 140 ? 81.101  91.893  80.981  1.00 113.40 ? 140 TYR A CD2   1 
ATOM   586  C CE1   . TYR A 1 140 ? 82.969  89.870  81.146  1.00 117.16 ? 140 TYR A CE1   1 
ATOM   587  C CE2   . TYR A 1 140 ? 81.090  91.031  82.060  1.00 114.10 ? 140 TYR A CE2   1 
ATOM   588  C CZ    . TYR A 1 140 ? 82.026  90.022  82.137  1.00 112.88 ? 140 TYR A CZ    1 
ATOM   589  O OH    . TYR A 1 140 ? 82.020  89.160  83.209  1.00 104.59 ? 140 TYR A OH    1 
ATOM   590  N N     . GLY A 1 141 ? 83.423  93.687  76.231  1.00 119.71 ? 141 GLY A N     1 
ATOM   591  C CA    . GLY A 1 141 ? 83.262  94.351  74.944  1.00 122.83 ? 141 GLY A CA    1 
ATOM   592  C C     . GLY A 1 141 ? 84.402  95.308  74.659  1.00 123.19 ? 141 GLY A C     1 
ATOM   593  O O     . GLY A 1 141 ? 85.580  94.970  74.810  1.00 122.36 ? 141 GLY A O     1 
ATOM   594  N N     . GLU A 1 142 ? 84.055  96.510  74.212  1.00 124.89 ? 142 GLU A N     1 
ATOM   595  C CA    . GLU A 1 142 ? 85.038  97.568  73.978  1.00 127.35 ? 142 GLU A CA    1 
ATOM   596  C C     . GLU A 1 142 ? 85.120  98.492  75.192  1.00 127.77 ? 142 GLU A C     1 
ATOM   597  O O     . GLU A 1 142 ? 84.903  99.702  75.115  1.00 130.28 ? 142 GLU A O     1 
ATOM   598  C CB    . GLU A 1 142 ? 84.694  98.339  72.705  1.00 129.81 ? 142 GLU A CB    1 
ATOM   599  C CG    . GLU A 1 142 ? 83.244  98.794  72.604  1.00 131.24 ? 142 GLU A CG    1 
ATOM   600  C CD    . GLU A 1 142 ? 82.352  97.762  71.942  1.00 131.70 ? 142 GLU A CD    1 
ATOM   601  O OE1   . GLU A 1 142 ? 82.854  96.670  71.603  1.00 132.63 ? 142 GLU A OE1   1 
ATOM   602  O OE2   . GLU A 1 142 ? 81.148  98.043  71.762  1.00 133.14 ? 142 GLU A OE2   1 
ATOM   603  N N     . GLY A 1 143 ? 85.452  97.894  76.333  1.00 123.21 ? 143 GLY A N     1 
ATOM   604  C CA    . GLY A 1 143 ? 85.484  98.642  77.573  1.00 119.72 ? 143 GLY A CA    1 
ATOM   605  C C     . GLY A 1 143 ? 84.122  98.949  78.148  1.00 120.21 ? 143 GLY A C     1 
ATOM   606  O O     . GLY A 1 143 ? 84.007  99.813  79.020  1.00 114.34 ? 143 GLY A O     1 
ATOM   607  N N     . ASP A 1 144 ? 83.083  98.263  77.681  1.00 122.97 ? 144 ASP A N     1 
ATOM   608  C CA    . ASP A 1 144 ? 81.739  98.519  78.166  1.00 124.07 ? 144 ASP A CA    1 
ATOM   609  C C     . ASP A 1 144 ? 81.572  97.998  79.593  1.00 125.22 ? 144 ASP A C     1 
ATOM   610  O O     . ASP A 1 144 ? 82.237  97.042  79.998  1.00 123.37 ? 144 ASP A O     1 
ATOM   611  C CB    . ASP A 1 144 ? 80.707  97.865  77.250  1.00 122.67 ? 144 ASP A CB    1 
ATOM   612  C CG    . ASP A 1 144 ? 80.596  98.559  75.910  1.00 124.46 ? 144 ASP A CG    1 
ATOM   613  O OD1   . ASP A 1 144 ? 81.094  99.697  75.784  1.00 126.39 ? 144 ASP A OD1   1 
ATOM   614  O OD2   . ASP A 1 144 ? 80.013  97.966  74.978  1.00 126.80 ? 144 ASP A OD2   1 
ATOM   615  N N     . PRO A 1 145 ? 80.693  98.617  80.375  1.00 123.59 ? 145 PRO A N     1 
ATOM   616  C CA    . PRO A 1 145 ? 80.451  98.139  81.738  1.00 116.46 ? 145 PRO A CA    1 
ATOM   617  C C     . PRO A 1 145 ? 79.673  96.834  81.745  1.00 118.83 ? 145 PRO A C     1 
ATOM   618  O O     . PRO A 1 145 ? 79.011  96.460  80.774  1.00 121.42 ? 145 PRO A O     1 
ATOM   619  C CB    . PRO A 1 145 ? 79.629  99.266  82.377  1.00 115.27 ? 145 PRO A CB    1 
ATOM   620  C CG    . PRO A 1 145 ? 79.738  100.424 81.432  1.00 119.20 ? 145 PRO A CG    1 
ATOM   621  C CD    . PRO A 1 145 ? 79.927  99.836  80.081  1.00 121.11 ? 145 PRO A CD    1 
ATOM   622  N N     . THR A 1 146 ? 79.763  96.139  82.874  1.00 117.95 ? 146 THR A N     1 
ATOM   623  C CA    . THR A 1 146 ? 78.928  94.974  83.100  1.00 110.68 ? 146 THR A CA    1 
ATOM   624  C C     . THR A 1 146 ? 77.498  95.413  83.410  1.00 111.21 ? 146 THR A C     1 
ATOM   625  O O     . THR A 1 146 ? 77.213  96.596  83.621  1.00 116.12 ? 146 THR A O     1 
ATOM   626  C CB    . THR A 1 146 ? 79.495  94.124  84.234  1.00 101.56 ? 146 THR A CB    1 
ATOM   627  O OG1   . THR A 1 146 ? 79.186  94.735  85.492  1.00 103.86 ? 146 THR A OG1   1 
ATOM   628  C CG2   . THR A 1 146 ? 81.003  94.003  84.089  1.00 99.26  ? 146 THR A CG2   1 
ATOM   629  N N     . ASP A 1 147 ? 76.586  94.438  83.428  1.00 106.03 ? 147 ASP A N     1 
ATOM   630  C CA    . ASP A 1 147 ? 75.170  94.757  83.582  1.00 110.57 ? 147 ASP A CA    1 
ATOM   631  C C     . ASP A 1 147 ? 74.896  95.456  84.908  1.00 110.42 ? 147 ASP A C     1 
ATOM   632  O O     . ASP A 1 147 ? 74.136  96.430  84.959  1.00 110.70 ? 147 ASP A O     1 
ATOM   633  C CB    . ASP A 1 147 ? 74.330  93.486  83.462  1.00 119.00 ? 147 ASP A CB    1 
ATOM   634  C CG    . ASP A 1 147 ? 72.877  93.777  83.134  1.00 128.10 ? 147 ASP A CG    1 
ATOM   635  O OD1   . ASP A 1 147 ? 72.560  94.943  82.818  1.00 126.98 ? 147 ASP A OD1   1 
ATOM   636  O OD2   . ASP A 1 147 ? 72.053  92.840  83.192  1.00 132.06 ? 147 ASP A OD2   1 
ATOM   637  N N     . ASN A 1 148 ? 75.507  94.977  85.993  1.00 108.58 ? 148 ASN A N     1 
ATOM   638  C CA    . ASN A 1 148 ? 75.281  95.598  87.294  1.00 109.99 ? 148 ASN A CA    1 
ATOM   639  C C     . ASN A 1 148 ? 76.028  96.919  87.431  1.00 113.74 ? 148 ASN A C     1 
ATOM   640  O O     . ASN A 1 148 ? 75.582  97.805  88.169  1.00 114.84 ? 148 ASN A O     1 
ATOM   641  C CB    . ASN A 1 148 ? 75.688  94.637  88.410  1.00 104.54 ? 148 ASN A CB    1 
ATOM   642  C CG    . ASN A 1 148 ? 76.957  93.875  88.089  1.00 100.07 ? 148 ASN A CG    1 
ATOM   643  O OD1   . ASN A 1 148 ? 77.098  93.312  87.005  1.00 101.95 ? 148 ASN A OD1   1 
ATOM   644  N ND2   . ASN A 1 148 ? 77.886  93.848  89.035  1.00 96.68  ? 148 ASN A ND2   1 
ATOM   645  N N     . ALA A 1 149 ? 77.151  97.075  86.735  1.00 113.04 ? 149 ALA A N     1 
ATOM   646  C CA    . ALA A 1 149 ? 77.991  98.258  86.867  1.00 109.13 ? 149 ALA A CA    1 
ATOM   647  C C     . ALA A 1 149 ? 77.666  99.348  85.853  1.00 114.17 ? 149 ALA A C     1 
ATOM   648  O O     . ALA A 1 149 ? 78.326  100.392 85.860  1.00 117.64 ? 149 ALA A O     1 
ATOM   649  C CB    . ALA A 1 149 ? 79.467  97.871  86.746  1.00 103.57 ? 149 ALA A CB    1 
ATOM   650  N N     . GLN A 1 150 ? 76.678  99.135  84.981  1.00 115.88 ? 150 GLN A N     1 
ATOM   651  C CA    . GLN A 1 150 ? 76.324  100.164 84.007  1.00 117.90 ? 150 GLN A CA    1 
ATOM   652  C C     . GLN A 1 150 ? 75.768  101.407 84.692  1.00 120.11 ? 150 GLN A C     1 
ATOM   653  O O     . GLN A 1 150 ? 76.063  102.536 84.279  1.00 120.82 ? 150 GLN A O     1 
ATOM   654  C CB    . GLN A 1 150 ? 75.319  99.609  82.998  1.00 118.43 ? 150 GLN A CB    1 
ATOM   655  C CG    . GLN A 1 150 ? 75.403  100.251 81.623  1.00 123.39 ? 150 GLN A CG    1 
ATOM   656  C CD    . GLN A 1 150 ? 74.712  101.600 81.563  1.00 131.55 ? 150 GLN A CD    1 
ATOM   657  O OE1   . GLN A 1 150 ? 73.753  101.852 82.292  1.00 131.11 ? 150 GLN A OE1   1 
ATOM   658  N NE2   . GLN A 1 150 ? 75.198  102.476 80.691  1.00 134.69 ? 150 GLN A NE2   1 
ATOM   659  N N     . ASP A 1 151 ? 74.946  101.220 85.727  1.00 118.58 ? 151 ASP A N     1 
ATOM   660  C CA    . ASP A 1 151 ? 74.433  102.361 86.478  1.00 118.83 ? 151 ASP A CA    1 
ATOM   661  C C     . ASP A 1 151 ? 75.563  103.116 87.165  1.00 121.01 ? 151 ASP A C     1 
ATOM   662  O O     . ASP A 1 151 ? 75.579  104.352 87.173  1.00 124.41 ? 151 ASP A O     1 
ATOM   663  C CB    . ASP A 1 151 ? 73.395  101.895 87.497  1.00 118.63 ? 151 ASP A CB    1 
ATOM   664  C CG    . ASP A 1 151 ? 72.135  101.367 86.843  1.00 122.11 ? 151 ASP A CG    1 
ATOM   665  O OD1   . ASP A 1 151 ? 72.221  100.872 85.700  1.00 125.92 ? 151 ASP A OD1   1 
ATOM   666  O OD2   . ASP A 1 151 ? 71.059  101.445 87.472  1.00 121.15 ? 151 ASP A OD2   1 
ATOM   667  N N     . PHE A 1 152 ? 76.524  102.392 87.738  1.00 117.29 ? 152 PHE A N     1 
ATOM   668  C CA    . PHE A 1 152 ? 77.681  103.055 88.329  1.00 115.37 ? 152 PHE A CA    1 
ATOM   669  C C     . PHE A 1 152 ? 78.447  103.851 87.279  1.00 119.66 ? 152 PHE A C     1 
ATOM   670  O O     . PHE A 1 152 ? 78.838  105.000 87.521  1.00 119.70 ? 152 PHE A O     1 
ATOM   671  C CB    . PHE A 1 152 ? 78.590  102.020 88.990  1.00 110.31 ? 152 PHE A CB    1 
ATOM   672  C CG    . PHE A 1 152 ? 79.847  102.597 89.572  1.00 107.25 ? 152 PHE A CG    1 
ATOM   673  C CD1   . PHE A 1 152 ? 79.809  103.750 90.333  1.00 107.78 ? 152 PHE A CD1   1 
ATOM   674  C CD2   . PHE A 1 152 ? 81.068  101.983 89.357  1.00 104.32 ? 152 PHE A CD2   1 
ATOM   675  C CE1   . PHE A 1 152 ? 80.965  104.279 90.871  1.00 109.58 ? 152 PHE A CE1   1 
ATOM   676  C CE2   . PHE A 1 152 ? 82.226  102.507 89.891  1.00 103.16 ? 152 PHE A CE2   1 
ATOM   677  C CZ    . PHE A 1 152 ? 82.175  103.657 90.648  1.00 106.69 ? 152 PHE A CZ    1 
ATOM   678  N N     . TYR A 1 153 ? 78.642  103.265 86.096  1.00 120.98 ? 153 TYR A N     1 
ATOM   679  C CA    . TYR A 1 153 ? 79.413  103.933 85.054  1.00 119.05 ? 153 TYR A CA    1 
ATOM   680  C C     . TYR A 1 153 ? 78.719  105.202 84.576  1.00 120.47 ? 153 TYR A C     1 
ATOM   681  O O     . TYR A 1 153 ? 79.351  106.257 84.455  1.00 120.53 ? 153 TYR A O     1 
ATOM   682  C CB    . TYR A 1 153 ? 79.646  102.981 83.883  1.00 116.67 ? 153 TYR A CB    1 
ATOM   683  C CG    . TYR A 1 153 ? 80.649  103.489 82.874  1.00 113.80 ? 153 TYR A CG    1 
ATOM   684  C CD1   . TYR A 1 153 ? 81.988  103.632 83.212  1.00 113.13 ? 153 TYR A CD1   1 
ATOM   685  C CD2   . TYR A 1 153 ? 80.257  103.836 81.589  1.00 114.53 ? 153 TYR A CD2   1 
ATOM   686  C CE1   . TYR A 1 153 ? 82.909  104.096 82.294  1.00 111.80 ? 153 TYR A CE1   1 
ATOM   687  C CE2   . TYR A 1 153 ? 81.171  104.302 80.665  1.00 117.88 ? 153 TYR A CE2   1 
ATOM   688  C CZ    . TYR A 1 153 ? 82.496  104.431 81.023  1.00 115.12 ? 153 TYR A CZ    1 
ATOM   689  O OH    . TYR A 1 153 ? 83.411  104.896 80.107  1.00 114.53 ? 153 TYR A OH    1 
ATOM   690  N N     . ASP A 1 154 ? 77.416  105.126 84.296  1.00 121.82 ? 154 ASP A N     1 
ATOM   691  C CA    . ASP A 1 154 ? 76.757  106.313 83.762  1.00 124.42 ? 154 ASP A CA    1 
ATOM   692  C C     . ASP A 1 154 ? 76.514  107.361 84.843  1.00 125.12 ? 154 ASP A C     1 
ATOM   693  O O     . ASP A 1 154 ? 76.464  108.558 84.534  1.00 127.87 ? 154 ASP A O     1 
ATOM   694  C CB    . ASP A 1 154 ? 75.463  105.938 83.019  1.00 123.38 ? 154 ASP A CB    1 
ATOM   695  C CG    . ASP A 1 154 ? 74.351  105.442 83.929  1.00 125.76 ? 154 ASP A CG    1 
ATOM   696  O OD1   . ASP A 1 154 ? 74.489  105.474 85.163  1.00 125.79 ? 154 ASP A OD1   1 
ATOM   697  O OD2   . ASP A 1 154 ? 73.312  105.009 83.389  1.00 128.14 ? 154 ASP A OD2   1 
ATOM   698  N N     . TRP A 1 155 ? 76.389  106.949 86.110  1.00 121.38 ? 155 TRP A N     1 
ATOM   699  C CA    . TRP A 1 155 ? 76.380  107.928 87.190  1.00 120.36 ? 155 TRP A CA    1 
ATOM   700  C C     . TRP A 1 155 ? 77.722  108.638 87.292  1.00 121.84 ? 155 TRP A C     1 
ATOM   701  O O     . TRP A 1 155 ? 77.770  109.854 87.502  1.00 123.54 ? 155 TRP A O     1 
ATOM   702  C CB    . TRP A 1 155 ? 76.029  107.255 88.516  1.00 119.68 ? 155 TRP A CB    1 
ATOM   703  C CG    . TRP A 1 155 ? 75.998  108.209 89.672  1.00 121.49 ? 155 TRP A CG    1 
ATOM   704  C CD1   . TRP A 1 155 ? 74.944  108.978 90.070  1.00 122.17 ? 155 TRP A CD1   1 
ATOM   705  C CD2   . TRP A 1 155 ? 77.069  108.497 90.579  1.00 122.20 ? 155 TRP A CD2   1 
ATOM   706  N NE1   . TRP A 1 155 ? 75.291  109.726 91.168  1.00 123.36 ? 155 TRP A NE1   1 
ATOM   707  C CE2   . TRP A 1 155 ? 76.591  109.449 91.500  1.00 123.67 ? 155 TRP A CE2   1 
ATOM   708  C CE3   . TRP A 1 155 ? 78.385  108.042 90.701  1.00 119.28 ? 155 TRP A CE3   1 
ATOM   709  C CZ2   . TRP A 1 155 ? 77.381  109.954 92.530  1.00 123.06 ? 155 TRP A CZ2   1 
ATOM   710  C CZ3   . TRP A 1 155 ? 79.168  108.545 91.725  1.00 119.98 ? 155 TRP A CZ3   1 
ATOM   711  C CH2   . TRP A 1 155 ? 78.664  109.491 92.625  1.00 122.87 ? 155 TRP A CH2   1 
ATOM   712  N N     . LEU A 1 156 ? 78.825  107.897 87.141  1.00 121.31 ? 156 LEU A N     1 
ATOM   713  C CA    . LEU A 1 156 ? 80.139  108.530 87.106  1.00 122.92 ? 156 LEU A CA    1 
ATOM   714  C C     . LEU A 1 156 ? 80.253  109.492 85.931  1.00 122.47 ? 156 LEU A C     1 
ATOM   715  O O     . LEU A 1 156 ? 80.860  110.563 86.048  1.00 119.10 ? 156 LEU A O     1 
ATOM   716  C CB    . LEU A 1 156 ? 81.235  107.468 87.031  1.00 120.46 ? 156 LEU A CB    1 
ATOM   717  C CG    . LEU A 1 156 ? 81.663  106.778 88.326  1.00 116.88 ? 156 LEU A CG    1 
ATOM   718  C CD1   . LEU A 1 156 ? 83.004  106.093 88.134  1.00 113.13 ? 156 LEU A CD1   1 
ATOM   719  C CD2   . LEU A 1 156 ? 81.736  107.774 89.468  1.00 115.10 ? 156 LEU A CD2   1 
ATOM   720  N N     . GLN A 1 157 ? 79.691  109.115 84.782  1.00 123.85 ? 157 GLN A N     1 
ATOM   721  C CA    . GLN A 1 157 ? 79.720  109.992 83.616  1.00 123.64 ? 157 GLN A CA    1 
ATOM   722  C C     . GLN A 1 157 ? 78.953  111.283 83.876  1.00 123.78 ? 157 GLN A C     1 
ATOM   723  O O     . GLN A 1 157 ? 79.426  112.377 83.549  1.00 121.90 ? 157 GLN A O     1 
ATOM   724  C CB    . GLN A 1 157 ? 79.146  109.267 82.397  1.00 119.96 ? 157 GLN A CB    1 
ATOM   725  C CG    . GLN A 1 157 ? 79.960  108.076 81.930  1.00 116.46 ? 157 GLN A CG    1 
ATOM   726  C CD    . GLN A 1 157 ? 80.897  108.420 80.792  1.00 116.61 ? 157 GLN A CD    1 
ATOM   727  O OE1   . GLN A 1 157 ? 80.615  109.310 79.989  1.00 120.47 ? 157 GLN A OE1   1 
ATOM   728  N NE2   . GLN A 1 157 ? 82.020  107.717 80.715  1.00 116.51 ? 157 GLN A NE2   1 
ATOM   729  N N     . GLU A 1 158 ? 77.765  111.176 84.471  1.00 125.62 ? 158 GLU A N     1 
ATOM   730  C CA    . GLU A 1 158 ? 76.876  112.322 84.615  1.00 127.39 ? 158 GLU A CA    1 
ATOM   731  C C     . GLU A 1 158 ? 77.051  113.084 85.925  1.00 130.34 ? 158 GLU A C     1 
ATOM   732  O O     . GLU A 1 158 ? 76.469  114.165 86.072  1.00 130.88 ? 158 GLU A O     1 
ATOM   733  C CB    . GLU A 1 158 ? 75.417  111.865 84.477  1.00 127.63 ? 158 GLU A CB    1 
ATOM   734  C CG    . GLU A 1 158 ? 74.696  111.632 85.797  1.00 130.61 ? 158 GLU A CG    1 
ATOM   735  C CD    . GLU A 1 158 ? 73.192  111.551 85.633  1.00 133.20 ? 158 GLU A CD    1 
ATOM   736  O OE1   . GLU A 1 158 ? 72.728  111.305 84.500  1.00 134.28 ? 158 GLU A OE1   1 
ATOM   737  O OE2   . GLU A 1 158 ? 72.472  111.734 86.638  1.00 135.61 ? 158 GLU A OE2   1 
ATOM   738  N N     . THR A 1 159 ? 77.844  112.575 86.865  1.00 130.26 ? 159 THR A N     1 
ATOM   739  C CA    . THR A 1 159 ? 77.938  113.211 88.172  1.00 131.34 ? 159 THR A CA    1 
ATOM   740  C C     . THR A 1 159 ? 78.685  114.538 88.093  1.00 133.28 ? 159 THR A C     1 
ATOM   741  O O     . THR A 1 159 ? 79.528  114.758 87.219  1.00 131.78 ? 159 THR A O     1 
ATOM   742  C CB    . THR A 1 159 ? 78.634  112.292 89.177  1.00 127.87 ? 159 THR A CB    1 
ATOM   743  O OG1   . THR A 1 159 ? 78.628  112.905 90.473  1.00 129.31 ? 159 THR A OG1   1 
ATOM   744  C CG2   . THR A 1 159 ? 80.069  112.024 88.756  1.00 125.87 ? 159 THR A CG2   1 
ATOM   745  N N     . ASP A 1 160 ? 78.349  115.434 89.022  1.00 137.68 ? 160 ASP A N     1 
ATOM   746  C CA    . ASP A 1 160 ? 79.059  116.695 89.171  1.00 139.54 ? 160 ASP A CA    1 
ATOM   747  C C     . ASP A 1 160 ? 79.286  117.084 90.625  1.00 140.71 ? 160 ASP A C     1 
ATOM   748  O O     . ASP A 1 160 ? 79.823  118.167 90.877  1.00 137.01 ? 160 ASP A O     1 
ATOM   749  C CB    . ASP A 1 160 ? 78.302  117.825 88.452  1.00 138.94 ? 160 ASP A CB    1 
ATOM   750  C CG    . ASP A 1 160 ? 76.846  117.906 88.865  1.00 141.50 ? 160 ASP A CG    1 
ATOM   751  O OD1   . ASP A 1 160 ? 76.383  117.007 89.599  1.00 141.65 ? 160 ASP A OD1   1 
ATOM   752  O OD2   . ASP A 1 160 ? 76.164  118.868 88.455  1.00 141.55 ? 160 ASP A OD2   1 
ATOM   753  N N     . VAL A 1 161 ? 78.898  116.243 91.583  1.00 141.31 ? 161 VAL A N     1 
ATOM   754  C CA    . VAL A 1 161 ? 79.075  116.531 93.002  1.00 141.03 ? 161 VAL A CA    1 
ATOM   755  C C     . VAL A 1 161 ? 80.539  116.323 93.368  1.00 139.56 ? 161 VAL A C     1 
ATOM   756  O O     . VAL A 1 161 ? 81.309  115.757 92.585  1.00 137.59 ? 161 VAL A O     1 
ATOM   757  C CB    . VAL A 1 161 ? 78.148  115.653 93.865  1.00 140.05 ? 161 VAL A CB    1 
ATOM   758  C CG1   . VAL A 1 161 ? 78.787  114.296 94.131  1.00 137.31 ? 161 VAL A CG1   1 
ATOM   759  C CG2   . VAL A 1 161 ? 77.791  116.360 95.167  1.00 139.88 ? 161 VAL A CG2   1 
ATOM   760  N N     . ASP A 1 162 ? 80.935  116.787 94.550  1.00 139.98 ? 162 ASP A N     1 
ATOM   761  C CA    . ASP A 1 162 ? 82.305  116.668 95.029  1.00 137.51 ? 162 ASP A CA    1 
ATOM   762  C C     . ASP A 1 162 ? 82.360  115.738 96.233  1.00 136.29 ? 162 ASP A C     1 
ATOM   763  O O     . ASP A 1 162 ? 81.506  115.805 97.122  1.00 135.43 ? 162 ASP A O     1 
ATOM   764  C CB    . ASP A 1 162 ? 82.875  118.040 95.401  1.00 135.90 ? 162 ASP A CB    1 
ATOM   765  C CG    . ASP A 1 162 ? 84.083  117.941 96.309  1.00 136.63 ? 162 ASP A CG    1 
ATOM   766  O OD1   . ASP A 1 162 ? 85.087  117.319 95.901  1.00 132.30 ? 162 ASP A OD1   1 
ATOM   767  O OD2   . ASP A 1 162 ? 84.029  118.483 97.432  1.00 141.16 ? 162 ASP A OD2   1 
ATOM   768  N N     . LEU A 1 163 ? 83.370  114.871 96.255  1.00 134.03 ? 163 LEU A N     1 
ATOM   769  C CA    . LEU A 1 163 ? 83.583  113.910 97.335  1.00 132.80 ? 163 LEU A CA    1 
ATOM   770  C C     . LEU A 1 163 ? 84.909  114.252 98.006  1.00 131.43 ? 163 LEU A C     1 
ATOM   771  O O     . LEU A 1 163 ? 85.974  113.838 97.538  1.00 130.25 ? 163 LEU A O     1 
ATOM   772  C CB    . LEU A 1 163 ? 83.583  112.479 96.805  1.00 132.40 ? 163 LEU A CB    1 
ATOM   773  C CG    . LEU A 1 163 ? 82.285  111.967 96.177  1.00 132.77 ? 163 LEU A CG    1 
ATOM   774  C CD1   . LEU A 1 163 ? 82.502  110.602 95.544  1.00 127.31 ? 163 LEU A CD1   1 
ATOM   775  C CD2   . LEU A 1 163 ? 81.167  111.916 97.201  1.00 132.73 ? 163 LEU A CD2   1 
ATOM   776  N N     . THR A 1 164 ? 84.845  115.003 99.101  1.00 132.97 ? 164 THR A N     1 
ATOM   777  C CA    . THR A 1 164 ? 86.034  115.453 99.810  1.00 132.64 ? 164 THR A CA    1 
ATOM   778  C C     . THR A 1 164 ? 86.243  114.627 101.071 1.00 132.37 ? 164 THR A C     1 
ATOM   779  O O     . THR A 1 164 ? 85.306  114.401 101.843 1.00 131.76 ? 164 THR A O     1 
ATOM   780  C CB    . THR A 1 164 ? 85.926  116.934 100.177 1.00 130.52 ? 164 THR A CB    1 
ATOM   781  O OG1   . THR A 1 164 ? 85.206  117.631 99.153  1.00 134.61 ? 164 THR A OG1   1 
ATOM   782  C CG2   . THR A 1 164 ? 87.310  117.547 100.320 1.00 128.39 ? 164 THR A CG2   1 
ATOM   783  N N     . GLY A 1 165 ? 87.479  114.177 101.273 1.00 131.79 ? 165 GLY A N     1 
ATOM   784  C CA    . GLY A 1 165 ? 87.837  113.416 102.449 1.00 125.32 ? 165 GLY A CA    1 
ATOM   785  C C     . GLY A 1 165 ? 87.505  111.942 102.393 1.00 123.64 ? 165 GLY A C     1 
ATOM   786  O O     . GLY A 1 165 ? 87.784  111.227 103.364 1.00 122.31 ? 165 GLY A O     1 
ATOM   787  N N     . VAL A 1 166 ? 86.924  111.461 101.300 1.00 126.61 ? 166 VAL A N     1 
ATOM   788  C CA    . VAL A 1 166 ? 86.604  110.045 101.174 1.00 123.04 ? 166 VAL A CA    1 
ATOM   789  C C     . VAL A 1 166 ? 87.852  109.283 100.747 1.00 117.48 ? 166 VAL A C     1 
ATOM   790  O O     . VAL A 1 166 ? 88.723  109.807 100.043 1.00 119.06 ? 166 VAL A O     1 
ATOM   791  C CB    . VAL A 1 166 ? 85.435  109.832 100.189 1.00 121.50 ? 166 VAL A CB    1 
ATOM   792  C CG1   . VAL A 1 166 ? 85.882  110.065 98.758  1.00 118.79 ? 166 VAL A CG1   1 
ATOM   793  C CG2   . VAL A 1 166 ? 84.846  108.441 100.351 1.00 114.24 ? 166 VAL A CG2   1 
ATOM   794  N N     . LYS A 1 167 ? 87.949  108.036 101.197 1.00 111.91 ? 167 LYS A N     1 
ATOM   795  C CA    . LYS A 1 167 ? 89.104  107.188 100.947 1.00 107.03 ? 167 LYS A CA    1 
ATOM   796  C C     . LYS A 1 167 ? 88.668  105.988 100.121 1.00 99.86  ? 167 LYS A C     1 
ATOM   797  O O     . LYS A 1 167 ? 87.667  105.342 100.446 1.00 101.78 ? 167 LYS A O     1 
ATOM   798  C CB    . LYS A 1 167 ? 89.736  106.740 102.267 1.00 105.22 ? 167 LYS A CB    1 
ATOM   799  C CG    . LYS A 1 167 ? 90.063  107.892 103.202 1.00 107.30 ? 167 LYS A CG    1 
ATOM   800  C CD    . LYS A 1 167 ? 89.741  107.551 104.646 1.00 108.97 ? 167 LYS A CD    1 
ATOM   801  C CE    . LYS A 1 167 ? 90.052  108.720 105.567 1.00 107.47 ? 167 LYS A CE    1 
ATOM   802  N NZ    . LYS A 1 167 ? 91.508  109.029 105.603 1.00 105.96 ? 167 LYS A NZ    1 
ATOM   803  N N     . PHE A 1 168 ? 89.414  105.689 99.059  1.00 97.48  ? 168 PHE A N     1 
ATOM   804  C CA    . PHE A 1 168 ? 89.010  104.650 98.125  1.00 97.43  ? 168 PHE A CA    1 
ATOM   805  C C     . PHE A 1 168 ? 90.228  103.857 97.668  1.00 95.03  ? 168 PHE A C     1 
ATOM   806  O O     . PHE A 1 168 ? 91.376  104.269 97.846  1.00 101.88 ? 168 PHE A O     1 
ATOM   807  C CB    . PHE A 1 168 ? 88.242  105.252 96.931  1.00 99.99  ? 168 PHE A CB    1 
ATOM   808  C CG    . PHE A 1 168 ? 89.105  105.982 95.929  1.00 104.87 ? 168 PHE A CG    1 
ATOM   809  C CD1   . PHE A 1 168 ? 89.926  105.295 95.044  1.00 104.14 ? 168 PHE A CD1   1 
ATOM   810  C CD2   . PHE A 1 168 ? 89.108  107.363 95.888  1.00 110.35 ? 168 PHE A CD2   1 
ATOM   811  C CE1   . PHE A 1 168 ? 90.713  105.970 94.137  1.00 108.24 ? 168 PHE A CE1   1 
ATOM   812  C CE2   . PHE A 1 168 ? 89.900  108.041 94.983  1.00 110.48 ? 168 PHE A CE2   1 
ATOM   813  C CZ    . PHE A 1 168 ? 90.697  107.345 94.106  1.00 108.93 ? 168 PHE A CZ    1 
ATOM   814  N N     . ALA A 1 169 ? 89.951  102.697 97.077  1.00 87.44  ? 169 ALA A N     1 
ATOM   815  C CA    . ALA A 1 169 ? 90.943  101.904 96.369  1.00 82.63  ? 169 ALA A CA    1 
ATOM   816  C C     . ALA A 1 169 ? 90.228  101.163 95.250  1.00 87.38  ? 169 ALA A C     1 
ATOM   817  O O     . ALA A 1 169 ? 89.036  100.865 95.354  1.00 91.09  ? 169 ALA A O     1 
ATOM   818  C CB    . ALA A 1 169 ? 91.664  100.921 97.297  1.00 82.25  ? 169 ALA A CB    1 
ATOM   819  N N     . VAL A 1 170 ? 90.957  100.872 94.176  1.00 86.52  ? 170 VAL A N     1 
ATOM   820  C CA    . VAL A 1 170 ? 90.372  100.269 92.985  1.00 82.40  ? 170 VAL A CA    1 
ATOM   821  C C     . VAL A 1 170 ? 91.231  99.093  92.547  1.00 78.90  ? 170 VAL A C     1 
ATOM   822  O O     . VAL A 1 170 ? 92.452  99.227  92.408  1.00 81.53  ? 170 VAL A O     1 
ATOM   823  C CB    . VAL A 1 170 ? 90.228  101.292 91.842  1.00 88.18  ? 170 VAL A CB    1 
ATOM   824  C CG1   . VAL A 1 170 ? 90.206  100.593 90.492  1.00 84.26  ? 170 VAL A CG1   1 
ATOM   825  C CG2   . VAL A 1 170 ? 88.971  102.122 92.034  1.00 91.89  ? 170 VAL A CG2   1 
ATOM   826  N N     . PHE A 1 171 ? 90.593  97.944  92.334  1.00 80.08  ? 171 PHE A N     1 
ATOM   827  C CA    . PHE A 1 171 ? 91.235  96.770  91.763  1.00 78.95  ? 171 PHE A CA    1 
ATOM   828  C C     . PHE A 1 171 ? 90.591  96.475  90.417  1.00 79.46  ? 171 PHE A C     1 
ATOM   829  O O     . PHE A 1 171 ? 89.363  96.383  90.320  1.00 79.97  ? 171 PHE A O     1 
ATOM   830  C CB    . PHE A 1 171 ? 91.114  95.562  92.695  1.00 78.21  ? 171 PHE A CB    1 
ATOM   831  C CG    . PHE A 1 171 ? 91.864  94.353  92.220  1.00 76.46  ? 171 PHE A CG    1 
ATOM   832  C CD1   . PHE A 1 171 ? 93.195  94.176  92.550  1.00 79.98  ? 171 PHE A CD1   1 
ATOM   833  C CD2   . PHE A 1 171 ? 91.238  93.389  91.452  1.00 75.78  ? 171 PHE A CD2   1 
ATOM   834  C CE1   . PHE A 1 171 ? 93.888  93.065  92.115  1.00 81.20  ? 171 PHE A CE1   1 
ATOM   835  C CE2   . PHE A 1 171 ? 91.927  92.278  91.017  1.00 76.91  ? 171 PHE A CE2   1 
ATOM   836  C CZ    . PHE A 1 171 ? 93.253  92.116  91.348  1.00 77.86  ? 171 PHE A CZ    1 
ATOM   837  N N     . GLY A 1 172 ? 91.416  96.327  89.386  1.00 83.28  ? 172 GLY A N     1 
ATOM   838  C CA    . GLY A 1 172 ? 90.934  96.162  88.025  1.00 88.89  ? 172 GLY A CA    1 
ATOM   839  C C     . GLY A 1 172 ? 91.020  94.718  87.561  1.00 88.77  ? 172 GLY A C     1 
ATOM   840  O O     . GLY A 1 172 ? 92.026  94.042  87.776  1.00 90.41  ? 172 GLY A O     1 
ATOM   841  N N     . LEU A 1 173 ? 89.950  94.260  86.918  1.00 87.83  ? 173 LEU A N     1 
ATOM   842  C CA    . LEU A 1 173 ? 89.871  92.922  86.351  1.00 92.54  ? 173 LEU A CA    1 
ATOM   843  C C     . LEU A 1 173 ? 89.762  93.035  84.840  1.00 101.92 ? 173 LEU A C     1 
ATOM   844  O O     . LEU A 1 173 ? 88.918  93.780  84.332  1.00 103.35 ? 173 LEU A O     1 
ATOM   845  C CB    . LEU A 1 173 ? 88.669  92.158  86.905  1.00 87.66  ? 173 LEU A CB    1 
ATOM   846  C CG    . LEU A 1 173 ? 88.675  91.825  88.394  1.00 85.81  ? 173 LEU A CG    1 
ATOM   847  C CD1   . LEU A 1 173 ? 87.332  91.275  88.789  1.00 87.44  ? 173 LEU A CD1   1 
ATOM   848  C CD2   . LEU A 1 173 ? 89.756  90.828  88.714  1.00 87.63  ? 173 LEU A CD2   1 
ATOM   849  N N     . GLY A 1 174 ? 90.606  92.303  84.126  1.00 106.41 ? 174 GLY A N     1 
ATOM   850  C CA    . GLY A 1 174 ? 90.576  92.390  82.683  1.00 109.46 ? 174 GLY A CA    1 
ATOM   851  C C     . GLY A 1 174 ? 91.461  91.351  82.035  1.00 109.07 ? 174 GLY A C     1 
ATOM   852  O O     . GLY A 1 174 ? 91.993  90.457  82.694  1.00 108.38 ? 174 GLY A O     1 
ATOM   853  N N     . ASN A 1 175 ? 91.603  91.486  80.718  1.00 107.49 ? 175 ASN A N     1 
ATOM   854  C CA    . ASN A 1 175 ? 92.393  90.572  79.907  1.00 109.68 ? 175 ASN A CA    1 
ATOM   855  C C     . ASN A 1 175 ? 93.369  91.364  79.050  1.00 113.03 ? 175 ASN A C     1 
ATOM   856  O O     . ASN A 1 175 ? 93.019  92.413  78.502  1.00 114.43 ? 175 ASN A O     1 
ATOM   857  C CB    . ASN A 1 175 ? 91.493  89.708  79.015  1.00 110.69 ? 175 ASN A CB    1 
ATOM   858  C CG    . ASN A 1 175 ? 92.066  88.327  78.775  1.00 109.46 ? 175 ASN A CG    1 
ATOM   859  O OD1   . ASN A 1 175 ? 93.262  88.102  78.947  1.00 108.79 ? 175 ASN A OD1   1 
ATOM   860  N ND2   . ASN A 1 175 ? 91.212  87.393  78.376  1.00 110.73 ? 175 ASN A ND2   1 
ATOM   861  N N     . LYS A 1 176 ? 94.599  90.855  78.942  1.00 113.76 ? 176 LYS A N     1 
ATOM   862  C CA    . LYS A 1 176 ? 95.616  91.507  78.124  1.00 115.11 ? 176 LYS A CA    1 
ATOM   863  C C     . LYS A 1 176 ? 95.322  91.408  76.633  1.00 115.75 ? 176 LYS A C     1 
ATOM   864  O O     . LYS A 1 176 ? 95.863  92.201  75.856  1.00 120.03 ? 176 LYS A O     1 
ATOM   865  C CB    . LYS A 1 176 ? 96.991  90.902  78.414  1.00 113.76 ? 176 LYS A CB    1 
ATOM   866  C CG    . LYS A 1 176 ? 97.708  91.509  79.607  1.00 110.67 ? 176 LYS A CG    1 
ATOM   867  C CD    . LYS A 1 176 ? 98.178  92.922  79.301  1.00 108.80 ? 176 LYS A CD    1 
ATOM   868  C CE    . LYS A 1 176 ? 99.410  93.281  80.115  1.00 106.99 ? 176 LYS A CE    1 
ATOM   869  N NZ    . LYS A 1 176 ? 100.077 94.509  79.601  1.00 109.22 ? 176 LYS A NZ    1 
ATOM   870  N N     . THR A 1 177 ? 94.485  90.457  76.216  1.00 109.82 ? 177 THR A N     1 
ATOM   871  C CA    . THR A 1 177 ? 94.275  90.221  74.793  1.00 107.97 ? 177 THR A CA    1 
ATOM   872  C C     . THR A 1 177 ? 93.429  91.302  74.129  1.00 114.03 ? 177 THR A C     1 
ATOM   873  O O     . THR A 1 177 ? 93.440  91.402  72.898  1.00 119.36 ? 177 THR A O     1 
ATOM   874  C CB    . THR A 1 177 ? 93.630  88.851  74.581  1.00 109.03 ? 177 THR A CB    1 
ATOM   875  O OG1   . THR A 1 177 ? 92.353  88.817  75.229  1.00 111.01 ? 177 THR A OG1   1 
ATOM   876  C CG2   . THR A 1 177 ? 94.514  87.754  75.153  1.00 110.91 ? 177 THR A CG2   1 
ATOM   877  N N     . TYR A 1 178 ? 92.704  92.106  74.900  1.00 115.05 ? 178 TYR A N     1 
ATOM   878  C CA    . TYR A 1 178 ? 91.902  93.193  74.357  1.00 116.93 ? 178 TYR A CA    1 
ATOM   879  C C     . TYR A 1 178 ? 92.536  94.542  74.669  1.00 118.16 ? 178 TYR A C     1 
ATOM   880  O O     . TYR A 1 178 ? 93.266  94.696  75.652  1.00 119.24 ? 178 TYR A O     1 
ATOM   881  C CB    . TYR A 1 178 ? 90.465  93.155  74.889  1.00 114.35 ? 178 TYR A CB    1 
ATOM   882  C CG    . TYR A 1 178 ? 89.930  91.769  75.174  1.00 111.14 ? 178 TYR A CG    1 
ATOM   883  C CD1   . TYR A 1 178 ? 89.991  90.767  74.213  1.00 114.92 ? 178 TYR A CD1   1 
ATOM   884  C CD2   . TYR A 1 178 ? 89.358  91.463  76.399  1.00 110.00 ? 178 TYR A CD2   1 
ATOM   885  C CE1   . TYR A 1 178 ? 89.496  89.503  74.466  1.00 116.27 ? 178 TYR A CE1   1 
ATOM   886  C CE2   . TYR A 1 178 ? 88.863  90.201  76.661  1.00 111.35 ? 178 TYR A CE2   1 
ATOM   887  C CZ    . TYR A 1 178 ? 88.935  89.225  75.693  1.00 114.10 ? 178 TYR A CZ    1 
ATOM   888  O OH    . TYR A 1 178 ? 88.443  87.966  75.953  1.00 112.59 ? 178 TYR A OH    1 
ATOM   889  N N     . GLU A 1 179 ? 92.248  95.521  73.805  1.00 118.43 ? 179 GLU A N     1 
ATOM   890  C CA    . GLU A 1 179 ? 92.865  96.838  73.927  1.00 124.28 ? 179 GLU A CA    1 
ATOM   891  C C     . GLU A 1 179 ? 92.441  97.548  75.208  1.00 125.90 ? 179 GLU A C     1 
ATOM   892  O O     . GLU A 1 179 ? 93.269  98.176  75.877  1.00 122.46 ? 179 GLU A O     1 
ATOM   893  C CB    . GLU A 1 179 ? 92.530  97.686  72.698  1.00 127.87 ? 179 GLU A CB    1 
ATOM   894  C CG    . GLU A 1 179 ? 91.055  97.701  72.321  1.00 128.05 ? 179 GLU A CG    1 
ATOM   895  C CD    . GLU A 1 179 ? 90.297  98.842  72.968  1.00 131.38 ? 179 GLU A CD    1 
ATOM   896  O OE1   . GLU A 1 179 ? 90.950  99.796  73.439  1.00 134.63 ? 179 GLU A OE1   1 
ATOM   897  O OE2   . GLU A 1 179 ? 89.050  98.786  73.005  1.00 129.85 ? 179 GLU A OE2   1 
ATOM   898  N N     . HIS A 1 180 ? 91.159  97.466  75.567  1.00 125.57 ? 180 HIS A N     1 
ATOM   899  C CA    . HIS A 1 180 ? 90.654  98.120  76.773  1.00 124.20 ? 180 HIS A CA    1 
ATOM   900  C C     . HIS A 1 180 ? 90.935  97.210  77.966  1.00 120.42 ? 180 HIS A C     1 
ATOM   901  O O     . HIS A 1 180 ? 90.066  96.506  78.485  1.00 119.20 ? 180 HIS A O     1 
ATOM   902  C CB    . HIS A 1 180 ? 89.175  98.448  76.629  1.00 125.70 ? 180 HIS A CB    1 
ATOM   903  C CG    . HIS A 1 180 ? 88.916  99.785  76.006  1.00 129.02 ? 180 HIS A CG    1 
ATOM   904  N ND1   . HIS A 1 180 ? 87.770  100.069 75.296  1.00 131.90 ? 180 HIS A ND1   1 
ATOM   905  C CD2   . HIS A 1 180 ? 89.657  100.919 75.992  1.00 125.21 ? 180 HIS A CD2   1 
ATOM   906  C CE1   . HIS A 1 180 ? 87.816  101.318 74.869  1.00 129.35 ? 180 HIS A CE1   1 
ATOM   907  N NE2   . HIS A 1 180 ? 88.951  101.856 75.278  1.00 125.83 ? 180 HIS A NE2   1 
ATOM   908  N N     . PHE A 1 181 ? 92.191  97.240  78.404  1.00 116.19 ? 181 PHE A N     1 
ATOM   909  C CA    . PHE A 1 181 ? 92.693  96.352  79.447  1.00 111.96 ? 181 PHE A CA    1 
ATOM   910  C C     . PHE A 1 181 ? 92.507  97.041  80.797  1.00 106.51 ? 181 PHE A C     1 
ATOM   911  O O     . PHE A 1 181 ? 93.157  98.051  81.086  1.00 105.66 ? 181 PHE A O     1 
ATOM   912  C CB    . PHE A 1 181 ? 94.142  95.980  79.124  1.00 113.04 ? 181 PHE A CB    1 
ATOM   913  C CG    . PHE A 1 181 ? 94.961  95.508  80.293  1.00 110.79 ? 181 PHE A CG    1 
ATOM   914  C CD1   . PHE A 1 181 ? 95.662  96.407  81.081  1.00 110.08 ? 181 PHE A CD1   1 
ATOM   915  C CD2   . PHE A 1 181 ? 95.037  94.161  80.596  1.00 107.83 ? 181 PHE A CD2   1 
ATOM   916  C CE1   . PHE A 1 181 ? 96.434  95.968  82.138  1.00 109.40 ? 181 PHE A CE1   1 
ATOM   917  C CE2   . PHE A 1 181 ? 95.792  93.718  81.661  1.00 107.14 ? 181 PHE A CE2   1 
ATOM   918  C CZ    . PHE A 1 181 ? 96.492  94.621  82.433  1.00 107.73 ? 181 PHE A CZ    1 
ATOM   919  N N     . ASN A 1 182 ? 91.610  96.488  81.612  1.00 106.18 ? 182 ASN A N     1 
ATOM   920  C CA    . ASN A 1 182 ? 91.032  97.152  82.783  1.00 106.39 ? 182 ASN A CA    1 
ATOM   921  C C     . ASN A 1 182 ? 90.698  98.610  82.480  1.00 105.81 ? 182 ASN A C     1 
ATOM   922  O O     . ASN A 1 182 ? 91.196  99.543  83.109  1.00 107.08 ? 182 ASN A O     1 
ATOM   923  C CB    . ASN A 1 182 ? 91.933  97.046  84.012  1.00 104.63 ? 182 ASN A CB    1 
ATOM   924  C CG    . ASN A 1 182 ? 92.751  95.782  84.032  1.00 105.35 ? 182 ASN A CG    1 
ATOM   925  O OD1   . ASN A 1 182 ? 92.220  94.687  84.206  1.00 105.82 ? 182 ASN A OD1   1 
ATOM   926  N ND2   . ASN A 1 182 ? 94.055  95.927  83.906  1.00 105.81 ? 182 ASN A ND2   1 
ATOM   927  N N     . ALA A 1 183 ? 89.834  98.788  81.481  1.00 105.55 ? 183 ALA A N     1 
ATOM   928  C CA    . ALA A 1 183 ? 89.338  100.123 81.173  1.00 108.61 ? 183 ALA A CA    1 
ATOM   929  C C     . ALA A 1 183 ? 88.509  100.678 82.324  1.00 109.03 ? 183 ALA A C     1 
ATOM   930  O O     . ALA A 1 183 ? 88.641  101.853 82.685  1.00 106.98 ? 183 ALA A O     1 
ATOM   931  C CB    . ALA A 1 183 ? 88.518  100.096 79.884  1.00 113.82 ? 183 ALA A CB    1 
ATOM   932  N N     . MET A 1 184 ? 87.657  99.841  82.922  1.00 108.49 ? 184 MET A N     1 
ATOM   933  C CA    . MET A 1 184 ? 86.759  100.324 83.966  1.00 107.75 ? 184 MET A CA    1 
ATOM   934  C C     . MET A 1 184 ? 87.508  100.674 85.244  1.00 107.75 ? 184 MET A C     1 
ATOM   935  O O     . MET A 1 184 ? 87.200  101.682 85.886  1.00 109.35 ? 184 MET A O     1 
ATOM   936  C CB    . MET A 1 184 ? 85.671  99.292  84.250  1.00 102.46 ? 184 MET A CB    1 
ATOM   937  C CG    . MET A 1 184 ? 84.840  99.614  85.481  1.00 101.72 ? 184 MET A CG    1 
ATOM   938  S SD    . MET A 1 184 ? 83.508  100.769 85.125  1.00 107.44 ? 184 MET A SD    1 
ATOM   939  C CE    . MET A 1 184 ? 82.840  100.035 83.642  1.00 108.30 ? 184 MET A CE    1 
ATOM   940  N N     . GLY A 1 185 ? 88.482  99.856  85.643  1.00 105.10 ? 185 GLY A N     1 
ATOM   941  C CA    . GLY A 1 185 ? 89.234  100.170 86.848  1.00 102.97 ? 185 GLY A CA    1 
ATOM   942  C C     . GLY A 1 185 ? 89.984  101.483 86.731  1.00 105.56 ? 185 GLY A C     1 
ATOM   943  O O     . GLY A 1 185 ? 89.923  102.335 87.624  1.00 107.27 ? 185 GLY A O     1 
ATOM   944  N N     . LYS A 1 186 ? 90.685  101.672 85.610  1.00 107.60 ? 186 LYS A N     1 
ATOM   945  C CA    . LYS A 1 186 ? 91.392  102.926 85.378  1.00 106.48 ? 186 LYS A CA    1 
ATOM   946  C C     . LYS A 1 186 ? 90.423  104.096 85.301  1.00 107.53 ? 186 LYS A C     1 
ATOM   947  O O     . LYS A 1 186 ? 90.699  105.175 85.837  1.00 108.93 ? 186 LYS A O     1 
ATOM   948  C CB    . LYS A 1 186 ? 92.219  102.833 84.096  1.00 101.32 ? 186 LYS A CB    1 
ATOM   949  C CG    . LYS A 1 186 ? 93.341  101.812 84.145  1.00 99.43  ? 186 LYS A CG    1 
ATOM   950  C CD    . LYS A 1 186 ? 93.966  101.624 82.774  1.00 92.15  ? 186 LYS A CD    1 
ATOM   951  C CE    . LYS A 1 186 ? 95.050  100.561 82.798  1.00 96.82  ? 186 LYS A CE    1 
ATOM   952  N NZ    . LYS A 1 186 ? 95.631  100.335 81.447  1.00 96.32  ? 186 LYS A NZ    1 
ATOM   953  N N     . TYR A 1 187 ? 89.280  103.901 84.637  1.00 105.71 ? 187 TYR A N     1 
ATOM   954  C CA    . TYR A 1 187 ? 88.303  104.977 84.518  1.00 107.04 ? 187 TYR A CA    1 
ATOM   955  C C     . TYR A 1 187 ? 87.777  105.387 85.886  1.00 107.32 ? 187 TYR A C     1 
ATOM   956  O O     . TYR A 1 187 ? 87.675  106.579 86.189  1.00 112.71 ? 187 TYR A O     1 
ATOM   957  C CB    . TYR A 1 187 ? 87.163  104.546 83.588  1.00 110.71 ? 187 TYR A CB    1 
ATOM   958  C CG    . TYR A 1 187 ? 86.006  105.525 83.482  1.00 115.85 ? 187 TYR A CG    1 
ATOM   959  C CD1   . TYR A 1 187 ? 85.072  105.659 84.505  1.00 115.14 ? 187 TYR A CD1   1 
ATOM   960  C CD2   . TYR A 1 187 ? 85.862  106.331 82.361  1.00 118.33 ? 187 TYR A CD2   1 
ATOM   961  C CE1   . TYR A 1 187 ? 84.027  106.554 84.406  1.00 117.04 ? 187 TYR A CE1   1 
ATOM   962  C CE2   . TYR A 1 187 ? 84.819  107.230 82.255  1.00 120.70 ? 187 TYR A CE2   1 
ATOM   963  C CZ    . TYR A 1 187 ? 83.906  107.338 83.281  1.00 121.03 ? 187 TYR A CZ    1 
ATOM   964  O OH    . TYR A 1 187 ? 82.866  108.232 83.182  1.00 122.98 ? 187 TYR A OH    1 
ATOM   965  N N     . VAL A 1 188 ? 87.439  104.409 86.727  1.00 104.52 ? 188 VAL A N     1 
ATOM   966  C CA    . VAL A 1 188 ? 86.913  104.719 88.053  1.00 107.51 ? 188 VAL A CA    1 
ATOM   967  C C     . VAL A 1 188 ? 87.970  105.417 88.896  1.00 111.09 ? 188 VAL A C     1 
ATOM   968  O O     . VAL A 1 188 ? 87.681  106.403 89.584  1.00 114.03 ? 188 VAL A O     1 
ATOM   969  C CB    . VAL A 1 188 ? 86.389  103.444 88.739  1.00 104.89 ? 188 VAL A CB    1 
ATOM   970  C CG1   . VAL A 1 188 ? 85.982  103.745 90.168  1.00 105.13 ? 188 VAL A CG1   1 
ATOM   971  C CG2   . VAL A 1 188 ? 85.205  102.884 87.973  1.00 105.49 ? 188 VAL A CG2   1 
ATOM   972  N N     . ASP A 1 189 ? 89.212  104.928 88.851  1.00 110.02 ? 189 ASP A N     1 
ATOM   973  C CA    . ASP A 1 189 ? 90.274  105.560 89.629  1.00 110.34 ? 189 ASP A CA    1 
ATOM   974  C C     . ASP A 1 189 ? 90.489  107.005 89.193  1.00 113.73 ? 189 ASP A C     1 
ATOM   975  O O     . ASP A 1 189 ? 90.558  107.917 90.028  1.00 117.55 ? 189 ASP A O     1 
ATOM   976  C CB    . ASP A 1 189 ? 91.567  104.757 89.495  1.00 109.15 ? 189 ASP A CB    1 
ATOM   977  C CG    . ASP A 1 189 ? 92.625  105.181 90.495  1.00 115.60 ? 189 ASP A CG    1 
ATOM   978  O OD1   . ASP A 1 189 ? 92.316  106.005 91.381  1.00 118.76 ? 189 ASP A OD1   1 
ATOM   979  O OD2   . ASP A 1 189 ? 93.768  104.687 90.397  1.00 115.95 ? 189 ASP A OD2   1 
ATOM   980  N N     . GLN A 1 190 ? 90.577  107.237 87.880  1.00 108.82 ? 190 GLN A N     1 
ATOM   981  C CA    . GLN A 1 190 ? 90.843  108.585 87.395  1.00 108.82 ? 190 GLN A CA    1 
ATOM   982  C C     . GLN A 1 190 ? 89.660  109.511 87.652  1.00 111.61 ? 190 GLN A C     1 
ATOM   983  O O     . GLN A 1 190 ? 89.852  110.687 87.975  1.00 115.45 ? 190 GLN A O     1 
ATOM   984  C CB    . GLN A 1 190 ? 91.214  108.552 85.908  1.00 108.90 ? 190 GLN A CB    1 
ATOM   985  C CG    . GLN A 1 190 ? 90.045  108.536 84.934  1.00 110.28 ? 190 GLN A CG    1 
ATOM   986  C CD    . GLN A 1 190 ? 90.425  107.969 83.581  1.00 110.02 ? 190 GLN A CD    1 
ATOM   987  O OE1   . GLN A 1 190 ? 91.606  107.847 83.256  1.00 107.70 ? 190 GLN A OE1   1 
ATOM   988  N NE2   . GLN A 1 190 ? 89.423  107.627 82.779  1.00 112.39 ? 190 GLN A NE2   1 
ATOM   989  N N     . ARG A 1 191 ? 88.430  109.000 87.539  1.00 108.96 ? 191 ARG A N     1 
ATOM   990  C CA    . ARG A 1 191 ? 87.264  109.836 87.796  1.00 112.56 ? 191 ARG A CA    1 
ATOM   991  C C     . ARG A 1 191 ? 87.154  110.189 89.271  1.00 115.57 ? 191 ARG A C     1 
ATOM   992  O O     . ARG A 1 191 ? 86.782  111.315 89.617  1.00 121.28 ? 191 ARG A O     1 
ATOM   993  C CB    . ARG A 1 191 ? 85.995  109.135 87.313  1.00 112.03 ? 191 ARG A CB    1 
ATOM   994  C CG    . ARG A 1 191 ? 85.804  109.175 85.807  1.00 114.27 ? 191 ARG A CG    1 
ATOM   995  C CD    . ARG A 1 191 ? 85.249  110.513 85.347  1.00 117.79 ? 191 ARG A CD    1 
ATOM   996  N NE    . ARG A 1 191 ? 84.415  111.143 86.363  1.00 121.19 ? 191 ARG A NE    1 
ATOM   997  C CZ    . ARG A 1 191 ? 84.264  112.454 86.500  1.00 119.10 ? 191 ARG A CZ    1 
ATOM   998  N NH1   . ARG A 1 191 ? 84.881  113.308 85.701  1.00 118.78 ? 191 ARG A NH1   1 
ATOM   999  N NH2   . ARG A 1 191 ? 83.473  112.919 87.463  1.00 117.21 ? 191 ARG A NH2   1 
ATOM   1000 N N     . LEU A 1 192 ? 87.470  109.243 90.157  1.00 113.70 ? 192 LEU A N     1 
ATOM   1001 C CA    . LEU A 1 192 ? 87.470  109.548 91.582  1.00 116.00 ? 192 LEU A CA    1 
ATOM   1002 C C     . LEU A 1 192 ? 88.551  110.565 91.927  1.00 120.46 ? 192 LEU A C     1 
ATOM   1003 O O     . LEU A 1 192 ? 88.316  111.477 92.729  1.00 120.98 ? 192 LEU A O     1 
ATOM   1004 C CB    . LEU A 1 192 ? 87.649  108.266 92.393  1.00 115.60 ? 192 LEU A CB    1 
ATOM   1005 C CG    . LEU A 1 192 ? 86.432  107.342 92.481  1.00 116.85 ? 192 LEU A CG    1 
ATOM   1006 C CD1   . LEU A 1 192 ? 86.773  106.073 93.244  1.00 111.44 ? 192 LEU A CD1   1 
ATOM   1007 C CD2   . LEU A 1 192 ? 85.257  108.058 93.127  1.00 120.40 ? 192 LEU A CD2   1 
ATOM   1008 N N     . GLU A 1 193 ? 89.741  110.427 91.335  1.00 121.57 ? 193 GLU A N     1 
ATOM   1009 C CA    . GLU A 1 193 ? 90.799  111.404 91.584  1.00 120.49 ? 193 GLU A CA    1 
ATOM   1010 C C     . GLU A 1 193 ? 90.413  112.787 91.073  1.00 119.67 ? 193 GLU A C     1 
ATOM   1011 O O     . GLU A 1 193 ? 90.613  113.791 91.766  1.00 119.93 ? 193 GLU A O     1 
ATOM   1012 C CB    . GLU A 1 193 ? 92.106  110.943 90.942  1.00 119.13 ? 193 GLU A CB    1 
ATOM   1013 C CG    . GLU A 1 193 ? 93.094  110.338 91.922  1.00 120.04 ? 193 GLU A CG    1 
ATOM   1014 C CD    . GLU A 1 193 ? 94.532  110.662 91.569  1.00 122.03 ? 193 GLU A CD    1 
ATOM   1015 O OE1   . GLU A 1 193 ? 94.797  110.993 90.395  1.00 123.36 ? 193 GLU A OE1   1 
ATOM   1016 O OE2   . GLU A 1 193 ? 95.397  110.589 92.467  1.00 122.00 ? 193 GLU A OE2   1 
ATOM   1017 N N     . GLN A 1 194 ? 89.859  112.859 89.861  1.00 117.26 ? 194 GLN A N     1 
ATOM   1018 C CA    . GLN A 1 194 ? 89.468  114.143 89.289  1.00 117.81 ? 194 GLN A CA    1 
ATOM   1019 C C     . GLN A 1 194 ? 88.339  114.783 90.085  1.00 121.62 ? 194 GLN A C     1 
ATOM   1020 O O     . GLN A 1 194 ? 88.319  116.005 90.275  1.00 122.32 ? 194 GLN A O     1 
ATOM   1021 C CB    . GLN A 1 194 ? 89.051  113.956 87.831  1.00 113.76 ? 194 GLN A CB    1 
ATOM   1022 C CG    . GLN A 1 194 ? 90.201  113.675 86.883  1.00 115.41 ? 194 GLN A CG    1 
ATOM   1023 C CD    . GLN A 1 194 ? 89.725  113.320 85.490  1.00 116.90 ? 194 GLN A CD    1 
ATOM   1024 O OE1   . GLN A 1 194 ? 88.622  112.804 85.313  1.00 115.74 ? 194 GLN A OE1   1 
ATOM   1025 N NE2   . GLN A 1 194 ? 90.557  113.592 84.492  1.00 119.94 ? 194 GLN A NE2   1 
ATOM   1026 N N     . LEU A 1 195 ? 87.390  113.973 90.555  1.00 122.24 ? 195 LEU A N     1 
ATOM   1027 C CA    . LEU A 1 195 ? 86.222  114.508 91.242  1.00 123.84 ? 195 LEU A CA    1 
ATOM   1028 C C     . LEU A 1 195 ? 86.585  115.108 92.594  1.00 125.64 ? 195 LEU A C     1 
ATOM   1029 O O     . LEU A 1 195 ? 85.866  115.981 93.094  1.00 131.87 ? 195 LEU A O     1 
ATOM   1030 C CB    . LEU A 1 195 ? 85.174  113.407 91.398  1.00 123.88 ? 195 LEU A CB    1 
ATOM   1031 C CG    . LEU A 1 195 ? 83.761  113.826 91.790  1.00 124.85 ? 195 LEU A CG    1 
ATOM   1032 C CD1   . LEU A 1 195 ? 82.740  113.035 90.997  1.00 125.20 ? 195 LEU A CD1   1 
ATOM   1033 C CD2   . LEU A 1 195 ? 83.558  113.609 93.269  1.00 127.25 ? 195 LEU A CD2   1 
ATOM   1034 N N     . GLY A 1 196 ? 87.683  114.663 93.198  1.00 122.53 ? 196 GLY A N     1 
ATOM   1035 C CA    . GLY A 1 196 ? 88.138  115.253 94.441  1.00 125.51 ? 196 GLY A CA    1 
ATOM   1036 C C     . GLY A 1 196 ? 88.374  114.259 95.558  1.00 127.69 ? 196 GLY A C     1 
ATOM   1037 O O     . GLY A 1 196 ? 88.585  114.651 96.709  1.00 129.10 ? 196 GLY A O     1 
ATOM   1038 N N     . ALA A 1 197 ? 88.343  112.970 95.235  1.00 127.42 ? 197 ALA A N     1 
ATOM   1039 C CA    . ALA A 1 197 ? 88.583  111.938 96.229  1.00 127.13 ? 197 ALA A CA    1 
ATOM   1040 C C     . ALA A 1 197 ? 90.085  111.723 96.410  1.00 124.67 ? 197 ALA A C     1 
ATOM   1041 O O     . ALA A 1 197 ? 90.915  112.365 95.759  1.00 126.04 ? 197 ALA A O     1 
ATOM   1042 C CB    . ALA A 1 197 ? 87.871  110.649 95.831  1.00 123.98 ? 197 ALA A CB    1 
ATOM   1043 N N     . GLN A 1 198 ? 90.446  110.805 97.304  1.00 119.05 ? 198 GLN A N     1 
ATOM   1044 C CA    . GLN A 1 198 ? 91.836  110.582 97.679  1.00 116.80 ? 198 GLN A CA    1 
ATOM   1045 C C     . GLN A 1 198 ? 92.226  109.134 97.418  1.00 112.57 ? 198 GLN A C     1 
ATOM   1046 O O     . GLN A 1 198 ? 91.519  108.210 97.834  1.00 107.45 ? 198 GLN A O     1 
ATOM   1047 C CB    . GLN A 1 198 ? 92.068  110.930 99.152  1.00 116.48 ? 198 GLN A CB    1 
ATOM   1048 C CG    . GLN A 1 198 ? 93.499  110.722 99.617  1.00 116.51 ? 198 GLN A CG    1 
ATOM   1049 C CD    . GLN A 1 198 ? 93.618  110.648 101.126 1.00 121.15 ? 198 GLN A CD    1 
ATOM   1050 O OE1   . GLN A 1 198 ? 92.731  111.093 101.853 1.00 125.11 ? 198 GLN A OE1   1 
ATOM   1051 N NE2   . GLN A 1 198 ? 94.720  110.083 101.605 1.00 120.37 ? 198 GLN A NE2   1 
ATOM   1052 N N     . ARG A 1 199 ? 93.351  108.945 96.733  1.00 116.99 ? 199 ARG A N     1 
ATOM   1053 C CA    . ARG A 1 199 ? 93.911  107.620 96.518  1.00 110.59 ? 199 ARG A CA    1 
ATOM   1054 C C     . ARG A 1 199 ? 94.704  107.169 97.738  1.00 108.36 ? 199 ARG A C     1 
ATOM   1055 O O     . ARG A 1 199 ? 95.285  107.980 98.464  1.00 114.61 ? 199 ARG A O     1 
ATOM   1056 C CB    . ARG A 1 199 ? 94.815  107.612 95.285  1.00 114.51 ? 199 ARG A CB    1 
ATOM   1057 C CG    . ARG A 1 199 ? 94.093  107.355 93.976  1.00 110.63 ? 199 ARG A CG    1 
ATOM   1058 C CD    . ARG A 1 199 ? 95.033  107.356 92.772  1.00 113.49 ? 199 ARG A CD    1 
ATOM   1059 N NE    . ARG A 1 199 ? 95.921  106.199 92.728  1.00 114.60 ? 199 ARG A NE    1 
ATOM   1060 C CZ    . ARG A 1 199 ? 97.131  106.154 93.271  1.00 115.57 ? 199 ARG A CZ    1 
ATOM   1061 N NH1   . ARG A 1 199 ? 97.651  107.200 93.891  1.00 119.24 ? 199 ARG A NH1   1 
ATOM   1062 N NH2   . ARG A 1 199 ? 97.843  105.036 93.176  1.00 106.03 ? 199 ARG A NH2   1 
ATOM   1063 N N     . ILE A 1 200 ? 94.722  105.855 97.960  1.00 98.92  ? 200 ILE A N     1 
ATOM   1064 C CA    . ILE A 1 200 ? 95.461  105.242 99.057  1.00 99.44  ? 200 ILE A CA    1 
ATOM   1065 C C     . ILE A 1 200 ? 96.450  104.201 98.548  1.00 98.96  ? 200 ILE A C     1 
ATOM   1066 O O     . ILE A 1 200 ? 97.630  104.218 98.910  1.00 101.71 ? 200 ILE A O     1 
ATOM   1067 C CB    . ILE A 1 200 ? 94.507  104.621 100.102 1.00 98.44  ? 200 ILE A CB    1 
ATOM   1068 C CG1   . ILE A 1 200 ? 93.822  105.717 100.916 1.00 104.50 ? 200 ILE A CG1   1 
ATOM   1069 C CG2   . ILE A 1 200 ? 95.260  103.669 101.016 1.00 97.47  ? 200 ILE A CG2   1 
ATOM   1070 C CD1   . ILE A 1 200 ? 92.563  106.242 100.285 1.00 105.40 ? 200 ILE A CD1   1 
ATOM   1071 N N     . PHE A 1 201 ? 95.986  103.290 97.698  1.00 97.16  ? 201 PHE A N     1 
ATOM   1072 C CA    . PHE A 1 201 ? 96.815  102.221 97.169  1.00 94.62  ? 201 PHE A CA    1 
ATOM   1073 C C     . PHE A 1 201 ? 96.731  102.218 95.650  1.00 96.24  ? 201 PHE A C     1 
ATOM   1074 O O     . PHE A 1 201 ? 95.723  102.624 95.067  1.00 96.51  ? 201 PHE A O     1 
ATOM   1075 C CB    . PHE A 1 201 ? 96.392  100.860 97.729  1.00 91.62  ? 201 PHE A CB    1 
ATOM   1076 C CG    . PHE A 1 201 ? 97.418  99.786  97.544  1.00 92.36  ? 201 PHE A CG    1 
ATOM   1077 C CD1   . PHE A 1 201 ? 98.572  99.778  98.306  1.00 92.13  ? 201 PHE A CD1   1 
ATOM   1078 C CD2   . PHE A 1 201 ? 97.228  98.782  96.613  1.00 92.43  ? 201 PHE A CD2   1 
ATOM   1079 C CE1   . PHE A 1 201 ? 99.520  98.790  98.138  1.00 96.36  ? 201 PHE A CE1   1 
ATOM   1080 C CE2   . PHE A 1 201 ? 98.172  97.790  96.442  1.00 90.89  ? 201 PHE A CE2   1 
ATOM   1081 C CZ    . PHE A 1 201 ? 99.319  97.794  97.205  1.00 93.54  ? 201 PHE A CZ    1 
ATOM   1082 N N     . GLU A 1 202 ? 97.806  101.755 95.016  1.00 97.30  ? 202 GLU A N     1 
ATOM   1083 C CA    . GLU A 1 202 ? 97.892  101.779 93.566  1.00 95.92  ? 202 GLU A CA    1 
ATOM   1084 C C     . GLU A 1 202 ? 96.878  100.824 92.944  1.00 94.56  ? 202 GLU A C     1 
ATOM   1085 O O     . GLU A 1 202 ? 96.437  99.850  93.558  1.00 96.31  ? 202 GLU A O     1 
ATOM   1086 C CB    . GLU A 1 202 ? 99.303  101.418 93.103  1.00 95.50  ? 202 GLU A CB    1 
ATOM   1087 C CG    . GLU A 1 202 ? 99.643  99.944  93.222  1.00 98.59  ? 202 GLU A CG    1 
ATOM   1088 C CD    . GLU A 1 202 ? 100.335 99.610  94.526  1.00 99.25  ? 202 GLU A CD    1 
ATOM   1089 O OE1   . GLU A 1 202 ? 100.264 100.430 95.466  1.00 95.87  ? 202 GLU A OE1   1 
ATOM   1090 O OE2   . GLU A 1 202 ? 100.952 98.528  94.613  1.00 102.34 ? 202 GLU A OE2   1 
ATOM   1091 N N     . LEU A 1 203 ? 96.501  101.129 91.704  1.00 90.12  ? 203 LEU A N     1 
ATOM   1092 C CA    . LEU A 1 203 ? 95.546  100.300 90.985  1.00 89.01  ? 203 LEU A CA    1 
ATOM   1093 C C     . LEU A 1 203 ? 96.105  98.902  90.760  1.00 87.90  ? 203 LEU A C     1 
ATOM   1094 O O     . LEU A 1 203 ? 97.302  98.723  90.516  1.00 88.29  ? 203 LEU A O     1 
ATOM   1095 C CB    . LEU A 1 203 ? 95.193  100.943 89.644  1.00 91.93  ? 203 LEU A CB    1 
ATOM   1096 C CG    . LEU A 1 203 ? 93.846  100.552 89.035  1.00 94.38  ? 203 LEU A CG    1 
ATOM   1097 C CD1   . LEU A 1 203 ? 93.168  101.760 88.428  1.00 98.27  ? 203 LEU A CD1   1 
ATOM   1098 C CD2   . LEU A 1 203 ? 94.031  99.462  87.991  1.00 92.50  ? 203 LEU A CD2   1 
ATOM   1099 N N     . GLY A 1 204 ? 95.229  97.906  90.847  1.00 85.32  ? 204 GLY A N     1 
ATOM   1100 C CA    . GLY A 1 204 ? 95.619  96.537  90.586  1.00 85.96  ? 204 GLY A CA    1 
ATOM   1101 C C     . GLY A 1 204 ? 95.464  96.165  89.127  1.00 88.87  ? 204 GLY A C     1 
ATOM   1102 O O     . GLY A 1 204 ? 94.347  96.127  88.603  1.00 91.18  ? 204 GLY A O     1 
ATOM   1103 N N     . LEU A 1 205 ? 96.583  95.892  88.456  1.00 89.74  ? 205 LEU A N     1 
ATOM   1104 C CA    . LEU A 1 205 ? 96.566  95.538  87.037  1.00 98.21  ? 205 LEU A CA    1 
ATOM   1105 C C     . LEU A 1 205 ? 96.333  94.035  86.922  1.00 100.37 ? 205 LEU A C     1 
ATOM   1106 O O     . LEU A 1 205 ? 97.222  93.253  86.580  1.00 102.97 ? 205 LEU A O     1 
ATOM   1107 C CB    . LEU A 1 205 ? 97.862  95.964  86.358  1.00 105.05 ? 205 LEU A CB    1 
ATOM   1108 C CG    . LEU A 1 205 ? 98.021  97.442  85.984  1.00 102.16 ? 205 LEU A CG    1 
ATOM   1109 C CD1   . LEU A 1 205 ? 96.768  97.968  85.295  1.00 97.22  ? 205 LEU A CD1   1 
ATOM   1110 C CD2   . LEU A 1 205 ? 98.380  98.294  87.195  1.00 96.23  ? 205 LEU A CD2   1 
ATOM   1111 N N     . GLY A 1 206 ? 95.100  93.630  87.214  1.00 100.37 ? 206 GLY A N     1 
ATOM   1112 C CA    . GLY A 1 206 ? 94.739  92.227  87.174  1.00 100.13 ? 206 GLY A CA    1 
ATOM   1113 C C     . GLY A 1 206 ? 94.374  91.749  85.785  1.00 102.75 ? 206 GLY A C     1 
ATOM   1114 O O     . GLY A 1 206 ? 93.345  92.149  85.234  1.00 103.77 ? 206 GLY A O     1 
ATOM   1115 N N     . ASP A 1 207 ? 95.210  90.891  85.209  1.00 103.61 ? 207 ASP A N     1 
ATOM   1116 C CA    . ASP A 1 207 ? 95.005  90.367  83.867  1.00 104.74 ? 207 ASP A CA    1 
ATOM   1117 C C     . ASP A 1 207 ? 94.582  88.905  83.933  1.00 102.42 ? 207 ASP A C     1 
ATOM   1118 O O     . ASP A 1 207 ? 95.145  88.122  84.704  1.00 102.76 ? 207 ASP A O     1 
ATOM   1119 C CB    . ASP A 1 207 ? 96.269  90.527  83.015  1.00 108.52 ? 207 ASP A CB    1 
ATOM   1120 C CG    . ASP A 1 207 ? 97.524  90.040  83.719  1.00 111.20 ? 207 ASP A CG    1 
ATOM   1121 O OD1   . ASP A 1 207 ? 97.423  89.477  84.827  1.00 110.60 ? 207 ASP A OD1   1 
ATOM   1122 O OD2   . ASP A 1 207 ? 98.623  90.225  83.156  1.00 113.16 ? 207 ASP A OD2   1 
ATOM   1123 N N     . ASP A 1 208 ? 93.579  88.548  83.136  1.00 104.10 ? 208 ASP A N     1 
ATOM   1124 C CA    . ASP A 1 208 ? 93.100  87.176  83.057  1.00 104.00 ? 208 ASP A CA    1 
ATOM   1125 C C     . ASP A 1 208 ? 93.851  86.345  82.025  1.00 104.86 ? 208 ASP A C     1 
ATOM   1126 O O     . ASP A 1 208 ? 93.593  85.142  81.916  1.00 105.63 ? 208 ASP A O     1 
ATOM   1127 C CB    . ASP A 1 208 ? 91.602  87.160  82.737  1.00 103.89 ? 208 ASP A CB    1 
ATOM   1128 C CG    . ASP A 1 208 ? 90.863  86.057  83.464  1.00 103.42 ? 208 ASP A CG    1 
ATOM   1129 O OD1   . ASP A 1 208 ? 91.523  85.106  83.933  1.00 102.14 ? 208 ASP A OD1   1 
ATOM   1130 O OD2   . ASP A 1 208 ? 89.622  86.139  83.569  1.00 105.81 ? 208 ASP A OD2   1 
ATOM   1131 N N     . ASP A 1 209 ? 94.763  86.956  81.264  1.00 105.90 ? 209 ASP A N     1 
ATOM   1132 C CA    . ASP A 1 209 ? 95.503  86.209  80.252  1.00 111.16 ? 209 ASP A CA    1 
ATOM   1133 C C     . ASP A 1 209 ? 96.392  85.149  80.889  1.00 112.30 ? 209 ASP A C     1 
ATOM   1134 O O     . ASP A 1 209 ? 96.481  84.020  80.391  1.00 115.32 ? 209 ASP A O     1 
ATOM   1135 C CB    . ASP A 1 209 ? 96.334  87.166  79.398  1.00 114.46 ? 209 ASP A CB    1 
ATOM   1136 C CG    . ASP A 1 209 ? 96.580  86.635  78.000  1.00 116.49 ? 209 ASP A CG    1 
ATOM   1137 O OD1   . ASP A 1 209 ? 96.074  85.538  77.683  1.00 118.75 ? 209 ASP A OD1   1 
ATOM   1138 O OD2   . ASP A 1 209 ? 97.278  87.315  77.219  1.00 112.65 ? 209 ASP A OD2   1 
ATOM   1139 N N     . GLY A 1 210 ? 97.055  85.490  81.989  1.00 107.21 ? 210 GLY A N     1 
ATOM   1140 C CA    . GLY A 1 210 ? 97.867  84.530  82.707  1.00 109.03 ? 210 GLY A CA    1 
ATOM   1141 C C     . GLY A 1 210 ? 97.107  83.929  83.869  1.00 108.73 ? 210 GLY A C     1 
ATOM   1142 O O     . GLY A 1 210 ? 96.216  83.097  83.671  1.00 111.16 ? 210 GLY A O     1 
ATOM   1143 N N     . ASN A 1 211 ? 97.447  84.339  85.087  1.00 104.26 ? 211 ASN A N     1 
ATOM   1144 C CA    . ASN A 1 211 ? 96.709  83.954  86.281  1.00 97.96  ? 211 ASN A CA    1 
ATOM   1145 C C     . ASN A 1 211 ? 96.146  85.201  86.940  1.00 96.39  ? 211 ASN A C     1 
ATOM   1146 O O     . ASN A 1 211 ? 96.858  86.196  87.107  1.00 98.37  ? 211 ASN A O     1 
ATOM   1147 C CB    . ASN A 1 211 ? 97.590  83.190  87.269  1.00 96.41  ? 211 ASN A CB    1 
ATOM   1148 C CG    . ASN A 1 211 ? 96.812  82.151  88.048  1.00 97.93  ? 211 ASN A CG    1 
ATOM   1149 O OD1   . ASN A 1 211 ? 95.598  82.024  87.893  1.00 99.74  ? 211 ASN A OD1   1 
ATOM   1150 N ND2   . ASN A 1 211 ? 97.503  81.414  88.904  1.00 92.35  ? 211 ASN A ND2   1 
ATOM   1151 N N     . LEU A 1 212 ? 94.869  85.145  87.311  1.00 90.38  ? 212 LEU A N     1 
ATOM   1152 C CA    . LEU A 1 212 ? 94.220  86.283  87.944  1.00 88.37  ? 212 LEU A CA    1 
ATOM   1153 C C     . LEU A 1 212 ? 94.297  86.225  89.463  1.00 86.18  ? 212 LEU A C     1 
ATOM   1154 O O     . LEU A 1 212 ? 94.392  87.273  90.112  1.00 86.54  ? 212 LEU A O     1 
ATOM   1155 C CB    . LEU A 1 212 ? 92.758  86.365  87.499  1.00 84.09  ? 212 LEU A CB    1 
ATOM   1156 C CG    . LEU A 1 212 ? 91.914  87.424  88.199  1.00 78.49  ? 212 LEU A CG    1 
ATOM   1157 C CD1   . LEU A 1 212 ? 92.464  88.789  87.849  1.00 85.45  ? 212 LEU A CD1   1 
ATOM   1158 C CD2   . LEU A 1 212 ? 90.457  87.306  87.796  1.00 79.37  ? 212 LEU A CD2   1 
ATOM   1159 N N     . GLU A 1 213 ? 94.271  85.023  90.043  1.00 86.11  ? 213 GLU A N     1 
ATOM   1160 C CA    . GLU A 1 213 ? 94.395  84.898  91.491  1.00 83.42  ? 213 GLU A CA    1 
ATOM   1161 C C     . GLU A 1 213 ? 95.757  85.370  91.978  1.00 87.26  ? 213 GLU A C     1 
ATOM   1162 O O     . GLU A 1 213 ? 95.863  85.931  93.074  1.00 89.62  ? 213 GLU A O     1 
ATOM   1163 C CB    . GLU A 1 213 ? 94.146  83.451  91.914  1.00 85.56  ? 213 GLU A CB    1 
ATOM   1164 C CG    . GLU A 1 213 ? 94.117  83.238  93.417  1.00 87.16  ? 213 GLU A CG    1 
ATOM   1165 C CD    . GLU A 1 213 ? 92.780  83.594  94.035  1.00 86.52  ? 213 GLU A CD    1 
ATOM   1166 O OE1   . GLU A 1 213 ? 91.875  84.031  93.294  1.00 83.72  ? 213 GLU A OE1   1 
ATOM   1167 O OE2   . GLU A 1 213 ? 92.635  83.436  95.265  1.00 87.65  ? 213 GLU A OE2   1 
ATOM   1168 N N     . GLU A 1 214 ? 96.807  85.147  91.185  1.00 89.04  ? 214 GLU A N     1 
ATOM   1169 C CA    . GLU A 1 214 ? 98.137  85.625  91.548  1.00 93.02  ? 214 GLU A CA    1 
ATOM   1170 C C     . GLU A 1 214 ? 98.144  87.136  91.746  1.00 92.33  ? 214 GLU A C     1 
ATOM   1171 O O     . GLU A 1 214 ? 98.625  87.642  92.769  1.00 93.44  ? 214 GLU A O     1 
ATOM   1172 C CB    . GLU A 1 214 ? 99.138  85.228  90.463  1.00 101.55 ? 214 GLU A CB    1 
ATOM   1173 C CG    . GLU A 1 214 ? 100.507 84.854  90.981  1.00 109.28 ? 214 GLU A CG    1 
ATOM   1174 C CD    . GLU A 1 214 ? 101.602 85.054  89.948  1.00 113.63 ? 214 GLU A CD    1 
ATOM   1175 O OE1   . GLU A 1 214 ? 101.542 86.052  89.200  1.00 113.64 ? 214 GLU A OE1   1 
ATOM   1176 O OE2   . GLU A 1 214 ? 102.524 84.214  89.888  1.00 114.30 ? 214 GLU A OE2   1 
ATOM   1177 N N     . ASP A 1 215 ? 97.613  87.871  90.768  1.00 93.05  ? 215 ASP A N     1 
ATOM   1178 C CA    . ASP A 1 215 ? 97.634  89.327  90.836  1.00 93.03  ? 215 ASP A CA    1 
ATOM   1179 C C     . ASP A 1 215 ? 96.831  89.834  92.024  1.00 91.55  ? 215 ASP A C     1 
ATOM   1180 O O     . ASP A 1 215 ? 97.272  90.742  92.737  1.00 92.39  ? 215 ASP A O     1 
ATOM   1181 C CB    . ASP A 1 215 ? 97.097  89.916  89.533  1.00 94.63  ? 215 ASP A CB    1 
ATOM   1182 C CG    . ASP A 1 215 ? 98.172  90.069  88.479  1.00 101.14 ? 215 ASP A CG    1 
ATOM   1183 O OD1   . ASP A 1 215 ? 99.294  89.565  88.695  1.00 103.71 ? 215 ASP A OD1   1 
ATOM   1184 O OD2   . ASP A 1 215 ? 97.894  90.687  87.431  1.00 105.58 ? 215 ASP A OD2   1 
ATOM   1185 N N     . PHE A 1 216 ? 95.652  89.256  92.258  1.00 87.82  ? 216 PHE A N     1 
ATOM   1186 C CA    . PHE A 1 216 ? 94.832  89.703  93.378  1.00 83.02  ? 216 PHE A CA    1 
ATOM   1187 C C     . PHE A 1 216 ? 95.492  89.387  94.711  1.00 84.14  ? 216 PHE A C     1 
ATOM   1188 O O     . PHE A 1 216 ? 95.421  90.190  95.645  1.00 86.82  ? 216 PHE A O     1 
ATOM   1189 C CB    . PHE A 1 216 ? 93.446  89.072  93.317  1.00 80.37  ? 216 PHE A CB    1 
ATOM   1190 C CG    . PHE A 1 216 ? 92.596  89.376  94.516  1.00 77.01  ? 216 PHE A CG    1 
ATOM   1191 C CD1   . PHE A 1 216 ? 91.962  90.599  94.637  1.00 75.10  ? 216 PHE A CD1   1 
ATOM   1192 C CD2   . PHE A 1 216 ? 92.437  88.446  95.526  1.00 78.63  ? 216 PHE A CD2   1 
ATOM   1193 C CE1   . PHE A 1 216 ? 91.182  90.886  95.736  1.00 71.84  ? 216 PHE A CE1   1 
ATOM   1194 C CE2   . PHE A 1 216 ? 91.658  88.728  96.628  1.00 78.02  ? 216 PHE A CE2   1 
ATOM   1195 C CZ    . PHE A 1 216 ? 91.029  89.950  96.733  1.00 73.35  ? 216 PHE A CZ    1 
ATOM   1196 N N     . ILE A 1 217 ? 96.124  88.218  94.829  1.00 85.58  ? 217 ILE A N     1 
ATOM   1197 C CA    . ILE A 1 217 ? 96.756  87.870  96.096  1.00 86.92  ? 217 ILE A CA    1 
ATOM   1198 C C     . ILE A 1 217 ? 97.941  88.792  96.367  1.00 91.03  ? 217 ILE A C     1 
ATOM   1199 O O     . ILE A 1 217 ? 98.144  89.238  97.503  1.00 94.41  ? 217 ILE A O     1 
ATOM   1200 C CB    . ILE A 1 217 ? 97.143  86.376  96.122  1.00 86.06  ? 217 ILE A CB    1 
ATOM   1201 C CG1   . ILE A 1 217 ? 96.968  85.810  97.531  1.00 86.59  ? 217 ILE A CG1   1 
ATOM   1202 C CG2   . ILE A 1 217 ? 98.569  86.135  95.651  1.00 91.11  ? 217 ILE A CG2   1 
ATOM   1203 C CD1   . ILE A 1 217 ? 95.523  85.665  97.952  1.00 86.72  ? 217 ILE A CD1   1 
ATOM   1204 N N     . THR A 1 218 ? 98.711  89.136  95.328  1.00 90.23  ? 218 THR A N     1 
ATOM   1205 C CA    . THR A 1 218 ? 99.813  90.075  95.524  1.00 88.35  ? 218 THR A CA    1 
ATOM   1206 C C     . THR A 1 218 ? 99.295  91.462  95.883  1.00 84.56  ? 218 THR A C     1 
ATOM   1207 O O     . THR A 1 218 ? 99.838  92.124  96.778  1.00 84.37  ? 218 THR A O     1 
ATOM   1208 C CB    . THR A 1 218 ? 100.691 90.138  94.275  1.00 90.80  ? 218 THR A CB    1 
ATOM   1209 O OG1   . THR A 1 218 ? 99.895  90.520  93.146  1.00 93.48  ? 218 THR A OG1   1 
ATOM   1210 C CG2   . THR A 1 218 ? 101.342 88.790  94.009  1.00 89.19  ? 218 THR A CG2   1 
ATOM   1211 N N     . TRP A 1 219 ? 98.239  91.913  95.203  1.00 81.44  ? 219 TRP A N     1 
ATOM   1212 C CA    . TRP A 1 219 ? 97.675  93.226  95.488  1.00 81.76  ? 219 TRP A CA    1 
ATOM   1213 C C     . TRP A 1 219 ? 97.136  93.295  96.909  1.00 83.62  ? 219 TRP A C     1 
ATOM   1214 O O     . TRP A 1 219 ? 97.336  94.292  97.606  1.00 90.05  ? 219 TRP A O     1 
ATOM   1215 C CB    . TRP A 1 219 ? 96.579  93.548  94.473  1.00 81.27  ? 219 TRP A CB    1 
ATOM   1216 C CG    . TRP A 1 219 ? 95.896  94.860  94.691  1.00 80.97  ? 219 TRP A CG    1 
ATOM   1217 C CD1   . TRP A 1 219 ? 96.268  96.069  94.185  1.00 79.69  ? 219 TRP A CD1   1 
ATOM   1218 C CD2   . TRP A 1 219 ? 94.705  95.093  95.452  1.00 78.98  ? 219 TRP A CD2   1 
ATOM   1219 N NE1   . TRP A 1 219 ? 95.391  97.044  94.591  1.00 80.00  ? 219 TRP A NE1   1 
ATOM   1220 C CE2   . TRP A 1 219 ? 94.421  96.470  95.370  1.00 79.79  ? 219 TRP A CE2   1 
ATOM   1221 C CE3   . TRP A 1 219 ? 93.855  94.273  96.198  1.00 75.60  ? 219 TRP A CE3   1 
ATOM   1222 C CZ2   . TRP A 1 219 ? 93.325  97.045  96.006  1.00 79.11  ? 219 TRP A CZ2   1 
ATOM   1223 C CZ3   . TRP A 1 219 ? 92.767  94.846  96.828  1.00 72.33  ? 219 TRP A CZ3   1 
ATOM   1224 C CH2   . TRP A 1 219 ? 92.511  96.218  96.728  1.00 75.28  ? 219 TRP A CH2   1 
ATOM   1225 N N     . ARG A 1 220 ? 96.463  92.237  97.362  1.00 83.36  ? 220 ARG A N     1 
ATOM   1226 C CA    . ARG A 1 220 ? 95.946  92.203  98.726  1.00 85.36  ? 220 ARG A CA    1 
ATOM   1227 C C     . ARG A 1 220 ? 97.076  92.176  99.751  1.00 89.85  ? 220 ARG A C     1 
ATOM   1228 O O     . ARG A 1 220 ? 97.027  92.896  100.760 1.00 89.71  ? 220 ARG A O     1 
ATOM   1229 C CB    . ARG A 1 220 ? 95.030  90.989  98.888  1.00 87.48  ? 220 ARG A CB    1 
ATOM   1230 C CG    . ARG A 1 220 ? 94.539  90.735  100.295 1.00 94.94  ? 220 ARG A CG    1 
ATOM   1231 C CD    . ARG A 1 220 ? 93.647  89.502  100.345 1.00 93.42  ? 220 ARG A CD    1 
ATOM   1232 N NE    . ARG A 1 220 ? 93.934  88.658  101.499 1.00 100.79 ? 220 ARG A NE    1 
ATOM   1233 C CZ    . ARG A 1 220 ? 95.006  87.885  101.617 1.00 102.32 ? 220 ARG A CZ    1 
ATOM   1234 N NH1   . ARG A 1 220 ? 95.916  87.813  100.660 1.00 100.07 ? 220 ARG A NH1   1 
ATOM   1235 N NH2   . ARG A 1 220 ? 95.166  87.163  102.722 1.00 101.28 ? 220 ARG A NH2   1 
ATOM   1236 N N     . GLU A 1 221 ? 98.107  91.360  99.502  1.00 92.51  ? 221 GLU A N     1 
ATOM   1237 C CA    . GLU A 1 221 ? 99.230  91.263  100.427 1.00 93.98  ? 221 GLU A CA    1 
ATOM   1238 C C     . GLU A 1 221 ? 100.002 92.570  100.519 1.00 92.56  ? 221 GLU A C     1 
ATOM   1239 O O     . GLU A 1 221 ? 100.592 92.867  101.563 1.00 91.34  ? 221 GLU A O     1 
ATOM   1240 C CB    . GLU A 1 221 ? 100.161 90.128  100.000 1.00 97.42  ? 221 GLU A CB    1 
ATOM   1241 C CG    . GLU A 1 221 ? 101.208 89.750  101.034 1.00 104.84 ? 221 GLU A CG    1 
ATOM   1242 C CD    . GLU A 1 221 ? 100.699 88.732  102.035 1.00 111.29 ? 221 GLU A CD    1 
ATOM   1243 O OE1   . GLU A 1 221 ? 100.133 87.705  101.606 1.00 106.41 ? 221 GLU A OE1   1 
ATOM   1244 O OE2   . GLU A 1 221 ? 100.867 88.958  103.252 1.00 117.70 ? 221 GLU A OE2   1 
ATOM   1245 N N     . GLN A 1 222 ? 100.031 93.353  99.441  1.00 94.79  ? 222 GLN A N     1 
ATOM   1246 C CA    . GLN A 1 222 ? 100.680 94.656  99.484  1.00 95.43  ? 222 GLN A CA    1 
ATOM   1247 C C     . GLN A 1 222 ? 99.756  95.769  99.960  1.00 92.01  ? 222 GLN A C     1 
ATOM   1248 O O     . GLN A 1 222 ? 100.246 96.811  100.408 1.00 96.24  ? 222 GLN A O     1 
ATOM   1249 C CB    . GLN A 1 222 ? 101.235 95.015  98.101  1.00 95.56  ? 222 GLN A CB    1 
ATOM   1250 C CG    . GLN A 1 222 ? 102.515 94.280  97.692  1.00 96.10  ? 222 GLN A CG    1 
ATOM   1251 C CD    . GLN A 1 222 ? 103.740 94.653  98.519  1.00 101.78 ? 222 GLN A CD    1 
ATOM   1252 O OE1   . GLN A 1 222 ? 103.678 94.789  99.741  1.00 105.29 ? 222 GLN A OE1   1 
ATOM   1253 N NE2   . GLN A 1 222 ? 104.870 94.820  97.841  1.00 105.41 ? 222 GLN A NE2   1 
ATOM   1254 N N     . PHE A 1 223 ? 98.441  95.569  99.886  1.00 90.39  ? 223 PHE A N     1 
ATOM   1255 C CA    . PHE A 1 223 ? 97.469  96.606  100.206 1.00 89.59  ? 223 PHE A CA    1 
ATOM   1256 C C     . PHE A 1 223 ? 97.078  96.617  101.676 1.00 92.07  ? 223 PHE A C     1 
ATOM   1257 O O     . PHE A 1 223 ? 96.932  97.695  102.262 1.00 95.73  ? 223 PHE A O     1 
ATOM   1258 C CB    . PHE A 1 223 ? 96.225  96.429  99.330  1.00 85.74  ? 223 PHE A CB    1 
ATOM   1259 C CG    . PHE A 1 223 ? 94.943  96.872  99.981  1.00 80.25  ? 223 PHE A CG    1 
ATOM   1260 C CD1   . PHE A 1 223 ? 94.553  98.198  99.941  1.00 80.75  ? 223 PHE A CD1   1 
ATOM   1261 C CD2   . PHE A 1 223 ? 94.113  95.957  100.603 1.00 79.99  ? 223 PHE A CD2   1 
ATOM   1262 C CE1   . PHE A 1 223 ? 93.372  98.605  100.528 1.00 78.55  ? 223 PHE A CE1   1 
ATOM   1263 C CE2   . PHE A 1 223 ? 92.932  96.360  101.192 1.00 78.11  ? 223 PHE A CE2   1 
ATOM   1264 C CZ    . PHE A 1 223 ? 92.562  97.684  101.153 1.00 75.42  ? 223 PHE A CZ    1 
ATOM   1265 N N     . TRP A 1 224 ? 96.886  95.446  102.285 1.00 93.34  ? 224 TRP A N     1 
ATOM   1266 C CA    . TRP A 1 224 ? 96.487  95.430  103.692 1.00 97.44  ? 224 TRP A CA    1 
ATOM   1267 C C     . TRP A 1 224 ? 97.515  96.087  104.607 1.00 102.52 ? 224 TRP A C     1 
ATOM   1268 O O     . TRP A 1 224 ? 97.111  96.877  105.477 1.00 102.69 ? 224 TRP A O     1 
ATOM   1269 C CB    . TRP A 1 224 ? 96.158  94.001  104.136 1.00 99.01  ? 224 TRP A CB    1 
ATOM   1270 C CG    . TRP A 1 224 ? 94.746  93.607  103.826 1.00 95.83  ? 224 TRP A CG    1 
ATOM   1271 C CD1   . TRP A 1 224 ? 94.339  92.553  103.070 1.00 93.49  ? 224 TRP A CD1   1 
ATOM   1272 C CD2   . TRP A 1 224 ? 93.553  94.274  104.259 1.00 92.21  ? 224 TRP A CD2   1 
ATOM   1273 N NE1   . TRP A 1 224 ? 92.969  92.516  103.005 1.00 91.01  ? 224 TRP A NE1   1 
ATOM   1274 C CE2   . TRP A 1 224 ? 92.462  93.563  103.728 1.00 89.67  ? 224 TRP A CE2   1 
ATOM   1275 C CE3   . TRP A 1 224 ? 93.303  95.401  105.047 1.00 89.50  ? 224 TRP A CE3   1 
ATOM   1276 C CZ2   . TRP A 1 224 ? 91.143  93.942  103.957 1.00 87.34  ? 224 TRP A CZ2   1 
ATOM   1277 C CZ3   . TRP A 1 224 ? 91.994  95.775  105.273 1.00 84.54  ? 224 TRP A CZ3   1 
ATOM   1278 C CH2   . TRP A 1 224 ? 90.930  95.048  104.730 1.00 85.44  ? 224 TRP A CH2   1 
ATOM   1279 N N     . PRO A 1 225 ? 98.821  95.820  104.492 1.00 105.66 ? 225 PRO A N     1 
ATOM   1280 C CA    . PRO A 1 225 ? 99.782  96.605  105.284 1.00 104.31 ? 225 PRO A CA    1 
ATOM   1281 C C     . PRO A 1 225 ? 99.743  98.093  104.982 1.00 102.00 ? 225 PRO A C     1 
ATOM   1282 O O     . PRO A 1 225 ? 99.939  98.906  105.895 1.00 106.11 ? 225 PRO A O     1 
ATOM   1283 C CB    . PRO A 1 225 ? 101.135 95.989  104.903 1.00 104.96 ? 225 PRO A CB    1 
ATOM   1284 C CG    . PRO A 1 225 ? 100.806 94.604  104.496 1.00 106.14 ? 225 PRO A CG    1 
ATOM   1285 C CD    . PRO A 1 225 ? 99.487  94.705  103.795 1.00 103.39 ? 225 PRO A CD    1 
ATOM   1286 N N     . ALA A 1 226 ? 99.486  98.477  103.730 1.00 98.81  ? 226 ALA A N     1 
ATOM   1287 C CA    . ALA A 1 226 ? 99.463  99.894  103.379 1.00 102.12 ? 226 ALA A CA    1 
ATOM   1288 C C     . ALA A 1 226 ? 98.331  100.621 104.093 1.00 104.82 ? 226 ALA A C     1 
ATOM   1289 O O     . ALA A 1 226 ? 98.547  101.656 104.733 1.00 108.61 ? 226 ALA A O     1 
ATOM   1290 C CB    . ALA A 1 226 ? 99.341  100.055 101.864 1.00 99.02  ? 226 ALA A CB    1 
ATOM   1291 N N     . VAL A 1 227 ? 97.110  100.088 104.002 1.00 101.85 ? 227 VAL A N     1 
ATOM   1292 C CA    . VAL A 1 227 ? 95.989  100.709 104.699 1.00 101.69 ? 227 VAL A CA    1 
ATOM   1293 C C     . VAL A 1 227 ? 96.156  100.574 106.208 1.00 107.69 ? 227 VAL A C     1 
ATOM   1294 O O     . VAL A 1 227 ? 95.714  101.443 106.970 1.00 113.29 ? 227 VAL A O     1 
ATOM   1295 C CB    . VAL A 1 227 ? 94.655  100.111 104.210 1.00 93.67  ? 227 VAL A CB    1 
ATOM   1296 C CG1   . VAL A 1 227 ? 94.628  98.609  104.424 1.00 93.81  ? 227 VAL A CG1   1 
ATOM   1297 C CG2   . VAL A 1 227 ? 93.476  100.781 104.900 1.00 91.85  ? 227 VAL A CG2   1 
ATOM   1298 N N     . CYS A 1 228 ? 96.802  99.498  106.665 1.00 106.72 ? 228 CYS A N     1 
ATOM   1299 C CA    . CYS A 1 228 ? 97.049  99.328  108.093 1.00 110.06 ? 228 CYS A CA    1 
ATOM   1300 C C     . CYS A 1 228 ? 97.944  100.436 108.634 1.00 111.79 ? 228 CYS A C     1 
ATOM   1301 O O     . CYS A 1 228 ? 97.682  100.989 109.709 1.00 110.36 ? 228 CYS A O     1 
ATOM   1302 C CB    . CYS A 1 228 ? 97.677  97.957  108.347 1.00 109.52 ? 228 CYS A CB    1 
ATOM   1303 S SG    . CYS A 1 228 ? 97.381  97.275  109.989 1.00 124.94 ? 228 CYS A SG    1 
ATOM   1304 N N     . GLU A 1 229 ? 99.005  100.775 107.901 1.00 111.75 ? 229 GLU A N     1 
ATOM   1305 C CA    . GLU A 1 229 ? 99.884  101.861 108.319 1.00 111.33 ? 229 GLU A CA    1 
ATOM   1306 C C     . GLU A 1 229 ? 99.257  103.228 108.073 1.00 113.34 ? 229 GLU A C     1 
ATOM   1307 O O     . GLU A 1 229 ? 99.589  104.191 108.773 1.00 117.39 ? 229 GLU A O     1 
ATOM   1308 C CB    . GLU A 1 229 ? 101.235 101.753 107.606 1.00 112.42 ? 229 GLU A CB    1 
ATOM   1309 C CG    . GLU A 1 229 ? 101.291 102.424 106.243 1.00 114.95 ? 229 GLU A CG    1 
ATOM   1310 C CD    . GLU A 1 229 ? 102.663 102.340 105.607 1.00 119.90 ? 229 GLU A CD    1 
ATOM   1311 O OE1   . GLU A 1 229 ? 103.442 101.441 105.987 1.00 122.74 ? 229 GLU A OE1   1 
ATOM   1312 O OE2   . GLU A 1 229 ? 102.963 103.172 104.726 1.00 123.67 ? 229 GLU A OE2   1 
ATOM   1313 N N     . PHE A 1 230 ? 98.358  103.336 107.091 1.00 111.11 ? 230 PHE A N     1 
ATOM   1314 C CA    . PHE A 1 230 ? 97.684  104.605 106.845 1.00 109.28 ? 230 PHE A CA    1 
ATOM   1315 C C     . PHE A 1 230 ? 96.652  104.910 107.922 1.00 111.90 ? 230 PHE A C     1 
ATOM   1316 O O     . PHE A 1 230 ? 96.408  106.082 108.230 1.00 114.97 ? 230 PHE A O     1 
ATOM   1317 C CB    . PHE A 1 230 ? 97.024  104.585 105.465 1.00 108.97 ? 230 PHE A CB    1 
ATOM   1318 C CG    . PHE A 1 230 ? 96.421  105.900 105.056 1.00 108.56 ? 230 PHE A CG    1 
ATOM   1319 C CD1   . PHE A 1 230 ? 97.175  106.841 104.379 1.00 111.70 ? 230 PHE A CD1   1 
ATOM   1320 C CD2   . PHE A 1 230 ? 95.097  106.190 105.339 1.00 108.10 ? 230 PHE A CD2   1 
ATOM   1321 C CE1   . PHE A 1 230 ? 96.623  108.048 103.998 1.00 114.84 ? 230 PHE A CE1   1 
ATOM   1322 C CE2   . PHE A 1 230 ? 94.539  107.394 104.962 1.00 108.54 ? 230 PHE A CE2   1 
ATOM   1323 C CZ    . PHE A 1 230 ? 95.303  108.325 104.290 1.00 111.81 ? 230 PHE A CZ    1 
ATOM   1324 N N     . PHE A 1 231 ? 96.037  103.880 108.503 1.00 112.96 ? 231 PHE A N     1 
ATOM   1325 C CA    . PHE A 1 231 ? 95.014  104.072 109.521 1.00 116.43 ? 231 PHE A CA    1 
ATOM   1326 C C     . PHE A 1 231 ? 95.528  103.871 110.940 1.00 119.98 ? 231 PHE A C     1 
ATOM   1327 O O     . PHE A 1 231 ? 94.886  104.341 111.885 1.00 120.89 ? 231 PHE A O     1 
ATOM   1328 C CB    . PHE A 1 231 ? 93.835  103.120 109.279 1.00 117.79 ? 231 PHE A CB    1 
ATOM   1329 C CG    . PHE A 1 231 ? 92.876  103.592 108.221 1.00 116.81 ? 231 PHE A CG    1 
ATOM   1330 C CD1   . PHE A 1 231 ? 93.294  103.771 106.915 1.00 114.34 ? 231 PHE A CD1   1 
ATOM   1331 C CD2   . PHE A 1 231 ? 91.557  103.864 108.537 1.00 112.87 ? 231 PHE A CD2   1 
ATOM   1332 C CE1   . PHE A 1 231 ? 92.411  104.204 105.944 1.00 111.55 ? 231 PHE A CE1   1 
ATOM   1333 C CE2   . PHE A 1 231 ? 90.671  104.299 107.572 1.00 107.73 ? 231 PHE A CE2   1 
ATOM   1334 C CZ    . PHE A 1 231 ? 91.099  104.470 106.274 1.00 108.24 ? 231 PHE A CZ    1 
ATOM   1335 N N     . GLY A 1 232 ? 96.659  103.190 111.112 1.00 121.07 ? 232 GLY A N     1 
ATOM   1336 C CA    . GLY A 1 232 ? 97.229  102.985 112.428 1.00 123.84 ? 232 GLY A CA    1 
ATOM   1337 C C     . GLY A 1 232 ? 96.653  101.834 113.220 1.00 124.15 ? 232 GLY A C     1 
ATOM   1338 O O     . GLY A 1 232 ? 96.953  101.715 114.413 1.00 124.18 ? 232 GLY A O     1 
ATOM   1339 N N     . VAL A 1 233 ? 95.837  100.982 112.601 1.00 122.07 ? 233 VAL A N     1 
ATOM   1340 C CA    . VAL A 1 233 ? 95.252  99.853  113.313 1.00 122.69 ? 233 VAL A CA    1 
ATOM   1341 C C     . VAL A 1 233 ? 96.281  98.731  113.439 1.00 123.85 ? 233 VAL A C     1 
ATOM   1342 O O     . VAL A 1 233 ? 97.309  98.712  112.759 1.00 122.35 ? 233 VAL A O     1 
ATOM   1343 C CB    . VAL A 1 233 ? 93.970  99.370  112.609 1.00 123.14 ? 233 VAL A CB    1 
ATOM   1344 C CG1   . VAL A 1 233 ? 94.312  98.488  111.419 1.00 124.54 ? 233 VAL A CG1   1 
ATOM   1345 C CG2   . VAL A 1 233 ? 93.044  98.652  113.586 1.00 121.03 ? 233 VAL A CG2   1 
ATOM   1346 N N     . GLU A 1 234 ? 96.003  97.792  114.338 1.00 126.25 ? 234 GLU A N     1 
ATOM   1347 C CA    . GLU A 1 234 ? 96.890  96.666  114.584 1.00 127.73 ? 234 GLU A CA    1 
ATOM   1348 C C     . GLU A 1 234 ? 96.488  95.463  113.733 1.00 125.64 ? 234 GLU A C     1 
ATOM   1349 O O     . GLU A 1 234 ? 95.419  95.425  113.120 1.00 123.13 ? 234 GLU A O     1 
ATOM   1350 C CB    . GLU A 1 234 ? 96.887  96.290  116.068 1.00 131.60 ? 234 GLU A CB    1 
ATOM   1351 C CG    . GLU A 1 234 ? 97.747  97.175  116.973 1.00 138.82 ? 234 GLU A CG    1 
ATOM   1352 C CD    . GLU A 1 234 ? 97.384  98.651  116.917 1.00 136.90 ? 234 GLU A CD    1 
ATOM   1353 O OE1   . GLU A 1 234 ? 96.242  98.983  116.532 1.00 135.81 ? 234 GLU A OE1   1 
ATOM   1354 O OE2   . GLU A 1 234 ? 98.248  99.485  117.263 1.00 130.42 ? 234 GLU A OE2   1 
ATOM   1355 N N     . ALA A 1 235 ? 97.370  94.466  113.702 1.00 128.33 ? 235 ALA A N     1 
ATOM   1356 C CA    . ALA A 1 235 ? 97.151  93.241  112.940 1.00 128.59 ? 235 ALA A CA    1 
ATOM   1357 C C     . ALA A 1 235 ? 97.566  92.025  113.756 1.00 132.89 ? 235 ALA A C     1 
ATOM   1358 O O     . ALA A 1 235 ? 98.157  91.075  113.232 1.00 130.18 ? 235 ALA A O     1 
ATOM   1359 C CB    . ALA A 1 235 ? 97.903  93.278  111.610 1.00 126.94 ? 235 ALA A CB    1 
ATOM   1360 N N     . THR A 1 236 ? 97.266  92.041  115.057 1.00 139.43 ? 236 THR A N     1 
ATOM   1361 C CA    . THR A 1 236 ? 97.678  90.946  115.930 1.00 141.13 ? 236 THR A CA    1 
ATOM   1362 C C     . THR A 1 236 ? 96.962  89.649  115.572 1.00 141.96 ? 236 THR A C     1 
ATOM   1363 O O     . THR A 1 236 ? 97.584  88.583  115.507 1.00 143.30 ? 236 THR A O     1 
ATOM   1364 C CB    . THR A 1 236 ? 97.421  91.314  117.392 1.00 137.42 ? 236 THR A CB    1 
ATOM   1365 O OG1   . THR A 1 236 ? 96.014  91.475  117.607 1.00 134.23 ? 236 THR A OG1   1 
ATOM   1366 C CG2   . THR A 1 236 ? 98.135  92.610  117.748 1.00 136.04 ? 236 THR A CG2   1 
ATOM   1367 N N     . GLY A 1 237 ? 95.652  89.719  115.344 1.00 140.72 ? 237 GLY A N     1 
ATOM   1368 C CA    . GLY A 1 237 ? 94.875  88.542  115.004 1.00 139.70 ? 237 GLY A CA    1 
ATOM   1369 C C     . GLY A 1 237 ? 95.318  87.880  113.716 1.00 139.53 ? 237 GLY A C     1 
ATOM   1370 O O     . GLY A 1 237 ? 95.515  88.556  112.703 1.00 139.23 ? 237 GLY A O     1 
ATOM   1371 N N     . GLU A 1 238 ? 95.483  86.559  113.741 1.00 138.46 ? 238 GLU A N     1 
ATOM   1372 C CA    . GLU A 1 238 ? 95.912  85.813  112.568 1.00 138.75 ? 238 GLU A CA    1 
ATOM   1373 C C     . GLU A 1 238 ? 95.143  84.503  112.482 1.00 137.59 ? 238 GLU A C     1 
ATOM   1374 O O     . GLU A 1 238 ? 94.775  83.914  113.502 1.00 136.44 ? 238 GLU A O     1 
ATOM   1375 C CB    . GLU A 1 238 ? 97.421  85.531  112.597 1.00 140.77 ? 238 GLU A CB    1 
ATOM   1376 C CG    . GLU A 1 238 ? 98.287  86.737  112.273 1.00 141.15 ? 238 GLU A CG    1 
ATOM   1377 C CD    . GLU A 1 238 ? 99.768  86.430  112.369 1.00 143.44 ? 238 GLU A CD    1 
ATOM   1378 O OE1   . GLU A 1 238 ? 100.118 85.272  112.680 1.00 144.89 ? 238 GLU A OE1   1 
ATOM   1379 O OE2   . GLU A 1 238 ? 100.583 87.347  112.132 1.00 143.32 ? 238 GLU A OE2   1 
ATOM   1380 N N     . GLU A 1 239 ? 94.915  84.054  111.245 1.00 135.00 ? 239 GLU A N     1 
ATOM   1381 C CA    . GLU A 1 239 ? 94.252  82.778  110.967 1.00 132.16 ? 239 GLU A CA    1 
ATOM   1382 C C     . GLU A 1 239 ? 92.887  82.689  111.647 1.00 133.65 ? 239 GLU A C     1 
ATOM   1383 O O     . GLU A 1 239 ? 92.501  81.642  112.170 1.00 134.49 ? 239 GLU A O     1 
ATOM   1384 C CB    . GLU A 1 239 ? 95.137  81.597  111.373 1.00 135.20 ? 239 GLU A CB    1 
ATOM   1385 C CG    . GLU A 1 239 ? 96.562  81.679  110.851 1.00 133.45 ? 239 GLU A CG    1 
ATOM   1386 C CD    . GLU A 1 239 ? 97.451  80.586  111.410 1.00 139.56 ? 239 GLU A CD    1 
ATOM   1387 O OE1   . GLU A 1 239 ? 97.630  80.537  112.645 1.00 148.50 ? 239 GLU A OE1   1 
ATOM   1388 O OE2   . GLU A 1 239 ? 97.971  79.774  110.615 1.00 136.04 ? 239 GLU A OE2   1 
ATOM   1389 N N     . SER A 1 240 ? 92.150  83.801  111.646 1.00 133.59 ? 240 SER A N     1 
ATOM   1390 C CA    . SER A 1 240 ? 90.818  83.799  112.242 1.00 128.99 ? 240 SER A CA    1 
ATOM   1391 C C     . SER A 1 240 ? 89.852  82.952  111.422 1.00 128.55 ? 240 SER A C     1 
ATOM   1392 O O     . SER A 1 240 ? 89.143  82.098  111.969 1.00 124.76 ? 240 SER A O     1 
ATOM   1393 C CB    . SER A 1 240 ? 90.303  85.232  112.380 1.00 129.50 ? 240 SER A CB    1 
ATOM   1394 O OG    . SER A 1 240 ? 91.123  85.983  113.258 1.00 130.12 ? 240 SER A OG    1 
ATOM   1395 N N     . SER A 1 241 ? 89.820  83.168  110.107 1.00 126.17 ? 241 SER A N     1 
ATOM   1396 C CA    . SER A 1 241 ? 89.001  82.389  109.179 1.00 115.53 ? 241 SER A CA    1 
ATOM   1397 C C     . SER A 1 241 ? 87.531  82.392  109.601 1.00 112.84 ? 241 SER A C     1 
ATOM   1398 O O     . SER A 1 241 ? 86.943  81.362  109.931 1.00 112.54 ? 241 SER A O     1 
ATOM   1399 C CB    . SER A 1 241 ? 89.538  80.961  109.052 1.00 114.17 ? 241 SER A CB    1 
ATOM   1400 O OG    . SER A 1 241 ? 90.817  80.952  108.444 1.00 108.74 ? 241 SER A OG    1 
ATOM   1401 N N     . ILE A 1 242 ? 86.943  83.589  109.586 1.00 108.09 ? 242 ILE A N     1 
ATOM   1402 C CA    . ILE A 1 242 ? 85.564  83.751  110.028 1.00 103.22 ? 242 ILE A CA    1 
ATOM   1403 C C     . ILE A 1 242 ? 84.616  83.105  109.025 1.00 97.58  ? 242 ILE A C     1 
ATOM   1404 O O     . ILE A 1 242 ? 84.911  83.015  107.825 1.00 98.11  ? 242 ILE A O     1 
ATOM   1405 C CB    . ILE A 1 242 ? 85.241  85.242  110.232 1.00 100.59 ? 242 ILE A CB    1 
ATOM   1406 C CG1   . ILE A 1 242 ? 83.986  85.410  111.093 1.00 96.33  ? 242 ILE A CG1   1 
ATOM   1407 C CG2   . ILE A 1 242 ? 85.076  85.951  108.896 1.00 96.12  ? 242 ILE A CG2   1 
ATOM   1408 C CD1   . ILE A 1 242 ? 84.054  84.685  112.419 1.00 90.68  ? 242 ILE A CD1   1 
ATOM   1409 N N     . ARG A 1 243 ? 83.478  82.629  109.522 1.00 93.55  ? 243 ARG A N     1 
ATOM   1410 C CA    . ARG A 1 243 ? 82.450  82.053  108.669 1.00 90.05  ? 243 ARG A CA    1 
ATOM   1411 C C     . ARG A 1 243 ? 81.483  83.130  108.194 1.00 87.44  ? 243 ARG A C     1 
ATOM   1412 O O     . ARG A 1 243 ? 81.313  84.171  108.835 1.00 92.97  ? 243 ARG A O     1 
ATOM   1413 C CB    . ARG A 1 243 ? 81.682  80.963  109.414 1.00 91.65  ? 243 ARG A CB    1 
ATOM   1414 C CG    . ARG A 1 243 ? 82.410  79.636  109.507 1.00 90.85  ? 243 ARG A CG    1 
ATOM   1415 C CD    . ARG A 1 243 ? 81.954  78.696  108.409 1.00 82.61  ? 243 ARG A CD    1 
ATOM   1416 N NE    . ARG A 1 243 ? 80.517  78.461  108.460 1.00 80.86  ? 243 ARG A NE    1 
ATOM   1417 C CZ    . ARG A 1 243 ? 79.932  77.318  108.131 1.00 81.54  ? 243 ARG A CZ    1 
ATOM   1418 N NH1   . ARG A 1 243 ? 80.636  76.275  107.722 1.00 79.31  ? 243 ARG A NH1   1 
ATOM   1419 N NH2   . ARG A 1 243 ? 78.609  77.218  108.215 1.00 83.76  ? 243 ARG A NH2   1 
ATOM   1420 N N     . GLN A 1 244 ? 80.841  82.867  107.055 1.00 83.59  ? 244 GLN A N     1 
ATOM   1421 C CA    . GLN A 1 244 ? 79.885  83.802  106.483 1.00 83.02  ? 244 GLN A CA    1 
ATOM   1422 C C     . GLN A 1 244 ? 78.445  83.311  106.530 1.00 83.70  ? 244 GLN A C     1 
ATOM   1423 O O     . GLN A 1 244 ? 77.531  84.140  106.537 1.00 82.82  ? 244 GLN A O     1 
ATOM   1424 C CB    . GLN A 1 244 ? 80.263  84.124  105.029 1.00 83.18  ? 244 GLN A CB    1 
ATOM   1425 C CG    . GLN A 1 244 ? 79.482  85.272  104.413 1.00 83.96  ? 244 GLN A CG    1 
ATOM   1426 C CD    . GLN A 1 244 ? 79.739  86.590  105.113 1.00 92.28  ? 244 GLN A CD    1 
ATOM   1427 O OE1   . GLN A 1 244 ? 80.886  86.993  105.301 1.00 97.99  ? 244 GLN A OE1   1 
ATOM   1428 N NE2   . GLN A 1 244 ? 78.668  87.269  105.505 1.00 96.36  ? 244 GLN A NE2   1 
ATOM   1429 N N     . TYR A 1 245 ? 78.217  82.001  106.580 1.00 82.17  ? 245 TYR A N     1 
ATOM   1430 C CA    . TYR A 1 245 ? 76.872  81.459  106.704 1.00 79.13  ? 245 TYR A CA    1 
ATOM   1431 C C     . TYR A 1 245 ? 76.868  80.340  107.735 1.00 84.36  ? 245 TYR A C     1 
ATOM   1432 O O     . TYR A 1 245 ? 77.887  79.685  107.968 1.00 87.10  ? 245 TYR A O     1 
ATOM   1433 C CB    . TYR A 1 245 ? 76.338  80.946  105.360 1.00 76.62  ? 245 TYR A CB    1 
ATOM   1434 C CG    . TYR A 1 245 ? 76.476  81.934  104.222 1.00 81.52  ? 245 TYR A CG    1 
ATOM   1435 C CD1   . TYR A 1 245 ? 75.487  82.873  103.968 1.00 81.34  ? 245 TYR A CD1   1 
ATOM   1436 C CD2   . TYR A 1 245 ? 77.594  81.927  103.402 1.00 79.92  ? 245 TYR A CD2   1 
ATOM   1437 C CE1   . TYR A 1 245 ? 75.610  83.776  102.931 1.00 76.03  ? 245 TYR A CE1   1 
ATOM   1438 C CE2   . TYR A 1 245 ? 77.726  82.824  102.365 1.00 74.91  ? 245 TYR A CE2   1 
ATOM   1439 C CZ    . TYR A 1 245 ? 76.731  83.746  102.133 1.00 74.12  ? 245 TYR A CZ    1 
ATOM   1440 O OH    . TYR A 1 245 ? 76.862  84.642  101.099 1.00 74.86  ? 245 TYR A OH    1 
ATOM   1441 N N     . GLU A 1 246 ? 75.708  80.129  108.354 1.00 85.04  ? 246 GLU A N     1 
ATOM   1442 C CA    . GLU A 1 246 ? 75.535  79.120  109.388 1.00 78.70  ? 246 GLU A CA    1 
ATOM   1443 C C     . GLU A 1 246 ? 74.527  78.072  108.937 1.00 80.62  ? 246 GLU A C     1 
ATOM   1444 O O     . GLU A 1 246 ? 73.578  78.370  108.206 1.00 83.06  ? 246 GLU A O     1 
ATOM   1445 C CB    . GLU A 1 246 ? 75.076  79.747  110.712 1.00 78.54  ? 246 GLU A CB    1 
ATOM   1446 C CG    . GLU A 1 246 ? 73.646  80.263  110.697 1.00 83.73  ? 246 GLU A CG    1 
ATOM   1447 C CD    . GLU A 1 246 ? 73.409  81.357  111.716 1.00 93.30  ? 246 GLU A CD    1 
ATOM   1448 O OE1   . GLU A 1 246 ? 74.197  81.453  112.679 1.00 98.84  ? 246 GLU A OE1   1 
ATOM   1449 O OE2   . GLU A 1 246 ? 72.435  82.122  111.554 1.00 96.24  ? 246 GLU A OE2   1 
ATOM   1450 N N     . LEU A 1 247 ? 74.743  76.837  109.381 1.00 77.36  ? 247 LEU A N     1 
ATOM   1451 C CA    . LEU A 1 247 ? 73.888  75.725  108.992 1.00 73.44  ? 247 LEU A CA    1 
ATOM   1452 C C     . LEU A 1 247 ? 72.580  75.766  109.770 1.00 78.05  ? 247 LEU A C     1 
ATOM   1453 O O     . LEU A 1 247 ? 72.559  76.090  110.960 1.00 80.02  ? 247 LEU A O     1 
ATOM   1454 C CB    . LEU A 1 247 ? 74.596  74.395  109.248 1.00 69.42  ? 247 LEU A CB    1 
ATOM   1455 C CG    . LEU A 1 247 ? 74.337  73.218  108.301 1.00 72.11  ? 247 LEU A CG    1 
ATOM   1456 C CD1   . LEU A 1 247 ? 75.364  72.126  108.539 1.00 77.22  ? 247 LEU A CD1   1 
ATOM   1457 C CD2   . LEU A 1 247 ? 72.934  72.664  108.419 1.00 75.08  ? 247 LEU A CD2   1 
ATOM   1458 N N     . VAL A 1 248 ? 71.483  75.434  109.090 1.00 80.18  ? 248 VAL A N     1 
ATOM   1459 C CA    . VAL A 1 248 ? 70.176  75.277  109.721 1.00 79.16  ? 248 VAL A CA    1 
ATOM   1460 C C     . VAL A 1 248 ? 69.546  74.018  109.137 1.00 81.27  ? 248 VAL A C     1 
ATOM   1461 O O     . VAL A 1 248 ? 69.094  74.026  107.986 1.00 84.34  ? 248 VAL A O     1 
ATOM   1462 C CB    . VAL A 1 248 ? 69.261  76.492  109.502 1.00 82.10  ? 248 VAL A CB    1 
ATOM   1463 C CG1   . VAL A 1 248 ? 67.840  76.175  109.943 1.00 82.46  ? 248 VAL A CG1   1 
ATOM   1464 C CG2   . VAL A 1 248 ? 69.794  77.703  110.251 1.00 80.31  ? 248 VAL A CG2   1 
ATOM   1465 N N     . VAL A 1 249 ? 69.517  72.940  109.917 1.00 84.04  ? 249 VAL A N     1 
ATOM   1466 C CA    . VAL A 1 249 ? 68.969  71.675  109.444 1.00 82.68  ? 249 VAL A CA    1 
ATOM   1467 C C     . VAL A 1 249 ? 67.450  71.724  109.515 1.00 88.45  ? 249 VAL A C     1 
ATOM   1468 O O     . VAL A 1 249 ? 66.865  72.406  110.364 1.00 95.08  ? 249 VAL A O     1 
ATOM   1469 C CB    . VAL A 1 249 ? 69.524  70.492  110.264 1.00 82.64  ? 249 VAL A CB    1 
ATOM   1470 C CG1   . VAL A 1 249 ? 69.296  69.179  109.532 1.00 77.78  ? 249 VAL A CG1   1 
ATOM   1471 C CG2   . VAL A 1 249 ? 70.993  70.690  110.576 1.00 80.78  ? 249 VAL A CG2   1 
ATOM   1472 N N     . HIS A 1 250 ? 66.800  70.995  108.611 1.00 88.83  ? 250 HIS A N     1 
ATOM   1473 C CA    . HIS A 1 250 ? 65.352  70.849  108.617 1.00 98.64  ? 250 HIS A CA    1 
ATOM   1474 C C     . HIS A 1 250 ? 65.012  69.368  108.629 1.00 102.71 ? 250 HIS A C     1 
ATOM   1475 O O     . HIS A 1 250 ? 65.542  68.600  107.820 1.00 98.77  ? 250 HIS A O     1 
ATOM   1476 C CB    . HIS A 1 250 ? 64.719  71.538  107.405 1.00 96.86  ? 250 HIS A CB    1 
ATOM   1477 C CG    . HIS A 1 250 ? 64.696  73.031  107.505 1.00 97.50  ? 250 HIS A CG    1 
ATOM   1478 N ND1   . HIS A 1 250 ? 63.529  73.751  107.643 1.00 102.06 ? 250 HIS A ND1   1 
ATOM   1479 C CD2   . HIS A 1 250 ? 65.699  73.941  107.487 1.00 92.18  ? 250 HIS A CD2   1 
ATOM   1480 C CE1   . HIS A 1 250 ? 63.814  75.040  107.707 1.00 98.57  ? 250 HIS A CE1   1 
ATOM   1481 N NE2   . HIS A 1 250 ? 65.124  75.182  107.614 1.00 93.34  ? 250 HIS A NE2   1 
ATOM   1482 N N     . GLU A 1 251 ? 64.131  68.969  109.547 1.00 107.77 ? 251 GLU A N     1 
ATOM   1483 C CA    . GLU A 1 251 ? 63.752  67.569  109.708 1.00 115.24 ? 251 GLU A CA    1 
ATOM   1484 C C     . GLU A 1 251 ? 62.451  67.246  108.982 1.00 123.84 ? 251 GLU A C     1 
ATOM   1485 O O     . GLU A 1 251 ? 62.405  66.325  108.161 1.00 128.70 ? 251 GLU A O     1 
ATOM   1486 C CB    . GLU A 1 251 ? 63.637  67.225  111.199 1.00 116.38 ? 251 GLU A CB    1 
ATOM   1487 C CG    . GLU A 1 251 ? 64.952  67.311  111.957 1.00 116.37 ? 251 GLU A CG    1 
ATOM   1488 C CD    . GLU A 1 251 ? 65.230  68.705  112.485 1.00 118.26 ? 251 GLU A CD    1 
ATOM   1489 O OE1   . GLU A 1 251 ? 64.382  69.599  112.281 1.00 117.04 ? 251 GLU A OE1   1 
ATOM   1490 O OE2   . GLU A 1 251 ? 66.297  68.906  113.102 1.00 119.66 ? 251 GLU A OE2   1 
ATOM   1491 N N     . ASP A 1 252 ? 61.387  67.989  109.272 1.00 125.49 ? 252 ASP A N     1 
ATOM   1492 C CA    . ASP A 1 252 ? 60.092  67.808  108.625 1.00 125.49 ? 252 ASP A CA    1 
ATOM   1493 C C     . ASP A 1 252 ? 59.815  69.033  107.764 1.00 119.09 ? 252 ASP A C     1 
ATOM   1494 O O     . ASP A 1 252 ? 59.469  70.099  108.283 1.00 114.92 ? 252 ASP A O     1 
ATOM   1495 C CB    . ASP A 1 252 ? 58.987  67.597  109.657 1.00 128.14 ? 252 ASP A CB    1 
ATOM   1496 C CG    . ASP A 1 252 ? 59.433  66.737  110.822 1.00 129.47 ? 252 ASP A CG    1 
ATOM   1497 O OD1   . ASP A 1 252 ? 60.208  65.784  110.597 1.00 128.92 ? 252 ASP A OD1   1 
ATOM   1498 O OD2   . ASP A 1 252 ? 59.009  67.014  111.964 1.00 128.12 ? 252 ASP A OD2   1 
ATOM   1499 N N     . MET A 1 253 ? 59.968  68.879  106.451 1.00 119.13 ? 253 MET A N     1 
ATOM   1500 C CA    . MET A 1 253 ? 59.720  69.969  105.514 1.00 117.33 ? 253 MET A CA    1 
ATOM   1501 C C     . MET A 1 253 ? 59.306  69.372  104.181 1.00 117.35 ? 253 MET A C     1 
ATOM   1502 O O     . MET A 1 253 ? 60.055  68.583  103.596 1.00 114.95 ? 253 MET A O     1 
ATOM   1503 C CB    . MET A 1 253 ? 60.960  70.849  105.351 1.00 108.05 ? 253 MET A CB    1 
ATOM   1504 C CG    . MET A 1 253 ? 60.665  72.246  104.835 1.00 106.95 ? 253 MET A CG    1 
ATOM   1505 S SD    . MET A 1 253 ? 61.874  73.451  105.411 1.00 120.36 ? 253 MET A SD    1 
ATOM   1506 C CE    . MET A 1 253 ? 61.209  74.961  104.719 1.00 100.38 ? 253 MET A CE    1 
ATOM   1507 N N     . ASP A 1 254 ? 58.122  69.744  103.706 1.00 118.04 ? 254 ASP A N     1 
ATOM   1508 C CA    . ASP A 1 254 ? 57.624  69.221  102.445 1.00 114.85 ? 254 ASP A CA    1 
ATOM   1509 C C     . ASP A 1 254 ? 58.439  69.768  101.277 1.00 108.98 ? 254 ASP A C     1 
ATOM   1510 O O     . ASP A 1 254 ? 59.015  70.858  101.338 1.00 108.13 ? 254 ASP A O     1 
ATOM   1511 C CB    . ASP A 1 254 ? 56.147  69.570  102.264 1.00 116.98 ? 254 ASP A CB    1 
ATOM   1512 C CG    . ASP A 1 254 ? 55.490  68.769  101.157 1.00 120.18 ? 254 ASP A CG    1 
ATOM   1513 O OD1   . ASP A 1 254 ? 55.510  67.523  101.231 1.00 124.76 ? 254 ASP A OD1   1 
ATOM   1514 O OD2   . ASP A 1 254 ? 54.956  69.385  100.211 1.00 116.01 ? 254 ASP A OD2   1 
ATOM   1515 N N     . VAL A 1 255 ? 58.480  68.987  100.193 1.00 107.46 ? 255 VAL A N     1 
ATOM   1516 C CA    . VAL A 1 255 ? 59.205  69.394  98.990  1.00 105.80 ? 255 VAL A CA    1 
ATOM   1517 C C     . VAL A 1 255 ? 58.532  70.540  98.257  1.00 106.50 ? 255 VAL A C     1 
ATOM   1518 O O     . VAL A 1 255 ? 59.089  71.039  97.270  1.00 105.70 ? 255 VAL A O     1 
ATOM   1519 C CB    . VAL A 1 255 ? 59.373  68.207  98.021  1.00 107.34 ? 255 VAL A CB    1 
ATOM   1520 C CG1   . VAL A 1 255 ? 60.108  67.066  98.705  1.00 108.78 ? 255 VAL A CG1   1 
ATOM   1521 C CG2   . VAL A 1 255 ? 58.017  67.745  97.511  1.00 103.91 ? 255 VAL A CG2   1 
ATOM   1522 N N     . ALA A 1 256 ? 57.349  70.970  98.701  1.00 107.74 ? 256 ALA A N     1 
ATOM   1523 C CA    . ALA A 1 256 ? 56.670  72.084  98.047  1.00 107.34 ? 256 ALA A CA    1 
ATOM   1524 C C     . ALA A 1 256 ? 57.479  73.369  98.161  1.00 103.93 ? 256 ALA A C     1 
ATOM   1525 O O     . ALA A 1 256 ? 57.562  74.146  97.203  1.00 103.72 ? 256 ALA A O     1 
ATOM   1526 C CB    . ALA A 1 256 ? 55.275  72.272  98.643  1.00 106.12 ? 256 ALA A CB    1 
ATOM   1527 N N     . LYS A 1 257 ? 58.083  73.611  99.324  1.00 100.25 ? 257 LYS A N     1 
ATOM   1528 C CA    . LYS A 1 257 ? 58.877  74.810  99.561  1.00 97.82  ? 257 LYS A CA    1 
ATOM   1529 C C     . LYS A 1 257 ? 60.363  74.492  99.712  1.00 95.21  ? 257 LYS A C     1 
ATOM   1530 O O     . LYS A 1 257 ? 61.094  75.208  100.401 1.00 96.34  ? 257 LYS A O     1 
ATOM   1531 C CB    . LYS A 1 257 ? 58.350  75.564  100.782 1.00 98.50  ? 257 LYS A CB    1 
ATOM   1532 C CG    . LYS A 1 257 ? 58.486  74.823  102.102 1.00 99.18  ? 257 LYS A CG    1 
ATOM   1533 C CD    . LYS A 1 257 ? 57.947  75.659  103.254 1.00 98.51  ? 257 LYS A CD    1 
ATOM   1534 C CE    . LYS A 1 257 ? 58.553  77.054  103.259 1.00 96.61  ? 257 LYS A CE    1 
ATOM   1535 N NZ    . LYS A 1 257 ? 57.995  77.899  104.351 1.00 89.15  ? 257 LYS A NZ    1 
ATOM   1536 N N     . VAL A 1 258 ? 60.823  73.426  99.062  1.00 91.49  ? 258 VAL A N     1 
ATOM   1537 C CA    . VAL A 1 258 ? 62.233  73.056  99.028  1.00 84.84  ? 258 VAL A CA    1 
ATOM   1538 C C     . VAL A 1 258 ? 62.690  73.076  97.577  1.00 87.95  ? 258 VAL A C     1 
ATOM   1539 O O     . VAL A 1 258 ? 62.069  72.441  96.716  1.00 93.16  ? 258 VAL A O     1 
ATOM   1540 C CB    . VAL A 1 258 ? 62.471  71.676  99.665  1.00 84.27  ? 258 VAL A CB    1 
ATOM   1541 C CG1   . VAL A 1 258 ? 63.772  71.073  99.160  1.00 77.01  ? 258 VAL A CG1   1 
ATOM   1542 C CG2   . VAL A 1 258 ? 62.484  71.791  101.177 1.00 91.55  ? 258 VAL A CG2   1 
ATOM   1543 N N     . TYR A 1 259 ? 63.767  73.808  97.306  1.00 86.69  ? 259 TYR A N     1 
ATOM   1544 C CA    . TYR A 1 259 ? 64.269  73.930  95.945  1.00 84.84  ? 259 TYR A CA    1 
ATOM   1545 C C     . TYR A 1 259 ? 64.841  72.604  95.460  1.00 82.88  ? 259 TYR A C     1 
ATOM   1546 O O     . TYR A 1 259 ? 65.525  71.895  96.202  1.00 80.05  ? 259 TYR A O     1 
ATOM   1547 C CB    . TYR A 1 259 ? 65.336  75.021  95.869  1.00 79.68  ? 259 TYR A CB    1 
ATOM   1548 C CG    . TYR A 1 259 ? 64.781  76.423  95.951  1.00 76.04  ? 259 TYR A CG    1 
ATOM   1549 C CD1   . TYR A 1 259 ? 64.141  77.002  94.865  1.00 79.55  ? 259 TYR A CD1   1 
ATOM   1550 C CD2   . TYR A 1 259 ? 64.898  77.168  97.114  1.00 76.58  ? 259 TYR A CD2   1 
ATOM   1551 C CE1   . TYR A 1 259 ? 63.633  78.284  94.936  1.00 83.98  ? 259 TYR A CE1   1 
ATOM   1552 C CE2   . TYR A 1 259 ? 64.393  78.450  97.195  1.00 80.16  ? 259 TYR A CE2   1 
ATOM   1553 C CZ    . TYR A 1 259 ? 63.761  79.003  96.104  1.00 84.42  ? 259 TYR A CZ    1 
ATOM   1554 O OH    . TYR A 1 259 ? 63.257  80.281  96.183  1.00 88.45  ? 259 TYR A OH    1 
ATOM   1555 N N     . THR A 1 260 ? 64.558  72.274  94.203  1.00 79.84  ? 260 THR A N     1 
ATOM   1556 C CA    . THR A 1 260 ? 65.026  71.042  93.580  1.00 78.74  ? 260 THR A CA    1 
ATOM   1557 C C     . THR A 1 260 ? 65.676  71.344  92.235  1.00 81.84  ? 260 THR A C     1 
ATOM   1558 O O     . THR A 1 260 ? 65.471  70.635  91.246  1.00 83.89  ? 260 THR A O     1 
ATOM   1559 C CB    . THR A 1 260 ? 63.882  70.042  93.422  1.00 84.93  ? 260 THR A CB    1 
ATOM   1560 O OG1   . THR A 1 260 ? 63.031  70.111  94.572  1.00 89.89  ? 260 THR A OG1   1 
ATOM   1561 C CG2   . THR A 1 260 ? 64.424  68.621  93.309  1.00 88.56  ? 260 THR A CG2   1 
ATOM   1562 N N     . GLY A 1 261 ? 66.465  72.412  92.178  1.00 77.21  ? 261 GLY A N     1 
ATOM   1563 C CA    . GLY A 1 261 ? 67.160  72.807  90.965  1.00 68.23  ? 261 GLY A CA    1 
ATOM   1564 C C     . GLY A 1 261 ? 66.739  74.141  90.391  1.00 71.19  ? 261 GLY A C     1 
ATOM   1565 O O     . GLY A 1 261 ? 67.372  74.611  89.434  1.00 72.85  ? 261 GLY A O     1 
ATOM   1566 N N     . GLU A 1 262 ? 65.702  74.776  90.926  1.00 75.94  ? 262 GLU A N     1 
ATOM   1567 C CA    . GLU A 1 262 ? 65.251  76.053  90.398  1.00 81.82  ? 262 GLU A CA    1 
ATOM   1568 C C     . GLU A 1 262 ? 66.288  77.141  90.656  1.00 80.50  ? 262 GLU A C     1 
ATOM   1569 O O     . GLU A 1 262 ? 66.959  77.159  91.691  1.00 81.75  ? 262 GLU A O     1 
ATOM   1570 C CB    . GLU A 1 262 ? 63.913  76.444  91.025  1.00 84.73  ? 262 GLU A CB    1 
ATOM   1571 C CG    . GLU A 1 262 ? 62.795  75.441  90.778  1.00 87.80  ? 262 GLU A CG    1 
ATOM   1572 C CD    . GLU A 1 262 ? 62.754  74.338  91.819  1.00 92.70  ? 262 GLU A CD    1 
ATOM   1573 O OE1   . GLU A 1 262 ? 63.833  73.858  92.226  1.00 89.95  ? 262 GLU A OE1   1 
ATOM   1574 O OE2   . GLU A 1 262 ? 61.643  73.947  92.231  1.00 98.33  ? 262 GLU A OE2   1 
ATOM   1575 N N     . MET A 1 263 ? 66.415  78.054  89.695  1.00 72.85  ? 263 MET A N     1 
ATOM   1576 C CA    . MET A 1 263 ? 67.352  79.164  89.818  1.00 73.05  ? 263 MET A CA    1 
ATOM   1577 C C     . MET A 1 263 ? 66.700  80.407  90.408  1.00 76.67  ? 263 MET A C     1 
ATOM   1578 O O     . MET A 1 263 ? 67.316  81.098  91.227  1.00 76.66  ? 263 MET A O     1 
ATOM   1579 C CB    . MET A 1 263 ? 67.958  79.496  88.453  1.00 66.53  ? 263 MET A CB    1 
ATOM   1580 C CG    . MET A 1 263 ? 69.093  78.580  88.036  1.00 59.60  ? 263 MET A CG    1 
ATOM   1581 S SD    . MET A 1 263 ? 70.546  78.756  89.084  1.00 73.34  ? 263 MET A SD    1 
ATOM   1582 C CE    . MET A 1 263 ? 71.504  77.335  88.572  1.00 58.18  ? 263 MET A CE    1 
ATOM   1583 N N     . GLY A 1 264 ? 65.467  80.706  90.011  1.00 78.71  ? 264 GLY A N     1 
ATOM   1584 C CA    . GLY A 1 264 ? 64.795  81.898  90.487  1.00 85.07  ? 264 GLY A CA    1 
ATOM   1585 C C     . GLY A 1 264 ? 63.615  81.615  91.392  1.00 88.44  ? 264 GLY A C     1 
ATOM   1586 O O     . GLY A 1 264 ? 63.789  81.301  92.573  1.00 89.79  ? 264 GLY A O     1 
ATOM   1587 N N     . ARG A 1 265 ? 62.407  81.727  90.846  1.00 91.10  ? 265 ARG A N     1 
ATOM   1588 C CA    . ARG A 1 265 ? 61.199  81.540  91.631  1.00 95.37  ? 265 ARG A CA    1 
ATOM   1589 C C     . ARG A 1 265 ? 61.080  80.096  92.112  1.00 97.77  ? 265 ARG A C     1 
ATOM   1590 O O     . ARG A 1 265 ? 61.625  79.163  91.516  1.00 97.29  ? 265 ARG A O     1 
ATOM   1591 C CB    . ARG A 1 265 ? 59.965  81.923  90.813  1.00 98.87  ? 265 ARG A CB    1 
ATOM   1592 C CG    . ARG A 1 265 ? 58.755  82.315  91.646  1.00 102.30 ? 265 ARG A CG    1 
ATOM   1593 C CD    . ARG A 1 265 ? 59.075  83.459  92.596  1.00 109.02 ? 265 ARG A CD    1 
ATOM   1594 N NE    . ARG A 1 265 ? 59.800  84.540  91.937  1.00 121.96 ? 265 ARG A NE    1 
ATOM   1595 C CZ    . ARG A 1 265 ? 59.257  85.404  91.090  1.00 128.53 ? 265 ARG A CZ    1 
ATOM   1596 N NH1   . ARG A 1 265 ? 57.973  85.350  90.775  1.00 129.85 ? 265 ARG A NH1   1 
ATOM   1597 N NH2   . ARG A 1 265 ? 60.021  86.348  90.547  1.00 127.30 ? 265 ARG A NH2   1 
ATOM   1598 N N     . LEU A 1 266 ? 60.362  79.925  93.219  1.00 98.62  ? 266 LEU A N     1 
ATOM   1599 C CA    . LEU A 1 266 ? 60.132  78.597  93.769  1.00 96.80  ? 266 LEU A CA    1 
ATOM   1600 C C     . LEU A 1 266 ? 59.254  77.775  92.834  1.00 97.19  ? 266 LEU A C     1 
ATOM   1601 O O     . LEU A 1 266 ? 58.261  78.270  92.293  1.00 97.33  ? 266 LEU A O     1 
ATOM   1602 C CB    . LEU A 1 266 ? 59.480  78.703  95.146  1.00 94.35  ? 266 LEU A CB    1 
ATOM   1603 C CG    . LEU A 1 266 ? 59.348  77.414  95.957  1.00 90.97  ? 266 LEU A CG    1 
ATOM   1604 C CD1   . LEU A 1 266 ? 60.668  76.662  96.005  1.00 86.32  ? 266 LEU A CD1   1 
ATOM   1605 C CD2   . LEU A 1 266 ? 58.858  77.729  97.358  1.00 92.48  ? 266 LEU A CD2   1 
ATOM   1606 N N     . LYS A 1 267 ? 59.633  76.509  92.646  1.00 97.66  ? 267 LYS A N     1 
ATOM   1607 C CA    . LYS A 1 267 ? 58.916  75.580  91.771  1.00 98.60  ? 267 LYS A CA    1 
ATOM   1608 C C     . LYS A 1 267 ? 58.783  76.124  90.353  1.00 98.55  ? 267 LYS A C     1 
ATOM   1609 O O     . LYS A 1 267 ? 57.777  75.892  89.679  1.00 100.00 ? 267 LYS A O     1 
ATOM   1610 C CB    . LYS A 1 267 ? 57.537  75.227  92.340  1.00 98.50  ? 267 LYS A CB    1 
ATOM   1611 C CG    . LYS A 1 267 ? 57.552  74.805  93.802  1.00 101.02 ? 267 LYS A CG    1 
ATOM   1612 C CD    . LYS A 1 267 ? 58.484  73.625  94.037  1.00 102.05 ? 267 LYS A CD    1 
ATOM   1613 C CE    . LYS A 1 267 ? 58.072  72.412  93.216  1.00 103.67 ? 267 LYS A CE    1 
ATOM   1614 N NZ    . LYS A 1 267 ? 58.957  71.243  93.475  1.00 105.52 ? 267 LYS A NZ    1 
ATOM   1615 N N     . SER A 1 268 ? 59.800  76.854  89.889  1.00 97.05  ? 268 SER A N     1 
ATOM   1616 C CA    . SER A 1 268 ? 59.749  77.420  88.546  1.00 95.58  ? 268 SER A CA    1 
ATOM   1617 C C     . SER A 1 268 ? 59.843  76.344  87.474  1.00 93.04  ? 268 SER A C     1 
ATOM   1618 O O     . SER A 1 268 ? 59.195  76.457  86.430  1.00 90.75  ? 268 SER A O     1 
ATOM   1619 C CB    . SER A 1 268 ? 60.867  78.445  88.365  1.00 92.92  ? 268 SER A CB    1 
ATOM   1620 O OG    . SER A 1 268 ? 62.139  77.830  88.459  1.00 92.36  ? 268 SER A OG    1 
ATOM   1621 N N     . TYR A 1 269 ? 60.625  75.291  87.716  1.00 93.66  ? 269 TYR A N     1 
ATOM   1622 C CA    . TYR A 1 269 ? 60.866  74.271  86.703  1.00 91.96  ? 269 TYR A CA    1 
ATOM   1623 C C     . TYR A 1 269 ? 59.624  73.456  86.365  1.00 95.63  ? 269 TYR A C     1 
ATOM   1624 O O     . TYR A 1 269 ? 59.645  72.717  85.376  1.00 92.74  ? 269 TYR A O     1 
ATOM   1625 C CB    . TYR A 1 269 ? 61.982  73.333  87.165  1.00 88.40  ? 269 TYR A CB    1 
ATOM   1626 C CG    . TYR A 1 269 ? 63.375  73.798  86.804  1.00 81.74  ? 269 TYR A CG    1 
ATOM   1627 C CD1   . TYR A 1 269 ? 63.665  75.147  86.661  1.00 76.65  ? 269 TYR A CD1   1 
ATOM   1628 C CD2   . TYR A 1 269 ? 64.403  72.885  86.618  1.00 76.69  ? 269 TYR A CD2   1 
ATOM   1629 C CE1   . TYR A 1 269 ? 64.937  75.573  86.336  1.00 67.32  ? 269 TYR A CE1   1 
ATOM   1630 C CE2   . TYR A 1 269 ? 65.677  73.302  86.294  1.00 71.35  ? 269 TYR A CE2   1 
ATOM   1631 C CZ    . TYR A 1 269 ? 65.939  74.646  86.154  1.00 64.66  ? 269 TYR A CZ    1 
ATOM   1632 O OH    . TYR A 1 269 ? 67.209  75.062  85.832  1.00 55.30  ? 269 TYR A OH    1 
ATOM   1633 N N     . GLU A 1 270 ? 58.554  73.565  87.153  1.00 98.76  ? 270 GLU A N     1 
ATOM   1634 C CA    . GLU A 1 270 ? 57.331  72.805  86.916  1.00 99.32  ? 270 GLU A CA    1 
ATOM   1635 C C     . GLU A 1 270 ? 56.316  73.591  86.091  1.00 99.89  ? 270 GLU A C     1 
ATOM   1636 O O     . GLU A 1 270 ? 55.899  73.139  85.021  1.00 99.01  ? 270 GLU A O     1 
ATOM   1637 C CB    . GLU A 1 270 ? 56.714  72.375  88.253  1.00 100.84 ? 270 GLU A CB    1 
ATOM   1638 C CG    . GLU A 1 270 ? 57.710  71.756  89.218  1.00 104.88 ? 270 GLU A CG    1 
ATOM   1639 C CD    . GLU A 1 270 ? 58.572  70.697  88.561  1.00 109.56 ? 270 GLU A CD    1 
ATOM   1640 O OE1   . GLU A 1 270 ? 58.013  69.688  88.080  1.00 109.85 ? 270 GLU A OE1   1 
ATOM   1641 O OE2   . GLU A 1 270 ? 59.807  70.873  88.522  1.00 111.68 ? 270 GLU A OE2   1 
ATOM   1642 N N     . ASN A 1 271 ? 55.911  74.763  86.571  1.00 100.93 ? 271 ASN A N     1 
ATOM   1643 C CA    . ASN A 1 271 ? 54.916  75.599  85.900  1.00 101.50 ? 271 ASN A CA    1 
ATOM   1644 C C     . ASN A 1 271 ? 55.572  76.931  85.546  1.00 97.17  ? 271 ASN A C     1 
ATOM   1645 O O     . ASN A 1 271 ? 55.554  77.877  86.337  1.00 95.50  ? 271 ASN A O     1 
ATOM   1646 C CB    . ASN A 1 271 ? 53.679  75.791  86.778  1.00 105.04 ? 271 ASN A CB    1 
ATOM   1647 C CG    . ASN A 1 271 ? 54.028  76.020  88.233  1.00 102.45 ? 271 ASN A CG    1 
ATOM   1648 O OD1   . ASN A 1 271 ? 55.201  76.096  88.595  1.00 99.94  ? 271 ASN A OD1   1 
ATOM   1649 N ND2   . ASN A 1 271 ? 53.009  76.129  89.077  1.00 102.79 ? 271 ASN A ND2   1 
ATOM   1650 N N     . GLN A 1 272 ? 56.148  76.999  84.350  1.00 96.20  ? 272 GLN A N     1 
ATOM   1651 C CA    . GLN A 1 272 ? 56.835  78.200  83.900  1.00 97.05  ? 272 GLN A CA    1 
ATOM   1652 C C     . GLN A 1 272 ? 55.870  79.217  83.307  1.00 95.71  ? 272 GLN A C     1 
ATOM   1653 O O     . GLN A 1 272 ? 54.858  78.860  82.698  1.00 97.08  ? 272 GLN A O     1 
ATOM   1654 C CB    . GLN A 1 272 ? 57.903  77.849  82.867  1.00 93.59  ? 272 GLN A CB    1 
ATOM   1655 C CG    . GLN A 1 272 ? 59.111  77.161  83.446  1.00 91.10  ? 272 GLN A CG    1 
ATOM   1656 C CD    . GLN A 1 272 ? 60.239  77.069  82.453  1.00 84.92  ? 272 GLN A CD    1 
ATOM   1657 O OE1   . GLN A 1 272 ? 61.376  76.782  82.812  1.00 86.95  ? 272 GLN A OE1   1 
ATOM   1658 N NE2   . GLN A 1 272 ? 59.924  77.285  81.187  1.00 82.56  ? 272 GLN A NE2   1 
ATOM   1659 N N     . LYS A 1 273 ? 56.200  80.491  83.487  1.00 90.80  ? 273 LYS A N     1 
ATOM   1660 C CA    . LYS A 1 273 ? 55.482  81.611  82.905  1.00 91.69  ? 273 LYS A CA    1 
ATOM   1661 C C     . LYS A 1 273 ? 56.471  82.537  82.214  1.00 90.11  ? 273 LYS A C     1 
ATOM   1662 O O     . LYS A 1 273 ? 57.615  82.672  82.659  1.00 93.08  ? 273 LYS A O     1 
ATOM   1663 C CB    . LYS A 1 273 ? 54.707  82.396  83.975  1.00 93.12  ? 273 LYS A CB    1 
ATOM   1664 C CG    . LYS A 1 273 ? 54.162  81.544  85.113  1.00 92.22  ? 273 LYS A CG    1 
ATOM   1665 C CD    . LYS A 1 273 ? 52.976  80.705  84.666  1.00 94.71  ? 273 LYS A CD    1 
ATOM   1666 C CE    . LYS A 1 273 ? 51.831  81.576  84.178  1.00 94.45  ? 273 LYS A CE    1 
ATOM   1667 N NZ    . LYS A 1 273 ? 50.852  80.796  83.372  1.00 89.77  ? 273 LYS A NZ    1 
ATOM   1668 N N     . PRO A 1 274 ? 56.062  83.184  81.128  1.00 86.80  ? 274 PRO A N     1 
ATOM   1669 C CA    . PRO A 1 274 ? 56.954  84.125  80.443  1.00 85.34  ? 274 PRO A CA    1 
ATOM   1670 C C     . PRO A 1 274 ? 57.082  85.415  81.232  1.00 89.22  ? 274 PRO A C     1 
ATOM   1671 O O     . PRO A 1 274 ? 56.219  85.726  82.066  1.00 86.82  ? 274 PRO A O     1 
ATOM   1672 C CB    . PRO A 1 274 ? 56.249  84.359  79.099  1.00 87.22  ? 274 PRO A CB    1 
ATOM   1673 C CG    . PRO A 1 274 ? 54.810  84.117  79.394  1.00 87.99  ? 274 PRO A CG    1 
ATOM   1674 C CD    . PRO A 1 274 ? 54.777  83.023  80.425  1.00 87.03  ? 274 PRO A CD    1 
ATOM   1675 N N     . PRO A 1 275 ? 58.147  86.200  81.004  1.00 94.57  ? 275 PRO A N     1 
ATOM   1676 C CA    . PRO A 1 275 ? 59.267  85.989  80.074  1.00 90.11  ? 275 PRO A CA    1 
ATOM   1677 C C     . PRO A 1 275 ? 60.343  85.074  80.645  1.00 84.97  ? 275 PRO A C     1 
ATOM   1678 O O     . PRO A 1 275 ? 60.306  84.725  81.820  1.00 81.03  ? 275 PRO A O     1 
ATOM   1679 C CB    . PRO A 1 275 ? 59.787  87.413  79.855  1.00 87.56  ? 275 PRO A CB    1 
ATOM   1680 C CG    . PRO A 1 275 ? 59.566  88.071  81.184  1.00 89.58  ? 275 PRO A CG    1 
ATOM   1681 C CD    . PRO A 1 275 ? 58.269  87.491  81.707  1.00 94.72  ? 275 PRO A CD    1 
ATOM   1682 N N     . PHE A 1 276 ? 61.317  84.669  79.834  1.00 80.56  ? 276 PHE A N     1 
ATOM   1683 C CA    . PHE A 1 276 ? 62.375  83.767  80.266  1.00 76.85  ? 276 PHE A CA    1 
ATOM   1684 C C     . PHE A 1 276 ? 63.732  84.398  79.990  1.00 76.81  ? 276 PHE A C     1 
ATOM   1685 O O     . PHE A 1 276 ? 63.996  84.849  78.871  1.00 80.25  ? 276 PHE A O     1 
ATOM   1686 C CB    . PHE A 1 276 ? 62.259  82.415  79.560  1.00 75.71  ? 276 PHE A CB    1 
ATOM   1687 C CG    . PHE A 1 276 ? 60.928  81.754  79.752  1.00 77.42  ? 276 PHE A CG    1 
ATOM   1688 C CD1   . PHE A 1 276 ? 60.682  80.978  80.869  1.00 76.44  ? 276 PHE A CD1   1 
ATOM   1689 C CD2   . PHE A 1 276 ? 59.920  81.913  78.817  1.00 80.74  ? 276 PHE A CD2   1 
ATOM   1690 C CE1   . PHE A 1 276 ? 59.457  80.376  81.051  1.00 78.33  ? 276 PHE A CE1   1 
ATOM   1691 C CE2   . PHE A 1 276 ? 58.693  81.308  78.993  1.00 81.70  ? 276 PHE A CE2   1 
ATOM   1692 C CZ    . PHE A 1 276 ? 58.462  80.538  80.112  1.00 81.40  ? 276 PHE A CZ    1 
ATOM   1693 N N     . ASP A 1 277 ? 64.585  84.420  81.006  1.00 76.51  ? 277 ASP A N     1 
ATOM   1694 C CA    . ASP A 1 277 ? 65.902  85.040  80.914  1.00 77.51  ? 277 ASP A CA    1 
ATOM   1695 C C     . ASP A 1 277 ? 66.843  84.286  81.847  1.00 74.91  ? 277 ASP A C     1 
ATOM   1696 O O     . ASP A 1 277 ? 66.574  83.141  82.226  1.00 75.19  ? 277 ASP A O     1 
ATOM   1697 C CB    . ASP A 1 277 ? 65.816  86.544  81.227  1.00 81.13  ? 277 ASP A CB    1 
ATOM   1698 C CG    . ASP A 1 277 ? 65.084  86.833  82.521  1.00 90.27  ? 277 ASP A CG    1 
ATOM   1699 O OD1   . ASP A 1 277 ? 64.684  85.873  83.211  1.00 87.31  ? 277 ASP A OD1   1 
ATOM   1700 O OD2   . ASP A 1 277 ? 64.909  88.024  82.849  1.00 98.32  ? 277 ASP A OD2   1 
ATOM   1701 N N     . ALA A 1 278 ? 67.960  84.923  82.207  1.00 72.18  ? 278 ALA A N     1 
ATOM   1702 C CA    . ALA A 1 278 ? 68.949  84.271  83.060  1.00 69.83  ? 278 ALA A CA    1 
ATOM   1703 C C     . ALA A 1 278 ? 68.357  83.880  84.408  1.00 71.60  ? 278 ALA A C     1 
ATOM   1704 O O     . ALA A 1 278 ? 68.690  82.824  84.958  1.00 69.21  ? 278 ALA A O     1 
ATOM   1705 C CB    . ALA A 1 278 ? 70.155  85.188  83.257  1.00 75.99  ? 278 ALA A CB    1 
ATOM   1706 N N     . LYS A 1 279 ? 67.483  84.722  84.963  1.00 78.25  ? 279 LYS A N     1 
ATOM   1707 C CA    . LYS A 1 279 ? 66.905  84.432  86.270  1.00 79.69  ? 279 LYS A CA    1 
ATOM   1708 C C     . LYS A 1 279 ? 65.814  83.371  86.199  1.00 78.04  ? 279 LYS A C     1 
ATOM   1709 O O     . LYS A 1 279 ? 65.626  82.620  87.161  1.00 80.87  ? 279 LYS A O     1 
ATOM   1710 C CB    . LYS A 1 279 ? 66.353  85.713  86.897  1.00 84.17  ? 279 LYS A CB    1 
ATOM   1711 C CG    . LYS A 1 279 ? 67.423  86.676  87.400  1.00 87.94  ? 279 LYS A CG    1 
ATOM   1712 C CD    . LYS A 1 279 ? 68.549  85.958  88.135  1.00 89.71  ? 279 LYS A CD    1 
ATOM   1713 C CE    . LYS A 1 279 ? 68.083  85.387  89.467  1.00 89.39  ? 279 LYS A CE    1 
ATOM   1714 N NZ    . LYS A 1 279 ? 69.122  84.519  90.088  1.00 86.49  ? 279 LYS A NZ    1 
ATOM   1715 N N     . ASN A 1 280 ? 65.086  83.296  85.086  1.00 74.05  ? 280 ASN A N     1 
ATOM   1716 C CA    . ASN A 1 280 ? 64.000  82.333  84.904  1.00 71.96  ? 280 ASN A CA    1 
ATOM   1717 C C     . ASN A 1 280 ? 64.202  81.612  83.579  1.00 72.10  ? 280 ASN A C     1 
ATOM   1718 O O     . ASN A 1 280 ? 63.547  81.932  82.579  1.00 76.35  ? 280 ASN A O     1 
ATOM   1719 C CB    . ASN A 1 280 ? 62.636  83.022  84.954  1.00 75.72  ? 280 ASN A CB    1 
ATOM   1720 C CG    . ASN A 1 280 ? 61.483  82.041  84.887  1.00 78.62  ? 280 ASN A CG    1 
ATOM   1721 O OD1   . ASN A 1 280 ? 61.674  80.830  84.987  1.00 73.82  ? 280 ASN A OD1   1 
ATOM   1722 N ND2   . ASN A 1 280 ? 60.275  82.563  84.715  1.00 88.03  ? 280 ASN A ND2   1 
ATOM   1723 N N     . PRO A 1 281 ? 65.102  80.635  83.533  1.00 66.07  ? 281 PRO A N     1 
ATOM   1724 C CA    . PRO A 1 281 ? 65.327  79.902  82.284  1.00 67.43  ? 281 PRO A CA    1 
ATOM   1725 C C     . PRO A 1 281 ? 64.125  79.053  81.903  1.00 69.39  ? 281 PRO A C     1 
ATOM   1726 O O     . PRO A 1 281 ? 63.305  78.680  82.743  1.00 76.66  ? 281 PRO A O     1 
ATOM   1727 C CB    . PRO A 1 281 ? 66.544  79.028  82.601  1.00 63.00  ? 281 PRO A CB    1 
ATOM   1728 C CG    . PRO A 1 281 ? 66.510  78.871  84.078  1.00 59.77  ? 281 PRO A CG    1 
ATOM   1729 C CD    . PRO A 1 281 ? 65.981  80.164  84.615  1.00 62.79  ? 281 PRO A CD    1 
ATOM   1730 N N     . PHE A 1 282 ? 64.026  78.765  80.608  1.00 64.81  ? 282 PHE A N     1 
ATOM   1731 C CA    . PHE A 1 282 ? 62.994  77.898  80.052  1.00 68.27  ? 282 PHE A CA    1 
ATOM   1732 C C     . PHE A 1 282 ? 63.603  76.548  79.701  1.00 71.24  ? 282 PHE A C     1 
ATOM   1733 O O     . PHE A 1 282 ? 64.610  76.489  78.988  1.00 73.67  ? 282 PHE A O     1 
ATOM   1734 C CB    . PHE A 1 282 ? 62.370  78.535  78.808  1.00 69.24  ? 282 PHE A CB    1 
ATOM   1735 C CG    . PHE A 1 282 ? 61.665  77.557  77.905  1.00 70.38  ? 282 PHE A CG    1 
ATOM   1736 C CD1   . PHE A 1 282 ? 60.375  77.141  78.176  1.00 74.93  ? 282 PHE A CD1   1 
ATOM   1737 C CD2   . PHE A 1 282 ? 62.295  77.063  76.775  1.00 66.58  ? 282 PHE A CD2   1 
ATOM   1738 C CE1   . PHE A 1 282 ? 59.731  76.245  77.347  1.00 71.80  ? 282 PHE A CE1   1 
ATOM   1739 C CE2   . PHE A 1 282 ? 61.656  76.168  75.944  1.00 69.46  ? 282 PHE A CE2   1 
ATOM   1740 C CZ    . PHE A 1 282 ? 60.373  75.759  76.230  1.00 71.86  ? 282 PHE A CZ    1 
ATOM   1741 N N     . LEU A 1 283 ? 62.993  75.466  80.188  1.00 70.80  ? 283 LEU A N     1 
ATOM   1742 C CA    . LEU A 1 283 ? 63.482  74.131  79.854  1.00 70.54  ? 283 LEU A CA    1 
ATOM   1743 C C     . LEU A 1 283 ? 63.000  73.765  78.458  1.00 73.36  ? 283 LEU A C     1 
ATOM   1744 O O     . LEU A 1 283 ? 61.800  73.575  78.235  1.00 74.11  ? 283 LEU A O     1 
ATOM   1745 C CB    . LEU A 1 283 ? 63.040  73.077  80.867  1.00 66.75  ? 283 LEU A CB    1 
ATOM   1746 C CG    . LEU A 1 283 ? 63.019  73.316  82.376  1.00 70.10  ? 283 LEU A CG    1 
ATOM   1747 C CD1   . LEU A 1 283 ? 61.664  73.817  82.818  1.00 76.12  ? 283 LEU A CD1   1 
ATOM   1748 C CD2   . LEU A 1 283 ? 63.401  72.049  83.125  1.00 76.48  ? 283 LEU A CD2   1 
ATOM   1749 N N     . ALA A 1 284 ? 63.934  73.668  77.521  1.00 69.61  ? 284 ALA A N     1 
ATOM   1750 C CA    . ALA A 1 284 ? 63.639  73.211  76.176  1.00 70.07  ? 284 ALA A CA    1 
ATOM   1751 C C     . ALA A 1 284 ? 63.664  71.688  76.123  1.00 72.42  ? 284 ALA A C     1 
ATOM   1752 O O     . ALA A 1 284 ? 64.172  71.016  77.022  1.00 74.79  ? 284 ALA A O     1 
ATOM   1753 C CB    . ALA A 1 284 ? 64.639  73.800  75.182  1.00 70.30  ? 284 ALA A CB    1 
ATOM   1754 N N     . ALA A 1 285 ? 63.102  71.140  75.053  1.00 69.40  ? 285 ALA A N     1 
ATOM   1755 C CA    . ALA A 1 285 ? 63.086  69.702  74.823  1.00 65.86  ? 285 ALA A CA    1 
ATOM   1756 C C     . ALA A 1 285 ? 64.037  69.387  73.679  1.00 62.06  ? 285 ALA A C     1 
ATOM   1757 O O     . ALA A 1 285 ? 63.865  69.896  72.567  1.00 65.15  ? 285 ALA A O     1 
ATOM   1758 C CB    . ALA A 1 285 ? 61.675  69.211  74.505  1.00 67.74  ? 285 ALA A CB    1 
ATOM   1759 N N     . VAL A 1 286 ? 65.034  68.548  73.950  1.00 59.29  ? 286 VAL A N     1 
ATOM   1760 C CA    . VAL A 1 286 ? 66.009  68.186  72.927  1.00 61.73  ? 286 VAL A CA    1 
ATOM   1761 C C     . VAL A 1 286 ? 65.311  67.279  71.917  1.00 66.56  ? 286 VAL A C     1 
ATOM   1762 O O     . VAL A 1 286 ? 65.061  66.102  72.193  1.00 76.55  ? 286 VAL A O     1 
ATOM   1763 C CB    . VAL A 1 286 ? 67.238  67.504  73.535  1.00 60.17  ? 286 VAL A CB    1 
ATOM   1764 C CG1   . VAL A 1 286 ? 68.135  66.952  72.440  1.00 60.32  ? 286 VAL A CG1   1 
ATOM   1765 C CG2   . VAL A 1 286 ? 68.000  68.479  74.409  1.00 56.79  ? 286 VAL A CG2   1 
ATOM   1766 N N     . THR A 1 287 ? 64.984  67.830  70.747  1.00 59.95  ? 287 THR A N     1 
ATOM   1767 C CA    . THR A 1 287 ? 64.306  67.042  69.725  1.00 65.86  ? 287 THR A CA    1 
ATOM   1768 C C     . THR A 1 287 ? 65.243  66.005  69.120  1.00 71.99  ? 287 THR A C     1 
ATOM   1769 O O     . THR A 1 287 ? 64.883  64.830  68.988  1.00 76.67  ? 287 THR A O     1 
ATOM   1770 C CB    . THR A 1 287 ? 63.750  67.956  68.635  1.00 67.37  ? 287 THR A CB    1 
ATOM   1771 O OG1   . THR A 1 287 ? 64.818  68.387  67.784  1.00 63.29  ? 287 THR A OG1   1 
ATOM   1772 C CG2   . THR A 1 287 ? 63.080  69.168  69.251  1.00 65.95  ? 287 THR A CG2   1 
ATOM   1773 N N     . ALA A 1 288 ? 66.452  66.419  68.750  1.00 65.61  ? 288 ALA A N     1 
ATOM   1774 C CA    . ALA A 1 288 ? 67.394  65.503  68.127  1.00 66.24  ? 288 ALA A CA    1 
ATOM   1775 C C     . ALA A 1 288 ? 68.810  66.015  68.336  1.00 57.20  ? 288 ALA A C     1 
ATOM   1776 O O     . ALA A 1 288 ? 69.030  67.192  68.627  1.00 57.64  ? 288 ALA A O     1 
ATOM   1777 C CB    . ALA A 1 288 ? 67.101  65.328  66.634  1.00 70.61  ? 288 ALA A CB    1 
ATOM   1778 N N     . ASN A 1 289 ? 69.765  65.103  68.184  1.00 58.03  ? 289 ASN A N     1 
ATOM   1779 C CA    . ASN A 1 289 ? 71.180  65.442  68.217  1.00 53.44  ? 289 ASN A CA    1 
ATOM   1780 C C     . ASN A 1 289 ? 71.952  64.370  67.461  1.00 53.34  ? 289 ASN A C     1 
ATOM   1781 O O     . ASN A 1 289 ? 71.461  63.256  67.260  1.00 62.10  ? 289 ASN A O     1 
ATOM   1782 C CB    . ASN A 1 289 ? 71.673  65.650  69.665  1.00 51.56  ? 289 ASN A CB    1 
ATOM   1783 C CG    . ASN A 1 289 ? 72.265  64.397  70.315  1.00 58.44  ? 289 ASN A CG    1 
ATOM   1784 O OD1   . ASN A 1 289 ? 72.017  63.262  69.908  1.00 71.16  ? 289 ASN A OD1   1 
ATOM   1785 N ND2   . ASN A 1 289 ? 73.064  64.617  71.352  1.00 51.17  ? 289 ASN A ND2   1 
ATOM   1786 N N     . ARG A 1 290 ? 73.159  64.723  67.027  1.00 48.79  ? 290 ARG A N     1 
ATOM   1787 C CA    . ARG A 1 290 ? 73.949  63.801  66.223  1.00 54.40  ? 290 ARG A CA    1 
ATOM   1788 C C     . ARG A 1 290 ? 75.422  64.161  66.332  1.00 51.79  ? 290 ARG A C     1 
ATOM   1789 O O     . ARG A 1 290 ? 75.783  65.261  66.757  1.00 56.22  ? 290 ARG A O     1 
ATOM   1790 C CB    . ARG A 1 290 ? 73.508  63.813  64.756  1.00 56.80  ? 290 ARG A CB    1 
ATOM   1791 C CG    . ARG A 1 290 ? 74.049  64.984  63.957  1.00 62.69  ? 290 ARG A CG    1 
ATOM   1792 C CD    . ARG A 1 290 ? 73.156  65.315  62.772  1.00 68.10  ? 290 ARG A CD    1 
ATOM   1793 N NE    . ARG A 1 290 ? 71.816  65.710  63.187  1.00 79.01  ? 290 ARG A NE    1 
ATOM   1794 C CZ    . ARG A 1 290 ? 71.107  66.671  62.611  1.00 77.72  ? 290 ARG A CZ    1 
ATOM   1795 N NH1   . ARG A 1 290 ? 71.584  67.365  61.591  1.00 64.16  ? 290 ARG A NH1   1 
ATOM   1796 N NH2   . ARG A 1 290 ? 69.890  66.945  63.071  1.00 81.73  ? 290 ARG A NH2   1 
ATOM   1797 N N     . LYS A 1 291 ? 76.266  63.212  65.938  1.00 53.43  ? 291 LYS A N     1 
ATOM   1798 C CA    . LYS A 1 291 ? 77.714  63.407  65.903  1.00 56.33  ? 291 LYS A CA    1 
ATOM   1799 C C     . LYS A 1 291 ? 78.089  63.863  64.499  1.00 59.71  ? 291 LYS A C     1 
ATOM   1800 O O     . LYS A 1 291 ? 78.102  63.068  63.557  1.00 66.83  ? 291 LYS A O     1 
ATOM   1801 C CB    . LYS A 1 291 ? 78.439  62.125  66.290  1.00 62.02  ? 291 LYS A CB    1 
ATOM   1802 C CG    . LYS A 1 291 ? 79.945  62.202  66.154  1.00 67.45  ? 291 LYS A CG    1 
ATOM   1803 C CD    . LYS A 1 291 ? 80.613  61.024  66.836  1.00 73.24  ? 291 LYS A CD    1 
ATOM   1804 C CE    . LYS A 1 291 ? 82.122  61.153  66.797  1.00 77.75  ? 291 LYS A CE    1 
ATOM   1805 N NZ    . LYS A 1 291 ? 82.794  60.068  67.560  1.00 84.21  ? 291 LYS A NZ    1 
ATOM   1806 N N     . LEU A 1 292 ? 78.394  65.154  64.359  1.00 60.77  ? 292 LEU A N     1 
ATOM   1807 C CA    . LEU A 1 292 ? 78.637  65.727  63.039  1.00 65.34  ? 292 LEU A CA    1 
ATOM   1808 C C     . LEU A 1 292 ? 79.910  65.174  62.414  1.00 73.98  ? 292 LEU A C     1 
ATOM   1809 O O     . LEU A 1 292 ? 79.902  64.718  61.265  1.00 83.75  ? 292 LEU A O     1 
ATOM   1810 C CB    . LEU A 1 292 ? 78.715  67.246  63.144  1.00 64.43  ? 292 LEU A CB    1 
ATOM   1811 C CG    . LEU A 1 292 ? 77.431  67.922  63.607  1.00 62.20  ? 292 LEU A CG    1 
ATOM   1812 C CD1   . LEU A 1 292 ? 77.717  69.363  63.959  1.00 68.16  ? 292 LEU A CD1   1 
ATOM   1813 C CD2   . LEU A 1 292 ? 76.362  67.822  62.536  1.00 60.46  ? 292 LEU A CD2   1 
ATOM   1814 N N     . ASN A 1 293 ? 81.014  65.209  63.152  1.00 69.44  ? 293 ASN A N     1 
ATOM   1815 C CA    . ASN A 1 293 ? 82.291  64.793  62.596  1.00 82.89  ? 293 ASN A CA    1 
ATOM   1816 C C     . ASN A 1 293 ? 82.313  63.287  62.359  1.00 92.62  ? 293 ASN A C     1 
ATOM   1817 O O     . ASN A 1 293 ? 81.737  62.504  63.119  1.00 89.63  ? 293 ASN A O     1 
ATOM   1818 C CB    . ASN A 1 293 ? 83.434  65.204  63.523  1.00 81.82  ? 293 ASN A CB    1 
ATOM   1819 C CG    . ASN A 1 293 ? 83.512  64.347  64.765  1.00 85.18  ? 293 ASN A CG    1 
ATOM   1820 O OD1   . ASN A 1 293 ? 82.502  64.091  65.418  1.00 83.12  ? 293 ASN A OD1   1 
ATOM   1821 N ND2   . ASN A 1 293 ? 84.716  63.903  65.104  1.00 92.26  ? 293 ASN A ND2   1 
ATOM   1822 N N     . GLN A 1 294 ? 82.983  62.887  61.279  1.00 100.54 ? 294 GLN A N     1 
ATOM   1823 C CA    . GLN A 1 294 ? 83.069  61.480  60.911  1.00 99.42  ? 294 GLN A CA    1 
ATOM   1824 C C     . GLN A 1 294 ? 84.155  60.731  61.669  1.00 100.84 ? 294 GLN A C     1 
ATOM   1825 O O     . GLN A 1 294 ? 84.175  59.497  61.629  1.00 99.82  ? 294 GLN A O     1 
ATOM   1826 C CB    . GLN A 1 294 ? 83.307  61.350  59.404  1.00 107.52 ? 294 GLN A CB    1 
ATOM   1827 C CG    . GLN A 1 294 ? 82.712  62.482  58.576  1.00 108.72 ? 294 GLN A CG    1 
ATOM   1828 C CD    . GLN A 1 294 ? 81.194  62.525  58.627  1.00 105.48 ? 294 GLN A CD    1 
ATOM   1829 O OE1   . GLN A 1 294 ? 80.544  61.561  59.032  1.00 100.62 ? 294 GLN A OE1   1 
ATOM   1830 N NE2   . GLN A 1 294 ? 80.622  63.651  58.217  1.00 106.10 ? 294 GLN A NE2   1 
ATOM   1831 N N     . GLY A 1 295 ? 85.051  61.437  62.353  1.00 102.52 ? 295 GLY A N     1 
ATOM   1832 C CA    . GLY A 1 295 ? 86.094  60.804  63.127  1.00 104.54 ? 295 GLY A CA    1 
ATOM   1833 C C     . GLY A 1 295 ? 85.606  60.389  64.502  1.00 101.75 ? 295 GLY A C     1 
ATOM   1834 O O     . GLY A 1 295 ? 84.411  60.363  64.797  1.00 97.79  ? 295 GLY A O     1 
ATOM   1835 N N     . THR A 1 296 ? 86.569  60.047  65.359  1.00 104.76 ? 296 THR A N     1 
ATOM   1836 C CA    . THR A 1 296 ? 86.250  59.645  66.723  1.00 104.48 ? 296 THR A CA    1 
ATOM   1837 C C     . THR A 1 296 ? 87.140  60.268  67.788  1.00 107.09 ? 296 THR A C     1 
ATOM   1838 O O     . THR A 1 296 ? 86.838  60.103  68.973  1.00 104.57 ? 296 THR A O     1 
ATOM   1839 C CB    . THR A 1 296 ? 86.313  58.116  66.861  1.00 110.26 ? 296 THR A CB    1 
ATOM   1840 O OG1   . THR A 1 296 ? 86.042  57.745  68.219  1.00 120.39 ? 296 THR A OG1   1 
ATOM   1841 C CG2   . THR A 1 296 ? 87.685  57.600  66.462  1.00 110.63 ? 296 THR A CG2   1 
ATOM   1842 N N     . GLU A 1 297 ? 88.221  60.963  67.425  1.00 113.87 ? 297 GLU A N     1 
ATOM   1843 C CA    . GLU A 1 297 ? 89.066  61.592  68.436  1.00 113.19 ? 297 GLU A CA    1 
ATOM   1844 C C     . GLU A 1 297 ? 88.313  62.684  69.186  1.00 106.66 ? 297 GLU A C     1 
ATOM   1845 O O     . GLU A 1 297 ? 88.437  62.805  70.410  1.00 104.11 ? 297 GLU A O     1 
ATOM   1846 C CB    . GLU A 1 297 ? 90.331  62.160  67.792  1.00 114.94 ? 297 GLU A CB    1 
ATOM   1847 C CG    . GLU A 1 297 ? 90.936  61.289  66.703  1.00 118.82 ? 297 GLU A CG    1 
ATOM   1848 C CD    . GLU A 1 297 ? 91.148  59.855  67.146  1.00 125.60 ? 297 GLU A CD    1 
ATOM   1849 O OE1   . GLU A 1 297 ? 91.856  59.639  68.152  1.00 127.19 ? 297 GLU A OE1   1 
ATOM   1850 O OE2   . GLU A 1 297 ? 90.614  58.942  66.482  1.00 124.31 ? 297 GLU A OE2   1 
ATOM   1851 N N     . ARG A 1 298 ? 87.530  63.487  68.472  1.00 102.78 ? 298 ARG A N     1 
ATOM   1852 C CA    . ARG A 1 298 ? 86.744  64.553  69.073  1.00 96.19  ? 298 ARG A CA    1 
ATOM   1853 C C     . ARG A 1 298 ? 85.283  64.376  68.696  1.00 88.39  ? 298 ARG A C     1 
ATOM   1854 O O     . ARG A 1 298 ? 84.964  64.073  67.543  1.00 90.86  ? 298 ARG A O     1 
ATOM   1855 C CB    . ARG A 1 298 ? 87.234  65.932  68.623  1.00 100.52 ? 298 ARG A CB    1 
ATOM   1856 C CG    . ARG A 1 298 ? 88.689  66.216  68.949  1.00 109.70 ? 298 ARG A CG    1 
ATOM   1857 C CD    . ARG A 1 298 ? 89.271  67.228  67.977  1.00 120.21 ? 298 ARG A CD    1 
ATOM   1858 N NE    . ARG A 1 298 ? 88.454  68.433  67.902  1.00 123.12 ? 298 ARG A NE    1 
ATOM   1859 C CZ    . ARG A 1 298 ? 88.489  69.303  66.902  1.00 127.57 ? 298 ARG A CZ    1 
ATOM   1860 N NH1   . ARG A 1 298 ? 89.293  69.132  65.865  1.00 129.64 ? 298 ARG A NH1   1 
ATOM   1861 N NH2   . ARG A 1 298 ? 87.696  70.369  66.942  1.00 128.58 ? 298 ARG A NH2   1 
ATOM   1862 N N     . HIS A 1 299 ? 84.398  64.566  69.670  1.00 79.90  ? 299 HIS A N     1 
ATOM   1863 C CA    . HIS A 1 299 ? 82.960  64.413  69.466  1.00 71.97  ? 299 HIS A CA    1 
ATOM   1864 C C     . HIS A 1 299 ? 82.360  65.792  69.216  1.00 66.64  ? 299 HIS A C     1 
ATOM   1865 O O     . HIS A 1 299 ? 81.944  66.487  70.143  1.00 68.04  ? 299 HIS A O     1 
ATOM   1866 C CB    . HIS A 1 299 ? 82.311  63.726  70.661  1.00 72.06  ? 299 HIS A CB    1 
ATOM   1867 C CG    . HIS A 1 299 ? 80.869  63.385  70.451  1.00 74.20  ? 299 HIS A CG    1 
ATOM   1868 N ND1   . HIS A 1 299 ? 80.455  62.160  69.976  1.00 77.00  ? 299 HIS A ND1   1 
ATOM   1869 C CD2   . HIS A 1 299 ? 79.743  64.111  70.649  1.00 69.54  ? 299 HIS A CD2   1 
ATOM   1870 C CE1   . HIS A 1 299 ? 79.136  62.144  69.894  1.00 72.98  ? 299 HIS A CE1   1 
ATOM   1871 N NE2   . HIS A 1 299 ? 78.680  63.316  70.296  1.00 69.54  ? 299 HIS A NE2   1 
ATOM   1872 N N     . LEU A 1 300 ? 82.312  66.185  67.948  1.00 64.51  ? 300 LEU A N     1 
ATOM   1873 C CA    . LEU A 1 300 ? 81.665  67.425  67.544  1.00 58.18  ? 300 LEU A CA    1 
ATOM   1874 C C     . LEU A 1 300 ? 80.177  67.152  67.373  1.00 56.88  ? 300 LEU A C     1 
ATOM   1875 O O     . LEU A 1 300 ? 79.779  66.403  66.475  1.00 67.85  ? 300 LEU A O     1 
ATOM   1876 C CB    . LEU A 1 300 ? 82.274  67.959  66.248  1.00 64.65  ? 300 LEU A CB    1 
ATOM   1877 C CG    . LEU A 1 300 ? 83.506  68.854  66.390  1.00 74.49  ? 300 LEU A CG    1 
ATOM   1878 C CD1   . LEU A 1 300 ? 84.732  68.045  66.789  1.00 83.67  ? 300 LEU A CD1   1 
ATOM   1879 C CD2   . LEU A 1 300 ? 83.771  69.622  65.108  1.00 80.01  ? 300 LEU A CD2   1 
ATOM   1880 N N     . MET A 1 301 ? 79.360  67.755  68.228  1.00 50.39  ? 301 MET A N     1 
ATOM   1881 C CA    . MET A 1 301 ? 77.952  67.408  68.334  1.00 49.38  ? 301 MET A CA    1 
ATOM   1882 C C     . MET A 1 301 ? 77.070  68.569  67.898  1.00 49.60  ? 301 MET A C     1 
ATOM   1883 O O     . MET A 1 301 ? 77.476  69.733  67.938  1.00 58.70  ? 301 MET A O     1 
ATOM   1884 C CB    . MET A 1 301 ? 77.604  66.986  69.766  1.00 48.35  ? 301 MET A CB    1 
ATOM   1885 C CG    . MET A 1 301 ? 77.019  68.093  70.618  1.00 48.93  ? 301 MET A CG    1 
ATOM   1886 S SD    . MET A 1 301 ? 77.235  67.803  72.384  1.00 81.00  ? 301 MET A SD    1 
ATOM   1887 C CE    . MET A 1 301 ? 79.012  67.609  72.476  1.00 66.18  ? 301 MET A CE    1 
ATOM   1888 N N     . HIS A 1 302 ? 75.857  68.229  67.467  1.00 47.85  ? 302 HIS A N     1 
ATOM   1889 C CA    . HIS A 1 302 ? 74.859  69.189  67.014  1.00 45.72  ? 302 HIS A CA    1 
ATOM   1890 C C     . HIS A 1 302 ? 73.592  68.991  67.831  1.00 46.44  ? 302 HIS A C     1 
ATOM   1891 O O     . HIS A 1 302 ? 73.104  67.865  67.950  1.00 56.33  ? 302 HIS A O     1 
ATOM   1892 C CB    . HIS A 1 302 ? 74.563  69.002  65.524  1.00 49.07  ? 302 HIS A CB    1 
ATOM   1893 C CG    . HIS A 1 302 ? 73.415  69.820  65.022  1.00 57.72  ? 302 HIS A CG    1 
ATOM   1894 N ND1   . HIS A 1 302 ? 73.567  71.107  64.555  1.00 62.33  ? 302 HIS A ND1   1 
ATOM   1895 C CD2   . HIS A 1 302 ? 72.098  69.530  64.904  1.00 57.34  ? 302 HIS A CD2   1 
ATOM   1896 C CE1   . HIS A 1 302 ? 72.392  71.577  64.175  1.00 59.32  ? 302 HIS A CE1   1 
ATOM   1897 N NE2   . HIS A 1 302 ? 71.484  70.640  64.377  1.00 61.23  ? 302 HIS A NE2   1 
ATOM   1898 N N     . LEU A 1 303 ? 73.060  70.075  68.385  1.00 45.08  ? 303 LEU A N     1 
ATOM   1899 C CA    . LEU A 1 303 ? 71.875  70.018  69.226  1.00 43.95  ? 303 LEU A CA    1 
ATOM   1900 C C     . LEU A 1 303 ? 70.740  70.805  68.589  1.00 45.70  ? 303 LEU A C     1 
ATOM   1901 O O     . LEU A 1 303 ? 70.965  71.792  67.887  1.00 51.91  ? 303 LEU A O     1 
ATOM   1902 C CB    . LEU A 1 303 ? 72.153  70.575  70.629  1.00 44.89  ? 303 LEU A CB    1 
ATOM   1903 C CG    . LEU A 1 303 ? 72.495  69.601  71.758  1.00 44.27  ? 303 LEU A CG    1 
ATOM   1904 C CD1   . LEU A 1 303 ? 71.307  68.717  72.085  1.00 53.94  ? 303 LEU A CD1   1 
ATOM   1905 C CD2   . LEU A 1 303 ? 73.698  68.760  71.398  1.00 43.43  ? 303 LEU A CD2   1 
ATOM   1906 N N     . GLU A 1 304 ? 69.514  70.353  68.840  1.00 44.19  ? 304 GLU A N     1 
ATOM   1907 C CA    . GLU A 1 304 ? 68.307  71.056  68.417  1.00 50.54  ? 304 GLU A CA    1 
ATOM   1908 C C     . GLU A 1 304 ? 67.357  71.102  69.604  1.00 50.94  ? 304 GLU A C     1 
ATOM   1909 O O     . GLU A 1 304 ? 66.847  70.064  70.035  1.00 63.97  ? 304 GLU A O     1 
ATOM   1910 C CB    . GLU A 1 304 ? 67.649  70.374  67.216  1.00 57.97  ? 304 GLU A CB    1 
ATOM   1911 C CG    . GLU A 1 304 ? 68.574  70.166  66.027  1.00 60.94  ? 304 GLU A CG    1 
ATOM   1912 C CD    . GLU A 1 304 ? 67.847  69.647  64.803  1.00 68.92  ? 304 GLU A CD    1 
ATOM   1913 O OE1   . GLU A 1 304 ? 66.654  69.299  64.922  1.00 76.50  ? 304 GLU A OE1   1 
ATOM   1914 O OE2   . GLU A 1 304 ? 68.470  69.585  63.723  1.00 68.40  ? 304 GLU A OE2   1 
ATOM   1915 N N     . LEU A 1 305 ? 67.122  72.298  70.131  1.00 44.94  ? 305 LEU A N     1 
ATOM   1916 C CA    . LEU A 1 305 ? 66.307  72.491  71.322  1.00 51.98  ? 305 LEU A CA    1 
ATOM   1917 C C     . LEU A 1 305 ? 64.960  73.064  70.907  1.00 57.15  ? 305 LEU A C     1 
ATOM   1918 O O     . LEU A 1 305 ? 64.906  74.094  70.229  1.00 56.56  ? 305 LEU A O     1 
ATOM   1919 C CB    . LEU A 1 305 ? 67.005  73.421  72.315  1.00 53.86  ? 305 LEU A CB    1 
ATOM   1920 C CG    . LEU A 1 305 ? 68.116  72.863  73.210  1.00 51.65  ? 305 LEU A CG    1 
ATOM   1921 C CD1   . LEU A 1 305 ? 69.333  72.428  72.410  1.00 49.82  ? 305 LEU A CD1   1 
ATOM   1922 C CD2   . LEU A 1 305 ? 68.511  73.901  74.242  1.00 55.00  ? 305 LEU A CD2   1 
ATOM   1923 N N     . ASP A 1 306 ? 63.881  72.402  71.314  1.00 64.41  ? 306 ASP A N     1 
ATOM   1924 C CA    . ASP A 1 306 ? 62.546  72.872  70.968  1.00 68.44  ? 306 ASP A CA    1 
ATOM   1925 C C     . ASP A 1 306 ? 62.179  74.084  71.813  1.00 69.61  ? 306 ASP A C     1 
ATOM   1926 O O     . ASP A 1 306 ? 62.297  74.057  73.041  1.00 69.89  ? 306 ASP A O     1 
ATOM   1927 C CB    . ASP A 1 306 ? 61.521  71.758  71.169  1.00 71.00  ? 306 ASP A CB    1 
ATOM   1928 C CG    . ASP A 1 306 ? 60.296  71.930  70.294  1.00 81.81  ? 306 ASP A CG    1 
ATOM   1929 O OD1   . ASP A 1 306 ? 59.952  73.085  69.969  1.00 84.39  ? 306 ASP A OD1   1 
ATOM   1930 O OD2   . ASP A 1 306 ? 59.677  70.908  69.930  1.00 87.41  ? 306 ASP A OD2   1 
ATOM   1931 N N     . ILE A 1 307 ? 61.722  75.145  71.153  1.00 70.34  ? 307 ILE A N     1 
ATOM   1932 C CA    . ILE A 1 307 ? 61.377  76.389  71.831  1.00 67.52  ? 307 ILE A CA    1 
ATOM   1933 C C     . ILE A 1 307 ? 59.902  76.680  71.597  1.00 75.20  ? 307 ILE A C     1 
ATOM   1934 O O     . ILE A 1 307 ? 59.484  77.843  71.554  1.00 80.75  ? 307 ILE A O     1 
ATOM   1935 C CB    . ILE A 1 307 ? 62.260  77.551  71.341  1.00 67.77  ? 307 ILE A CB    1 
ATOM   1936 C CG1   . ILE A 1 307 ? 63.645  77.037  70.953  1.00 64.03  ? 307 ILE A CG1   1 
ATOM   1937 C CG2   . ILE A 1 307 ? 62.406  78.606  72.417  1.00 70.51  ? 307 ILE A CG2   1 
ATOM   1938 C CD1   . ILE A 1 307 ? 64.494  76.647  72.134  1.00 60.65  ? 307 ILE A CD1   1 
ATOM   1939 N N     . SER A 1 308 ? 59.107  75.626  71.440  1.00 77.73  ? 308 SER A N     1 
ATOM   1940 C CA    . SER A 1 308 ? 57.700  75.791  71.103  1.00 83.61  ? 308 SER A CA    1 
ATOM   1941 C C     . SER A 1 308 ? 56.931  76.437  72.248  1.00 89.67  ? 308 SER A C     1 
ATOM   1942 O O     . SER A 1 308 ? 57.094  76.069  73.415  1.00 86.06  ? 308 SER A O     1 
ATOM   1943 C CB    . SER A 1 308 ? 57.079  74.439  70.755  1.00 84.50  ? 308 SER A CB    1 
ATOM   1944 O OG    . SER A 1 308 ? 57.669  73.893  69.588  1.00 85.37  ? 308 SER A OG    1 
ATOM   1945 N N     . ASP A 1 309 ? 56.094  77.415  71.902  1.00 93.74  ? 309 ASP A N     1 
ATOM   1946 C CA    . ASP A 1 309 ? 55.164  78.067  72.823  1.00 96.04  ? 309 ASP A CA    1 
ATOM   1947 C C     . ASP A 1 309 ? 55.863  78.738  74.000  1.00 92.19  ? 309 ASP A C     1 
ATOM   1948 O O     . ASP A 1 309 ? 55.215  79.080  74.995  1.00 96.30  ? 309 ASP A O     1 
ATOM   1949 C CB    . ASP A 1 309 ? 54.112  77.076  73.336  1.00 101.76 ? 309 ASP A CB    1 
ATOM   1950 C CG    . ASP A 1 309 ? 52.944  76.921  72.382  1.00 111.47 ? 309 ASP A CG    1 
ATOM   1951 O OD1   . ASP A 1 309 ? 52.651  77.880  71.638  1.00 113.73 ? 309 ASP A OD1   1 
ATOM   1952 O OD2   . ASP A 1 309 ? 52.320  75.839  72.376  1.00 115.47 ? 309 ASP A OD2   1 
ATOM   1953 N N     . SER A 1 310 ? 57.175  78.943  73.915  1.00 86.04  ? 310 SER A N     1 
ATOM   1954 C CA    . SER A 1 310 ? 57.927  79.557  74.999  1.00 88.76  ? 310 SER A CA    1 
ATOM   1955 C C     . SER A 1 310 ? 58.007  81.073  74.886  1.00 87.23  ? 310 SER A C     1 
ATOM   1956 O O     . SER A 1 310 ? 58.594  81.710  75.767  1.00 84.41  ? 310 SER A O     1 
ATOM   1957 C CB    . SER A 1 310 ? 59.343  78.983  75.054  1.00 84.63  ? 310 SER A CB    1 
ATOM   1958 O OG    . SER A 1 310 ? 60.231  79.788  74.302  1.00 82.17  ? 310 SER A OG    1 
ATOM   1959 N N     . LYS A 1 311 ? 57.462  81.657  73.819  1.00 86.56  ? 311 LYS A N     1 
ATOM   1960 C CA    . LYS A 1 311 ? 57.430  83.093  73.556  1.00 87.68  ? 311 LYS A CA    1 
ATOM   1961 C C     . LYS A 1 311 ? 58.824  83.660  73.295  1.00 87.52  ? 311 LYS A C     1 
ATOM   1962 O O     . LYS A 1 311 ? 58.954  84.862  73.035  1.00 91.53  ? 311 LYS A O     1 
ATOM   1963 C CB    . LYS A 1 311 ? 56.748  83.869  74.697  1.00 90.99  ? 311 LYS A CB    1 
ATOM   1964 C CG    . LYS A 1 311 ? 56.380  85.317  74.393  1.00 95.06  ? 311 LYS A CG    1 
ATOM   1965 C CD    . LYS A 1 311 ? 54.979  85.645  74.878  1.00 94.23  ? 311 LYS A CD    1 
ATOM   1966 C CE    . LYS A 1 311 ? 54.383  86.801  74.094  1.00 98.69  ? 311 LYS A CE    1 
ATOM   1967 N NZ    . LYS A 1 311 ? 54.510  86.598  72.625  1.00 91.77  ? 311 LYS A NZ    1 
ATOM   1968 N N     . ILE A 1 312 ? 59.870  82.835  73.328  1.00 83.97  ? 312 ILE A N     1 
ATOM   1969 C CA    . ILE A 1 312 ? 61.225  83.327  73.106  1.00 82.19  ? 312 ILE A CA    1 
ATOM   1970 C C     . ILE A 1 312 ? 61.354  83.773  71.656  1.00 84.86  ? 312 ILE A C     1 
ATOM   1971 O O     . ILE A 1 312 ? 61.084  83.004  70.726  1.00 87.16  ? 312 ILE A O     1 
ATOM   1972 C CB    . ILE A 1 312 ? 62.264  82.254  73.456  1.00 76.62  ? 312 ILE A CB    1 
ATOM   1973 C CG1   . ILE A 1 312 ? 62.624  82.327  74.939  1.00 79.90  ? 312 ILE A CG1   1 
ATOM   1974 C CG2   . ILE A 1 312 ? 63.524  82.427  72.621  1.00 72.30  ? 312 ILE A CG2   1 
ATOM   1975 C CD1   . ILE A 1 312 ? 63.586  81.249  75.382  1.00 76.16  ? 312 ILE A CD1   1 
ATOM   1976 N N     . ARG A 1 313 ? 61.751  85.026  71.459  1.00 82.16  ? 313 ARG A N     1 
ATOM   1977 C CA    . ARG A 1 313 ? 61.980  85.588  70.135  1.00 82.28  ? 313 ARG A CA    1 
ATOM   1978 C C     . ARG A 1 313 ? 63.455  85.935  70.010  1.00 79.61  ? 313 ARG A C     1 
ATOM   1979 O O     . ARG A 1 313 ? 63.987  86.700  70.821  1.00 84.21  ? 313 ARG A O     1 
ATOM   1980 C CB    . ARG A 1 313 ? 61.108  86.822  69.904  1.00 85.07  ? 313 ARG A CB    1 
ATOM   1981 C CG    . ARG A 1 313 ? 60.605  86.965  68.479  1.00 83.41  ? 313 ARG A CG    1 
ATOM   1982 C CD    . ARG A 1 313 ? 59.208  87.568  68.445  1.00 89.76  ? 313 ARG A CD    1 
ATOM   1983 N NE    . ARG A 1 313 ? 58.249  86.791  69.223  1.00 97.92  ? 313 ARG A NE    1 
ATOM   1984 C CZ    . ARG A 1 313 ? 57.823  85.576  68.905  1.00 98.52  ? 313 ARG A CZ    1 
ATOM   1985 N NH1   . ARG A 1 313 ? 58.231  84.964  67.804  1.00 98.51  ? 313 ARG A NH1   1 
ATOM   1986 N NH2   . ARG A 1 313 ? 56.960  84.960  69.707  1.00 95.10  ? 313 ARG A NH2   1 
ATOM   1987 N N     . TYR A 1 314 ? 64.112  85.376  68.996  1.00 72.46  ? 314 TYR A N     1 
ATOM   1988 C CA    . TYR A 1 314 ? 65.544  85.574  68.828  1.00 68.96  ? 314 TYR A CA    1 
ATOM   1989 C C     . TYR A 1 314 ? 65.890  85.918  67.387  1.00 74.86  ? 314 TYR A C     1 
ATOM   1990 O O     . TYR A 1 314 ? 65.000  86.166  66.567  1.00 79.18  ? 314 TYR A O     1 
ATOM   1991 C CB    . TYR A 1 314 ? 66.310  84.328  69.270  1.00 65.61  ? 314 TYR A CB    1 
ATOM   1992 C CG    . TYR A 1 314 ? 66.188  83.161  68.318  1.00 64.95  ? 314 TYR A CG    1 
ATOM   1993 C CD1   . TYR A 1 314 ? 65.006  82.443  68.214  1.00 69.61  ? 314 TYR A CD1   1 
ATOM   1994 C CD2   . TYR A 1 314 ? 67.257  82.778  67.523  1.00 61.43  ? 314 TYR A CD2   1 
ATOM   1995 C CE1   . TYR A 1 314 ? 64.894  81.375  67.347  1.00 69.90  ? 314 TYR A CE1   1 
ATOM   1996 C CE2   . TYR A 1 314 ? 67.154  81.712  66.653  1.00 64.28  ? 314 TYR A CE2   1 
ATOM   1997 C CZ    . TYR A 1 314 ? 65.971  81.015  66.569  1.00 67.24  ? 314 TYR A CZ    1 
ATOM   1998 O OH    . TYR A 1 314 ? 65.868  79.953  65.702  1.00 67.40  ? 314 TYR A OH    1 
ATOM   1999 N N     . GLU A 1 315 ? 67.183  85.941  67.075  1.00 78.89  ? 315 GLU A N     1 
ATOM   2000 C CA    . GLU A 1 315 ? 67.649  86.226  65.728  1.00 78.34  ? 315 GLU A CA    1 
ATOM   2001 C C     . GLU A 1 315 ? 68.934  85.447  65.491  1.00 74.65  ? 315 GLU A C     1 
ATOM   2002 O O     . GLU A 1 315 ? 69.619  85.044  66.433  1.00 73.69  ? 315 GLU A O     1 
ATOM   2003 C CB    . GLU A 1 315 ? 67.871  87.729  65.518  1.00 76.28  ? 315 GLU A CB    1 
ATOM   2004 C CG    . GLU A 1 315 ? 67.961  88.158  64.064  1.00 80.45  ? 315 GLU A CG    1 
ATOM   2005 C CD    . GLU A 1 315 ? 67.321  89.509  63.818  1.00 90.07  ? 315 GLU A CD    1 
ATOM   2006 O OE1   . GLU A 1 315 ? 66.723  90.063  64.763  1.00 91.35  ? 315 GLU A OE1   1 
ATOM   2007 O OE2   . GLU A 1 315 ? 67.417  90.016  62.681  1.00 96.04  ? 315 GLU A OE2   1 
ATOM   2008 N N     . SER A 1 316 ? 69.248  85.231  64.216  1.00 73.46  ? 316 SER A N     1 
ATOM   2009 C CA    . SER A 1 316 ? 70.448  84.490  63.860  1.00 71.89  ? 316 SER A CA    1 
ATOM   2010 C C     . SER A 1 316 ? 71.693  85.233  64.329  1.00 72.12  ? 316 SER A C     1 
ATOM   2011 O O     . SER A 1 316 ? 71.737  86.465  64.358  1.00 73.02  ? 316 SER A O     1 
ATOM   2012 C CB    . SER A 1 316 ? 70.505  84.264  62.351  1.00 74.39  ? 316 SER A CB    1 
ATOM   2013 O OG    . SER A 1 316 ? 71.308  85.244  61.721  1.00 78.53  ? 316 SER A OG    1 
ATOM   2014 N N     . GLY A 1 317 ? 72.710  84.466  64.712  1.00 64.53  ? 317 GLY A N     1 
ATOM   2015 C CA    . GLY A 1 317 ? 73.935  85.030  65.230  1.00 64.88  ? 317 GLY A CA    1 
ATOM   2016 C C     . GLY A 1 317 ? 73.907  85.382  66.700  1.00 67.57  ? 317 GLY A C     1 
ATOM   2017 O O     . GLY A 1 317 ? 74.934  85.821  67.233  1.00 67.05  ? 317 GLY A O     1 
ATOM   2018 N N     . ASP A 1 318 ? 72.777  85.195  67.375  1.00 66.93  ? 318 ASP A N     1 
ATOM   2019 C CA    . ASP A 1 318 ? 72.664  85.513  68.791  1.00 64.82  ? 318 ASP A CA    1 
ATOM   2020 C C     . ASP A 1 318 ? 73.310  84.400  69.612  1.00 60.75  ? 318 ASP A C     1 
ATOM   2021 O O     . ASP A 1 318 ? 73.993  83.519  69.085  1.00 60.88  ? 318 ASP A O     1 
ATOM   2022 C CB    . ASP A 1 318 ? 71.204  85.728  69.172  1.00 68.96  ? 318 ASP A CB    1 
ATOM   2023 C CG    . ASP A 1 318 ? 70.846  87.191  69.295  1.00 72.71  ? 318 ASP A CG    1 
ATOM   2024 O OD1   . ASP A 1 318 ? 71.606  88.034  68.776  1.00 73.72  ? 318 ASP A OD1   1 
ATOM   2025 O OD2   . ASP A 1 318 ? 69.804  87.500  69.909  1.00 74.78  ? 318 ASP A OD2   1 
ATOM   2026 N N     . HIS A 1 319 ? 73.097  84.429  70.923  1.00 59.98  ? 319 HIS A N     1 
ATOM   2027 C CA    . HIS A 1 319 ? 73.717  83.478  71.832  1.00 56.33  ? 319 HIS A CA    1 
ATOM   2028 C C     . HIS A 1 319 ? 72.649  82.786  72.660  1.00 56.45  ? 319 HIS A C     1 
ATOM   2029 O O     . HIS A 1 319 ? 71.782  83.447  73.241  1.00 58.45  ? 319 HIS A O     1 
ATOM   2030 C CB    . HIS A 1 319 ? 74.725  84.176  72.744  1.00 57.20  ? 319 HIS A CB    1 
ATOM   2031 C CG    . HIS A 1 319 ? 76.096  84.270  72.156  1.00 61.76  ? 319 HIS A CG    1 
ATOM   2032 N ND1   . HIS A 1 319 ? 76.537  83.416  71.170  1.00 63.13  ? 319 HIS A ND1   1 
ATOM   2033 C CD2   . HIS A 1 319 ? 77.118  85.122  72.403  1.00 64.67  ? 319 HIS A CD2   1 
ATOM   2034 C CE1   . HIS A 1 319 ? 77.776  83.731  70.840  1.00 66.62  ? 319 HIS A CE1   1 
ATOM   2035 N NE2   . HIS A 1 319 ? 78.151  84.765  71.571  1.00 67.71  ? 319 HIS A NE2   1 
ATOM   2036 N N     . VAL A 1 320 ? 72.716  81.459  72.713  1.00 56.50  ? 320 VAL A N     1 
ATOM   2037 C CA    . VAL A 1 320 ? 71.851  80.653  73.565  1.00 50.65  ? 320 VAL A CA    1 
ATOM   2038 C C     . VAL A 1 320 ? 72.666  80.198  74.766  1.00 49.91  ? 320 VAL A C     1 
ATOM   2039 O O     . VAL A 1 320 ? 73.804  79.733  74.620  1.00 50.39  ? 320 VAL A O     1 
ATOM   2040 C CB    . VAL A 1 320 ? 71.238  79.462  72.805  1.00 51.32  ? 320 VAL A CB    1 
ATOM   2041 C CG1   . VAL A 1 320 ? 72.304  78.494  72.324  1.00 47.39  ? 320 VAL A CG1   1 
ATOM   2042 C CG2   . VAL A 1 320 ? 70.239  78.739  73.688  1.00 54.56  ? 320 VAL A CG2   1 
ATOM   2043 N N     . ALA A 1 321 ? 72.100  80.373  75.953  1.00 52.68  ? 321 ALA A N     1 
ATOM   2044 C CA    . ALA A 1 321 ? 72.764  80.050  77.203  1.00 49.05  ? 321 ALA A CA    1 
ATOM   2045 C C     . ALA A 1 321 ? 72.031  78.909  77.891  1.00 51.63  ? 321 ALA A C     1 
ATOM   2046 O O     . ALA A 1 321 ? 70.801  78.847  77.884  1.00 55.65  ? 321 ALA A O     1 
ATOM   2047 C CB    . ALA A 1 321 ? 72.822  81.270  78.123  1.00 45.65  ? 321 ALA A CB    1 
ATOM   2048 N N     . VAL A 1 322 ? 72.798  78.004  78.485  1.00 48.79  ? 322 VAL A N     1 
ATOM   2049 C CA    . VAL A 1 322 ? 72.255  76.794  79.085  1.00 42.13  ? 322 VAL A CA    1 
ATOM   2050 C C     . VAL A 1 322 ? 72.734  76.699  80.527  1.00 48.67  ? 322 VAL A C     1 
ATOM   2051 O O     . VAL A 1 322 ? 73.887  77.024  80.834  1.00 52.14  ? 322 VAL A O     1 
ATOM   2052 C CB    . VAL A 1 322 ? 72.652  75.540  78.278  1.00 37.14  ? 322 VAL A CB    1 
ATOM   2053 C CG1   . VAL A 1 322 ? 74.148  75.281  78.365  1.00 39.11  ? 322 VAL A CG1   1 
ATOM   2054 C CG2   . VAL A 1 322 ? 71.870  74.342  78.752  1.00 52.44  ? 322 VAL A CG2   1 
ATOM   2055 N N     . TYR A 1 323 ? 71.833  76.289  81.422  1.00 48.69  ? 323 TYR A N     1 
ATOM   2056 C CA    . TYR A 1 323 ? 72.189  76.061  82.814  1.00 43.12  ? 323 TYR A CA    1 
ATOM   2057 C C     . TYR A 1 323 ? 72.481  74.580  82.999  1.00 43.87  ? 323 TYR A C     1 
ATOM   2058 O O     . TYR A 1 323 ? 71.543  73.772  83.065  1.00 44.03  ? 323 TYR A O     1 
ATOM   2059 C CB    . TYR A 1 323 ? 71.062  76.508  83.746  1.00 45.12  ? 323 TYR A CB    1 
ATOM   2060 C CG    . TYR A 1 323 ? 71.028  77.994  84.002  1.00 42.57  ? 323 TYR A CG    1 
ATOM   2061 C CD1   . TYR A 1 323 ? 72.055  78.623  84.689  1.00 45.82  ? 323 TYR A CD1   1 
ATOM   2062 C CD2   . TYR A 1 323 ? 69.961  78.766  83.569  1.00 46.14  ? 323 TYR A CD2   1 
ATOM   2063 C CE1   . TYR A 1 323 ? 72.025  79.981  84.929  1.00 55.36  ? 323 TYR A CE1   1 
ATOM   2064 C CE2   . TYR A 1 323 ? 69.920  80.123  83.806  1.00 53.08  ? 323 TYR A CE2   1 
ATOM   2065 C CZ    . TYR A 1 323 ? 70.954  80.728  84.487  1.00 58.12  ? 323 TYR A CZ    1 
ATOM   2066 O OH    . TYR A 1 323 ? 70.919  82.083  84.726  1.00 57.32  ? 323 TYR A OH    1 
ATOM   2067 N N     . PRO A 1 324 ? 73.742  74.172  83.093  1.00 43.77  ? 324 PRO A N     1 
ATOM   2068 C CA    . PRO A 1 324 ? 74.052  72.742  83.140  1.00 43.64  ? 324 PRO A CA    1 
ATOM   2069 C C     . PRO A 1 324 ? 73.740  72.132  84.497  1.00 46.24  ? 324 PRO A C     1 
ATOM   2070 O O     . PRO A 1 324 ? 73.490  72.821  85.487  1.00 46.19  ? 324 PRO A O     1 
ATOM   2071 C CB    . PRO A 1 324 ? 75.554  72.698  82.849  1.00 43.18  ? 324 PRO A CB    1 
ATOM   2072 C CG    . PRO A 1 324 ? 76.056  74.003  83.340  1.00 48.37  ? 324 PRO A CG    1 
ATOM   2073 C CD    . PRO A 1 324 ? 74.958  75.001  83.088  1.00 47.36  ? 324 PRO A CD    1 
ATOM   2074 N N     . ALA A 1 325 ? 73.747  70.804  84.519  1.00 51.45  ? 325 ALA A N     1 
ATOM   2075 C CA    . ALA A 1 325 ? 73.632  70.021  85.740  1.00 49.07  ? 325 ALA A CA    1 
ATOM   2076 C C     . ALA A 1 325 ? 74.899  69.196  85.900  1.00 47.47  ? 325 ALA A C     1 
ATOM   2077 O O     . ALA A 1 325 ? 75.342  68.543  84.950  1.00 48.68  ? 325 ALA A O     1 
ATOM   2078 C CB    . ALA A 1 325 ? 72.404  69.112  85.699  1.00 50.55  ? 325 ALA A CB    1 
ATOM   2079 N N     . ASN A 1 326 ? 75.478  69.229  87.093  1.00 49.23  ? 326 ASN A N     1 
ATOM   2080 C CA    . ASN A 1 326 ? 76.777  68.610  87.292  1.00 54.03  ? 326 ASN A CA    1 
ATOM   2081 C C     . ASN A 1 326 ? 76.660  67.089  87.293  1.00 60.37  ? 326 ASN A C     1 
ATOM   2082 O O     . ASN A 1 326 ? 75.573  66.519  87.425  1.00 63.30  ? 326 ASN A O     1 
ATOM   2083 C CB    . ASN A 1 326 ? 77.404  69.101  88.594  1.00 56.22  ? 326 ASN A CB    1 
ATOM   2084 C CG    . ASN A 1 326 ? 78.908  69.177  88.517  1.00 57.29  ? 326 ASN A CG    1 
ATOM   2085 O OD1   . ASN A 1 326 ? 79.535  68.527  87.681  1.00 60.88  ? 326 ASN A OD1   1 
ATOM   2086 N ND2   . ASN A 1 326 ? 79.498  69.998  89.373  1.00 55.46  ? 326 ASN A ND2   1 
ATOM   2087 N N     . ASP A 1 327 ? 77.807  66.433  87.131  1.00 64.05  ? 327 ASP A N     1 
ATOM   2088 C CA    . ASP A 1 327 ? 77.840  64.980  87.044  1.00 70.31  ? 327 ASP A CA    1 
ATOM   2089 C C     . ASP A 1 327 ? 77.353  64.354  88.344  1.00 72.56  ? 327 ASP A C     1 
ATOM   2090 O O     . ASP A 1 327 ? 77.769  64.754  89.435  1.00 74.54  ? 327 ASP A O     1 
ATOM   2091 C CB    . ASP A 1 327 ? 79.260  64.509  86.728  1.00 74.18  ? 327 ASP A CB    1 
ATOM   2092 C CG    . ASP A 1 327 ? 79.320  63.044  86.356  1.00 79.65  ? 327 ASP A CG    1 
ATOM   2093 O OD1   . ASP A 1 327 ? 78.250  62.439  86.137  1.00 83.41  ? 327 ASP A OD1   1 
ATOM   2094 O OD2   . ASP A 1 327 ? 80.439  62.496  86.279  1.00 80.39  ? 327 ASP A OD2   1 
ATOM   2095 N N     . SER A 1 328 ? 76.465  63.363  88.223  1.00 72.63  ? 328 SER A N     1 
ATOM   2096 C CA    . SER A 1 328 ? 75.959  62.681  89.409  1.00 72.61  ? 328 SER A CA    1 
ATOM   2097 C C     . SER A 1 328 ? 77.015  61.779  90.032  1.00 73.78  ? 328 SER A C     1 
ATOM   2098 O O     . SER A 1 328 ? 77.035  61.606  91.256  1.00 78.35  ? 328 SER A O     1 
ATOM   2099 C CB    . SER A 1 328 ? 74.709  61.877  89.060  1.00 72.04  ? 328 SER A CB    1 
ATOM   2100 O OG    . SER A 1 328 ? 73.577  62.723  88.956  1.00 75.91  ? 328 SER A OG    1 
ATOM   2101 N N     . ALA A 1 329 ? 77.894  61.198  89.213  1.00 70.70  ? 329 ALA A N     1 
ATOM   2102 C CA    . ALA A 1 329 ? 78.976  60.380  89.752  1.00 69.19  ? 329 ALA A CA    1 
ATOM   2103 C C     . ALA A 1 329 ? 79.918  61.212  90.612  1.00 74.45  ? 329 ALA A C     1 
ATOM   2104 O O     . ALA A 1 329 ? 80.377  60.752  91.663  1.00 76.30  ? 329 ALA A O     1 
ATOM   2105 C CB    . ALA A 1 329 ? 79.742  59.706  88.615  1.00 68.30  ? 329 ALA A CB    1 
ATOM   2106 N N     . LEU A 1 330 ? 80.220  62.437  90.177  1.00 74.98  ? 330 LEU A N     1 
ATOM   2107 C CA    . LEU A 1 330 ? 81.100  63.309  90.950  1.00 70.93  ? 330 LEU A CA    1 
ATOM   2108 C C     . LEU A 1 330 ? 80.496  63.627  92.312  1.00 69.57  ? 330 LEU A C     1 
ATOM   2109 O O     . LEU A 1 330 ? 81.178  63.555  93.341  1.00 73.91  ? 330 LEU A O     1 
ATOM   2110 C CB    . LEU A 1 330 ? 81.371  64.595  90.169  1.00 71.04  ? 330 LEU A CB    1 
ATOM   2111 C CG    . LEU A 1 330 ? 82.683  64.701  89.389  1.00 73.82  ? 330 LEU A CG    1 
ATOM   2112 C CD1   . LEU A 1 330 ? 83.871  64.615  90.322  1.00 71.08  ? 330 LEU A CD1   1 
ATOM   2113 C CD2   . LEU A 1 330 ? 82.764  63.627  88.318  1.00 74.13  ? 330 LEU A CD2   1 
ATOM   2114 N N     . VAL A 1 331 ? 79.207  63.973  92.336  1.00 67.37  ? 331 VAL A N     1 
ATOM   2115 C CA    . VAL A 1 331 ? 78.535  64.282  93.595  1.00 69.98  ? 331 VAL A CA    1 
ATOM   2116 C C     . VAL A 1 331 ? 78.490  63.054  94.493  1.00 71.72  ? 331 VAL A C     1 
ATOM   2117 O O     . VAL A 1 331 ? 78.724  63.143  95.705  1.00 70.20  ? 331 VAL A O     1 
ATOM   2118 C CB    . VAL A 1 331 ? 77.125  64.834  93.323  1.00 62.11  ? 331 VAL A CB    1 
ATOM   2119 C CG1   . VAL A 1 331 ? 76.440  65.204  94.625  1.00 61.85  ? 331 VAL A CG1   1 
ATOM   2120 C CG2   . VAL A 1 331 ? 77.207  66.033  92.401  1.00 62.15  ? 331 VAL A CG2   1 
ATOM   2121 N N     . ASN A 1 332 ? 78.178  61.891  93.917  1.00 72.09  ? 332 ASN A N     1 
ATOM   2122 C CA    . ASN A 1 332 ? 78.115  60.668  94.708  1.00 69.93  ? 332 ASN A CA    1 
ATOM   2123 C C     . ASN A 1 332 ? 79.469  60.342  95.325  1.00 71.62  ? 332 ASN A C     1 
ATOM   2124 O O     . ASN A 1 332 ? 79.552  59.998  96.509  1.00 78.22  ? 332 ASN A O     1 
ATOM   2125 C CB    . ASN A 1 332 ? 77.627  59.510  93.839  1.00 72.98  ? 332 ASN A CB    1 
ATOM   2126 C CG    . ASN A 1 332 ? 76.506  58.730  94.487  1.00 78.74  ? 332 ASN A CG    1 
ATOM   2127 O OD1   . ASN A 1 332 ? 75.965  59.137  95.514  1.00 76.13  ? 332 ASN A OD1   1 
ATOM   2128 N ND2   . ASN A 1 332 ? 76.147  57.601  93.888  1.00 88.59  ? 332 ASN A ND2   1 
ATOM   2129 N N     . GLN A 1 333 ? 80.543  60.460  94.542  1.00 69.72  ? 333 GLN A N     1 
ATOM   2130 C CA    . GLN A 1 333 ? 81.873  60.168  95.065  1.00 69.35  ? 333 GLN A CA    1 
ATOM   2131 C C     . GLN A 1 333 ? 82.289  61.181  96.124  1.00 73.23  ? 333 GLN A C     1 
ATOM   2132 O O     . GLN A 1 333 ? 82.925  60.816  97.120  1.00 79.23  ? 333 GLN A O     1 
ATOM   2133 C CB    . GLN A 1 333 ? 82.888  60.127  93.926  1.00 66.61  ? 333 GLN A CB    1 
ATOM   2134 C CG    . GLN A 1 333 ? 82.760  58.901  93.040  1.00 74.19  ? 333 GLN A CG    1 
ATOM   2135 C CD    . GLN A 1 333 ? 83.804  58.860  91.945  1.00 80.29  ? 333 GLN A CD    1 
ATOM   2136 O OE1   . GLN A 1 333 ? 84.591  59.792  91.785  1.00 77.81  ? 333 GLN A OE1   1 
ATOM   2137 N NE2   . GLN A 1 333 ? 83.818  57.773  91.182  1.00 85.30  ? 333 GLN A NE2   1 
ATOM   2138 N N     . ILE A 1 334 ? 81.947  62.457  95.927  1.00 71.68  ? 334 ILE A N     1 
ATOM   2139 C CA    . ILE A 1 334 ? 82.288  63.475  96.917  1.00 73.71  ? 334 ILE A CA    1 
ATOM   2140 C C     . ILE A 1 334 ? 81.565  63.201  98.229  1.00 76.01  ? 334 ILE A C     1 
ATOM   2141 O O     . ILE A 1 334 ? 82.155  63.290  99.312  1.00 77.43  ? 334 ILE A O     1 
ATOM   2142 C CB    . ILE A 1 334 ? 81.969  64.879  96.372  1.00 68.86  ? 334 ILE A CB    1 
ATOM   2143 C CG1   . ILE A 1 334 ? 83.153  65.421  95.574  1.00 66.72  ? 334 ILE A CG1   1 
ATOM   2144 C CG2   . ILE A 1 334 ? 81.626  65.831  97.505  1.00 68.25  ? 334 ILE A CG2   1 
ATOM   2145 C CD1   . ILE A 1 334 ? 82.845  66.690  94.820  1.00 65.26  ? 334 ILE A CD1   1 
ATOM   2146 N N     . GLY A 1 335 ? 80.280  62.854  98.153  1.00 72.54  ? 335 GLY A N     1 
ATOM   2147 C CA    . GLY A 1 335 ? 79.548  62.516  99.362  1.00 72.37  ? 335 GLY A CA    1 
ATOM   2148 C C     . GLY A 1 335 ? 80.083  61.269  100.039 1.00 80.34  ? 335 GLY A C     1 
ATOM   2149 O O     . GLY A 1 335 ? 80.142  61.195  101.268 1.00 81.82  ? 335 GLY A O     1 
ATOM   2150 N N     . GLU A 1 336 ? 80.474  60.269  99.245  1.00 81.48  ? 336 GLU A N     1 
ATOM   2151 C CA    . GLU A 1 336 ? 81.018  59.041  99.813  1.00 79.21  ? 336 GLU A CA    1 
ATOM   2152 C C     . GLU A 1 336 ? 82.340  59.295  100.527 1.00 83.16  ? 336 GLU A C     1 
ATOM   2153 O O     . GLU A 1 336 ? 82.559  58.787  101.633 1.00 87.65  ? 336 GLU A O     1 
ATOM   2154 C CB    . GLU A 1 336 ? 81.192  57.993  98.715  1.00 79.77  ? 336 GLU A CB    1 
ATOM   2155 C CG    . GLU A 1 336 ? 81.187  56.560  99.215  1.00 86.10  ? 336 GLU A CG    1 
ATOM   2156 C CD    . GLU A 1 336 ? 82.569  56.074  99.601  1.00 95.04  ? 336 GLU A CD    1 
ATOM   2157 O OE1   . GLU A 1 336 ? 83.560  56.605  99.057  1.00 96.46  ? 336 GLU A OE1   1 
ATOM   2158 O OE2   . GLU A 1 336 ? 82.665  55.160  100.447 1.00 98.79  ? 336 GLU A OE2   1 
ATOM   2159 N N     . ILE A 1 337 ? 83.236  60.072  99.915  1.00 78.84  ? 337 ILE A N     1 
ATOM   2160 C CA    . ILE A 1 337 ? 84.527  60.326  100.547 1.00 79.90  ? 337 ILE A CA    1 
ATOM   2161 C C     . ILE A 1 337 ? 84.372  61.258  101.743 1.00 81.05  ? 337 ILE A C     1 
ATOM   2162 O O     . ILE A 1 337 ? 85.110  61.141  102.728 1.00 81.86  ? 337 ILE A O     1 
ATOM   2163 C CB    . ILE A 1 337 ? 85.543  60.869  99.522  1.00 81.34  ? 337 ILE A CB    1 
ATOM   2164 C CG1   . ILE A 1 337 ? 86.943  60.924  100.137 1.00 83.71  ? 337 ILE A CG1   1 
ATOM   2165 C CG2   . ILE A 1 337 ? 85.136  62.239  99.017  1.00 84.25  ? 337 ILE A CG2   1 
ATOM   2166 C CD1   . ILE A 1 337 ? 88.057  60.818  99.123  1.00 86.58  ? 337 ILE A CD1   1 
ATOM   2167 N N     . LEU A 1 338 ? 83.419  62.191  101.689 1.00 80.41  ? 338 LEU A N     1 
ATOM   2168 C CA    . LEU A 1 338 ? 83.193  63.075  102.825 1.00 80.17  ? 338 LEU A CA    1 
ATOM   2169 C C     . LEU A 1 338 ? 82.476  62.366  103.965 1.00 81.75  ? 338 LEU A C     1 
ATOM   2170 O O     . LEU A 1 338 ? 82.699  62.699  105.134 1.00 85.06  ? 338 LEU A O     1 
ATOM   2171 C CB    . LEU A 1 338 ? 82.394  64.303  102.388 1.00 80.74  ? 338 LEU A CB    1 
ATOM   2172 C CG    . LEU A 1 338 ? 83.201  65.543  102.001 1.00 77.90  ? 338 LEU A CG    1 
ATOM   2173 C CD1   . LEU A 1 338 ? 82.351  66.795  102.132 1.00 70.33  ? 338 LEU A CD1   1 
ATOM   2174 C CD2   . LEU A 1 338 ? 84.464  65.657  102.840 1.00 82.44  ? 338 LEU A CD2   1 
ATOM   2175 N N     . GLY A 1 339 ? 81.622  61.395  103.651 1.00 82.98  ? 339 GLY A N     1 
ATOM   2176 C CA    . GLY A 1 339 ? 80.881  60.683  104.672 1.00 88.36  ? 339 GLY A CA    1 
ATOM   2177 C C     . GLY A 1 339 ? 79.780  61.521  105.287 1.00 91.04  ? 339 GLY A C     1 
ATOM   2178 O O     . GLY A 1 339 ? 79.800  61.801  106.488 1.00 92.75  ? 339 GLY A O     1 
ATOM   2179 N N     . ALA A 1 340 ? 78.812  61.928  104.470 1.00 89.96  ? 340 ALA A N     1 
ATOM   2180 C CA    . ALA A 1 340 ? 77.705  62.750  104.931 1.00 88.60  ? 340 ALA A CA    1 
ATOM   2181 C C     . ALA A 1 340 ? 76.427  62.315  104.230 1.00 90.01  ? 340 ALA A C     1 
ATOM   2182 O O     . ALA A 1 340 ? 76.457  61.692  103.167 1.00 87.75  ? 340 ALA A O     1 
ATOM   2183 C CB    . ALA A 1 340 ? 77.967  64.241  104.685 1.00 82.54  ? 340 ALA A CB    1 
ATOM   2184 N N     . ASP A 1 341 ? 75.296  62.652  104.845 1.00 92.89  ? 341 ASP A N     1 
ATOM   2185 C CA    . ASP A 1 341 ? 73.987  62.337  104.281 1.00 92.64  ? 341 ASP A CA    1 
ATOM   2186 C C     . ASP A 1 341 ? 73.618  63.414  103.268 1.00 84.94  ? 341 ASP A C     1 
ATOM   2187 O O     . ASP A 1 341 ? 73.273  64.539  103.641 1.00 84.44  ? 341 ASP A O     1 
ATOM   2188 C CB    . ASP A 1 341 ? 72.939  62.234  105.385 1.00 95.59  ? 341 ASP A CB    1 
ATOM   2189 C CG    . ASP A 1 341 ? 71.807  61.293  105.026 1.00 99.43  ? 341 ASP A CG    1 
ATOM   2190 O OD1   . ASP A 1 341 ? 72.074  60.259  104.377 1.00 96.57  ? 341 ASP A OD1   1 
ATOM   2191 O OD2   . ASP A 1 341 ? 70.649  61.587  105.391 1.00 101.27 ? 341 ASP A OD2   1 
ATOM   2192 N N     . LEU A 1 342 ? 73.682  63.064  101.983 1.00 80.52  ? 342 LEU A N     1 
ATOM   2193 C CA    . LEU A 1 342 ? 73.458  64.025  100.911 1.00 77.47  ? 342 LEU A CA    1 
ATOM   2194 C C     . LEU A 1 342 ? 72.002  64.450  100.784 1.00 78.43  ? 342 LEU A C     1 
ATOM   2195 O O     . LEU A 1 342 ? 71.722  65.424  100.077 1.00 79.10  ? 342 LEU A O     1 
ATOM   2196 C CB    . LEU A 1 342 ? 73.942  63.439  99.584  1.00 75.53  ? 342 LEU A CB    1 
ATOM   2197 C CG    . LEU A 1 342 ? 75.368  63.773  99.140  1.00 69.74  ? 342 LEU A CG    1 
ATOM   2198 C CD1   . LEU A 1 342 ? 75.444  65.186  98.601  1.00 74.46  ? 342 LEU A CD1   1 
ATOM   2199 C CD2   . LEU A 1 342 ? 76.346  63.597  100.285 1.00 70.33  ? 342 LEU A CD2   1 
ATOM   2200 N N     . ASP A 1 343 ? 71.076  63.757  101.443 1.00 84.06  ? 343 ASP A N     1 
ATOM   2201 C CA    . ASP A 1 343 ? 69.647  64.044  101.331 1.00 86.93  ? 343 ASP A CA    1 
ATOM   2202 C C     . ASP A 1 343 ? 69.114  64.779  102.553 1.00 82.16  ? 343 ASP A C     1 
ATOM   2203 O O     . ASP A 1 343 ? 67.988  64.533  102.993 1.00 83.20  ? 343 ASP A O     1 
ATOM   2204 C CB    . ASP A 1 343 ? 68.867  62.753  101.102 1.00 91.62  ? 343 ASP A CB    1 
ATOM   2205 C CG    . ASP A 1 343 ? 69.204  62.097  99.778  1.00 87.91  ? 343 ASP A CG    1 
ATOM   2206 O OD1   . ASP A 1 343 ? 69.571  62.822  98.831  1.00 79.61  ? 343 ASP A OD1   1 
ATOM   2207 O OD2   . ASP A 1 343 ? 69.102  60.857  99.684  1.00 89.44  ? 343 ASP A OD2   1 
ATOM   2208 N N     . VAL A 1 344 ? 69.899  65.689  103.119 1.00 78.10  ? 344 VAL A N     1 
ATOM   2209 C CA    . VAL A 1 344 ? 69.510  66.436  104.309 1.00 77.31  ? 344 VAL A CA    1 
ATOM   2210 C C     . VAL A 1 344 ? 69.056  67.824  103.881 1.00 72.12  ? 344 VAL A C     1 
ATOM   2211 O O     . VAL A 1 344 ? 69.849  68.611  103.351 1.00 76.15  ? 344 VAL A O     1 
ATOM   2212 C CB    . VAL A 1 344 ? 70.664  66.521  105.320 1.00 80.26  ? 344 VAL A CB    1 
ATOM   2213 C CG1   . VAL A 1 344 ? 70.382  67.597  106.356 1.00 78.65  ? 344 VAL A CG1   1 
ATOM   2214 C CG2   . VAL A 1 344 ? 70.876  65.177  105.992 1.00 85.02  ? 344 VAL A CG2   1 
ATOM   2215 N N     . ILE A 1 345 ? 67.781  68.128  104.111 1.00 70.24  ? 345 ILE A N     1 
ATOM   2216 C CA    . ILE A 1 345 ? 67.257  69.456  103.817 1.00 71.53  ? 345 ILE A CA    1 
ATOM   2217 C C     . ILE A 1 345 ? 67.851  70.442  104.814 1.00 77.72  ? 345 ILE A C     1 
ATOM   2218 O O     . ILE A 1 345 ? 67.768  70.241  106.031 1.00 86.18  ? 345 ILE A O     1 
ATOM   2219 C CB    . ILE A 1 345 ? 65.725  69.466  103.869 1.00 71.09  ? 345 ILE A CB    1 
ATOM   2220 C CG1   . ILE A 1 345 ? 65.156  68.455  102.872 1.00 66.92  ? 345 ILE A CG1   1 
ATOM   2221 C CG2   . ILE A 1 345 ? 65.191  70.861  103.591 1.00 76.05  ? 345 ILE A CG2   1 
ATOM   2222 C CD1   . ILE A 1 345 ? 63.649  68.481  102.769 1.00 70.13  ? 345 ILE A CD1   1 
ATOM   2223 N N     . MET A 1 346 ? 68.455  71.513  104.303 1.00 74.92  ? 346 MET A N     1 
ATOM   2224 C CA    . MET A 1 346 ? 69.153  72.459  105.164 1.00 76.76  ? 346 MET A CA    1 
ATOM   2225 C C     . MET A 1 346 ? 69.012  73.890  104.668 1.00 74.48  ? 346 MET A C     1 
ATOM   2226 O O     . MET A 1 346 ? 68.204  74.175  103.779 1.00 74.81  ? 346 MET A O     1 
ATOM   2227 C CB    . MET A 1 346 ? 70.633  72.092  105.258 1.00 73.56  ? 346 MET A CB    1 
ATOM   2228 C CG    . MET A 1 346 ? 71.258  71.763  103.918 1.00 74.06  ? 346 MET A CG    1 
ATOM   2229 S SD    . MET A 1 346 ? 71.810  73.206  102.987 1.00 80.00  ? 346 MET A SD    1 
ATOM   2230 C CE    . MET A 1 346 ? 73.475  73.402  103.612 1.00 73.37  ? 346 MET A CE    1 
ATOM   2231 N N     . SER A 1 347 ? 69.797  74.793  105.248 1.00 73.19  ? 347 SER A N     1 
ATOM   2232 C CA    . SER A 1 347 ? 69.864  76.177  104.806 1.00 75.91  ? 347 SER A CA    1 
ATOM   2233 C C     . SER A 1 347 ? 71.142  76.791  105.352 1.00 79.31  ? 347 SER A C     1 
ATOM   2234 O O     . SER A 1 347 ? 71.651  76.370  106.393 1.00 82.20  ? 347 SER A O     1 
ATOM   2235 C CB    . SER A 1 347 ? 68.645  76.982  105.269 1.00 80.43  ? 347 SER A CB    1 
ATOM   2236 O OG    . SER A 1 347 ? 67.474  76.570  104.587 1.00 85.62  ? 347 SER A OG    1 
ATOM   2237 N N     . LEU A 1 348 ? 71.658  77.784  104.635 1.00 77.88  ? 348 LEU A N     1 
ATOM   2238 C CA    . LEU A 1 348 ? 72.806  78.563  105.080 1.00 75.25  ? 348 LEU A CA    1 
ATOM   2239 C C     . LEU A 1 348 ? 72.377  80.018  105.182 1.00 77.80  ? 348 LEU A C     1 
ATOM   2240 O O     . LEU A 1 348 ? 71.948  80.613  104.187 1.00 83.05  ? 348 LEU A O     1 
ATOM   2241 C CB    . LEU A 1 348 ? 73.991  78.404  104.126 1.00 73.29  ? 348 LEU A CB    1 
ATOM   2242 C CG    . LEU A 1 348 ? 74.592  77.000  104.037 1.00 68.91  ? 348 LEU A CG    1 
ATOM   2243 C CD1   . LEU A 1 348 ? 75.842  77.000  103.172 1.00 66.66  ? 348 LEU A CD1   1 
ATOM   2244 C CD2   . LEU A 1 348 ? 74.897  76.457  105.420 1.00 72.96  ? 348 LEU A CD2   1 
ATOM   2245 N N     . ASN A 1 349 ? 72.489  80.585  106.379 1.00 74.21  ? 349 ASN A N     1 
ATOM   2246 C CA    . ASN A 1 349 ? 72.017  81.933  106.661 1.00 77.51  ? 349 ASN A CA    1 
ATOM   2247 C C     . ASN A 1 349 ? 73.202  82.834  106.972 1.00 81.49  ? 349 ASN A C     1 
ATOM   2248 O O     . ASN A 1 349 ? 74.051  82.487  107.799 1.00 87.09  ? 349 ASN A O     1 
ATOM   2249 C CB    . ASN A 1 349 ? 71.030  81.934  107.830 1.00 87.27  ? 349 ASN A CB    1 
ATOM   2250 C CG    . ASN A 1 349 ? 69.678  81.369  107.451 1.00 89.00  ? 349 ASN A CG    1 
ATOM   2251 O OD1   . ASN A 1 349 ? 69.124  81.703  106.405 1.00 91.49  ? 349 ASN A OD1   1 
ATOM   2252 N ND2   . ASN A 1 349 ? 69.137  80.505  108.302 1.00 87.85  ? 349 ASN A ND2   1 
ATOM   2253 N N     . ASN A 1 350 ? 73.252  83.986  106.310 1.00 82.51  ? 350 ASN A N     1 
ATOM   2254 C CA    . ASN A 1 350 ? 74.304  84.959  106.563 1.00 87.30  ? 350 ASN A CA    1 
ATOM   2255 C C     . ASN A 1 350 ? 74.173  85.530  107.968 1.00 96.20  ? 350 ASN A C     1 
ATOM   2256 O O     . ASN A 1 350 ? 73.073  85.864  108.419 1.00 101.63 ? 350 ASN A O     1 
ATOM   2257 C CB    . ASN A 1 350 ? 74.235  86.080  105.526 1.00 86.43  ? 350 ASN A CB    1 
ATOM   2258 C CG    . ASN A 1 350 ? 75.471  86.952  105.522 1.00 90.67  ? 350 ASN A CG    1 
ATOM   2259 O OD1   . ASN A 1 350 ? 76.481  86.623  106.140 1.00 90.63  ? 350 ASN A OD1   1 
ATOM   2260 N ND2   . ASN A 1 350 ? 75.397  88.075  104.818 1.00 94.47  ? 350 ASN A ND2   1 
ATOM   2261 N N     . LEU A 1 351 ? 75.305  85.636  108.670 1.00 96.70  ? 351 LEU A N     1 
ATOM   2262 C CA    . LEU A 1 351 ? 75.284  86.232  110.002 1.00 98.50  ? 351 LEU A CA    1 
ATOM   2263 C C     . LEU A 1 351 ? 74.879  87.699  109.941 1.00 102.03 ? 351 LEU A C     1 
ATOM   2264 O O     . LEU A 1 351 ? 74.107  88.170  110.784 1.00 108.67 ? 351 LEU A O     1 
ATOM   2265 C CB    . LEU A 1 351 ? 76.642  86.084  110.691 1.00 96.40  ? 351 LEU A CB    1 
ATOM   2266 C CG    . LEU A 1 351 ? 77.230  84.693  110.962 1.00 93.04  ? 351 LEU A CG    1 
ATOM   2267 C CD1   . LEU A 1 351 ? 76.183  83.773  111.574 1.00 91.03  ? 351 LEU A CD1   1 
ATOM   2268 C CD2   . LEU A 1 351 ? 77.865  84.067  109.737 1.00 91.10  ? 351 LEU A CD2   1 
ATOM   2269 N N     . ASP A 1 352 ? 75.385  88.434  108.957 1.00 95.90  ? 352 ASP A N     1 
ATOM   2270 C CA    . ASP A 1 352 ? 75.019  89.836  108.782 1.00 98.24  ? 352 ASP A CA    1 
ATOM   2271 C C     . ASP A 1 352 ? 73.594  89.868  108.247 1.00 100.70 ? 352 ASP A C     1 
ATOM   2272 O O     . ASP A 1 352 ? 73.348  89.578  107.075 1.00 100.50 ? 352 ASP A O     1 
ATOM   2273 C CB    . ASP A 1 352 ? 76.013  90.524  107.847 1.00 103.69 ? 352 ASP A CB    1 
ATOM   2274 C CG    . ASP A 1 352 ? 75.579  91.925  107.418 1.00 110.71 ? 352 ASP A CG    1 
ATOM   2275 O OD1   . ASP A 1 352 ? 74.453  92.116  106.917 1.00 109.65 ? 352 ASP A OD1   1 
ATOM   2276 O OD2   . ASP A 1 352 ? 76.391  92.859  107.590 1.00 112.68 ? 352 ASP A OD2   1 
ATOM   2277 N N     . GLU A 1 353 ? 72.640  90.210  109.117 1.00 104.87 ? 353 GLU A N     1 
ATOM   2278 C CA    . GLU A 1 353 ? 71.236  90.184  108.722 1.00 105.78 ? 353 GLU A CA    1 
ATOM   2279 C C     . GLU A 1 353 ? 70.916  91.258  107.691 1.00 108.12 ? 353 GLU A C     1 
ATOM   2280 O O     . GLU A 1 353 ? 70.092  91.029  106.799 1.00 106.17 ? 353 GLU A O     1 
ATOM   2281 C CB    . GLU A 1 353 ? 70.339  90.344  109.950 1.00 107.28 ? 353 GLU A CB    1 
ATOM   2282 C CG    . GLU A 1 353 ? 70.787  91.430  110.914 1.00 112.73 ? 353 GLU A CG    1 
ATOM   2283 C CD    . GLU A 1 353 ? 71.473  90.870  112.144 1.00 120.79 ? 353 GLU A CD    1 
ATOM   2284 O OE1   . GLU A 1 353 ? 72.314  89.960  111.994 1.00 121.51 ? 353 GLU A OE1   1 
ATOM   2285 O OE2   . GLU A 1 353 ? 71.171  91.339  113.261 1.00 126.41 ? 353 GLU A OE2   1 
ATOM   2286 N N     . GLU A 1 354 ? 71.546  92.424  107.792 1.00 110.31 ? 354 GLU A N     1 
ATOM   2287 C CA    . GLU A 1 354 ? 71.280  93.529  106.872 1.00 108.80 ? 354 GLU A CA    1 
ATOM   2288 C C     . GLU A 1 354 ? 72.110  93.410  105.597 1.00 106.45 ? 354 GLU A C     1 
ATOM   2289 O O     . GLU A 1 354 ? 72.820  94.333  105.203 1.00 104.99 ? 354 GLU A O     1 
ATOM   2290 C CB    . GLU A 1 354 ? 71.536  94.857  107.572 1.00 108.43 ? 354 GLU A CB    1 
ATOM   2291 C CG    . GLU A 1 354 ? 70.558  95.161  108.695 1.00 112.91 ? 354 GLU A CG    1 
ATOM   2292 C CD    . GLU A 1 354 ? 70.215  96.634  108.787 1.00 120.87 ? 354 GLU A CD    1 
ATOM   2293 O OE1   . GLU A 1 354 ? 69.520  97.142  107.882 1.00 119.29 ? 354 GLU A OE1   1 
ATOM   2294 O OE2   . GLU A 1 354 ? 70.639  97.284  109.765 1.00 123.53 ? 354 GLU A OE2   1 
ATOM   2295 N N     . SER A 1 355 ? 72.025  92.255  104.943 1.00 103.61 ? 355 SER A N     1 
ATOM   2296 C CA    . SER A 1 355 ? 72.710  92.007  103.684 1.00 100.05 ? 355 SER A CA    1 
ATOM   2297 C C     . SER A 1 355 ? 71.739  91.361  102.710 1.00 96.72  ? 355 SER A C     1 
ATOM   2298 O O     . SER A 1 355 ? 70.906  90.541  103.104 1.00 95.90  ? 355 SER A O     1 
ATOM   2299 C CB    . SER A 1 355 ? 73.936  91.109  103.879 1.00 97.35  ? 355 SER A CB    1 
ATOM   2300 O OG    . SER A 1 355 ? 74.369  90.566  102.646 1.00 94.83  ? 355 SER A OG    1 
ATOM   2301 N N     . ASN A 1 356 ? 71.850  91.733  101.434 1.00 92.73  ? 356 ASN A N     1 
ATOM   2302 C CA    . ASN A 1 356 ? 70.933  91.220  100.425 1.00 91.81  ? 356 ASN A CA    1 
ATOM   2303 C C     . ASN A 1 356 ? 71.247  89.789  100.012 1.00 90.09  ? 356 ASN A C     1 
ATOM   2304 O O     . ASN A 1 356 ? 70.388  89.129  99.419  1.00 92.07  ? 356 ASN A O     1 
ATOM   2305 C CB    . ASN A 1 356 ? 70.947  92.127  99.194  1.00 94.42  ? 356 ASN A CB    1 
ATOM   2306 C CG    . ASN A 1 356 ? 70.348  93.490  99.471  1.00 98.04  ? 356 ASN A CG    1 
ATOM   2307 O OD1   . ASN A 1 356 ? 71.058  94.492  99.532  1.00 107.50 ? 356 ASN A OD1   1 
ATOM   2308 N ND2   . ASN A 1 356 ? 69.032  93.534  99.642  1.00 93.73  ? 356 ASN A ND2   1 
ATOM   2309 N N     . LYS A 1 357 ? 72.448  89.296  100.307 1.00 86.30  ? 357 LYS A N     1 
ATOM   2310 C CA    . LYS A 1 357 ? 72.830  87.926  99.968  1.00 79.96  ? 357 LYS A CA    1 
ATOM   2311 C C     . LYS A 1 357 ? 72.388  87.021  101.110 1.00 80.26  ? 357 LYS A C     1 
ATOM   2312 O O     . LYS A 1 357 ? 73.136  86.761  102.052 1.00 84.02  ? 357 LYS A O     1 
ATOM   2313 C CB    . LYS A 1 357 ? 74.328  87.831  99.714  1.00 78.70  ? 357 LYS A CB    1 
ATOM   2314 C CG    . LYS A 1 357 ? 74.722  86.747  98.728  1.00 73.81  ? 357 LYS A CG    1 
ATOM   2315 C CD    . LYS A 1 357 ? 76.231  86.605  98.648  1.00 73.41  ? 357 LYS A CD    1 
ATOM   2316 C CE    . LYS A 1 357 ? 76.630  85.433  97.768  1.00 72.80  ? 357 LYS A CE    1 
ATOM   2317 N NZ    . LYS A 1 357 ? 78.088  85.147  97.855  1.00 75.13  ? 357 LYS A NZ    1 
ATOM   2318 N N     . LYS A 1 358 ? 71.146  86.538  101.022 1.00 79.84  ? 358 LYS A N     1 
ATOM   2319 C CA    . LYS A 1 358 ? 70.597  85.699  102.082 1.00 82.94  ? 358 LYS A CA    1 
ATOM   2320 C C     . LYS A 1 358 ? 71.371  84.392  102.207 1.00 78.61  ? 358 LYS A C     1 
ATOM   2321 O O     . LYS A 1 358 ? 71.817  84.022  103.298 1.00 80.79  ? 358 LYS A O     1 
ATOM   2322 C CB    . LYS A 1 358 ? 69.117  85.423  101.815 1.00 82.18  ? 358 LYS A CB    1 
ATOM   2323 C CG    . LYS A 1 358 ? 68.178  86.544  102.234 1.00 87.27  ? 358 LYS A CG    1 
ATOM   2324 C CD    . LYS A 1 358 ? 68.653  87.233  103.501 1.00 94.90  ? 358 LYS A CD    1 
ATOM   2325 C CE    . LYS A 1 358 ? 68.304  88.710  103.482 1.00 99.20  ? 358 LYS A CE    1 
ATOM   2326 N NZ    . LYS A 1 358 ? 69.050  89.470  104.522 1.00 105.25 ? 358 LYS A NZ    1 
ATOM   2327 N N     . HIS A 1 359 ? 71.541  83.682  101.097 1.00 76.91  ? 359 HIS A N     1 
ATOM   2328 C CA    . HIS A 1 359 ? 72.237  82.406  101.069 1.00 70.93  ? 359 HIS A CA    1 
ATOM   2329 C C     . HIS A 1 359 ? 73.157  82.379  99.859  1.00 70.52  ? 359 HIS A C     1 
ATOM   2330 O O     . HIS A 1 359 ? 72.894  83.066  98.865  1.00 75.77  ? 359 HIS A O     1 
ATOM   2331 C CB    . HIS A 1 359 ? 71.253  81.227  100.996 1.00 70.60  ? 359 HIS A CB    1 
ATOM   2332 C CG    . HIS A 1 359 ? 69.951  81.480  101.690 1.00 76.60  ? 359 HIS A CG    1 
ATOM   2333 N ND1   . HIS A 1 359 ? 69.812  81.421  103.060 1.00 80.69  ? 359 HIS A ND1   1 
ATOM   2334 C CD2   . HIS A 1 359 ? 68.728  81.794  101.201 1.00 80.23  ? 359 HIS A CD2   1 
ATOM   2335 C CE1   . HIS A 1 359 ? 68.559  81.687  103.384 1.00 82.96  ? 359 HIS A CE1   1 
ATOM   2336 N NE2   . HIS A 1 359 ? 67.881  81.918  102.275 1.00 82.34  ? 359 HIS A NE2   1 
ATOM   2337 N N     . PRO A 1 360 ? 74.247  81.607  99.914  1.00 64.27  ? 360 PRO A N     1 
ATOM   2338 C CA    . PRO A 1 360 ? 75.112  81.500  98.727  1.00 66.24  ? 360 PRO A CA    1 
ATOM   2339 C C     . PRO A 1 360 ? 74.382  80.958  97.512  1.00 67.89  ? 360 PRO A C     1 
ATOM   2340 O O     . PRO A 1 360 ? 74.659  81.378  96.382  1.00 72.59  ? 360 PRO A O     1 
ATOM   2341 C CB    . PRO A 1 360 ? 76.235  80.563  99.195  1.00 63.07  ? 360 PRO A CB    1 
ATOM   2342 C CG    . PRO A 1 360 ? 75.667  79.830  100.357 1.00 63.74  ? 360 PRO A CG    1 
ATOM   2343 C CD    . PRO A 1 360 ? 74.735  80.783  101.030 1.00 63.59  ? 360 PRO A CD    1 
ATOM   2344 N N     . PHE A 1 361 ? 73.454  80.031  97.718  1.00 67.57  ? 361 PHE A N     1 
ATOM   2345 C CA    . PHE A 1 361 ? 72.536  79.547  96.701  1.00 67.67  ? 361 PHE A CA    1 
ATOM   2346 C C     . PHE A 1 361 ? 71.151  79.492  97.324  1.00 76.03  ? 361 PHE A C     1 
ATOM   2347 O O     . PHE A 1 361 ? 71.030  79.266  98.533  1.00 82.88  ? 361 PHE A O     1 
ATOM   2348 C CB    . PHE A 1 361 ? 72.943  78.161  96.181  1.00 61.69  ? 361 PHE A CB    1 
ATOM   2349 C CG    . PHE A 1 361 ? 73.543  77.271  97.229  1.00 59.24  ? 361 PHE A CG    1 
ATOM   2350 C CD1   . PHE A 1 361 ? 72.744  76.649  98.170  1.00 58.82  ? 361 PHE A CD1   1 
ATOM   2351 C CD2   . PHE A 1 361 ? 74.909  77.052  97.267  1.00 58.91  ? 361 PHE A CD2   1 
ATOM   2352 C CE1   . PHE A 1 361 ? 73.295  75.828  99.132  1.00 60.34  ? 361 PHE A CE1   1 
ATOM   2353 C CE2   . PHE A 1 361 ? 75.465  76.233  98.226  1.00 58.48  ? 361 PHE A CE2   1 
ATOM   2354 C CZ    . PHE A 1 361 ? 74.658  75.620  99.160  1.00 58.57  ? 361 PHE A CZ    1 
ATOM   2355 N N     . PRO A 1 362 ? 70.094  79.701  96.538  1.00 76.48  ? 362 PRO A N     1 
ATOM   2356 C CA    . PRO A 1 362 ? 68.754  79.771  97.133  1.00 80.78  ? 362 PRO A CA    1 
ATOM   2357 C C     . PRO A 1 362 ? 68.395  78.487  97.866  1.00 80.25  ? 362 PRO A C     1 
ATOM   2358 O O     . PRO A 1 362 ? 68.659  77.379  97.395  1.00 77.77  ? 362 PRO A O     1 
ATOM   2359 C CB    . PRO A 1 362 ? 67.841  80.026  95.929  1.00 80.75  ? 362 PRO A CB    1 
ATOM   2360 C CG    . PRO A 1 362 ? 68.580  79.486  94.777  1.00 79.38  ? 362 PRO A CG    1 
ATOM   2361 C CD    . PRO A 1 362 ? 70.038  79.733  95.067  1.00 76.62  ? 362 PRO A CD    1 
ATOM   2362 N N     . CYS A 1 363 ? 67.786  78.657  99.031  1.00 80.90  ? 363 CYS A N     1 
ATOM   2363 C CA    . CYS A 1 363 ? 67.561  77.605  100.008 1.00 78.29  ? 363 CYS A CA    1 
ATOM   2364 C C     . CYS A 1 363 ? 66.138  77.735  100.529 1.00 78.12  ? 363 CYS A C     1 
ATOM   2365 O O     . CYS A 1 363 ? 65.510  78.786  100.364 1.00 79.10  ? 363 CYS A O     1 
ATOM   2366 C CB    . CYS A 1 363 ? 68.580  77.708  101.153 1.00 79.07  ? 363 CYS A CB    1 
ATOM   2367 S SG    . CYS A 1 363 ? 70.223  77.077  100.742 1.00 69.64  ? 363 CYS A SG    1 
ATOM   2368 N N     . PRO A 1 364 ? 65.595  76.682  101.170 1.00 75.73  ? 364 PRO A N     1 
ATOM   2369 C CA    . PRO A 1 364 ? 66.202  75.397  101.566 1.00 76.17  ? 364 PRO A CA    1 
ATOM   2370 C C     . PRO A 1 364 ? 66.454  74.441  100.410 1.00 79.06  ? 364 PRO A C     1 
ATOM   2371 O O     . PRO A 1 364 ? 65.712  74.411  99.433  1.00 84.53  ? 364 PRO A O     1 
ATOM   2372 C CB    . PRO A 1 364 ? 65.169  74.809  102.547 1.00 79.09  ? 364 PRO A CB    1 
ATOM   2373 C CG    . PRO A 1 364 ? 64.261  75.951  102.916 1.00 80.71  ? 364 PRO A CG    1 
ATOM   2374 C CD    . PRO A 1 364 ? 64.224  76.794  101.686 1.00 77.50  ? 364 PRO A CD    1 
ATOM   2375 N N     . THR A 1 365 ? 67.511  73.641  100.516 1.00 74.42  ? 365 THR A N     1 
ATOM   2376 C CA    . THR A 1 365 ? 67.814  72.625  99.520  1.00 72.96  ? 365 THR A CA    1 
ATOM   2377 C C     . THR A 1 365 ? 68.682  71.561  100.171 1.00 69.14  ? 365 THR A C     1 
ATOM   2378 O O     . THR A 1 365 ? 69.321  71.800  101.199 1.00 72.22  ? 365 THR A O     1 
ATOM   2379 C CB    . THR A 1 365 ? 68.513  73.221  98.293  1.00 78.04  ? 365 THR A CB    1 
ATOM   2380 O OG1   . THR A 1 365 ? 68.331  72.352  97.171  1.00 78.37  ? 365 THR A OG1   1 
ATOM   2381 C CG2   . THR A 1 365 ? 70.002  73.396  98.554  1.00 70.71  ? 365 THR A CG2   1 
ATOM   2382 N N     . THR A 1 366 ? 68.690  70.380  99.564  1.00 68.35  ? 366 THR A N     1 
ATOM   2383 C CA    . THR A 1 366 ? 69.495  69.286  100.076 1.00 68.20  ? 366 THR A CA    1 
ATOM   2384 C C     . THR A 1 366 ? 70.948  69.440  99.634  1.00 68.03  ? 366 THR A C     1 
ATOM   2385 O O     . THR A 1 366 ? 71.288  70.274  98.792  1.00 71.58  ? 366 THR A O     1 
ATOM   2386 C CB    . THR A 1 366 ? 68.941  67.942  99.606  1.00 69.14  ? 366 THR A CB    1 
ATOM   2387 O OG1   . THR A 1 366 ? 69.535  67.592  98.350  1.00 70.22  ? 366 THR A OG1   1 
ATOM   2388 C CG2   . THR A 1 366 ? 67.433  68.018  99.439  1.00 72.52  ? 366 THR A CG2   1 
ATOM   2389 N N     . TYR A 1 367 ? 71.816  68.623  100.232 1.00 65.47  ? 367 TYR A N     1 
ATOM   2390 C CA    . TYR A 1 367 ? 73.212  68.591  99.808  1.00 64.31  ? 367 TYR A CA    1 
ATOM   2391 C C     . TYR A 1 367 ? 73.336  68.130  98.362  1.00 66.73  ? 367 TYR A C     1 
ATOM   2392 O O     . TYR A 1 367 ? 74.108  68.703  97.585  1.00 65.36  ? 367 TYR A O     1 
ATOM   2393 C CB    . TYR A 1 367 ? 74.015  67.674  100.728 1.00 68.28  ? 367 TYR A CB    1 
ATOM   2394 C CG    . TYR A 1 367 ? 74.172  68.169  102.146 1.00 76.04  ? 367 TYR A CG    1 
ATOM   2395 C CD1   . TYR A 1 367 ? 73.904  69.487  102.481 1.00 75.18  ? 367 TYR A CD1   1 
ATOM   2396 C CD2   . TYR A 1 367 ? 74.558  67.304  103.159 1.00 81.85  ? 367 TYR A CD2   1 
ATOM   2397 C CE1   . TYR A 1 367 ? 74.048  69.933  103.778 1.00 77.82  ? 367 TYR A CE1   1 
ATOM   2398 C CE2   . TYR A 1 367 ? 74.689  67.740  104.460 1.00 81.07  ? 367 TYR A CE2   1 
ATOM   2399 C CZ    . TYR A 1 367 ? 74.436  69.056  104.764 1.00 81.15  ? 367 TYR A CZ    1 
ATOM   2400 O OH    . TYR A 1 367 ? 74.571  69.498  106.059 1.00 85.71  ? 367 TYR A OH    1 
ATOM   2401 N N     . ARG A 1 368 ? 72.581  67.097  97.984  1.00 66.94  ? 368 ARG A N     1 
ATOM   2402 C CA    . ARG A 1 368 ? 72.676  66.559  96.630  1.00 60.42  ? 368 ARG A CA    1 
ATOM   2403 C C     . ARG A 1 368 ? 72.314  67.615  95.595  1.00 59.55  ? 368 ARG A C     1 
ATOM   2404 O O     . ARG A 1 368 ? 73.020  67.793  94.596  1.00 58.75  ? 368 ARG A O     1 
ATOM   2405 C CB    . ARG A 1 368 ? 71.771  65.335  96.494  1.00 64.82  ? 368 ARG A CB    1 
ATOM   2406 C CG    . ARG A 1 368 ? 72.007  64.518  95.238  1.00 69.69  ? 368 ARG A CG    1 
ATOM   2407 C CD    . ARG A 1 368 ? 71.225  63.217  95.279  1.00 70.41  ? 368 ARG A CD    1 
ATOM   2408 N NE    . ARG A 1 368 ? 71.776  62.281  96.251  1.00 73.53  ? 368 ARG A NE    1 
ATOM   2409 C CZ    . ARG A 1 368 ? 72.876  61.565  96.062  1.00 73.85  ? 368 ARG A CZ    1 
ATOM   2410 N NH1   . ARG A 1 368 ? 73.572  61.648  94.940  1.00 72.69  ? 368 ARG A NH1   1 
ATOM   2411 N NH2   . ARG A 1 368 ? 73.289  60.745  97.024  1.00 70.98  ? 368 ARG A NH2   1 
ATOM   2412 N N     . THR A 1 369 ? 71.220  68.342  95.830  1.00 60.15  ? 369 THR A N     1 
ATOM   2413 C CA    . THR A 1 369 ? 70.837  69.408  94.912  1.00 59.12  ? 369 THR A CA    1 
ATOM   2414 C C     . THR A 1 369 ? 71.895  70.502  94.873  1.00 57.70  ? 369 THR A C     1 
ATOM   2415 O O     . THR A 1 369 ? 72.206  71.037  93.804  1.00 60.72  ? 369 THR A O     1 
ATOM   2416 C CB    . THR A 1 369 ? 69.480  69.984  95.311  1.00 61.71  ? 369 THR A CB    1 
ATOM   2417 O OG1   . THR A 1 369 ? 68.505  68.935  95.333  1.00 64.65  ? 369 THR A OG1   1 
ATOM   2418 C CG2   . THR A 1 369 ? 69.039  71.042  94.317  1.00 65.52  ? 369 THR A CG2   1 
ATOM   2419 N N     . ALA A 1 370 ? 72.466  70.842  96.030  1.00 58.04  ? 370 ALA A N     1 
ATOM   2420 C CA    . ALA A 1 370 ? 73.470  71.900  96.078  1.00 55.50  ? 370 ALA A CA    1 
ATOM   2421 C C     . ALA A 1 370 ? 74.705  71.535  95.264  1.00 53.81  ? 370 ALA A C     1 
ATOM   2422 O O     . ALA A 1 370 ? 75.228  72.368  94.516  1.00 56.18  ? 370 ALA A O     1 
ATOM   2423 C CB    . ALA A 1 370 ? 73.852  72.197  97.527  1.00 56.10  ? 370 ALA A CB    1 
ATOM   2424 N N     . LEU A 1 371 ? 75.187  70.299  95.391  1.00 53.82  ? 371 LEU A N     1 
ATOM   2425 C CA    . LEU A 1 371 ? 76.365  69.900  94.629  1.00 52.13  ? 371 LEU A CA    1 
ATOM   2426 C C     . LEU A 1 371 ? 76.055  69.486  93.196  1.00 55.71  ? 371 LEU A C     1 
ATOM   2427 O O     . LEU A 1 371 ? 76.992  69.329  92.407  1.00 59.92  ? 371 LEU A O     1 
ATOM   2428 C CB    . LEU A 1 371 ? 77.117  68.763  95.329  1.00 58.09  ? 371 LEU A CB    1 
ATOM   2429 C CG    . LEU A 1 371 ? 77.896  69.070  96.612  1.00 58.03  ? 371 LEU A CG    1 
ATOM   2430 C CD1   . LEU A 1 371 ? 77.132  68.694  97.863  1.00 53.43  ? 371 LEU A CD1   1 
ATOM   2431 C CD2   . LEU A 1 371 ? 79.241  68.368  96.580  1.00 59.17  ? 371 LEU A CD2   1 
ATOM   2432 N N     . THR A 1 372 ? 74.785  69.303  92.833  1.00 57.19  ? 372 THR A N     1 
ATOM   2433 C CA    . THR A 1 372 ? 74.476  68.995  91.441  1.00 56.67  ? 372 THR A CA    1 
ATOM   2434 C C     . THR A 1 372 ? 74.141  70.235  90.621  1.00 55.06  ? 372 THR A C     1 
ATOM   2435 O O     . THR A 1 372 ? 74.720  70.442  89.551  1.00 53.14  ? 372 THR A O     1 
ATOM   2436 C CB    . THR A 1 372 ? 73.309  68.008  91.350  1.00 58.31  ? 372 THR A CB    1 
ATOM   2437 O OG1   . THR A 1 372 ? 72.244  68.443  92.203  1.00 63.51  ? 372 THR A OG1   1 
ATOM   2438 C CG2   . THR A 1 372 ? 73.746  66.611  91.750  1.00 63.02  ? 372 THR A CG2   1 
ATOM   2439 N N     . TYR A 1 373 ? 73.220  71.069  91.099  1.00 55.40  ? 373 TYR A N     1 
ATOM   2440 C CA    . TYR A 1 373 ? 72.681  72.152  90.294  1.00 51.36  ? 373 TYR A CA    1 
ATOM   2441 C C     . TYR A 1 373 ? 73.134  73.539  90.721  1.00 50.96  ? 373 TYR A C     1 
ATOM   2442 O O     . TYR A 1 373 ? 72.894  74.495  89.976  1.00 54.39  ? 373 TYR A O     1 
ATOM   2443 C CB    . TYR A 1 373 ? 71.145  72.124  90.326  1.00 52.03  ? 373 TYR A CB    1 
ATOM   2444 C CG    . TYR A 1 373 ? 70.533  70.793  89.959  1.00 52.88  ? 373 TYR A CG    1 
ATOM   2445 C CD1   . TYR A 1 373 ? 71.005  70.057  88.884  1.00 57.10  ? 373 TYR A CD1   1 
ATOM   2446 C CD2   . TYR A 1 373 ? 69.481  70.270  90.697  1.00 58.55  ? 373 TYR A CD2   1 
ATOM   2447 C CE1   . TYR A 1 373 ? 70.443  68.838  88.554  1.00 59.88  ? 373 TYR A CE1   1 
ATOM   2448 C CE2   . TYR A 1 373 ? 68.914  69.056  90.374  1.00 65.55  ? 373 TYR A CE2   1 
ATOM   2449 C CZ    . TYR A 1 373 ? 69.398  68.344  89.302  1.00 60.78  ? 373 TYR A CZ    1 
ATOM   2450 O OH    . TYR A 1 373 ? 68.834  67.132  88.979  1.00 56.62  ? 373 TYR A OH    1 
ATOM   2451 N N     . TYR A 1 374 ? 73.765  73.688  91.886  1.00 49.89  ? 374 TYR A N     1 
ATOM   2452 C CA    . TYR A 1 374 ? 74.019  75.006  92.450  1.00 45.83  ? 374 TYR A CA    1 
ATOM   2453 C C     . TYR A 1 374 ? 75.485  75.286  92.748  1.00 42.48  ? 374 TYR A C     1 
ATOM   2454 O O     . TYR A 1 374 ? 75.804  76.397  93.183  1.00 43.80  ? 374 TYR A O     1 
ATOM   2455 C CB    . TYR A 1 374 ? 73.216  75.205  93.744  1.00 51.21  ? 374 TYR A CB    1 
ATOM   2456 C CG    . TYR A 1 374 ? 71.715  75.275  93.569  1.00 57.16  ? 374 TYR A CG    1 
ATOM   2457 C CD1   . TYR A 1 374 ? 71.004  74.204  93.058  1.00 65.18  ? 374 TYR A CD1   1 
ATOM   2458 C CD2   . TYR A 1 374 ? 71.013  76.418  93.907  1.00 61.00  ? 374 TYR A CD2   1 
ATOM   2459 C CE1   . TYR A 1 374 ? 69.641  74.264  92.896  1.00 71.86  ? 374 TYR A CE1   1 
ATOM   2460 C CE2   . TYR A 1 374 ? 69.648  76.486  93.747  1.00 69.44  ? 374 TYR A CE2   1 
ATOM   2461 C CZ    . TYR A 1 374 ? 68.967  75.408  93.242  1.00 76.14  ? 374 TYR A CZ    1 
ATOM   2462 O OH    . TYR A 1 374 ? 67.603  75.475  93.080  1.00 82.77  ? 374 TYR A OH    1 
ATOM   2463 N N     . LEU A 1 375 ? 76.382  74.329  92.539  1.00 43.67  ? 375 LEU A N     1 
ATOM   2464 C CA    . LEU A 1 375 ? 77.780  74.501  92.899  1.00 40.65  ? 375 LEU A CA    1 
ATOM   2465 C C     . LEU A 1 375 ? 78.667  74.132  91.722  1.00 41.46  ? 375 LEU A C     1 
ATOM   2466 O O     . LEU A 1 375 ? 78.225  73.514  90.751  1.00 46.77  ? 375 LEU A O     1 
ATOM   2467 C CB    . LEU A 1 375 ? 78.160  73.651  94.119  1.00 47.71  ? 375 LEU A CB    1 
ATOM   2468 C CG    . LEU A 1 375 ? 77.921  74.268  95.497  1.00 46.13  ? 375 LEU A CG    1 
ATOM   2469 C CD1   . LEU A 1 375 ? 78.296  73.281  96.587  1.00 50.03  ? 375 LEU A CD1   1 
ATOM   2470 C CD2   . LEU A 1 375 ? 78.695  75.563  95.656  1.00 42.04  ? 375 LEU A CD2   1 
ATOM   2471 N N     . ASP A 1 376 ? 79.934  74.522  91.822  1.00 41.18  ? 376 ASP A N     1 
ATOM   2472 C CA    . ASP A 1 376 ? 80.930  74.264  90.789  1.00 48.08  ? 376 ASP A CA    1 
ATOM   2473 C C     . ASP A 1 376 ? 82.041  73.447  91.432  1.00 50.02  ? 376 ASP A C     1 
ATOM   2474 O O     . ASP A 1 376 ? 82.884  73.995  92.149  1.00 52.84  ? 376 ASP A O     1 
ATOM   2475 C CB    . ASP A 1 376 ? 81.458  75.576  90.206  1.00 51.34  ? 376 ASP A CB    1 
ATOM   2476 C CG    . ASP A 1 376 ? 82.441  75.370  89.064  1.00 63.43  ? 376 ASP A CG    1 
ATOM   2477 O OD1   . ASP A 1 376 ? 82.909  74.232  88.850  1.00 69.60  ? 376 ASP A OD1   1 
ATOM   2478 O OD2   . ASP A 1 376 ? 82.746  76.362  88.369  1.00 60.31  ? 376 ASP A OD2   1 
ATOM   2479 N N     . ILE A 1 377 ? 82.043  72.142  91.175  1.00 55.17  ? 377 ILE A N     1 
ATOM   2480 C CA    . ILE A 1 377 ? 82.995  71.229  91.789  1.00 61.67  ? 377 ILE A CA    1 
ATOM   2481 C C     . ILE A 1 377 ? 84.001  70.699  90.769  1.00 66.06  ? 377 ILE A C     1 
ATOM   2482 O O     . ILE A 1 377 ? 84.710  69.739  91.041  1.00 71.25  ? 377 ILE A O     1 
ATOM   2483 C CB    . ILE A 1 377 ? 82.270  70.072  92.504  1.00 58.16  ? 377 ILE A CB    1 
ATOM   2484 C CG1   . ILE A 1 377 ? 81.684  69.096  91.485  1.00 55.12  ? 377 ILE A CG1   1 
ATOM   2485 C CG2   . ILE A 1 377 ? 81.171  70.609  93.401  1.00 54.39  ? 377 ILE A CG2   1 
ATOM   2486 C CD1   . ILE A 1 377 ? 80.721  68.095  92.075  1.00 58.35  ? 377 ILE A CD1   1 
ATOM   2487 N N     . THR A 1 378 ? 84.075  71.322  89.595  1.00 58.56  ? 378 THR A N     1 
ATOM   2488 C CA    . THR A 1 378 ? 84.913  70.842  88.503  1.00 59.40  ? 378 THR A CA    1 
ATOM   2489 C C     . THR A 1 378 ? 86.162  71.678  88.274  1.00 66.34  ? 378 THR A C     1 
ATOM   2490 O O     . THR A 1 378 ? 87.232  71.119  88.024  1.00 68.31  ? 378 THR A O     1 
ATOM   2491 C CB    . THR A 1 378 ? 84.104  70.790  87.204  1.00 60.96  ? 378 THR A CB    1 
ATOM   2492 O OG1   . THR A 1 378 ? 82.807  70.245  87.473  1.00 60.46  ? 378 THR A OG1   1 
ATOM   2493 C CG2   . THR A 1 378 ? 84.807  69.922  86.175  1.00 67.24  ? 378 THR A CG2   1 
ATOM   2494 N N     . ASN A 1 379 ? 86.058  73.000  88.337  1.00 68.39  ? 379 ASN A N     1 
ATOM   2495 C CA    . ASN A 1 379 ? 87.214  73.856  88.135  1.00 65.77  ? 379 ASN A CA    1 
ATOM   2496 C C     . ASN A 1 379 ? 88.075  73.901  89.395  1.00 65.47  ? 379 ASN A C     1 
ATOM   2497 O O     . ASN A 1 379 ? 87.587  73.650  90.499  1.00 66.44  ? 379 ASN A O     1 
ATOM   2498 C CB    . ASN A 1 379 ? 86.763  75.259  87.740  1.00 61.38  ? 379 ASN A CB    1 
ATOM   2499 C CG    . ASN A 1 379 ? 85.717  75.819  88.675  1.00 67.84  ? 379 ASN A CG    1 
ATOM   2500 O OD1   . ASN A 1 379 ? 85.413  75.230  89.711  1.00 68.39  ? 379 ASN A OD1   1 
ATOM   2501 N ND2   . ASN A 1 379 ? 85.150  76.962  88.309  1.00 68.03  ? 379 ASN A ND2   1 
ATOM   2502 N N     . PRO A 1 380 ? 89.364  74.199  89.254  1.00 63.15  ? 380 PRO A N     1 
ATOM   2503 C CA    . PRO A 1 380 ? 90.252  74.245  90.419  1.00 64.46  ? 380 PRO A CA    1 
ATOM   2504 C C     . PRO A 1 380 ? 89.792  75.286  91.421  1.00 64.61  ? 380 PRO A C     1 
ATOM   2505 O O     . PRO A 1 380 ? 89.313  76.364  91.038  1.00 68.59  ? 380 PRO A O     1 
ATOM   2506 C CB    . PRO A 1 380 ? 91.610  74.622  89.810  1.00 66.25  ? 380 PRO A CB    1 
ATOM   2507 C CG    . PRO A 1 380 ? 91.526  74.162  88.407  1.00 68.45  ? 380 PRO A CG    1 
ATOM   2508 C CD    . PRO A 1 380 ? 90.106  74.398  87.998  1.00 65.68  ? 380 PRO A CD    1 
ATOM   2509 N N     . PRO A 1 381 ? 89.915  75.002  92.713  1.00 59.08  ? 381 PRO A N     1 
ATOM   2510 C CA    . PRO A 1 381 ? 89.507  75.972  93.730  1.00 61.37  ? 381 PRO A CA    1 
ATOM   2511 C C     . PRO A 1 381 ? 90.509  77.110  93.853  1.00 71.16  ? 381 PRO A C     1 
ATOM   2512 O O     . PRO A 1 381 ? 91.686  76.987  93.511  1.00 73.78  ? 381 PRO A O     1 
ATOM   2513 C CB    . PRO A 1 381 ? 89.459  75.143  95.021  1.00 57.37  ? 381 PRO A CB    1 
ATOM   2514 C CG    . PRO A 1 381 ? 89.623  73.706  94.592  1.00 56.23  ? 381 PRO A CG    1 
ATOM   2515 C CD    . PRO A 1 381 ? 90.385  73.747  93.315  1.00 56.99  ? 381 PRO A CD    1 
ATOM   2516 N N     . ARG A 1 382 ? 90.013  78.236  94.358  1.00 71.72  ? 382 ARG A N     1 
ATOM   2517 C CA    . ARG A 1 382 ? 90.869  79.382  94.606  1.00 70.39  ? 382 ARG A CA    1 
ATOM   2518 C C     . ARG A 1 382 ? 91.711  79.159  95.861  1.00 71.59  ? 382 ARG A C     1 
ATOM   2519 O O     . ARG A 1 382 ? 91.521  78.198  96.611  1.00 76.82  ? 382 ARG A O     1 
ATOM   2520 C CB    . ARG A 1 382 ? 90.034  80.653  94.738  1.00 75.79  ? 382 ARG A CB    1 
ATOM   2521 C CG    . ARG A 1 382 ? 89.920  81.449  93.453  1.00 81.90  ? 382 ARG A CG    1 
ATOM   2522 C CD    . ARG A 1 382 ? 88.834  80.905  92.546  1.00 78.88  ? 382 ARG A CD    1 
ATOM   2523 N NE    . ARG A 1 382 ? 88.491  81.856  91.495  1.00 87.33  ? 382 ARG A NE    1 
ATOM   2524 C CZ    . ARG A 1 382 ? 89.177  82.008  90.372  1.00 92.36  ? 382 ARG A CZ    1 
ATOM   2525 N NH1   . ARG A 1 382 ? 90.258  81.288  90.119  1.00 91.49  ? 382 ARG A NH1   1 
ATOM   2526 N NH2   . ARG A 1 382 ? 88.771  82.907  89.480  1.00 94.52  ? 382 ARG A NH2   1 
ATOM   2527 N N     . THR A 1 383 ? 92.663  80.068  96.080  1.00 69.57  ? 383 THR A N     1 
ATOM   2528 C CA    . THR A 1 383 ? 93.552  79.947  97.231  1.00 69.11  ? 383 THR A CA    1 
ATOM   2529 C C     . THR A 1 383 ? 92.805  80.121  98.546  1.00 69.99  ? 383 THR A C     1 
ATOM   2530 O O     . THR A 1 383 ? 93.169  79.493  99.549  1.00 76.06  ? 383 THR A O     1 
ATOM   2531 C CB    . THR A 1 383 ? 94.684  80.966  97.131  1.00 75.32  ? 383 THR A CB    1 
ATOM   2532 O OG1   . THR A 1 383 ? 94.134  82.272  96.920  1.00 82.14  ? 383 THR A OG1   1 
ATOM   2533 C CG2   . THR A 1 383 ? 95.610  80.618  95.979  1.00 80.06  ? 383 THR A CG2   1 
ATOM   2534 N N     . ASN A 1 384 ? 91.771  80.964  98.569  1.00 67.01  ? 384 ASN A N     1 
ATOM   2535 C CA    . ASN A 1 384 ? 91.024  81.171  99.804  1.00 68.09  ? 384 ASN A CA    1 
ATOM   2536 C C     . ASN A 1 384 ? 90.312  79.902  100.259 1.00 69.73  ? 384 ASN A C     1 
ATOM   2537 O O     . ASN A 1 384 ? 90.235  79.639  101.463 1.00 72.50  ? 384 ASN A O     1 
ATOM   2538 C CB    . ASN A 1 384 ? 90.059  82.358  99.642  1.00 70.36  ? 384 ASN A CB    1 
ATOM   2539 C CG    . ASN A 1 384 ? 88.645  81.954  99.220  1.00 71.71  ? 384 ASN A CG    1 
ATOM   2540 O OD1   . ASN A 1 384 ? 88.421  80.908  98.615  1.00 71.64  ? 384 ASN A OD1   1 
ATOM   2541 N ND2   . ASN A 1 384 ? 87.679  82.802  99.553  1.00 74.20  ? 384 ASN A ND2   1 
ATOM   2542 N N     . VAL A 1 385 ? 89.798  79.105  99.320  1.00 70.35  ? 385 VAL A N     1 
ATOM   2543 C CA    . VAL A 1 385 ? 89.139  77.853  99.684  1.00 63.10  ? 385 VAL A CA    1 
ATOM   2544 C C     . VAL A 1 385 ? 90.127  76.913  100.360 1.00 64.06  ? 385 VAL A C     1 
ATOM   2545 O O     . VAL A 1 385 ? 89.831  76.310  101.397 1.00 70.54  ? 385 VAL A O     1 
ATOM   2546 C CB    . VAL A 1 385 ? 88.501  77.202  98.443  1.00 61.71  ? 385 VAL A CB    1 
ATOM   2547 C CG1   . VAL A 1 385 ? 88.145  75.755  98.727  1.00 61.74  ? 385 VAL A CG1   1 
ATOM   2548 C CG2   . VAL A 1 385 ? 87.273  77.980  98.005  1.00 63.40  ? 385 VAL A CG2   1 
ATOM   2549 N N     . LEU A 1 386 ? 91.323  76.781  99.785  1.00 64.16  ? 386 LEU A N     1 
ATOM   2550 C CA    . LEU A 1 386 ? 92.328  75.900  100.370 1.00 68.90  ? 386 LEU A CA    1 
ATOM   2551 C C     . LEU A 1 386 ? 92.790  76.411  101.729 1.00 75.36  ? 386 LEU A C     1 
ATOM   2552 O O     . LEU A 1 386 ? 92.996  75.621  102.659 1.00 75.24  ? 386 LEU A O     1 
ATOM   2553 C CB    . LEU A 1 386 ? 93.513  75.747  99.416  1.00 67.29  ? 386 LEU A CB    1 
ATOM   2554 C CG    . LEU A 1 386 ? 93.364  74.663  98.346  1.00 69.39  ? 386 LEU A CG    1 
ATOM   2555 C CD1   . LEU A 1 386 ? 92.371  75.076  97.273  1.00 67.13  ? 386 LEU A CD1   1 
ATOM   2556 C CD2   . LEU A 1 386 ? 94.706  74.323  97.730  1.00 71.41  ? 386 LEU A CD2   1 
ATOM   2557 N N     . TYR A 1 387 ? 92.962  77.727  101.867 1.00 76.07  ? 387 TYR A N     1 
ATOM   2558 C CA    . TYR A 1 387 ? 93.357  78.279  103.159 1.00 75.71  ? 387 TYR A CA    1 
ATOM   2559 C C     . TYR A 1 387 ? 92.282  78.034  104.212 1.00 77.09  ? 387 TYR A C     1 
ATOM   2560 O O     . TYR A 1 387 ? 92.593  77.708  105.363 1.00 87.18  ? 387 TYR A O     1 
ATOM   2561 C CB    . TYR A 1 387 ? 93.654  79.772  103.025 1.00 78.77  ? 387 TYR A CB    1 
ATOM   2562 C CG    . TYR A 1 387 ? 94.120  80.421  104.308 1.00 84.33  ? 387 TYR A CG    1 
ATOM   2563 C CD1   . TYR A 1 387 ? 95.442  80.315  104.719 1.00 89.03  ? 387 TYR A CD1   1 
ATOM   2564 C CD2   . TYR A 1 387 ? 93.243  81.143  105.105 1.00 84.15  ? 387 TYR A CD2   1 
ATOM   2565 C CE1   . TYR A 1 387 ? 95.876  80.905  105.888 1.00 89.22  ? 387 TYR A CE1   1 
ATOM   2566 C CE2   . TYR A 1 387 ? 93.669  81.737  106.277 1.00 91.62  ? 387 TYR A CE2   1 
ATOM   2567 C CZ    . TYR A 1 387 ? 94.986  81.615  106.663 1.00 94.89  ? 387 TYR A CZ    1 
ATOM   2568 O OH    . TYR A 1 387 ? 95.416  82.205  107.828 1.00 105.46 ? 387 TYR A OH    1 
ATOM   2569 N N     . GLU A 1 388 ? 91.010  78.182  103.835 1.00 72.73  ? 388 GLU A N     1 
ATOM   2570 C CA    . GLU A 1 388 ? 89.914  77.934  104.763 1.00 72.31  ? 388 GLU A CA    1 
ATOM   2571 C C     . GLU A 1 388 ? 89.730  76.453  105.067 1.00 70.49  ? 388 GLU A C     1 
ATOM   2572 O O     . GLU A 1 388 ? 89.141  76.114  106.097 1.00 74.39  ? 388 GLU A O     1 
ATOM   2573 C CB    . GLU A 1 388 ? 88.616  78.509  104.199 1.00 73.52  ? 388 GLU A CB    1 
ATOM   2574 C CG    . GLU A 1 388 ? 87.692  79.119  105.233 1.00 78.92  ? 388 GLU A CG    1 
ATOM   2575 C CD    . GLU A 1 388 ? 88.032  80.563  105.533 1.00 88.68  ? 388 GLU A CD    1 
ATOM   2576 O OE1   . GLU A 1 388 ? 88.822  81.158  104.772 1.00 82.07  ? 388 GLU A OE1   1 
ATOM   2577 O OE2   . GLU A 1 388 ? 87.501  81.106  106.524 1.00 102.92 ? 388 GLU A OE2   1 
ATOM   2578 N N     . LEU A 1 389 ? 90.186  75.567  104.183 1.00 71.03  ? 389 LEU A N     1 
ATOM   2579 C CA    . LEU A 1 389 ? 90.107  74.133  104.428 1.00 73.93  ? 389 LEU A CA    1 
ATOM   2580 C C     . LEU A 1 389 ? 91.361  73.566  105.078 1.00 80.40  ? 389 LEU A C     1 
ATOM   2581 O O     . LEU A 1 389 ? 91.373  72.382  105.431 1.00 82.56  ? 389 LEU A O     1 
ATOM   2582 C CB    . LEU A 1 389 ? 89.846  73.384  103.118 1.00 75.13  ? 389 LEU A CB    1 
ATOM   2583 C CG    . LEU A 1 389 ? 88.424  73.425  102.559 1.00 70.19  ? 389 LEU A CG    1 
ATOM   2584 C CD1   . LEU A 1 389 ? 88.258  72.388  101.463 1.00 65.33  ? 389 LEU A CD1   1 
ATOM   2585 C CD2   . LEU A 1 389 ? 87.403  73.213  103.663 1.00 67.15  ? 389 LEU A CD2   1 
ATOM   2586 N N     . ALA A 1 390 ? 92.414  74.374  105.225 1.00 81.33  ? 390 ALA A N     1 
ATOM   2587 C CA    . ALA A 1 390 ? 93.665  73.869  105.783 1.00 86.91  ? 390 ALA A CA    1 
ATOM   2588 C C     . ALA A 1 390 ? 93.480  73.306  107.188 1.00 90.80  ? 390 ALA A C     1 
ATOM   2589 O O     . ALA A 1 390 ? 94.001  72.229  107.501 1.00 94.73  ? 390 ALA A O     1 
ATOM   2590 C CB    . ALA A 1 390 ? 94.717  74.978  105.793 1.00 90.68  ? 390 ALA A CB    1 
ATOM   2591 N N     . GLN A 1 391 ? 92.735  74.007  108.047 1.00 88.13  ? 391 GLN A N     1 
ATOM   2592 C CA    . GLN A 1 391 ? 92.635  73.592  109.443 1.00 85.04  ? 391 GLN A CA    1 
ATOM   2593 C C     . GLN A 1 391 ? 91.913  72.264  109.626 1.00 84.54  ? 391 GLN A C     1 
ATOM   2594 O O     . GLN A 1 391 ? 91.982  71.693  110.719 1.00 89.48  ? 391 GLN A O     1 
ATOM   2595 C CB    . GLN A 1 391 ? 91.934  74.664  110.278 1.00 78.86  ? 391 GLN A CB    1 
ATOM   2596 C CG    . GLN A 1 391 ? 90.426  74.683  110.133 1.00 75.40  ? 391 GLN A CG    1 
ATOM   2597 C CD    . GLN A 1 391 ? 89.959  75.764  109.189 1.00 82.73  ? 391 GLN A CD    1 
ATOM   2598 O OE1   . GLN A 1 391 ? 90.697  76.180  108.298 1.00 85.37  ? 391 GLN A OE1   1 
ATOM   2599 N NE2   . GLN A 1 391 ? 88.730  76.230  109.380 1.00 84.56  ? 391 GLN A NE2   1 
ATOM   2600 N N     . TYR A 1 392 ? 91.227  71.763  108.604 1.00 80.52  ? 392 TYR A N     1 
ATOM   2601 C CA    . TYR A 1 392 ? 90.552  70.476  108.692 1.00 82.11  ? 392 TYR A CA    1 
ATOM   2602 C C     . TYR A 1 392 ? 91.458  69.306  108.335 1.00 85.85  ? 392 TYR A C     1 
ATOM   2603 O O     . TYR A 1 392 ? 91.012  68.157  108.396 1.00 84.85  ? 392 TYR A O     1 
ATOM   2604 C CB    . TYR A 1 392 ? 89.315  70.466  107.791 1.00 81.92  ? 392 TYR A CB    1 
ATOM   2605 C CG    . TYR A 1 392 ? 88.195  71.344  108.297 1.00 80.56  ? 392 TYR A CG    1 
ATOM   2606 C CD1   . TYR A 1 392 ? 87.635  71.133  109.547 1.00 80.61  ? 392 TYR A CD1   1 
ATOM   2607 C CD2   . TYR A 1 392 ? 87.698  72.382  107.524 1.00 79.54  ? 392 TYR A CD2   1 
ATOM   2608 C CE1   . TYR A 1 392 ? 86.612  71.932  110.015 1.00 83.71  ? 392 TYR A CE1   1 
ATOM   2609 C CE2   . TYR A 1 392 ? 86.674  73.186  107.983 1.00 79.27  ? 392 TYR A CE2   1 
ATOM   2610 C CZ    . TYR A 1 392 ? 86.135  72.957  109.229 1.00 84.24  ? 392 TYR A CZ    1 
ATOM   2611 O OH    . TYR A 1 392 ? 85.115  73.755  109.691 1.00 87.88  ? 392 TYR A OH    1 
ATOM   2612 N N     . ALA A 1 393 ? 92.710  69.566  107.969 1.00 89.04  ? 393 ALA A N     1 
ATOM   2613 C CA    . ALA A 1 393 ? 93.649  68.499  107.648 1.00 95.90  ? 393 ALA A CA    1 
ATOM   2614 C C     . ALA A 1 393 ? 94.277  67.970  108.932 1.00 102.14 ? 393 ALA A C     1 
ATOM   2615 O O     . ALA A 1 393 ? 94.881  68.732  109.695 1.00 101.64 ? 393 ALA A O     1 
ATOM   2616 C CB    . ALA A 1 393 ? 94.724  69.003  106.688 1.00 91.62  ? 393 ALA A CB    1 
ATOM   2617 N N     . SER A 1 394 ? 94.133  66.666  109.172 1.00 99.19  ? 394 SER A N     1 
ATOM   2618 C CA    . SER A 1 394 ? 94.675  66.073  110.390 1.00 97.82  ? 394 SER A CA    1 
ATOM   2619 C C     . SER A 1 394 ? 96.197  66.009  110.346 1.00 101.51 ? 394 SER A C     1 
ATOM   2620 O O     . SER A 1 394 ? 96.871  66.367  111.319 1.00 101.58 ? 394 SER A O     1 
ATOM   2621 C CB    . SER A 1 394 ? 94.082  64.680  110.601 1.00 99.68  ? 394 SER A CB    1 
ATOM   2622 O OG    . SER A 1 394 ? 94.449  63.807  109.548 1.00 104.64 ? 394 SER A OG    1 
ATOM   2623 N N     . GLU A 1 395 ? 96.755  65.556  109.231 1.00 103.10 ? 395 GLU A N     1 
ATOM   2624 C CA    . GLU A 1 395 ? 98.202  65.403  109.132 1.00 108.77 ? 395 GLU A CA    1 
ATOM   2625 C C     . GLU A 1 395 ? 98.870  66.774  109.080 1.00 110.90 ? 395 GLU A C     1 
ATOM   2626 O O     . GLU A 1 395 ? 98.464  67.625  108.280 1.00 110.26 ? 395 GLU A O     1 
ATOM   2627 C CB    . GLU A 1 395 ? 98.570  64.584  107.898 1.00 111.58 ? 395 GLU A CB    1 
ATOM   2628 C CG    . GLU A 1 395 ? 100.063 64.482  107.646 1.00 116.14 ? 395 GLU A CG    1 
ATOM   2629 C CD    . GLU A 1 395 ? 100.403 63.516  106.529 1.00 119.30 ? 395 GLU A CD    1 
ATOM   2630 O OE1   . GLU A 1 395 ? 99.477  62.862  106.005 1.00 120.58 ? 395 GLU A OE1   1 
ATOM   2631 O OE2   . GLU A 1 395 ? 101.596 63.410  106.175 1.00 120.68 ? 395 GLU A OE2   1 
ATOM   2632 N N     . PRO A 1 396 ? 99.880  67.030  109.918 1.00 111.58 ? 396 PRO A N     1 
ATOM   2633 C CA    . PRO A 1 396 ? 100.490 68.372  109.938 1.00 111.62 ? 396 PRO A CA    1 
ATOM   2634 C C     . PRO A 1 396 ? 101.111 68.793  108.616 1.00 111.88 ? 396 PRO A C     1 
ATOM   2635 O O     . PRO A 1 396 ? 101.043 69.976  108.263 1.00 110.92 ? 396 PRO A O     1 
ATOM   2636 C CB    . PRO A 1 396 ? 101.543 68.257  111.050 1.00 113.51 ? 396 PRO A CB    1 
ATOM   2637 C CG    . PRO A 1 396 ? 101.813 66.792  111.177 1.00 115.90 ? 396 PRO A CG    1 
ATOM   2638 C CD    . PRO A 1 396 ? 100.510 66.118  110.886 1.00 112.91 ? 396 PRO A CD    1 
ATOM   2639 N N     . SER A 1 397 ? 101.723 67.866  107.874 1.00 111.76 ? 397 SER A N     1 
ATOM   2640 C CA    . SER A 1 397 ? 102.365 68.241  106.617 1.00 114.77 ? 397 SER A CA    1 
ATOM   2641 C C     . SER A 1 397 ? 101.340 68.672  105.575 1.00 115.88 ? 397 SER A C     1 
ATOM   2642 O O     . SER A 1 397 ? 101.544 69.666  104.866 1.00 113.30 ? 397 SER A O     1 
ATOM   2643 C CB    . SER A 1 397 ? 103.212 67.083  106.091 1.00 117.96 ? 397 SER A CB    1 
ATOM   2644 O OG    . SER A 1 397 ? 102.481 65.871  106.092 1.00 117.04 ? 397 SER A OG    1 
ATOM   2645 N N     . GLU A 1 398 ? 100.232 67.937  105.465 1.00 113.76 ? 398 GLU A N     1 
ATOM   2646 C CA    . GLU A 1 398 ? 99.182  68.318  104.527 1.00 109.46 ? 398 GLU A CA    1 
ATOM   2647 C C     . GLU A 1 398 ? 98.552  69.647  104.923 1.00 109.83 ? 398 GLU A C     1 
ATOM   2648 O O     . GLU A 1 398 ? 98.233  70.475  104.061 1.00 110.50 ? 398 GLU A O     1 
ATOM   2649 C CB    . GLU A 1 398 ? 98.127  67.215  104.450 1.00 104.07 ? 398 GLU A CB    1 
ATOM   2650 C CG    . GLU A 1 398 ? 98.718  65.814  104.389 1.00 109.23 ? 398 GLU A CG    1 
ATOM   2651 C CD    . GLU A 1 398 ? 97.958  64.891  103.456 1.00 106.72 ? 398 GLU A CD    1 
ATOM   2652 O OE1   . GLU A 1 398 ? 96.733  64.733  103.641 1.00 103.30 ? 398 GLU A OE1   1 
ATOM   2653 O OE2   . GLU A 1 398 ? 98.587  64.320  102.540 1.00 106.81 ? 398 GLU A OE2   1 
ATOM   2654 N N     . GLN A 1 399 ? 98.368  69.870  106.226 1.00 107.73 ? 399 GLN A N     1 
ATOM   2655 C CA    . GLN A 1 399 ? 97.851  71.152  106.693 1.00 105.15 ? 399 GLN A CA    1 
ATOM   2656 C C     . GLN A 1 399 ? 98.801  72.291  106.345 1.00 105.09 ? 399 GLN A C     1 
ATOM   2657 O O     . GLN A 1 399 ? 98.363  73.369  105.926 1.00 103.34 ? 399 GLN A O     1 
ATOM   2658 C CB    . GLN A 1 399 ? 97.606  71.099  108.200 1.00 103.05 ? 399 GLN A CB    1 
ATOM   2659 C CG    . GLN A 1 399 ? 96.887  72.316  108.752 1.00 100.86 ? 399 GLN A CG    1 
ATOM   2660 C CD    . GLN A 1 399 ? 96.511  72.157  110.210 1.00 103.56 ? 399 GLN A CD    1 
ATOM   2661 O OE1   . GLN A 1 399 ? 96.861  71.166  110.849 1.00 108.31 ? 399 GLN A OE1   1 
ATOM   2662 N NE2   . GLN A 1 399 ? 95.791  73.137  110.746 1.00 101.14 ? 399 GLN A NE2   1 
ATOM   2663 N N     . GLU A 1 400 ? 100.107 72.072  106.513 1.00 107.59 ? 400 GLU A N     1 
ATOM   2664 C CA    . GLU A 1 400 ? 101.081 73.102  106.164 1.00 112.92 ? 400 GLU A CA    1 
ATOM   2665 C C     . GLU A 1 400 ? 101.073 73.380  104.667 1.00 112.62 ? 400 GLU A C     1 
ATOM   2666 O O     . GLU A 1 400 ? 101.185 74.537  104.242 1.00 110.35 ? 400 GLU A O     1 
ATOM   2667 C CB    . GLU A 1 400 ? 102.476 72.684  106.630 1.00 117.38 ? 400 GLU A CB    1 
ATOM   2668 C CG    . GLU A 1 400 ? 103.584 73.644  106.227 1.00 117.36 ? 400 GLU A CG    1 
ATOM   2669 C CD    . GLU A 1 400 ? 104.403 73.135  105.058 1.00 120.50 ? 400 GLU A CD    1 
ATOM   2670 O OE1   . GLU A 1 400 ? 104.376 71.913  104.798 1.00 121.22 ? 400 GLU A OE1   1 
ATOM   2671 O OE2   . GLU A 1 400 ? 105.074 73.956  104.398 1.00 119.86 ? 400 GLU A OE2   1 
ATOM   2672 N N     . HIS A 1 401 ? 100.948 72.331  103.851 1.00 110.94 ? 401 HIS A N     1 
ATOM   2673 C CA    . HIS A 1 401 ? 100.853 72.524  102.407 1.00 109.33 ? 401 HIS A CA    1 
ATOM   2674 C C     . HIS A 1 401 ? 99.619  73.342  102.046 1.00 101.29 ? 401 HIS A C     1 
ATOM   2675 O O     . HIS A 1 401 ? 99.692  74.277  101.241 1.00 101.86 ? 401 HIS A O     1 
ATOM   2676 C CB    . HIS A 1 401 ? 100.825 71.171  101.696 1.00 108.64 ? 401 HIS A CB    1 
ATOM   2677 C CG    . HIS A 1 401 ? 102.181 70.597  101.433 1.00 114.62 ? 401 HIS A CG    1 
ATOM   2678 N ND1   . HIS A 1 401 ? 102.372 69.291  101.034 1.00 113.86 ? 401 HIS A ND1   1 
ATOM   2679 C CD2   . HIS A 1 401 ? 103.414 71.151  101.509 1.00 116.00 ? 401 HIS A CD2   1 
ATOM   2680 C CE1   . HIS A 1 401 ? 103.664 69.065  100.877 1.00 118.81 ? 401 HIS A CE1   1 
ATOM   2681 N NE2   . HIS A 1 401 ? 104.318 70.177  101.159 1.00 119.90 ? 401 HIS A NE2   1 
ATOM   2682 N N     . LEU A 1 402 ? 98.476  73.011  102.649 1.00 96.43  ? 402 LEU A N     1 
ATOM   2683 C CA    . LEU A 1 402 ? 97.249  73.744  102.359 1.00 93.06  ? 402 LEU A CA    1 
ATOM   2684 C C     . LEU A 1 402 ? 97.351  75.196  102.810 1.00 95.77  ? 402 LEU A C     1 
ATOM   2685 O O     . LEU A 1 402 ? 96.812  76.096  102.156 1.00 94.00  ? 402 LEU A O     1 
ATOM   2686 C CB    . LEU A 1 402 ? 96.057  73.058  103.025 1.00 90.95  ? 402 LEU A CB    1 
ATOM   2687 C CG    . LEU A 1 402 ? 95.497  71.806  102.346 1.00 95.40  ? 402 LEU A CG    1 
ATOM   2688 C CD1   . LEU A 1 402 ? 94.018  71.652  102.658 1.00 89.56  ? 402 LEU A CD1   1 
ATOM   2689 C CD2   . LEU A 1 402 ? 95.722  71.854  100.845 1.00 89.87  ? 402 LEU A CD2   1 
ATOM   2690 N N     . HIS A 1 403 ? 98.029  75.443  103.932 1.00 100.21 ? 403 HIS A N     1 
ATOM   2691 C CA    . HIS A 1 403 ? 98.190  76.812  104.413 1.00 99.30  ? 403 HIS A CA    1 
ATOM   2692 C C     . HIS A 1 403 ? 99.102  77.617  103.494 1.00 97.72  ? 403 HIS A C     1 
ATOM   2693 O O     . HIS A 1 403 ? 98.782  78.753  103.126 1.00 94.46  ? 403 HIS A O     1 
ATOM   2694 C CB    . HIS A 1 403 ? 98.733  76.805  105.841 1.00 99.46  ? 403 HIS A CB    1 
ATOM   2695 C CG    . HIS A 1 403 ? 97.672  76.923  106.890 1.00 98.01  ? 403 HIS A CG    1 
ATOM   2696 N ND1   . HIS A 1 403 ? 96.693  77.891  106.850 1.00 94.23  ? 403 HIS A ND1   1 
ATOM   2697 C CD2   . HIS A 1 403 ? 97.435  76.194  108.005 1.00 99.33  ? 403 HIS A CD2   1 
ATOM   2698 C CE1   . HIS A 1 403 ? 95.899  77.754  107.897 1.00 98.75  ? 403 HIS A CE1   1 
ATOM   2699 N NE2   . HIS A 1 403 ? 96.328  76.731  108.614 1.00 101.58 ? 403 HIS A NE2   1 
ATOM   2700 N N     . LYS A 1 404 ? 100.244 77.043  103.111 1.00 98.83  ? 404 LYS A N     1 
ATOM   2701 C CA    . LYS A 1 404 ? 101.181 77.746  102.244 1.00 98.83  ? 404 LYS A CA    1 
ATOM   2702 C C     . LYS A 1 404 ? 100.702 77.834  100.803 1.00 97.24  ? 404 LYS A C     1 
ATOM   2703 O O     . LYS A 1 404 ? 101.284 78.595  100.022 1.00 98.60  ? 404 LYS A O     1 
ATOM   2704 C CB    . LYS A 1 404 ? 102.552 77.069  102.291 1.00 100.79 ? 404 LYS A CB    1 
ATOM   2705 C CG    . LYS A 1 404 ? 103.198 77.058  103.669 1.00 103.32 ? 404 LYS A CG    1 
ATOM   2706 C CD    . LYS A 1 404 ? 103.082 78.410  104.358 1.00 102.67 ? 404 LYS A CD    1 
ATOM   2707 C CE    . LYS A 1 404 ? 103.973 79.451  103.697 1.00 103.74 ? 404 LYS A CE    1 
ATOM   2708 N NZ    . LYS A 1 404 ? 103.734 80.812  104.251 1.00 108.28 ? 404 LYS A NZ    1 
ATOM   2709 N N     . MET A 1 405 ? 99.669  77.075  100.431 1.00 94.76  ? 405 MET A N     1 
ATOM   2710 C CA    . MET A 1 405 ? 99.157  77.143  99.067  1.00 89.99  ? 405 MET A CA    1 
ATOM   2711 C C     . MET A 1 405 ? 98.593  78.520  98.737  1.00 88.03  ? 405 MET A C     1 
ATOM   2712 O O     . MET A 1 405 ? 98.528  78.896  97.562  1.00 88.07  ? 405 MET A O     1 
ATOM   2713 C CB    . MET A 1 405 ? 98.091  76.068  98.863  1.00 88.69  ? 405 MET A CB    1 
ATOM   2714 C CG    . MET A 1 405 ? 98.031  75.514  97.456  1.00 84.53  ? 405 MET A CG    1 
ATOM   2715 S SD    . MET A 1 405 ? 99.201  74.172  97.182  1.00 85.70  ? 405 MET A SD    1 
ATOM   2716 C CE    . MET A 1 405 ? 98.224  72.766  97.704  1.00 91.72  ? 405 MET A CE    1 
ATOM   2717 N N     . ALA A 1 406 ? 98.183  79.284  99.749  1.00 90.64  ? 406 ALA A N     1 
ATOM   2718 C CA    . ALA A 1 406 ? 97.573  80.591  99.547  1.00 88.78  ? 406 ALA A CA    1 
ATOM   2719 C C     . ALA A 1 406 ? 98.547  81.740  99.787  1.00 93.06  ? 406 ALA A C     1 
ATOM   2720 O O     . ALA A 1 406 ? 98.113  82.869  100.039 1.00 88.60  ? 406 ALA A O     1 
ATOM   2721 C CB    . ALA A 1 406 ? 96.346  80.745  100.446 1.00 85.61  ? 406 ALA A CB    1 
ATOM   2722 N N     . SER A 1 407 ? 99.850  81.478  99.714  1.00 97.17  ? 407 SER A N     1 
ATOM   2723 C CA    . SER A 1 407 ? 100.847 82.510  99.949  1.00 98.45  ? 407 SER A CA    1 
ATOM   2724 C C     . SER A 1 407 ? 101.005 83.389  98.711  1.00 99.81  ? 407 SER A C     1 
ATOM   2725 O O     . SER A 1 407 ? 100.331 83.210  97.693  1.00 99.20  ? 407 SER A O     1 
ATOM   2726 C CB    . SER A 1 407 ? 102.179 81.880  100.346 1.00 101.72 ? 407 SER A CB    1 
ATOM   2727 O OG    . SER A 1 407 ? 102.783 81.230  99.242  1.00 104.59 ? 407 SER A OG    1 
ATOM   2728 N N     . SER A 1 408 ? 101.914 84.358  98.799  1.00 103.91 ? 408 SER A N     1 
ATOM   2729 C CA    . SER A 1 408 ? 102.186 85.268  97.694  1.00 104.25 ? 408 SER A CA    1 
ATOM   2730 C C     . SER A 1 408 ? 103.429 84.895  96.903  1.00 104.35 ? 408 SER A C     1 
ATOM   2731 O O     . SER A 1 408 ? 103.539 85.268  95.731  1.00 100.21 ? 408 SER A O     1 
ATOM   2732 C CB    . SER A 1 408 ? 102.336 86.702  98.213  1.00 105.01 ? 408 SER A CB    1 
ATOM   2733 O OG    . SER A 1 408 ? 103.501 86.835  99.009  1.00 110.71 ? 408 SER A OG    1 
ATOM   2734 N N     . SER A 1 409 ? 104.367 84.179  97.513  1.00 108.39 ? 409 SER A N     1 
ATOM   2735 C CA    . SER A 1 409 ? 105.576 83.736  96.834  1.00 109.13 ? 409 SER A CA    1 
ATOM   2736 C C     . SER A 1 409 ? 106.039 82.437  97.484  1.00 111.78 ? 409 SER A C     1 
ATOM   2737 O O     . SER A 1 409 ? 105.294 81.796  98.232  1.00 111.83 ? 409 SER A O     1 
ATOM   2738 C CB    . SER A 1 409 ? 106.654 84.826  96.877  1.00 109.02 ? 409 SER A CB    1 
ATOM   2739 O OG    . SER A 1 409 ? 107.340 84.815  98.117  1.00 109.64 ? 409 SER A OG    1 
ATOM   2740 N N     . GLY A 1 410 ? 107.277 82.048  97.198  1.00 111.85 ? 410 GLY A N     1 
ATOM   2741 C CA    . GLY A 1 410 ? 107.847 80.855  97.788  1.00 112.44 ? 410 GLY A CA    1 
ATOM   2742 C C     . GLY A 1 410 ? 107.496 79.594  97.027  1.00 110.41 ? 410 GLY A C     1 
ATOM   2743 O O     . GLY A 1 410 ? 106.756 79.595  96.040  1.00 109.59 ? 410 GLY A O     1 
ATOM   2744 N N     . GLU A 1 411 ? 108.051 78.482  97.517  1.00 109.68 ? 411 GLU A N     1 
ATOM   2745 C CA    . GLU A 1 411 ? 107.846 77.196  96.858  1.00 107.62 ? 411 GLU A CA    1 
ATOM   2746 C C     . GLU A 1 411 ? 106.382 76.777  96.878  1.00 106.26 ? 411 GLU A C     1 
ATOM   2747 O O     . GLU A 1 411 ? 105.925 76.087  95.959  1.00 104.61 ? 411 GLU A O     1 
ATOM   2748 C CB    . GLU A 1 411 ? 108.724 76.126  97.513  1.00 106.87 ? 411 GLU A CB    1 
ATOM   2749 C CG    . GLU A 1 411 ? 108.256 75.666  98.887  1.00 109.67 ? 411 GLU A CG    1 
ATOM   2750 C CD    . GLU A 1 411 ? 108.760 76.556  100.007 1.00 116.53 ? 411 GLU A CD    1 
ATOM   2751 O OE1   . GLU A 1 411 ? 109.213 77.684  99.720  1.00 115.83 ? 411 GLU A OE1   1 
ATOM   2752 O OE2   . GLU A 1 411 ? 108.703 76.127  101.178 1.00 114.80 ? 411 GLU A OE2   1 
ATOM   2753 N N     . GLY A 1 412 ? 105.633 77.184  97.906  1.00 105.92 ? 412 GLY A N     1 
ATOM   2754 C CA    . GLY A 1 412 ? 104.215 76.870  97.949  1.00 102.55 ? 412 GLY A CA    1 
ATOM   2755 C C     . GLY A 1 412 ? 103.437 77.506  96.817  1.00 102.26 ? 412 GLY A C     1 
ATOM   2756 O O     . GLY A 1 412 ? 102.456 76.936  96.334  1.00 100.74 ? 412 GLY A O     1 
ATOM   2757 N N     . LYS A 1 413 ? 103.862 78.690  96.375  1.00 104.02 ? 413 LYS A N     1 
ATOM   2758 C CA    . LYS A 1 413 ? 103.193 79.360  95.266  1.00 102.06 ? 413 LYS A CA    1 
ATOM   2759 C C     . LYS A 1 413 ? 103.313 78.548  93.981  1.00 98.79  ? 413 LYS A C     1 
ATOM   2760 O O     . LYS A 1 413 ? 102.315 78.294  93.293  1.00 94.88  ? 413 LYS A O     1 
ATOM   2761 C CB    . LYS A 1 413 ? 103.789 80.755  95.089  1.00 104.92 ? 413 LYS A CB    1 
ATOM   2762 C CG    . LYS A 1 413 ? 103.245 81.544  93.925  1.00 104.74 ? 413 LYS A CG    1 
ATOM   2763 C CD    . LYS A 1 413 ? 101.785 81.875  94.139  1.00 104.87 ? 413 LYS A CD    1 
ATOM   2764 C CE    . LYS A 1 413 ? 101.559 83.364  93.992  1.00 104.66 ? 413 LYS A CE    1 
ATOM   2765 N NZ    . LYS A 1 413 ? 102.632 83.992  93.172  1.00 105.82 ? 413 LYS A NZ    1 
ATOM   2766 N N     . GLU A 1 414 ? 104.532 78.116  93.646  1.00 102.40 ? 414 GLU A N     1 
ATOM   2767 C CA    . GLU A 1 414 ? 104.711 77.275  92.467  1.00 100.99 ? 414 GLU A CA    1 
ATOM   2768 C C     . GLU A 1 414 ? 104.064 75.909  92.650  1.00 96.25  ? 414 GLU A C     1 
ATOM   2769 O O     . GLU A 1 414 ? 103.603 75.311  91.671  1.00 92.53  ? 414 GLU A O     1 
ATOM   2770 C CB    . GLU A 1 414 ? 106.195 77.119  92.135  1.00 102.24 ? 414 GLU A CB    1 
ATOM   2771 C CG    . GLU A 1 414 ? 106.883 78.411  91.722  1.00 103.29 ? 414 GLU A CG    1 
ATOM   2772 C CD    . GLU A 1 414 ? 106.236 79.060  90.518  1.00 109.39 ? 414 GLU A CD    1 
ATOM   2773 O OE1   . GLU A 1 414 ? 105.847 78.329  89.586  1.00 108.33 ? 414 GLU A OE1   1 
ATOM   2774 O OE2   . GLU A 1 414 ? 106.115 80.303  90.504  1.00 113.19 ? 414 GLU A OE2   1 
ATOM   2775 N N     . LEU A 1 415 ? 104.020 75.398  93.883  1.00 96.12  ? 415 LEU A N     1 
ATOM   2776 C CA    . LEU A 1 415 ? 103.313 74.146  94.126  1.00 98.35  ? 415 LEU A CA    1 
ATOM   2777 C C     . LEU A 1 415 ? 101.831 74.289  93.810  1.00 96.66  ? 415 LEU A C     1 
ATOM   2778 O O     . LEU A 1 415 ? 101.242 73.417  93.165  1.00 98.91  ? 415 LEU A O     1 
ATOM   2779 C CB    . LEU A 1 415 ? 103.517 73.695  95.571  1.00 101.09 ? 415 LEU A CB    1 
ATOM   2780 C CG    . LEU A 1 415 ? 104.809 72.925  95.848  1.00 103.72 ? 415 LEU A CG    1 
ATOM   2781 C CD1   . LEU A 1 415 ? 104.911 72.552  97.318  1.00 109.12 ? 415 LEU A CD1   1 
ATOM   2782 C CD2   . LEU A 1 415 ? 104.893 71.686  94.969  1.00 97.39  ? 415 LEU A CD2   1 
ATOM   2783 N N     . TYR A 1 416 ? 101.218 75.394  94.239  1.00 94.44  ? 416 TYR A N     1 
ATOM   2784 C CA    . TYR A 1 416 ? 99.831  75.662  93.872  1.00 90.05  ? 416 TYR A CA    1 
ATOM   2785 C C     . TYR A 1 416 ? 99.687  75.766  92.361  1.00 89.10  ? 416 TYR A C     1 
ATOM   2786 O O     . TYR A 1 416 ? 98.798  75.146  91.765  1.00 87.57  ? 416 TYR A O     1 
ATOM   2787 C CB    . TYR A 1 416 ? 99.348  76.947  94.542  1.00 86.43  ? 416 TYR A CB    1 
ATOM   2788 C CG    . TYR A 1 416 ? 98.017  77.449  94.025  1.00 77.21  ? 416 TYR A CG    1 
ATOM   2789 C CD1   . TYR A 1 416 ? 96.828  76.878  94.450  1.00 74.19  ? 416 TYR A CD1   1 
ATOM   2790 C CD2   . TYR A 1 416 ? 97.951  78.497  93.120  1.00 79.29  ? 416 TYR A CD2   1 
ATOM   2791 C CE1   . TYR A 1 416 ? 95.610  77.334  93.986  1.00 70.63  ? 416 TYR A CE1   1 
ATOM   2792 C CE2   . TYR A 1 416 ? 96.737  78.959  92.650  1.00 80.56  ? 416 TYR A CE2   1 
ATOM   2793 C CZ    . TYR A 1 416 ? 95.571  78.373  93.086  1.00 72.24  ? 416 TYR A CZ    1 
ATOM   2794 O OH    . TYR A 1 416 ? 94.359  78.828  92.622  1.00 70.06  ? 416 TYR A OH    1 
ATOM   2795 N N     . LEU A 1 417 ? 100.591 76.515  91.725  1.00 90.11  ? 417 LEU A N     1 
ATOM   2796 C CA    . LEU A 1 417 ? 100.509 76.731  90.284  1.00 89.85  ? 417 LEU A CA    1 
ATOM   2797 C C     . LEU A 1 417 ? 100.559 75.417  89.516  1.00 91.77  ? 417 LEU A C     1 
ATOM   2798 O O     . LEU A 1 417 ? 99.793  75.215  88.568  1.00 89.62  ? 417 LEU A O     1 
ATOM   2799 C CB    . LEU A 1 417 ? 101.643 77.652  89.832  1.00 93.85  ? 417 LEU A CB    1 
ATOM   2800 C CG    . LEU A 1 417 ? 101.333 79.145  89.752  1.00 94.08  ? 417 LEU A CG    1 
ATOM   2801 C CD1   . LEU A 1 417 ? 102.245 79.827  88.745  1.00 97.62  ? 417 LEU A CD1   1 
ATOM   2802 C CD2   . LEU A 1 417 ? 99.880  79.358  89.387  1.00 87.34  ? 417 LEU A CD2   1 
ATOM   2803 N N     . SER A 1 418 ? 101.448 74.511  89.909  1.00 93.61  ? 418 SER A N     1 
ATOM   2804 C CA    . SER A 1 418 ? 101.634 73.255  89.198  1.00 91.92  ? 418 SER A CA    1 
ATOM   2805 C C     . SER A 1 418 ? 100.767 72.123  89.732  1.00 85.15  ? 418 SER A C     1 
ATOM   2806 O O     . SER A 1 418 ? 100.785 71.029  89.158  1.00 86.37  ? 418 SER A O     1 
ATOM   2807 C CB    . SER A 1 418 ? 103.107 72.839  89.249  1.00 96.29  ? 418 SER A CB    1 
ATOM   2808 O OG    . SER A 1 418 ? 103.949 73.897  88.825  1.00 100.19 ? 418 SER A OG    1 
ATOM   2809 N N     . TRP A 1 419 ? 100.013 72.346  90.803  1.00 83.67  ? 419 TRP A N     1 
ATOM   2810 C CA    . TRP A 1 419 ? 99.243  71.276  91.419  1.00 87.27  ? 419 TRP A CA    1 
ATOM   2811 C C     . TRP A 1 419 ? 97.740  71.472  91.332  1.00 84.67  ? 419 TRP A C     1 
ATOM   2812 O O     . TRP A 1 419 ? 97.002  70.484  91.299  1.00 85.23  ? 419 TRP A O     1 
ATOM   2813 C CB    . TRP A 1 419 ? 99.656  71.135  92.893  1.00 90.90  ? 419 TRP A CB    1 
ATOM   2814 C CG    . TRP A 1 419 ? 98.972  70.026  93.632  1.00 88.78  ? 419 TRP A CG    1 
ATOM   2815 C CD1   . TRP A 1 419 ? 97.823  70.112  94.362  1.00 88.38  ? 419 TRP A CD1   1 
ATOM   2816 C CD2   . TRP A 1 419 ? 99.407  68.666  93.727  1.00 91.09  ? 419 TRP A CD2   1 
ATOM   2817 N NE1   . TRP A 1 419 ? 97.512  68.887  94.900  1.00 90.45  ? 419 TRP A NE1   1 
ATOM   2818 C CE2   . TRP A 1 419 ? 98.469  67.982  94.524  1.00 92.26  ? 419 TRP A CE2   1 
ATOM   2819 C CE3   . TRP A 1 419 ? 100.497 67.959  93.212  1.00 91.03  ? 419 TRP A CE3   1 
ATOM   2820 C CZ2   . TRP A 1 419 ? 98.587  66.627  94.818  1.00 93.36  ? 419 TRP A CZ2   1 
ATOM   2821 C CZ3   . TRP A 1 419 ? 100.612 66.614  93.504  1.00 92.48  ? 419 TRP A CZ3   1 
ATOM   2822 C CH2   . TRP A 1 419 ? 99.664  65.962  94.300  1.00 92.28  ? 419 TRP A CH2   1 
ATOM   2823 N N     . VAL A 1 420 ? 97.254  72.709  91.295  1.00 82.55  ? 420 VAL A N     1 
ATOM   2824 C CA    . VAL A 1 420 ? 95.822  72.965  91.323  1.00 77.84  ? 420 VAL A CA    1 
ATOM   2825 C C     . VAL A 1 420 ? 95.306  73.463  89.980  1.00 82.59  ? 420 VAL A C     1 
ATOM   2826 O O     . VAL A 1 420 ? 94.331  72.927  89.455  1.00 87.40  ? 420 VAL A O     1 
ATOM   2827 C CB    . VAL A 1 420 ? 95.482  73.957  92.455  1.00 74.02  ? 420 VAL A CB    1 
ATOM   2828 C CG1   . VAL A 1 420 ? 93.998  74.262  92.464  1.00 67.08  ? 420 VAL A CG1   1 
ATOM   2829 C CG2   . VAL A 1 420 ? 95.917  73.393  93.793  1.00 80.25  ? 420 VAL A CG2   1 
ATOM   2830 N N     . VAL A 1 421 ? 95.946  74.477  89.400  1.00 81.56  ? 421 VAL A N     1 
ATOM   2831 C CA    . VAL A 1 421 ? 95.440  75.084  88.173  1.00 82.81  ? 421 VAL A CA    1 
ATOM   2832 C C     . VAL A 1 421 ? 96.025  74.393  86.947  1.00 89.18  ? 421 VAL A C     1 
ATOM   2833 O O     . VAL A 1 421 ? 95.290  74.024  86.025  1.00 90.18  ? 421 VAL A O     1 
ATOM   2834 C CB    . VAL A 1 421 ? 95.720  76.598  88.145  1.00 82.49  ? 421 VAL A CB    1 
ATOM   2835 C CG1   . VAL A 1 421 ? 94.672  77.340  88.956  1.00 84.61  ? 421 VAL A CG1   1 
ATOM   2836 C CG2   . VAL A 1 421 ? 97.105  76.896  88.689  1.00 86.39  ? 421 VAL A CG2   1 
ATOM   2837 N N     . GLU A 1 422 ? 97.349  74.220  86.919  1.00 92.67  ? 422 GLU A N     1 
ATOM   2838 C CA    . GLU A 1 422 ? 97.984  73.577  85.772  1.00 97.00  ? 422 GLU A CA    1 
ATOM   2839 C C     . GLU A 1 422 ? 97.552  72.123  85.638  1.00 91.88  ? 422 GLU A C     1 
ATOM   2840 O O     . GLU A 1 422 ? 97.284  71.645  84.530  1.00 88.64  ? 422 GLU A O     1 
ATOM   2841 C CB    . GLU A 1 422 ? 99.508  73.671  85.888  1.00 96.48  ? 422 GLU A CB    1 
ATOM   2842 C CG    . GLU A 1 422 ? 100.299 72.675  85.033  1.00 101.84 ? 422 GLU A CG    1 
ATOM   2843 C CD    . GLU A 1 422 ? 100.107 72.839  83.526  1.00 108.53 ? 422 GLU A CD    1 
ATOM   2844 O OE1   . GLU A 1 422 ? 99.263  73.648  83.085  1.00 106.36 ? 422 GLU A OE1   1 
ATOM   2845 O OE2   . GLU A 1 422 ? 100.817 72.143  82.771  1.00 109.29 ? 422 GLU A OE2   1 
ATOM   2846 N N     . ALA A 1 423 ? 97.477  71.404  86.756  1.00 89.46  ? 423 ALA A N     1 
ATOM   2847 C CA    . ALA A 1 423 ? 97.057  70.011  86.732  1.00 88.47  ? 423 ALA A CA    1 
ATOM   2848 C C     . ALA A 1 423 ? 95.548  69.850  86.638  1.00 87.39  ? 423 ALA A C     1 
ATOM   2849 O O     . ALA A 1 423 ? 95.078  68.730  86.409  1.00 89.57  ? 423 ALA A O     1 
ATOM   2850 C CB    . ALA A 1 423 ? 97.573  69.284  87.976  1.00 88.18  ? 423 ALA A CB    1 
ATOM   2851 N N     . ARG A 1 424 ? 94.787  70.933  86.807  1.00 82.58  ? 424 ARG A N     1 
ATOM   2852 C CA    . ARG A 1 424 ? 93.328  70.913  86.714  1.00 78.13  ? 424 ARG A CA    1 
ATOM   2853 C C     . ARG A 1 424 ? 92.741  69.907  87.709  1.00 78.06  ? 424 ARG A C     1 
ATOM   2854 O O     . ARG A 1 424 ? 92.108  68.914  87.346  1.00 80.23  ? 424 ARG A O     1 
ATOM   2855 C CB    . ARG A 1 424 ? 92.884  70.621  85.275  1.00 81.33  ? 424 ARG A CB    1 
ATOM   2856 C CG    . ARG A 1 424 ? 91.391  70.746  85.018  1.00 79.00  ? 424 ARG A CG    1 
ATOM   2857 C CD    . ARG A 1 424 ? 90.870  72.128  85.353  1.00 71.73  ? 424 ARG A CD    1 
ATOM   2858 N NE    . ARG A 1 424 ? 91.477  73.161  84.524  1.00 73.87  ? 424 ARG A NE    1 
ATOM   2859 C CZ    . ARG A 1 424 ? 90.918  74.335  84.265  1.00 73.36  ? 424 ARG A CZ    1 
ATOM   2860 N NH1   . ARG A 1 424 ? 89.726  74.653  84.742  1.00 68.14  ? 424 ARG A NH1   1 
ATOM   2861 N NH2   . ARG A 1 424 ? 91.570  75.211  83.506  1.00 72.06  ? 424 ARG A NH2   1 
ATOM   2862 N N     . ARG A 1 425 ? 92.986  70.179  88.990  1.00 76.88  ? 425 ARG A N     1 
ATOM   2863 C CA    . ARG A 1 425 ? 92.527  69.330  90.084  1.00 71.09  ? 425 ARG A CA    1 
ATOM   2864 C C     . ARG A 1 425 ? 91.288  69.966  90.702  1.00 65.29  ? 425 ARG A C     1 
ATOM   2865 O O     . ARG A 1 425 ? 91.360  71.066  91.256  1.00 69.28  ? 425 ARG A O     1 
ATOM   2866 C CB    . ARG A 1 425 ? 93.624  69.151  91.131  1.00 72.81  ? 425 ARG A CB    1 
ATOM   2867 C CG    . ARG A 1 425 ? 94.486  67.918  90.935  1.00 75.43  ? 425 ARG A CG    1 
ATOM   2868 C CD    . ARG A 1 425 ? 95.296  67.615  92.183  1.00 80.60  ? 425 ARG A CD    1 
ATOM   2869 N NE    . ARG A 1 425 ? 96.169  66.461  92.007  1.00 85.52  ? 425 ARG A NE    1 
ATOM   2870 C CZ    . ARG A 1 425 ? 97.350  66.500  91.407  1.00 89.10  ? 425 ARG A CZ    1 
ATOM   2871 N NH1   . ARG A 1 425 ? 97.839  67.626  90.914  1.00 87.92  ? 425 ARG A NH1   1 
ATOM   2872 N NH2   . ARG A 1 425 ? 98.061  65.381  91.301  1.00 93.30  ? 425 ARG A NH2   1 
ATOM   2873 N N     . HIS A 1 426 ? 90.157  69.273  90.616  1.00 64.08  ? 426 HIS A N     1 
ATOM   2874 C CA    . HIS A 1 426 ? 88.916  69.783  91.183  1.00 62.98  ? 426 HIS A CA    1 
ATOM   2875 C C     . HIS A 1 426 ? 88.900  69.517  92.687  1.00 70.33  ? 426 HIS A C     1 
ATOM   2876 O O     . HIS A 1 426 ? 89.903  69.120  93.285  1.00 74.35  ? 426 HIS A O     1 
ATOM   2877 C CB    . HIS A 1 426 ? 87.713  69.172  90.470  1.00 65.70  ? 426 HIS A CB    1 
ATOM   2878 C CG    . HIS A 1 426 ? 87.890  67.734  90.096  1.00 67.94  ? 426 HIS A CG    1 
ATOM   2879 N ND1   . HIS A 1 426 ? 87.930  66.720  91.028  1.00 71.16  ? 426 HIS A ND1   1 
ATOM   2880 C CD2   . HIS A 1 426 ? 88.025  67.139  88.887  1.00 67.87  ? 426 HIS A CD2   1 
ATOM   2881 C CE1   . HIS A 1 426 ? 88.090  65.563  90.411  1.00 73.25  ? 426 HIS A CE1   1 
ATOM   2882 N NE2   . HIS A 1 426 ? 88.150  65.790  89.111  1.00 71.22  ? 426 HIS A NE2   1 
ATOM   2883 N N     . ILE A 1 427 ? 87.749  69.746  93.323  1.00 70.52  ? 427 ILE A N     1 
ATOM   2884 C CA    . ILE A 1 427 ? 87.660  69.568  94.768  1.00 72.05  ? 427 ILE A CA    1 
ATOM   2885 C C     . ILE A 1 427 ? 87.754  68.091  95.138  1.00 70.85  ? 427 ILE A C     1 
ATOM   2886 O O     . ILE A 1 427 ? 88.393  67.728  96.133  1.00 71.95  ? 427 ILE A O     1 
ATOM   2887 C CB    . ILE A 1 427 ? 86.375  70.224  95.310  1.00 66.07  ? 427 ILE A CB    1 
ATOM   2888 C CG1   . ILE A 1 427 ? 86.341  70.158  96.837  1.00 62.63  ? 427 ILE A CG1   1 
ATOM   2889 C CG2   . ILE A 1 427 ? 85.134  69.594  94.704  1.00 64.57  ? 427 ILE A CG2   1 
ATOM   2890 C CD1   . ILE A 1 427 ? 87.557  70.762  97.497  1.00 58.22  ? 427 ILE A CD1   1 
ATOM   2891 N N     . LEU A 1 428 ? 87.134  67.213  94.345  1.00 66.32  ? 428 LEU A N     1 
ATOM   2892 C CA    . LEU A 1 428 ? 87.218  65.785  94.630  1.00 69.50  ? 428 LEU A CA    1 
ATOM   2893 C C     . LEU A 1 428 ? 88.643  65.274  94.470  1.00 74.09  ? 428 LEU A C     1 
ATOM   2894 O O     . LEU A 1 428 ? 89.099  64.436  95.255  1.00 82.53  ? 428 LEU A O     1 
ATOM   2895 C CB    . LEU A 1 428 ? 86.267  65.001  93.729  1.00 73.27  ? 428 LEU A CB    1 
ATOM   2896 C CG    . LEU A 1 428 ? 86.328  63.483  93.913  1.00 76.91  ? 428 LEU A CG    1 
ATOM   2897 C CD1   . LEU A 1 428 ? 86.068  63.104  95.364  1.00 71.48  ? 428 LEU A CD1   1 
ATOM   2898 C CD2   . LEU A 1 428 ? 85.352  62.776  92.993  1.00 78.80  ? 428 LEU A CD2   1 
ATOM   2899 N N     . ALA A 1 429 ? 89.358  65.753  93.451  1.00 69.38  ? 429 ALA A N     1 
ATOM   2900 C CA    . ALA A 1 429 ? 90.744  65.337  93.268  1.00 73.68  ? 429 ALA A CA    1 
ATOM   2901 C C     . ALA A 1 429 ? 91.612  65.794  94.432  1.00 79.05  ? 429 ALA A C     1 
ATOM   2902 O O     . ALA A 1 429 ? 92.473  65.044  94.906  1.00 83.38  ? 429 ALA A O     1 
ATOM   2903 C CB    . ALA A 1 429 ? 91.286  65.880  91.947  1.00 76.34  ? 429 ALA A CB    1 
ATOM   2904 N N     . ILE A 1 430 ? 91.400  67.023  94.908  1.00 77.35  ? 430 ILE A N     1 
ATOM   2905 C CA    . ILE A 1 430 ? 92.182  67.521  96.033  1.00 79.73  ? 430 ILE A CA    1 
ATOM   2906 C C     . ILE A 1 430 ? 91.824  66.769  97.310  1.00 81.18  ? 430 ILE A C     1 
ATOM   2907 O O     . ILE A 1 430 ? 92.668  66.604  98.198  1.00 82.48  ? 430 ILE A O     1 
ATOM   2908 C CB    . ILE A 1 430 ? 92.001  69.047  96.180  1.00 70.99  ? 430 ILE A CB    1 
ATOM   2909 C CG1   . ILE A 1 430 ? 93.325  69.706  96.566  1.00 67.86  ? 430 ILE A CG1   1 
ATOM   2910 C CG2   . ILE A 1 430 ? 90.933  69.391  97.204  1.00 73.11  ? 430 ILE A CG2   1 
ATOM   2911 C CD1   . ILE A 1 430 ? 94.367  69.655  95.478  1.00 76.28  ? 430 ILE A CD1   1 
ATOM   2912 N N     . LEU A 1 431 ? 90.578  66.301  97.428  1.00 77.20  ? 431 LEU A N     1 
ATOM   2913 C CA    . LEU A 1 431 ? 90.206  65.485  98.578  1.00 74.64  ? 431 LEU A CA    1 
ATOM   2914 C C     . LEU A 1 431 ? 90.860  64.111  98.513  1.00 79.83  ? 431 LEU A C     1 
ATOM   2915 O O     . LEU A 1 431 ? 91.357  63.604  99.525  1.00 86.85  ? 431 LEU A O     1 
ATOM   2916 C CB    . LEU A 1 431 ? 88.686  65.350  98.655  1.00 70.94  ? 431 LEU A CB    1 
ATOM   2917 C CG    . LEU A 1 431 ? 87.960  66.228  99.673  1.00 66.40  ? 431 LEU A CG    1 
ATOM   2918 C CD1   . LEU A 1 431 ? 88.329  67.686  99.480  1.00 71.00  ? 431 LEU A CD1   1 
ATOM   2919 C CD2   . LEU A 1 431 ? 86.459  66.037  99.566  1.00 59.83  ? 431 LEU A CD2   1 
ATOM   2920 N N     . GLN A 1 432 ? 90.869  63.495  97.330  1.00 79.64  ? 432 GLN A N     1 
ATOM   2921 C CA    . GLN A 1 432 ? 91.407  62.146  97.195  1.00 81.43  ? 432 GLN A CA    1 
ATOM   2922 C C     . GLN A 1 432 ? 92.922  62.130  97.350  1.00 86.72  ? 432 GLN A C     1 
ATOM   2923 O O     . GLN A 1 432 ? 93.472  61.245  98.016  1.00 90.96  ? 432 GLN A O     1 
ATOM   2924 C CB    . GLN A 1 432 ? 91.002  61.553  95.847  1.00 80.21  ? 432 GLN A CB    1 
ATOM   2925 C CG    . GLN A 1 432 ? 89.521  61.244  95.726  1.00 76.79  ? 432 GLN A CG    1 
ATOM   2926 C CD    . GLN A 1 432 ? 89.122  60.866  94.315  1.00 79.27  ? 432 GLN A CD    1 
ATOM   2927 O OE1   . GLN A 1 432 ? 89.495  61.535  93.353  1.00 83.37  ? 432 GLN A OE1   1 
ATOM   2928 N NE2   . GLN A 1 432 ? 88.358  59.788  94.185  1.00 77.71  ? 432 GLN A NE2   1 
ATOM   2929 N N     . ASP A 1 433 ? 93.616  63.094  96.743  1.00 83.26  ? 433 ASP A N     1 
ATOM   2930 C CA    . ASP A 1 433 ? 95.069  63.138  96.850  1.00 84.48  ? 433 ASP A CA    1 
ATOM   2931 C C     . ASP A 1 433 ? 95.543  63.560  98.233  1.00 89.38  ? 433 ASP A C     1 
ATOM   2932 O O     . ASP A 1 433 ? 96.728  63.392  98.538  1.00 92.55  ? 433 ASP A O     1 
ATOM   2933 C CB    . ASP A 1 433 ? 95.646  64.078  95.792  1.00 87.26  ? 433 ASP A CB    1 
ATOM   2934 C CG    . ASP A 1 433 ? 95.710  63.439  94.420  1.00 95.78  ? 433 ASP A CG    1 
ATOM   2935 O OD1   . ASP A 1 433 ? 94.647  63.289  93.782  1.00 96.73  ? 433 ASP A OD1   1 
ATOM   2936 O OD2   . ASP A 1 433 ? 96.823  63.085  93.979  1.00 101.15 ? 433 ASP A OD2   1 
ATOM   2937 N N     . TYR A 1 434 ? 94.652  64.083  99.071  1.00 89.69  ? 434 TYR A N     1 
ATOM   2938 C CA    . TYR A 1 434 ? 94.964  64.463  100.449 1.00 92.90  ? 434 TYR A CA    1 
ATOM   2939 C C     . TYR A 1 434 ? 93.986  63.736  101.362 1.00 94.64  ? 434 TYR A C     1 
ATOM   2940 O O     . TYR A 1 434 ? 93.039  64.333  101.888 1.00 94.43  ? 434 TYR A O     1 
ATOM   2941 C CB    . TYR A 1 434 ? 94.879  65.978  100.639 1.00 92.75  ? 434 TYR A CB    1 
ATOM   2942 C CG    . TYR A 1 434 ? 96.147  66.727  100.289 1.00 96.90  ? 434 TYR A CG    1 
ATOM   2943 C CD1   . TYR A 1 434 ? 97.277  66.055  99.845  1.00 98.38  ? 434 TYR A CD1   1 
ATOM   2944 C CD2   . TYR A 1 434 ? 96.209  68.110  100.395 1.00 95.19  ? 434 TYR A CD2   1 
ATOM   2945 C CE1   . TYR A 1 434 ? 98.434  66.737  99.522  1.00 102.92 ? 434 TYR A CE1   1 
ATOM   2946 C CE2   . TYR A 1 434 ? 97.362  68.800  100.073 1.00 100.65 ? 434 TYR A CE2   1 
ATOM   2947 C CZ    . TYR A 1 434 ? 98.470  68.108  99.637  1.00 105.72 ? 434 TYR A CZ    1 
ATOM   2948 O OH    . TYR A 1 434 ? 99.620  68.792  99.317  1.00 107.26 ? 434 TYR A OH    1 
ATOM   2949 N N     . PRO A 1 435 ? 94.186  62.431  101.565 1.00 94.77  ? 435 PRO A N     1 
ATOM   2950 C CA    . PRO A 1 435 ? 93.194  61.640  102.311 1.00 94.81  ? 435 PRO A CA    1 
ATOM   2951 C C     . PRO A 1 435 ? 93.013  62.078  103.751 1.00 95.21  ? 435 PRO A C     1 
ATOM   2952 O O     . PRO A 1 435 ? 91.939  61.849  104.319 1.00 96.12  ? 435 PRO A O     1 
ATOM   2953 C CB    . PRO A 1 435 ? 93.748  60.213  102.223 1.00 94.81  ? 435 PRO A CB    1 
ATOM   2954 C CG    . PRO A 1 435 ? 95.218  60.396  102.045 1.00 96.54  ? 435 PRO A CG    1 
ATOM   2955 C CD    . PRO A 1 435 ? 95.383  61.643  101.224 1.00 93.71  ? 435 PRO A CD    1 
ATOM   2956 N N     . SER A 1 436 ? 94.020  62.699  104.362 1.00 94.85  ? 436 SER A N     1 
ATOM   2957 C CA    . SER A 1 436 ? 93.888  63.176  105.732 1.00 97.42  ? 436 SER A CA    1 
ATOM   2958 C C     . SER A 1 436 ? 93.196  64.531  105.757 1.00 94.54  ? 436 SER A C     1 
ATOM   2959 O O     . SER A 1 436 ? 93.701  65.484  106.358 1.00 95.53  ? 436 SER A O     1 
ATOM   2960 C CB    . SER A 1 436 ? 95.258  63.265  106.404 1.00 104.15 ? 436 SER A CB    1 
ATOM   2961 O OG    . SER A 1 436 ? 96.059  64.258  105.789 1.00 108.33 ? 436 SER A OG    1 
ATOM   2962 N N     . LEU A 1 437 ? 92.037  64.624  105.109 1.00 90.45  ? 437 LEU A N     1 
ATOM   2963 C CA    . LEU A 1 437 ? 91.298  65.879  105.021 1.00 86.32  ? 437 LEU A CA    1 
ATOM   2964 C C     . LEU A 1 437 ? 89.829  65.530  104.838 1.00 84.08  ? 437 LEU A C     1 
ATOM   2965 O O     . LEU A 1 437 ? 89.427  65.088  103.757 1.00 83.96  ? 437 LEU A O     1 
ATOM   2966 C CB    . LEU A 1 437 ? 91.811  66.739  103.869 1.00 83.48  ? 437 LEU A CB    1 
ATOM   2967 C CG    . LEU A 1 437 ? 90.951  67.920  103.411 1.00 78.89  ? 437 LEU A CG    1 
ATOM   2968 C CD1   . LEU A 1 437 ? 90.677  68.867  104.565 1.00 82.19  ? 437 LEU A CD1   1 
ATOM   2969 C CD2   . LEU A 1 437 ? 91.619  68.655  102.261 1.00 83.39  ? 437 LEU A CD2   1 
ATOM   2970 N N     . ARG A 1 438 ? 89.036  65.716  105.888 1.00 83.44  ? 438 ARG A N     1 
ATOM   2971 C CA    . ARG A 1 438 ? 87.603  65.428  105.865 1.00 81.79  ? 438 ARG A CA    1 
ATOM   2972 C C     . ARG A 1 438 ? 86.848  66.644  106.382 1.00 80.94  ? 438 ARG A C     1 
ATOM   2973 O O     . ARG A 1 438 ? 86.301  66.631  107.492 1.00 85.49  ? 438 ARG A O     1 
ATOM   2974 C CB    . ARG A 1 438 ? 87.278  64.184  106.693 1.00 83.56  ? 438 ARG A CB    1 
ATOM   2975 C CG    . ARG A 1 438 ? 87.979  62.919  106.221 1.00 86.39  ? 438 ARG A CG    1 
ATOM   2976 C CD    . ARG A 1 438 ? 87.275  62.315  105.016 1.00 93.59  ? 438 ARG A CD    1 
ATOM   2977 N NE    . ARG A 1 438 ? 88.012  62.539  103.778 1.00 93.78  ? 438 ARG A NE    1 
ATOM   2978 C CZ    . ARG A 1 438 ? 89.013  61.780  103.355 1.00 91.62  ? 438 ARG A CZ    1 
ATOM   2979 N NH1   . ARG A 1 438 ? 89.428  60.733  104.048 1.00 96.21  ? 438 ARG A NH1   1 
ATOM   2980 N NH2   . ARG A 1 438 ? 89.614  62.079  102.207 1.00 85.16  ? 438 ARG A NH2   1 
ATOM   2981 N N     . PRO A 1 439 ? 86.800  67.722  105.597 1.00 72.16  ? 439 PRO A N     1 
ATOM   2982 C CA    . PRO A 1 439 ? 86.087  68.911  106.044 1.00 69.40  ? 439 PRO A CA    1 
ATOM   2983 C C     . PRO A 1 439 ? 84.591  68.661  106.065 1.00 73.49  ? 439 PRO A C     1 
ATOM   2984 O O     . PRO A 1 439 ? 84.083  67.789  105.339 1.00 77.47  ? 439 PRO A O     1 
ATOM   2985 C CB    . PRO A 1 439 ? 86.466  69.966  104.991 1.00 69.21  ? 439 PRO A CB    1 
ATOM   2986 C CG    . PRO A 1 439 ? 86.709  69.175  103.762 1.00 70.05  ? 439 PRO A CG    1 
ATOM   2987 C CD    . PRO A 1 439 ? 87.254  67.839  104.200 1.00 71.61  ? 439 PRO A CD    1 
ATOM   2988 N N     . PRO A 1 440 ? 83.844  69.391  106.890 1.00 74.81  ? 440 PRO A N     1 
ATOM   2989 C CA    . PRO A 1 440 ? 82.388  69.238  106.882 1.00 71.75  ? 440 PRO A CA    1 
ATOM   2990 C C     . PRO A 1 440 ? 81.802  69.628  105.535 1.00 73.47  ? 440 PRO A C     1 
ATOM   2991 O O     . PRO A 1 440 ? 82.310  70.512  104.841 1.00 69.76  ? 440 PRO A O     1 
ATOM   2992 C CB    . PRO A 1 440 ? 81.922  70.184  107.995 1.00 74.71  ? 440 PRO A CB    1 
ATOM   2993 C CG    . PRO A 1 440 ? 83.037  71.156  108.160 1.00 79.88  ? 440 PRO A CG    1 
ATOM   2994 C CD    . PRO A 1 440 ? 84.290  70.393  107.869 1.00 78.77  ? 440 PRO A CD    1 
ATOM   2995 N N     . ILE A 1 441 ? 80.722  68.939  105.166 1.00 77.92  ? 441 ILE A N     1 
ATOM   2996 C CA    . ILE A 1 441 ? 80.082  69.169  103.874 1.00 74.59  ? 441 ILE A CA    1 
ATOM   2997 C C     . ILE A 1 441 ? 79.561  70.598  103.773 1.00 74.65  ? 441 ILE A C     1 
ATOM   2998 O O     . ILE A 1 441 ? 79.622  71.222  102.706 1.00 76.80  ? 441 ILE A O     1 
ATOM   2999 C CB    . ILE A 1 441 ? 78.967  68.131  103.651 1.00 62.58  ? 441 ILE A CB    1 
ATOM   3000 C CG1   . ILE A 1 441 ? 78.246  68.375  102.322 1.00 62.74  ? 441 ILE A CG1   1 
ATOM   3001 C CG2   . ILE A 1 441 ? 78.014  68.112  104.832 1.00 73.84  ? 441 ILE A CG2   1 
ATOM   3002 C CD1   . ILE A 1 441 ? 79.104  68.121  101.108 1.00 69.39  ? 441 ILE A CD1   1 
ATOM   3003 N N     . ASP A 1 442 ? 79.045  71.141  104.877 1.00 68.86  ? 442 ASP A N     1 
ATOM   3004 C CA    . ASP A 1 442 ? 78.506  72.496  104.840 1.00 67.87  ? 442 ASP A CA    1 
ATOM   3005 C C     . ASP A 1 442 ? 79.603  73.523  104.593 1.00 69.33  ? 442 ASP A C     1 
ATOM   3006 O O     . ASP A 1 442 ? 79.379  74.516  103.896 1.00 69.96  ? 442 ASP A O     1 
ATOM   3007 C CB    . ASP A 1 442 ? 77.756  72.804  106.134 1.00 71.68  ? 442 ASP A CB    1 
ATOM   3008 C CG    . ASP A 1 442 ? 78.681  73.152  107.281 1.00 79.59  ? 442 ASP A CG    1 
ATOM   3009 O OD1   . ASP A 1 442 ? 79.586  72.346  107.581 1.00 84.09  ? 442 ASP A OD1   1 
ATOM   3010 O OD2   . ASP A 1 442 ? 78.500  74.231  107.884 1.00 78.38  ? 442 ASP A OD2   1 
ATOM   3011 N N     . HIS A 1 443 ? 80.798  73.299  105.141 1.00 70.40  ? 443 HIS A N     1 
ATOM   3012 C CA    . HIS A 1 443 ? 81.905  74.214  104.880 1.00 69.69  ? 443 HIS A CA    1 
ATOM   3013 C C     . HIS A 1 443 ? 82.318  74.170  103.413 1.00 68.18  ? 443 HIS A C     1 
ATOM   3014 O O     . HIS A 1 443 ? 82.610  75.210  102.809 1.00 69.35  ? 443 HIS A O     1 
ATOM   3015 C CB    . HIS A 1 443 ? 83.088  73.875  105.784 1.00 70.61  ? 443 HIS A CB    1 
ATOM   3016 C CG    . HIS A 1 443 ? 83.955  75.050  106.113 1.00 69.43  ? 443 HIS A CG    1 
ATOM   3017 N ND1   . HIS A 1 443 ? 83.659  75.929  107.132 1.00 71.25  ? 443 HIS A ND1   1 
ATOM   3018 C CD2   . HIS A 1 443 ? 85.112  75.487  105.562 1.00 71.83  ? 443 HIS A CD2   1 
ATOM   3019 C CE1   . HIS A 1 443 ? 84.595  76.859  107.193 1.00 77.24  ? 443 HIS A CE1   1 
ATOM   3020 N NE2   . HIS A 1 443 ? 85.488  76.614  106.251 1.00 77.74  ? 443 HIS A NE2   1 
ATOM   3021 N N     . LEU A 1 444 ? 82.351  72.972  102.825 1.00 65.00  ? 444 LEU A N     1 
ATOM   3022 C CA    . LEU A 1 444 ? 82.678  72.855  101.409 1.00 61.58  ? 444 LEU A CA    1 
ATOM   3023 C C     . LEU A 1 444 ? 81.635  73.548  100.543 1.00 61.99  ? 444 LEU A C     1 
ATOM   3024 O O     . LEU A 1 444 ? 81.979  74.233  99.574  1.00 63.66  ? 444 LEU A O     1 
ATOM   3025 C CB    . LEU A 1 444 ? 82.809  71.384  101.021 1.00 63.68  ? 444 LEU A CB    1 
ATOM   3026 C CG    . LEU A 1 444 ? 83.657  71.117  99.779  1.00 67.34  ? 444 LEU A CG    1 
ATOM   3027 C CD1   . LEU A 1 444 ? 84.965  71.880  99.869  1.00 66.77  ? 444 LEU A CD1   1 
ATOM   3028 C CD2   . LEU A 1 444 ? 83.911  69.629  99.613  1.00 66.74  ? 444 LEU A CD2   1 
ATOM   3029 N N     . CYS A 1 445 ? 80.352  73.381  100.875 1.00 61.30  ? 445 CYS A N     1 
ATOM   3030 C CA    . CYS A 1 445 ? 79.310  74.101  100.152 1.00 60.11  ? 445 CYS A CA    1 
ATOM   3031 C C     . CYS A 1 445 ? 79.426  75.604  100.365 1.00 61.68  ? 445 CYS A C     1 
ATOM   3032 O O     . CYS A 1 445 ? 79.057  76.390  99.486  1.00 64.61  ? 445 CYS A O     1 
ATOM   3033 C CB    . CYS A 1 445 ? 77.931  73.607  100.587 1.00 60.02  ? 445 CYS A CB    1 
ATOM   3034 S SG    . CYS A 1 445 ? 77.599  71.878  100.184 1.00 68.30  ? 445 CYS A SG    1 
ATOM   3035 N N     . GLU A 1 446 ? 79.925  76.016  101.530 1.00 61.42  ? 446 GLU A N     1 
ATOM   3036 C CA    . GLU A 1 446 ? 80.156  77.428  101.806 1.00 63.06  ? 446 GLU A CA    1 
ATOM   3037 C C     . GLU A 1 446 ? 81.225  78.002  100.887 1.00 60.38  ? 446 GLU A C     1 
ATOM   3038 O O     . GLU A 1 446 ? 81.042  79.070  100.292 1.00 61.52  ? 446 GLU A O     1 
ATOM   3039 C CB    . GLU A 1 446 ? 80.570  77.593  103.269 1.00 72.50  ? 446 GLU A CB    1 
ATOM   3040 C CG    . GLU A 1 446 ? 81.057  78.974  103.649 1.00 75.26  ? 446 GLU A CG    1 
ATOM   3041 C CD    . GLU A 1 446 ? 79.971  79.810  104.272 1.00 81.68  ? 446 GLU A CD    1 
ATOM   3042 O OE1   . GLU A 1 446 ? 78.838  79.302  104.397 1.00 79.42  ? 446 GLU A OE1   1 
ATOM   3043 O OE2   . GLU A 1 446 ? 80.250  80.966  104.649 1.00 87.31  ? 446 GLU A OE2   1 
ATOM   3044 N N     . LEU A 1 447 ? 82.353  77.303  100.762 1.00 59.13  ? 447 LEU A N     1 
ATOM   3045 C CA    . LEU A 1 447 ? 83.505  77.868  100.068 1.00 56.60  ? 447 LEU A CA    1 
ATOM   3046 C C     . LEU A 1 447 ? 83.351  77.829  98.551  1.00 54.24  ? 447 LEU A C     1 
ATOM   3047 O O     . LEU A 1 447 ? 83.779  78.762  97.862  1.00 55.16  ? 447 LEU A O     1 
ATOM   3048 C CB    . LEU A 1 447 ? 84.773  77.129  100.488 1.00 57.34  ? 447 LEU A CB    1 
ATOM   3049 C CG    . LEU A 1 447 ? 85.104  77.204  101.977 1.00 60.91  ? 447 LEU A CG    1 
ATOM   3050 C CD1   . LEU A 1 447 ? 86.389  76.456  102.265 1.00 67.52  ? 447 LEU A CD1   1 
ATOM   3051 C CD2   . LEU A 1 447 ? 85.202  78.650  102.434 1.00 59.30  ? 447 LEU A CD2   1 
ATOM   3052 N N     . LEU A 1 448 ? 82.752  76.770  98.016  1.00 52.24  ? 448 LEU A N     1 
ATOM   3053 C CA    . LEU A 1 448 ? 82.771  76.553  96.576  1.00 46.64  ? 448 LEU A CA    1 
ATOM   3054 C C     . LEU A 1 448 ? 81.954  77.622  95.851  1.00 42.34  ? 448 LEU A C     1 
ATOM   3055 O O     . LEU A 1 448 ? 80.906  78.049  96.347  1.00 44.70  ? 448 LEU A O     1 
ATOM   3056 C CB    . LEU A 1 448 ? 82.233  75.164  96.241  1.00 45.04  ? 448 LEU A CB    1 
ATOM   3057 C CG    . LEU A 1 448 ? 83.199  74.010  96.505  1.00 45.39  ? 448 LEU A CG    1 
ATOM   3058 C CD1   . LEU A 1 448 ? 82.624  72.703  95.999  1.00 48.69  ? 448 LEU A CD1   1 
ATOM   3059 C CD2   . LEU A 1 448 ? 84.546  74.289  95.863  1.00 49.05  ? 448 LEU A CD2   1 
ATOM   3060 N N     . PRO A 1 449 ? 82.404  78.070  94.683  1.00 37.97  ? 449 PRO A N     1 
ATOM   3061 C CA    . PRO A 1 449 ? 81.664  79.088  93.932  1.00 36.92  ? 449 PRO A CA    1 
ATOM   3062 C C     . PRO A 1 449 ? 80.434  78.500  93.253  1.00 40.64  ? 449 PRO A C     1 
ATOM   3063 O O     . PRO A 1 449 ? 80.241  77.287  93.183  1.00 49.94  ? 449 PRO A O     1 
ATOM   3064 C CB    . PRO A 1 449 ? 82.685  79.571  92.899  1.00 39.07  ? 449 PRO A CB    1 
ATOM   3065 C CG    . PRO A 1 449 ? 83.584  78.405  92.702  1.00 37.85  ? 449 PRO A CG    1 
ATOM   3066 C CD    . PRO A 1 449 ? 83.680  77.722  94.035  1.00 39.02  ? 449 PRO A CD    1 
ATOM   3067 N N     . ARG A 1 450 ? 79.597  79.398  92.741  1.00 37.73  ? 450 ARG A N     1 
ATOM   3068 C CA    . ARG A 1 450 ? 78.365  78.996  92.086  1.00 42.28  ? 450 ARG A CA    1 
ATOM   3069 C C     . ARG A 1 450 ? 78.660  78.345  90.736  1.00 44.87  ? 450 ARG A C     1 
ATOM   3070 O O     . ARG A 1 450 ? 79.774  78.408  90.210  1.00 48.99  ? 450 ARG A O     1 
ATOM   3071 C CB    . ARG A 1 450 ? 77.443  80.198  91.900  1.00 45.35  ? 450 ARG A CB    1 
ATOM   3072 C CG    . ARG A 1 450 ? 76.716  80.623  93.159  1.00 45.67  ? 450 ARG A CG    1 
ATOM   3073 C CD    . ARG A 1 450 ? 75.691  79.591  93.580  1.00 45.62  ? 450 ARG A CD    1 
ATOM   3074 N NE    . ARG A 1 450 ? 74.635  79.429  92.589  1.00 50.56  ? 450 ARG A NE    1 
ATOM   3075 C CZ    . ARG A 1 450 ? 73.586  80.232  92.476  1.00 53.95  ? 450 ARG A CZ    1 
ATOM   3076 N NH1   . ARG A 1 450 ? 73.427  81.277  93.270  1.00 52.29  ? 450 ARG A NH1   1 
ATOM   3077 N NH2   . ARG A 1 450 ? 72.674  79.980  91.543  1.00 55.89  ? 450 ARG A NH2   1 
ATOM   3078 N N     . LEU A 1 451 ? 77.636  77.707  90.177  1.00 47.30  ? 451 LEU A N     1 
ATOM   3079 C CA    . LEU A 1 451 ? 77.731  77.073  88.869  1.00 49.80  ? 451 LEU A CA    1 
ATOM   3080 C C     . LEU A 1 451 ? 77.328  78.083  87.803  1.00 54.63  ? 451 LEU A C     1 
ATOM   3081 O O     . LEU A 1 451 ? 76.213  78.615  87.835  1.00 58.15  ? 451 LEU A O     1 
ATOM   3082 C CB    . LEU A 1 451 ? 76.840  75.834  88.803  1.00 47.69  ? 451 LEU A CB    1 
ATOM   3083 C CG    . LEU A 1 451 ? 76.909  75.005  87.521  1.00 43.56  ? 451 LEU A CG    1 
ATOM   3084 C CD1   . LEU A 1 451 ? 78.295  74.413  87.344  1.00 45.52  ? 451 LEU A CD1   1 
ATOM   3085 C CD2   . LEU A 1 451 ? 75.857  73.911  87.535  1.00 46.73  ? 451 LEU A CD2   1 
ATOM   3086 N N     . GLN A 1 452 ? 78.232  78.347  86.864  1.00 53.44  ? 452 GLN A N     1 
ATOM   3087 C CA    . GLN A 1 452 ? 78.021  79.380  85.862  1.00 52.22  ? 452 GLN A CA    1 
ATOM   3088 C C     . GLN A 1 452 ? 77.398  78.796  84.602  1.00 54.25  ? 452 GLN A C     1 
ATOM   3089 O O     . GLN A 1 452 ? 77.750  77.696  84.169  1.00 53.24  ? 452 GLN A O     1 
ATOM   3090 C CB    . GLN A 1 452 ? 79.343  80.070  85.520  1.00 52.50  ? 452 GLN A CB    1 
ATOM   3091 C CG    . GLN A 1 452 ? 79.653  81.295  86.371  1.00 63.85  ? 452 GLN A CG    1 
ATOM   3092 C CD    . GLN A 1 452 ? 78.414  82.073  86.771  1.00 71.10  ? 452 GLN A CD    1 
ATOM   3093 O OE1   . GLN A 1 452 ? 77.635  82.505  85.922  1.00 75.32  ? 452 GLN A OE1   1 
ATOM   3094 N NE2   . GLN A 1 452 ? 78.227  82.255  88.072  1.00 67.47  ? 452 GLN A NE2   1 
ATOM   3095 N N     . ALA A 1 453 ? 76.467  79.545  84.019  1.00 56.34  ? 453 ALA A N     1 
ATOM   3096 C CA    . ALA A 1 453 ? 75.846  79.140  82.768  1.00 53.43  ? 453 ALA A CA    1 
ATOM   3097 C C     . ALA A 1 453 ? 76.859  79.177  81.629  1.00 49.76  ? 453 ALA A C     1 
ATOM   3098 O O     . ALA A 1 453 ? 77.813  79.958  81.640  1.00 51.13  ? 453 ALA A O     1 
ATOM   3099 C CB    . ALA A 1 453 ? 74.658  80.044  82.445  1.00 50.77  ? 453 ALA A CB    1 
ATOM   3100 N N     . ARG A 1 454 ? 76.645  78.313  80.642  1.00 47.81  ? 454 ARG A N     1 
ATOM   3101 C CA    . ARG A 1 454 ? 77.518  78.208  79.483  1.00 49.66  ? 454 ARG A CA    1 
ATOM   3102 C C     . ARG A 1 454 ? 76.749  78.614  78.236  1.00 49.87  ? 454 ARG A C     1 
ATOM   3103 O O     . ARG A 1 454 ? 75.588  78.235  78.060  1.00 51.26  ? 454 ARG A O     1 
ATOM   3104 C CB    . ARG A 1 454 ? 78.079  76.794  79.332  1.00 50.94  ? 454 ARG A CB    1 
ATOM   3105 C CG    . ARG A 1 454 ? 78.403  76.137  80.658  1.00 51.14  ? 454 ARG A CG    1 
ATOM   3106 C CD    . ARG A 1 454 ? 79.568  76.841  81.327  1.00 55.97  ? 454 ARG A CD    1 
ATOM   3107 N NE    . ARG A 1 454 ? 79.740  76.451  82.721  1.00 54.25  ? 454 ARG A NE    1 
ATOM   3108 C CZ    . ARG A 1 454 ? 80.430  75.392  83.118  1.00 53.36  ? 454 ARG A CZ    1 
ATOM   3109 N NH1   . ARG A 1 454 ? 81.053  74.612  82.252  1.00 54.21  ? 454 ARG A NH1   1 
ATOM   3110 N NH2   . ARG A 1 454 ? 80.511  75.119  84.416  1.00 56.59  ? 454 ARG A NH2   1 
ATOM   3111 N N     . TYR A 1 455 ? 77.399  79.388  77.375  1.00 48.02  ? 455 TYR A N     1 
ATOM   3112 C CA    . TYR A 1 455 ? 76.732  80.060  76.273  1.00 46.54  ? 455 TYR A CA    1 
ATOM   3113 C C     . TYR A 1 455 ? 77.221  79.488  74.952  1.00 51.26  ? 455 TYR A C     1 
ATOM   3114 O O     . TYR A 1 455 ? 78.414  79.219  74.788  1.00 54.17  ? 455 TYR A O     1 
ATOM   3115 C CB    . TYR A 1 455 ? 76.991  81.571  76.323  1.00 50.21  ? 455 TYR A CB    1 
ATOM   3116 C CG    . TYR A 1 455 ? 77.173  82.116  77.726  1.00 52.85  ? 455 TYR A CG    1 
ATOM   3117 C CD1   . TYR A 1 455 ? 78.428  82.129  78.329  1.00 55.84  ? 455 TYR A CD1   1 
ATOM   3118 C CD2   . TYR A 1 455 ? 76.091  82.580  78.461  1.00 54.65  ? 455 TYR A CD2   1 
ATOM   3119 C CE1   . TYR A 1 455 ? 78.604  82.611  79.610  1.00 63.95  ? 455 TYR A CE1   1 
ATOM   3120 C CE2   . TYR A 1 455 ? 76.258  83.066  79.747  1.00 62.34  ? 455 TYR A CE2   1 
ATOM   3121 C CZ    . TYR A 1 455 ? 77.513  83.079  80.315  1.00 67.80  ? 455 TYR A CZ    1 
ATOM   3122 O OH    . TYR A 1 455 ? 77.694  83.556  81.593  1.00 70.64  ? 455 TYR A OH    1 
ATOM   3123 N N     . TYR A 1 456 ? 76.298  79.295  74.012  1.00 50.74  ? 456 TYR A N     1 
ATOM   3124 C CA    . TYR A 1 456 ? 76.635  78.798  72.686  1.00 47.62  ? 456 TYR A CA    1 
ATOM   3125 C C     . TYR A 1 456 ? 76.001  79.672  71.614  1.00 54.13  ? 456 TYR A C     1 
ATOM   3126 O O     . TYR A 1 456 ? 74.961  80.301  71.826  1.00 58.76  ? 456 TYR A O     1 
ATOM   3127 C CB    . TYR A 1 456 ? 76.199  77.340  72.488  1.00 40.57  ? 456 TYR A CB    1 
ATOM   3128 C CG    . TYR A 1 456 ? 76.675  76.406  73.569  1.00 45.19  ? 456 TYR A CG    1 
ATOM   3129 C CD1   . TYR A 1 456 ? 75.977  76.268  74.756  1.00 49.63  ? 456 TYR A CD1   1 
ATOM   3130 C CD2   . TYR A 1 456 ? 77.843  75.677  73.409  1.00 49.18  ? 456 TYR A CD2   1 
ATOM   3131 C CE1   . TYR A 1 456 ? 76.421  75.417  75.744  1.00 50.87  ? 456 TYR A CE1   1 
ATOM   3132 C CE2   . TYR A 1 456 ? 78.295  74.830  74.390  1.00 46.62  ? 456 TYR A CE2   1 
ATOM   3133 C CZ    . TYR A 1 456 ? 77.584  74.703  75.552  1.00 47.87  ? 456 TYR A CZ    1 
ATOM   3134 O OH    . TYR A 1 456 ? 78.053  73.850  76.518  1.00 55.53  ? 456 TYR A OH    1 
ATOM   3135 N N     . SER A 1 457 ? 76.649  79.703  70.453  1.00 56.38  ? 457 SER A N     1 
ATOM   3136 C CA    . SER A 1 457 ? 76.138  80.468  69.326  1.00 51.91  ? 457 SER A CA    1 
ATOM   3137 C C     . SER A 1 457 ? 74.990  79.727  68.652  1.00 44.00  ? 457 SER A C     1 
ATOM   3138 O O     . SER A 1 457 ? 75.005  78.500  68.533  1.00 43.67  ? 457 SER A O     1 
ATOM   3139 C CB    . SER A 1 457 ? 77.250  80.734  68.317  1.00 57.19  ? 457 SER A CB    1 
ATOM   3140 O OG    . SER A 1 457 ? 77.719  79.521  67.759  1.00 60.86  ? 457 SER A OG    1 
ATOM   3141 N N     . ILE A 1 458 ? 74.000  80.484  68.200  1.00 42.86  ? 458 ILE A N     1 
ATOM   3142 C CA    . ILE A 1 458 ? 72.803  79.905  67.602  1.00 42.41  ? 458 ILE A CA    1 
ATOM   3143 C C     . ILE A 1 458 ? 73.074  79.601  66.135  1.00 47.96  ? 458 ILE A C     1 
ATOM   3144 O O     . ILE A 1 458 ? 73.558  80.460  65.389  1.00 56.33  ? 458 ILE A O     1 
ATOM   3145 C CB    . ILE A 1 458 ? 71.609  80.857  67.765  1.00 46.47  ? 458 ILE A CB    1 
ATOM   3146 C CG1   . ILE A 1 458 ? 71.141  80.864  69.219  1.00 46.79  ? 458 ILE A CG1   1 
ATOM   3147 C CG2   . ILE A 1 458 ? 70.474  80.452  66.843  1.00 48.36  ? 458 ILE A CG2   1 
ATOM   3148 C CD1   . ILE A 1 458 ? 69.943  81.740  69.469  1.00 54.85  ? 458 ILE A CD1   1 
ATOM   3149 N N     . ALA A 1 459 ? 72.767  78.374  65.717  1.00 45.69  ? 459 ALA A N     1 
ATOM   3150 C CA    . ALA A 1 459 ? 72.975  77.940  64.342  1.00 43.64  ? 459 ALA A CA    1 
ATOM   3151 C C     . ALA A 1 459 ? 71.695  77.946  63.518  1.00 47.57  ? 459 ALA A C     1 
ATOM   3152 O O     . ALA A 1 459 ? 71.700  77.460  62.384  1.00 52.86  ? 459 ALA A O     1 
ATOM   3153 C CB    . ALA A 1 459 ? 73.601  76.546  64.316  1.00 42.10  ? 459 ALA A CB    1 
ATOM   3154 N N     . SER A 1 460 ? 70.603  78.473  64.058  1.00 49.93  ? 460 SER A N     1 
ATOM   3155 C CA    . SER A 1 460 ? 69.342  78.569  63.346  1.00 56.08  ? 460 SER A CA    1 
ATOM   3156 C C     . SER A 1 460 ? 69.120  80.007  62.878  1.00 63.32  ? 460 SER A C     1 
ATOM   3157 O O     . SER A 1 460 ? 70.002  80.863  62.983  1.00 68.53  ? 460 SER A O     1 
ATOM   3158 C CB    . SER A 1 460 ? 68.199  78.077  64.235  1.00 55.29  ? 460 SER A CB    1 
ATOM   3159 O OG    . SER A 1 460 ? 67.959  78.976  65.301  1.00 56.05  ? 460 SER A OG    1 
ATOM   3160 N N     . SER A 1 461 ? 67.930  80.278  62.346  1.00 62.14  ? 461 SER A N     1 
ATOM   3161 C CA    . SER A 1 461 ? 67.556  81.619  61.923  1.00 65.32  ? 461 SER A CA    1 
ATOM   3162 C C     . SER A 1 461 ? 66.119  81.894  62.333  1.00 71.59  ? 461 SER A C     1 
ATOM   3163 O O     . SER A 1 461 ? 65.299  80.978  62.428  1.00 72.20  ? 461 SER A O     1 
ATOM   3164 C CB    . SER A 1 461 ? 67.715  81.796  60.411  1.00 65.02  ? 461 SER A CB    1 
ATOM   3165 O OG    . SER A 1 461 ? 68.844  81.085  59.939  1.00 65.98  ? 461 SER A OG    1 
ATOM   3166 N N     . SER A 1 462 ? 65.822  83.170  62.590  1.00 77.22  ? 462 SER A N     1 
ATOM   3167 C CA    . SER A 1 462 ? 64.471  83.553  62.987  1.00 79.03  ? 462 SER A CA    1 
ATOM   3168 C C     . SER A 1 462 ? 63.508  83.549  61.804  1.00 86.28  ? 462 SER A C     1 
ATOM   3169 O O     . SER A 1 462 ? 62.355  83.128  61.944  1.00 85.89  ? 462 SER A O     1 
ATOM   3170 C CB    . SER A 1 462 ? 64.491  84.928  63.654  1.00 78.61  ? 462 SER A CB    1 
ATOM   3171 O OG    . SER A 1 462 ? 64.565  85.963  62.690  1.00 91.60  ? 462 SER A OG    1 
ATOM   3172 N N     . LYS A 1 463 ? 63.956  84.021  60.638  1.00 83.99  ? 463 LYS A N     1 
ATOM   3173 C CA    . LYS A 1 463 ? 63.119  83.999  59.444  1.00 81.29  ? 463 LYS A CA    1 
ATOM   3174 C C     . LYS A 1 463 ? 62.961  82.593  58.881  1.00 82.69  ? 463 LYS A C     1 
ATOM   3175 O O     . LYS A 1 463 ? 62.126  82.379  57.996  1.00 89.97  ? 463 LYS A O     1 
ATOM   3176 C CB    . LYS A 1 463 ? 63.701  84.940  58.387  1.00 86.85  ? 463 LYS A CB    1 
ATOM   3177 C CG    . LYS A 1 463 ? 62.716  85.396  57.320  1.00 92.35  ? 463 LYS A CG    1 
ATOM   3178 C CD    . LYS A 1 463 ? 61.358  85.726  57.915  1.00 95.65  ? 463 LYS A CD    1 
ATOM   3179 C CE    . LYS A 1 463 ? 60.320  85.938  56.826  1.00 95.06  ? 463 LYS A CE    1 
ATOM   3180 N NZ    . LYS A 1 463 ? 58.945  86.056  57.384  1.00 103.78 ? 463 LYS A NZ    1 
ATOM   3181 N N     . VAL A 1 464 ? 63.733  81.637  59.389  1.00 79.04  ? 464 VAL A N     1 
ATOM   3182 C CA    . VAL A 1 464 ? 63.563  80.214  59.129  1.00 76.21  ? 464 VAL A CA    1 
ATOM   3183 C C     . VAL A 1 464 ? 63.089  79.653  60.461  1.00 79.44  ? 464 VAL A C     1 
ATOM   3184 O O     . VAL A 1 464 ? 62.851  80.425  61.397  1.00 82.24  ? 464 VAL A O     1 
ATOM   3185 C CB    . VAL A 1 464 ? 64.861  79.550  58.633  1.00 71.83  ? 464 VAL A CB    1 
ATOM   3186 C CG1   . VAL A 1 464 ? 64.558  78.258  57.885  1.00 64.94  ? 464 VAL A CG1   1 
ATOM   3187 C CG2   . VAL A 1 464 ? 65.633  80.505  57.741  1.00 72.96  ? 464 VAL A CG2   1 
ATOM   3188 N N     . HIS A 1 465 ? 62.906  78.329  60.550  1.00 76.11  ? 465 HIS A N     1 
ATOM   3189 C CA    . HIS A 1 465 ? 62.231  77.673  61.668  1.00 75.85  ? 465 HIS A CA    1 
ATOM   3190 C C     . HIS A 1 465 ? 62.578  78.318  63.006  1.00 72.82  ? 465 HIS A C     1 
ATOM   3191 O O     . HIS A 1 465 ? 63.713  78.202  63.484  1.00 68.91  ? 465 HIS A O     1 
ATOM   3192 C CB    . HIS A 1 465 ? 62.605  76.190  61.700  1.00 74.59  ? 465 HIS A CB    1 
ATOM   3193 C CG    . HIS A 1 465 ? 64.067  75.931  61.498  1.00 72.92  ? 465 HIS A CG    1 
ATOM   3194 N ND1   . HIS A 1 465 ? 64.631  75.785  60.249  1.00 77.58  ? 465 HIS A ND1   1 
ATOM   3195 C CD2   . HIS A 1 465 ? 65.079  75.787  62.385  1.00 67.70  ? 465 HIS A CD2   1 
ATOM   3196 C CE1   . HIS A 1 465 ? 65.927  75.566  60.376  1.00 71.50  ? 465 HIS A CE1   1 
ATOM   3197 N NE2   . HIS A 1 465 ? 66.225  75.562  61.662  1.00 65.85  ? 465 HIS A NE2   1 
ATOM   3198 N N     . PRO A 1 466 ? 61.624  79.016  63.631  1.00 75.82  ? 466 PRO A N     1 
ATOM   3199 C CA    . PRO A 1 466 ? 61.912  79.689  64.902  1.00 76.88  ? 466 PRO A CA    1 
ATOM   3200 C C     . PRO A 1 466 ? 61.505  78.861  66.108  1.00 74.60  ? 466 PRO A C     1 
ATOM   3201 O O     . PRO A 1 466 ? 61.815  79.212  67.250  1.00 74.21  ? 466 PRO A O     1 
ATOM   3202 C CB    . PRO A 1 466 ? 61.083  80.973  64.800  1.00 76.55  ? 466 PRO A CB    1 
ATOM   3203 C CG    . PRO A 1 466 ? 59.891  80.564  63.980  1.00 81.53  ? 466 PRO A CG    1 
ATOM   3204 C CD    . PRO A 1 466 ? 60.314  79.413  63.085  1.00 78.77  ? 466 PRO A CD    1 
ATOM   3205 N N     . ASN A 1 467 ? 60.804  77.755  65.861  1.00 72.69  ? 467 ASN A N     1 
ATOM   3206 C CA    . ASN A 1 467 ? 60.340  76.901  66.945  1.00 76.52  ? 467 ASN A CA    1 
ATOM   3207 C C     . ASN A 1 467 ? 61.467  76.114  67.596  1.00 71.69  ? 467 ASN A C     1 
ATOM   3208 O O     . ASN A 1 467 ? 61.241  75.498  68.643  1.00 71.32  ? 467 ASN A O     1 
ATOM   3209 C CB    . ASN A 1 467 ? 59.268  75.941  66.429  1.00 85.30  ? 467 ASN A CB    1 
ATOM   3210 C CG    . ASN A 1 467 ? 58.056  76.666  65.880  1.00 89.27  ? 467 ASN A CG    1 
ATOM   3211 O OD1   . ASN A 1 467 ? 57.744  76.567  64.693  1.00 88.11  ? 467 ASN A OD1   1 
ATOM   3212 N ND2   . ASN A 1 467 ? 57.368  77.405  66.742  1.00 91.11  ? 467 ASN A ND2   1 
ATOM   3213 N N     . SER A 1 468 ? 62.661  76.113  67.010  1.00 66.83  ? 468 SER A N     1 
ATOM   3214 C CA    . SER A 1 468 ? 63.776  75.361  67.560  1.00 63.26  ? 468 SER A CA    1 
ATOM   3215 C C     . SER A 1 468 ? 65.069  76.122  67.320  1.00 59.19  ? 468 SER A C     1 
ATOM   3216 O O     . SER A 1 468 ? 65.270  76.695  66.247  1.00 59.39  ? 468 SER A O     1 
ATOM   3217 C CB    . SER A 1 468 ? 63.867  73.966  66.936  1.00 63.69  ? 468 SER A CB    1 
ATOM   3218 O OG    . SER A 1 468 ? 64.142  74.049  65.549  1.00 59.67  ? 468 SER A OG    1 
ATOM   3219 N N     . VAL A 1 469 ? 65.939  76.121  68.322  1.00 56.75  ? 469 VAL A N     1 
ATOM   3220 C CA    . VAL A 1 469 ? 67.267  76.682  68.192  1.00 50.52  ? 469 VAL A CA    1 
ATOM   3221 C C     . VAL A 1 469 ? 68.250  75.544  67.952  1.00 48.78  ? 469 VAL A C     1 
ATOM   3222 O O     . VAL A 1 469 ? 67.939  74.372  68.147  1.00 56.02  ? 469 VAL A O     1 
ATOM   3223 C CB    . VAL A 1 469 ? 67.668  77.519  69.430  1.00 48.88  ? 469 VAL A CB    1 
ATOM   3224 C CG1   . VAL A 1 469 ? 66.657  78.625  69.677  1.00 54.05  ? 469 VAL A CG1   1 
ATOM   3225 C CG2   . VAL A 1 469 ? 67.810  76.630  70.647  1.00 51.64  ? 469 VAL A CG2   1 
ATOM   3226 N N     . HIS A 1 470 ? 69.457  75.890  67.521  1.00 44.79  ? 470 HIS A N     1 
ATOM   3227 C CA    . HIS A 1 470 ? 70.467  74.900  67.190  1.00 43.53  ? 470 HIS A CA    1 
ATOM   3228 C C     . HIS A 1 470 ? 71.760  75.236  67.913  1.00 40.70  ? 470 HIS A C     1 
ATOM   3229 O O     . HIS A 1 470 ? 72.054  76.403  68.184  1.00 46.71  ? 470 HIS A O     1 
ATOM   3230 C CB    . HIS A 1 470 ? 70.707  74.835  65.680  1.00 50.17  ? 470 HIS A CB    1 
ATOM   3231 C CG    . HIS A 1 470 ? 69.574  74.225  64.916  1.00 54.99  ? 470 HIS A CG    1 
ATOM   3232 N ND1   . HIS A 1 470 ? 69.694  73.037  64.228  1.00 56.44  ? 470 HIS A ND1   1 
ATOM   3233 C CD2   . HIS A 1 470 ? 68.298  74.637  64.735  1.00 57.12  ? 470 HIS A CD2   1 
ATOM   3234 C CE1   . HIS A 1 470 ? 68.541  72.746  63.654  1.00 58.92  ? 470 HIS A CE1   1 
ATOM   3235 N NE2   . HIS A 1 470 ? 67.676  73.700  63.947  1.00 60.59  ? 470 HIS A NE2   1 
ATOM   3236 N N     . ILE A 1 471 ? 72.528  74.199  68.230  1.00 38.79  ? 471 ILE A N     1 
ATOM   3237 C CA    . ILE A 1 471 ? 73.770  74.346  68.977  1.00 36.48  ? 471 ILE A CA    1 
ATOM   3238 C C     . ILE A 1 471 ? 74.829  73.472  68.327  1.00 38.68  ? 471 ILE A C     1 
ATOM   3239 O O     . ILE A 1 471 ? 74.600  72.281  68.093  1.00 46.96  ? 471 ILE A O     1 
ATOM   3240 C CB    . ILE A 1 471 ? 73.593  73.961  70.460  1.00 37.34  ? 471 ILE A CB    1 
ATOM   3241 C CG1   . ILE A 1 471 ? 72.922  75.096  71.231  1.00 42.37  ? 471 ILE A CG1   1 
ATOM   3242 C CG2   . ILE A 1 471 ? 74.929  73.612  71.092  1.00 36.50  ? 471 ILE A CG2   1 
ATOM   3243 C CD1   . ILE A 1 471 ? 72.327  74.660  72.547  1.00 37.85  ? 471 ILE A CD1   1 
ATOM   3244 N N     . CYS A 1 472 ? 75.983  74.058  68.032  1.00 37.62  ? 472 CYS A N     1 
ATOM   3245 C CA    . CYS A 1 472 ? 77.161  73.312  67.613  1.00 42.50  ? 472 CYS A CA    1 
ATOM   3246 C C     . CYS A 1 472 ? 78.176  73.378  68.744  1.00 48.74  ? 472 CYS A C     1 
ATOM   3247 O O     . CYS A 1 472 ? 78.610  74.469  69.129  1.00 55.56  ? 472 CYS A O     1 
ATOM   3248 C CB    . CYS A 1 472 ? 77.746  73.878  66.320  1.00 53.00  ? 472 CYS A CB    1 
ATOM   3249 S SG    . CYS A 1 472 ? 78.958  72.803  65.525  1.00 68.36  ? 472 CYS A SG    1 
ATOM   3250 N N     . ALA A 1 473 ? 78.549  72.218  69.275  1.00 48.82  ? 473 ALA A N     1 
ATOM   3251 C CA    . ALA A 1 473 ? 79.417  72.156  70.438  1.00 45.02  ? 473 ALA A CA    1 
ATOM   3252 C C     . ALA A 1 473 ? 80.454  71.062  70.248  1.00 48.64  ? 473 ALA A C     1 
ATOM   3253 O O     . ALA A 1 473 ? 80.270  70.131  69.463  1.00 62.81  ? 473 ALA A O     1 
ATOM   3254 C CB    . ALA A 1 473 ? 78.618  71.908  71.722  1.00 42.09  ? 473 ALA A CB    1 
ATOM   3255 N N     . VAL A 1 474 ? 81.555  71.191  70.980  1.00 46.24  ? 474 VAL A N     1 
ATOM   3256 C CA    . VAL A 1 474 ? 82.612  70.189  71.015  1.00 52.28  ? 474 VAL A CA    1 
ATOM   3257 C C     . VAL A 1 474 ? 82.594  69.544  72.392  1.00 61.76  ? 474 VAL A C     1 
ATOM   3258 O O     . VAL A 1 474 ? 82.640  70.244  73.411  1.00 71.41  ? 474 VAL A O     1 
ATOM   3259 C CB    . VAL A 1 474 ? 83.989  70.808  70.715  1.00 51.81  ? 474 VAL A CB    1 
ATOM   3260 C CG1   . VAL A 1 474 ? 85.100  69.977  71.340  1.00 59.55  ? 474 VAL A CG1   1 
ATOM   3261 C CG2   . VAL A 1 474 ? 84.199  70.936  69.226  1.00 54.33  ? 474 VAL A CG2   1 
ATOM   3262 N N     . ALA A 1 475 ? 82.511  68.218  72.426  1.00 56.39  ? 475 ALA A N     1 
ATOM   3263 C CA    . ALA A 1 475 ? 82.544  67.507  73.696  1.00 62.08  ? 475 ALA A CA    1 
ATOM   3264 C C     . ALA A 1 475 ? 83.922  67.659  74.325  1.00 67.66  ? 475 ALA A C     1 
ATOM   3265 O O     . ALA A 1 475 ? 84.933  67.282  73.723  1.00 72.77  ? 475 ALA A O     1 
ATOM   3266 C CB    . ALA A 1 475 ? 82.204  66.034  73.489  1.00 67.73  ? 475 ALA A CB    1 
ATOM   3267 N N     . VAL A 1 476 ? 83.965  68.213  75.532  1.00 63.10  ? 476 VAL A N     1 
ATOM   3268 C CA    . VAL A 1 476 ? 85.222  68.447  76.231  1.00 63.15  ? 476 VAL A CA    1 
ATOM   3269 C C     . VAL A 1 476 ? 85.655  67.160  76.915  1.00 73.87  ? 476 VAL A C     1 
ATOM   3270 O O     . VAL A 1 476 ? 84.895  66.569  77.690  1.00 77.54  ? 476 VAL A O     1 
ATOM   3271 C CB    . VAL A 1 476 ? 85.087  69.594  77.245  1.00 64.45  ? 476 VAL A CB    1 
ATOM   3272 C CG1   . VAL A 1 476 ? 86.459  70.098  77.648  1.00 73.49  ? 476 VAL A CG1   1 
ATOM   3273 C CG2   . VAL A 1 476 ? 84.267  70.721  76.654  1.00 59.80  ? 476 VAL A CG2   1 
ATOM   3274 N N     . GLU A 1 477 ? 86.879  66.729  76.626  1.00 78.15  ? 477 GLU A N     1 
ATOM   3275 C CA    . GLU A 1 477 ? 87.448  65.523  77.211  1.00 83.35  ? 477 GLU A CA    1 
ATOM   3276 C C     . GLU A 1 477 ? 88.956  65.606  77.055  1.00 86.55  ? 477 GLU A C     1 
ATOM   3277 O O     . GLU A 1 477 ? 89.451  65.790  75.940  1.00 90.38  ? 477 GLU A O     1 
ATOM   3278 C CB    . GLU A 1 477 ? 86.905  64.262  76.527  1.00 81.24  ? 477 GLU A CB    1 
ATOM   3279 C CG    . GLU A 1 477 ? 85.804  63.550  77.292  1.00 86.86  ? 477 GLU A CG    1 
ATOM   3280 C CD    . GLU A 1 477 ? 85.100  62.500  76.454  1.00 92.83  ? 477 GLU A CD    1 
ATOM   3281 O OE1   . GLU A 1 477 ? 85.148  62.602  75.210  1.00 87.67  ? 477 GLU A OE1   1 
ATOM   3282 O OE2   . GLU A 1 477 ? 84.500  61.574  77.039  1.00 96.86  ? 477 GLU A OE2   1 
ATOM   3283 N N     . TYR A 1 478 ? 89.681  65.475  78.162  1.00 79.57  ? 478 TYR A N     1 
ATOM   3284 C CA    . TYR A 1 478 ? 91.127  65.617  78.102  1.00 80.79  ? 478 TYR A CA    1 
ATOM   3285 C C     . TYR A 1 478 ? 91.762  64.837  79.241  1.00 87.78  ? 478 TYR A C     1 
ATOM   3286 O O     . TYR A 1 478 ? 91.123  64.544  80.254  1.00 89.59  ? 478 TYR A O     1 
ATOM   3287 C CB    . TYR A 1 478 ? 91.549  67.090  78.152  1.00 83.11  ? 478 TYR A CB    1 
ATOM   3288 C CG    . TYR A 1 478 ? 90.941  67.887  79.287  1.00 85.52  ? 478 TYR A CG    1 
ATOM   3289 C CD1   . TYR A 1 478 ? 89.650  68.390  79.197  1.00 83.32  ? 478 TYR A CD1   1 
ATOM   3290 C CD2   . TYR A 1 478 ? 91.666  68.154  80.439  1.00 87.49  ? 478 TYR A CD2   1 
ATOM   3291 C CE1   . TYR A 1 478 ? 89.095  69.123  80.226  1.00 83.17  ? 478 TYR A CE1   1 
ATOM   3292 C CE2   . TYR A 1 478 ? 91.120  68.888  81.473  1.00 83.02  ? 478 TYR A CE2   1 
ATOM   3293 C CZ    . TYR A 1 478 ? 89.834  69.369  81.362  1.00 81.22  ? 478 TYR A CZ    1 
ATOM   3294 O OH    . TYR A 1 478 ? 89.283  70.101  82.388  1.00 78.52  ? 478 TYR A OH    1 
ATOM   3295 N N     . GLU A 1 479 ? 93.036  64.504  79.052  1.00 92.76  ? 479 GLU A N     1 
ATOM   3296 C CA    . GLU A 1 479 ? 93.830  63.816  80.066  1.00 96.96  ? 479 GLU A CA    1 
ATOM   3297 C C     . GLU A 1 479 ? 94.552  64.876  80.887  1.00 98.89  ? 479 GLU A C     1 
ATOM   3298 O O     . GLU A 1 479 ? 95.619  65.358  80.499  1.00 104.16 ? 479 GLU A O     1 
ATOM   3299 C CB    . GLU A 1 479 ? 94.811  62.845  79.419  1.00 99.84  ? 479 GLU A CB    1 
ATOM   3300 C CG    . GLU A 1 479 ? 94.201  61.518  78.988  1.00 105.68 ? 479 GLU A CG    1 
ATOM   3301 C CD    . GLU A 1 479 ? 93.737  60.675  80.160  1.00 108.37 ? 479 GLU A CD    1 
ATOM   3302 O OE1   . GLU A 1 479 ? 92.631  60.929  80.680  1.00 103.36 ? 479 GLU A OE1   1 
ATOM   3303 O OE2   . GLU A 1 479 ? 94.479  59.754  80.561  1.00 112.92 ? 479 GLU A OE2   1 
ATOM   3304 N N     . ALA A 1 480 ? 93.967  65.244  82.022  1.00 96.76  ? 480 ALA A N     1 
ATOM   3305 C CA    . ALA A 1 480 ? 94.581  66.236  82.890  1.00 96.04  ? 480 ALA A CA    1 
ATOM   3306 C C     . ALA A 1 480 ? 95.891  65.707  83.460  1.00 98.55  ? 480 ALA A C     1 
ATOM   3307 O O     . ALA A 1 480 ? 96.091  64.498  83.601  1.00 104.99 ? 480 ALA A O     1 
ATOM   3308 C CB    . ALA A 1 480 ? 93.630  66.619  84.023  1.00 88.68  ? 480 ALA A CB    1 
ATOM   3309 N N     . LYS A 1 481 ? 96.794  66.633  83.789  1.00 91.39  ? 481 LYS A N     1 
ATOM   3310 C CA    . LYS A 1 481 ? 98.092  66.254  84.332  1.00 94.42  ? 481 LYS A CA    1 
ATOM   3311 C C     . LYS A 1 481 ? 97.985  65.588  85.697  1.00 98.19  ? 481 LYS A C     1 
ATOM   3312 O O     . LYS A 1 481 ? 98.968  64.997  86.156  1.00 99.86  ? 481 LYS A O     1 
ATOM   3313 C CB    . LYS A 1 481 ? 99.003  67.478  84.418  1.00 93.44  ? 481 LYS A CB    1 
ATOM   3314 C CG    . LYS A 1 481 ? 99.230  68.171  83.084  1.00 97.43  ? 481 LYS A CG    1 
ATOM   3315 C CD    . LYS A 1 481 ? 100.700 68.495  82.860  1.00 99.58  ? 481 LYS A CD    1 
ATOM   3316 C CE    . LYS A 1 481 ? 101.361 69.008  84.129  1.00 102.48 ? 481 LYS A CE    1 
ATOM   3317 N NZ    . LYS A 1 481 ? 102.780 69.395  83.898  1.00 101.65 ? 481 LYS A NZ    1 
ATOM   3318 N N     . SER A 1 482 ? 96.825  65.669  86.350  1.00 100.17 ? 482 SER A N     1 
ATOM   3319 C CA    . SER A 1 482 ? 96.602  64.956  87.600  1.00 98.57  ? 482 SER A CA    1 
ATOM   3320 C C     . SER A 1 482 ? 96.432  63.457  87.400  1.00 98.31  ? 482 SER A C     1 
ATOM   3321 O O     . SER A 1 482 ? 96.363  62.722  88.390  1.00 99.39  ? 482 SER A O     1 
ATOM   3322 C CB    . SER A 1 482 ? 95.372  65.520  88.312  1.00 94.82  ? 482 SER A CB    1 
ATOM   3323 O OG    . SER A 1 482 ? 94.373  65.899  87.382  1.00 93.40  ? 482 SER A OG    1 
ATOM   3324 N N     . GLY A 1 483 ? 96.358  62.989  86.155  1.00 96.31  ? 483 GLY A N     1 
ATOM   3325 C CA    . GLY A 1 483 ? 96.135  61.585  85.885  1.00 98.91  ? 483 GLY A CA    1 
ATOM   3326 C C     . GLY A 1 483 ? 94.690  61.153  85.938  1.00 100.50 ? 483 GLY A C     1 
ATOM   3327 O O     . GLY A 1 483 ? 94.416  59.949  85.888  1.00 96.90  ? 483 GLY A O     1 
ATOM   3328 N N     . ARG A 1 484 ? 93.759  62.095  86.037  1.00 100.28 ? 484 ARG A N     1 
ATOM   3329 C CA    . ARG A 1 484 ? 92.340  61.806  86.156  1.00 96.03  ? 484 ARG A CA    1 
ATOM   3330 C C     . ARG A 1 484 ? 91.609  62.294  84.913  1.00 93.02  ? 484 ARG A C     1 
ATOM   3331 O O     . ARG A 1 484 ? 91.890  63.384  84.407  1.00 98.39  ? 484 ARG A O     1 
ATOM   3332 C CB    . ARG A 1 484 ? 91.761  62.472  87.406  1.00 95.03  ? 484 ARG A CB    1 
ATOM   3333 C CG    . ARG A 1 484 ? 90.253  62.388  87.538  1.00 90.94  ? 484 ARG A CG    1 
ATOM   3334 C CD    . ARG A 1 484 ? 89.798  62.851  88.914  1.00 95.27  ? 484 ARG A CD    1 
ATOM   3335 N NE    . ARG A 1 484 ? 90.107  61.878  89.957  1.00 100.22 ? 484 ARG A NE    1 
ATOM   3336 C CZ    . ARG A 1 484 ? 91.180  61.922  90.736  1.00 97.99  ? 484 ARG A CZ    1 
ATOM   3337 N NH1   . ARG A 1 484 ? 92.076  62.888  90.625  1.00 92.56  ? 484 ARG A NH1   1 
ATOM   3338 N NH2   . ARG A 1 484 ? 91.357  60.973  91.650  1.00 96.79  ? 484 ARG A NH2   1 
ATOM   3339 N N     . VAL A 1 485 ? 90.680  61.479  84.417  1.00 86.65  ? 485 VAL A N     1 
ATOM   3340 C CA    . VAL A 1 485 ? 89.874  61.881  83.271  1.00 82.39  ? 485 VAL A CA    1 
ATOM   3341 C C     . VAL A 1 485 ? 88.997  63.052  83.691  1.00 80.53  ? 485 VAL A C     1 
ATOM   3342 O O     . VAL A 1 485 ? 88.166  62.933  84.599  1.00 84.28  ? 485 VAL A O     1 
ATOM   3343 C CB    . VAL A 1 485 ? 89.032  60.709  82.748  1.00 83.68  ? 485 VAL A CB    1 
ATOM   3344 C CG1   . VAL A 1 485 ? 87.814  61.218  81.990  1.00 78.05  ? 485 VAL A CG1   1 
ATOM   3345 C CG2   . VAL A 1 485 ? 89.873  59.804  81.866  1.00 88.76  ? 485 VAL A CG2   1 
ATOM   3346 N N     . ASN A 1 486 ? 89.189  64.195  83.042  1.00 78.74  ? 486 ASN A N     1 
ATOM   3347 C CA    . ASN A 1 486 ? 88.464  65.416  83.363  1.00 77.32  ? 486 ASN A CA    1 
ATOM   3348 C C     . ASN A 1 486 ? 87.453  65.679  82.258  1.00 77.16  ? 486 ASN A C     1 
ATOM   3349 O O     . ASN A 1 486 ? 87.803  65.670  81.074  1.00 80.26  ? 486 ASN A O     1 
ATOM   3350 C CB    . ASN A 1 486 ? 89.422  66.594  83.524  1.00 78.58  ? 486 ASN A CB    1 
ATOM   3351 C CG    . ASN A 1 486 ? 89.233  67.317  84.840  1.00 77.66  ? 486 ASN A CG    1 
ATOM   3352 O OD1   . ASN A 1 486 ? 88.108  67.530  85.288  1.00 74.37  ? 486 ASN A OD1   1 
ATOM   3353 N ND2   . ASN A 1 486 ? 90.338  67.686  85.475  1.00 78.40  ? 486 ASN A ND2   1 
ATOM   3354 N N     . LYS A 1 487 ? 86.206  65.913  82.649  1.00 74.04  ? 487 LYS A N     1 
ATOM   3355 C CA    . LYS A 1 487 ? 85.087  65.979  81.723  1.00 72.42  ? 487 LYS A CA    1 
ATOM   3356 C C     . LYS A 1 487 ? 84.386  67.323  81.856  1.00 72.68  ? 487 LYS A C     1 
ATOM   3357 O O     . LYS A 1 487 ? 84.148  67.796  82.971  1.00 72.71  ? 487 LYS A O     1 
ATOM   3358 C CB    . LYS A 1 487 ? 84.112  64.831  81.995  1.00 72.81  ? 487 LYS A CB    1 
ATOM   3359 C CG    . LYS A 1 487 ? 82.795  64.923  81.261  1.00 72.40  ? 487 LYS A CG    1 
ATOM   3360 C CD    . LYS A 1 487 ? 81.866  63.779  81.643  1.00 80.55  ? 487 LYS A CD    1 
ATOM   3361 C CE    . LYS A 1 487 ? 82.505  62.420  81.396  1.00 81.77  ? 487 LYS A CE    1 
ATOM   3362 N NZ    . LYS A 1 487 ? 83.268  62.368  80.117  1.00 79.40  ? 487 LYS A NZ    1 
ATOM   3363 N N     . GLY A 1 488 ? 84.064  67.936  80.719  1.00 68.54  ? 488 GLY A N     1 
ATOM   3364 C CA    . GLY A 1 488 ? 83.335  69.184  80.740  1.00 61.88  ? 488 GLY A CA    1 
ATOM   3365 C C     . GLY A 1 488 ? 81.928  69.012  81.273  1.00 61.24  ? 488 GLY A C     1 
ATOM   3366 O O     . GLY A 1 488 ? 81.330  67.939  81.207  1.00 67.15  ? 488 GLY A O     1 
ATOM   3367 N N     . VAL A 1 489 ? 81.387  70.098  81.817  1.00 55.69  ? 489 VAL A N     1 
ATOM   3368 C CA    . VAL A 1 489 ? 80.098  70.030  82.494  1.00 54.40  ? 489 VAL A CA    1 
ATOM   3369 C C     . VAL A 1 489 ? 78.961  70.086  81.483  1.00 59.02  ? 489 VAL A C     1 
ATOM   3370 O O     . VAL A 1 489 ? 78.217  69.113  81.317  1.00 62.96  ? 489 VAL A O     1 
ATOM   3371 C CB    . VAL A 1 489 ? 79.961  71.157  83.531  1.00 55.22  ? 489 VAL A CB    1 
ATOM   3372 C CG1   . VAL A 1 489 ? 78.563  71.167  84.121  1.00 51.33  ? 489 VAL A CG1   1 
ATOM   3373 C CG2   . VAL A 1 489 ? 81.003  70.999  84.623  1.00 62.82  ? 489 VAL A CG2   1 
ATOM   3374 N N     . ALA A 1 490 ? 78.834  71.212  80.778  1.00 56.46  ? 490 ALA A N     1 
ATOM   3375 C CA    . ALA A 1 490 ? 77.668  71.419  79.925  1.00 55.07  ? 490 ALA A CA    1 
ATOM   3376 C C     . ALA A 1 490 ? 77.740  70.602  78.643  1.00 55.56  ? 490 ALA A C     1 
ATOM   3377 O O     . ALA A 1 490 ? 76.722  70.068  78.191  1.00 54.49  ? 490 ALA A O     1 
ATOM   3378 C CB    . ALA A 1 490 ? 77.513  72.901  79.597  1.00 52.95  ? 490 ALA A CB    1 
ATOM   3379 N N     . THR A 1 491 ? 78.925  70.499  78.038  1.00 57.59  ? 491 THR A N     1 
ATOM   3380 C CA    . THR A 1 491 ? 79.050  69.750  76.792  1.00 59.63  ? 491 THR A CA    1 
ATOM   3381 C C     . THR A 1 491 ? 78.693  68.285  76.998  1.00 62.86  ? 491 THR A C     1 
ATOM   3382 O O     . THR A 1 491 ? 77.891  67.719  76.249  1.00 66.49  ? 491 THR A O     1 
ATOM   3383 C CB    . THR A 1 491 ? 80.464  69.882  76.232  1.00 59.92  ? 491 THR A CB    1 
ATOM   3384 O OG1   . THR A 1 491 ? 81.405  69.370  77.182  1.00 62.68  ? 491 THR A OG1   1 
ATOM   3385 C CG2   . THR A 1 491 ? 80.781  71.334  75.937  1.00 60.05  ? 491 THR A CG2   1 
ATOM   3386 N N     . SER A 1 492 ? 79.260  67.657  78.029  1.00 59.38  ? 492 SER A N     1 
ATOM   3387 C CA    . SER A 1 492 ? 78.939  66.260  78.296  1.00 58.24  ? 492 SER A CA    1 
ATOM   3388 C C     . SER A 1 492 ? 77.531  66.103  78.853  1.00 56.62  ? 492 SER A C     1 
ATOM   3389 O O     . SER A 1 492 ? 76.887  65.073  78.623  1.00 61.77  ? 492 SER A O     1 
ATOM   3390 C CB    . SER A 1 492 ? 79.964  65.661  79.250  1.00 59.23  ? 492 SER A CB    1 
ATOM   3391 O OG    . SER A 1 492 ? 81.221  65.536  78.610  1.00 62.34  ? 492 SER A OG    1 
ATOM   3392 N N     . TRP A 1 493 ? 77.035  67.107  79.579  1.00 52.63  ? 493 TRP A N     1 
ATOM   3393 C CA    . TRP A 1 493 ? 75.658  67.062  80.052  1.00 53.36  ? 493 TRP A CA    1 
ATOM   3394 C C     . TRP A 1 493 ? 74.680  67.011  78.886  1.00 57.56  ? 493 TRP A C     1 
ATOM   3395 O O     . TRP A 1 493 ? 73.708  66.249  78.914  1.00 61.71  ? 493 TRP A O     1 
ATOM   3396 C CB    . TRP A 1 493 ? 75.380  68.272  80.942  1.00 50.87  ? 493 TRP A CB    1 
ATOM   3397 C CG    . TRP A 1 493 ? 73.989  68.335  81.470  1.00 47.59  ? 493 TRP A CG    1 
ATOM   3398 C CD1   . TRP A 1 493 ? 73.381  67.429  82.285  1.00 47.85  ? 493 TRP A CD1   1 
ATOM   3399 C CD2   . TRP A 1 493 ? 73.029  69.368  81.232  1.00 48.75  ? 493 TRP A CD2   1 
ATOM   3400 N NE1   . TRP A 1 493 ? 72.099  67.830  82.566  1.00 50.12  ? 493 TRP A NE1   1 
ATOM   3401 C CE2   . TRP A 1 493 ? 71.859  69.019  81.931  1.00 51.38  ? 493 TRP A CE2   1 
ATOM   3402 C CE3   . TRP A 1 493 ? 73.045  70.552  80.492  1.00 47.15  ? 493 TRP A CE3   1 
ATOM   3403 C CZ2   . TRP A 1 493 ? 70.716  69.812  81.913  1.00 55.40  ? 493 TRP A CZ2   1 
ATOM   3404 C CZ3   . TRP A 1 493 ? 71.912  71.337  80.476  1.00 46.56  ? 493 TRP A CZ3   1 
ATOM   3405 C CH2   . TRP A 1 493 ? 70.763  70.965  81.181  1.00 53.75  ? 493 TRP A CH2   1 
ATOM   3406 N N     . LEU A 1 494 ? 74.924  67.815  77.848  1.00 57.40  ? 494 LEU A N     1 
ATOM   3407 C CA    . LEU A 1 494 ? 74.080  67.769  76.658  1.00 56.74  ? 494 LEU A CA    1 
ATOM   3408 C C     . LEU A 1 494 ? 74.361  66.530  75.817  1.00 55.10  ? 494 LEU A C     1 
ATOM   3409 O O     . LEU A 1 494 ? 73.460  66.025  75.141  1.00 54.69  ? 494 LEU A O     1 
ATOM   3410 C CB    . LEU A 1 494 ? 74.278  69.033  75.823  1.00 54.77  ? 494 LEU A CB    1 
ATOM   3411 C CG    . LEU A 1 494 ? 73.761  70.345  76.415  1.00 45.81  ? 494 LEU A CG    1 
ATOM   3412 C CD1   . LEU A 1 494 ? 74.271  71.526  75.611  1.00 42.29  ? 494 LEU A CD1   1 
ATOM   3413 C CD2   . LEU A 1 494 ? 72.246  70.348  76.464  1.00 47.90  ? 494 LEU A CD2   1 
ATOM   3414 N N     . ARG A 1 495 ? 75.601  66.036  75.837  1.00 56.29  ? 495 ARG A N     1 
ATOM   3415 C CA    . ARG A 1 495 ? 75.927  64.809  75.121  1.00 55.63  ? 495 ARG A CA    1 
ATOM   3416 C C     . ARG A 1 495 ? 75.134  63.630  75.664  1.00 56.36  ? 495 ARG A C     1 
ATOM   3417 O O     . ARG A 1 495 ? 74.623  62.807  74.896  1.00 63.17  ? 495 ARG A O     1 
ATOM   3418 C CB    . ARG A 1 495 ? 77.428  64.540  75.219  1.00 57.12  ? 495 ARG A CB    1 
ATOM   3419 C CG    . ARG A 1 495 ? 77.922  63.360  74.409  1.00 61.11  ? 495 ARG A CG    1 
ATOM   3420 C CD    . ARG A 1 495 ? 79.440  63.331  74.404  1.00 64.59  ? 495 ARG A CD    1 
ATOM   3421 N NE    . ARG A 1 495 ? 79.974  62.078  73.887  1.00 71.38  ? 495 ARG A NE    1 
ATOM   3422 C CZ    . ARG A 1 495 ? 81.267  61.797  73.802  1.00 76.72  ? 495 ARG A CZ    1 
ATOM   3423 N NH1   . ARG A 1 495 ? 82.189  62.660  74.196  1.00 75.29  ? 495 ARG A NH1   1 
ATOM   3424 N NH2   . ARG A 1 495 ? 81.645  60.621  73.310  1.00 82.58  ? 495 ARG A NH2   1 
ATOM   3425 N N     . ALA A 1 496 ? 75.016  63.533  76.989  1.00 58.21  ? 496 ALA A N     1 
ATOM   3426 C CA    . ALA A 1 496 ? 74.214  62.481  77.595  1.00 65.46  ? 496 ALA A CA    1 
ATOM   3427 C C     . ALA A 1 496 ? 72.718  62.692  77.404  1.00 68.45  ? 496 ALA A C     1 
ATOM   3428 O O     . ALA A 1 496 ? 71.942  61.771  77.681  1.00 70.65  ? 496 ALA A O     1 
ATOM   3429 C CB    . ALA A 1 496 ? 74.533  62.371  79.086  1.00 66.22  ? 496 ALA A CB    1 
ATOM   3430 N N     . LYS A 1 497 ? 72.294  63.867  76.946  1.00 66.61  ? 497 LYS A N     1 
ATOM   3431 C CA    . LYS A 1 497 ? 70.876  64.144  76.730  1.00 67.70  ? 497 LYS A CA    1 
ATOM   3432 C C     . LYS A 1 497 ? 70.410  63.367  75.507  1.00 76.63  ? 497 LYS A C     1 
ATOM   3433 O O     . LYS A 1 497 ? 70.630  63.786  74.369  1.00 79.61  ? 497 LYS A O     1 
ATOM   3434 C CB    . LYS A 1 497 ? 70.640  65.638  76.547  1.00 61.89  ? 497 LYS A CB    1 
ATOM   3435 C CG    . LYS A 1 497 ? 70.782  66.461  77.813  1.00 62.33  ? 497 LYS A CG    1 
ATOM   3436 C CD    . LYS A 1 497 ? 69.744  66.085  78.849  1.00 69.99  ? 497 LYS A CD    1 
ATOM   3437 C CE    . LYS A 1 497 ? 69.387  67.282  79.710  1.00 66.88  ? 497 LYS A CE    1 
ATOM   3438 N NZ    . LYS A 1 497 ? 68.226  67.010  80.600  1.00 73.06  ? 497 LYS A NZ    1 
ATOM   3439 N N     . GLU A 1 498 ? 69.768  62.226  75.737  1.00 81.94  ? 498 GLU A N     1 
ATOM   3440 C CA    . GLU A 1 498 ? 69.255  61.432  74.636  1.00 85.00  ? 498 GLU A CA    1 
ATOM   3441 C C     . GLU A 1 498 ? 68.086  62.152  73.966  1.00 87.11  ? 498 GLU A C     1 
ATOM   3442 O O     . GLU A 1 498 ? 67.299  62.828  74.634  1.00 85.41  ? 498 GLU A O     1 
ATOM   3443 C CB    . GLU A 1 498 ? 68.807  60.061  75.129  1.00 86.04  ? 498 GLU A CB    1 
ATOM   3444 C CG    . GLU A 1 498 ? 69.948  59.092  75.392  1.00 86.85  ? 498 GLU A CG    1 
ATOM   3445 C CD    . GLU A 1 498 ? 71.061  59.209  74.369  1.00 93.19  ? 498 GLU A CD    1 
ATOM   3446 O OE1   . GLU A 1 498 ? 70.795  58.981  73.170  1.00 94.87  ? 498 GLU A OE1   1 
ATOM   3447 O OE2   . GLU A 1 498 ? 72.204  59.524  74.762  1.00 91.72  ? 498 GLU A OE2   1 
ATOM   3448 N N     . PRO A 1 499 ? 67.960  62.036  72.641  1.00 86.80  ? 499 PRO A N     1 
ATOM   3449 C CA    . PRO A 1 499 ? 66.806  62.654  71.967  1.00 87.26  ? 499 PRO A CA    1 
ATOM   3450 C C     . PRO A 1 499 ? 65.476  62.170  72.512  1.00 100.11 ? 499 PRO A C     1 
ATOM   3451 O O     . PRO A 1 499 ? 64.529  62.960  72.619  1.00 98.24  ? 499 PRO A O     1 
ATOM   3452 C CB    . PRO A 1 499 ? 67.003  62.252  70.499  1.00 80.62  ? 499 PRO A CB    1 
ATOM   3453 C CG    . PRO A 1 499 ? 68.465  61.992  70.368  1.00 78.41  ? 499 PRO A CG    1 
ATOM   3454 C CD    . PRO A 1 499 ? 68.915  61.443  71.689  1.00 83.08  ? 499 PRO A CD    1 
ATOM   3455 N N     . ALA A 1 500 ? 65.386  60.885  72.861  1.00 110.34 ? 500 ALA A N     1 
ATOM   3456 C CA    . ALA A 1 500 ? 64.226  60.312  73.534  1.00 118.01 ? 500 ALA A CA    1 
ATOM   3457 C C     . ALA A 1 500 ? 62.939  60.530  72.751  1.00 128.37 ? 500 ALA A C     1 
ATOM   3458 O O     . ALA A 1 500 ? 62.712  59.884  71.723  1.00 130.30 ? 500 ALA A O     1 
ATOM   3459 C CB    . ALA A 1 500 ? 64.090  60.888  74.945  1.00 115.89 ? 500 ALA A CB    1 
ATOM   3460 N N     . GLY A 1 501 ? 62.093  61.438  73.231  1.00 135.06 ? 501 GLY A N     1 
ATOM   3461 C CA    . GLY A 1 501 ? 60.780  61.628  72.648  1.00 142.74 ? 501 GLY A CA    1 
ATOM   3462 C C     . GLY A 1 501 ? 59.849  60.497  73.026  1.00 152.34 ? 501 GLY A C     1 
ATOM   3463 O O     . GLY A 1 501 ? 59.573  60.285  74.212  1.00 150.32 ? 501 GLY A O     1 
ATOM   3464 N N     . GLU A 1 502 ? 59.359  59.765  72.025  1.00 159.43 ? 502 GLU A N     1 
ATOM   3465 C CA    . GLU A 1 502 ? 58.569  58.546  72.221  1.00 162.45 ? 502 GLU A CA    1 
ATOM   3466 C C     . GLU A 1 502 ? 57.312  58.904  73.006  1.00 167.72 ? 502 GLU A C     1 
ATOM   3467 O O     . GLU A 1 502 ? 56.553  59.778  72.551  1.00 167.42 ? 502 GLU A O     1 
ATOM   3468 C CB    . GLU A 1 502 ? 59.471  57.481  72.850  1.00 158.41 ? 502 GLU A CB    1 
ATOM   3469 C CG    . GLU A 1 502 ? 59.132  56.057  72.449  1.00 155.61 ? 502 GLU A CG    1 
ATOM   3470 C CD    . GLU A 1 502 ? 60.221  55.075  72.831  1.00 152.67 ? 502 GLU A CD    1 
ATOM   3471 O OE1   . GLU A 1 502 ? 61.242  55.512  73.402  1.00 145.03 ? 502 GLU A OE1   1 
ATOM   3472 O OE2   . GLU A 1 502 ? 60.056  53.867  72.561  1.00 156.50 ? 502 GLU A OE2   1 
ATOM   3473 N N     . ASN A 1 503 ? 57.044  58.282  74.155  1.00 168.82 ? 503 ASN A N     1 
ATOM   3474 C CA    . ASN A 1 503 ? 55.801  58.538  74.874  1.00 168.43 ? 503 ASN A CA    1 
ATOM   3475 C C     . ASN A 1 503 ? 55.900  59.785  75.747  1.00 168.06 ? 503 ASN A C     1 
ATOM   3476 O O     . ASN A 1 503 ? 55.168  60.759  75.542  1.00 168.06 ? 503 ASN A O     1 
ATOM   3477 C CB    . ASN A 1 503 ? 55.427  57.317  75.720  1.00 166.00 ? 503 ASN A CB    1 
ATOM   3478 C CG    . ASN A 1 503 ? 54.019  57.402  76.276  1.00 164.22 ? 503 ASN A CG    1 
ATOM   3479 O OD1   . ASN A 1 503 ? 53.215  58.228  75.843  1.00 162.28 ? 503 ASN A OD1   1 
ATOM   3480 N ND2   . ASN A 1 503 ? 53.712  56.543  77.242  1.00 168.63 ? 503 ASN A ND2   1 
ATOM   3481 N N     . GLY A 1 504 ? 56.804  59.773  76.729  1.00 164.36 ? 504 GLY A N     1 
ATOM   3482 C CA    . GLY A 1 504 ? 56.878  60.872  77.686  1.00 159.69 ? 504 GLY A CA    1 
ATOM   3483 C C     . GLY A 1 504 ? 58.284  61.371  77.981  1.00 152.67 ? 504 GLY A C     1 
ATOM   3484 O O     . GLY A 1 504 ? 58.410  62.453  78.562  1.00 144.49 ? 504 GLY A O     1 
ATOM   3485 N N     . GLY A 1 505 ? 59.337  60.641  77.621  1.00 153.33 ? 505 GLY A N     1 
ATOM   3486 C CA    . GLY A 1 505 ? 60.691  61.116  77.871  1.00 140.75 ? 505 GLY A CA    1 
ATOM   3487 C C     . GLY A 1 505 ? 60.986  62.329  76.997  1.00 133.75 ? 505 GLY A C     1 
ATOM   3488 O O     . GLY A 1 505 ? 60.675  62.337  75.803  1.00 134.66 ? 505 GLY A O     1 
ATOM   3489 N N     . ARG A 1 506 ? 61.584  63.358  77.595  1.00 124.75 ? 506 ARG A N     1 
ATOM   3490 C CA    . ARG A 1 506 ? 61.845  64.591  76.863  1.00 119.42 ? 506 ARG A CA    1 
ATOM   3491 C C     . ARG A 1 506 ? 63.299  65.027  76.987  1.00 104.73 ? 506 ARG A C     1 
ATOM   3492 O O     . ARG A 1 506 ? 63.835  65.667  76.076  1.00 94.61  ? 506 ARG A O     1 
ATOM   3493 C CB    . ARG A 1 506 ? 60.920  65.708  77.351  1.00 116.33 ? 506 ARG A CB    1 
ATOM   3494 C CG    . ARG A 1 506 ? 59.474  65.552  76.918  1.00 121.47 ? 506 ARG A CG    1 
ATOM   3495 C CD    . ARG A 1 506 ? 58.597  66.625  77.541  1.00 121.84 ? 506 ARG A CD    1 
ATOM   3496 N NE    . ARG A 1 506 ? 58.851  66.780  78.969  1.00 119.55 ? 506 ARG A NE    1 
ATOM   3497 C CZ    . ARG A 1 506 ? 58.359  65.985  79.909  1.00 115.18 ? 506 ARG A CZ    1 
ATOM   3498 N NH1   . ARG A 1 506 ? 57.571  64.965  79.610  1.00 120.31 ? 506 ARG A NH1   1 
ATOM   3499 N NH2   . ARG A 1 506 ? 58.665  66.221  81.182  1.00 112.08 ? 506 ARG A NH2   1 
ATOM   3500 N N     . ALA A 1 507 ? 63.940  64.684  78.103  1.00 99.77  ? 507 ALA A N     1 
ATOM   3501 C CA    . ALA A 1 507 ? 65.292  65.141  78.417  1.00 89.07  ? 507 ALA A CA    1 
ATOM   3502 C C     . ALA A 1 507 ? 65.361  66.667  78.368  1.00 86.16  ? 507 ALA A C     1 
ATOM   3503 O O     . ALA A 1 507 ? 66.060  67.266  77.549  1.00 82.06  ? 507 ALA A O     1 
ATOM   3504 C CB    . ALA A 1 507 ? 66.323  64.503  77.483  1.00 83.53  ? 507 ALA A CB    1 
ATOM   3505 N N     . LEU A 1 508 ? 64.605  67.289  79.270  1.00 83.24  ? 508 LEU A N     1 
ATOM   3506 C CA    . LEU A 1 508 ? 64.453  68.735  79.270  1.00 78.52  ? 508 LEU A CA    1 
ATOM   3507 C C     . LEU A 1 508 ? 65.786  69.423  79.548  1.00 75.65  ? 508 LEU A C     1 
ATOM   3508 O O     . LEU A 1 508 ? 66.679  68.875  80.199  1.00 78.32  ? 508 LEU A O     1 
ATOM   3509 C CB    . LEU A 1 508 ? 63.417  69.158  80.310  1.00 76.34  ? 508 LEU A CB    1 
ATOM   3510 C CG    . LEU A 1 508 ? 61.951  69.016  79.899  1.00 84.49  ? 508 LEU A CG    1 
ATOM   3511 C CD1   . LEU A 1 508 ? 61.083  70.011  80.651  1.00 81.84  ? 508 LEU A CD1   1 
ATOM   3512 C CD2   . LEU A 1 508 ? 61.789  69.186  78.397  1.00 84.73  ? 508 LEU A CD2   1 
ATOM   3513 N N     . VAL A 1 509 ? 65.910  70.644  79.038  1.00 71.27  ? 509 VAL A N     1 
ATOM   3514 C CA    . VAL A 1 509 ? 67.142  71.418  79.170  1.00 66.96  ? 509 VAL A CA    1 
ATOM   3515 C C     . VAL A 1 509 ? 66.809  72.897  79.344  1.00 64.57  ? 509 VAL A C     1 
ATOM   3516 O O     . VAL A 1 509 ? 66.226  73.519  78.445  1.00 65.51  ? 509 VAL A O     1 
ATOM   3517 C CB    . VAL A 1 509 ? 68.076  71.163  77.973  1.00 60.71  ? 509 VAL A CB    1 
ATOM   3518 C CG1   . VAL A 1 509 ? 67.375  71.437  76.652  1.00 63.75  ? 509 VAL A CG1   1 
ATOM   3519 C CG2   . VAL A 1 509 ? 69.317  72.010  78.088  1.00 52.79  ? 509 VAL A CG2   1 
ATOM   3520 N N     . PRO A 1 510 ? 67.142  73.496  80.487  1.00 60.60  ? 510 PRO A N     1 
ATOM   3521 C CA    . PRO A 1 510 ? 66.824  74.912  80.702  1.00 63.66  ? 510 PRO A CA    1 
ATOM   3522 C C     . PRO A 1 510 ? 67.744  75.810  79.894  1.00 64.35  ? 510 PRO A C     1 
ATOM   3523 O O     . PRO A 1 510 ? 68.932  75.524  79.726  1.00 65.32  ? 510 PRO A O     1 
ATOM   3524 C CB    . PRO A 1 510 ? 67.043  75.105  82.210  1.00 61.15  ? 510 PRO A CB    1 
ATOM   3525 C CG    . PRO A 1 510 ? 67.335  73.728  82.767  1.00 61.46  ? 510 PRO A CG    1 
ATOM   3526 C CD    . PRO A 1 510 ? 67.856  72.919  81.633  1.00 56.14  ? 510 PRO A CD    1 
ATOM   3527 N N     . MET A 1 511 ? 67.190  76.913  79.395  1.00 62.02  ? 511 MET A N     1 
ATOM   3528 C CA    . MET A 1 511 ? 67.976  77.795  78.545  1.00 59.54  ? 511 MET A CA    1 
ATOM   3529 C C     . MET A 1 511 ? 67.335  79.173  78.484  1.00 66.08  ? 511 MET A C     1 
ATOM   3530 O O     . MET A 1 511 ? 66.154  79.348  78.793  1.00 70.75  ? 511 MET A O     1 
ATOM   3531 C CB    . MET A 1 511 ? 68.127  77.219  77.134  1.00 57.07  ? 511 MET A CB    1 
ATOM   3532 C CG    . MET A 1 511 ? 66.820  76.787  76.504  1.00 60.81  ? 511 MET A CG    1 
ATOM   3533 S SD    . MET A 1 511 ? 66.793  77.138  74.741  1.00 68.55  ? 511 MET A SD    1 
ATOM   3534 C CE    . MET A 1 511 ? 66.288  78.855  74.754  1.00 63.26  ? 511 MET A CE    1 
ATOM   3535 N N     . PHE A 1 512 ? 68.144  80.151  78.078  1.00 64.91  ? 512 PHE A N     1 
ATOM   3536 C CA    . PHE A 1 512 ? 67.674  81.499  77.796  1.00 61.52  ? 512 PHE A CA    1 
ATOM   3537 C C     . PHE A 1 512 ? 68.580  82.107  76.735  1.00 61.98  ? 512 PHE A C     1 
ATOM   3538 O O     . PHE A 1 512 ? 69.727  81.690  76.559  1.00 61.17  ? 512 PHE A O     1 
ATOM   3539 C CB    . PHE A 1 512 ? 67.642  82.371  79.056  1.00 57.98  ? 512 PHE A CB    1 
ATOM   3540 C CG    . PHE A 1 512 ? 69.000  82.722  79.592  1.00 60.98  ? 512 PHE A CG    1 
ATOM   3541 C CD1   . PHE A 1 512 ? 69.703  81.829  80.376  1.00 63.10  ? 512 PHE A CD1   1 
ATOM   3542 C CD2   . PHE A 1 512 ? 69.567  83.954  79.319  1.00 64.08  ? 512 PHE A CD2   1 
ATOM   3543 C CE1   . PHE A 1 512 ? 70.947  82.155  80.871  1.00 61.05  ? 512 PHE A CE1   1 
ATOM   3544 C CE2   . PHE A 1 512 ? 70.810  84.283  79.809  1.00 62.40  ? 512 PHE A CE2   1 
ATOM   3545 C CZ    . PHE A 1 512 ? 71.502  83.382  80.585  1.00 61.67  ? 512 PHE A CZ    1 
ATOM   3546 N N     . VAL A 1 513 ? 68.052  83.108  76.031  1.00 61.79  ? 513 VAL A N     1 
ATOM   3547 C CA    . VAL A 1 513 ? 68.718  83.697  74.871  1.00 58.21  ? 513 VAL A CA    1 
ATOM   3548 C C     . VAL A 1 513 ? 69.288  85.058  75.248  1.00 61.60  ? 513 VAL A C     1 
ATOM   3549 O O     . VAL A 1 513 ? 68.729  85.765  76.099  1.00 60.97  ? 513 VAL A O     1 
ATOM   3550 C CB    . VAL A 1 513 ? 67.745  83.807  73.678  1.00 59.70  ? 513 VAL A CB    1 
ATOM   3551 C CG1   . VAL A 1 513 ? 66.650  84.823  73.957  1.00 70.19  ? 513 VAL A CG1   1 
ATOM   3552 C CG2   . VAL A 1 513 ? 68.491  84.148  72.402  1.00 60.45  ? 513 VAL A CG2   1 
ATOM   3553 N N     . ARG A 1 514 ? 70.420  85.417  74.638  1.00 60.86  ? 514 ARG A N     1 
ATOM   3554 C CA    . ARG A 1 514 ? 71.064  86.709  74.848  1.00 58.24  ? 514 ARG A CA    1 
ATOM   3555 C C     . ARG A 1 514 ? 71.198  87.435  73.517  1.00 64.86  ? 514 ARG A C     1 
ATOM   3556 O O     . ARG A 1 514 ? 71.683  86.858  72.538  1.00 69.21  ? 514 ARG A O     1 
ATOM   3557 C CB    . ARG A 1 514 ? 72.441  86.547  75.494  1.00 57.61  ? 514 ARG A CB    1 
ATOM   3558 C CG    . ARG A 1 514 ? 73.146  87.878  75.705  1.00 63.08  ? 514 ARG A CG    1 
ATOM   3559 C CD    . ARG A 1 514 ? 74.578  87.699  76.174  1.00 62.13  ? 514 ARG A CD    1 
ATOM   3560 N NE    . ARG A 1 514 ? 74.662  87.309  77.576  1.00 70.02  ? 514 ARG A NE    1 
ATOM   3561 C CZ    . ARG A 1 514 ? 74.831  86.064  78.001  1.00 65.20  ? 514 ARG A CZ    1 
ATOM   3562 N NH1   . ARG A 1 514 ? 74.932  85.054  77.154  1.00 57.21  ? 514 ARG A NH1   1 
ATOM   3563 N NH2   . ARG A 1 514 ? 74.907  85.830  79.308  1.00 60.88  ? 514 ARG A NH2   1 
ATOM   3564 N N     . LYS A 1 515 ? 70.781  88.698  73.487  1.00 65.75  ? 515 LYS A N     1 
ATOM   3565 C CA    . LYS A 1 515 ? 70.939  89.520  72.296  1.00 66.22  ? 515 LYS A CA    1 
ATOM   3566 C C     . LYS A 1 515 ? 72.392  89.953  72.131  1.00 67.97  ? 515 LYS A C     1 
ATOM   3567 O O     . LYS A 1 515 ? 73.151  90.044  73.099  1.00 72.16  ? 515 LYS A O     1 
ATOM   3568 C CB    . LYS A 1 515 ? 70.034  90.750  72.376  1.00 69.33  ? 515 LYS A CB    1 
ATOM   3569 C CG    . LYS A 1 515 ? 68.616  90.518  71.878  1.00 73.13  ? 515 LYS A CG    1 
ATOM   3570 C CD    . LYS A 1 515 ? 67.739  91.748  72.074  1.00 78.98  ? 515 LYS A CD    1 
ATOM   3571 C CE    . LYS A 1 515 ? 68.292  92.969  71.351  1.00 76.03  ? 515 LYS A CE    1 
ATOM   3572 N NZ    . LYS A 1 515 ? 68.787  92.658  69.982  1.00 75.50  ? 515 LYS A NZ    1 
ATOM   3573 N N     . SER A 1 516 ? 72.776  90.228  70.885  1.00 69.65  ? 516 SER A N     1 
ATOM   3574 C CA    . SER A 1 516 ? 74.115  90.716  70.584  1.00 73.45  ? 516 SER A CA    1 
ATOM   3575 C C     . SER A 1 516 ? 74.073  91.511  69.285  1.00 79.02  ? 516 SER A C     1 
ATOM   3576 O O     . SER A 1 516 ? 73.059  91.546  68.584  1.00 80.05  ? 516 SER A O     1 
ATOM   3577 C CB    . SER A 1 516 ? 75.130  89.571  70.488  1.00 68.48  ? 516 SER A CB    1 
ATOM   3578 O OG    . SER A 1 516 ? 74.932  88.808  69.312  1.00 77.52  ? 516 SER A OG    1 
ATOM   3579 N N     . GLN A 1 517 ? 75.198  92.151  68.971  1.00 77.81  ? 517 GLN A N     1 
ATOM   3580 C CA    . GLN A 1 517 ? 75.318  93.008  67.798  1.00 74.92  ? 517 GLN A CA    1 
ATOM   3581 C C     . GLN A 1 517 ? 75.815  92.266  66.564  1.00 74.62  ? 517 GLN A C     1 
ATOM   3582 O O     . GLN A 1 517 ? 76.004  92.893  65.517  1.00 77.82  ? 517 GLN A O     1 
ATOM   3583 C CB    . GLN A 1 517 ? 76.256  94.179  68.101  1.00 80.50  ? 517 GLN A CB    1 
ATOM   3584 C CG    . GLN A 1 517 ? 75.972  94.883  69.420  1.00 86.54  ? 517 GLN A CG    1 
ATOM   3585 C CD    . GLN A 1 517 ? 74.537  95.362  69.536  1.00 90.26  ? 517 GLN A CD    1 
ATOM   3586 O OE1   . GLN A 1 517 ? 73.655  94.626  69.982  1.00 86.70  ? 517 GLN A OE1   1 
ATOM   3587 N NE2   . GLN A 1 517 ? 74.296  96.604  69.134  1.00 96.60  ? 517 GLN A NE2   1 
ATOM   3588 N N     . PHE A 1 518 ? 76.033  90.958  66.665  1.00 72.33  ? 518 PHE A N     1 
ATOM   3589 C CA    . PHE A 1 518 ? 76.476  90.131  65.544  1.00 68.61  ? 518 PHE A CA    1 
ATOM   3590 C C     . PHE A 1 518 ? 75.260  89.831  64.676  1.00 69.30  ? 518 PHE A C     1 
ATOM   3591 O O     . PHE A 1 518 ? 74.535  88.862  64.899  1.00 71.06  ? 518 PHE A O     1 
ATOM   3592 C CB    . PHE A 1 518 ? 77.126  88.856  66.063  1.00 63.47  ? 518 PHE A CB    1 
ATOM   3593 C CG    . PHE A 1 518 ? 78.198  88.306  65.173  1.00 59.29  ? 518 PHE A CG    1 
ATOM   3594 C CD1   . PHE A 1 518 ? 79.513  88.701  65.332  1.00 61.12  ? 518 PHE A CD1   1 
ATOM   3595 C CD2   . PHE A 1 518 ? 77.898  87.371  64.202  1.00 59.40  ? 518 PHE A CD2   1 
ATOM   3596 C CE1   . PHE A 1 518 ? 80.505  88.189  64.526  1.00 63.13  ? 518 PHE A CE1   1 
ATOM   3597 C CE2   . PHE A 1 518 ? 78.888  86.854  63.394  1.00 59.05  ? 518 PHE A CE2   1 
ATOM   3598 C CZ    . PHE A 1 518 ? 80.193  87.263  63.557  1.00 61.16  ? 518 PHE A CZ    1 
ATOM   3599 N N     . ARG A 1 519 ? 75.028  90.676  63.673  1.00 67.85  ? 519 ARG A N     1 
ATOM   3600 C CA    . ARG A 1 519 ? 73.826  90.585  62.858  1.00 70.82  ? 519 ARG A CA    1 
ATOM   3601 C C     . ARG A 1 519 ? 74.178  90.756  61.387  1.00 71.43  ? 519 ARG A C     1 
ATOM   3602 O O     . ARG A 1 519 ? 75.233  91.287  61.035  1.00 75.25  ? 519 ARG A O     1 
ATOM   3603 C CB    . ARG A 1 519 ? 72.785  91.637  63.266  1.00 73.99  ? 519 ARG A CB    1 
ATOM   3604 C CG    . ARG A 1 519 ? 72.269  91.499  64.688  1.00 71.07  ? 519 ARG A CG    1 
ATOM   3605 C CD    . ARG A 1 519 ? 71.551  90.180  64.896  1.00 75.09  ? 519 ARG A CD    1 
ATOM   3606 N NE    . ARG A 1 519 ? 71.290  89.919  66.306  1.00 79.13  ? 519 ARG A NE    1 
ATOM   3607 C CZ    . ARG A 1 519 ? 70.257  90.407  66.979  1.00 82.08  ? 519 ARG A CZ    1 
ATOM   3608 N NH1   . ARG A 1 519 ? 69.365  91.194  66.402  1.00 84.81  ? 519 ARG A NH1   1 
ATOM   3609 N NH2   . ARG A 1 519 ? 70.115  90.095  68.264  1.00 80.81  ? 519 ARG A NH2   1 
ATOM   3610 N N     . LEU A 1 520 ? 73.272  90.294  60.529  1.00 68.66  ? 520 LEU A N     1 
ATOM   3611 C CA    . LEU A 1 520 ? 73.404  90.462  59.092  1.00 69.63  ? 520 LEU A CA    1 
ATOM   3612 C C     . LEU A 1 520 ? 73.108  91.905  58.694  1.00 78.76  ? 520 LEU A C     1 
ATOM   3613 O O     . LEU A 1 520 ? 72.457  92.643  59.438  1.00 83.35  ? 520 LEU A O     1 
ATOM   3614 C CB    . LEU A 1 520 ? 72.456  89.514  58.364  1.00 75.05  ? 520 LEU A CB    1 
ATOM   3615 C CG    . LEU A 1 520 ? 72.966  88.096  58.104  1.00 76.14  ? 520 LEU A CG    1 
ATOM   3616 C CD1   . LEU A 1 520 ? 71.828  87.195  57.668  1.00 72.37  ? 520 LEU A CD1   1 
ATOM   3617 C CD2   . LEU A 1 520 ? 74.082  88.085  57.074  1.00 76.48  ? 520 LEU A CD2   1 
ATOM   3618 N N     . PRO A 1 521 ? 73.584  92.337  57.524  1.00 83.17  ? 521 PRO A N     1 
ATOM   3619 C CA    . PRO A 1 521 ? 73.284  93.700  57.071  1.00 85.67  ? 521 PRO A CA    1 
ATOM   3620 C C     . PRO A 1 521 ? 71.792  93.898  56.855  1.00 92.28  ? 521 PRO A C     1 
ATOM   3621 O O     . PRO A 1 521 ? 71.053  92.959  56.553  1.00 91.61  ? 521 PRO A O     1 
ATOM   3622 C CB    . PRO A 1 521 ? 74.060  93.818  55.754  1.00 84.51  ? 521 PRO A CB    1 
ATOM   3623 C CG    . PRO A 1 521 ? 75.115  92.774  55.836  1.00 79.93  ? 521 PRO A CG    1 
ATOM   3624 C CD    . PRO A 1 521 ? 74.509  91.650  56.608  1.00 79.44  ? 521 PRO A CD    1 
ATOM   3625 N N     . PHE A 1 522 ? 71.354  95.148  57.026  1.00 95.02  ? 522 PHE A N     1 
ATOM   3626 C CA    . PHE A 1 522 ? 69.933  95.461  56.909  1.00 102.56 ? 522 PHE A CA    1 
ATOM   3627 C C     . PHE A 1 522 ? 69.412  95.177  55.506  1.00 104.12 ? 522 PHE A C     1 
ATOM   3628 O O     . PHE A 1 522 ? 68.303  94.655  55.342  1.00 105.49 ? 522 PHE A O     1 
ATOM   3629 C CB    . PHE A 1 522 ? 69.687  96.920  57.288  1.00 111.42 ? 522 PHE A CB    1 
ATOM   3630 C CG    . PHE A 1 522 ? 68.239  97.312  57.281  1.00 117.05 ? 522 PHE A CG    1 
ATOM   3631 C CD1   . PHE A 1 522 ? 67.372  96.827  58.246  1.00 113.60 ? 522 PHE A CD1   1 
ATOM   3632 C CD2   . PHE A 1 522 ? 67.744  98.167  56.311  1.00 118.26 ? 522 PHE A CD2   1 
ATOM   3633 C CE1   . PHE A 1 522 ? 66.037  97.187  58.243  1.00 117.13 ? 522 PHE A CE1   1 
ATOM   3634 C CE2   . PHE A 1 522 ? 66.410  98.531  56.302  1.00 121.96 ? 522 PHE A CE2   1 
ATOM   3635 C CZ    . PHE A 1 522 ? 65.556  98.040  57.269  1.00 123.26 ? 522 PHE A CZ    1 
ATOM   3636 N N     . LYS A 1 523 ? 70.192  95.513  54.483  1.00 101.09 ? 523 LYS A N     1 
ATOM   3637 C CA    . LYS A 1 523 ? 69.799  95.298  53.097  1.00 101.44 ? 523 LYS A CA    1 
ATOM   3638 C C     . LYS A 1 523 ? 70.512  94.071  52.546  1.00 99.26  ? 523 LYS A C     1 
ATOM   3639 O O     . LYS A 1 523 ? 71.725  93.916  52.726  1.00 94.86  ? 523 LYS A O     1 
ATOM   3640 C CB    . LYS A 1 523 ? 70.107  96.529  52.242  1.00 101.91 ? 523 LYS A CB    1 
ATOM   3641 C CG    . LYS A 1 523 ? 71.517  97.073  52.394  1.00 107.09 ? 523 LYS A CG    1 
ATOM   3642 C CD    . LYS A 1 523 ? 71.673  98.396  51.663  1.00 110.42 ? 523 LYS A CD    1 
ATOM   3643 C CE    . LYS A 1 523 ? 73.123  98.658  51.293  1.00 104.44 ? 523 LYS A CE    1 
ATOM   3644 N NZ    . LYS A 1 523 ? 73.443  98.169  49.924  1.00 98.53  ? 523 LYS A NZ    1 
ATOM   3645 N N     . SER A 1 524 ? 69.753  93.200  51.877  1.00 101.52 ? 524 SER A N     1 
ATOM   3646 C CA    . SER A 1 524 ? 70.301  91.944  51.377  1.00 99.24  ? 524 SER A CA    1 
ATOM   3647 C C     . SER A 1 524 ? 71.312  92.146  50.256  1.00 98.92  ? 524 SER A C     1 
ATOM   3648 O O     . SER A 1 524 ? 72.053  91.211  49.935  1.00 97.76  ? 524 SER A O     1 
ATOM   3649 C CB    . SER A 1 524 ? 69.170  91.036  50.895  1.00 99.94  ? 524 SER A CB    1 
ATOM   3650 O OG    . SER A 1 524 ? 68.306  91.726  50.010  1.00 105.43 ? 524 SER A OG    1 
ATOM   3651 N N     . THR A 1 525 ? 71.358  93.335  49.652  1.00 101.07 ? 525 THR A N     1 
ATOM   3652 C CA    . THR A 1 525 ? 72.310  93.588  48.578  1.00 99.95  ? 525 THR A CA    1 
ATOM   3653 C C     . THR A 1 525 ? 73.749  93.623  49.075  1.00 99.32  ? 525 THR A C     1 
ATOM   3654 O O     . THR A 1 525 ? 74.673  93.472  48.269  1.00 100.81 ? 525 THR A O     1 
ATOM   3655 C CB    . THR A 1 525 ? 71.981  94.908  47.880  1.00 104.07 ? 525 THR A CB    1 
ATOM   3656 O OG1   . THR A 1 525 ? 72.417  96.002  48.696  1.00 105.58 ? 525 THR A OG1   1 
ATOM   3657 C CG2   . THR A 1 525 ? 70.484  95.028  47.655  1.00 103.13 ? 525 THR A CG2   1 
ATOM   3658 N N     . THR A 1 526 ? 73.957  93.818  50.371  1.00 93.50  ? 526 THR A N     1 
ATOM   3659 C CA    . THR A 1 526 ? 75.308  93.944  50.903  1.00 88.46  ? 526 THR A CA    1 
ATOM   3660 C C     . THR A 1 526 ? 76.013  92.593  50.882  1.00 83.09  ? 526 THR A C     1 
ATOM   3661 O O     . THR A 1 526 ? 75.465  91.605  51.384  1.00 83.37  ? 526 THR A O     1 
ATOM   3662 C CB    . THR A 1 526 ? 75.272  94.489  52.327  1.00 89.96  ? 526 THR A CB    1 
ATOM   3663 O OG1   . THR A 1 526 ? 74.520  95.708  52.356  1.00 98.14  ? 526 THR A OG1   1 
ATOM   3664 C CG2   . THR A 1 526 ? 76.680  94.759  52.826  1.00 83.07  ? 526 THR A CG2   1 
ATOM   3665 N N     . PRO A 1 527 ? 77.209  92.503  50.308  1.00 81.79  ? 527 PRO A N     1 
ATOM   3666 C CA    . PRO A 1 527 ? 77.977  91.259  50.401  1.00 79.23  ? 527 PRO A CA    1 
ATOM   3667 C C     . PRO A 1 527 ? 78.406  90.987  51.833  1.00 82.41  ? 527 PRO A C     1 
ATOM   3668 O O     . PRO A 1 527 ? 78.596  91.904  52.635  1.00 85.68  ? 527 PRO A O     1 
ATOM   3669 C CB    . PRO A 1 527 ? 79.189  91.515  49.497  1.00 82.19  ? 527 PRO A CB    1 
ATOM   3670 C CG    . PRO A 1 527 ? 78.812  92.695  48.657  1.00 88.97  ? 527 PRO A CG    1 
ATOM   3671 C CD    . PRO A 1 527 ? 77.899  93.518  49.500  1.00 89.94  ? 527 PRO A CD    1 
ATOM   3672 N N     . VAL A 1 528 ? 78.553  89.704  52.151  1.00 79.12  ? 528 VAL A N     1 
ATOM   3673 C CA    . VAL A 1 528 ? 78.951  89.263  53.482  1.00 69.78  ? 528 VAL A CA    1 
ATOM   3674 C C     . VAL A 1 528 ? 80.144  88.330  53.349  1.00 63.12  ? 528 VAL A C     1 
ATOM   3675 O O     . VAL A 1 528 ? 80.119  87.393  52.544  1.00 70.36  ? 528 VAL A O     1 
ATOM   3676 C CB    . VAL A 1 528 ? 77.797  88.563  54.223  1.00 69.34  ? 528 VAL A CB    1 
ATOM   3677 C CG1   . VAL A 1 528 ? 76.892  89.590  54.871  1.00 69.79  ? 528 VAL A CG1   1 
ATOM   3678 C CG2   . VAL A 1 528 ? 77.006  87.692  53.266  1.00 74.16  ? 528 VAL A CG2   1 
ATOM   3679 N N     . ILE A 1 529 ? 81.185  88.586  54.135  1.00 57.61  ? 529 ILE A N     1 
ATOM   3680 C CA    . ILE A 1 529 ? 82.370  87.739  54.184  1.00 58.71  ? 529 ILE A CA    1 
ATOM   3681 C C     . ILE A 1 529 ? 82.399  87.071  55.549  1.00 64.64  ? 529 ILE A C     1 
ATOM   3682 O O     . ILE A 1 529 ? 82.468  87.751  56.580  1.00 72.39  ? 529 ILE A O     1 
ATOM   3683 C CB    . ILE A 1 529 ? 83.654  88.541  53.929  1.00 60.73  ? 529 ILE A CB    1 
ATOM   3684 C CG1   . ILE A 1 529 ? 83.644  89.114  52.512  1.00 64.86  ? 529 ILE A CG1   1 
ATOM   3685 C CG2   . ILE A 1 529 ? 84.876  87.665  54.141  1.00 61.89  ? 529 ILE A CG2   1 
ATOM   3686 C CD1   . ILE A 1 529 ? 84.748  90.106  52.247  1.00 71.79  ? 529 ILE A CD1   1 
ATOM   3687 N N     . MET A 1 530 ? 82.347  85.742  55.558  1.00 62.25  ? 530 MET A N     1 
ATOM   3688 C CA    . MET A 1 530 ? 82.253  84.960  56.783  1.00 60.45  ? 530 MET A CA    1 
ATOM   3689 C C     . MET A 1 530 ? 83.475  84.062  56.888  1.00 65.14  ? 530 MET A C     1 
ATOM   3690 O O     . MET A 1 530 ? 83.703  83.216  56.018  1.00 70.91  ? 530 MET A O     1 
ATOM   3691 C CB    . MET A 1 530 ? 80.969  84.131  56.793  1.00 59.95  ? 530 MET A CB    1 
ATOM   3692 C CG    . MET A 1 530 ? 79.749  84.899  56.322  1.00 56.31  ? 530 MET A CG    1 
ATOM   3693 S SD    . MET A 1 530 ? 78.256  83.901  56.367  1.00 61.37  ? 530 MET A SD    1 
ATOM   3694 C CE    . MET A 1 530 ? 78.889  82.361  55.714  1.00 61.21  ? 530 MET A CE    1 
ATOM   3695 N N     . VAL A 1 531 ? 84.253  84.242  57.952  1.00 60.00  ? 531 VAL A N     1 
ATOM   3696 C CA    . VAL A 1 531 ? 85.479  83.484  58.168  1.00 63.42  ? 531 VAL A CA    1 
ATOM   3697 C C     . VAL A 1 531 ? 85.485  82.974  59.602  1.00 63.37  ? 531 VAL A C     1 
ATOM   3698 O O     . VAL A 1 531 ? 85.367  83.763  60.547  1.00 68.07  ? 531 VAL A O     1 
ATOM   3699 C CB    . VAL A 1 531 ? 86.732  84.329  57.883  1.00 64.45  ? 531 VAL A CB    1 
ATOM   3700 C CG1   . VAL A 1 531 ? 86.808  85.499  58.843  1.00 61.60  ? 531 VAL A CG1   1 
ATOM   3701 C CG2   . VAL A 1 531 ? 87.987  83.479  57.983  1.00 68.63  ? 531 VAL A CG2   1 
ATOM   3702 N N     . GLY A 1 532 ? 85.601  81.658  59.763  1.00 61.88  ? 532 GLY A N     1 
ATOM   3703 C CA    . GLY A 1 532 ? 85.777  81.058  61.063  1.00 65.80  ? 532 GLY A CA    1 
ATOM   3704 C C     . GLY A 1 532 ? 85.955  79.556  60.982  1.00 72.49  ? 532 GLY A C     1 
ATOM   3705 O O     . GLY A 1 532 ? 85.172  78.847  60.343  1.00 78.02  ? 532 GLY A O     1 
ATOM   3706 N N     . PRO A 1 533 ? 86.991  79.039  61.638  1.00 77.17  ? 533 PRO A N     1 
ATOM   3707 C CA    . PRO A 1 533 ? 87.207  77.588  61.650  1.00 83.38  ? 533 PRO A CA    1 
ATOM   3708 C C     . PRO A 1 533 ? 86.552  76.910  62.841  1.00 85.40  ? 533 PRO A C     1 
ATOM   3709 O O     . PRO A 1 533 ? 85.965  77.577  63.700  1.00 83.90  ? 533 PRO A O     1 
ATOM   3710 C CB    . PRO A 1 533 ? 88.732  77.470  61.709  1.00 85.04  ? 533 PRO A CB    1 
ATOM   3711 C CG    . PRO A 1 533 ? 89.153  78.679  62.478  1.00 87.40  ? 533 PRO A CG    1 
ATOM   3712 C CD    . PRO A 1 533 ? 88.137  79.769  62.206  1.00 81.37  ? 533 PRO A CD    1 
ATOM   3713 N N     . GLY A 1 534 ? 86.655  75.585  62.903  1.00 91.57  ? 534 GLY A N     1 
ATOM   3714 C CA    . GLY A 1 534 ? 86.129  74.853  64.042  1.00 92.17  ? 534 GLY A CA    1 
ATOM   3715 C C     . GLY A 1 534 ? 84.628  75.000  64.165  1.00 85.29  ? 534 GLY A C     1 
ATOM   3716 O O     . GLY A 1 534 ? 83.896  75.053  63.171  1.00 83.51  ? 534 GLY A O     1 
ATOM   3717 N N     . THR A 1 535 ? 84.157  75.075  65.408  1.00 81.65  ? 535 THR A N     1 
ATOM   3718 C CA    . THR A 1 535 ? 82.736  75.211  65.701  1.00 78.39  ? 535 THR A CA    1 
ATOM   3719 C C     . THR A 1 535 ? 82.212  76.623  65.482  1.00 74.58  ? 535 THR A C     1 
ATOM   3720 O O     . THR A 1 535 ? 81.082  76.916  65.885  1.00 70.96  ? 535 THR A O     1 
ATOM   3721 C CB    . THR A 1 535 ? 82.448  74.777  67.140  1.00 72.67  ? 535 THR A CB    1 
ATOM   3722 O OG1   . THR A 1 535 ? 83.522  75.194  67.991  1.00 67.67  ? 535 THR A OG1   1 
ATOM   3723 C CG2   . THR A 1 535 ? 82.292  73.270  67.217  1.00 66.02  ? 535 THR A CG2   1 
ATOM   3724 N N     . GLY A 1 536 ? 82.996  77.500  64.857  1.00 76.76  ? 536 GLY A N     1 
ATOM   3725 C CA    . GLY A 1 536 ? 82.523  78.841  64.573  1.00 76.72  ? 536 GLY A CA    1 
ATOM   3726 C C     . GLY A 1 536 ? 81.526  78.924  63.439  1.00 70.30  ? 536 GLY A C     1 
ATOM   3727 O O     . GLY A 1 536 ? 81.000  80.010  63.176  1.00 70.48  ? 536 GLY A O     1 
ATOM   3728 N N     . ILE A 1 537 ? 81.253  77.806  62.764  1.00 68.19  ? 537 ILE A N     1 
ATOM   3729 C CA    . ILE A 1 537 ? 80.357  77.816  61.616  1.00 73.33  ? 537 ILE A CA    1 
ATOM   3730 C C     . ILE A 1 537 ? 78.898  78.002  62.005  1.00 73.17  ? 537 ILE A C     1 
ATOM   3731 O O     . ILE A 1 537 ? 78.077  78.331  61.141  1.00 72.38  ? 537 ILE A O     1 
ATOM   3732 C CB    . ILE A 1 537 ? 80.552  76.511  60.815  1.00 79.13  ? 537 ILE A CB    1 
ATOM   3733 C CG1   . ILE A 1 537 ? 79.927  76.618  59.423  1.00 75.37  ? 537 ILE A CG1   1 
ATOM   3734 C CG2   . ILE A 1 537 ? 79.971  75.332  61.572  1.00 80.95  ? 537 ILE A CG2   1 
ATOM   3735 C CD1   . ILE A 1 537 ? 80.601  75.746  58.389  1.00 84.53  ? 537 ILE A CD1   1 
ATOM   3736 N N     . ALA A 1 538 ? 78.553  77.822  63.283  1.00 65.95  ? 538 ALA A N     1 
ATOM   3737 C CA    . ALA A 1 538 ? 77.145  77.853  63.679  1.00 61.55  ? 538 ALA A CA    1 
ATOM   3738 C C     . ALA A 1 538 ? 76.469  79.189  63.390  1.00 62.91  ? 538 ALA A C     1 
ATOM   3739 O O     . ALA A 1 538 ? 75.433  79.192  62.700  1.00 68.13  ? 538 ALA A O     1 
ATOM   3740 C CB    . ALA A 1 538 ? 77.018  77.458  65.154  1.00 53.46  ? 538 ALA A CB    1 
ATOM   3741 N N     . PRO A 1 539 ? 76.973  80.341  63.852  1.00 58.09  ? 539 PRO A N     1 
ATOM   3742 C CA    . PRO A 1 539 ? 76.360  81.602  63.409  1.00 60.58  ? 539 PRO A CA    1 
ATOM   3743 C C     . PRO A 1 539 ? 76.488  81.802  61.915  1.00 65.91  ? 539 PRO A C     1 
ATOM   3744 O O     . PRO A 1 539 ? 75.606  82.404  61.288  1.00 69.67  ? 539 PRO A O     1 
ATOM   3745 C CB    . PRO A 1 539 ? 77.130  82.665  64.202  1.00 56.61  ? 539 PRO A CB    1 
ATOM   3746 C CG    . PRO A 1 539 ? 78.447  82.052  64.445  1.00 58.13  ? 539 PRO A CG    1 
ATOM   3747 C CD    . PRO A 1 539 ? 78.182  80.591  64.659  1.00 58.00  ? 539 PRO A CD    1 
ATOM   3748 N N     . PHE A 1 540 ? 77.567  81.291  61.322  1.00 64.00  ? 540 PHE A N     1 
ATOM   3749 C CA    . PHE A 1 540 ? 77.719  81.358  59.877  1.00 59.91  ? 540 PHE A CA    1 
ATOM   3750 C C     . PHE A 1 540 ? 76.661  80.520  59.174  1.00 61.41  ? 540 PHE A C     1 
ATOM   3751 O O     . PHE A 1 540 ? 76.137  80.931  58.136  1.00 66.47  ? 540 PHE A O     1 
ATOM   3752 C CB    . PHE A 1 540 ? 79.126  80.921  59.482  1.00 60.75  ? 540 PHE A CB    1 
ATOM   3753 C CG    . PHE A 1 540 ? 80.197  81.849  59.970  1.00 60.46  ? 540 PHE A CG    1 
ATOM   3754 C CD1   . PHE A 1 540 ? 79.913  83.183  60.210  1.00 59.50  ? 540 PHE A CD1   1 
ATOM   3755 C CD2   . PHE A 1 540 ? 81.480  81.390  60.202  1.00 62.51  ? 540 PHE A CD2   1 
ATOM   3756 C CE1   . PHE A 1 540 ? 80.889  84.042  60.664  1.00 59.04  ? 540 PHE A CE1   1 
ATOM   3757 C CE2   . PHE A 1 540 ? 82.460  82.245  60.657  1.00 62.54  ? 540 PHE A CE2   1 
ATOM   3758 C CZ    . PHE A 1 540 ? 82.166  83.572  60.887  1.00 61.22  ? 540 PHE A CZ    1 
ATOM   3759 N N     . MET A 1 541 ? 76.322  79.349  59.721  1.00 60.19  ? 541 MET A N     1 
ATOM   3760 C CA    . MET A 1 541 ? 75.218  78.587  59.142  1.00 61.58  ? 541 MET A CA    1 
ATOM   3761 C C     . MET A 1 541 ? 73.891  79.308  59.303  1.00 61.87  ? 541 MET A C     1 
ATOM   3762 O O     . MET A 1 541 ? 73.042  79.256  58.405  1.00 70.92  ? 541 MET A O     1 
ATOM   3763 C CB    . MET A 1 541 ? 75.111  77.198  59.755  1.00 57.90  ? 541 MET A CB    1 
ATOM   3764 C CG    . MET A 1 541 ? 76.274  76.285  59.528  1.00 63.95  ? 541 MET A CG    1 
ATOM   3765 S SD    . MET A 1 541 ? 75.658  75.017  58.414  1.00 92.11  ? 541 MET A SD    1 
ATOM   3766 C CE    . MET A 1 541 ? 75.011  73.855  59.598  1.00 87.00  ? 541 MET A CE    1 
ATOM   3767 N N     . GLY A 1 542 ? 73.667  79.942  60.454  1.00 55.06  ? 542 GLY A N     1 
ATOM   3768 C CA    . GLY A 1 542 ? 72.456  80.732  60.604  1.00 58.07  ? 542 GLY A CA    1 
ATOM   3769 C C     . GLY A 1 542 ? 72.356  81.806  59.540  1.00 65.40  ? 542 GLY A C     1 
ATOM   3770 O O     . GLY A 1 542 ? 71.316  81.973  58.895  1.00 70.35  ? 542 GLY A O     1 
ATOM   3771 N N     . PHE A 1 543 ? 73.462  82.517  59.311  1.00 65.04  ? 543 PHE A N     1 
ATOM   3772 C CA    . PHE A 1 543 ? 73.504  83.519  58.252  1.00 66.56  ? 543 PHE A CA    1 
ATOM   3773 C C     . PHE A 1 543 ? 73.258  82.885  56.889  1.00 68.51  ? 543 PHE A C     1 
ATOM   3774 O O     . PHE A 1 543 ? 72.558  83.456  56.046  1.00 73.06  ? 543 PHE A O     1 
ATOM   3775 C CB    . PHE A 1 543 ? 74.856  84.232  58.261  1.00 65.27  ? 543 PHE A CB    1 
ATOM   3776 C CG    . PHE A 1 543 ? 75.076  85.107  59.460  1.00 66.87  ? 543 PHE A CG    1 
ATOM   3777 C CD1   . PHE A 1 543 ? 74.009  85.572  60.206  1.00 70.04  ? 543 PHE A CD1   1 
ATOM   3778 C CD2   . PHE A 1 543 ? 76.357  85.464  59.841  1.00 64.72  ? 543 PHE A CD2   1 
ATOM   3779 C CE1   . PHE A 1 543 ? 74.216  86.377  61.307  1.00 69.76  ? 543 PHE A CE1   1 
ATOM   3780 C CE2   . PHE A 1 543 ? 76.568  86.267  60.939  1.00 67.38  ? 543 PHE A CE2   1 
ATOM   3781 C CZ    . PHE A 1 543 ? 75.496  86.724  61.674  1.00 71.05  ? 543 PHE A CZ    1 
ATOM   3782 N N     . ILE A 1 544 ? 73.836  81.706  56.655  1.00 66.37  ? 544 ILE A N     1 
ATOM   3783 C CA    . ILE A 1 544 ? 73.744  81.062  55.350  1.00 60.89  ? 544 ILE A CA    1 
ATOM   3784 C C     . ILE A 1 544 ? 72.304  80.689  55.035  1.00 64.98  ? 544 ILE A C     1 
ATOM   3785 O O     . ILE A 1 544 ? 71.803  80.964  53.940  1.00 71.80  ? 544 ILE A O     1 
ATOM   3786 C CB    . ILE A 1 544 ? 74.664  79.832  55.296  1.00 59.58  ? 544 ILE A CB    1 
ATOM   3787 C CG1   . ILE A 1 544 ? 76.094  80.251  54.982  1.00 58.12  ? 544 ILE A CG1   1 
ATOM   3788 C CG2   . ILE A 1 544 ? 74.174  78.849  54.256  1.00 67.85  ? 544 ILE A CG2   1 
ATOM   3789 C CD1   . ILE A 1 544 ? 77.077  79.133  55.126  1.00 61.50  ? 544 ILE A CD1   1 
ATOM   3790 N N     . GLN A 1 545 ? 71.615  80.049  55.981  1.00 65.62  ? 545 GLN A N     1 
ATOM   3791 C CA    . GLN A 1 545 ? 70.229  79.694  55.702  1.00 68.58  ? 545 GLN A CA    1 
ATOM   3792 C C     . GLN A 1 545 ? 69.315  80.910  55.731  1.00 74.06  ? 545 GLN A C     1 
ATOM   3793 O O     . GLN A 1 545 ? 68.279  80.897  55.062  1.00 82.79  ? 545 GLN A O     1 
ATOM   3794 C CB    . GLN A 1 545 ? 69.713  78.612  56.655  1.00 62.73  ? 545 GLN A CB    1 
ATOM   3795 C CG    . GLN A 1 545 ? 70.069  78.768  58.110  1.00 68.34  ? 545 GLN A CG    1 
ATOM   3796 C CD    . GLN A 1 545 ? 69.965  77.454  58.861  1.00 63.52  ? 545 GLN A CD    1 
ATOM   3797 O OE1   . GLN A 1 545 ? 68.906  77.105  59.383  1.00 64.65  ? 545 GLN A OE1   1 
ATOM   3798 N NE2   . GLN A 1 545 ? 71.064  76.712  58.907  1.00 59.57  ? 545 GLN A NE2   1 
ATOM   3799 N N     . GLU A 1 546 ? 69.689  81.979  56.440  1.00 69.48  ? 546 GLU A N     1 
ATOM   3800 C CA    . GLU A 1 546 ? 68.948  83.229  56.307  1.00 72.31  ? 546 GLU A CA    1 
ATOM   3801 C C     . GLU A 1 546 ? 69.045  83.771  54.884  1.00 80.99  ? 546 GLU A C     1 
ATOM   3802 O O     . GLU A 1 546 ? 68.042  84.185  54.290  1.00 85.57  ? 546 GLU A O     1 
ATOM   3803 C CB    . GLU A 1 546 ? 69.469  84.254  57.313  1.00 75.73  ? 546 GLU A CB    1 
ATOM   3804 C CG    . GLU A 1 546 ? 68.662  85.540  57.381  1.00 86.07  ? 546 GLU A CG    1 
ATOM   3805 C CD    . GLU A 1 546 ? 67.202  85.303  57.696  1.00 89.74  ? 546 GLU A CD    1 
ATOM   3806 O OE1   . GLU A 1 546 ? 66.425  85.021  56.760  1.00 90.28  ? 546 GLU A OE1   1 
ATOM   3807 O OE2   . GLU A 1 546 ? 66.831  85.399  58.885  1.00 85.73  ? 546 GLU A OE2   1 
ATOM   3808 N N     . ARG A 1 547 ? 70.253  83.760  54.316  1.00 80.84  ? 547 ARG A N     1 
ATOM   3809 C CA    . ARG A 1 547 ? 70.433  84.224  52.943  1.00 81.61  ? 547 ARG A CA    1 
ATOM   3810 C C     . ARG A 1 547 ? 69.731  83.303  51.953  1.00 83.72  ? 547 ARG A C     1 
ATOM   3811 O O     . ARG A 1 547 ? 69.180  83.764  50.947  1.00 89.70  ? 547 ARG A O     1 
ATOM   3812 C CB    . ARG A 1 547 ? 71.922  84.332  52.613  1.00 77.21  ? 547 ARG A CB    1 
ATOM   3813 C CG    . ARG A 1 547 ? 72.692  85.280  53.519  1.00 78.02  ? 547 ARG A CG    1 
ATOM   3814 C CD    . ARG A 1 547 ? 72.299  86.728  53.288  1.00 83.27  ? 547 ARG A CD    1 
ATOM   3815 N NE    . ARG A 1 547 ? 73.317  87.460  52.545  1.00 86.33  ? 547 ARG A NE    1 
ATOM   3816 C CZ    . ARG A 1 547 ? 73.398  88.782  52.491  1.00 86.98  ? 547 ARG A CZ    1 
ATOM   3817 N NH1   . ARG A 1 547 ? 72.529  89.554  53.124  1.00 89.26  ? 547 ARG A NH1   1 
ATOM   3818 N NH2   . ARG A 1 547 ? 74.374  89.345  51.785  1.00 85.48  ? 547 ARG A NH2   1 
ATOM   3819 N N     . ALA A 1 548 ? 69.750  81.995  52.216  1.00 79.97  ? 548 ALA A N     1 
ATOM   3820 C CA    . ALA A 1 548 ? 69.026  81.055  51.368  1.00 81.76  ? 548 ALA A CA    1 
ATOM   3821 C C     . ALA A 1 548 ? 67.530  81.333  51.397  1.00 87.59  ? 548 ALA A C     1 
ATOM   3822 O O     . ALA A 1 548 ? 66.866  81.310  50.354  1.00 94.31  ? 548 ALA A O     1 
ATOM   3823 C CB    . ALA A 1 548 ? 69.311  79.621  51.811  1.00 82.50  ? 548 ALA A CB    1 
ATOM   3824 N N     . TRP A 1 549 ? 66.982  81.597  52.585  1.00 84.55  ? 549 TRP A N     1 
ATOM   3825 C CA    . TRP A 1 549 ? 65.573  81.952  52.694  1.00 87.19  ? 549 TRP A CA    1 
ATOM   3826 C C     . TRP A 1 549 ? 65.273  83.241  51.942  1.00 91.64  ? 549 TRP A C     1 
ATOM   3827 O O     . TRP A 1 549 ? 64.237  83.355  51.278  1.00 96.91  ? 549 TRP A O     1 
ATOM   3828 C CB    . TRP A 1 549 ? 65.187  82.090  54.165  1.00 85.43  ? 549 TRP A CB    1 
ATOM   3829 C CG    . TRP A 1 549 ? 63.736  82.352  54.386  1.00 85.70  ? 549 TRP A CG    1 
ATOM   3830 C CD1   . TRP A 1 549 ? 63.136  83.568  54.518  1.00 85.36  ? 549 TRP A CD1   1 
ATOM   3831 C CD2   . TRP A 1 549 ? 62.700  81.375  54.526  1.00 86.69  ? 549 TRP A CD2   1 
ATOM   3832 N NE1   . TRP A 1 549 ? 61.787  83.411  54.722  1.00 87.24  ? 549 TRP A NE1   1 
ATOM   3833 C CE2   . TRP A 1 549 ? 61.494  82.073  54.732  1.00 89.03  ? 549 TRP A CE2   1 
ATOM   3834 C CE3   . TRP A 1 549 ? 62.675  79.978  54.494  1.00 89.60  ? 549 TRP A CE3   1 
ATOM   3835 C CZ2   . TRP A 1 549 ? 60.275  81.421  54.903  1.00 92.21  ? 549 TRP A CZ2   1 
ATOM   3836 C CZ3   . TRP A 1 549 ? 61.464  79.333  54.664  1.00 91.69  ? 549 TRP A CZ3   1 
ATOM   3837 C CH2   . TRP A 1 549 ? 60.281  80.054  54.866  1.00 93.03  ? 549 TRP A CH2   1 
ATOM   3838 N N     . LEU A 1 550 ? 66.168  84.227  52.041  1.00 88.59  ? 550 LEU A N     1 
ATOM   3839 C CA    . LEU A 1 550 ? 65.967  85.477  51.315  1.00 94.17  ? 550 LEU A CA    1 
ATOM   3840 C C     . LEU A 1 550 ? 65.962  85.247  49.808  1.00 100.36 ? 550 LEU A C     1 
ATOM   3841 O O     . LEU A 1 550 ? 65.129  85.813  49.090  1.00 103.79 ? 550 LEU A O     1 
ATOM   3842 C CB    . LEU A 1 550 ? 67.047  86.488  51.698  1.00 91.26  ? 550 LEU A CB    1 
ATOM   3843 C CG    . LEU A 1 550 ? 66.998  87.043  53.122  1.00 91.33  ? 550 LEU A CG    1 
ATOM   3844 C CD1   . LEU A 1 550 ? 68.386  87.467  53.575  1.00 85.42  ? 550 LEU A CD1   1 
ATOM   3845 C CD2   . LEU A 1 550 ? 66.021  88.204  53.213  1.00 96.55  ? 550 LEU A CD2   1 
ATOM   3846 N N     . ARG A 1 551 ? 66.887  84.422  49.312  1.00 99.96  ? 551 ARG A N     1 
ATOM   3847 C CA    . ARG A 1 551 ? 66.928  84.131  47.881  1.00 99.25  ? 551 ARG A CA    1 
ATOM   3848 C C     . ARG A 1 551 ? 65.676  83.390  47.430  1.00 97.53  ? 551 ARG A C     1 
ATOM   3849 O O     . ARG A 1 551 ? 65.090  83.720  46.393  1.00 102.13 ? 551 ARG A O     1 
ATOM   3850 C CB    . ARG A 1 551 ? 68.176  83.320  47.539  1.00 98.21  ? 551 ARG A CB    1 
ATOM   3851 C CG    . ARG A 1 551 ? 69.461  84.123  47.532  1.00 99.18  ? 551 ARG A CG    1 
ATOM   3852 C CD    . ARG A 1 551 ? 70.668  83.211  47.626  1.00 96.72  ? 551 ARG A CD    1 
ATOM   3853 N NE    . ARG A 1 551 ? 70.615  82.147  46.631  1.00 98.42  ? 551 ARG A NE    1 
ATOM   3854 C CZ    . ARG A 1 551 ? 70.962  82.291  45.360  1.00 100.38 ? 551 ARG A CZ    1 
ATOM   3855 N NH1   . ARG A 1 551 ? 71.403  83.447  44.891  1.00 101.69 ? 551 ARG A NH1   1 
ATOM   3856 N NH2   . ARG A 1 551 ? 70.866  81.249  44.539  1.00 98.78  ? 551 ARG A NH2   1 
ATOM   3857 N N     . GLU A 1 552 ? 65.250  82.385  48.196  1.00 93.93  ? 552 GLU A N     1 
ATOM   3858 C CA    . GLU A 1 552 ? 64.058  81.627  47.841  1.00 96.29  ? 552 GLU A CA    1 
ATOM   3859 C C     . GLU A 1 552 ? 62.775  82.426  48.023  1.00 98.30  ? 552 GLU A C     1 
ATOM   3860 O O     . GLU A 1 552 ? 61.733  82.014  47.504  1.00 101.95 ? 552 GLU A O     1 
ATOM   3861 C CB    . GLU A 1 552 ? 63.990  80.340  48.664  1.00 95.80  ? 552 GLU A CB    1 
ATOM   3862 C CG    . GLU A 1 552 ? 65.163  79.400  48.436  1.00 95.61  ? 552 GLU A CG    1 
ATOM   3863 C CD    . GLU A 1 552 ? 65.286  78.346  49.519  1.00 94.67  ? 552 GLU A CD    1 
ATOM   3864 O OE1   . GLU A 1 552 ? 64.372  78.252  50.365  1.00 99.99  ? 552 GLU A OE1   1 
ATOM   3865 O OE2   . GLU A 1 552 ? 66.296  77.612  49.524  1.00 90.98  ? 552 GLU A OE2   1 
ATOM   3866 N N     . GLN A 1 553 ? 62.822  83.546  48.739  1.00 98.11  ? 553 GLN A N     1 
ATOM   3867 C CA    . GLN A 1 553 ? 61.654  84.394  48.929  1.00 101.60 ? 553 GLN A CA    1 
ATOM   3868 C C     . GLN A 1 553 ? 61.451  85.384  47.790  1.00 104.63 ? 553 GLN A C     1 
ATOM   3869 O O     . GLN A 1 553 ? 60.437  86.089  47.775  1.00 108.02 ? 553 GLN A O     1 
ATOM   3870 C CB    . GLN A 1 553 ? 61.763  85.150  50.258  1.00 98.65  ? 553 GLN A CB    1 
ATOM   3871 C CG    . GLN A 1 553 ? 60.435  85.370  50.967  1.00 97.32  ? 553 GLN A CG    1 
ATOM   3872 C CD    . GLN A 1 553 ? 59.870  84.099  51.577  1.00 99.14  ? 553 GLN A CD    1 
ATOM   3873 O OE1   . GLN A 1 553 ? 60.494  83.038  51.526  1.00 96.65  ? 553 GLN A OE1   1 
ATOM   3874 N NE2   . GLN A 1 553 ? 58.682  84.203  52.159  1.00 102.74 ? 553 GLN A NE2   1 
ATOM   3875 N N     . GLY A 1 554 ? 62.381  85.453  46.841  1.00 102.80 ? 554 GLY A N     1 
ATOM   3876 C CA    . GLY A 1 554 ? 62.239  86.344  45.707  1.00 103.71 ? 554 GLY A CA    1 
ATOM   3877 C C     . GLY A 1 554 ? 63.256  87.466  45.681  1.00 109.13 ? 554 GLY A C     1 
ATOM   3878 O O     . GLY A 1 554 ? 63.765  87.826  44.615  1.00 112.09 ? 554 GLY A O     1 
ATOM   3879 N N     . LYS A 1 555 ? 63.559  88.028  46.848  1.00 111.02 ? 555 LYS A N     1 
ATOM   3880 C CA    . LYS A 1 555 ? 64.512  89.126  46.925  1.00 111.49 ? 555 LYS A CA    1 
ATOM   3881 C C     . LYS A 1 555 ? 65.916  88.644  46.580  1.00 112.78 ? 555 LYS A C     1 
ATOM   3882 O O     . LYS A 1 555 ? 66.350  87.575  47.017  1.00 112.51 ? 555 LYS A O     1 
ATOM   3883 C CB    . LYS A 1 555 ? 64.495  89.744  48.322  1.00 106.04 ? 555 LYS A CB    1 
ATOM   3884 C CG    . LYS A 1 555 ? 63.098  89.974  48.877  1.00 107.44 ? 555 LYS A CG    1 
ATOM   3885 C CD    . LYS A 1 555 ? 63.134  90.835  50.129  1.00 109.84 ? 555 LYS A CD    1 
ATOM   3886 C CE    . LYS A 1 555 ? 63.491  92.274  49.798  1.00 105.96 ? 555 LYS A CE    1 
ATOM   3887 N NZ    . LYS A 1 555 ? 62.741  93.240  50.646  1.00 103.50 ? 555 LYS A NZ    1 
ATOM   3888 N N     . GLU A 1 556 ? 66.627  89.442  45.788  1.00 112.01 ? 556 GLU A N     1 
ATOM   3889 C CA    . GLU A 1 556 ? 67.985  89.092  45.398  1.00 109.75 ? 556 GLU A CA    1 
ATOM   3890 C C     . GLU A 1 556 ? 68.954  89.327  46.552  1.00 106.58 ? 556 GLU A C     1 
ATOM   3891 O O     . GLU A 1 556 ? 68.747  90.196  47.403  1.00 105.27 ? 556 GLU A O     1 
ATOM   3892 C CB    . GLU A 1 556 ? 68.413  89.900  44.173  1.00 109.14 ? 556 GLU A CB    1 
ATOM   3893 C CG    . GLU A 1 556 ? 68.199  91.396  44.307  1.00 110.48 ? 556 GLU A CG    1 
ATOM   3894 C CD    . GLU A 1 556 ? 69.444  92.123  44.766  1.00 108.30 ? 556 GLU A CD    1 
ATOM   3895 O OE1   . GLU A 1 556 ? 70.544  91.538  44.675  1.00 107.11 ? 556 GLU A OE1   1 
ATOM   3896 O OE2   . GLU A 1 556 ? 69.323  93.280  45.217  1.00 108.59 ? 556 GLU A OE2   1 
ATOM   3897 N N     . VAL A 1 557 ? 70.023  88.535  46.573  1.00 105.67 ? 557 VAL A N     1 
ATOM   3898 C CA    . VAL A 1 557 ? 71.011  88.561  47.644  1.00 100.58 ? 557 VAL A CA    1 
ATOM   3899 C C     . VAL A 1 557 ? 72.394  88.670  47.019  1.00 97.57  ? 557 VAL A C     1 
ATOM   3900 O O     . VAL A 1 557 ? 72.699  87.965  46.050  1.00 100.10 ? 557 VAL A O     1 
ATOM   3901 C CB    . VAL A 1 557 ? 70.906  87.309  48.538  1.00 95.08  ? 557 VAL A CB    1 
ATOM   3902 C CG1   . VAL A 1 557 ? 72.246  86.971  49.172  1.00 92.29  ? 557 VAL A CG1   1 
ATOM   3903 C CG2   . VAL A 1 557 ? 69.844  87.513  49.604  1.00 94.18  ? 557 VAL A CG2   1 
ATOM   3904 N N     . GLY A 1 558 ? 73.224  89.550  47.567  1.00 92.32  ? 558 GLY A N     1 
ATOM   3905 C CA    . GLY A 1 558 ? 74.563  89.750  47.060  1.00 86.49  ? 558 GLY A CA    1 
ATOM   3906 C C     . GLY A 1 558 ? 75.461  88.550  47.316  1.00 83.38  ? 558 GLY A C     1 
ATOM   3907 O O     . GLY A 1 558 ? 75.029  87.463  47.701  1.00 78.94  ? 558 GLY A O     1 
ATOM   3908 N N     . GLU A 1 559 ? 76.751  88.769  47.083  1.00 83.29  ? 559 GLU A N     1 
ATOM   3909 C CA    . GLU A 1 559 ? 77.730  87.705  47.247  1.00 83.56  ? 559 GLU A CA    1 
ATOM   3910 C C     . GLU A 1 559 ? 77.836  87.290  48.709  1.00 84.33  ? 559 GLU A C     1 
ATOM   3911 O O     . GLU A 1 559 ? 77.845  88.130  49.612  1.00 86.07  ? 559 GLU A O     1 
ATOM   3912 C CB    . GLU A 1 559 ? 79.096  88.158  46.732  1.00 84.97  ? 559 GLU A CB    1 
ATOM   3913 C CG    . GLU A 1 559 ? 79.029  89.105  45.546  1.00 89.98  ? 559 GLU A CG    1 
ATOM   3914 C CD    . GLU A 1 559 ? 78.809  88.382  44.232  1.00 100.80 ? 559 GLU A CD    1 
ATOM   3915 O OE1   . GLU A 1 559 ? 78.990  87.147  44.192  1.00 98.26  ? 559 GLU A OE1   1 
ATOM   3916 O OE2   . GLU A 1 559 ? 78.454  89.050  43.238  1.00 106.20 ? 559 GLU A OE2   1 
ATOM   3917 N N     . THR A 1 560 ? 77.914  85.982  48.937  1.00 83.50  ? 560 THR A N     1 
ATOM   3918 C CA    . THR A 1 560 ? 78.092  85.421  50.271  1.00 79.91  ? 560 THR A CA    1 
ATOM   3919 C C     . THR A 1 560 ? 79.296  84.493  50.234  1.00 79.25  ? 560 THR A C     1 
ATOM   3920 O O     . THR A 1 560 ? 79.334  83.558  49.429  1.00 90.34  ? 560 THR A O     1 
ATOM   3921 C CB    . THR A 1 560 ? 76.842  84.664  50.731  1.00 80.83  ? 560 THR A CB    1 
ATOM   3922 O OG1   . THR A 1 560 ? 75.808  85.600  51.060  1.00 79.82  ? 560 THR A OG1   1 
ATOM   3923 C CG2   . THR A 1 560 ? 77.153  83.816  51.952  1.00 72.01  ? 560 THR A CG2   1 
ATOM   3924 N N     . LEU A 1 561 ? 80.271  84.749  51.098  1.00 68.70  ? 561 LEU A N     1 
ATOM   3925 C CA    . LEU A 1 561 ? 81.522  84.007  51.103  1.00 70.63  ? 561 LEU A CA    1 
ATOM   3926 C C     . LEU A 1 561 ? 81.716  83.314  52.444  1.00 72.59  ? 561 LEU A C     1 
ATOM   3927 O O     . LEU A 1 561 ? 81.474  83.905  53.500  1.00 75.33  ? 561 LEU A O     1 
ATOM   3928 C CB    . LEU A 1 561 ? 82.709  84.932  50.820  1.00 67.08  ? 561 LEU A CB    1 
ATOM   3929 C CG    . LEU A 1 561 ? 82.937  85.348  49.365  1.00 66.93  ? 561 LEU A CG    1 
ATOM   3930 C CD1   . LEU A 1 561 ? 81.999  86.476  48.961  1.00 71.09  ? 561 LEU A CD1   1 
ATOM   3931 C CD2   . LEU A 1 561 ? 84.386  85.748  49.141  1.00 73.12  ? 561 LEU A CD2   1 
ATOM   3932 N N     . LEU A 1 562 ? 82.152  82.059  52.395  1.00 75.14  ? 562 LEU A N     1 
ATOM   3933 C CA    . LEU A 1 562 ? 82.468  81.285  53.586  1.00 72.99  ? 562 LEU A CA    1 
ATOM   3934 C C     . LEU A 1 562 ? 83.946  80.929  53.545  1.00 76.56  ? 562 LEU A C     1 
ATOM   3935 O O     . LEU A 1 562 ? 84.449  80.474  52.513  1.00 83.85  ? 562 LEU A O     1 
ATOM   3936 C CB    . LEU A 1 562 ? 81.620  80.011  53.669  1.00 77.04  ? 562 LEU A CB    1 
ATOM   3937 C CG    . LEU A 1 562 ? 81.275  79.413  55.041  1.00 73.60  ? 562 LEU A CG    1 
ATOM   3938 C CD1   . LEU A 1 562 ? 80.429  78.165  54.870  1.00 81.99  ? 562 LEU A CD1   1 
ATOM   3939 C CD2   . LEU A 1 562 ? 82.490  79.106  55.894  1.00 72.01  ? 562 LEU A CD2   1 
ATOM   3940 N N     . TYR A 1 563 ? 84.636  81.136  54.663  1.00 72.22  ? 563 TYR A N     1 
ATOM   3941 C CA    . TYR A 1 563 ? 86.046  80.777  54.799  1.00 76.83  ? 563 TYR A CA    1 
ATOM   3942 C C     . TYR A 1 563 ? 86.178  79.939  56.068  1.00 78.26  ? 563 TYR A C     1 
ATOM   3943 O O     . TYR A 1 563 ? 86.232  80.480  57.175  1.00 79.73  ? 563 TYR A O     1 
ATOM   3944 C CB    . TYR A 1 563 ? 86.924  82.021  54.843  1.00 80.89  ? 563 TYR A CB    1 
ATOM   3945 C CG    . TYR A 1 563 ? 87.058  82.713  53.507  1.00 83.10  ? 563 TYR A CG    1 
ATOM   3946 C CD1   . TYR A 1 563 ? 86.073  83.579  53.052  1.00 78.20  ? 563 TYR A CD1   1 
ATOM   3947 C CD2   . TYR A 1 563 ? 88.166  82.499  52.698  1.00 88.58  ? 563 TYR A CD2   1 
ATOM   3948 C CE1   . TYR A 1 563 ? 86.188  84.212  51.832  1.00 80.78  ? 563 TYR A CE1   1 
ATOM   3949 C CE2   . TYR A 1 563 ? 88.289  83.129  51.476  1.00 90.44  ? 563 TYR A CE2   1 
ATOM   3950 C CZ    . TYR A 1 563 ? 87.297  83.984  51.049  1.00 86.04  ? 563 TYR A CZ    1 
ATOM   3951 O OH    . TYR A 1 563 ? 87.412  84.615  49.833  1.00 87.93  ? 563 TYR A OH    1 
ATOM   3952 N N     . TYR A 1 564 ? 86.228  78.621  55.902  1.00 83.17  ? 564 TYR A N     1 
ATOM   3953 C CA    . TYR A 1 564 ? 86.168  77.679  57.008  1.00 85.13  ? 564 TYR A CA    1 
ATOM   3954 C C     . TYR A 1 564 ? 87.455  76.865  57.065  1.00 92.24  ? 564 TYR A C     1 
ATOM   3955 O O     . TYR A 1 564 ? 88.161  76.709  56.066  1.00 98.86  ? 564 TYR A O     1 
ATOM   3956 C CB    . TYR A 1 564 ? 84.933  76.769  56.866  1.00 82.71  ? 564 TYR A CB    1 
ATOM   3957 C CG    . TYR A 1 564 ? 84.878  75.555  57.768  1.00 87.87  ? 564 TYR A CG    1 
ATOM   3958 C CD1   . TYR A 1 564 ? 85.516  74.372  57.421  1.00 96.61  ? 564 TYR A CD1   1 
ATOM   3959 C CD2   . TYR A 1 564 ? 84.179  75.593  58.966  1.00 87.25  ? 564 TYR A CD2   1 
ATOM   3960 C CE1   . TYR A 1 564 ? 85.460  73.265  58.240  1.00 99.67  ? 564 TYR A CE1   1 
ATOM   3961 C CE2   . TYR A 1 564 ? 84.120  74.490  59.794  1.00 89.76  ? 564 TYR A CE2   1 
ATOM   3962 C CZ    . TYR A 1 564 ? 84.763  73.329  59.426  1.00 96.44  ? 564 TYR A CZ    1 
ATOM   3963 O OH    . TYR A 1 564 ? 84.708  72.226  60.246  1.00 101.34 ? 564 TYR A OH    1 
ATOM   3964 N N     . GLY A 1 565 ? 87.764  76.364  58.252  1.00 90.78  ? 565 GLY A N     1 
ATOM   3965 C CA    . GLY A 1 565 ? 88.954  75.556  58.444  1.00 97.69  ? 565 GLY A CA    1 
ATOM   3966 C C     . GLY A 1 565 ? 88.646  74.321  59.262  1.00 100.18 ? 565 GLY A C     1 
ATOM   3967 O O     . GLY A 1 565 ? 87.771  74.324  60.130  1.00 98.56  ? 565 GLY A O     1 
ATOM   3968 N N     . CYS A 1 566 ? 89.386  73.255  58.971  1.00 108.03 ? 566 CYS A N     1 
ATOM   3969 C CA    . CYS A 1 566 ? 89.247  71.991  59.683  1.00 111.39 ? 566 CYS A CA    1 
ATOM   3970 C C     . CYS A 1 566 ? 90.528  71.194  59.495  1.00 118.89 ? 566 CYS A C     1 
ATOM   3971 O O     . CYS A 1 566 ? 91.364  71.517  58.648  1.00 123.68 ? 566 CYS A O     1 
ATOM   3972 C CB    . CYS A 1 566 ? 88.029  71.202  59.196  1.00 111.70 ? 566 CYS A CB    1 
ATOM   3973 S SG    . CYS A 1 566 ? 88.000  70.898  57.418  1.00 125.32 ? 566 CYS A SG    1 
ATOM   3974 N N     . ARG A 1 567 ? 90.673  70.139  60.297  1.00 118.23 ? 567 ARG A N     1 
ATOM   3975 C CA    . ARG A 1 567 ? 91.887  69.331  60.244  1.00 125.34 ? 567 ARG A CA    1 
ATOM   3976 C C     . ARG A 1 567 ? 91.918  68.457  58.995  1.00 130.67 ? 567 ARG A C     1 
ATOM   3977 O O     . ARG A 1 567 ? 92.807  68.596  58.148  1.00 134.31 ? 567 ARG A O     1 
ATOM   3978 C CB    . ARG A 1 567 ? 92.001  68.473  61.508  1.00 127.04 ? 567 ARG A CB    1 
ATOM   3979 C CG    . ARG A 1 567 ? 91.969  69.272  62.799  1.00 131.88 ? 567 ARG A CG    1 
ATOM   3980 C CD    . ARG A 1 567 ? 92.668  68.532  63.926  1.00 137.79 ? 567 ARG A CD    1 
ATOM   3981 N NE    . ARG A 1 567 ? 92.350  69.104  65.229  1.00 138.13 ? 567 ARG A NE    1 
ATOM   3982 C CZ    . ARG A 1 567 ? 92.361  68.425  66.368  1.00 135.72 ? 567 ARG A CZ    1 
ATOM   3983 N NH1   . ARG A 1 567 ? 92.672  67.139  66.403  1.00 134.19 ? 567 ARG A NH1   1 
ATOM   3984 N NH2   . ARG A 1 567 ? 92.052  69.051  67.499  1.00 131.21 ? 567 ARG A NH2   1 
ATOM   3985 N N     . ARG A 1 568 ? 90.956  67.546  58.867  1.00 129.82 ? 568 ARG A N     1 
ATOM   3986 C CA    . ARG A 1 568 ? 90.848  66.677  57.705  1.00 129.00 ? 568 ARG A CA    1 
ATOM   3987 C C     . ARG A 1 568 ? 89.398  66.618  57.247  1.00 125.48 ? 568 ARG A C     1 
ATOM   3988 O O     . ARG A 1 568 ? 88.472  66.826  58.035  1.00 121.62 ? 568 ARG A O     1 
ATOM   3989 C CB    . ARG A 1 568 ? 91.355  65.254  57.997  1.00 131.56 ? 568 ARG A CB    1 
ATOM   3990 C CG    . ARG A 1 568 ? 92.395  65.156  59.103  1.00 132.59 ? 568 ARG A CG    1 
ATOM   3991 C CD    . ARG A 1 568 ? 92.811  63.712  59.340  1.00 135.09 ? 568 ARG A CD    1 
ATOM   3992 N NE    . ARG A 1 568 ? 93.627  63.187  58.251  1.00 138.90 ? 568 ARG A NE    1 
ATOM   3993 C CZ    . ARG A 1 568 ? 94.899  63.502  58.044  1.00 138.16 ? 568 ARG A CZ    1 
ATOM   3994 N NH1   . ARG A 1 568 ? 95.546  64.330  58.847  1.00 138.99 ? 568 ARG A NH1   1 
ATOM   3995 N NH2   . ARG A 1 568 ? 95.538  62.969  57.007  1.00 134.09 ? 568 ARG A NH2   1 
ATOM   3996 N N     . SER A 1 569 ? 89.211  66.327  55.957  1.00 126.39 ? 569 SER A N     1 
ATOM   3997 C CA    . SER A 1 569 ? 87.862  66.241  55.408  1.00 125.15 ? 569 SER A CA    1 
ATOM   3998 C C     . SER A 1 569 ? 87.103  65.042  55.959  1.00 129.29 ? 569 SER A C     1 
ATOM   3999 O O     . SER A 1 569 ? 85.873  65.084  56.065  1.00 129.15 ? 569 SER A O     1 
ATOM   4000 C CB    . SER A 1 569 ? 87.919  66.173  53.882  1.00 122.25 ? 569 SER A CB    1 
ATOM   4001 O OG    . SER A 1 569 ? 86.617  66.122  53.326  1.00 122.26 ? 569 SER A OG    1 
ATOM   4002 N N     . ASP A 1 570 ? 87.810  63.970  56.311  1.00 132.86 ? 570 ASP A N     1 
ATOM   4003 C CA    . ASP A 1 570 ? 87.195  62.766  56.850  1.00 128.81 ? 570 ASP A CA    1 
ATOM   4004 C C     . ASP A 1 570 ? 87.277  62.692  58.369  1.00 125.44 ? 570 ASP A C     1 
ATOM   4005 O O     . ASP A 1 570 ? 86.945  61.652  58.946  1.00 119.94 ? 570 ASP A O     1 
ATOM   4006 C CB    . ASP A 1 570 ? 87.842  61.526  56.231  1.00 132.32 ? 570 ASP A CB    1 
ATOM   4007 C CG    . ASP A 1 570 ? 89.354  61.533  56.356  1.00 136.31 ? 570 ASP A CG    1 
ATOM   4008 O OD1   . ASP A 1 570 ? 89.906  62.521  56.884  1.00 133.79 ? 570 ASP A OD1   1 
ATOM   4009 O OD2   . ASP A 1 570 ? 89.991  60.549  55.924  1.00 141.12 ? 570 ASP A OD2   1 
ATOM   4010 N N     . GLU A 1 571 ? 87.711  63.766  59.028  1.00 126.55 ? 571 GLU A N     1 
ATOM   4011 C CA    . GLU A 1 571 ? 87.900  63.770  60.472  1.00 121.98 ? 571 GLU A CA    1 
ATOM   4012 C C     . GLU A 1 571 ? 86.929  64.705  61.182  1.00 112.62 ? 571 GLU A C     1 
ATOM   4013 O O     . GLU A 1 571 ? 86.211  64.277  62.089  1.00 106.07 ? 571 GLU A O     1 
ATOM   4014 C CB    . GLU A 1 571 ? 89.347  64.156  60.803  1.00 124.32 ? 571 GLU A CB    1 
ATOM   4015 C CG    . GLU A 1 571 ? 89.662  64.200  62.284  1.00 125.16 ? 571 GLU A CG    1 
ATOM   4016 C CD    . GLU A 1 571 ? 90.204  62.885  62.801  1.00 128.90 ? 571 GLU A CD    1 
ATOM   4017 O OE1   . GLU A 1 571 ? 90.214  61.901  62.032  1.00 128.91 ? 571 GLU A OE1   1 
ATOM   4018 O OE2   . GLU A 1 571 ? 90.625  62.837  63.974  1.00 129.55 ? 571 GLU A OE2   1 
ATOM   4019 N N     . ASP A 1 572 ? 86.887  65.984  60.792  1.00 118.86 ? 572 ASP A N     1 
ATOM   4020 C CA    . ASP A 1 572 ? 86.054  66.951  61.498  1.00 118.12 ? 572 ASP A CA    1 
ATOM   4021 C C     . ASP A 1 572 ? 85.383  67.950  60.560  1.00 112.83 ? 572 ASP A C     1 
ATOM   4022 O O     . ASP A 1 572 ? 85.039  69.056  60.995  1.00 108.03 ? 572 ASP A O     1 
ATOM   4023 C CB    . ASP A 1 572 ? 86.878  67.706  62.545  1.00 119.49 ? 572 ASP A CB    1 
ATOM   4024 C CG    . ASP A 1 572 ? 88.127  68.335  61.960  1.00 128.34 ? 572 ASP A CG    1 
ATOM   4025 O OD1   . ASP A 1 572 ? 88.598  67.856  60.907  1.00 131.98 ? 572 ASP A OD1   1 
ATOM   4026 O OD2   . ASP A 1 572 ? 88.639  69.308  62.554  1.00 129.67 ? 572 ASP A OD2   1 
ATOM   4027 N N     . TYR A 1 573 ? 85.190  67.598  59.292  1.00 111.03 ? 573 TYR A N     1 
ATOM   4028 C CA    . TYR A 1 573 ? 84.543  68.496  58.341  1.00 108.07 ? 573 TYR A CA    1 
ATOM   4029 C C     . TYR A 1 573 ? 83.076  68.641  58.726  1.00 102.77 ? 573 TYR A C     1 
ATOM   4030 O O     . TYR A 1 573 ? 82.320  67.666  58.698  1.00 103.72 ? 573 TYR A O     1 
ATOM   4031 C CB    . TYR A 1 573 ? 84.698  67.950  56.924  1.00 113.33 ? 573 TYR A CB    1 
ATOM   4032 C CG    . TYR A 1 573 ? 84.380  68.930  55.814  1.00 109.81 ? 573 TYR A CG    1 
ATOM   4033 C CD1   . TYR A 1 573 ? 83.102  69.447  55.654  1.00 104.70 ? 573 TYR A CD1   1 
ATOM   4034 C CD2   . TYR A 1 573 ? 85.363  69.329  54.919  1.00 111.76 ? 573 TYR A CD2   1 
ATOM   4035 C CE1   . TYR A 1 573 ? 82.815  70.334  54.639  1.00 107.39 ? 573 TYR A CE1   1 
ATOM   4036 C CE2   . TYR A 1 573 ? 85.084  70.217  53.901  1.00 111.91 ? 573 TYR A CE2   1 
ATOM   4037 C CZ    . TYR A 1 573 ? 83.808  70.717  53.765  1.00 113.10 ? 573 TYR A CZ    1 
ATOM   4038 O OH    . TYR A 1 573 ? 83.524  71.602  52.752  1.00 119.27 ? 573 TYR A OH    1 
ATOM   4039 N N     . LEU A 1 574 ? 82.670  69.856  59.084  1.00 96.83  ? 574 LEU A N     1 
ATOM   4040 C CA    . LEU A 1 574 ? 81.336  70.081  59.624  1.00 93.82  ? 574 LEU A CA    1 
ATOM   4041 C C     . LEU A 1 574 ? 80.322  70.308  58.510  1.00 93.66  ? 574 LEU A C     1 
ATOM   4042 O O     . LEU A 1 574 ? 80.500  71.189  57.663  1.00 98.69  ? 574 LEU A O     1 
ATOM   4043 C CB    . LEU A 1 574 ? 81.346  71.273  60.578  1.00 92.12  ? 574 LEU A CB    1 
ATOM   4044 C CG    . LEU A 1 574 ? 81.969  71.016  61.948  1.00 86.33  ? 574 LEU A CG    1 
ATOM   4045 C CD1   . LEU A 1 574 ? 82.117  72.312  62.724  1.00 81.40  ? 574 LEU A CD1   1 
ATOM   4046 C CD2   . LEU A 1 574 ? 81.120  70.023  62.718  1.00 79.33  ? 574 LEU A CD2   1 
ATOM   4047 N N     . TYR A 1 575 ? 79.253  69.516  58.531  1.00 93.15  ? 575 TYR A N     1 
ATOM   4048 C CA    . TYR A 1 575 ? 78.122  69.629  57.610  1.00 98.94  ? 575 TYR A CA    1 
ATOM   4049 C C     . TYR A 1 575 ? 78.582  69.634  56.150  1.00 107.56 ? 575 TYR A C     1 
ATOM   4050 O O     . TYR A 1 575 ? 78.420  70.610  55.420  1.00 107.97 ? 575 TYR A O     1 
ATOM   4051 C CB    . TYR A 1 575 ? 77.285  70.879  57.899  1.00 91.72  ? 575 TYR A CB    1 
ATOM   4052 C CG    . TYR A 1 575 ? 77.134  71.256  59.353  1.00 89.12  ? 575 TYR A CG    1 
ATOM   4053 C CD1   . TYR A 1 575 ? 76.098  70.740  60.121  1.00 93.37  ? 575 TYR A CD1   1 
ATOM   4054 C CD2   . TYR A 1 575 ? 78.019  72.139  59.956  1.00 87.07  ? 575 TYR A CD2   1 
ATOM   4055 C CE1   . TYR A 1 575 ? 75.948  71.098  61.449  1.00 83.49  ? 575 TYR A CE1   1 
ATOM   4056 C CE2   . TYR A 1 575 ? 77.877  72.499  61.280  1.00 83.27  ? 575 TYR A CE2   1 
ATOM   4057 C CZ    . TYR A 1 575 ? 76.842  71.978  62.021  1.00 76.27  ? 575 TYR A CZ    1 
ATOM   4058 O OH    . TYR A 1 575 ? 76.703  72.334  63.342  1.00 61.86  ? 575 TYR A OH    1 
ATOM   4059 N N     . ARG A 1 576 ? 79.165  68.506  55.741  1.00 108.98 ? 576 ARG A N     1 
ATOM   4060 C CA    . ARG A 1 576 ? 79.527  68.339  54.337  1.00 107.64 ? 576 ARG A CA    1 
ATOM   4061 C C     . ARG A 1 576 ? 78.306  68.491  53.439  1.00 109.51 ? 576 ARG A C     1 
ATOM   4062 O O     . ARG A 1 576 ? 78.301  69.300  52.503  1.00 111.83 ? 576 ARG A O     1 
ATOM   4063 C CB    . ARG A 1 576 ? 80.174  66.971  54.120  1.00 112.94 ? 576 ARG A CB    1 
ATOM   4064 C CG    . ARG A 1 576 ? 81.635  67.017  53.719  1.00 116.65 ? 576 ARG A CG    1 
ATOM   4065 C CD    . ARG A 1 576 ? 82.026  65.763  52.957  1.00 121.50 ? 576 ARG A CD    1 
ATOM   4066 N NE    . ARG A 1 576 ? 82.357  64.661  53.851  1.00 122.08 ? 576 ARG A NE    1 
ATOM   4067 C CZ    . ARG A 1 576 ? 83.593  64.298  54.166  1.00 124.37 ? 576 ARG A CZ    1 
ATOM   4068 N NH1   . ARG A 1 576 ? 84.645  64.934  53.679  1.00 127.26 ? 576 ARG A NH1   1 
ATOM   4069 N NH2   . ARG A 1 576 ? 83.777  63.272  54.992  1.00 120.74 ? 576 ARG A NH2   1 
ATOM   4070 N N     . GLU A 1 577 ? 77.246  67.734  53.733  1.00 109.94 ? 577 GLU A N     1 
ATOM   4071 C CA    . GLU A 1 577 ? 76.063  67.735  52.880  1.00 114.82 ? 577 GLU A CA    1 
ATOM   4072 C C     . GLU A 1 577 ? 75.354  69.083  52.907  1.00 113.80 ? 577 GLU A C     1 
ATOM   4073 O O     . GLU A 1 577 ? 74.875  69.558  51.870  1.00 117.07 ? 577 GLU A O     1 
ATOM   4074 C CB    . GLU A 1 577 ? 75.112  66.619  53.310  1.00 113.93 ? 577 GLU A CB    1 
ATOM   4075 C CG    . GLU A 1 577 ? 75.601  65.219  52.977  1.00 119.27 ? 577 GLU A CG    1 
ATOM   4076 C CD    . GLU A 1 577 ? 75.336  64.831  51.535  1.00 124.64 ? 577 GLU A CD    1 
ATOM   4077 O OE1   . GLU A 1 577 ? 74.718  65.632  50.802  1.00 116.95 ? 577 GLU A OE1   1 
ATOM   4078 O OE2   . GLU A 1 577 ? 75.745  63.721  51.134  1.00 132.65 ? 577 GLU A OE2   1 
ATOM   4079 N N     . GLU A 1 578 ? 75.273  69.713  54.081  1.00 107.37 ? 578 GLU A N     1 
ATOM   4080 C CA    . GLU A 1 578 ? 74.541  70.970  54.194  1.00 104.83 ? 578 GLU A CA    1 
ATOM   4081 C C     . GLU A 1 578 ? 75.174  72.055  53.332  1.00 105.76 ? 578 GLU A C     1 
ATOM   4082 O O     . GLU A 1 578 ? 74.499  72.677  52.503  1.00 107.94 ? 578 GLU A O     1 
ATOM   4083 C CB    . GLU A 1 578 ? 74.474  71.410  55.656  1.00 105.96 ? 578 GLU A CB    1 
ATOM   4084 C CG    . GLU A 1 578 ? 73.384  70.724  56.465  1.00 109.67 ? 578 GLU A CG    1 
ATOM   4085 C CD    . GLU A 1 578 ? 73.804  69.362  56.984  1.00 110.49 ? 578 GLU A CD    1 
ATOM   4086 O OE1   . GLU A 1 578 ? 74.953  68.951  56.722  1.00 111.37 ? 578 GLU A OE1   1 
ATOM   4087 O OE2   . GLU A 1 578 ? 72.983  68.702  57.653  1.00 105.99 ? 578 GLU A OE2   1 
ATOM   4088 N N     . LEU A 1 579 ? 76.480  72.280  53.491  1.00 106.73 ? 579 LEU A N     1 
ATOM   4089 C CA    . LEU A 1 579 ? 77.130  73.307  52.685  1.00 108.75 ? 579 LEU A CA    1 
ATOM   4090 C C     . LEU A 1 579 ? 77.254  72.881  51.229  1.00 109.76 ? 579 LEU A C     1 
ATOM   4091 O O     . LEU A 1 579 ? 77.292  73.738  50.340  1.00 105.19 ? 579 LEU A O     1 
ATOM   4092 C CB    . LEU A 1 579 ? 78.498  73.670  53.270  1.00 108.88 ? 579 LEU A CB    1 
ATOM   4093 C CG    . LEU A 1 579 ? 79.640  72.655  53.331  1.00 111.62 ? 579 LEU A CG    1 
ATOM   4094 C CD1   . LEU A 1 579 ? 80.493  72.694  52.074  1.00 114.37 ? 579 LEU A CD1   1 
ATOM   4095 C CD2   . LEU A 1 579 ? 80.491  72.934  54.558  1.00 106.91 ? 579 LEU A CD2   1 
ATOM   4096 N N     . ALA A 1 580 ? 77.299  71.573  50.957  1.00 110.13 ? 580 ALA A N     1 
ATOM   4097 C CA    . ALA A 1 580 ? 77.273  71.116  49.572  1.00 102.32 ? 580 ALA A CA    1 
ATOM   4098 C C     . ALA A 1 580 ? 75.985  71.547  48.881  1.00 101.66 ? 580 ALA A C     1 
ATOM   4099 O O     . ALA A 1 580 ? 76.014  72.114  47.782  1.00 104.11 ? 580 ALA A O     1 
ATOM   4100 C CB    . ALA A 1 580 ? 77.436  69.597  49.518  1.00 100.66 ? 580 ALA A CB    1 
ATOM   4101 N N     . ARG A 1 581 ? 74.839  71.300  49.523  1.00 100.19 ? 581 ARG A N     1 
ATOM   4102 C CA    . ARG A 1 581 ? 73.572  71.743  48.946  1.00 100.56 ? 581 ARG A CA    1 
ATOM   4103 C C     . ARG A 1 581 ? 73.459  73.261  48.930  1.00 102.51 ? 581 ARG A C     1 
ATOM   4104 O O     . ARG A 1 581 ? 72.824  73.822  48.030  1.00 103.03 ? 581 ARG A O     1 
ATOM   4105 C CB    . ARG A 1 581 ? 72.386  71.142  49.700  1.00 102.83 ? 581 ARG A CB    1 
ATOM   4106 C CG    . ARG A 1 581 ? 72.460  69.644  49.928  1.00 111.99 ? 581 ARG A CG    1 
ATOM   4107 C CD    . ARG A 1 581 ? 71.156  69.128  50.518  1.00 119.60 ? 581 ARG A CD    1 
ATOM   4108 N NE    . ARG A 1 581 ? 70.909  69.652  51.856  1.00 126.28 ? 581 ARG A NE    1 
ATOM   4109 C CZ    . ARG A 1 581 ? 71.443  69.160  52.966  1.00 118.09 ? 581 ARG A CZ    1 
ATOM   4110 N NH1   . ARG A 1 581 ? 72.252  68.115  52.939  1.00 117.85 ? 581 ARG A NH1   1 
ATOM   4111 N NH2   . ARG A 1 581 ? 71.153  69.729  54.133  1.00 110.06 ? 581 ARG A NH2   1 
ATOM   4112 N N     . PHE A 1 582 ? 74.050  73.940  49.915  1.00 105.43 ? 582 PHE A N     1 
ATOM   4113 C CA    . PHE A 1 582 ? 74.017  75.400  49.920  1.00 102.66 ? 582 PHE A CA    1 
ATOM   4114 C C     . PHE A 1 582 ? 74.771  75.974  48.726  1.00 98.74  ? 582 PHE A C     1 
ATOM   4115 O O     . PHE A 1 582 ? 74.294  76.914  48.079  1.00 98.22  ? 582 PHE A O     1 
ATOM   4116 C CB    . PHE A 1 582 ? 74.594  75.932  51.231  1.00 99.52  ? 582 PHE A CB    1 
ATOM   4117 C CG    . PHE A 1 582 ? 73.720  75.674  52.424  1.00 97.50  ? 582 PHE A CG    1 
ATOM   4118 C CD1   . PHE A 1 582 ? 72.342  75.643  52.293  1.00 98.83  ? 582 PHE A CD1   1 
ATOM   4119 C CD2   . PHE A 1 582 ? 74.275  75.451  53.672  1.00 95.53  ? 582 PHE A CD2   1 
ATOM   4120 C CE1   . PHE A 1 582 ? 71.534  75.403  53.385  1.00 97.00  ? 582 PHE A CE1   1 
ATOM   4121 C CE2   . PHE A 1 582 ? 73.471  75.210  54.768  1.00 95.98  ? 582 PHE A CE2   1 
ATOM   4122 C CZ    . PHE A 1 582 ? 72.099  75.186  54.624  1.00 95.21  ? 582 PHE A CZ    1 
ATOM   4123 N N     . HIS A 1 583 ? 75.948  75.425  48.421  1.00 99.29  ? 583 HIS A N     1 
ATOM   4124 C CA    . HIS A 1 583 ? 76.699  75.886  47.258  1.00 98.38  ? 583 HIS A CA    1 
ATOM   4125 C C     . HIS A 1 583 ? 76.004  75.498  45.960  1.00 100.79 ? 583 HIS A C     1 
ATOM   4126 O O     . HIS A 1 583 ? 75.956  76.293  45.014  1.00 100.05 ? 583 HIS A O     1 
ATOM   4127 C CB    . HIS A 1 583 ? 78.120  75.326  47.287  1.00 98.16  ? 583 HIS A CB    1 
ATOM   4128 C CG    . HIS A 1 583 ? 79.070  76.049  46.384  1.00 97.36  ? 583 HIS A CG    1 
ATOM   4129 N ND1   . HIS A 1 583 ? 80.339  75.585  46.111  1.00 97.13  ? 583 HIS A ND1   1 
ATOM   4130 C CD2   . HIS A 1 583 ? 78.936  77.205  45.693  1.00 96.04  ? 583 HIS A CD2   1 
ATOM   4131 C CE1   . HIS A 1 583 ? 80.946  76.424  45.291  1.00 98.15  ? 583 HIS A CE1   1 
ATOM   4132 N NE2   . HIS A 1 583 ? 80.116  77.416  45.022  1.00 99.83  ? 583 HIS A NE2   1 
ATOM   4133 N N     . LYS A 1 584 ? 75.461  74.279  45.891  1.00 101.59 ? 584 LYS A N     1 
ATOM   4134 C CA    . LYS A 1 584 ? 74.806  73.829  44.669  1.00 96.53  ? 584 LYS A CA    1 
ATOM   4135 C C     . LYS A 1 584 ? 73.526  74.602  44.375  1.00 97.70  ? 584 LYS A C     1 
ATOM   4136 O O     . LYS A 1 584 ? 73.091  74.634  43.220  1.00 98.66  ? 584 LYS A O     1 
ATOM   4137 C CB    . LYS A 1 584 ? 74.509  72.330  44.753  1.00 95.37  ? 584 LYS A CB    1 
ATOM   4138 C CG    . LYS A 1 584 ? 73.099  71.988  45.206  1.00 100.91 ? 584 LYS A CG    1 
ATOM   4139 C CD    . LYS A 1 584 ? 72.836  70.495  45.105  1.00 107.46 ? 584 LYS A CD    1 
ATOM   4140 C CE    . LYS A 1 584 ? 71.795  70.047  46.118  1.00 110.44 ? 584 LYS A CE    1 
ATOM   4141 N NZ    . LYS A 1 584 ? 71.756  68.566  46.259  1.00 104.34 ? 584 LYS A NZ    1 
ATOM   4142 N N     . ASP A 1 585 ? 72.918  75.223  45.384  1.00 101.19 ? 585 ASP A N     1 
ATOM   4143 C CA    . ASP A 1 585 ? 71.704  76.005  45.199  1.00 103.99 ? 585 ASP A CA    1 
ATOM   4144 C C     . ASP A 1 585 ? 71.981  77.494  45.034  1.00 101.24 ? 585 ASP A C     1 
ATOM   4145 O O     . ASP A 1 585 ? 71.043  78.264  44.809  1.00 101.09 ? 585 ASP A O     1 
ATOM   4146 C CB    . ASP A 1 585 ? 70.750  75.782  46.377  1.00 105.10 ? 585 ASP A CB    1 
ATOM   4147 C CG    . ASP A 1 585 ? 69.296  75.728  45.950  1.00 109.98 ? 585 ASP A CG    1 
ATOM   4148 O OD1   . ASP A 1 585 ? 68.825  76.682  45.296  1.00 117.26 ? 585 ASP A OD1   1 
ATOM   4149 O OD2   . ASP A 1 585 ? 68.621  74.726  46.268  1.00 104.62 ? 585 ASP A OD2   1 
ATOM   4150 N N     . GLY A 1 586 ? 73.238  77.916  45.139  1.00 97.35  ? 586 GLY A N     1 
ATOM   4151 C CA    . GLY A 1 586 ? 73.593  79.308  44.979  1.00 94.51  ? 586 GLY A CA    1 
ATOM   4152 C C     . GLY A 1 586 ? 73.451  80.164  46.218  1.00 97.24  ? 586 GLY A C     1 
ATOM   4153 O O     . GLY A 1 586 ? 73.769  81.359  46.161  1.00 97.95  ? 586 GLY A O     1 
ATOM   4154 N N     . ALA A 1 587 ? 72.979  79.601  47.333  1.00 99.90  ? 587 ALA A N     1 
ATOM   4155 C CA    . ALA A 1 587 ? 72.876  80.375  48.567  1.00 92.93  ? 587 ALA A CA    1 
ATOM   4156 C C     . ALA A 1 587 ? 74.252  80.821  49.045  1.00 89.63  ? 587 ALA A C     1 
ATOM   4157 O O     . ALA A 1 587 ? 74.470  82.001  49.341  1.00 83.59  ? 587 ALA A O     1 
ATOM   4158 C CB    . ALA A 1 587 ? 72.170  79.554  49.643  1.00 83.85  ? 587 ALA A CB    1 
ATOM   4159 N N     . LEU A 1 588 ? 75.192  79.886  49.127  1.00 92.26  ? 588 LEU A N     1 
ATOM   4160 C CA    . LEU A 1 588 ? 76.584  80.196  49.427  1.00 86.57  ? 588 LEU A CA    1 
ATOM   4161 C C     . LEU A 1 588 ? 77.319  80.344  48.101  1.00 90.21  ? 588 LEU A C     1 
ATOM   4162 O O     . LEU A 1 588 ? 77.531  79.358  47.388  1.00 94.81  ? 588 LEU A O     1 
ATOM   4163 C CB    . LEU A 1 588 ? 77.204  79.103  50.293  1.00 83.08  ? 588 LEU A CB    1 
ATOM   4164 C CG    . LEU A 1 588 ? 78.719  79.129  50.489  1.00 80.79  ? 588 LEU A CG    1 
ATOM   4165 C CD1   . LEU A 1 588 ? 79.175  80.489  50.989  1.00 81.72  ? 588 LEU A CD1   1 
ATOM   4166 C CD2   . LEU A 1 588 ? 79.138  78.033  51.449  1.00 77.59  ? 588 LEU A CD2   1 
ATOM   4167 N N     . THR A 1 589 ? 77.697  81.579  47.763  1.00 87.59  ? 589 THR A N     1 
ATOM   4168 C CA    . THR A 1 589 ? 78.240  81.848  46.435  1.00 89.65  ? 589 THR A CA    1 
ATOM   4169 C C     . THR A 1 589 ? 79.564  81.123  46.221  1.00 90.80  ? 589 THR A C     1 
ATOM   4170 O O     . THR A 1 589 ? 79.782  80.503  45.173  1.00 95.48  ? 589 THR A O     1 
ATOM   4171 C CB    . THR A 1 589 ? 78.401  83.355  46.230  1.00 88.79  ? 589 THR A CB    1 
ATOM   4172 O OG1   . THR A 1 589 ? 77.141  84.001  46.446  1.00 90.18  ? 589 THR A OG1   1 
ATOM   4173 C CG2   . THR A 1 589 ? 78.861  83.648  44.814  1.00 91.27  ? 589 THR A CG2   1 
ATOM   4174 N N     . GLN A 1 590 ? 80.463  81.183  47.203  1.00 87.89  ? 590 GLN A N     1 
ATOM   4175 C CA    . GLN A 1 590 ? 81.722  80.446  47.141  1.00 88.33  ? 590 GLN A CA    1 
ATOM   4176 C C     . GLN A 1 590 ? 82.032  79.882  48.518  1.00 90.33  ? 590 GLN A C     1 
ATOM   4177 O O     . GLN A 1 590 ? 82.144  80.638  49.486  1.00 89.54  ? 590 GLN A O     1 
ATOM   4178 C CB    . GLN A 1 590 ? 82.888  81.327  46.670  1.00 86.84  ? 590 GLN A CB    1 
ATOM   4179 C CG    . GLN A 1 590 ? 82.605  82.221  45.478  1.00 89.26  ? 590 GLN A CG    1 
ATOM   4180 C CD    . GLN A 1 590 ? 82.084  83.581  45.888  1.00 90.57  ? 590 GLN A CD    1 
ATOM   4181 O OE1   . GLN A 1 590 ? 81.483  83.731  46.950  1.00 91.18  ? 590 GLN A OE1   1 
ATOM   4182 N NE2   . GLN A 1 590 ? 82.314  84.583  45.048  1.00 91.53  ? 590 GLN A NE2   1 
ATOM   4183 N N     . LEU A 1 591 ? 82.171  78.562  48.606  1.00 92.60  ? 591 LEU A N     1 
ATOM   4184 C CA    . LEU A 1 591 ? 82.703  77.949  49.812  1.00 90.23  ? 591 LEU A CA    1 
ATOM   4185 C C     . LEU A 1 591 ? 84.217  77.845  49.703  1.00 91.15  ? 591 LEU A C     1 
ATOM   4186 O O     . LEU A 1 591 ? 84.760  77.559  48.632  1.00 95.96  ? 591 LEU A O     1 
ATOM   4187 C CB    . LEU A 1 591 ? 82.085  76.567  50.047  1.00 97.05  ? 591 LEU A CB    1 
ATOM   4188 C CG    . LEU A 1 591 ? 82.496  75.362  49.193  1.00 108.04 ? 591 LEU A CG    1 
ATOM   4189 C CD1   . LEU A 1 591 ? 83.641  74.585  49.832  1.00 105.89 ? 591 LEU A CD1   1 
ATOM   4190 C CD2   . LEU A 1 591 ? 81.305  74.448  48.969  1.00 104.75 ? 591 LEU A CD2   1 
ATOM   4191 N N     . ASN A 1 592 ? 84.899  78.087  50.817  1.00 87.18  ? 592 ASN A N     1 
ATOM   4192 C CA    . ASN A 1 592 ? 86.356  78.030  50.863  1.00 89.21  ? 592 ASN A CA    1 
ATOM   4193 C C     . ASN A 1 592 ? 86.749  77.374  52.178  1.00 92.68  ? 592 ASN A C     1 
ATOM   4194 O O     . ASN A 1 592 ? 86.559  77.962  53.247  1.00 94.86  ? 592 ASN A O     1 
ATOM   4195 C CB    . ASN A 1 592 ? 86.968  79.424  50.733  1.00 87.46  ? 592 ASN A CB    1 
ATOM   4196 C CG    . ASN A 1 592 ? 86.700  80.053  49.380  1.00 92.02  ? 592 ASN A CG    1 
ATOM   4197 O OD1   . ASN A 1 592 ? 87.168  79.564  48.352  1.00 96.45  ? 592 ASN A OD1   1 
ATOM   4198 N ND2   . ASN A 1 592 ? 85.939  81.140  49.372  1.00 88.08  ? 592 ASN A ND2   1 
ATOM   4199 N N     . VAL A 1 593 ? 87.289  76.162  52.100  1.00 95.46  ? 593 VAL A N     1 
ATOM   4200 C CA    . VAL A 1 593 ? 87.614  75.364  53.274  1.00 95.53  ? 593 VAL A CA    1 
ATOM   4201 C C     . VAL A 1 593 ? 89.119  75.146  53.306  1.00 100.39 ? 593 VAL A C     1 
ATOM   4202 O O     . VAL A 1 593 ? 89.712  74.726  52.306  1.00 102.09 ? 593 VAL A O     1 
ATOM   4203 C CB    . VAL A 1 593 ? 86.862  74.022  53.271  1.00 98.80  ? 593 VAL A CB    1 
ATOM   4204 C CG1   . VAL A 1 593 ? 87.254  73.195  54.480  1.00 102.70 ? 593 VAL A CG1   1 
ATOM   4205 C CG2   . VAL A 1 593 ? 85.362  74.261  53.244  1.00 96.09  ? 593 VAL A CG2   1 
ATOM   4206 N N     . ALA A 1 594 ? 89.731  75.431  54.451  1.00 101.88 ? 594 ALA A N     1 
ATOM   4207 C CA    . ALA A 1 594 ? 91.177  75.333  54.628  1.00 107.55 ? 594 ALA A CA    1 
ATOM   4208 C C     . ALA A 1 594 ? 91.482  74.105  55.480  1.00 115.00 ? 594 ALA A C     1 
ATOM   4209 O O     . ALA A 1 594 ? 91.364  74.145  56.708  1.00 115.83 ? 594 ALA A O     1 
ATOM   4210 C CB    . ALA A 1 594 ? 91.734  76.602  55.264  1.00 103.22 ? 594 ALA A CB    1 
ATOM   4211 N N     . PHE A 1 595 ? 91.872  73.017  54.822  1.00 119.15 ? 595 PHE A N     1 
ATOM   4212 C CA    . PHE A 1 595 ? 92.292  71.817  55.532  1.00 122.15 ? 595 PHE A CA    1 
ATOM   4213 C C     . PHE A 1 595 ? 93.571  72.098  56.311  1.00 125.73 ? 595 PHE A C     1 
ATOM   4214 O O     . PHE A 1 595 ? 94.446  72.834  55.851  1.00 128.61 ? 595 PHE A O     1 
ATOM   4215 C CB    . PHE A 1 595 ? 92.509  70.670  54.543  1.00 124.09 ? 595 PHE A CB    1 
ATOM   4216 C CG    . PHE A 1 595 ? 91.246  70.183  53.880  1.00 125.44 ? 595 PHE A CG    1 
ATOM   4217 C CD1   . PHE A 1 595 ? 90.013  70.731  54.196  1.00 119.36 ? 595 PHE A CD1   1 
ATOM   4218 C CD2   . PHE A 1 595 ? 91.300  69.193  52.914  1.00 128.19 ? 595 PHE A CD2   1 
ATOM   4219 C CE1   . PHE A 1 595 ? 88.861  70.284  53.579  1.00 120.18 ? 595 PHE A CE1   1 
ATOM   4220 C CE2   . PHE A 1 595 ? 90.150  68.744  52.294  1.00 126.33 ? 595 PHE A CE2   1 
ATOM   4221 C CZ    . PHE A 1 595 ? 88.930  69.292  52.626  1.00 122.77 ? 595 PHE A CZ    1 
ATOM   4222 N N     . SER A 1 596 ? 93.682  71.509  57.502  1.00 124.87 ? 596 SER A N     1 
ATOM   4223 C CA    . SER A 1 596 ? 94.774  71.840  58.405  1.00 129.78 ? 596 SER A CA    1 
ATOM   4224 C C     . SER A 1 596 ? 95.773  70.714  58.628  1.00 134.97 ? 596 SER A C     1 
ATOM   4225 O O     . SER A 1 596 ? 96.853  70.974  59.169  1.00 137.89 ? 596 SER A O     1 
ATOM   4226 C CB    . SER A 1 596 ? 94.220  72.289  59.765  1.00 131.58 ? 596 SER A CB    1 
ATOM   4227 O OG    . SER A 1 596 ? 93.014  73.016  59.609  1.00 125.22 ? 596 SER A OG    1 
ATOM   4228 N N     . ARG A 1 597 ? 95.457  69.477  58.237  1.00 135.95 ? 597 ARG A N     1 
ATOM   4229 C CA    . ARG A 1 597 ? 96.350  68.357  58.507  1.00 140.84 ? 597 ARG A CA    1 
ATOM   4230 C C     . ARG A 1 597 ? 96.569  67.408  57.337  1.00 145.29 ? 597 ARG A C     1 
ATOM   4231 O O     . ARG A 1 597 ? 97.475  66.571  57.420  1.00 149.56 ? 597 ARG A O     1 
ATOM   4232 C CB    . ARG A 1 597 ? 95.840  67.539  59.704  1.00 140.34 ? 597 ARG A CB    1 
ATOM   4233 C CG    . ARG A 1 597 ? 95.841  68.294  61.022  1.00 139.38 ? 597 ARG A CG    1 
ATOM   4234 C CD    . ARG A 1 597 ? 95.827  67.343  62.206  1.00 141.19 ? 597 ARG A CD    1 
ATOM   4235 N NE    . ARG A 1 597 ? 95.941  68.053  63.475  1.00 141.87 ? 597 ARG A NE    1 
ATOM   4236 C CZ    . ARG A 1 597 ? 96.003  67.462  64.660  1.00 143.82 ? 597 ARG A CZ    1 
ATOM   4237 N NH1   . ARG A 1 597 ? 95.974  66.144  64.778  1.00 144.30 ? 597 ARG A NH1   1 
ATOM   4238 N NH2   . ARG A 1 597 ? 96.097  68.211  65.755  1.00 144.76 ? 597 ARG A NH2   1 
ATOM   4239 N N     . GLU A 1 598 ? 95.785  67.498  56.261  1.00 142.71 ? 598 GLU A N     1 
ATOM   4240 C CA    . GLU A 1 598 ? 95.925  66.531  55.175  1.00 142.61 ? 598 GLU A CA    1 
ATOM   4241 C C     . GLU A 1 598 ? 97.225  66.736  54.405  1.00 144.27 ? 598 GLU A C     1 
ATOM   4242 O O     . GLU A 1 598 ? 97.953  65.775  54.134  1.00 140.81 ? 598 GLU A O     1 
ATOM   4243 C CB    . GLU A 1 598 ? 94.722  66.611  54.235  1.00 137.47 ? 598 GLU A CB    1 
ATOM   4244 C CG    . GLU A 1 598 ? 93.382  66.658  54.943  1.00 134.84 ? 598 GLU A CG    1 
ATOM   4245 C CD    . GLU A 1 598 ? 92.235  66.299  54.022  1.00 131.86 ? 598 GLU A CD    1 
ATOM   4246 O OE1   . GLU A 1 598 ? 92.461  66.215  52.796  1.00 131.33 ? 598 GLU A OE1   1 
ATOM   4247 O OE2   . GLU A 1 598 ? 91.107  66.100  54.519  1.00 129.95 ? 598 GLU A OE2   1 
ATOM   4248 N N     . GLN A 1 599 ? 97.535  67.978  54.046  1.00 148.74 ? 599 GLN A N     1 
ATOM   4249 C CA    . GLN A 1 599 ? 98.734  68.245  53.270  1.00 153.21 ? 599 GLN A CA    1 
ATOM   4250 C C     . GLN A 1 599 ? 99.965  68.266  54.176  1.00 154.93 ? 599 GLN A C     1 
ATOM   4251 O O     . GLN A 1 599 ? 99.869  68.243  55.406  1.00 154.96 ? 599 GLN A O     1 
ATOM   4252 C CB    . GLN A 1 599 ? 98.599  69.562  52.507  1.00 151.36 ? 599 GLN A CB    1 
ATOM   4253 C CG    . GLN A 1 599 ? 98.729  70.804  53.368  1.00 149.59 ? 599 GLN A CG    1 
ATOM   4254 C CD    . GLN A 1 599 ? 97.479  71.089  54.177  1.00 148.09 ? 599 GLN A CD    1 
ATOM   4255 O OE1   . GLN A 1 599 ? 96.387  70.636  53.835  1.00 147.17 ? 599 GLN A OE1   1 
ATOM   4256 N NE2   . GLN A 1 599 ? 97.635  71.841  55.260  1.00 144.58 ? 599 GLN A NE2   1 
ATOM   4257 N N     . ALA A 1 600 ? 101.141 68.302  53.543  1.00 154.57 ? 600 ALA A N     1 
ATOM   4258 C CA    . ALA A 1 600 ? 102.391 68.250  54.295  1.00 152.72 ? 600 ALA A CA    1 
ATOM   4259 C C     . ALA A 1 600 ? 102.544 69.460  55.209  1.00 156.02 ? 600 ALA A C     1 
ATOM   4260 O O     . ALA A 1 600 ? 102.950 69.323  56.369  1.00 157.15 ? 600 ALA A O     1 
ATOM   4261 C CB    . ALA A 1 600 ? 103.576 68.151  53.335  1.00 148.93 ? 600 ALA A CB    1 
ATOM   4262 N N     . HIS A 1 601 ? 102.225 70.648  54.707  1.00 156.44 ? 601 HIS A N     1 
ATOM   4263 C CA    . HIS A 1 601 ? 102.293 71.864  55.501  1.00 154.53 ? 601 HIS A CA    1 
ATOM   4264 C C     . HIS A 1 601 ? 100.936 72.116  56.157  1.00 151.80 ? 601 HIS A C     1 
ATOM   4265 O O     . HIS A 1 601 ? 100.059 71.248  56.177  1.00 151.85 ? 601 HIS A O     1 
ATOM   4266 C CB    . HIS A 1 601 ? 102.746 73.037  54.633  1.00 150.13 ? 601 HIS A CB    1 
ATOM   4267 C CG    . HIS A 1 601 ? 101.672 73.585  53.748  1.00 148.88 ? 601 HIS A CG    1 
ATOM   4268 N ND1   . HIS A 1 601 ? 101.252 72.945  52.601  1.00 149.86 ? 601 HIS A ND1   1 
ATOM   4269 C CD2   . HIS A 1 601 ? 100.932 74.716  53.839  1.00 145.48 ? 601 HIS A CD2   1 
ATOM   4270 C CE1   . HIS A 1 601 ? 100.300 73.657  52.026  1.00 147.11 ? 601 HIS A CE1   1 
ATOM   4271 N NE2   . HIS A 1 601 ? 100.086 74.736  52.757  1.00 144.72 ? 601 HIS A NE2   1 
ATOM   4272 N N     . LYS A 1 602 ? 100.754 73.306  56.721  1.00 147.21 ? 602 LYS A N     1 
ATOM   4273 C CA    . LYS A 1 602 ? 99.483  73.714  57.305  1.00 140.88 ? 602 LYS A CA    1 
ATOM   4274 C C     . LYS A 1 602 ? 98.997  74.963  56.587  1.00 137.53 ? 602 LYS A C     1 
ATOM   4275 O O     . LYS A 1 602 ? 99.707  75.974  56.548  1.00 134.88 ? 602 LYS A O     1 
ATOM   4276 C CB    . LYS A 1 602 ? 99.620  73.977  58.807  1.00 138.53 ? 602 LYS A CB    1 
ATOM   4277 C CG    . LYS A 1 602 ? 100.108 72.785  59.613  1.00 139.44 ? 602 LYS A CG    1 
ATOM   4278 C CD    . LYS A 1 602 ? 101.196 73.195  60.591  1.00 137.45 ? 602 LYS A CD    1 
ATOM   4279 C CE    . LYS A 1 602 ? 101.496 72.085  61.584  1.00 133.03 ? 602 LYS A CE    1 
ATOM   4280 N NZ    . LYS A 1 602 ? 102.666 72.412  62.444  1.00 134.82 ? 602 LYS A NZ    1 
ATOM   4281 N N     . VAL A 1 603 ? 97.795  74.895  56.023  1.00 133.92 ? 603 VAL A N     1 
ATOM   4282 C CA    . VAL A 1 603 ? 97.153  76.039  55.387  1.00 128.80 ? 603 VAL A CA    1 
ATOM   4283 C C     . VAL A 1 603 ? 95.913  76.397  56.193  1.00 125.80 ? 603 VAL A C     1 
ATOM   4284 O O     . VAL A 1 603 ? 95.030  75.556  56.401  1.00 119.93 ? 603 VAL A O     1 
ATOM   4285 C CB    . VAL A 1 603 ? 96.810  75.759  53.912  1.00 125.64 ? 603 VAL A CB    1 
ATOM   4286 C CG1   . VAL A 1 603 ? 96.150  74.402  53.749  1.00 128.47 ? 603 VAL A CG1   1 
ATOM   4287 C CG2   . VAL A 1 603 ? 95.912  76.856  53.362  1.00 119.48 ? 603 VAL A CG2   1 
ATOM   4288 N N     . TYR A 1 604 ? 95.855  77.640  56.654  1.00 124.71 ? 604 TYR A N     1 
ATOM   4289 C CA    . TYR A 1 604 ? 94.790  78.118  57.521  1.00 113.66 ? 604 TYR A CA    1 
ATOM   4290 C C     . TYR A 1 604 ? 93.882  79.068  56.743  1.00 107.94 ? 604 TYR A C     1 
ATOM   4291 O O     . TYR A 1 604 ? 94.037  79.265  55.535  1.00 111.50 ? 604 TYR A O     1 
ATOM   4292 C CB    . TYR A 1 604 ? 95.378  78.785  58.765  1.00 112.41 ? 604 TYR A CB    1 
ATOM   4293 C CG    . TYR A 1 604 ? 96.112  77.832  59.681  1.00 123.04 ? 604 TYR A CG    1 
ATOM   4294 C CD1   . TYR A 1 604 ? 95.644  76.543  59.891  1.00 128.18 ? 604 TYR A CD1   1 
ATOM   4295 C CD2   . TYR A 1 604 ? 97.273  78.222  60.334  1.00 127.91 ? 604 TYR A CD2   1 
ATOM   4296 C CE1   . TYR A 1 604 ? 96.311  75.668  60.727  1.00 135.08 ? 604 TYR A CE1   1 
ATOM   4297 C CE2   . TYR A 1 604 ? 97.946  77.354  61.172  1.00 134.42 ? 604 TYR A CE2   1 
ATOM   4298 C CZ    . TYR A 1 604 ? 97.461  76.079  61.365  1.00 139.27 ? 604 TYR A CZ    1 
ATOM   4299 O OH    . TYR A 1 604 ? 98.128  75.212  62.198  1.00 143.80 ? 604 TYR A OH    1 
ATOM   4300 N N     . VAL A 1 605 ? 92.923  79.658  57.455  1.00 101.69 ? 605 VAL A N     1 
ATOM   4301 C CA    . VAL A 1 605 ? 91.919  80.495  56.807  1.00 99.55  ? 605 VAL A CA    1 
ATOM   4302 C C     . VAL A 1 605 ? 92.538  81.792  56.299  1.00 100.90 ? 605 VAL A C     1 
ATOM   4303 O O     . VAL A 1 605 ? 92.189  82.279  55.215  1.00 102.47 ? 605 VAL A O     1 
ATOM   4304 C CB    . VAL A 1 605 ? 90.755  80.762  57.776  1.00 93.00  ? 605 VAL A CB    1 
ATOM   4305 C CG1   . VAL A 1 605 ? 89.496  81.051  57.002  1.00 88.63  ? 605 VAL A CG1   1 
ATOM   4306 C CG2   . VAL A 1 605 ? 90.556  79.573  58.701  1.00 91.78  ? 605 VAL A CG2   1 
ATOM   4307 N N     . GLN A 1 606 ? 93.459  82.376  57.071  1.00 99.24  ? 606 GLN A N     1 
ATOM   4308 C CA    . GLN A 1 606 ? 94.088  83.624  56.651  1.00 98.74  ? 606 GLN A CA    1 
ATOM   4309 C C     . GLN A 1 606 ? 94.844  83.458  55.340  1.00 100.65 ? 606 GLN A C     1 
ATOM   4310 O O     . GLN A 1 606 ? 94.956  84.415  54.565  1.00 100.81 ? 606 GLN A O     1 
ATOM   4311 C CB    . GLN A 1 606 ? 95.018  84.143  57.750  1.00 98.80  ? 606 GLN A CB    1 
ATOM   4312 C CG    . GLN A 1 606 ? 96.271  83.310  57.962  1.00 101.30 ? 606 GLN A CG    1 
ATOM   4313 C CD    . GLN A 1 606 ? 96.283  82.614  59.307  1.00 106.41 ? 606 GLN A CD    1 
ATOM   4314 O OE1   . GLN A 1 606 ? 95.364  81.869  59.642  1.00 112.64 ? 606 GLN A OE1   1 
ATOM   4315 N NE2   . GLN A 1 606 ? 97.333  82.849  60.085  1.00 105.52 ? 606 GLN A NE2   1 
ATOM   4316 N N     . HIS A 1 607 ? 95.355  82.256  55.064  1.00 102.01 ? 607 HIS A N     1 
ATOM   4317 C CA    . HIS A 1 607 ? 95.974  82.002  53.769  1.00 100.91 ? 607 HIS A CA    1 
ATOM   4318 C C     . HIS A 1 607 ? 94.958  82.148  52.643  1.00 99.82  ? 607 HIS A C     1 
ATOM   4319 O O     . HIS A 1 607 ? 95.254  82.742  51.601  1.00 99.96  ? 607 HIS A O     1 
ATOM   4320 C CB    . HIS A 1 607 ? 96.601  80.610  53.751  1.00 101.61 ? 607 HIS A CB    1 
ATOM   4321 C CG    . HIS A 1 607 ? 97.695  80.429  54.756  1.00 105.90 ? 607 HIS A CG    1 
ATOM   4322 N ND1   . HIS A 1 607 ? 98.099  79.189  55.202  1.00 112.54 ? 607 HIS A ND1   1 
ATOM   4323 C CD2   . HIS A 1 607 ? 98.469  81.331  55.404  1.00 105.68 ? 607 HIS A CD2   1 
ATOM   4324 C CE1   . HIS A 1 607 ? 99.074  79.334  56.081  1.00 110.53 ? 607 HIS A CE1   1 
ATOM   4325 N NE2   . HIS A 1 607 ? 99.318  80.625  56.221  1.00 106.32 ? 607 HIS A NE2   1 
ATOM   4326 N N     . LEU A 1 608 ? 93.749  81.622  52.842  1.00 97.79  ? 608 LEU A N     1 
ATOM   4327 C CA    . LEU A 1 608 ? 92.703  81.765  51.835  1.00 94.20  ? 608 LEU A CA    1 
ATOM   4328 C C     . LEU A 1 608 ? 92.274  83.219  51.689  1.00 96.04  ? 608 LEU A C     1 
ATOM   4329 O O     . LEU A 1 608 ? 91.989  83.680  50.577  1.00 100.11 ? 608 LEU A O     1 
ATOM   4330 C CB    . LEU A 1 608 ? 91.510  80.879  52.192  1.00 94.14  ? 608 LEU A CB    1 
ATOM   4331 C CG    . LEU A 1 608 ? 91.524  79.452  51.636  1.00 97.97  ? 608 LEU A CG    1 
ATOM   4332 C CD1   . LEU A 1 608 ? 92.713  78.661  52.160  1.00 103.24 ? 608 LEU A CD1   1 
ATOM   4333 C CD2   . LEU A 1 608 ? 90.229  78.741  51.975  1.00 94.52  ? 608 LEU A CD2   1 
ATOM   4334 N N     . LEU A 1 609 ? 92.221  83.958  52.800  1.00 95.77  ? 609 LEU A N     1 
ATOM   4335 C CA    . LEU A 1 609 ? 91.917  85.384  52.723  1.00 97.17  ? 609 LEU A CA    1 
ATOM   4336 C C     . LEU A 1 609 ? 92.963  86.118  51.890  1.00 99.74  ? 609 LEU A C     1 
ATOM   4337 O O     . LEU A 1 609 ? 92.629  86.920  51.007  1.00 101.63 ? 609 LEU A O     1 
ATOM   4338 C CB    . LEU A 1 609 ? 91.833  85.980  54.131  1.00 97.92  ? 609 LEU A CB    1 
ATOM   4339 C CG    . LEU A 1 609 ? 90.507  85.957  54.904  1.00 94.07  ? 609 LEU A CG    1 
ATOM   4340 C CD1   . LEU A 1 609 ? 89.450  86.797  54.209  1.00 92.64  ? 609 LEU A CD1   1 
ATOM   4341 C CD2   . LEU A 1 609 ? 90.000  84.543  55.121  1.00 89.04  ? 609 LEU A CD2   1 
ATOM   4342 N N     . LYS A 1 610 ? 94.241  85.837  52.145  1.00 101.20 ? 610 LYS A N     1 
ATOM   4343 C CA    . LYS A 1 610 ? 95.310  86.471  51.381  1.00 102.31 ? 610 LYS A CA    1 
ATOM   4344 C C     . LYS A 1 610 ? 95.244  86.077  49.910  1.00 102.71 ? 610 LYS A C     1 
ATOM   4345 O O     . LYS A 1 610 ? 95.524  86.894  49.026  1.00 102.21 ? 610 LYS A O     1 
ATOM   4346 C CB    . LYS A 1 610 ? 96.666  86.106  51.987  1.00 101.69 ? 610 LYS A CB    1 
ATOM   4347 C CG    . LYS A 1 610 ? 97.865  86.417  51.109  1.00 103.87 ? 610 LYS A CG    1 
ATOM   4348 C CD    . LYS A 1 610 ? 98.505  85.142  50.584  1.00 104.46 ? 610 LYS A CD    1 
ATOM   4349 C CE    . LYS A 1 610 ? 98.971  84.249  51.723  1.00 102.33 ? 610 LYS A CE    1 
ATOM   4350 N NZ    . LYS A 1 610 ? 99.581  82.986  51.226  1.00 101.63 ? 610 LYS A NZ    1 
ATOM   4351 N N     . ARG A 1 611 ? 94.872  84.827  49.627  1.00 101.62 ? 611 ARG A N     1 
ATOM   4352 C CA    . ARG A 1 611 ? 94.832  84.368  48.242  1.00 99.28  ? 611 ARG A CA    1 
ATOM   4353 C C     . ARG A 1 611 ? 93.642  84.954  47.485  1.00 99.51  ? 611 ARG A C     1 
ATOM   4354 O O     . ARG A 1 611 ? 93.730  85.168  46.271  1.00 102.99 ? 611 ARG A O     1 
ATOM   4355 C CB    . ARG A 1 611 ? 94.825  82.837  48.213  1.00 95.62  ? 611 ARG A CB    1 
ATOM   4356 C CG    . ARG A 1 611 ? 94.564  82.200  46.857  1.00 88.07  ? 611 ARG A CG    1 
ATOM   4357 C CD    . ARG A 1 611 ? 93.140  81.694  46.744  1.00 87.98  ? 611 ARG A CD    1 
ATOM   4358 N NE    . ARG A 1 611 ? 92.959  80.404  47.399  1.00 96.93  ? 611 ARG A NE    1 
ATOM   4359 C CZ    . ARG A 1 611 ? 91.782  79.828  47.603  1.00 97.93  ? 611 ARG A CZ    1 
ATOM   4360 N NH1   . ARG A 1 611 ? 90.654  80.409  47.227  1.00 95.59  ? 611 ARG A NH1   1 
ATOM   4361 N NH2   . ARG A 1 611 ? 91.736  78.641  48.200  1.00 94.72  ? 611 ARG A NH2   1 
ATOM   4362 N N     . ASP A 1 612 ? 92.535  85.235  48.173  1.00 99.40  ? 612 ASP A N     1 
ATOM   4363 C CA    . ASP A 1 612 ? 91.383  85.889  47.561  1.00 98.10  ? 612 ASP A CA    1 
ATOM   4364 C C     . ASP A 1 612 ? 91.413  87.408  47.701  1.00 100.92 ? 612 ASP A C     1 
ATOM   4365 O O     . ASP A 1 612 ? 90.435  88.070  47.333  1.00 102.26 ? 612 ASP A O     1 
ATOM   4366 C CB    . ASP A 1 612 ? 90.079  85.351  48.157  1.00 97.61  ? 612 ASP A CB    1 
ATOM   4367 C CG    . ASP A 1 612 ? 89.682  84.009  47.579  1.00 99.35  ? 612 ASP A CG    1 
ATOM   4368 O OD1   . ASP A 1 612 ? 90.562  83.300  47.057  1.00 96.54  ? 612 ASP A OD1   1 
ATOM   4369 O OD2   . ASP A 1 612 ? 88.483  83.665  47.641  1.00 99.52  ? 612 ASP A OD2   1 
ATOM   4370 N N     . ARG A 1 613 ? 92.493  87.961  48.257  1.00 100.60 ? 613 ARG A N     1 
ATOM   4371 C CA    . ARG A 1 613 ? 92.676  89.405  48.390  1.00 100.23 ? 613 ARG A CA    1 
ATOM   4372 C C     . ARG A 1 613 ? 92.217  90.217  47.179  1.00 102.03 ? 613 ARG A C     1 
ATOM   4373 O O     . ARG A 1 613 ? 91.641  91.296  47.350  1.00 103.18 ? 613 ARG A O     1 
ATOM   4374 C CB    . ARG A 1 613 ? 94.148  89.715  48.693  1.00 101.98 ? 613 ARG A CB    1 
ATOM   4375 C CG    . ARG A 1 613 ? 95.057  89.870  47.479  1.00 104.59 ? 613 ARG A CG    1 
ATOM   4376 C CD    . ARG A 1 613 ? 96.504  90.117  47.876  1.00 107.76 ? 613 ARG A CD    1 
ATOM   4377 N NE    . ARG A 1 613 ? 97.237  88.876  48.095  1.00 111.27 ? 613 ARG A NE    1 
ATOM   4378 C CZ    . ARG A 1 613 ? 97.653  88.070  47.128  1.00 110.60 ? 613 ARG A CZ    1 
ATOM   4379 N NH1   . ARG A 1 613 ? 97.430  88.346  45.853  1.00 107.06 ? 613 ARG A NH1   1 
ATOM   4380 N NH2   . ARG A 1 613 ? 98.310  86.959  47.447  1.00 111.16 ? 613 ARG A NH2   1 
ATOM   4381 N N     . GLU A 1 614 ? 92.448  89.717  45.960  1.00 104.96 ? 614 GLU A N     1 
ATOM   4382 C CA    . GLU A 1 614 ? 92.127  90.508  44.775  1.00 106.30 ? 614 GLU A CA    1 
ATOM   4383 C C     . GLU A 1 614 ? 90.628  90.758  44.662  1.00 104.45 ? 614 GLU A C     1 
ATOM   4384 O O     . GLU A 1 614 ? 90.200  91.867  44.321  1.00 102.29 ? 614 GLU A O     1 
ATOM   4385 C CB    . GLU A 1 614 ? 92.669  89.827  43.514  1.00 109.01 ? 614 GLU A CB    1 
ATOM   4386 C CG    . GLU A 1 614 ? 92.107  88.443  43.222  1.00 105.71 ? 614 GLU A CG    1 
ATOM   4387 C CD    . GLU A 1 614 ? 92.849  87.344  43.954  1.00 105.58 ? 614 GLU A CD    1 
ATOM   4388 O OE1   . GLU A 1 614 ? 93.948  87.615  44.480  1.00 109.77 ? 614 GLU A OE1   1 
ATOM   4389 O OE2   . GLU A 1 614 ? 92.334  86.207  43.999  1.00 101.05 ? 614 GLU A OE2   1 
ATOM   4390 N N     . HIS A 1 615 ? 89.814  89.741  44.945  1.00 103.70 ? 615 HIS A N     1 
ATOM   4391 C CA    . HIS A 1 615 ? 88.369  89.933  44.964  1.00 103.24 ? 615 HIS A CA    1 
ATOM   4392 C C     . HIS A 1 615 ? 87.922  90.644  46.235  1.00 104.53 ? 615 HIS A C     1 
ATOM   4393 O O     . HIS A 1 615 ? 87.000  91.468  46.198  1.00 105.42 ? 615 HIS A O     1 
ATOM   4394 C CB    . HIS A 1 615 ? 87.662  88.583  44.831  1.00 103.52 ? 615 HIS A CB    1 
ATOM   4395 C CG    . HIS A 1 615 ? 86.179  88.688  44.657  1.00 106.59 ? 615 HIS A CG    1 
ATOM   4396 N ND1   . HIS A 1 615 ? 85.336  87.608  44.803  1.00 106.85 ? 615 HIS A ND1   1 
ATOM   4397 C CD2   . HIS A 1 615 ? 85.389  89.742  44.343  1.00 106.37 ? 615 HIS A CD2   1 
ATOM   4398 C CE1   . HIS A 1 615 ? 84.090  87.993  44.591  1.00 106.85 ? 615 HIS A CE1   1 
ATOM   4399 N NE2   . HIS A 1 615 ? 84.095  89.283  44.310  1.00 107.98 ? 615 HIS A NE2   1 
ATOM   4400 N N     . LEU A 1 616 ? 88.568  90.335  47.362  1.00 104.04 ? 616 LEU A N     1 
ATOM   4401 C CA    . LEU A 1 616 ? 88.123  90.869  48.646  1.00 99.89  ? 616 LEU A CA    1 
ATOM   4402 C C     . LEU A 1 616 ? 88.278  92.384  48.712  1.00 101.68 ? 616 LEU A C     1 
ATOM   4403 O O     . LEU A 1 616 ? 87.401  93.078  49.241  1.00 100.03 ? 616 LEU A O     1 
ATOM   4404 C CB    . LEU A 1 616 ? 88.893  90.202  49.783  1.00 96.16  ? 616 LEU A CB    1 
ATOM   4405 C CG    . LEU A 1 616 ? 88.684  88.693  49.910  1.00 96.21  ? 616 LEU A CG    1 
ATOM   4406 C CD1   . LEU A 1 616 ? 89.684  88.101  50.881  1.00 94.11  ? 616 LEU A CD1   1 
ATOM   4407 C CD2   . LEU A 1 616 ? 87.263  88.372  50.334  1.00 90.01  ? 616 LEU A CD2   1 
ATOM   4408 N N     . TRP A 1 617 ? 89.389  92.915  48.196  1.00 104.91 ? 617 TRP A N     1 
ATOM   4409 C CA    . TRP A 1 617 ? 89.612  94.357  48.233  1.00 106.50 ? 617 TRP A CA    1 
ATOM   4410 C C     . TRP A 1 617 ? 88.544  95.095  47.437  1.00 108.11 ? 617 TRP A C     1 
ATOM   4411 O O     . TRP A 1 617 ? 87.976  96.090  47.905  1.00 107.70 ? 617 TRP A O     1 
ATOM   4412 C CB    . TRP A 1 617 ? 91.002  94.684  47.689  1.00 107.96 ? 617 TRP A CB    1 
ATOM   4413 C CG    . TRP A 1 617 ? 91.253  96.150  47.476  1.00 107.29 ? 617 TRP A CG    1 
ATOM   4414 C CD1   . TRP A 1 617 ? 91.755  96.734  46.350  1.00 108.04 ? 617 TRP A CD1   1 
ATOM   4415 C CD2   . TRP A 1 617 ? 91.059  97.210  48.423  1.00 108.67 ? 617 TRP A CD2   1 
ATOM   4416 N NE1   . TRP A 1 617 ? 91.864  98.091  46.528  1.00 111.02 ? 617 TRP A NE1   1 
ATOM   4417 C CE2   . TRP A 1 617 ? 91.445  98.408  47.792  1.00 112.70 ? 617 TRP A CE2   1 
ATOM   4418 C CE3   . TRP A 1 617 ? 90.589  97.263  49.739  1.00 109.49 ? 617 TRP A CE3   1 
ATOM   4419 C CZ2   . TRP A 1 617 ? 91.377  99.643  48.431  1.00 113.11 ? 617 TRP A CZ2   1 
ATOM   4420 C CZ3   . TRP A 1 617 ? 90.518  98.491  50.369  1.00 111.76 ? 617 TRP A CZ3   1 
ATOM   4421 C CH2   . TRP A 1 617 ? 90.911  99.663  49.715  1.00 111.69 ? 617 TRP A CH2   1 
ATOM   4422 N N     . LYS A 1 618 ? 88.258  94.614  46.225  1.00 108.59 ? 618 LYS A N     1 
ATOM   4423 C CA    . LYS A 1 618 ? 87.224  95.234  45.405  1.00 108.44 ? 618 LYS A CA    1 
ATOM   4424 C C     . LYS A 1 618 ? 85.860  95.119  46.068  1.00 106.53 ? 618 LYS A C     1 
ATOM   4425 O O     . LYS A 1 618 ? 85.059  96.062  46.027  1.00 106.14 ? 618 LYS A O     1 
ATOM   4426 C CB    . LYS A 1 618 ? 87.206  94.595  44.017  1.00 109.82 ? 618 LYS A CB    1 
ATOM   4427 C CG    . LYS A 1 618 ? 86.225  95.232  43.048  1.00 113.12 ? 618 LYS A CG    1 
ATOM   4428 C CD    . LYS A 1 618 ? 86.084  94.399  41.785  1.00 109.64 ? 618 LYS A CD    1 
ATOM   4429 C CE    . LYS A 1 618 ? 85.594  92.995  42.103  1.00 107.77 ? 618 LYS A CE    1 
ATOM   4430 N NZ    . LYS A 1 618 ? 85.723  92.082  40.933  1.00 107.15 ? 618 LYS A NZ    1 
ATOM   4431 N N     . LEU A 1 619 ? 85.577  93.969  46.685  1.00 107.49 ? 619 LEU A N     1 
ATOM   4432 C CA    . LEU A 1 619 ? 84.299  93.787  47.363  1.00 106.12 ? 619 LEU A CA    1 
ATOM   4433 C C     . LEU A 1 619 ? 84.136  94.794  48.494  1.00 103.82 ? 619 LEU A C     1 
ATOM   4434 O O     . LEU A 1 619 ? 83.100  95.460  48.605  1.00 104.53 ? 619 LEU A O     1 
ATOM   4435 C CB    . LEU A 1 619 ? 84.192  92.357  47.891  1.00 100.39 ? 619 LEU A CB    1 
ATOM   4436 C CG    . LEU A 1 619 ? 82.790  91.753  47.986  1.00 96.71  ? 619 LEU A CG    1 
ATOM   4437 C CD1   . LEU A 1 619 ? 81.906  92.281  46.870  1.00 100.10 ? 619 LEU A CD1   1 
ATOM   4438 C CD2   . LEU A 1 619 ? 82.862  90.237  47.942  1.00 94.22  ? 619 LEU A CD2   1 
ATOM   4439 N N     . ILE A 1 620 ? 85.171  94.942  49.325  1.00 100.87 ? 620 ILE A N     1 
ATOM   4440 C CA    . ILE A 1 620 ? 85.108  95.884  50.439  1.00 99.55  ? 620 ILE A CA    1 
ATOM   4441 C C     . ILE A 1 620 ? 84.966  97.313  49.929  1.00 104.72 ? 620 ILE A C     1 
ATOM   4442 O O     . ILE A 1 620 ? 84.178  98.102  50.466  1.00 102.27 ? 620 ILE A O     1 
ATOM   4443 C CB    . ILE A 1 620 ? 86.343  95.728  51.345  1.00 98.93  ? 620 ILE A CB    1 
ATOM   4444 C CG1   . ILE A 1 620 ? 86.387  94.328  51.956  1.00 96.12  ? 620 ILE A CG1   1 
ATOM   4445 C CG2   . ILE A 1 620 ? 86.340  96.781  52.440  1.00 99.63  ? 620 ILE A CG2   1 
ATOM   4446 C CD1   . ILE A 1 620 ? 87.682  94.019  52.673  1.00 90.89  ? 620 ILE A CD1   1 
ATOM   4447 N N     . HIS A 1 621 ? 85.722  97.670  48.887  1.00 108.95 ? 621 HIS A N     1 
ATOM   4448 C CA    . HIS A 1 621 ? 85.688  99.043  48.391  1.00 109.25 ? 621 HIS A CA    1 
ATOM   4449 C C     . HIS A 1 621 ? 84.332  99.394  47.792  1.00 109.79 ? 621 HIS A C     1 
ATOM   4450 O O     . HIS A 1 621 ? 83.741  100.424 48.137  1.00 107.79 ? 621 HIS A O     1 
ATOM   4451 C CB    . HIS A 1 621 ? 86.797  99.261  47.362  1.00 112.69 ? 621 HIS A CB    1 
ATOM   4452 C CG    . HIS A 1 621 ? 87.367  100.645 47.376  1.00 117.75 ? 621 HIS A CG    1 
ATOM   4453 N ND1   . HIS A 1 621 ? 88.574  100.949 47.965  1.00 117.73 ? 621 HIS A ND1   1 
ATOM   4454 C CD2   . HIS A 1 621 ? 86.891  101.809 46.873  1.00 118.06 ? 621 HIS A CD2   1 
ATOM   4455 C CE1   . HIS A 1 621 ? 88.819  102.239 47.824  1.00 114.03 ? 621 HIS A CE1   1 
ATOM   4456 N NE2   . HIS A 1 621 ? 87.813  102.785 47.165  1.00 114.68 ? 621 HIS A NE2   1 
ATOM   4457 N N     . GLU A 1 622 ? 83.816  98.553  46.896  1.00 110.50 ? 622 GLU A N     1 
ATOM   4458 C CA    . GLU A 1 622 ? 82.618  98.922  46.151  1.00 111.46 ? 622 GLU A CA    1 
ATOM   4459 C C     . GLU A 1 622 ? 81.336  98.435  46.819  1.00 107.94 ? 622 GLU A C     1 
ATOM   4460 O O     . GLU A 1 622 ? 80.423  99.230  47.061  1.00 107.73 ? 622 GLU A O     1 
ATOM   4461 C CB    . GLU A 1 622 ? 82.709  98.386  44.719  1.00 117.41 ? 622 GLU A CB    1 
ATOM   4462 C CG    . GLU A 1 622 ? 83.917  98.897  43.949  1.00 117.24 ? 622 GLU A CG    1 
ATOM   4463 C CD    . GLU A 1 622 ? 84.130  98.167  42.638  1.00 120.17 ? 622 GLU A CD    1 
ATOM   4464 O OE1   . GLU A 1 622 ? 83.311  97.284  42.306  1.00 121.91 ? 622 GLU A OE1   1 
ATOM   4465 O OE2   . GLU A 1 622 ? 85.117  98.475  41.939  1.00 115.87 ? 622 GLU A OE2   1 
ATOM   4466 N N     . GLY A 1 623 ? 81.246  97.140  47.122  1.00 106.46 ? 623 GLY A N     1 
ATOM   4467 C CA    . GLY A 1 623 ? 80.013  96.606  47.666  1.00 105.08 ? 623 GLY A CA    1 
ATOM   4468 C C     . GLY A 1 623 ? 79.751  96.930  49.119  1.00 103.05 ? 623 GLY A C     1 
ATOM   4469 O O     . GLY A 1 623 ? 78.639  96.691  49.598  1.00 100.53 ? 623 GLY A O     1 
ATOM   4470 N N     . GLY A 1 624 ? 80.736  97.476  49.826  1.00 100.00 ? 624 GLY A N     1 
ATOM   4471 C CA    . GLY A 1 624 ? 80.572  97.717  51.250  1.00 93.78  ? 624 GLY A CA    1 
ATOM   4472 C C     . GLY A 1 624 ? 80.382  96.442  52.042  1.00 93.62  ? 624 GLY A C     1 
ATOM   4473 O O     . GLY A 1 624 ? 79.527  96.387  52.935  1.00 93.45  ? 624 GLY A O     1 
ATOM   4474 N N     . ALA A 1 625 ? 81.162  95.411  51.729  1.00 92.25  ? 625 ALA A N     1 
ATOM   4475 C CA    . ALA A 1 625 ? 80.974  94.104  52.337  1.00 85.80  ? 625 ALA A CA    1 
ATOM   4476 C C     . ALA A 1 625 ? 81.252  94.145  53.833  1.00 82.76  ? 625 ALA A C     1 
ATOM   4477 O O     . ALA A 1 625 ? 82.162  94.832  54.304  1.00 84.01  ? 625 ALA A O     1 
ATOM   4478 C CB    . ALA A 1 625 ? 81.881  93.071  51.670  1.00 85.24  ? 625 ALA A CB    1 
ATOM   4479 N N     . HIS A 1 626 ? 80.451  93.394  54.581  1.00 79.49  ? 626 HIS A N     1 
ATOM   4480 C CA    . HIS A 1 626 ? 80.615  93.252  56.019  1.00 69.41  ? 626 HIS A CA    1 
ATOM   4481 C C     . HIS A 1 626 ? 81.488  92.043  56.318  1.00 63.40  ? 626 HIS A C     1 
ATOM   4482 O O     . HIS A 1 626 ? 81.411  91.023  55.628  1.00 68.71  ? 626 HIS A O     1 
ATOM   4483 C CB    . HIS A 1 626 ? 79.261  93.103  56.713  1.00 71.42  ? 626 HIS A CB    1 
ATOM   4484 C CG    . HIS A 1 626 ? 78.450  94.360  56.729  1.00 78.67  ? 626 HIS A CG    1 
ATOM   4485 N ND1   . HIS A 1 626 ? 77.475  94.605  57.671  1.00 81.41  ? 626 HIS A ND1   1 
ATOM   4486 C CD2   . HIS A 1 626 ? 78.472  95.445  55.920  1.00 84.30  ? 626 HIS A CD2   1 
ATOM   4487 C CE1   . HIS A 1 626 ? 76.929  95.785  57.441  1.00 85.74  ? 626 HIS A CE1   1 
ATOM   4488 N NE2   . HIS A 1 626 ? 77.516  96.317  56.384  1.00 87.69  ? 626 HIS A NE2   1 
ATOM   4489 N N     . ILE A 1 627 ? 82.319  92.162  57.347  1.00 60.58  ? 627 ILE A N     1 
ATOM   4490 C CA    . ILE A 1 627 ? 83.242  91.108  57.748  1.00 59.22  ? 627 ILE A CA    1 
ATOM   4491 C C     . ILE A 1 627 ? 82.762  90.525  59.067  1.00 64.12  ? 627 ILE A C     1 
ATOM   4492 O O     . ILE A 1 627 ? 82.465  91.268  60.011  1.00 73.28  ? 627 ILE A O     1 
ATOM   4493 C CB    . ILE A 1 627 ? 84.680  91.635  57.876  1.00 58.90  ? 627 ILE A CB    1 
ATOM   4494 C CG1   . ILE A 1 627 ? 84.998  92.596  56.732  1.00 63.67  ? 627 ILE A CG1   1 
ATOM   4495 C CG2   . ILE A 1 627 ? 85.662  90.480  57.899  1.00 58.79  ? 627 ILE A CG2   1 
ATOM   4496 C CD1   . ILE A 1 627 ? 84.989  91.947  55.374  1.00 70.04  ? 627 ILE A CD1   1 
ATOM   4497 N N     . TYR A 1 628 ? 82.680  89.199  59.132  1.00 55.12  ? 628 TYR A N     1 
ATOM   4498 C CA    . TYR A 1 628 ? 82.300  88.499  60.349  1.00 56.01  ? 628 TYR A CA    1 
ATOM   4499 C C     . TYR A 1 628 ? 83.361  87.465  60.685  1.00 58.59  ? 628 TYR A C     1 
ATOM   4500 O O     . TYR A 1 628 ? 83.742  86.661  59.829  1.00 62.21  ? 628 TYR A O     1 
ATOM   4501 C CB    . TYR A 1 628 ? 80.937  87.826  60.200  1.00 61.14  ? 628 TYR A CB    1 
ATOM   4502 C CG    . TYR A 1 628 ? 79.823  88.775  59.841  1.00 59.87  ? 628 TYR A CG    1 
ATOM   4503 C CD1   . TYR A 1 628 ? 79.174  89.508  60.820  1.00 63.40  ? 628 TYR A CD1   1 
ATOM   4504 C CD2   . TYR A 1 628 ? 79.411  88.929  58.528  1.00 63.75  ? 628 TYR A CD2   1 
ATOM   4505 C CE1   . TYR A 1 628 ? 78.153  90.373  60.504  1.00 65.93  ? 628 TYR A CE1   1 
ATOM   4506 C CE2   . TYR A 1 628 ? 78.388  89.793  58.201  1.00 67.44  ? 628 TYR A CE2   1 
ATOM   4507 C CZ    . TYR A 1 628 ? 77.763  90.512  59.194  1.00 68.41  ? 628 TYR A CZ    1 
ATOM   4508 O OH    . TYR A 1 628 ? 76.743  91.376  58.877  1.00 78.07  ? 628 TYR A OH    1 
ATOM   4509 N N     . VAL A 1 629 ? 83.835  87.490  61.928  1.00 52.78  ? 629 VAL A N     1 
ATOM   4510 C CA    . VAL A 1 629 ? 84.837  86.553  62.418  1.00 53.55  ? 629 VAL A CA    1 
ATOM   4511 C C     . VAL A 1 629 ? 84.374  86.018  63.764  1.00 63.26  ? 629 VAL A C     1 
ATOM   4512 O O     . VAL A 1 629 ? 83.923  86.784  64.622  1.00 69.36  ? 629 VAL A O     1 
ATOM   4513 C CB    . VAL A 1 629 ? 86.225  87.216  62.548  1.00 55.84  ? 629 VAL A CB    1 
ATOM   4514 C CG1   . VAL A 1 629 ? 87.256  86.202  62.999  1.00 66.05  ? 629 VAL A CG1   1 
ATOM   4515 C CG2   . VAL A 1 629 ? 86.644  87.854  61.236  1.00 57.62  ? 629 VAL A CG2   1 
ATOM   4516 N N     . CYS A 1 630 ? 84.480  84.704  63.948  1.00 63.92  ? 630 CYS A N     1 
ATOM   4517 C CA    . CYS A 1 630 ? 84.153  84.098  65.231  1.00 67.67  ? 630 CYS A CA    1 
ATOM   4518 C C     . CYS A 1 630 ? 84.860  82.756  65.343  1.00 71.37  ? 630 CYS A C     1 
ATOM   4519 O O     . CYS A 1 630 ? 85.078  82.068  64.343  1.00 73.56  ? 630 CYS A O     1 
ATOM   4520 C CB    . CYS A 1 630 ? 82.642  83.928  65.409  1.00 67.86  ? 630 CYS A CB    1 
ATOM   4521 S SG    . CYS A 1 630 ? 81.828  83.010  64.099  1.00 74.37  ? 630 CYS A SG    1 
ATOM   4522 N N     . GLY A 1 631 ? 85.206  82.396  66.564  1.00 76.00  ? 631 GLY A N     1 
ATOM   4523 C CA    . GLY A 1 631 ? 85.960  81.193  66.841  1.00 81.99  ? 631 GLY A CA    1 
ATOM   4524 C C     . GLY A 1 631 ? 86.833  81.404  68.072  1.00 87.85  ? 631 GLY A C     1 
ATOM   4525 O O     . GLY A 1 631 ? 86.449  82.131  68.991  1.00 86.98  ? 631 GLY A O     1 
ATOM   4526 N N     . ASP A 1 632 ? 87.996  80.760  68.073  1.00 99.32  ? 632 ASP A N     1 
ATOM   4527 C CA    . ASP A 1 632 ? 88.956  80.957  69.150  1.00 107.54 ? 632 ASP A CA    1 
ATOM   4528 C C     . ASP A 1 632 ? 89.733  82.253  68.942  1.00 109.19 ? 632 ASP A C     1 
ATOM   4529 O O     . ASP A 1 632 ? 90.054  82.631  67.813  1.00 110.23 ? 632 ASP A O     1 
ATOM   4530 C CB    . ASP A 1 632 ? 89.904  79.759  69.260  1.00 115.27 ? 632 ASP A CB    1 
ATOM   4531 C CG    . ASP A 1 632 ? 91.008  79.777  68.220  1.00 120.94 ? 632 ASP A CG    1 
ATOM   4532 O OD1   . ASP A 1 632 ? 90.738  80.153  67.061  1.00 114.36 ? 632 ASP A OD1   1 
ATOM   4533 O OD2   . ASP A 1 632 ? 92.152  79.415  68.566  1.00 123.42 ? 632 ASP A OD2   1 
ATOM   4534 N N     . ALA A 1 633 ? 90.008  82.947  70.044  1.00 109.18 ? 633 ALA A N     1 
ATOM   4535 C CA    . ALA A 1 633 ? 90.635  84.260  70.005  1.00 106.81 ? 633 ALA A CA    1 
ATOM   4536 C C     . ALA A 1 633 ? 92.121  84.229  70.322  1.00 117.54 ? 633 ALA A C     1 
ATOM   4537 O O     . ALA A 1 633 ? 92.753  85.289  70.355  1.00 117.41 ? 633 ALA A O     1 
ATOM   4538 C CB    . ALA A 1 633 ? 89.932  85.208  70.978  1.00 104.78 ? 633 ALA A CB    1 
ATOM   4539 N N     . ARG A 1 634 ? 92.693  83.048  70.565  1.00 125.51 ? 634 ARG A N     1 
ATOM   4540 C CA    . ARG A 1 634 ? 94.095  82.978  70.963  1.00 132.03 ? 634 ARG A CA    1 
ATOM   4541 C C     . ARG A 1 634 ? 95.011  83.457  69.844  1.00 131.10 ? 634 ARG A C     1 
ATOM   4542 O O     . ARG A 1 634 ? 95.899  84.288  70.065  1.00 134.77 ? 634 ARG A O     1 
ATOM   4543 C CB    . ARG A 1 634 ? 94.447  81.551  71.384  1.00 131.32 ? 634 ARG A CB    1 
ATOM   4544 C CG    . ARG A 1 634 ? 95.714  81.448  72.213  1.00 136.48 ? 634 ARG A CG    1 
ATOM   4545 C CD    . ARG A 1 634 ? 95.486  81.956  73.628  1.00 141.76 ? 634 ARG A CD    1 
ATOM   4546 N NE    . ARG A 1 634 ? 94.678  81.036  74.419  1.00 144.13 ? 634 ARG A NE    1 
ATOM   4547 C CZ    . ARG A 1 634 ? 93.863  81.407  75.397  1.00 145.71 ? 634 ARG A CZ    1 
ATOM   4548 N NH1   . ARG A 1 634 ? 93.721  82.679  75.734  1.00 140.37 ? 634 ARG A NH1   1 
ATOM   4549 N NH2   . ARG A 1 634 ? 93.173  80.479  76.054  1.00 150.37 ? 634 ARG A NH2   1 
ATOM   4550 N N     . ASN A 1 635 ? 94.810  82.945  68.631  1.00 123.29 ? 635 ASN A N     1 
ATOM   4551 C CA    . ASN A 1 635 ? 95.655  83.332  67.509  1.00 121.00 ? 635 ASN A CA    1 
ATOM   4552 C C     . ASN A 1 635 ? 94.835  83.724  66.287  1.00 115.21 ? 635 ASN A C     1 
ATOM   4553 O O     . ASN A 1 635 ? 95.262  84.571  65.496  1.00 114.08 ? 635 ASN A O     1 
ATOM   4554 C CB    . ASN A 1 635 ? 96.614  82.193  67.151  1.00 128.42 ? 635 ASN A CB    1 
ATOM   4555 C CG    . ASN A 1 635 ? 97.796  82.106  68.096  1.00 131.05 ? 635 ASN A CG    1 
ATOM   4556 O OD1   . ASN A 1 635 ? 97.631  81.989  69.310  1.00 135.97 ? 635 ASN A OD1   1 
ATOM   4557 N ND2   . ASN A 1 635 ? 99.001  82.161  67.540  1.00 125.97 ? 635 ASN A ND2   1 
ATOM   4558 N N     . MET A 1 636 ? 93.653  83.122  66.134  1.00 114.16 ? 636 MET A N     1 
ATOM   4559 C CA    . MET A 1 636 ? 92.906  83.238  64.883  1.00 108.78 ? 636 MET A CA    1 
ATOM   4560 C C     . MET A 1 636 ? 92.501  84.681  64.602  1.00 103.96 ? 636 MET A C     1 
ATOM   4561 O O     . MET A 1 636 ? 92.726  85.196  63.501  1.00 107.75 ? 636 MET A O     1 
ATOM   4562 C CB    . MET A 1 636 ? 91.676  82.330  64.930  1.00 111.68 ? 636 MET A CB    1 
ATOM   4563 C CG    . MET A 1 636 ? 90.845  82.302  63.657  1.00 105.23 ? 636 MET A CG    1 
ATOM   4564 S SD    . MET A 1 636 ? 89.631  83.631  63.570  1.00 105.76 ? 636 MET A SD    1 
ATOM   4565 C CE    . MET A 1 636 ? 88.162  82.788  64.138  1.00 84.49  ? 636 MET A CE    1 
ATOM   4566 N N     . ALA A 1 637 ? 91.888  85.345  65.584  1.00 99.02  ? 637 ALA A N     1 
ATOM   4567 C CA    . ALA A 1 637 ? 91.412  86.707  65.361  1.00 94.75  ? 637 ALA A CA    1 
ATOM   4568 C C     . ALA A 1 637 ? 92.566  87.653  65.061  1.00 95.09  ? 637 ALA A C     1 
ATOM   4569 O O     . ALA A 1 637 ? 92.460  88.513  64.178  1.00 92.02  ? 637 ALA A O     1 
ATOM   4570 C CB    . ALA A 1 637 ? 90.619  87.193  66.573  1.00 93.34  ? 637 ALA A CB    1 
ATOM   4571 N N     . LYS A 1 638 ? 93.680  87.505  65.781  1.00 98.82  ? 638 LYS A N     1 
ATOM   4572 C CA    . LYS A 1 638 ? 94.823  88.385  65.566  1.00 99.45  ? 638 LYS A CA    1 
ATOM   4573 C C     . LYS A 1 638 ? 95.402  88.214  64.166  1.00 99.64  ? 638 LYS A C     1 
ATOM   4574 O O     . LYS A 1 638 ? 95.709  89.204  63.490  1.00 101.48 ? 638 LYS A O     1 
ATOM   4575 C CB    . LYS A 1 638 ? 95.892  88.122  66.626  1.00 99.90  ? 638 LYS A CB    1 
ATOM   4576 C CG    . LYS A 1 638 ? 96.911  89.239  66.766  1.00 94.19  ? 638 LYS A CG    1 
ATOM   4577 C CD    . LYS A 1 638 ? 96.391  90.335  67.680  1.00 97.15  ? 638 LYS A CD    1 
ATOM   4578 C CE    . LYS A 1 638 ? 97.525  91.042  68.403  1.00 99.86  ? 638 LYS A CE    1 
ATOM   4579 N NZ    . LYS A 1 638 ? 97.038  92.220  69.173  1.00 97.98  ? 638 LYS A NZ    1 
ATOM   4580 N N     . ASP A 1 639 ? 95.554  86.969  63.705  1.00 96.98  ? 639 ASP A N     1 
ATOM   4581 C CA    . ASP A 1 639 ? 96.130  86.769  62.379  1.00 98.04  ? 639 ASP A CA    1 
ATOM   4582 C C     . ASP A 1 639 ? 95.158  87.177  61.279  1.00 97.99  ? 639 ASP A C     1 
ATOM   4583 O O     . ASP A 1 639 ? 95.589  87.664  60.230  1.00 99.81  ? 639 ASP A O     1 
ATOM   4584 C CB    . ASP A 1 639 ? 96.592  85.319  62.195  1.00 104.31 ? 639 ASP A CB    1 
ATOM   4585 C CG    . ASP A 1 639 ? 95.457  84.312  62.263  1.00 111.99 ? 639 ASP A CG    1 
ATOM   4586 O OD1   . ASP A 1 639 ? 94.480  84.434  61.493  1.00 108.03 ? 639 ASP A OD1   1 
ATOM   4587 O OD2   . ASP A 1 639 ? 95.559  83.368  63.074  1.00 118.57 ? 639 ASP A OD2   1 
ATOM   4588 N N     . VAL A 1 640 ? 93.853  86.993  61.495  1.00 95.10  ? 640 VAL A N     1 
ATOM   4589 C CA    . VAL A 1 640 ? 92.875  87.485  60.528  1.00 90.81  ? 640 VAL A CA    1 
ATOM   4590 C C     . VAL A 1 640 ? 92.946  89.004  60.436  1.00 90.95  ? 640 VAL A C     1 
ATOM   4591 O O     . VAL A 1 640 ? 92.909  89.580  59.341  1.00 92.07  ? 640 VAL A O     1 
ATOM   4592 C CB    . VAL A 1 640 ? 91.462  86.997  60.898  1.00 87.89  ? 640 VAL A CB    1 
ATOM   4593 C CG1   . VAL A 1 640 ? 90.406  87.975  60.407  1.00 79.09  ? 640 VAL A CG1   1 
ATOM   4594 C CG2   . VAL A 1 640 ? 91.217  85.612  60.324  1.00 87.16  ? 640 VAL A CG2   1 
ATOM   4595 N N     . GLN A 1 641 ? 93.061  89.676  61.585  1.00 91.33  ? 641 GLN A N     1 
ATOM   4596 C CA    . GLN A 1 641 ? 93.235  91.124  61.593  1.00 89.92  ? 641 GLN A CA    1 
ATOM   4597 C C     . GLN A 1 641 ? 94.496  91.540  60.848  1.00 94.61  ? 641 GLN A C     1 
ATOM   4598 O O     . GLN A 1 641 ? 94.477  92.502  60.073  1.00 96.26  ? 641 GLN A O     1 
ATOM   4599 C CB    . GLN A 1 641 ? 93.282  91.633  63.034  1.00 93.90  ? 641 GLN A CB    1 
ATOM   4600 C CG    . GLN A 1 641 ? 93.317  93.145  63.171  1.00 99.81  ? 641 GLN A CG    1 
ATOM   4601 C CD    . GLN A 1 641 ? 93.195  93.636  64.598  1.00 100.23 ? 641 GLN A CD    1 
ATOM   4602 O OE1   . GLN A 1 641 ? 93.298  94.831  64.879  1.00 92.19  ? 641 GLN A OE1   1 
ATOM   4603 N NE2   . GLN A 1 641 ? 92.984  92.703  65.516  1.00 102.93 ? 641 GLN A NE2   1 
ATOM   4604 N N     . ASN A 1 642 ? 95.605  90.838  61.083  1.00 95.05  ? 642 ASN A N     1 
ATOM   4605 C CA    . ASN A 1 642 ? 96.854  91.190  60.415  1.00 94.48  ? 642 ASN A CA    1 
ATOM   4606 C C     . ASN A 1 642 ? 96.752  90.987  58.908  1.00 93.49  ? 642 ASN A C     1 
ATOM   4607 O O     . ASN A 1 642 ? 97.239  91.815  58.127  1.00 96.57  ? 642 ASN A O     1 
ATOM   4608 C CB    . ASN A 1 642 ? 98.004  90.369  60.996  1.00 95.61  ? 642 ASN A CB    1 
ATOM   4609 C CG    . ASN A 1 642 ? 98.489  90.910  62.324  1.00 98.52  ? 642 ASN A CG    1 
ATOM   4610 O OD1   . ASN A 1 642 ? 97.836  91.754  62.938  1.00 96.79  ? 642 ASN A OD1   1 
ATOM   4611 N ND2   . ASN A 1 642 ? 99.639  90.426  62.778  1.00 99.84  ? 642 ASN A ND2   1 
ATOM   4612 N N     . THR A 1 643 ? 96.124  89.891  58.481  1.00 91.70  ? 643 THR A N     1 
ATOM   4613 C CA    . THR A 1 643 ? 95.938  89.651  57.054  1.00 91.83  ? 643 THR A CA    1 
ATOM   4614 C C     . THR A 1 643 ? 95.062  90.727  56.428  1.00 91.94  ? 643 THR A C     1 
ATOM   4615 O O     . THR A 1 643 ? 95.347  91.204  55.323  1.00 96.74  ? 643 THR A O     1 
ATOM   4616 C CB    . THR A 1 643 ? 95.335  88.264  56.830  1.00 91.60  ? 643 THR A CB    1 
ATOM   4617 O OG1   . THR A 1 643 ? 96.308  87.263  57.152  1.00 94.34  ? 643 THR A OG1   1 
ATOM   4618 C CG2   . THR A 1 643 ? 94.904  88.091  55.383  1.00 92.80  ? 643 THR A CG2   1 
ATOM   4619 N N     . PHE A 1 644 ? 93.994  91.127  57.120  1.00 89.01  ? 644 PHE A N     1 
ATOM   4620 C CA    . PHE A 1 644 ? 93.148  92.198  56.604  1.00 88.04  ? 644 PHE A CA    1 
ATOM   4621 C C     . PHE A 1 644 ? 93.916  93.509  56.511  1.00 94.27  ? 644 PHE A C     1 
ATOM   4622 O O     . PHE A 1 644 ? 93.752  94.265  55.546  1.00 97.63  ? 644 PHE A O     1 
ATOM   4623 C CB    . PHE A 1 644 ? 91.908  92.359  57.480  1.00 84.95  ? 644 PHE A CB    1 
ATOM   4624 C CG    . PHE A 1 644 ? 90.664  91.791  56.868  1.00 81.91  ? 644 PHE A CG    1 
ATOM   4625 C CD1   . PHE A 1 644 ? 90.563  90.435  56.611  1.00 81.85  ? 644 PHE A CD1   1 
ATOM   4626 C CD2   . PHE A 1 644 ? 89.602  92.612  56.538  1.00 76.64  ? 644 PHE A CD2   1 
ATOM   4627 C CE1   . PHE A 1 644 ? 89.423  89.907  56.044  1.00 75.01  ? 644 PHE A CE1   1 
ATOM   4628 C CE2   . PHE A 1 644 ? 88.460  92.089  55.970  1.00 75.88  ? 644 PHE A CE2   1 
ATOM   4629 C CZ    . PHE A 1 644 ? 88.371  90.735  55.722  1.00 74.44  ? 644 PHE A CZ    1 
ATOM   4630 N N     . TYR A 1 645 ? 94.753  93.799  57.510  1.00 95.31  ? 645 TYR A N     1 
ATOM   4631 C CA    . TYR A 1 645 ? 95.617  94.974  57.446  1.00 96.12  ? 645 TYR A CA    1 
ATOM   4632 C C     . TYR A 1 645 ? 96.497  94.931  56.206  1.00 97.26  ? 645 TYR A C     1 
ATOM   4633 O O     . TYR A 1 645 ? 96.590  95.911  55.458  1.00 98.59  ? 645 TYR A O     1 
ATOM   4634 C CB    . TYR A 1 645 ? 96.489  95.059  58.699  1.00 98.41  ? 645 TYR A CB    1 
ATOM   4635 C CG    . TYR A 1 645 ? 95.772  95.482  59.958  1.00 99.26  ? 645 TYR A CG    1 
ATOM   4636 C CD1   . TYR A 1 645 ? 94.558  96.146  59.902  1.00 101.38 ? 645 TYR A CD1   1 
ATOM   4637 C CD2   . TYR A 1 645 ? 96.321  95.224  61.207  1.00 99.71  ? 645 TYR A CD2   1 
ATOM   4638 C CE1   . TYR A 1 645 ? 93.908  96.535  61.055  1.00 103.12 ? 645 TYR A CE1   1 
ATOM   4639 C CE2   . TYR A 1 645 ? 95.678  95.611  62.364  1.00 104.43 ? 645 TYR A CE2   1 
ATOM   4640 C CZ    . TYR A 1 645 ? 94.471  96.266  62.282  1.00 105.87 ? 645 TYR A CZ    1 
ATOM   4641 O OH    . TYR A 1 645 ? 93.822  96.654  63.431  1.00 109.89 ? 645 TYR A OH    1 
ATOM   4642 N N     . ASP A 1 646 ? 97.153  93.791  55.976  1.00 97.99  ? 646 ASP A N     1 
ATOM   4643 C CA    . ASP A 1 646 ? 98.047  93.666  54.830  1.00 97.70  ? 646 ASP A CA    1 
ATOM   4644 C C     . ASP A 1 646 ? 97.294  93.851  53.520  1.00 100.32 ? 646 ASP A C     1 
ATOM   4645 O O     . ASP A 1 646 ? 97.782  94.522  52.604  1.00 106.56 ? 646 ASP A O     1 
ATOM   4646 C CB    . ASP A 1 646 ? 98.746  92.307  54.855  1.00 99.65  ? 646 ASP A CB    1 
ATOM   4647 C CG    . ASP A 1 646 ? 99.535  92.082  56.128  1.00 103.19 ? 646 ASP A CG    1 
ATOM   4648 O OD1   . ASP A 1 646 ? 99.590  93.006  56.966  1.00 104.69 ? 646 ASP A OD1   1 
ATOM   4649 O OD2   . ASP A 1 646 ? 100.099 90.979  56.291  1.00 103.39 ? 646 ASP A OD2   1 
ATOM   4650 N N     . ILE A 1 647 ? 96.101  93.266  53.415  1.00 99.02  ? 647 ILE A N     1 
ATOM   4651 C CA    . ILE A 1 647 ? 95.348  93.347  52.167  1.00 101.60 ? 647 ILE A CA    1 
ATOM   4652 C C     . ILE A 1 647 ? 94.861  94.770  51.922  1.00 101.98 ? 647 ILE A C     1 
ATOM   4653 O O     . ILE A 1 647 ? 94.936  95.279  50.797  1.00 104.20 ? 647 ILE A O     1 
ATOM   4654 C CB    . ILE A 1 647 ? 94.183  92.341  52.176  1.00 104.04 ? 647 ILE A CB    1 
ATOM   4655 C CG1   . ILE A 1 647 ? 94.713  90.909  52.304  1.00 106.07 ? 647 ILE A CG1   1 
ATOM   4656 C CG2   . ILE A 1 647 ? 93.329  92.496  50.928  1.00 101.24 ? 647 ILE A CG2   1 
ATOM   4657 C CD1   . ILE A 1 647 ? 95.986  90.639  51.523  1.00 104.83 ? 647 ILE A CD1   1 
ATOM   4658 N N     . VAL A 1 648 ? 94.361  95.439  52.964  1.00 101.84 ? 648 VAL A N     1 
ATOM   4659 C CA    . VAL A 1 648 ? 93.839  96.788  52.790  1.00 103.52 ? 648 VAL A CA    1 
ATOM   4660 C C     . VAL A 1 648 ? 94.956  97.813  52.638  1.00 109.70 ? 648 VAL A C     1 
ATOM   4661 O O     . VAL A 1 648 ? 94.711  98.921  52.147  1.00 111.34 ? 648 VAL A O     1 
ATOM   4662 C CB    . VAL A 1 648 ? 92.910  97.152  53.965  1.00 103.55 ? 648 VAL A CB    1 
ATOM   4663 C CG1   . VAL A 1 648 ? 93.720  97.507  55.201  1.00 104.29 ? 648 VAL A CG1   1 
ATOM   4664 C CG2   . VAL A 1 648 ? 91.972  98.287  53.581  1.00 100.24 ? 648 VAL A CG2   1 
ATOM   4665 N N     . ALA A 1 649 ? 96.183  97.475  53.036  1.00 111.07 ? 649 ALA A N     1 
ATOM   4666 C CA    . ALA A 1 649 ? 97.294  98.406  52.887  1.00 111.87 ? 649 ALA A CA    1 
ATOM   4667 C C     . ALA A 1 649 ? 98.033  98.229  51.567  1.00 112.99 ? 649 ALA A C     1 
ATOM   4668 O O     . ALA A 1 649 ? 98.375  99.219  50.913  1.00 116.28 ? 649 ALA A O     1 
ATOM   4669 C CB    . ALA A 1 649 ? 98.272  98.246  54.054  1.00 110.90 ? 649 ALA A CB    1 
ATOM   4670 N N     . GLU A 1 650 ? 98.291  96.983  51.163  1.00 110.56 ? 650 GLU A N     1 
ATOM   4671 C CA    . GLU A 1 650 ? 99.030  96.741  49.930  1.00 111.93 ? 650 GLU A CA    1 
ATOM   4672 C C     . GLU A 1 650 ? 98.220  97.135  48.700  1.00 115.51 ? 650 GLU A C     1 
ATOM   4673 O O     . GLU A 1 650 ? 98.790  97.604  47.708  1.00 118.85 ? 650 GLU A O     1 
ATOM   4674 C CB    . GLU A 1 650 ? 99.451  95.271  49.863  1.00 110.81 ? 650 GLU A CB    1 
ATOM   4675 C CG    . GLU A 1 650 ? 99.379  94.642  48.484  1.00 114.91 ? 650 GLU A CG    1 
ATOM   4676 C CD    . GLU A 1 650 ? 100.003 93.262  48.443  1.00 120.59 ? 650 GLU A CD    1 
ATOM   4677 O OE1   . GLU A 1 650 ? 100.780 92.932  49.363  1.00 120.55 ? 650 GLU A OE1   1 
ATOM   4678 O OE2   . GLU A 1 650 ? 99.712  92.505  47.494  1.00 123.19 ? 650 GLU A OE2   1 
ATOM   4679 N N     . PHE A 1 651 ? 96.899  96.972  48.749  1.00 113.47 ? 651 PHE A N     1 
ATOM   4680 C CA    . PHE A 1 651 ? 96.026  97.318  47.636  1.00 112.03 ? 651 PHE A CA    1 
ATOM   4681 C C     . PHE A 1 651 ? 95.473  98.734  47.736  1.00 114.80 ? 651 PHE A C     1 
ATOM   4682 O O     . PHE A 1 651 ? 94.579  99.092  46.964  1.00 112.98 ? 651 PHE A O     1 
ATOM   4683 C CB    . PHE A 1 651 ? 94.873  96.319  47.534  1.00 108.27 ? 651 PHE A CB    1 
ATOM   4684 C CG    . PHE A 1 651 ? 95.186  95.112  46.697  1.00 108.98 ? 651 PHE A CG    1 
ATOM   4685 C CD1   . PHE A 1 651 ? 96.339  94.381  46.914  1.00 111.25 ? 651 PHE A CD1   1 
ATOM   4686 C CD2   . PHE A 1 651 ? 94.326  94.713  45.688  1.00 110.48 ? 651 PHE A CD2   1 
ATOM   4687 C CE1   . PHE A 1 651 ? 96.629  93.272  46.144  1.00 115.05 ? 651 PHE A CE1   1 
ATOM   4688 C CE2   . PHE A 1 651 ? 94.609  93.605  44.914  1.00 109.86 ? 651 PHE A CE2   1 
ATOM   4689 C CZ    . PHE A 1 651 ? 95.762  92.884  45.142  1.00 112.59 ? 651 PHE A CZ    1 
ATOM   4690 N N     . GLY A 1 652 ? 95.973  99.540  48.667  1.00 118.03 ? 652 GLY A N     1 
ATOM   4691 C CA    . GLY A 1 652 ? 95.549  100.915 48.780  1.00 120.64 ? 652 GLY A CA    1 
ATOM   4692 C C     . GLY A 1 652 ? 96.033  101.763 47.620  1.00 122.12 ? 652 GLY A C     1 
ATOM   4693 O O     . GLY A 1 652 ? 95.242  102.208 46.781  1.00 120.67 ? 652 GLY A O     1 
ATOM   4694 N N     . PRO A 1 653 ? 97.350  102.014 47.547  1.00 124.53 ? 653 PRO A N     1 
ATOM   4695 C CA    . PRO A 1 653 ? 98.387  101.695 48.543  1.00 125.11 ? 653 PRO A CA    1 
ATOM   4696 C C     . PRO A 1 653 ? 98.222  102.547 49.795  1.00 125.48 ? 653 PRO A C     1 
ATOM   4697 O O     . PRO A 1 653 ? 97.832  103.708 49.706  1.00 123.77 ? 653 PRO A O     1 
ATOM   4698 C CB    . PRO A 1 653 ? 99.695  102.015 47.804  1.00 125.22 ? 653 PRO A CB    1 
ATOM   4699 C CG    . PRO A 1 653 ? 99.353  101.905 46.350  1.00 122.76 ? 653 PRO A CG    1 
ATOM   4700 C CD    . PRO A 1 653 ? 97.943  102.414 46.259  1.00 122.45 ? 653 PRO A CD    1 
ATOM   4701 N N     . MET A 1 654 ? 98.518  102.004 50.973  1.00 125.47 ? 654 MET A N     1 
ATOM   4702 C CA    . MET A 1 654 ? 98.221  102.687 52.222  1.00 124.63 ? 654 MET A CA    1 
ATOM   4703 C C     . MET A 1 654 ? 99.217  102.229 53.277  1.00 125.61 ? 654 MET A C     1 
ATOM   4704 O O     . MET A 1 654 ? 99.695  101.092 53.246  1.00 127.36 ? 654 MET A O     1 
ATOM   4705 C CB    . MET A 1 654 ? 96.775  102.405 52.656  1.00 124.06 ? 654 MET A CB    1 
ATOM   4706 C CG    . MET A 1 654 ? 95.756  103.375 52.065  1.00 123.60 ? 654 MET A CG    1 
ATOM   4707 S SD    . MET A 1 654 ? 94.118  103.323 52.819  1.00 123.89 ? 654 MET A SD    1 
ATOM   4708 C CE    . MET A 1 654 ? 94.528  103.363 54.555  1.00 116.58 ? 654 MET A CE    1 
ATOM   4709 N N     . GLU A 1 655 ? 99.533  103.126 54.208  1.00 127.03 ? 655 GLU A N     1 
ATOM   4710 C CA    . GLU A 1 655 ? 100.501 102.816 55.248  1.00 130.55 ? 655 GLU A CA    1 
ATOM   4711 C C     . GLU A 1 655 ? 99.854  101.984 56.355  1.00 129.47 ? 655 GLU A C     1 
ATOM   4712 O O     . GLU A 1 655 ? 98.632  101.826 56.423  1.00 126.42 ? 655 GLU A O     1 
ATOM   4713 C CB    . GLU A 1 655 ? 101.103 104.096 55.825  1.00 131.95 ? 655 GLU A CB    1 
ATOM   4714 C CG    . GLU A 1 655 ? 101.968 104.874 54.848  1.00 133.68 ? 655 GLU A CG    1 
ATOM   4715 C CD    . GLU A 1 655 ? 102.865 103.975 54.020  1.00 134.92 ? 655 GLU A CD    1 
ATOM   4716 O OE1   . GLU A 1 655 ? 103.773 103.343 54.600  1.00 134.99 ? 655 GLU A OE1   1 
ATOM   4717 O OE2   . GLU A 1 655 ? 102.663 103.900 52.790  1.00 134.63 ? 655 GLU A OE2   1 
ATOM   4718 N N     . HIS A 1 656 ? 100.704 101.444 57.232  1.00 131.41 ? 656 HIS A N     1 
ATOM   4719 C CA    . HIS A 1 656 ? 100.220 100.583 58.308  1.00 132.95 ? 656 HIS A CA    1 
ATOM   4720 C C     . HIS A 1 656 ? 99.284  101.337 59.244  1.00 132.66 ? 656 HIS A C     1 
ATOM   4721 O O     . HIS A 1 656 ? 98.191  100.857 59.565  1.00 131.99 ? 656 HIS A O     1 
ATOM   4722 C CB    . HIS A 1 656 ? 101.402 100.003 59.086  1.00 134.85 ? 656 HIS A CB    1 
ATOM   4723 C CG    . HIS A 1 656 ? 101.843 98.657  58.602  1.00 134.65 ? 656 HIS A CG    1 
ATOM   4724 N ND1   . HIS A 1 656 ? 102.480 98.472  57.394  1.00 134.99 ? 656 HIS A ND1   1 
ATOM   4725 C CD2   . HIS A 1 656 ? 101.741 97.430  59.166  1.00 130.26 ? 656 HIS A CD2   1 
ATOM   4726 C CE1   . HIS A 1 656 ? 102.751 97.189  57.234  1.00 137.72 ? 656 HIS A CE1   1 
ATOM   4727 N NE2   . HIS A 1 656 ? 102.313 96.535  58.294  1.00 133.39 ? 656 HIS A NE2   1 
ATOM   4728 N N     . THR A 1 657 ? 99.698  102.524 59.695  1.00 132.30 ? 657 THR A N     1 
ATOM   4729 C CA    . THR A 1 657 ? 98.867  103.295 60.615  1.00 131.56 ? 657 THR A CA    1 
ATOM   4730 C C     . THR A 1 657 ? 97.553  103.703 59.961  1.00 128.98 ? 657 THR A C     1 
ATOM   4731 O O     . THR A 1 657 ? 96.486  103.615 60.582  1.00 126.63 ? 657 THR A O     1 
ATOM   4732 C CB    . THR A 1 657 ? 99.629  104.527 61.103  1.00 134.60 ? 657 THR A CB    1 
ATOM   4733 O OG1   . THR A 1 657 ? 100.817 104.114 61.789  1.00 136.12 ? 657 THR A OG1   1 
ATOM   4734 C CG2   . THR A 1 657 ? 98.766  105.350 62.049  1.00 133.21 ? 657 THR A CG2   1 
ATOM   4735 N N     . GLN A 1 658 ? 97.609  104.147 58.704  1.00 127.68 ? 658 GLN A N     1 
ATOM   4736 C CA    . GLN A 1 658 ? 96.388  104.522 58.002  1.00 125.42 ? 658 GLN A CA    1 
ATOM   4737 C C     . GLN A 1 658 ? 95.477  103.318 57.794  1.00 124.10 ? 658 GLN A C     1 
ATOM   4738 O O     . GLN A 1 658 ? 94.253  103.436 57.905  1.00 124.56 ? 658 GLN A O     1 
ATOM   4739 C CB    . GLN A 1 658 ? 96.728  105.179 56.665  1.00 125.66 ? 658 GLN A CB    1 
ATOM   4740 C CG    . GLN A 1 658 ? 98.081  105.865 56.628  1.00 128.25 ? 658 GLN A CG    1 
ATOM   4741 C CD    . GLN A 1 658 ? 98.437  106.368 55.244  1.00 128.47 ? 658 GLN A CD    1 
ATOM   4742 O OE1   . GLN A 1 658 ? 98.678  105.583 54.327  1.00 128.41 ? 658 GLN A OE1   1 
ATOM   4743 N NE2   . GLN A 1 658 ? 98.473  107.686 55.085  1.00 125.38 ? 658 GLN A NE2   1 
ATOM   4744 N N     . ALA A 1 659 ? 96.053  102.153 57.485  1.00 124.00 ? 659 ALA A N     1 
ATOM   4745 C CA    . ALA A 1 659 ? 95.243  100.949 57.326  1.00 119.15 ? 659 ALA A CA    1 
ATOM   4746 C C     . ALA A 1 659 ? 94.572  100.556 58.637  1.00 115.32 ? 659 ALA A C     1 
ATOM   4747 O O     . ALA A 1 659 ? 93.399  100.162 58.653  1.00 112.00 ? 659 ALA A O     1 
ATOM   4748 C CB    . ALA A 1 659 ? 96.105  99.802  56.800  1.00 114.73 ? 659 ALA A CB    1 
ATOM   4749 N N     . VAL A 1 660 ? 95.305  100.653 59.748  1.00 117.04 ? 660 VAL A N     1 
ATOM   4750 C CA    . VAL A 1 660 ? 94.723  100.358 61.054  1.00 114.48 ? 660 VAL A CA    1 
ATOM   4751 C C     . VAL A 1 660 ? 93.587  101.325 61.358  1.00 114.84 ? 660 VAL A C     1 
ATOM   4752 O O     . VAL A 1 660 ? 92.528  100.925 61.858  1.00 112.55 ? 660 VAL A O     1 
ATOM   4753 C CB    . VAL A 1 660 ? 95.811  100.394 62.143  1.00 114.65 ? 660 VAL A CB    1 
ATOM   4754 C CG1   . VAL A 1 660 ? 95.188  100.285 63.522  1.00 112.38 ? 660 VAL A CG1   1 
ATOM   4755 C CG2   . VAL A 1 660 ? 96.809  99.271  61.927  1.00 111.44 ? 660 VAL A CG2   1 
ATOM   4756 N N     . ASP A 1 661 ? 93.788  102.611 61.062  1.00 116.02 ? 661 ASP A N     1 
ATOM   4757 C CA    . ASP A 1 661 ? 92.729  103.591 61.280  1.00 116.74 ? 661 ASP A CA    1 
ATOM   4758 C C     . ASP A 1 661 ? 91.512  103.288 60.414  1.00 113.38 ? 661 ASP A C     1 
ATOM   4759 O O     . ASP A 1 661 ? 90.370  103.431 60.864  1.00 112.18 ? 661 ASP A O     1 
ATOM   4760 C CB    . ASP A 1 661 ? 93.251  105.000 61.005  1.00 119.93 ? 661 ASP A CB    1 
ATOM   4761 C CG    . ASP A 1 661 ? 93.889  105.633 62.226  1.00 129.15 ? 661 ASP A CG    1 
ATOM   4762 O OD1   . ASP A 1 661 ? 94.439  104.888 63.064  1.00 126.93 ? 661 ASP A OD1   1 
ATOM   4763 O OD2   . ASP A 1 661 ? 93.840  106.875 62.348  1.00 135.35 ? 661 ASP A OD2   1 
ATOM   4764 N N     . TYR A 1 662 ? 91.739  102.866 59.169  1.00 112.02 ? 662 TYR A N     1 
ATOM   4765 C CA    . TYR A 1 662 ? 90.630  102.498 58.293  1.00 109.80 ? 662 TYR A CA    1 
ATOM   4766 C C     . TYR A 1 662 ? 89.861  101.308 58.848  1.00 110.06 ? 662 TYR A C     1 
ATOM   4767 O O     . TYR A 1 662 ? 88.627  101.280 58.802  1.00 109.43 ? 662 TYR A O     1 
ATOM   4768 C CB    . TYR A 1 662 ? 91.149  102.190 56.889  1.00 109.07 ? 662 TYR A CB    1 
ATOM   4769 C CG    . TYR A 1 662 ? 90.058  101.997 55.860  1.00 110.43 ? 662 TYR A CG    1 
ATOM   4770 C CD1   . TYR A 1 662 ? 88.863  102.700 55.945  1.00 111.83 ? 662 TYR A CD1   1 
ATOM   4771 C CD2   . TYR A 1 662 ? 90.222  101.110 54.805  1.00 109.11 ? 662 TYR A CD2   1 
ATOM   4772 C CE1   . TYR A 1 662 ? 87.864  102.524 55.007  1.00 112.60 ? 662 TYR A CE1   1 
ATOM   4773 C CE2   . TYR A 1 662 ? 89.229  100.928 53.863  1.00 106.82 ? 662 TYR A CE2   1 
ATOM   4774 C CZ    . TYR A 1 662 ? 88.052  101.637 53.969  1.00 108.94 ? 662 TYR A CZ    1 
ATOM   4775 O OH    . TYR A 1 662 ? 87.060  101.460 53.033  1.00 109.41 ? 662 TYR A OH    1 
ATOM   4776 N N     . VAL A 1 663 ? 90.571  100.311 59.375  1.00 112.71 ? 663 VAL A N     1 
ATOM   4777 C CA    . VAL A 1 663 ? 89.897  99.139  59.929  1.00 108.52 ? 663 VAL A CA    1 
ATOM   4778 C C     . VAL A 1 663 ? 89.103  99.513  61.178  1.00 107.29 ? 663 VAL A C     1 
ATOM   4779 O O     . VAL A 1 663 ? 87.978  99.037  61.380  1.00 105.05 ? 663 VAL A O     1 
ATOM   4780 C CB    . VAL A 1 663 ? 90.916  98.020  60.207  1.00 104.18 ? 663 VAL A CB    1 
ATOM   4781 C CG1   . VAL A 1 663 ? 90.422  97.102  61.311  1.00 101.88 ? 663 VAL A CG1   1 
ATOM   4782 C CG2   . VAL A 1 663 ? 91.183  97.228  58.937  1.00 96.16  ? 663 VAL A CG2   1 
ATOM   4783 N N     . LYS A 1 664 ? 89.669  100.365 62.037  1.00 106.42 ? 664 LYS A N     1 
ATOM   4784 C CA    . LYS A 1 664 ? 88.924  100.819 63.210  1.00 106.57 ? 664 LYS A CA    1 
ATOM   4785 C C     . LYS A 1 664 ? 87.687  101.611 62.803  1.00 108.62 ? 664 LYS A C     1 
ATOM   4786 O O     . LYS A 1 664 ? 86.622  101.477 63.419  1.00 107.37 ? 664 LYS A O     1 
ATOM   4787 C CB    . LYS A 1 664 ? 89.814  101.655 64.135  1.00 108.32 ? 664 LYS A CB    1 
ATOM   4788 C CG    . LYS A 1 664 ? 91.131  101.020 64.600  1.00 105.99 ? 664 LYS A CG    1 
ATOM   4789 C CD    . LYS A 1 664 ? 91.133  99.497  64.542  1.00 104.53 ? 664 LYS A CD    1 
ATOM   4790 C CE    . LYS A 1 664 ? 92.297  98.919  65.326  1.00 104.41 ? 664 LYS A CE    1 
ATOM   4791 N NZ    . LYS A 1 664 ? 92.209  99.254  66.773  1.00 105.81 ? 664 LYS A NZ    1 
ATOM   4792 N N     . LYS A 1 665 ? 87.810  102.446 61.769  1.00 110.17 ? 665 LYS A N     1 
ATOM   4793 C CA    . LYS A 1 665 ? 86.653  103.158 61.240  1.00 110.26 ? 665 LYS A CA    1 
ATOM   4794 C C     . LYS A 1 665 ? 85.618  102.187 60.687  1.00 106.47 ? 665 LYS A C     1 
ATOM   4795 O O     . LYS A 1 665 ? 84.411  102.430 60.800  1.00 105.61 ? 665 LYS A O     1 
ATOM   4796 C CB    . LYS A 1 665 ? 87.118  104.148 60.169  1.00 108.46 ? 665 LYS A CB    1 
ATOM   4797 C CG    . LYS A 1 665 ? 86.053  104.670 59.220  1.00 110.18 ? 665 LYS A CG    1 
ATOM   4798 C CD    . LYS A 1 665 ? 85.120  105.651 59.907  1.00 111.05 ? 665 LYS A CD    1 
ATOM   4799 C CE    . LYS A 1 665 ? 84.091  106.197 58.931  1.00 114.78 ? 665 LYS A CE    1 
ATOM   4800 N NZ    . LYS A 1 665 ? 83.324  105.121 58.251  1.00 112.52 ? 665 LYS A NZ    1 
ATOM   4801 N N     . LEU A 1 666 ? 86.074  101.083 60.093  1.00 103.72 ? 666 LEU A N     1 
ATOM   4802 C CA    . LEU A 1 666 ? 85.164  100.039 59.633  1.00 102.16 ? 666 LEU A CA    1 
ATOM   4803 C C     . LEU A 1 666 ? 84.395  99.434  60.801  1.00 98.32  ? 666 LEU A C     1 
ATOM   4804 O O     . LEU A 1 666 ? 83.177  99.235  60.723  1.00 97.64  ? 666 LEU A O     1 
ATOM   4805 C CB    . LEU A 1 666 ? 85.951  98.957  58.894  1.00 99.29  ? 666 LEU A CB    1 
ATOM   4806 C CG    . LEU A 1 666 ? 85.930  98.976  57.367  1.00 100.36 ? 666 LEU A CG    1 
ATOM   4807 C CD1   . LEU A 1 666 ? 86.935  97.982  56.811  1.00 96.83  ? 666 LEU A CD1   1 
ATOM   4808 C CD2   . LEU A 1 666 ? 84.539  98.670  56.856  1.00 89.02  ? 666 LEU A CD2   1 
ATOM   4809 N N     . MET A 1 667 ? 85.097  99.132  61.896  1.00 98.87  ? 667 MET A N     1 
ATOM   4810 C CA    . MET A 1 667 ? 84.423  98.589  63.074  1.00 98.14  ? 667 MET A CA    1 
ATOM   4811 C C     . MET A 1 667 ? 83.432  99.586  63.658  1.00 101.55 ? 667 MET A C     1 
ATOM   4812 O O     . MET A 1 667 ? 82.351  99.198  64.116  1.00 102.63 ? 667 MET A O     1 
ATOM   4813 C CB    . MET A 1 667 ? 85.431  98.170  64.145  1.00 96.40  ? 667 MET A CB    1 
ATOM   4814 C CG    . MET A 1 667 ? 86.641  97.427  63.643  1.00 93.74  ? 667 MET A CG    1 
ATOM   4815 S SD    . MET A 1 667 ? 86.989  96.032  64.727  1.00 91.02  ? 667 MET A SD    1 
ATOM   4816 C CE    . MET A 1 667 ? 88.595  95.531  64.134  1.00 87.54  ? 667 MET A CE    1 
ATOM   4817 N N     . THR A 1 668 ? 83.786  100.873 63.663  1.00 101.57 ? 668 THR A N     1 
ATOM   4818 C CA    . THR A 1 668 ? 82.898  101.878 64.238  1.00 104.56 ? 668 THR A CA    1 
ATOM   4819 C C     . THR A 1 668 ? 81.558  101.925 63.515  1.00 104.30 ? 668 THR A C     1 
ATOM   4820 O O     . THR A 1 668 ? 80.535  102.257 64.125  1.00 104.13 ? 668 THR A O     1 
ATOM   4821 C CB    . THR A 1 668 ? 83.570  103.251 64.205  1.00 107.02 ? 668 THR A CB    1 
ATOM   4822 O OG1   . THR A 1 668 ? 84.938  103.121 64.611  1.00 107.46 ? 668 THR A OG1   1 
ATOM   4823 C CG2   . THR A 1 668 ? 82.863  104.213 65.146  1.00 103.87 ? 668 THR A CG2   1 
ATOM   4824 N N     . LYS A 1 669 ? 81.537  101.589 62.226  1.00 103.81 ? 669 LYS A N     1 
ATOM   4825 C CA    . LYS A 1 669 ? 80.299  101.548 61.461  1.00 103.56 ? 669 LYS A CA    1 
ATOM   4826 C C     . LYS A 1 669 ? 79.589  100.205 61.544  1.00 100.58 ? 669 LYS A C     1 
ATOM   4827 O O     . LYS A 1 669 ? 78.485  100.073 61.005  1.00 100.70 ? 669 LYS A O     1 
ATOM   4828 C CB    . LYS A 1 669 ? 80.574  101.884 59.990  1.00 101.89 ? 669 LYS A CB    1 
ATOM   4829 C CG    . LYS A 1 669 ? 81.261  103.228 59.753  1.00 107.46 ? 669 LYS A CG    1 
ATOM   4830 C CD    . LYS A 1 669 ? 80.625  104.408 60.500  1.00 109.20 ? 669 LYS A CD    1 
ATOM   4831 C CE    . LYS A 1 669 ? 79.111  104.492 60.304  1.00 108.87 ? 669 LYS A CE    1 
ATOM   4832 N NZ    . LYS A 1 669 ? 78.497  105.529 61.178  1.00 107.82 ? 669 LYS A NZ    1 
ATOM   4833 N N     . GLY A 1 670 ? 80.185  99.214  62.199  1.00 97.10  ? 670 GLY A N     1 
ATOM   4834 C CA    . GLY A 1 670 ? 79.575  97.908  62.321  1.00 91.21  ? 670 GLY A CA    1 
ATOM   4835 C C     . GLY A 1 670 ? 79.793  96.976  61.152  1.00 89.42  ? 670 GLY A C     1 
ATOM   4836 O O     . GLY A 1 670 ? 79.228  95.876  61.148  1.00 91.26  ? 670 GLY A O     1 
ATOM   4837 N N     . ARG A 1 671 ? 80.589  97.373  60.160  1.00 87.71  ? 671 ARG A N     1 
ATOM   4838 C CA    . ARG A 1 671 ? 80.880  96.496  59.034  1.00 82.88  ? 671 ARG A CA    1 
ATOM   4839 C C     . ARG A 1 671 ? 81.932  95.447  59.364  1.00 74.50  ? 671 ARG A C     1 
ATOM   4840 O O     . ARG A 1 671 ? 82.167  94.550  58.549  1.00 73.13  ? 671 ARG A O     1 
ATOM   4841 C CB    . ARG A 1 671 ? 81.326  97.321  57.825  1.00 84.56  ? 671 ARG A CB    1 
ATOM   4842 C CG    . ARG A 1 671 ? 80.326  98.390  57.408  1.00 87.22  ? 671 ARG A CG    1 
ATOM   4843 C CD    . ARG A 1 671 ? 80.763  99.117  56.146  1.00 87.52  ? 671 ARG A CD    1 
ATOM   4844 N NE    . ARG A 1 671 ? 81.483  98.243  55.228  1.00 87.53  ? 671 ARG A NE    1 
ATOM   4845 C CZ    . ARG A 1 671 ? 82.316  98.668  54.288  1.00 93.47  ? 671 ARG A CZ    1 
ATOM   4846 N NH1   . ARG A 1 671 ? 82.549  99.957  54.102  1.00 96.69  ? 671 ARG A NH1   1 
ATOM   4847 N NH2   . ARG A 1 671 ? 82.935  97.777  53.519  1.00 95.94  ? 671 ARG A NH2   1 
ATOM   4848 N N     . TYR A 1 672 ? 82.566  95.538  60.530  1.00 71.92  ? 672 TYR A N     1 
ATOM   4849 C CA    . TYR A 1 672 ? 83.496  94.527  61.012  1.00 66.43  ? 672 TYR A CA    1 
ATOM   4850 C C     . TYR A 1 672 ? 83.020  94.068  62.380  1.00 68.74  ? 672 TYR A C     1 
ATOM   4851 O O     . TYR A 1 672 ? 82.843  94.891  63.284  1.00 79.11  ? 672 TYR A O     1 
ATOM   4852 C CB    . TYR A 1 672 ? 84.922  95.081  61.092  1.00 71.00  ? 672 TYR A CB    1 
ATOM   4853 C CG    . TYR A 1 672 ? 86.005  94.028  61.148  1.00 66.81  ? 672 TYR A CG    1 
ATOM   4854 C CD1   . TYR A 1 672 ? 86.223  93.286  62.299  1.00 69.34  ? 672 TYR A CD1   1 
ATOM   4855 C CD2   . TYR A 1 672 ? 86.818  93.786  60.052  1.00 64.64  ? 672 TYR A CD2   1 
ATOM   4856 C CE1   . TYR A 1 672 ? 87.214  92.327  62.354  1.00 67.29  ? 672 TYR A CE1   1 
ATOM   4857 C CE2   . TYR A 1 672 ? 87.812  92.830  60.098  1.00 67.10  ? 672 TYR A CE2   1 
ATOM   4858 C CZ    . TYR A 1 672 ? 88.005  92.104  61.251  1.00 67.98  ? 672 TYR A CZ    1 
ATOM   4859 O OH    . TYR A 1 672 ? 88.994  91.150  61.302  1.00 71.52  ? 672 TYR A OH    1 
ATOM   4860 N N     . SER A 1 673 ? 82.813  92.763  62.533  1.00 61.13  ? 673 SER A N     1 
ATOM   4861 C CA    . SER A 1 673 ? 82.241  92.212  63.752  1.00 64.31  ? 673 SER A CA    1 
ATOM   4862 C C     . SER A 1 673 ? 83.082  91.046  64.248  1.00 66.47  ? 673 SER A C     1 
ATOM   4863 O O     . SER A 1 673 ? 83.730  90.347  63.465  1.00 66.19  ? 673 SER A O     1 
ATOM   4864 C CB    . SER A 1 673 ? 80.796  91.753  63.532  1.00 66.02  ? 673 SER A CB    1 
ATOM   4865 O OG    . SER A 1 673 ? 79.997  92.810  63.032  1.00 62.56  ? 673 SER A OG    1 
ATOM   4866 N N     . LEU A 1 674 ? 83.065  90.849  65.564  1.00 66.44  ? 674 LEU A N     1 
ATOM   4867 C CA    . LEU A 1 674 ? 83.790  89.768  66.214  1.00 64.24  ? 674 LEU A CA    1 
ATOM   4868 C C     . LEU A 1 674 ? 82.876  89.063  67.204  1.00 67.90  ? 674 LEU A C     1 
ATOM   4869 O O     . LEU A 1 674 ? 82.158  89.711  67.972  1.00 73.11  ? 674 LEU A O     1 
ATOM   4870 C CB    . LEU A 1 674 ? 85.037  90.288  66.936  1.00 61.73  ? 674 LEU A CB    1 
ATOM   4871 C CG    . LEU A 1 674 ? 86.231  90.667  66.063  1.00 61.64  ? 674 LEU A CG    1 
ATOM   4872 C CD1   . LEU A 1 674 ? 87.245  91.458  66.868  1.00 65.01  ? 674 LEU A CD1   1 
ATOM   4873 C CD2   . LEU A 1 674 ? 86.870  89.421  65.482  1.00 60.48  ? 674 LEU A CD2   1 
ATOM   4874 N N     . ASP A 1 675 ? 82.907  87.733  67.179  1.00 68.89  ? 675 ASP A N     1 
ATOM   4875 C CA    . ASP A 1 675 ? 82.173  86.884  68.113  1.00 71.72  ? 675 ASP A CA    1 
ATOM   4876 C C     . ASP A 1 675 ? 83.080  85.776  68.623  1.00 72.38  ? 675 ASP A C     1 
ATOM   4877 O O     . ASP A 1 675 ? 82.710  84.602  68.682  1.00 75.32  ? 675 ASP A O     1 
ATOM   4878 C CB    . ASP A 1 675 ? 80.919  86.308  67.462  1.00 72.16  ? 675 ASP A CB    1 
ATOM   4879 C CG    . ASP A 1 675 ? 79.885  85.864  68.476  1.00 76.76  ? 675 ASP A CG    1 
ATOM   4880 O OD1   . ASP A 1 675 ? 79.079  86.710  68.917  1.00 81.18  ? 675 ASP A OD1   1 
ATOM   4881 O OD2   . ASP A 1 675 ? 79.872  84.666  68.827  1.00 74.75  ? 675 ASP A OD2   1 
ATOM   4882 N N     . VAL A 1 676 ? 84.301  86.150  68.996  1.00 71.10  ? 676 VAL A N     1 
ATOM   4883 C CA    . VAL A 1 676 ? 85.319  85.191  69.405  1.00 76.39  ? 676 VAL A CA    1 
ATOM   4884 C C     . VAL A 1 676 ? 85.082  84.739  70.839  1.00 83.23  ? 676 VAL A C     1 
ATOM   4885 O O     . VAL A 1 676 ? 84.343  85.380  71.595  1.00 82.48  ? 676 VAL A O     1 
ATOM   4886 C CB    . VAL A 1 676 ? 86.727  85.789  69.246  1.00 80.40  ? 676 VAL A CB    1 
ATOM   4887 C CG1   . VAL A 1 676 ? 86.941  86.260  67.820  1.00 76.47  ? 676 VAL A CG1   1 
ATOM   4888 C CG2   . VAL A 1 676 ? 86.914  86.942  70.217  1.00 89.50  ? 676 VAL A CG2   1 
ATOM   4889 N N     . TRP A 1 677 ? 85.706  83.625  71.214  1.00 87.94  ? 677 TRP A N     1 
ATOM   4890 C CA    . TRP A 1 677 ? 85.634  83.095  72.567  1.00 84.80  ? 677 TRP A CA    1 
ATOM   4891 C C     . TRP A 1 677 ? 86.833  82.185  72.785  1.00 93.66  ? 677 TRP A C     1 
ATOM   4892 O O     . TRP A 1 677 ? 87.278  81.508  71.855  1.00 98.49  ? 677 TRP A O     1 
ATOM   4893 C CB    . TRP A 1 677 ? 84.320  82.339  72.807  1.00 72.64  ? 677 TRP A CB    1 
ATOM   4894 C CG    . TRP A 1 677 ? 84.199  81.045  72.051  1.00 72.89  ? 677 TRP A CG    1 
ATOM   4895 C CD1   . TRP A 1 677 ? 84.787  79.851  72.359  1.00 73.19  ? 677 TRP A CD1   1 
ATOM   4896 C CD2   . TRP A 1 677 ? 83.432  80.816  70.863  1.00 69.66  ? 677 TRP A CD2   1 
ATOM   4897 N NE1   . TRP A 1 677 ? 84.440  78.898  71.433  1.00 69.40  ? 677 TRP A NE1   1 
ATOM   4898 C CE2   . TRP A 1 677 ? 83.608  79.466  70.504  1.00 68.77  ? 677 TRP A CE2   1 
ATOM   4899 C CE3   . TRP A 1 677 ? 82.616  81.624  70.066  1.00 65.73  ? 677 TRP A CE3   1 
ATOM   4900 C CZ2   . TRP A 1 677 ? 82.997  78.906  69.385  1.00 68.03  ? 677 TRP A CZ2   1 
ATOM   4901 C CZ3   . TRP A 1 677 ? 82.012  81.066  68.957  1.00 64.38  ? 677 TRP A CZ3   1 
ATOM   4902 C CH2   . TRP A 1 677 ? 82.205  79.721  68.626  1.00 64.80  ? 677 TRP A CH2   1 
ATOM   4903 N N     . SER A 1 678 ? 87.351  82.175  74.007  1.00 100.51 ? 678 SER A N     1 
ATOM   4904 C CA    . SER A 1 678 ? 88.515  81.355  74.323  1.00 109.13 ? 678 SER A CA    1 
ATOM   4905 C C     . SER A 1 678 ? 88.492  80.890  75.773  1.00 117.33 ? 678 SER A C     1 
ATOM   4906 O O     . SER A 1 678 ? 88.993  79.814  76.098  1.00 122.98 ? 678 SER A O     1 
ATOM   4907 C CB    . SER A 1 678 ? 89.804  82.127  74.040  1.00 116.72 ? 678 SER A CB    1 
ATOM   4908 O OG    . SER A 1 678 ? 90.943  81.313  74.255  1.00 127.97 ? 678 SER A OG    1 
ATOM   4909 O OXT   . SER A 1 678 ? 87.972  81.578  76.651  1.00 116.43 ? 678 SER A OXT   1 
HETATM 4910 N N1    . FMN B 2 .   ? 88.637  92.420  79.944  1.00 112.54 ? 701 FMN A N1    1 
HETATM 4911 C C2    . FMN B 2 .   ? 88.990  93.734  79.696  1.00 113.39 ? 701 FMN A C2    1 
HETATM 4912 O O2    . FMN B 2 .   ? 89.908  94.265  80.318  1.00 111.03 ? 701 FMN A O2    1 
HETATM 4913 N N3    . FMN B 2 .   ? 88.317  94.468  78.746  1.00 118.10 ? 701 FMN A N3    1 
HETATM 4914 C C4    . FMN B 2 .   ? 87.286  93.893  78.039  1.00 118.52 ? 701 FMN A C4    1 
HETATM 4915 O O4    . FMN B 2 .   ? 86.688  94.550  77.195  1.00 120.05 ? 701 FMN A O4    1 
HETATM 4916 C C4A   . FMN B 2 .   ? 86.924  92.577  78.282  1.00 116.28 ? 701 FMN A C4A   1 
HETATM 4917 N N5    . FMN B 2 .   ? 85.895  92.007  77.565  1.00 113.73 ? 701 FMN A N5    1 
HETATM 4918 C C5A   . FMN B 2 .   ? 85.527  90.701  77.801  1.00 113.25 ? 701 FMN A C5A   1 
HETATM 4919 C C6    . FMN B 2 .   ? 84.484  90.138  77.076  1.00 112.95 ? 701 FMN A C6    1 
HETATM 4920 C C7    . FMN B 2 .   ? 84.109  88.820  77.307  1.00 119.88 ? 701 FMN A C7    1 
HETATM 4921 C C7M   . FMN B 2 .   ? 82.983  88.215  76.522  1.00 121.79 ? 701 FMN A C7M   1 
HETATM 4922 C C8    . FMN B 2 .   ? 84.781  88.068  78.263  1.00 123.69 ? 701 FMN A C8    1 
HETATM 4923 C C8M   . FMN B 2 .   ? 84.384  86.643  78.518  1.00 123.00 ? 701 FMN A C8M   1 
HETATM 4924 C C9    . FMN B 2 .   ? 85.824  88.634  78.984  1.00 120.18 ? 701 FMN A C9    1 
HETATM 4925 C C9A   . FMN B 2 .   ? 86.201  89.954  78.758  1.00 116.03 ? 701 FMN A C9A   1 
HETATM 4926 N N10   . FMN B 2 .   ? 87.237  90.524  79.478  1.00 115.37 ? 701 FMN A N10   1 
HETATM 4927 C C10   . FMN B 2 .   ? 87.603  91.836  79.239  1.00 115.09 ? 701 FMN A C10   1 
HETATM 4928 C "C1'" . FMN B 2 .   ? 87.974  89.722  80.511  1.00 112.80 ? 701 FMN A "C1'" 1 
HETATM 4929 C "C2'" . FMN B 2 .   ? 87.269  89.802  81.861  1.00 110.84 ? 701 FMN A "C2'" 1 
HETATM 4930 O "O2'" . FMN B 2 .   ? 87.339  91.122  82.350  1.00 109.26 ? 701 FMN A "O2'" 1 
HETATM 4931 C "C3'" . FMN B 2 .   ? 87.921  88.846  82.852  1.00 106.41 ? 701 FMN A "C3'" 1 
HETATM 4932 O "O3'" . FMN B 2 .   ? 87.660  87.518  82.458  1.00 103.61 ? 701 FMN A "O3'" 1 
HETATM 4933 C "C4'" . FMN B 2 .   ? 87.409  89.060  84.271  1.00 98.31  ? 701 FMN A "C4'" 1 
HETATM 4934 O "O4'" . FMN B 2 .   ? 88.091  88.187  85.142  1.00 95.59  ? 701 FMN A "O4'" 1 
HETATM 4935 C "C5'" . FMN B 2 .   ? 85.912  88.800  84.377  1.00 96.85  ? 701 FMN A "C5'" 1 
HETATM 4936 O "O5'" . FMN B 2 .   ? 85.473  89.201  85.654  1.00 96.49  ? 701 FMN A "O5'" 1 
HETATM 4937 P P     . FMN B 2 .   ? 84.046  88.731  86.229  1.00 95.69  ? 701 FMN A P     1 
HETATM 4938 O O1P   . FMN B 2 .   ? 84.124  87.256  86.526  1.00 97.88  ? 701 FMN A O1P   1 
HETATM 4939 O O2P   . FMN B 2 .   ? 82.959  88.992  85.217  1.00 95.12  ? 701 FMN A O2P   1 
HETATM 4940 O O3P   . FMN B 2 .   ? 83.747  89.475  87.506  1.00 94.56  ? 701 FMN A O3P   1 
HETATM 4941 P PA    . FAD C 3 .   ? 83.949  73.537  81.410  1.00 62.06  ? 702 FAD A PA    1 
HETATM 4942 O O1A   . FAD C 3 .   ? 83.523  72.205  81.970  1.00 67.66  ? 702 FAD A O1A   1 
HETATM 4943 O O2A   . FAD C 3 .   ? 84.239  74.689  82.311  1.00 55.54  ? 702 FAD A O2A   1 
HETATM 4944 O O5B   . FAD C 3 .   ? 85.253  73.192  80.494  1.00 63.79  ? 702 FAD A O5B   1 
HETATM 4945 C C5B   . FAD C 3 .   ? 86.040  74.250  79.996  1.00 62.40  ? 702 FAD A C5B   1 
HETATM 4946 C C4B   . FAD C 3 .   ? 87.242  74.439  80.910  1.00 64.09  ? 702 FAD A C4B   1 
HETATM 4947 O O4B   . FAD C 3 .   ? 88.151  73.355  80.697  1.00 64.63  ? 702 FAD A O4B   1 
HETATM 4948 C C3B   . FAD C 3 .   ? 88.032  75.714  80.653  1.00 66.72  ? 702 FAD A C3B   1 
HETATM 4949 O O3B   . FAD C 3 .   ? 88.650  76.084  81.861  1.00 71.78  ? 702 FAD A O3B   1 
HETATM 4950 C C2B   . FAD C 3 .   ? 89.061  75.226  79.643  1.00 67.67  ? 702 FAD A C2B   1 
HETATM 4951 O O2B   . FAD C 3 .   ? 90.166  76.073  79.595  1.00 71.69  ? 702 FAD A O2B   1 
HETATM 4952 C C1B   . FAD C 3 .   ? 89.369  73.838  80.206  1.00 69.51  ? 702 FAD A C1B   1 
HETATM 4953 N N9A   . FAD C 3 .   ? 89.882  72.920  79.228  1.00 72.12  ? 702 FAD A N9A   1 
HETATM 4954 C C8A   . FAD C 3 .   ? 89.201  72.374  78.175  1.00 73.42  ? 702 FAD A C8A   1 
HETATM 4955 N N7A   . FAD C 3 .   ? 89.924  71.573  77.453  1.00 76.83  ? 702 FAD A N7A   1 
HETATM 4956 C C5A   . FAD C 3 .   ? 91.153  71.588  78.057  1.00 78.32  ? 702 FAD A C5A   1 
HETATM 4957 C C6A   . FAD C 3 .   ? 92.367  70.939  77.770  1.00 81.14  ? 702 FAD A C6A   1 
HETATM 4958 N N6A   . FAD C 3 .   ? 92.515  70.110  76.736  1.00 76.75  ? 702 FAD A N6A   1 
HETATM 4959 N N1A   . FAD C 3 .   ? 93.408  71.172  78.576  1.00 83.83  ? 702 FAD A N1A   1 
HETATM 4960 C C2A   . FAD C 3 .   ? 93.257  71.999  79.606  1.00 79.91  ? 702 FAD A C2A   1 
HETATM 4961 N N3A   . FAD C 3 .   ? 92.176  72.662  79.975  1.00 76.98  ? 702 FAD A N3A   1 
HETATM 4962 C C4A   . FAD C 3 .   ? 91.150  72.419  79.164  1.00 76.00  ? 702 FAD A C4A   1 
HETATM 4963 N N1    . FAD C 3 .   ? 81.121  76.689  72.770  1.00 53.57  ? 702 FAD A N1    1 
HETATM 4964 C C2    . FAD C 3 .   ? 80.707  75.947  71.716  1.00 46.57  ? 702 FAD A C2    1 
HETATM 4965 O O2    . FAD C 3 .   ? 80.910  74.754  71.639  1.00 46.28  ? 702 FAD A O2    1 
HETATM 4966 N N3    . FAD C 3 .   ? 80.018  76.580  70.681  1.00 44.49  ? 702 FAD A N3    1 
HETATM 4967 C C4    . FAD C 3 .   ? 79.707  77.901  70.608  1.00 49.72  ? 702 FAD A C4    1 
HETATM 4968 O O4    . FAD C 3 .   ? 79.108  78.389  69.679  1.00 52.57  ? 702 FAD A O4    1 
HETATM 4969 C C4X   . FAD C 3 .   ? 80.175  78.681  71.776  1.00 52.63  ? 702 FAD A C4X   1 
HETATM 4970 N N5    . FAD C 3 .   ? 79.933  79.944  71.809  1.00 55.22  ? 702 FAD A N5    1 
HETATM 4971 C C5X   . FAD C 3 .   ? 80.359  80.657  72.873  1.00 54.10  ? 702 FAD A C5X   1 
HETATM 4972 C C6    . FAD C 3 .   ? 80.094  82.037  72.906  1.00 54.99  ? 702 FAD A C6    1 
HETATM 4973 C C7    . FAD C 3 .   ? 80.496  82.820  73.955  1.00 52.86  ? 702 FAD A C7    1 
HETATM 4974 C C7M   . FAD C 3 .   ? 80.215  84.289  73.992  1.00 56.35  ? 702 FAD A C7M   1 
HETATM 4975 C C8    . FAD C 3 .   ? 81.196  82.207  75.022  1.00 54.73  ? 702 FAD A C8    1 
HETATM 4976 C C8M   . FAD C 3 .   ? 81.649  83.035  76.181  1.00 62.71  ? 702 FAD A C8M   1 
HETATM 4977 C C9    . FAD C 3 .   ? 81.465  80.855  75.003  1.00 53.94  ? 702 FAD A C9    1 
HETATM 4978 C C9A   . FAD C 3 .   ? 81.058  80.049  73.936  1.00 50.83  ? 702 FAD A C9A   1 
HETATM 4979 N N10   . FAD C 3 .   ? 81.298  78.696  73.871  1.00 49.76  ? 702 FAD A N10   1 
HETATM 4980 C C10   . FAD C 3 .   ? 80.876  77.967  72.806  1.00 52.09  ? 702 FAD A C10   1 
HETATM 4981 C "C1'" . FAD C 3 .   ? 82.011  77.991  74.938  1.00 50.75  ? 702 FAD A "C1'" 1 
HETATM 4982 C "C2'" . FAD C 3 .   ? 81.043  77.406  75.970  1.00 52.14  ? 702 FAD A "C2'" 1 
HETATM 4983 O "O2'" . FAD C 3 .   ? 80.312  78.458  76.537  1.00 56.41  ? 702 FAD A "O2'" 1 
HETATM 4984 C "C3'" . FAD C 3 .   ? 81.825  76.595  77.019  1.00 52.77  ? 702 FAD A "C3'" 1 
HETATM 4985 O "O3'" . FAD C 3 .   ? 82.841  77.438  77.516  1.00 62.96  ? 702 FAD A "O3'" 1 
HETATM 4986 C "C4'" . FAD C 3 .   ? 82.446  75.322  76.422  1.00 53.28  ? 702 FAD A "C4'" 1 
HETATM 4987 O "O4'" . FAD C 3 .   ? 81.387  74.545  75.917  1.00 52.61  ? 702 FAD A "O4'" 1 
HETATM 4988 C "C5'" . FAD C 3 .   ? 83.270  74.572  77.461  1.00 59.95  ? 702 FAD A "C5'" 1 
HETATM 4989 O "O5'" . FAD C 3 .   ? 82.584  73.405  77.877  1.00 64.72  ? 702 FAD A "O5'" 1 
HETATM 4990 P P     . FAD C 3 .   ? 81.805  73.319  79.314  1.00 67.20  ? 702 FAD A P     1 
HETATM 4991 O O1P   . FAD C 3 .   ? 80.568  74.136  79.160  1.00 65.54  ? 702 FAD A O1P   1 
HETATM 4992 O O2P   . FAD C 3 .   ? 81.767  71.905  79.795  1.00 58.74  ? 702 FAD A O2P   1 
HETATM 4993 O O3P   . FAD C 3 .   ? 82.857  74.098  80.335  1.00 62.16  ? 702 FAD A O3P   1 
# 
